data_9G7J
# 
_entry.id   9G7J 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9G7J         pdb_00009g7j 10.2210/pdb9g7j/pdb 
WWPDB D_1292140473 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-28 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9G7J 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              olemaire@mpi-bremen.de 
_pdbx_contact_author.name_first         Olivier 
_pdbx_contact_author.name_last          Lemaire 
_pdbx_contact_author.name_mi            N. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4389-5786 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lemaire, O.N.' 1 0000-0002-4389-5786 
'Wagner, T.'    2 0000-0002-3382-8969 
# 
_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                     'Carbon monoxide-driven bioethanol production operates via a tungsten-dependent catalyst' 
_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 'Lemaire, O.N.'  1 0000-0002-4389-5786 
primary 'Belhamri, M.'   2 0000-0001-6208-1983 
primary 'Shevchenko, A.' 3 0009-0008-6157-4442 
primary 'Wagner, T.'     4 0000-0002-3382-8969 
# 
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     nat 'Aldehyde ferredoxin oxidoreductase' 66411.727 2    1.-.-.- ? ? 
'Monomeric metalloenzyme containing an [4Fe-4S] cluster, a tungsten-dependent bis-pyranopterin cofacor and a Mg ion.' 
2 non-polymer syn 'IRON/SULFUR CLUSTER'                351.640   2    ?       ? ? ? 
3 non-polymer syn 'Tungstopterin cofactor'             992.801   2    ?       ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                       35.453    3    ?       ? ? ? 
5 non-polymer syn 'MAGNESIUM ION'                      24.305    1    ?       ? ? ? 
6 non-polymer syn 1,2-ETHANEDIOL                       62.068    2    ?       ? ? ? 
7 water       nat water                                18.015    1504 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Oxidoreductase YdhV' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MYGYDGKVLRINLKERTCKSENLDLDKAKKFIGCRGLGVKTLFDEIDPKIDALSPENKFIIVTGPLTGAPVPTSGRFMVV
TKAPLTGTIGISNSGGKWGVDLKKAGWDMIIVEDKADSPVYIEIVDDKVEIKDASQLWGKVTSETTKELEKITENKSKVL
CIGPAGERLSLMAAVMNDVDRTAARGGVGAVMGSKNLKAITVKGTGKIALADKEKVKKVSVEKITTLKNDPVAGQGMPTY
GTAILVNIINENGVHPVKNFQESYTNQADKISGETLTANQLVRKNPCYSCPIGCGRWVRLKDGTECGGPEYETLWCFGSD
CGSYDLDAINEANMLCNEYGIDTITCGATIAAAMELYQRGYIKDEEIAGDNLSLKWGDTESMIGWIKRMVYSEGFGAKMT
NGSYRLCEGYGAPEYSMTVKKQEIPAYDPRGIQGHGITYAVNNRGGCHIKGYMINPEILGYPEKLDRFALDGKAAYAKLF
HDLTAVIDSLGLCIFTTFGLGIQDYVDMYNAVVGESTYDADSLLEAGDRIWTLEKLFNLAAGIDSSQDTLPKRLLEEPIP
DGPSKGEVHRLDVLLPEYYSVRGWSKEGIPTEETLKKLGLDEYIGKF
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MYGYDGKVLRINLKERTCKSENLDLDKAKKFIGCRGLGVKTLFDEIDPKIDALSPENKFIIVTGPLTGAPVPTSGRFMVV
TKAPLTGTIGISNSGGKWGVDLKKAGWDMIIVEDKADSPVYIEIVDDKVEIKDASQLWGKVTSETTKELEKITENKSKVL
CIGPAGERLSLMAAVMNDVDRTAARGGVGAVMGSKNLKAITVKGTGKIALADKEKVKKVSVEKITTLKNDPVAGQGMPTY
GTAILVNIINENGVHPVKNFQESYTNQADKISGETLTANQLVRKNPCYSCPIGCGRWVRLKDGTECGGPEYETLWCFGSD
CGSYDLDAINEANMLCNEYGIDTITCGATIAAAMELYQRGYIKDEEIAGDNLSLKWGDTESMIGWIKRMVYSEGFGAKMT
NGSYRLCEGYGAPEYSMTVKKQEIPAYDPRGIQGHGITYAVNNRGGCHIKGYMINPEILGYPEKLDRFALDGKAAYAKLF
HDLTAVIDSLGLCIFTTFGLGIQDYVDMYNAVVGESTYDADSLLEAGDRIWTLEKLFNLAAGIDSSQDTLPKRLLEEPIP
DGPSKGEVHRLDVLLPEYYSVRGWSKEGIPTEETLKKLGLDEYIGKF
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'IRON/SULFUR CLUSTER'    SF4   
3 'Tungstopterin cofactor' A1IJH 
4 'CHLORIDE ION'           CL    
5 'MAGNESIUM ION'          MG    
6 1,2-ETHANEDIOL           EDO   
7 water                    HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   TYR n 
1 3   GLY n 
1 4   TYR n 
1 5   ASP n 
1 6   GLY n 
1 7   LYS n 
1 8   VAL n 
1 9   LEU n 
1 10  ARG n 
1 11  ILE n 
1 12  ASN n 
1 13  LEU n 
1 14  LYS n 
1 15  GLU n 
1 16  ARG n 
1 17  THR n 
1 18  CYS n 
1 19  LYS n 
1 20  SER n 
1 21  GLU n 
1 22  ASN n 
1 23  LEU n 
1 24  ASP n 
1 25  LEU n 
1 26  ASP n 
1 27  LYS n 
1 28  ALA n 
1 29  LYS n 
1 30  LYS n 
1 31  PHE n 
1 32  ILE n 
1 33  GLY n 
1 34  CYS n 
1 35  ARG n 
1 36  GLY n 
1 37  LEU n 
1 38  GLY n 
1 39  VAL n 
1 40  LYS n 
1 41  THR n 
1 42  LEU n 
1 43  PHE n 
1 44  ASP n 
1 45  GLU n 
1 46  ILE n 
1 47  ASP n 
1 48  PRO n 
1 49  LYS n 
1 50  ILE n 
1 51  ASP n 
1 52  ALA n 
1 53  LEU n 
1 54  SER n 
1 55  PRO n 
1 56  GLU n 
1 57  ASN n 
1 58  LYS n 
1 59  PHE n 
1 60  ILE n 
1 61  ILE n 
1 62  VAL n 
1 63  THR n 
1 64  GLY n 
1 65  PRO n 
1 66  LEU n 
1 67  THR n 
1 68  GLY n 
1 69  ALA n 
1 70  PRO n 
1 71  VAL n 
1 72  PRO n 
1 73  THR n 
1 74  SER n 
1 75  GLY n 
1 76  ARG n 
1 77  PHE n 
1 78  MET n 
1 79  VAL n 
1 80  VAL n 
1 81  THR n 
1 82  LYS n 
1 83  ALA n 
1 84  PRO n 
1 85  LEU n 
1 86  THR n 
1 87  GLY n 
1 88  THR n 
1 89  ILE n 
1 90  GLY n 
1 91  ILE n 
1 92  SER n 
1 93  ASN n 
1 94  SER n 
1 95  GLY n 
1 96  GLY n 
1 97  LYS n 
1 98  TRP n 
1 99  GLY n 
1 100 VAL n 
1 101 ASP n 
1 102 LEU n 
1 103 LYS n 
1 104 LYS n 
1 105 ALA n 
1 106 GLY n 
1 107 TRP n 
1 108 ASP n 
1 109 MET n 
1 110 ILE n 
1 111 ILE n 
1 112 VAL n 
1 113 GLU n 
1 114 ASP n 
1 115 LYS n 
1 116 ALA n 
1 117 ASP n 
1 118 SER n 
1 119 PRO n 
1 120 VAL n 
1 121 TYR n 
1 122 ILE n 
1 123 GLU n 
1 124 ILE n 
1 125 VAL n 
1 126 ASP n 
1 127 ASP n 
1 128 LYS n 
1 129 VAL n 
1 130 GLU n 
1 131 ILE n 
1 132 LYS n 
1 133 ASP n 
1 134 ALA n 
1 135 SER n 
1 136 GLN n 
1 137 LEU n 
1 138 TRP n 
1 139 GLY n 
1 140 LYS n 
1 141 VAL n 
1 142 THR n 
1 143 SER n 
1 144 GLU n 
1 145 THR n 
1 146 THR n 
1 147 LYS n 
1 148 GLU n 
1 149 LEU n 
1 150 GLU n 
1 151 LYS n 
1 152 ILE n 
1 153 THR n 
1 154 GLU n 
1 155 ASN n 
1 156 LYS n 
1 157 SER n 
1 158 LYS n 
1 159 VAL n 
1 160 LEU n 
1 161 CYS n 
1 162 ILE n 
1 163 GLY n 
1 164 PRO n 
1 165 ALA n 
1 166 GLY n 
1 167 GLU n 
1 168 ARG n 
1 169 LEU n 
1 170 SER n 
1 171 LEU n 
1 172 MET n 
1 173 ALA n 
1 174 ALA n 
1 175 VAL n 
1 176 MET n 
1 177 ASN n 
1 178 ASP n 
1 179 VAL n 
1 180 ASP n 
1 181 ARG n 
1 182 THR n 
1 183 ALA n 
1 184 ALA n 
1 185 ARG n 
1 186 GLY n 
1 187 GLY n 
1 188 VAL n 
1 189 GLY n 
1 190 ALA n 
1 191 VAL n 
1 192 MET n 
1 193 GLY n 
1 194 SER n 
1 195 LYS n 
1 196 ASN n 
1 197 LEU n 
1 198 LYS n 
1 199 ALA n 
1 200 ILE n 
1 201 THR n 
1 202 VAL n 
1 203 LYS n 
1 204 GLY n 
1 205 THR n 
1 206 GLY n 
1 207 LYS n 
1 208 ILE n 
1 209 ALA n 
1 210 LEU n 
1 211 ALA n 
1 212 ASP n 
1 213 LYS n 
1 214 GLU n 
1 215 LYS n 
1 216 VAL n 
1 217 LYS n 
1 218 LYS n 
1 219 VAL n 
1 220 SER n 
1 221 VAL n 
1 222 GLU n 
1 223 LYS n 
1 224 ILE n 
1 225 THR n 
1 226 THR n 
1 227 LEU n 
1 228 LYS n 
1 229 ASN n 
1 230 ASP n 
1 231 PRO n 
1 232 VAL n 
1 233 ALA n 
1 234 GLY n 
1 235 GLN n 
1 236 GLY n 
1 237 MET n 
1 238 PRO n 
1 239 THR n 
1 240 TYR n 
1 241 GLY n 
1 242 THR n 
1 243 ALA n 
1 244 ILE n 
1 245 LEU n 
1 246 VAL n 
1 247 ASN n 
1 248 ILE n 
1 249 ILE n 
1 250 ASN n 
1 251 GLU n 
1 252 ASN n 
1 253 GLY n 
1 254 VAL n 
1 255 HIS n 
1 256 PRO n 
1 257 VAL n 
1 258 LYS n 
1 259 ASN n 
1 260 PHE n 
1 261 GLN n 
1 262 GLU n 
1 263 SER n 
1 264 TYR n 
1 265 THR n 
1 266 ASN n 
1 267 GLN n 
1 268 ALA n 
1 269 ASP n 
1 270 LYS n 
1 271 ILE n 
1 272 SER n 
1 273 GLY n 
1 274 GLU n 
1 275 THR n 
1 276 LEU n 
1 277 THR n 
1 278 ALA n 
1 279 ASN n 
1 280 GLN n 
1 281 LEU n 
1 282 VAL n 
1 283 ARG n 
1 284 LYS n 
1 285 ASN n 
1 286 PRO n 
1 287 CYS n 
1 288 TYR n 
1 289 SER n 
1 290 CYS n 
1 291 PRO n 
1 292 ILE n 
1 293 GLY n 
1 294 CYS n 
1 295 GLY n 
1 296 ARG n 
1 297 TRP n 
1 298 VAL n 
1 299 ARG n 
1 300 LEU n 
1 301 LYS n 
1 302 ASP n 
1 303 GLY n 
1 304 THR n 
1 305 GLU n 
1 306 CYS n 
1 307 GLY n 
1 308 GLY n 
1 309 PRO n 
1 310 GLU n 
1 311 TYR n 
1 312 GLU n 
1 313 THR n 
1 314 LEU n 
1 315 TRP n 
1 316 CYS n 
1 317 PHE n 
1 318 GLY n 
1 319 SER n 
1 320 ASP n 
1 321 CYS n 
1 322 GLY n 
1 323 SER n 
1 324 TYR n 
1 325 ASP n 
1 326 LEU n 
1 327 ASP n 
1 328 ALA n 
1 329 ILE n 
1 330 ASN n 
1 331 GLU n 
1 332 ALA n 
1 333 ASN n 
1 334 MET n 
1 335 LEU n 
1 336 CYS n 
1 337 ASN n 
1 338 GLU n 
1 339 TYR n 
1 340 GLY n 
1 341 ILE n 
1 342 ASP n 
1 343 THR n 
1 344 ILE n 
1 345 THR n 
1 346 CYS n 
1 347 GLY n 
1 348 ALA n 
1 349 THR n 
1 350 ILE n 
1 351 ALA n 
1 352 ALA n 
1 353 ALA n 
1 354 MET n 
1 355 GLU n 
1 356 LEU n 
1 357 TYR n 
1 358 GLN n 
1 359 ARG n 
1 360 GLY n 
1 361 TYR n 
1 362 ILE n 
1 363 LYS n 
1 364 ASP n 
1 365 GLU n 
1 366 GLU n 
1 367 ILE n 
1 368 ALA n 
1 369 GLY n 
1 370 ASP n 
1 371 ASN n 
1 372 LEU n 
1 373 SER n 
1 374 LEU n 
1 375 LYS n 
1 376 TRP n 
1 377 GLY n 
1 378 ASP n 
1 379 THR n 
1 380 GLU n 
1 381 SER n 
1 382 MET n 
1 383 ILE n 
1 384 GLY n 
1 385 TRP n 
1 386 ILE n 
1 387 LYS n 
1 388 ARG n 
1 389 MET n 
1 390 VAL n 
1 391 TYR n 
1 392 SER n 
1 393 GLU n 
1 394 GLY n 
1 395 PHE n 
1 396 GLY n 
1 397 ALA n 
1 398 LYS n 
1 399 MET n 
1 400 THR n 
1 401 ASN n 
1 402 GLY n 
1 403 SER n 
1 404 TYR n 
1 405 ARG n 
1 406 LEU n 
1 407 CYS n 
1 408 GLU n 
1 409 GLY n 
1 410 TYR n 
1 411 GLY n 
1 412 ALA n 
1 413 PRO n 
1 414 GLU n 
1 415 TYR n 
1 416 SER n 
1 417 MET n 
1 418 THR n 
1 419 VAL n 
1 420 LYS n 
1 421 LYS n 
1 422 GLN n 
1 423 GLU n 
1 424 ILE n 
1 425 PRO n 
1 426 ALA n 
1 427 TYR n 
1 428 ASP n 
1 429 PRO n 
1 430 ARG n 
1 431 GLY n 
1 432 ILE n 
1 433 GLN n 
1 434 GLY n 
1 435 HIS n 
1 436 GLY n 
1 437 ILE n 
1 438 THR n 
1 439 TYR n 
1 440 ALA n 
1 441 VAL n 
1 442 ASN n 
1 443 ASN n 
1 444 ARG n 
1 445 GLY n 
1 446 GLY n 
1 447 CYS n 
1 448 HIS n 
1 449 ILE n 
1 450 LYS n 
1 451 GLY n 
1 452 TYR n 
1 453 MET n 
1 454 ILE n 
1 455 ASN n 
1 456 PRO n 
1 457 GLU n 
1 458 ILE n 
1 459 LEU n 
1 460 GLY n 
1 461 TYR n 
1 462 PRO n 
1 463 GLU n 
1 464 LYS n 
1 465 LEU n 
1 466 ASP n 
1 467 ARG n 
1 468 PHE n 
1 469 ALA n 
1 470 LEU n 
1 471 ASP n 
1 472 GLY n 
1 473 LYS n 
1 474 ALA n 
1 475 ALA n 
1 476 TYR n 
1 477 ALA n 
1 478 LYS n 
1 479 LEU n 
1 480 PHE n 
1 481 HIS n 
1 482 ASP n 
1 483 LEU n 
1 484 THR n 
1 485 ALA n 
1 486 VAL n 
1 487 ILE n 
1 488 ASP n 
1 489 SER n 
1 490 LEU n 
1 491 GLY n 
1 492 LEU n 
1 493 CYS n 
1 494 ILE n 
1 495 PHE n 
1 496 THR n 
1 497 THR n 
1 498 PHE n 
1 499 GLY n 
1 500 LEU n 
1 501 GLY n 
1 502 ILE n 
1 503 GLN n 
1 504 ASP n 
1 505 TYR n 
1 506 VAL n 
1 507 ASP n 
1 508 MET n 
1 509 TYR n 
1 510 ASN n 
1 511 ALA n 
1 512 VAL n 
1 513 VAL n 
1 514 GLY n 
1 515 GLU n 
1 516 SER n 
1 517 THR n 
1 518 TYR n 
1 519 ASP n 
1 520 ALA n 
1 521 ASP n 
1 522 SER n 
1 523 LEU n 
1 524 LEU n 
1 525 GLU n 
1 526 ALA n 
1 527 GLY n 
1 528 ASP n 
1 529 ARG n 
1 530 ILE n 
1 531 TRP n 
1 532 THR n 
1 533 LEU n 
1 534 GLU n 
1 535 LYS n 
1 536 LEU n 
1 537 PHE n 
1 538 ASN n 
1 539 LEU n 
1 540 ALA n 
1 541 ALA n 
1 542 GLY n 
1 543 ILE n 
1 544 ASP n 
1 545 SER n 
1 546 SER n 
1 547 GLN n 
1 548 ASP n 
1 549 THR n 
1 550 LEU n 
1 551 PRO n 
1 552 LYS n 
1 553 ARG n 
1 554 LEU n 
1 555 LEU n 
1 556 GLU n 
1 557 GLU n 
1 558 PRO n 
1 559 ILE n 
1 560 PRO n 
1 561 ASP n 
1 562 GLY n 
1 563 PRO n 
1 564 SER n 
1 565 LYS n 
1 566 GLY n 
1 567 GLU n 
1 568 VAL n 
1 569 HIS n 
1 570 ARG n 
1 571 LEU n 
1 572 ASP n 
1 573 VAL n 
1 574 LEU n 
1 575 LEU n 
1 576 PRO n 
1 577 GLU n 
1 578 TYR n 
1 579 TYR n 
1 580 SER n 
1 581 VAL n 
1 582 ARG n 
1 583 GLY n 
1 584 TRP n 
1 585 SER n 
1 586 LYS n 
1 587 GLU n 
1 588 GLY n 
1 589 ILE n 
1 590 PRO n 
1 591 THR n 
1 592 GLU n 
1 593 GLU n 
1 594 THR n 
1 595 LEU n 
1 596 LYS n 
1 597 LYS n 
1 598 LEU n 
1 599 GLY n 
1 600 LEU n 
1 601 ASP n 
1 602 GLU n 
1 603 TYR n 
1 604 ILE n 
1 605 GLY n 
1 606 LYS n 
1 607 PHE n 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           1 
_entity_src_nat.pdbx_end_seq_num           607 
_entity_src_nat.common_name                ? 
_entity_src_nat.pdbx_organism_scientific   'Clostridium autoethanogenum DSM 10061' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      1341692 
_entity_src_nat.genus                      ? 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     'DSM 10061' 
_entity_src_nat.tissue                     / 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               'wild type' 
_entity_src_nat.pdbx_cell_line             / 
_entity_src_nat.pdbx_atcc                  / 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 / 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       / 
_entity_src_nat.details                    ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1IJH non-polymer         . 'Tungstopterin cofactor' ?                 'C20 H22 Mg N10 O12 P2 S4 W' 992.801 
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 
CL    non-polymer         . 'CHLORIDE ION'           ?                 'Cl -1'                      35.453  
CYS   'L-peptide linking' y CYSTEINE                 ?                 'C3 H7 N O2 S'               121.158 
EDO   non-polymer         . 1,2-ETHANEDIOL           'ETHYLENE GLYCOL' 'C2 H6 O2'                   62.068  
GLN   'L-peptide linking' y GLUTAMINE                ?                 'C5 H10 N2 O3'               146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'          ?                 'C5 H9 N O4'                 147.129 
GLY   'peptide linking'   y GLYCINE                  ?                 'C2 H5 N O2'                 75.067  
HIS   'L-peptide linking' y HISTIDINE                ?                 'C6 H10 N3 O2 1'             156.162 
HOH   non-polymer         . WATER                    ?                 'H2 O'                       18.015  
ILE   'L-peptide linking' y ISOLEUCINE               ?                 'C6 H13 N O2'                131.173 
LEU   'L-peptide linking' y LEUCINE                  ?                 'C6 H13 N O2'                131.173 
LYS   'L-peptide linking' y LYSINE                   ?                 'C6 H15 N2 O2 1'             147.195 
MET   'L-peptide linking' y METHIONINE               ?                 'C5 H11 N O2 S'              149.211 
MG    non-polymer         . 'MAGNESIUM ION'          ?                 'Mg 2'                       24.305  
PHE   'L-peptide linking' y PHENYLALANINE            ?                 'C9 H11 N O2'                165.189 
PRO   'L-peptide linking' y PROLINE                  ?                 'C5 H9 N O2'                 115.130 
SER   'L-peptide linking' y SERINE                   ?                 'C3 H7 N O3'                 105.093 
SF4   non-polymer         . 'IRON/SULFUR CLUSTER'    ?                 'Fe4 S4'                     351.640 
THR   'L-peptide linking' y THREONINE                ?                 'C4 H9 N O3'                 119.119 
TRP   'L-peptide linking' y TRYPTOPHAN               ?                 'C11 H12 N2 O2'              204.225 
TYR   'L-peptide linking' y TYROSINE                 ?                 'C9 H11 N O3'                181.189 
VAL   'L-peptide linking' y VALINE                   ?                 'C5 H11 N O2'                117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   TYR 2   2   2   TYR TYR A . n 
A 1 3   GLY 3   3   3   GLY GLY A . n 
A 1 4   TYR 4   4   4   TYR TYR A . n 
A 1 5   ASP 5   5   5   ASP ASP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   LYS 7   7   7   LYS LYS A . n 
A 1 8   VAL 8   8   8   VAL VAL A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  ARG 10  10  10  ARG ARG A . n 
A 1 11  ILE 11  11  11  ILE ILE A . n 
A 1 12  ASN 12  12  12  ASN ASN A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  LYS 14  14  14  LYS LYS A . n 
A 1 15  GLU 15  15  15  GLU GLU A . n 
A 1 16  ARG 16  16  16  ARG ARG A . n 
A 1 17  THR 17  17  17  THR THR A . n 
A 1 18  CYS 18  18  18  CYS CYS A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  SER 20  20  20  SER SER A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  ASN 22  22  22  ASN ASN A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  ASP 24  24  24  ASP ASP A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  ASP 26  26  26  ASP ASP A . n 
A 1 27  LYS 27  27  27  LYS LYS A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  PHE 31  31  31  PHE PHE A . n 
A 1 32  ILE 32  32  32  ILE ILE A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  CYS 34  34  34  CYS CYS A . n 
A 1 35  ARG 35  35  35  ARG ARG A . n 
A 1 36  GLY 36  36  36  GLY GLY A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  GLY 38  38  38  GLY GLY A . n 
A 1 39  VAL 39  39  39  VAL VAL A . n 
A 1 40  LYS 40  40  40  LYS LYS A . n 
A 1 41  THR 41  41  41  THR THR A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  PHE 43  43  43  PHE PHE A . n 
A 1 44  ASP 44  44  44  ASP ASP A . n 
A 1 45  GLU 45  45  45  GLU GLU A . n 
A 1 46  ILE 46  46  46  ILE ILE A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  PRO 48  48  48  PRO PRO A . n 
A 1 49  LYS 49  49  49  LYS LYS A . n 
A 1 50  ILE 50  50  50  ILE ILE A . n 
A 1 51  ASP 51  51  51  ASP ASP A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  SER 54  54  54  SER SER A . n 
A 1 55  PRO 55  55  55  PRO PRO A . n 
A 1 56  GLU 56  56  56  GLU GLU A . n 
A 1 57  ASN 57  57  57  ASN ASN A . n 
A 1 58  LYS 58  58  58  LYS LYS A . n 
A 1 59  PHE 59  59  59  PHE PHE A . n 
A 1 60  ILE 60  60  60  ILE ILE A . n 
A 1 61  ILE 61  61  61  ILE ILE A . n 
A 1 62  VAL 62  62  62  VAL VAL A . n 
A 1 63  THR 63  63  63  THR THR A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  PRO 65  65  65  PRO PRO A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  THR 67  67  67  THR THR A . n 
A 1 68  GLY 68  68  68  GLY GLY A . n 
A 1 69  ALA 69  69  69  ALA ALA A . n 
A 1 70  PRO 70  70  70  PRO PRO A . n 
A 1 71  VAL 71  71  71  VAL VAL A . n 
A 1 72  PRO 72  72  72  PRO PRO A . n 
A 1 73  THR 73  73  73  THR THR A . n 
A 1 74  SER 74  74  74  SER SER A . n 
A 1 75  GLY 75  75  75  GLY GLY A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  PHE 77  77  77  PHE PHE A . n 
A 1 78  MET 78  78  78  MET MET A . n 
A 1 79  VAL 79  79  79  VAL VAL A . n 
A 1 80  VAL 80  80  80  VAL VAL A . n 
A 1 81  THR 81  81  81  THR THR A . n 
A 1 82  LYS 82  82  82  LYS LYS A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  PRO 84  84  84  PRO PRO A . n 
A 1 85  LEU 85  85  85  LEU LEU A . n 
A 1 86  THR 86  86  86  THR THR A . n 
A 1 87  GLY 87  87  87  GLY GLY A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  ILE 89  89  89  ILE ILE A . n 
A 1 90  GLY 90  90  90  GLY GLY A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  SER 92  92  92  SER SER A . n 
A 1 93  ASN 93  93  93  ASN ASN A . n 
A 1 94  SER 94  94  94  SER SER A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  GLY 96  96  96  GLY GLY A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  TRP 98  98  98  TRP TRP A . n 
A 1 99  GLY 99  99  99  GLY GLY A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 LYS 103 103 103 LYS LYS A . n 
A 1 104 LYS 104 104 104 LYS LYS A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 GLY 106 106 106 GLY GLY A . n 
A 1 107 TRP 107 107 107 TRP TRP A . n 
A 1 108 ASP 108 108 108 ASP ASP A . n 
A 1 109 MET 109 109 109 MET MET A . n 
A 1 110 ILE 110 110 110 ILE ILE A . n 
A 1 111 ILE 111 111 111 ILE ILE A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 GLU 113 113 113 GLU GLU A . n 
A 1 114 ASP 114 114 114 ASP ASP A . n 
A 1 115 LYS 115 115 115 LYS LYS A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 ASP 117 117 117 ASP ASP A . n 
A 1 118 SER 118 118 118 SER SER A . n 
A 1 119 PRO 119 119 119 PRO PRO A . n 
A 1 120 VAL 120 120 120 VAL VAL A . n 
A 1 121 TYR 121 121 121 TYR TYR A . n 
A 1 122 ILE 122 122 122 ILE ILE A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 ILE 124 124 124 ILE ILE A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 ASP 126 126 126 ASP ASP A . n 
A 1 127 ASP 127 127 127 ASP ASP A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 VAL 129 129 129 VAL VAL A . n 
A 1 130 GLU 130 130 130 GLU GLU A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 LYS 132 132 132 LYS LYS A . n 
A 1 133 ASP 133 133 133 ASP ASP A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 SER 135 135 135 SER SER A . n 
A 1 136 GLN 136 136 136 GLN GLN A . n 
A 1 137 LEU 137 137 137 LEU LEU A . n 
A 1 138 TRP 138 138 138 TRP TRP A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 LYS 140 140 140 LYS LYS A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 THR 142 142 142 THR THR A . n 
A 1 143 SER 143 143 143 SER SER A . n 
A 1 144 GLU 144 144 144 GLU GLU A . n 
A 1 145 THR 145 145 145 THR THR A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 LYS 147 147 147 LYS LYS A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 GLU 150 150 150 GLU GLU A . n 
A 1 151 LYS 151 151 151 LYS LYS A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 THR 153 153 153 THR THR A . n 
A 1 154 GLU 154 154 154 GLU GLU A . n 
A 1 155 ASN 155 155 155 ASN ASN A . n 
A 1 156 LYS 156 156 156 LYS LYS A . n 
A 1 157 SER 157 157 157 SER SER A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 CYS 161 161 161 CYS CYS A . n 
A 1 162 ILE 162 162 162 ILE ILE A . n 
A 1 163 GLY 163 163 163 GLY GLY A . n 
A 1 164 PRO 164 164 164 PRO PRO A . n 
A 1 165 ALA 165 165 165 ALA ALA A . n 
A 1 166 GLY 166 166 166 GLY GLY A . n 
A 1 167 GLU 167 167 167 GLU GLU A . n 
A 1 168 ARG 168 168 168 ARG ARG A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
A 1 170 SER 170 170 170 SER SER A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 MET 172 172 172 MET MET A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 ALA 174 174 174 ALA ALA A . n 
A 1 175 VAL 175 175 175 VAL VAL A . n 
A 1 176 MET 176 176 176 MET MET A . n 
A 1 177 ASN 177 177 177 ASN ASN A . n 
A 1 178 ASP 178 178 178 ASP ASP A . n 
A 1 179 VAL 179 179 179 VAL VAL A . n 
A 1 180 ASP 180 180 180 ASP ASP A . n 
A 1 181 ARG 181 181 181 ARG ARG A . n 
A 1 182 THR 182 182 182 THR THR A . n 
A 1 183 ALA 183 183 183 ALA ALA A . n 
A 1 184 ALA 184 184 184 ALA ALA A . n 
A 1 185 ARG 185 185 185 ARG ARG A . n 
A 1 186 GLY 186 186 186 GLY GLY A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 VAL 188 188 188 VAL VAL A . n 
A 1 189 GLY 189 189 189 GLY GLY A . n 
A 1 190 ALA 190 190 190 ALA ALA A . n 
A 1 191 VAL 191 191 191 VAL VAL A . n 
A 1 192 MET 192 192 192 MET MET A . n 
A 1 193 GLY 193 193 193 GLY GLY A . n 
A 1 194 SER 194 194 194 SER SER A . n 
A 1 195 LYS 195 195 195 LYS LYS A . n 
A 1 196 ASN 196 196 196 ASN ASN A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 LYS 198 198 198 LYS LYS A . n 
A 1 199 ALA 199 199 199 ALA ALA A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 LYS 203 203 203 LYS LYS A . n 
A 1 204 GLY 204 204 204 GLY GLY A . n 
A 1 205 THR 205 205 205 THR THR A . n 
A 1 206 GLY 206 206 206 GLY GLY A . n 
A 1 207 LYS 207 207 207 LYS LYS A . n 
A 1 208 ILE 208 208 208 ILE ILE A . n 
A 1 209 ALA 209 209 209 ALA ALA A . n 
A 1 210 LEU 210 210 210 LEU LEU A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 ASP 212 212 212 ASP ASP A . n 
A 1 213 LYS 213 213 213 LYS LYS A . n 
A 1 214 GLU 214 214 214 GLU GLU A . n 
A 1 215 LYS 215 215 215 LYS LYS A . n 
A 1 216 VAL 216 216 216 VAL VAL A . n 
A 1 217 LYS 217 217 217 LYS LYS A . n 
A 1 218 LYS 218 218 218 LYS LYS A . n 
A 1 219 VAL 219 219 219 VAL VAL A . n 
A 1 220 SER 220 220 220 SER SER A . n 
A 1 221 VAL 221 221 221 VAL VAL A . n 
A 1 222 GLU 222 222 222 GLU GLU A . n 
A 1 223 LYS 223 223 223 LYS LYS A . n 
A 1 224 ILE 224 224 224 ILE ILE A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 LYS 228 228 228 LYS LYS A . n 
A 1 229 ASN 229 229 229 ASN ASN A . n 
A 1 230 ASP 230 230 230 ASP ASP A . n 
A 1 231 PRO 231 231 231 PRO PRO A . n 
A 1 232 VAL 232 232 232 VAL VAL A . n 
A 1 233 ALA 233 233 233 ALA ALA A . n 
A 1 234 GLY 234 234 234 GLY GLY A . n 
A 1 235 GLN 235 235 235 GLN GLN A . n 
A 1 236 GLY 236 236 236 GLY GLY A . n 
A 1 237 MET 237 237 237 MET MET A . n 
A 1 238 PRO 238 238 238 PRO PRO A . n 
A 1 239 THR 239 239 239 THR THR A . n 
A 1 240 TYR 240 240 240 TYR TYR A . n 
A 1 241 GLY 241 241 241 GLY GLY A . n 
A 1 242 THR 242 242 242 THR THR A . n 
A 1 243 ALA 243 243 243 ALA ALA A . n 
A 1 244 ILE 244 244 244 ILE ILE A . n 
A 1 245 LEU 245 245 245 LEU LEU A . n 
A 1 246 VAL 246 246 246 VAL VAL A . n 
A 1 247 ASN 247 247 247 ASN ASN A . n 
A 1 248 ILE 248 248 248 ILE ILE A . n 
A 1 249 ILE 249 249 249 ILE ILE A . n 
A 1 250 ASN 250 250 250 ASN ASN A . n 
A 1 251 GLU 251 251 251 GLU GLU A . n 
A 1 252 ASN 252 252 252 ASN ASN A . n 
A 1 253 GLY 253 253 253 GLY GLY A . n 
A 1 254 VAL 254 254 254 VAL VAL A . n 
A 1 255 HIS 255 255 255 HIS HIS A . n 
A 1 256 PRO 256 256 256 PRO PRO A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 LYS 258 258 258 LYS LYS A . n 
A 1 259 ASN 259 259 259 ASN ASN A . n 
A 1 260 PHE 260 260 260 PHE PHE A . n 
A 1 261 GLN 261 261 261 GLN GLN A . n 
A 1 262 GLU 262 262 262 GLU GLU A . n 
A 1 263 SER 263 263 263 SER SER A . n 
A 1 264 TYR 264 264 264 TYR TYR A . n 
A 1 265 THR 265 265 265 THR THR A . n 
A 1 266 ASN 266 266 266 ASN ASN A . n 
A 1 267 GLN 267 267 267 GLN GLN A . n 
A 1 268 ALA 268 268 268 ALA ALA A . n 
A 1 269 ASP 269 269 269 ASP ASP A . n 
A 1 270 LYS 270 270 270 LYS LYS A . n 
A 1 271 ILE 271 271 271 ILE ILE A . n 
A 1 272 SER 272 272 272 SER SER A . n 
A 1 273 GLY 273 273 273 GLY GLY A . n 
A 1 274 GLU 274 274 274 GLU GLU A . n 
A 1 275 THR 275 275 275 THR THR A . n 
A 1 276 LEU 276 276 276 LEU LEU A . n 
A 1 277 THR 277 277 277 THR THR A . n 
A 1 278 ALA 278 278 278 ALA ALA A . n 
A 1 279 ASN 279 279 279 ASN ASN A . n 
A 1 280 GLN 280 280 280 GLN GLN A . n 
A 1 281 LEU 281 281 281 LEU LEU A . n 
A 1 282 VAL 282 282 282 VAL VAL A . n 
A 1 283 ARG 283 283 283 ARG ARG A . n 
A 1 284 LYS 284 284 284 LYS LYS A . n 
A 1 285 ASN 285 285 285 ASN ASN A . n 
A 1 286 PRO 286 286 286 PRO PRO A . n 
A 1 287 CYS 287 287 287 CYS CYS A . n 
A 1 288 TYR 288 288 288 TYR TYR A . n 
A 1 289 SER 289 289 289 SER SER A . n 
A 1 290 CYS 290 290 290 CYS CYS A . n 
A 1 291 PRO 291 291 291 PRO PRO A . n 
A 1 292 ILE 292 292 292 ILE ILE A . n 
A 1 293 GLY 293 293 293 GLY GLY A . n 
A 1 294 CYS 294 294 294 CYS CYS A . n 
A 1 295 GLY 295 295 295 GLY GLY A . n 
A 1 296 ARG 296 296 296 ARG ARG A . n 
A 1 297 TRP 297 297 297 TRP TRP A . n 
A 1 298 VAL 298 298 298 VAL VAL A . n 
A 1 299 ARG 299 299 299 ARG ARG A . n 
A 1 300 LEU 300 300 300 LEU LEU A . n 
A 1 301 LYS 301 301 301 LYS LYS A . n 
A 1 302 ASP 302 302 302 ASP ASP A . n 
A 1 303 GLY 303 303 303 GLY GLY A . n 
A 1 304 THR 304 304 304 THR THR A . n 
A 1 305 GLU 305 305 305 GLU GLU A . n 
A 1 306 CYS 306 306 306 CYS CYS A . n 
A 1 307 GLY 307 307 307 GLY GLY A . n 
A 1 308 GLY 308 308 308 GLY GLY A . n 
A 1 309 PRO 309 309 309 PRO PRO A . n 
A 1 310 GLU 310 310 310 GLU GLU A . n 
A 1 311 TYR 311 311 311 TYR TYR A . n 
A 1 312 GLU 312 312 312 GLU GLU A . n 
A 1 313 THR 313 313 313 THR THR A . n 
A 1 314 LEU 314 314 314 LEU LEU A . n 
A 1 315 TRP 315 315 315 TRP TRP A . n 
A 1 316 CYS 316 316 316 CYS CYS A . n 
A 1 317 PHE 317 317 317 PHE PHE A . n 
A 1 318 GLY 318 318 318 GLY GLY A . n 
A 1 319 SER 319 319 319 SER SER A . n 
A 1 320 ASP 320 320 320 ASP ASP A . n 
A 1 321 CYS 321 321 321 CYS CYS A . n 
A 1 322 GLY 322 322 322 GLY GLY A . n 
A 1 323 SER 323 323 323 SER SER A . n 
A 1 324 TYR 324 324 324 TYR TYR A . n 
A 1 325 ASP 325 325 325 ASP ASP A . n 
A 1 326 LEU 326 326 326 LEU LEU A . n 
A 1 327 ASP 327 327 327 ASP ASP A . n 
A 1 328 ALA 328 328 328 ALA ALA A . n 
A 1 329 ILE 329 329 329 ILE ILE A . n 
A 1 330 ASN 330 330 330 ASN ASN A . n 
A 1 331 GLU 331 331 331 GLU GLU A . n 
A 1 332 ALA 332 332 332 ALA ALA A . n 
A 1 333 ASN 333 333 333 ASN ASN A . n 
A 1 334 MET 334 334 334 MET MET A . n 
A 1 335 LEU 335 335 335 LEU LEU A . n 
A 1 336 CYS 336 336 336 CYS CYS A . n 
A 1 337 ASN 337 337 337 ASN ASN A . n 
A 1 338 GLU 338 338 338 GLU GLU A . n 
A 1 339 TYR 339 339 339 TYR TYR A . n 
A 1 340 GLY 340 340 340 GLY GLY A . n 
A 1 341 ILE 341 341 341 ILE ILE A . n 
A 1 342 ASP 342 342 342 ASP ASP A . n 
A 1 343 THR 343 343 343 THR THR A . n 
A 1 344 ILE 344 344 344 ILE ILE A . n 
A 1 345 THR 345 345 345 THR THR A . n 
A 1 346 CYS 346 346 346 CYS CYS A . n 
A 1 347 GLY 347 347 347 GLY GLY A . n 
A 1 348 ALA 348 348 348 ALA ALA A . n 
A 1 349 THR 349 349 349 THR THR A . n 
A 1 350 ILE 350 350 350 ILE ILE A . n 
A 1 351 ALA 351 351 351 ALA ALA A . n 
A 1 352 ALA 352 352 352 ALA ALA A . n 
A 1 353 ALA 353 353 353 ALA ALA A . n 
A 1 354 MET 354 354 354 MET MET A . n 
A 1 355 GLU 355 355 355 GLU GLU A . n 
A 1 356 LEU 356 356 356 LEU LEU A . n 
A 1 357 TYR 357 357 357 TYR TYR A . n 
A 1 358 GLN 358 358 358 GLN GLN A . n 
A 1 359 ARG 359 359 359 ARG ARG A . n 
A 1 360 GLY 360 360 360 GLY GLY A . n 
A 1 361 TYR 361 361 361 TYR TYR A . n 
A 1 362 ILE 362 362 362 ILE ILE A . n 
A 1 363 LYS 363 363 363 LYS LYS A . n 
A 1 364 ASP 364 364 364 ASP ASP A . n 
A 1 365 GLU 365 365 365 GLU GLU A . n 
A 1 366 GLU 366 366 366 GLU GLU A . n 
A 1 367 ILE 367 367 367 ILE ILE A . n 
A 1 368 ALA 368 368 368 ALA ALA A . n 
A 1 369 GLY 369 369 369 GLY GLY A . n 
A 1 370 ASP 370 370 370 ASP ASP A . n 
A 1 371 ASN 371 371 371 ASN ASN A . n 
A 1 372 LEU 372 372 372 LEU LEU A . n 
A 1 373 SER 373 373 373 SER SER A . n 
A 1 374 LEU 374 374 374 LEU LEU A . n 
A 1 375 LYS 375 375 375 LYS LYS A . n 
A 1 376 TRP 376 376 376 TRP TRP A . n 
A 1 377 GLY 377 377 377 GLY GLY A . n 
A 1 378 ASP 378 378 378 ASP ASP A . n 
A 1 379 THR 379 379 379 THR THR A . n 
A 1 380 GLU 380 380 380 GLU GLU A . n 
A 1 381 SER 381 381 381 SER SER A . n 
A 1 382 MET 382 382 382 MET MET A . n 
A 1 383 ILE 383 383 383 ILE ILE A . n 
A 1 384 GLY 384 384 384 GLY GLY A . n 
A 1 385 TRP 385 385 385 TRP TRP A . n 
A 1 386 ILE 386 386 386 ILE ILE A . n 
A 1 387 LYS 387 387 387 LYS LYS A . n 
A 1 388 ARG 388 388 388 ARG ARG A . n 
A 1 389 MET 389 389 389 MET MET A . n 
A 1 390 VAL 390 390 390 VAL VAL A . n 
A 1 391 TYR 391 391 391 TYR TYR A . n 
A 1 392 SER 392 392 392 SER SER A . n 
A 1 393 GLU 393 393 393 GLU GLU A . n 
A 1 394 GLY 394 394 394 GLY GLY A . n 
A 1 395 PHE 395 395 395 PHE PHE A . n 
A 1 396 GLY 396 396 396 GLY GLY A . n 
A 1 397 ALA 397 397 397 ALA ALA A . n 
A 1 398 LYS 398 398 398 LYS LYS A . n 
A 1 399 MET 399 399 399 MET MET A . n 
A 1 400 THR 400 400 400 THR THR A . n 
A 1 401 ASN 401 401 401 ASN ASN A . n 
A 1 402 GLY 402 402 402 GLY GLY A . n 
A 1 403 SER 403 403 403 SER SER A . n 
A 1 404 TYR 404 404 404 TYR TYR A . n 
A 1 405 ARG 405 405 405 ARG ARG A . n 
A 1 406 LEU 406 406 406 LEU LEU A . n 
A 1 407 CYS 407 407 407 CYS CYS A . n 
A 1 408 GLU 408 408 408 GLU GLU A . n 
A 1 409 GLY 409 409 409 GLY GLY A . n 
A 1 410 TYR 410 410 410 TYR TYR A . n 
A 1 411 GLY 411 411 411 GLY GLY A . n 
A 1 412 ALA 412 412 412 ALA ALA A . n 
A 1 413 PRO 413 413 413 PRO PRO A . n 
A 1 414 GLU 414 414 414 GLU GLU A . n 
A 1 415 TYR 415 415 415 TYR TYR A . n 
A 1 416 SER 416 416 416 SER SER A . n 
A 1 417 MET 417 417 417 MET MET A . n 
A 1 418 THR 418 418 418 THR THR A . n 
A 1 419 VAL 419 419 419 VAL VAL A . n 
A 1 420 LYS 420 420 420 LYS LYS A . n 
A 1 421 LYS 421 421 421 LYS LYS A . n 
A 1 422 GLN 422 422 422 GLN GLN A . n 
A 1 423 GLU 423 423 423 GLU GLU A . n 
A 1 424 ILE 424 424 424 ILE ILE A . n 
A 1 425 PRO 425 425 425 PRO PRO A . n 
A 1 426 ALA 426 426 426 ALA ALA A . n 
A 1 427 TYR 427 427 427 TYR TYR A . n 
A 1 428 ASP 428 428 428 ASP ASP A . n 
A 1 429 PRO 429 429 429 PRO PRO A . n 
A 1 430 ARG 430 430 430 ARG ARG A . n 
A 1 431 GLY 431 431 431 GLY GLY A . n 
A 1 432 ILE 432 432 432 ILE ILE A . n 
A 1 433 GLN 433 433 433 GLN GLN A . n 
A 1 434 GLY 434 434 434 GLY GLY A . n 
A 1 435 HIS 435 435 435 HIS HIS A . n 
A 1 436 GLY 436 436 436 GLY GLY A . n 
A 1 437 ILE 437 437 437 ILE ILE A . n 
A 1 438 THR 438 438 438 THR THR A . n 
A 1 439 TYR 439 439 439 TYR TYR A . n 
A 1 440 ALA 440 440 440 ALA ALA A . n 
A 1 441 VAL 441 441 441 VAL VAL A . n 
A 1 442 ASN 442 442 442 ASN ASN A . n 
A 1 443 ASN 443 443 443 ASN ASN A . n 
A 1 444 ARG 444 444 444 ARG ARG A . n 
A 1 445 GLY 445 445 445 GLY GLY A . n 
A 1 446 GLY 446 446 446 GLY GLY A . n 
A 1 447 CYS 447 447 447 CYS CYS A . n 
A 1 448 HIS 448 448 448 HIS HIS A . n 
A 1 449 ILE 449 449 449 ILE ILE A . n 
A 1 450 LYS 450 450 450 LYS LYS A . n 
A 1 451 GLY 451 451 451 GLY GLY A . n 
A 1 452 TYR 452 452 452 TYR TYR A . n 
A 1 453 MET 453 453 453 MET MET A . n 
A 1 454 ILE 454 454 454 ILE ILE A . n 
A 1 455 ASN 455 455 455 ASN ASN A . n 
A 1 456 PRO 456 456 456 PRO PRO A . n 
A 1 457 GLU 457 457 457 GLU GLU A . n 
A 1 458 ILE 458 458 458 ILE ILE A . n 
A 1 459 LEU 459 459 459 LEU LEU A . n 
A 1 460 GLY 460 460 460 GLY GLY A . n 
A 1 461 TYR 461 461 461 TYR TYR A . n 
A 1 462 PRO 462 462 462 PRO PRO A . n 
A 1 463 GLU 463 463 463 GLU GLU A . n 
A 1 464 LYS 464 464 464 LYS LYS A . n 
A 1 465 LEU 465 465 465 LEU LEU A . n 
A 1 466 ASP 466 466 466 ASP ASP A . n 
A 1 467 ARG 467 467 467 ARG ARG A . n 
A 1 468 PHE 468 468 468 PHE PHE A . n 
A 1 469 ALA 469 469 469 ALA ALA A . n 
A 1 470 LEU 470 470 470 LEU LEU A . n 
A 1 471 ASP 471 471 471 ASP ASP A . n 
A 1 472 GLY 472 472 472 GLY GLY A . n 
A 1 473 LYS 473 473 473 LYS LYS A . n 
A 1 474 ALA 474 474 474 ALA ALA A . n 
A 1 475 ALA 475 475 475 ALA ALA A . n 
A 1 476 TYR 476 476 476 TYR TYR A . n 
A 1 477 ALA 477 477 477 ALA ALA A . n 
A 1 478 LYS 478 478 478 LYS LYS A . n 
A 1 479 LEU 479 479 479 LEU LEU A . n 
A 1 480 PHE 480 480 480 PHE PHE A . n 
A 1 481 HIS 481 481 481 HIS HIS A . n 
A 1 482 ASP 482 482 482 ASP ASP A . n 
A 1 483 LEU 483 483 483 LEU LEU A . n 
A 1 484 THR 484 484 484 THR THR A . n 
A 1 485 ALA 485 485 485 ALA ALA A . n 
A 1 486 VAL 486 486 486 VAL VAL A . n 
A 1 487 ILE 487 487 487 ILE ILE A . n 
A 1 488 ASP 488 488 488 ASP ASP A . n 
A 1 489 SER 489 489 489 SER SER A . n 
A 1 490 LEU 490 490 490 LEU LEU A . n 
A 1 491 GLY 491 491 491 GLY GLY A . n 
A 1 492 LEU 492 492 492 LEU LEU A . n 
A 1 493 CYS 493 493 493 CYS CYS A . n 
A 1 494 ILE 494 494 494 ILE ILE A . n 
A 1 495 PHE 495 495 495 PHE PHE A . n 
A 1 496 THR 496 496 496 THR THR A . n 
A 1 497 THR 497 497 497 THR THR A . n 
A 1 498 PHE 498 498 498 PHE PHE A . n 
A 1 499 GLY 499 499 499 GLY GLY A . n 
A 1 500 LEU 500 500 500 LEU LEU A . n 
A 1 501 GLY 501 501 501 GLY GLY A . n 
A 1 502 ILE 502 502 502 ILE ILE A . n 
A 1 503 GLN 503 503 503 GLN GLN A . n 
A 1 504 ASP 504 504 504 ASP ASP A . n 
A 1 505 TYR 505 505 505 TYR TYR A . n 
A 1 506 VAL 506 506 506 VAL VAL A . n 
A 1 507 ASP 507 507 507 ASP ASP A . n 
A 1 508 MET 508 508 508 MET MET A . n 
A 1 509 TYR 509 509 509 TYR TYR A . n 
A 1 510 ASN 510 510 510 ASN ASN A . n 
A 1 511 ALA 511 511 511 ALA ALA A . n 
A 1 512 VAL 512 512 512 VAL VAL A . n 
A 1 513 VAL 513 513 513 VAL VAL A . n 
A 1 514 GLY 514 514 514 GLY GLY A . n 
A 1 515 GLU 515 515 515 GLU GLU A . n 
A 1 516 SER 516 516 516 SER SER A . n 
A 1 517 THR 517 517 517 THR THR A . n 
A 1 518 TYR 518 518 518 TYR TYR A . n 
A 1 519 ASP 519 519 519 ASP ASP A . n 
A 1 520 ALA 520 520 520 ALA ALA A . n 
A 1 521 ASP 521 521 521 ASP ASP A . n 
A 1 522 SER 522 522 522 SER SER A . n 
A 1 523 LEU 523 523 523 LEU LEU A . n 
A 1 524 LEU 524 524 524 LEU LEU A . n 
A 1 525 GLU 525 525 525 GLU GLU A . n 
A 1 526 ALA 526 526 526 ALA ALA A . n 
A 1 527 GLY 527 527 527 GLY GLY A . n 
A 1 528 ASP 528 528 528 ASP ASP A . n 
A 1 529 ARG 529 529 529 ARG ARG A . n 
A 1 530 ILE 530 530 530 ILE ILE A . n 
A 1 531 TRP 531 531 531 TRP TRP A . n 
A 1 532 THR 532 532 532 THR THR A . n 
A 1 533 LEU 533 533 533 LEU LEU A . n 
A 1 534 GLU 534 534 534 GLU GLU A . n 
A 1 535 LYS 535 535 535 LYS LYS A . n 
A 1 536 LEU 536 536 536 LEU LEU A . n 
A 1 537 PHE 537 537 537 PHE PHE A . n 
A 1 538 ASN 538 538 538 ASN ASN A . n 
A 1 539 LEU 539 539 539 LEU LEU A . n 
A 1 540 ALA 540 540 540 ALA ALA A . n 
A 1 541 ALA 541 541 541 ALA ALA A . n 
A 1 542 GLY 542 542 542 GLY GLY A . n 
A 1 543 ILE 543 543 543 ILE ILE A . n 
A 1 544 ASP 544 544 544 ASP ASP A . n 
A 1 545 SER 545 545 545 SER SER A . n 
A 1 546 SER 546 546 546 SER SER A . n 
A 1 547 GLN 547 547 547 GLN GLN A . n 
A 1 548 ASP 548 548 548 ASP ASP A . n 
A 1 549 THR 549 549 549 THR THR A . n 
A 1 550 LEU 550 550 550 LEU LEU A . n 
A 1 551 PRO 551 551 551 PRO PRO A . n 
A 1 552 LYS 552 552 552 LYS LYS A . n 
A 1 553 ARG 553 553 553 ARG ARG A . n 
A 1 554 LEU 554 554 554 LEU LEU A . n 
A 1 555 LEU 555 555 555 LEU LEU A . n 
A 1 556 GLU 556 556 556 GLU GLU A . n 
A 1 557 GLU 557 557 557 GLU GLU A . n 
A 1 558 PRO 558 558 558 PRO PRO A . n 
A 1 559 ILE 559 559 559 ILE ILE A . n 
A 1 560 PRO 560 560 560 PRO PRO A . n 
A 1 561 ASP 561 561 561 ASP ASP A . n 
A 1 562 GLY 562 562 562 GLY GLY A . n 
A 1 563 PRO 563 563 563 PRO PRO A . n 
A 1 564 SER 564 564 564 SER SER A . n 
A 1 565 LYS 565 565 565 LYS LYS A . n 
A 1 566 GLY 566 566 566 GLY GLY A . n 
A 1 567 GLU 567 567 567 GLU GLU A . n 
A 1 568 VAL 568 568 568 VAL VAL A . n 
A 1 569 HIS 569 569 569 HIS HIS A . n 
A 1 570 ARG 570 570 570 ARG ARG A . n 
A 1 571 LEU 571 571 571 LEU LEU A . n 
A 1 572 ASP 572 572 572 ASP ASP A . n 
A 1 573 VAL 573 573 573 VAL VAL A . n 
A 1 574 LEU 574 574 574 LEU LEU A . n 
A 1 575 LEU 575 575 575 LEU LEU A . n 
A 1 576 PRO 576 576 576 PRO PRO A . n 
A 1 577 GLU 577 577 577 GLU GLU A . n 
A 1 578 TYR 578 578 578 TYR TYR A . n 
A 1 579 TYR 579 579 579 TYR TYR A . n 
A 1 580 SER 580 580 580 SER SER A . n 
A 1 581 VAL 581 581 581 VAL VAL A . n 
A 1 582 ARG 582 582 582 ARG ARG A . n 
A 1 583 GLY 583 583 583 GLY GLY A . n 
A 1 584 TRP 584 584 584 TRP TRP A . n 
A 1 585 SER 585 585 585 SER SER A . n 
A 1 586 LYS 586 586 586 LYS LYS A . n 
A 1 587 GLU 587 587 587 GLU GLU A . n 
A 1 588 GLY 588 588 588 GLY GLY A . n 
A 1 589 ILE 589 589 589 ILE ILE A . n 
A 1 590 PRO 590 590 590 PRO PRO A . n 
A 1 591 THR 591 591 591 THR THR A . n 
A 1 592 GLU 592 592 592 GLU GLU A . n 
A 1 593 GLU 593 593 593 GLU GLU A . n 
A 1 594 THR 594 594 594 THR THR A . n 
A 1 595 LEU 595 595 595 LEU LEU A . n 
A 1 596 LYS 596 596 596 LYS LYS A . n 
A 1 597 LYS 597 597 597 LYS LYS A . n 
A 1 598 LEU 598 598 598 LEU LEU A . n 
A 1 599 GLY 599 599 599 GLY GLY A . n 
A 1 600 LEU 600 600 600 LEU LEU A . n 
A 1 601 ASP 601 601 601 ASP ASP A . n 
A 1 602 GLU 602 602 602 GLU GLU A . n 
A 1 603 TYR 603 603 603 TYR TYR A . n 
A 1 604 ILE 604 604 604 ILE ILE A . n 
A 1 605 GLY 605 605 605 GLY GLY A . n 
A 1 606 LYS 606 606 606 LYS LYS A . n 
A 1 607 PHE 607 607 607 PHE PHE A . n 
B 1 1   MET 1   1   1   MET MET B . n 
B 1 2   TYR 2   2   2   TYR TYR B . n 
B 1 3   GLY 3   3   3   GLY GLY B . n 
B 1 4   TYR 4   4   4   TYR TYR B . n 
B 1 5   ASP 5   5   5   ASP ASP B . n 
B 1 6   GLY 6   6   6   GLY GLY B . n 
B 1 7   LYS 7   7   7   LYS LYS B . n 
B 1 8   VAL 8   8   8   VAL VAL B . n 
B 1 9   LEU 9   9   9   LEU LEU B . n 
B 1 10  ARG 10  10  10  ARG ARG B . n 
B 1 11  ILE 11  11  11  ILE ILE B . n 
B 1 12  ASN 12  12  12  ASN ASN B . n 
B 1 13  LEU 13  13  13  LEU LEU B . n 
B 1 14  LYS 14  14  14  LYS LYS B . n 
B 1 15  GLU 15  15  15  GLU GLU B . n 
B 1 16  ARG 16  16  16  ARG ARG B . n 
B 1 17  THR 17  17  17  THR THR B . n 
B 1 18  CYS 18  18  18  CYS CYS B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  SER 20  20  20  SER SER B . n 
B 1 21  GLU 21  21  21  GLU GLU B . n 
B 1 22  ASN 22  22  22  ASN ASN B . n 
B 1 23  LEU 23  23  23  LEU LEU B . n 
B 1 24  ASP 24  24  24  ASP ASP B . n 
B 1 25  LEU 25  25  25  LEU LEU B . n 
B 1 26  ASP 26  26  26  ASP ASP B . n 
B 1 27  LYS 27  27  27  LYS LYS B . n 
B 1 28  ALA 28  28  28  ALA ALA B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  LYS 30  30  30  LYS LYS B . n 
B 1 31  PHE 31  31  31  PHE PHE B . n 
B 1 32  ILE 32  32  32  ILE ILE B . n 
B 1 33  GLY 33  33  33  GLY GLY B . n 
B 1 34  CYS 34  34  34  CYS CYS B . n 
B 1 35  ARG 35  35  35  ARG ARG B . n 
B 1 36  GLY 36  36  36  GLY GLY B . n 
B 1 37  LEU 37  37  37  LEU LEU B . n 
B 1 38  GLY 38  38  38  GLY GLY B . n 
B 1 39  VAL 39  39  39  VAL VAL B . n 
B 1 40  LYS 40  40  40  LYS LYS B . n 
B 1 41  THR 41  41  41  THR THR B . n 
B 1 42  LEU 42  42  42  LEU LEU B . n 
B 1 43  PHE 43  43  43  PHE PHE B . n 
B 1 44  ASP 44  44  44  ASP ASP B . n 
B 1 45  GLU 45  45  45  GLU GLU B . n 
B 1 46  ILE 46  46  46  ILE ILE B . n 
B 1 47  ASP 47  47  47  ASP ASP B . n 
B 1 48  PRO 48  48  48  PRO PRO B . n 
B 1 49  LYS 49  49  49  LYS LYS B . n 
B 1 50  ILE 50  50  50  ILE ILE B . n 
B 1 51  ASP 51  51  51  ASP ASP B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  SER 54  54  54  SER SER B . n 
B 1 55  PRO 55  55  55  PRO PRO B . n 
B 1 56  GLU 56  56  56  GLU GLU B . n 
B 1 57  ASN 57  57  57  ASN ASN B . n 
B 1 58  LYS 58  58  58  LYS LYS B . n 
B 1 59  PHE 59  59  59  PHE PHE B . n 
B 1 60  ILE 60  60  60  ILE ILE B . n 
B 1 61  ILE 61  61  61  ILE ILE B . n 
B 1 62  VAL 62  62  62  VAL VAL B . n 
B 1 63  THR 63  63  63  THR THR B . n 
B 1 64  GLY 64  64  64  GLY GLY B . n 
B 1 65  PRO 65  65  65  PRO PRO B . n 
B 1 66  LEU 66  66  66  LEU LEU B . n 
B 1 67  THR 67  67  67  THR THR B . n 
B 1 68  GLY 68  68  68  GLY GLY B . n 
B 1 69  ALA 69  69  69  ALA ALA B . n 
B 1 70  PRO 70  70  70  PRO PRO B . n 
B 1 71  VAL 71  71  71  VAL VAL B . n 
B 1 72  PRO 72  72  72  PRO PRO B . n 
B 1 73  THR 73  73  73  THR THR B . n 
B 1 74  SER 74  74  74  SER SER B . n 
B 1 75  GLY 75  75  75  GLY GLY B . n 
B 1 76  ARG 76  76  76  ARG ARG B . n 
B 1 77  PHE 77  77  77  PHE PHE B . n 
B 1 78  MET 78  78  78  MET MET B . n 
B 1 79  VAL 79  79  79  VAL VAL B . n 
B 1 80  VAL 80  80  80  VAL VAL B . n 
B 1 81  THR 81  81  81  THR THR B . n 
B 1 82  LYS 82  82  82  LYS LYS B . n 
B 1 83  ALA 83  83  83  ALA ALA B . n 
B 1 84  PRO 84  84  84  PRO PRO B . n 
B 1 85  LEU 85  85  85  LEU LEU B . n 
B 1 86  THR 86  86  86  THR THR B . n 
B 1 87  GLY 87  87  87  GLY GLY B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  ILE 89  89  89  ILE ILE B . n 
B 1 90  GLY 90  90  90  GLY GLY B . n 
B 1 91  ILE 91  91  91  ILE ILE B . n 
B 1 92  SER 92  92  92  SER SER B . n 
B 1 93  ASN 93  93  93  ASN ASN B . n 
B 1 94  SER 94  94  94  SER SER B . n 
B 1 95  GLY 95  95  95  GLY GLY B . n 
B 1 96  GLY 96  96  96  GLY GLY B . n 
B 1 97  LYS 97  97  97  LYS LYS B . n 
B 1 98  TRP 98  98  98  TRP TRP B . n 
B 1 99  GLY 99  99  99  GLY GLY B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASP 101 101 101 ASP ASP B . n 
B 1 102 LEU 102 102 102 LEU LEU B . n 
B 1 103 LYS 103 103 103 LYS LYS B . n 
B 1 104 LYS 104 104 104 LYS LYS B . n 
B 1 105 ALA 105 105 105 ALA ALA B . n 
B 1 106 GLY 106 106 106 GLY GLY B . n 
B 1 107 TRP 107 107 107 TRP TRP B . n 
B 1 108 ASP 108 108 108 ASP ASP B . n 
B 1 109 MET 109 109 109 MET MET B . n 
B 1 110 ILE 110 110 110 ILE ILE B . n 
B 1 111 ILE 111 111 111 ILE ILE B . n 
B 1 112 VAL 112 112 112 VAL VAL B . n 
B 1 113 GLU 113 113 113 GLU GLU B . n 
B 1 114 ASP 114 114 114 ASP ASP B . n 
B 1 115 LYS 115 115 115 LYS LYS B . n 
B 1 116 ALA 116 116 116 ALA ALA B . n 
B 1 117 ASP 117 117 117 ASP ASP B . n 
B 1 118 SER 118 118 118 SER SER B . n 
B 1 119 PRO 119 119 119 PRO PRO B . n 
B 1 120 VAL 120 120 120 VAL VAL B . n 
B 1 121 TYR 121 121 121 TYR TYR B . n 
B 1 122 ILE 122 122 122 ILE ILE B . n 
B 1 123 GLU 123 123 123 GLU GLU B . n 
B 1 124 ILE 124 124 124 ILE ILE B . n 
B 1 125 VAL 125 125 125 VAL VAL B . n 
B 1 126 ASP 126 126 126 ASP ASP B . n 
B 1 127 ASP 127 127 127 ASP ASP B . n 
B 1 128 LYS 128 128 128 LYS LYS B . n 
B 1 129 VAL 129 129 129 VAL VAL B . n 
B 1 130 GLU 130 130 130 GLU GLU B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 LYS 132 132 132 LYS LYS B . n 
B 1 133 ASP 133 133 133 ASP ASP B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 SER 135 135 135 SER SER B . n 
B 1 136 GLN 136 136 136 GLN GLN B . n 
B 1 137 LEU 137 137 137 LEU LEU B . n 
B 1 138 TRP 138 138 138 TRP TRP B . n 
B 1 139 GLY 139 139 139 GLY GLY B . n 
B 1 140 LYS 140 140 140 LYS LYS B . n 
B 1 141 VAL 141 141 141 VAL VAL B . n 
B 1 142 THR 142 142 142 THR THR B . n 
B 1 143 SER 143 143 143 SER SER B . n 
B 1 144 GLU 144 144 144 GLU GLU B . n 
B 1 145 THR 145 145 145 THR THR B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 LYS 147 147 147 LYS LYS B . n 
B 1 148 GLU 148 148 148 GLU GLU B . n 
B 1 149 LEU 149 149 149 LEU LEU B . n 
B 1 150 GLU 150 150 150 GLU GLU B . n 
B 1 151 LYS 151 151 151 LYS LYS B . n 
B 1 152 ILE 152 152 152 ILE ILE B . n 
B 1 153 THR 153 153 153 THR THR B . n 
B 1 154 GLU 154 154 154 GLU GLU B . n 
B 1 155 ASN 155 155 155 ASN ASN B . n 
B 1 156 LYS 156 156 156 LYS LYS B . n 
B 1 157 SER 157 157 157 SER SER B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 VAL 159 159 159 VAL VAL B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 CYS 161 161 161 CYS CYS B . n 
B 1 162 ILE 162 162 162 ILE ILE B . n 
B 1 163 GLY 163 163 163 GLY GLY B . n 
B 1 164 PRO 164 164 164 PRO PRO B . n 
B 1 165 ALA 165 165 165 ALA ALA B . n 
B 1 166 GLY 166 166 166 GLY GLY B . n 
B 1 167 GLU 167 167 167 GLU GLU B . n 
B 1 168 ARG 168 168 168 ARG ARG B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
B 1 170 SER 170 170 170 SER SER B . n 
B 1 171 LEU 171 171 171 LEU LEU B . n 
B 1 172 MET 172 172 172 MET MET B . n 
B 1 173 ALA 173 173 173 ALA ALA B . n 
B 1 174 ALA 174 174 174 ALA ALA B . n 
B 1 175 VAL 175 175 175 VAL VAL B . n 
B 1 176 MET 176 176 176 MET MET B . n 
B 1 177 ASN 177 177 177 ASN ASN B . n 
B 1 178 ASP 178 178 178 ASP ASP B . n 
B 1 179 VAL 179 179 179 VAL VAL B . n 
B 1 180 ASP 180 180 180 ASP ASP B . n 
B 1 181 ARG 181 181 181 ARG ARG B . n 
B 1 182 THR 182 182 182 THR THR B . n 
B 1 183 ALA 183 183 183 ALA ALA B . n 
B 1 184 ALA 184 184 184 ALA ALA B . n 
B 1 185 ARG 185 185 185 ARG ARG B . n 
B 1 186 GLY 186 186 186 GLY GLY B . n 
B 1 187 GLY 187 187 187 GLY GLY B . n 
B 1 188 VAL 188 188 188 VAL VAL B . n 
B 1 189 GLY 189 189 189 GLY GLY B . n 
B 1 190 ALA 190 190 190 ALA ALA B . n 
B 1 191 VAL 191 191 191 VAL VAL B . n 
B 1 192 MET 192 192 192 MET MET B . n 
B 1 193 GLY 193 193 193 GLY GLY B . n 
B 1 194 SER 194 194 194 SER SER B . n 
B 1 195 LYS 195 195 195 LYS LYS B . n 
B 1 196 ASN 196 196 196 ASN ASN B . n 
B 1 197 LEU 197 197 197 LEU LEU B . n 
B 1 198 LYS 198 198 198 LYS LYS B . n 
B 1 199 ALA 199 199 199 ALA ALA B . n 
B 1 200 ILE 200 200 200 ILE ILE B . n 
B 1 201 THR 201 201 201 THR THR B . n 
B 1 202 VAL 202 202 202 VAL VAL B . n 
B 1 203 LYS 203 203 203 LYS LYS B . n 
B 1 204 GLY 204 204 204 GLY GLY B . n 
B 1 205 THR 205 205 205 THR THR B . n 
B 1 206 GLY 206 206 206 GLY GLY B . n 
B 1 207 LYS 207 207 207 LYS LYS B . n 
B 1 208 ILE 208 208 208 ILE ILE B . n 
B 1 209 ALA 209 209 209 ALA ALA B . n 
B 1 210 LEU 210 210 210 LEU LEU B . n 
B 1 211 ALA 211 211 211 ALA ALA B . n 
B 1 212 ASP 212 212 212 ASP ASP B . n 
B 1 213 LYS 213 213 213 LYS LYS B . n 
B 1 214 GLU 214 214 214 GLU GLU B . n 
B 1 215 LYS 215 215 215 LYS LYS B . n 
B 1 216 VAL 216 216 216 VAL VAL B . n 
B 1 217 LYS 217 217 217 LYS LYS B . n 
B 1 218 LYS 218 218 218 LYS LYS B . n 
B 1 219 VAL 219 219 219 VAL VAL B . n 
B 1 220 SER 220 220 220 SER SER B . n 
B 1 221 VAL 221 221 221 VAL VAL B . n 
B 1 222 GLU 222 222 222 GLU GLU B . n 
B 1 223 LYS 223 223 223 LYS LYS B . n 
B 1 224 ILE 224 224 224 ILE ILE B . n 
B 1 225 THR 225 225 225 THR THR B . n 
B 1 226 THR 226 226 226 THR THR B . n 
B 1 227 LEU 227 227 227 LEU LEU B . n 
B 1 228 LYS 228 228 228 LYS LYS B . n 
B 1 229 ASN 229 229 229 ASN ASN B . n 
B 1 230 ASP 230 230 230 ASP ASP B . n 
B 1 231 PRO 231 231 231 PRO PRO B . n 
B 1 232 VAL 232 232 232 VAL VAL B . n 
B 1 233 ALA 233 233 233 ALA ALA B . n 
B 1 234 GLY 234 234 234 GLY GLY B . n 
B 1 235 GLN 235 235 235 GLN GLN B . n 
B 1 236 GLY 236 236 236 GLY GLY B . n 
B 1 237 MET 237 237 237 MET MET B . n 
B 1 238 PRO 238 238 238 PRO PRO B . n 
B 1 239 THR 239 239 239 THR THR B . n 
B 1 240 TYR 240 240 240 TYR TYR B . n 
B 1 241 GLY 241 241 241 GLY GLY B . n 
B 1 242 THR 242 242 242 THR THR B . n 
B 1 243 ALA 243 243 243 ALA ALA B . n 
B 1 244 ILE 244 244 244 ILE ILE B . n 
B 1 245 LEU 245 245 245 LEU LEU B . n 
B 1 246 VAL 246 246 246 VAL VAL B . n 
B 1 247 ASN 247 247 247 ASN ASN B . n 
B 1 248 ILE 248 248 248 ILE ILE B . n 
B 1 249 ILE 249 249 249 ILE ILE B . n 
B 1 250 ASN 250 250 250 ASN ASN B . n 
B 1 251 GLU 251 251 251 GLU GLU B . n 
B 1 252 ASN 252 252 252 ASN ASN B . n 
B 1 253 GLY 253 253 253 GLY GLY B . n 
B 1 254 VAL 254 254 254 VAL VAL B . n 
B 1 255 HIS 255 255 255 HIS HIS B . n 
B 1 256 PRO 256 256 256 PRO PRO B . n 
B 1 257 VAL 257 257 257 VAL VAL B . n 
B 1 258 LYS 258 258 258 LYS LYS B . n 
B 1 259 ASN 259 259 259 ASN ASN B . n 
B 1 260 PHE 260 260 260 PHE PHE B . n 
B 1 261 GLN 261 261 261 GLN GLN B . n 
B 1 262 GLU 262 262 262 GLU GLU B . n 
B 1 263 SER 263 263 263 SER SER B . n 
B 1 264 TYR 264 264 264 TYR TYR B . n 
B 1 265 THR 265 265 265 THR THR B . n 
B 1 266 ASN 266 266 266 ASN ASN B . n 
B 1 267 GLN 267 267 267 GLN GLN B . n 
B 1 268 ALA 268 268 268 ALA ALA B . n 
B 1 269 ASP 269 269 269 ASP ASP B . n 
B 1 270 LYS 270 270 270 LYS LYS B . n 
B 1 271 ILE 271 271 271 ILE ILE B . n 
B 1 272 SER 272 272 272 SER SER B . n 
B 1 273 GLY 273 273 273 GLY GLY B . n 
B 1 274 GLU 274 274 274 GLU GLU B . n 
B 1 275 THR 275 275 275 THR THR B . n 
B 1 276 LEU 276 276 276 LEU LEU B . n 
B 1 277 THR 277 277 277 THR THR B . n 
B 1 278 ALA 278 278 278 ALA ALA B . n 
B 1 279 ASN 279 279 279 ASN ASN B . n 
B 1 280 GLN 280 280 280 GLN GLN B . n 
B 1 281 LEU 281 281 281 LEU LEU B . n 
B 1 282 VAL 282 282 282 VAL VAL B . n 
B 1 283 ARG 283 283 283 ARG ARG B . n 
B 1 284 LYS 284 284 284 LYS LYS B . n 
B 1 285 ASN 285 285 285 ASN ASN B . n 
B 1 286 PRO 286 286 286 PRO PRO B . n 
B 1 287 CYS 287 287 287 CYS CYS B . n 
B 1 288 TYR 288 288 288 TYR TYR B . n 
B 1 289 SER 289 289 289 SER SER B . n 
B 1 290 CYS 290 290 290 CYS CYS B . n 
B 1 291 PRO 291 291 291 PRO PRO B . n 
B 1 292 ILE 292 292 292 ILE ILE B . n 
B 1 293 GLY 293 293 293 GLY GLY B . n 
B 1 294 CYS 294 294 294 CYS CYS B . n 
B 1 295 GLY 295 295 295 GLY GLY B . n 
B 1 296 ARG 296 296 296 ARG ARG B . n 
B 1 297 TRP 297 297 297 TRP TRP B . n 
B 1 298 VAL 298 298 298 VAL VAL B . n 
B 1 299 ARG 299 299 299 ARG ARG B . n 
B 1 300 LEU 300 300 300 LEU LEU B . n 
B 1 301 LYS 301 301 301 LYS LYS B . n 
B 1 302 ASP 302 302 302 ASP ASP B . n 
B 1 303 GLY 303 303 303 GLY GLY B . n 
B 1 304 THR 304 304 304 THR THR B . n 
B 1 305 GLU 305 305 305 GLU GLU B . n 
B 1 306 CYS 306 306 306 CYS CYS B . n 
B 1 307 GLY 307 307 307 GLY GLY B . n 
B 1 308 GLY 308 308 308 GLY GLY B . n 
B 1 309 PRO 309 309 309 PRO PRO B . n 
B 1 310 GLU 310 310 310 GLU GLU B . n 
B 1 311 TYR 311 311 311 TYR TYR B . n 
B 1 312 GLU 312 312 312 GLU GLU B . n 
B 1 313 THR 313 313 313 THR THR B . n 
B 1 314 LEU 314 314 314 LEU LEU B . n 
B 1 315 TRP 315 315 315 TRP TRP B . n 
B 1 316 CYS 316 316 316 CYS CYS B . n 
B 1 317 PHE 317 317 317 PHE PHE B . n 
B 1 318 GLY 318 318 318 GLY GLY B . n 
B 1 319 SER 319 319 319 SER SER B . n 
B 1 320 ASP 320 320 320 ASP ASP B . n 
B 1 321 CYS 321 321 321 CYS CYS B . n 
B 1 322 GLY 322 322 322 GLY GLY B . n 
B 1 323 SER 323 323 323 SER SER B . n 
B 1 324 TYR 324 324 324 TYR TYR B . n 
B 1 325 ASP 325 325 325 ASP ASP B . n 
B 1 326 LEU 326 326 326 LEU LEU B . n 
B 1 327 ASP 327 327 327 ASP ASP B . n 
B 1 328 ALA 328 328 328 ALA ALA B . n 
B 1 329 ILE 329 329 329 ILE ILE B . n 
B 1 330 ASN 330 330 330 ASN ASN B . n 
B 1 331 GLU 331 331 331 GLU GLU B . n 
B 1 332 ALA 332 332 332 ALA ALA B . n 
B 1 333 ASN 333 333 333 ASN ASN B . n 
B 1 334 MET 334 334 334 MET MET B . n 
B 1 335 LEU 335 335 335 LEU LEU B . n 
B 1 336 CYS 336 336 336 CYS CYS B . n 
B 1 337 ASN 337 337 337 ASN ASN B . n 
B 1 338 GLU 338 338 338 GLU GLU B . n 
B 1 339 TYR 339 339 339 TYR TYR B . n 
B 1 340 GLY 340 340 340 GLY GLY B . n 
B 1 341 ILE 341 341 341 ILE ILE B . n 
B 1 342 ASP 342 342 342 ASP ASP B . n 
B 1 343 THR 343 343 343 THR THR B . n 
B 1 344 ILE 344 344 344 ILE ILE B . n 
B 1 345 THR 345 345 345 THR THR B . n 
B 1 346 CYS 346 346 346 CYS CYS B . n 
B 1 347 GLY 347 347 347 GLY GLY B . n 
B 1 348 ALA 348 348 348 ALA ALA B . n 
B 1 349 THR 349 349 349 THR THR B . n 
B 1 350 ILE 350 350 350 ILE ILE B . n 
B 1 351 ALA 351 351 351 ALA ALA B . n 
B 1 352 ALA 352 352 352 ALA ALA B . n 
B 1 353 ALA 353 353 353 ALA ALA B . n 
B 1 354 MET 354 354 354 MET MET B . n 
B 1 355 GLU 355 355 355 GLU GLU B . n 
B 1 356 LEU 356 356 356 LEU LEU B . n 
B 1 357 TYR 357 357 357 TYR TYR B . n 
B 1 358 GLN 358 358 358 GLN GLN B . n 
B 1 359 ARG 359 359 359 ARG ARG B . n 
B 1 360 GLY 360 360 360 GLY GLY B . n 
B 1 361 TYR 361 361 361 TYR TYR B . n 
B 1 362 ILE 362 362 362 ILE ILE B . n 
B 1 363 LYS 363 363 363 LYS LYS B . n 
B 1 364 ASP 364 364 364 ASP ASP B . n 
B 1 365 GLU 365 365 365 GLU GLU B . n 
B 1 366 GLU 366 366 366 GLU GLU B . n 
B 1 367 ILE 367 367 367 ILE ILE B . n 
B 1 368 ALA 368 368 368 ALA ALA B . n 
B 1 369 GLY 369 369 369 GLY GLY B . n 
B 1 370 ASP 370 370 370 ASP ASP B . n 
B 1 371 ASN 371 371 371 ASN ASN B . n 
B 1 372 LEU 372 372 372 LEU LEU B . n 
B 1 373 SER 373 373 373 SER SER B . n 
B 1 374 LEU 374 374 374 LEU LEU B . n 
B 1 375 LYS 375 375 375 LYS LYS B . n 
B 1 376 TRP 376 376 376 TRP TRP B . n 
B 1 377 GLY 377 377 377 GLY GLY B . n 
B 1 378 ASP 378 378 378 ASP ASP B . n 
B 1 379 THR 379 379 379 THR THR B . n 
B 1 380 GLU 380 380 380 GLU GLU B . n 
B 1 381 SER 381 381 381 SER SER B . n 
B 1 382 MET 382 382 382 MET MET B . n 
B 1 383 ILE 383 383 383 ILE ILE B . n 
B 1 384 GLY 384 384 384 GLY GLY B . n 
B 1 385 TRP 385 385 385 TRP TRP B . n 
B 1 386 ILE 386 386 386 ILE ILE B . n 
B 1 387 LYS 387 387 387 LYS LYS B . n 
B 1 388 ARG 388 388 388 ARG ARG B . n 
B 1 389 MET 389 389 389 MET MET B . n 
B 1 390 VAL 390 390 390 VAL VAL B . n 
B 1 391 TYR 391 391 391 TYR TYR B . n 
B 1 392 SER 392 392 392 SER SER B . n 
B 1 393 GLU 393 393 393 GLU GLU B . n 
B 1 394 GLY 394 394 394 GLY GLY B . n 
B 1 395 PHE 395 395 395 PHE PHE B . n 
B 1 396 GLY 396 396 396 GLY GLY B . n 
B 1 397 ALA 397 397 397 ALA ALA B . n 
B 1 398 LYS 398 398 398 LYS LYS B . n 
B 1 399 MET 399 399 399 MET MET B . n 
B 1 400 THR 400 400 400 THR THR B . n 
B 1 401 ASN 401 401 401 ASN ASN B . n 
B 1 402 GLY 402 402 402 GLY GLY B . n 
B 1 403 SER 403 403 403 SER SER B . n 
B 1 404 TYR 404 404 404 TYR TYR B . n 
B 1 405 ARG 405 405 405 ARG ARG B . n 
B 1 406 LEU 406 406 406 LEU LEU B . n 
B 1 407 CYS 407 407 407 CYS CYS B . n 
B 1 408 GLU 408 408 408 GLU GLU B . n 
B 1 409 GLY 409 409 409 GLY GLY B . n 
B 1 410 TYR 410 410 410 TYR TYR B . n 
B 1 411 GLY 411 411 411 GLY GLY B . n 
B 1 412 ALA 412 412 412 ALA ALA B . n 
B 1 413 PRO 413 413 413 PRO PRO B . n 
B 1 414 GLU 414 414 414 GLU GLU B . n 
B 1 415 TYR 415 415 415 TYR TYR B . n 
B 1 416 SER 416 416 416 SER SER B . n 
B 1 417 MET 417 417 417 MET MET B . n 
B 1 418 THR 418 418 418 THR THR B . n 
B 1 419 VAL 419 419 419 VAL VAL B . n 
B 1 420 LYS 420 420 420 LYS LYS B . n 
B 1 421 LYS 421 421 421 LYS LYS B . n 
B 1 422 GLN 422 422 422 GLN GLN B . n 
B 1 423 GLU 423 423 423 GLU GLU B . n 
B 1 424 ILE 424 424 424 ILE ILE B . n 
B 1 425 PRO 425 425 425 PRO PRO B . n 
B 1 426 ALA 426 426 426 ALA ALA B . n 
B 1 427 TYR 427 427 427 TYR TYR B . n 
B 1 428 ASP 428 428 428 ASP ASP B . n 
B 1 429 PRO 429 429 429 PRO PRO B . n 
B 1 430 ARG 430 430 430 ARG ARG B . n 
B 1 431 GLY 431 431 431 GLY GLY B . n 
B 1 432 ILE 432 432 432 ILE ILE B . n 
B 1 433 GLN 433 433 433 GLN GLN B . n 
B 1 434 GLY 434 434 434 GLY GLY B . n 
B 1 435 HIS 435 435 435 HIS HIS B . n 
B 1 436 GLY 436 436 436 GLY GLY B . n 
B 1 437 ILE 437 437 437 ILE ILE B . n 
B 1 438 THR 438 438 438 THR THR B . n 
B 1 439 TYR 439 439 439 TYR TYR B . n 
B 1 440 ALA 440 440 440 ALA ALA B . n 
B 1 441 VAL 441 441 441 VAL VAL B . n 
B 1 442 ASN 442 442 442 ASN ASN B . n 
B 1 443 ASN 443 443 443 ASN ASN B . n 
B 1 444 ARG 444 444 444 ARG ARG B . n 
B 1 445 GLY 445 445 445 GLY GLY B . n 
B 1 446 GLY 446 446 446 GLY GLY B . n 
B 1 447 CYS 447 447 447 CYS CYS B . n 
B 1 448 HIS 448 448 448 HIS HIS B . n 
B 1 449 ILE 449 449 449 ILE ILE B . n 
B 1 450 LYS 450 450 450 LYS LYS B . n 
B 1 451 GLY 451 451 451 GLY GLY B . n 
B 1 452 TYR 452 452 452 TYR TYR B . n 
B 1 453 MET 453 453 453 MET MET B . n 
B 1 454 ILE 454 454 454 ILE ILE B . n 
B 1 455 ASN 455 455 455 ASN ASN B . n 
B 1 456 PRO 456 456 456 PRO PRO B . n 
B 1 457 GLU 457 457 457 GLU GLU B . n 
B 1 458 ILE 458 458 458 ILE ILE B . n 
B 1 459 LEU 459 459 459 LEU LEU B . n 
B 1 460 GLY 460 460 460 GLY GLY B . n 
B 1 461 TYR 461 461 461 TYR TYR B . n 
B 1 462 PRO 462 462 462 PRO PRO B . n 
B 1 463 GLU 463 463 463 GLU GLU B . n 
B 1 464 LYS 464 464 464 LYS LYS B . n 
B 1 465 LEU 465 465 465 LEU LEU B . n 
B 1 466 ASP 466 466 466 ASP ASP B . n 
B 1 467 ARG 467 467 467 ARG ARG B . n 
B 1 468 PHE 468 468 468 PHE PHE B . n 
B 1 469 ALA 469 469 469 ALA ALA B . n 
B 1 470 LEU 470 470 470 LEU LEU B . n 
B 1 471 ASP 471 471 471 ASP ASP B . n 
B 1 472 GLY 472 472 472 GLY GLY B . n 
B 1 473 LYS 473 473 473 LYS LYS B . n 
B 1 474 ALA 474 474 474 ALA ALA B . n 
B 1 475 ALA 475 475 475 ALA ALA B . n 
B 1 476 TYR 476 476 476 TYR TYR B . n 
B 1 477 ALA 477 477 477 ALA ALA B . n 
B 1 478 LYS 478 478 478 LYS LYS B . n 
B 1 479 LEU 479 479 479 LEU LEU B . n 
B 1 480 PHE 480 480 480 PHE PHE B . n 
B 1 481 HIS 481 481 481 HIS HIS B . n 
B 1 482 ASP 482 482 482 ASP ASP B . n 
B 1 483 LEU 483 483 483 LEU LEU B . n 
B 1 484 THR 484 484 484 THR THR B . n 
B 1 485 ALA 485 485 485 ALA ALA B . n 
B 1 486 VAL 486 486 486 VAL VAL B . n 
B 1 487 ILE 487 487 487 ILE ILE B . n 
B 1 488 ASP 488 488 488 ASP ASP B . n 
B 1 489 SER 489 489 489 SER SER B . n 
B 1 490 LEU 490 490 490 LEU LEU B . n 
B 1 491 GLY 491 491 491 GLY GLY B . n 
B 1 492 LEU 492 492 492 LEU LEU B . n 
B 1 493 CYS 493 493 493 CYS CYS B . n 
B 1 494 ILE 494 494 494 ILE ILE B . n 
B 1 495 PHE 495 495 495 PHE PHE B . n 
B 1 496 THR 496 496 496 THR THR B . n 
B 1 497 THR 497 497 497 THR THR B . n 
B 1 498 PHE 498 498 498 PHE PHE B . n 
B 1 499 GLY 499 499 499 GLY GLY B . n 
B 1 500 LEU 500 500 500 LEU LEU B . n 
B 1 501 GLY 501 501 501 GLY GLY B . n 
B 1 502 ILE 502 502 502 ILE ILE B . n 
B 1 503 GLN 503 503 503 GLN GLN B . n 
B 1 504 ASP 504 504 504 ASP ASP B . n 
B 1 505 TYR 505 505 505 TYR TYR B . n 
B 1 506 VAL 506 506 506 VAL VAL B . n 
B 1 507 ASP 507 507 507 ASP ASP B . n 
B 1 508 MET 508 508 508 MET MET B . n 
B 1 509 TYR 509 509 509 TYR TYR B . n 
B 1 510 ASN 510 510 510 ASN ASN B . n 
B 1 511 ALA 511 511 511 ALA ALA B . n 
B 1 512 VAL 512 512 512 VAL VAL B . n 
B 1 513 VAL 513 513 513 VAL VAL B . n 
B 1 514 GLY 514 514 514 GLY GLY B . n 
B 1 515 GLU 515 515 515 GLU GLU B . n 
B 1 516 SER 516 516 516 SER SER B . n 
B 1 517 THR 517 517 517 THR THR B . n 
B 1 518 TYR 518 518 518 TYR TYR B . n 
B 1 519 ASP 519 519 519 ASP ASP B . n 
B 1 520 ALA 520 520 520 ALA ALA B . n 
B 1 521 ASP 521 521 521 ASP ASP B . n 
B 1 522 SER 522 522 522 SER SER B . n 
B 1 523 LEU 523 523 523 LEU LEU B . n 
B 1 524 LEU 524 524 524 LEU LEU B . n 
B 1 525 GLU 525 525 525 GLU GLU B . n 
B 1 526 ALA 526 526 526 ALA ALA B . n 
B 1 527 GLY 527 527 527 GLY GLY B . n 
B 1 528 ASP 528 528 528 ASP ASP B . n 
B 1 529 ARG 529 529 529 ARG ARG B . n 
B 1 530 ILE 530 530 530 ILE ILE B . n 
B 1 531 TRP 531 531 531 TRP TRP B . n 
B 1 532 THR 532 532 532 THR THR B . n 
B 1 533 LEU 533 533 533 LEU LEU B . n 
B 1 534 GLU 534 534 534 GLU GLU B . n 
B 1 535 LYS 535 535 535 LYS LYS B . n 
B 1 536 LEU 536 536 536 LEU LEU B . n 
B 1 537 PHE 537 537 537 PHE PHE B . n 
B 1 538 ASN 538 538 538 ASN ASN B . n 
B 1 539 LEU 539 539 539 LEU LEU B . n 
B 1 540 ALA 540 540 540 ALA ALA B . n 
B 1 541 ALA 541 541 541 ALA ALA B . n 
B 1 542 GLY 542 542 542 GLY GLY B . n 
B 1 543 ILE 543 543 543 ILE ILE B . n 
B 1 544 ASP 544 544 544 ASP ASP B . n 
B 1 545 SER 545 545 545 SER SER B . n 
B 1 546 SER 546 546 546 SER SER B . n 
B 1 547 GLN 547 547 547 GLN GLN B . n 
B 1 548 ASP 548 548 548 ASP ASP B . n 
B 1 549 THR 549 549 549 THR THR B . n 
B 1 550 LEU 550 550 550 LEU LEU B . n 
B 1 551 PRO 551 551 551 PRO PRO B . n 
B 1 552 LYS 552 552 552 LYS LYS B . n 
B 1 553 ARG 553 553 553 ARG ARG B . n 
B 1 554 LEU 554 554 554 LEU LEU B . n 
B 1 555 LEU 555 555 555 LEU LEU B . n 
B 1 556 GLU 556 556 556 GLU GLU B . n 
B 1 557 GLU 557 557 557 GLU GLU B . n 
B 1 558 PRO 558 558 558 PRO PRO B . n 
B 1 559 ILE 559 559 559 ILE ILE B . n 
B 1 560 PRO 560 560 560 PRO PRO B . n 
B 1 561 ASP 561 561 561 ASP ASP B . n 
B 1 562 GLY 562 562 562 GLY GLY B . n 
B 1 563 PRO 563 563 563 PRO PRO B . n 
B 1 564 SER 564 564 564 SER SER B . n 
B 1 565 LYS 565 565 565 LYS LYS B . n 
B 1 566 GLY 566 566 566 GLY GLY B . n 
B 1 567 GLU 567 567 567 GLU GLU B . n 
B 1 568 VAL 568 568 568 VAL VAL B . n 
B 1 569 HIS 569 569 569 HIS HIS B . n 
B 1 570 ARG 570 570 570 ARG ARG B . n 
B 1 571 LEU 571 571 571 LEU LEU B . n 
B 1 572 ASP 572 572 572 ASP ASP B . n 
B 1 573 VAL 573 573 573 VAL VAL B . n 
B 1 574 LEU 574 574 574 LEU LEU B . n 
B 1 575 LEU 575 575 575 LEU LEU B . n 
B 1 576 PRO 576 576 576 PRO PRO B . n 
B 1 577 GLU 577 577 577 GLU GLU B . n 
B 1 578 TYR 578 578 578 TYR TYR B . n 
B 1 579 TYR 579 579 579 TYR TYR B . n 
B 1 580 SER 580 580 580 SER SER B . n 
B 1 581 VAL 581 581 581 VAL VAL B . n 
B 1 582 ARG 582 582 582 ARG ARG B . n 
B 1 583 GLY 583 583 583 GLY GLY B . n 
B 1 584 TRP 584 584 584 TRP TRP B . n 
B 1 585 SER 585 585 585 SER SER B . n 
B 1 586 LYS 586 586 586 LYS LYS B . n 
B 1 587 GLU 587 587 587 GLU GLU B . n 
B 1 588 GLY 588 588 588 GLY GLY B . n 
B 1 589 ILE 589 589 589 ILE ILE B . n 
B 1 590 PRO 590 590 590 PRO PRO B . n 
B 1 591 THR 591 591 591 THR THR B . n 
B 1 592 GLU 592 592 592 GLU GLU B . n 
B 1 593 GLU 593 593 593 GLU GLU B . n 
B 1 594 THR 594 594 594 THR THR B . n 
B 1 595 LEU 595 595 595 LEU LEU B . n 
B 1 596 LYS 596 596 596 LYS LYS B . n 
B 1 597 LYS 597 597 597 LYS LYS B . n 
B 1 598 LEU 598 598 598 LEU LEU B . n 
B 1 599 GLY 599 599 599 GLY GLY B . n 
B 1 600 LEU 600 600 600 LEU LEU B . n 
B 1 601 ASP 601 601 601 ASP ASP B . n 
B 1 602 GLU 602 602 602 GLU GLU B . n 
B 1 603 TYR 603 603 603 TYR TYR B . n 
B 1 604 ILE 604 604 604 ILE ILE B . n 
B 1 605 GLY 605 605 605 GLY GLY B . n 
B 1 606 LYS 606 606 606 LYS LYS B . n 
B 1 607 PHE 607 607 607 PHE PHE B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 A1IJH ? ? A1IJH ? ? 'SUBJECT OF INVESTIGATION' ? 
2 SF4   ? ? SF4   ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 SF4   1   701  701  SF4   SF4 A . 
D 3 A1IJH 1   702  801  A1IJH PTE A . 
E 4 CL    1   703  2    CL    CL  A . 
F 5 MG    1   704  1    MG    MG  A . 
G 2 SF4   1   701  701  SF4   SF4 B . 
H 3 A1IJH 1   702  801  A1IJH PTE B . 
I 6 EDO   1   703  1302 EDO   EDO B . 
J 6 EDO   1   704  1303 EDO   EDO B . 
K 4 CL    1   705  1    CL    CL  B . 
L 4 CL    1   706  3    CL    CL  B . 
M 7 HOH   1   801  580  HOH   HOH A . 
M 7 HOH   2   802  744  HOH   HOH A . 
M 7 HOH   3   803  7    HOH   HOH A . 
M 7 HOH   4   804  22   HOH   HOH A . 
M 7 HOH   5   805  1118 HOH   HOH A . 
M 7 HOH   6   806  1176 HOH   HOH A . 
M 7 HOH   7   807  1524 HOH   HOH A . 
M 7 HOH   8   808  782  HOH   HOH A . 
M 7 HOH   9   809  554  HOH   HOH A . 
M 7 HOH   10  810  220  HOH   HOH A . 
M 7 HOH   11  811  1041 HOH   HOH A . 
M 7 HOH   12  812  599  HOH   HOH A . 
M 7 HOH   13  813  84   HOH   HOH A . 
M 7 HOH   14  814  1284 HOH   HOH A . 
M 7 HOH   15  815  1049 HOH   HOH A . 
M 7 HOH   16  816  114  HOH   HOH A . 
M 7 HOH   17  817  877  HOH   HOH A . 
M 7 HOH   18  818  822  HOH   HOH A . 
M 7 HOH   19  819  528  HOH   HOH A . 
M 7 HOH   20  820  802  HOH   HOH A . 
M 7 HOH   21  821  741  HOH   HOH A . 
M 7 HOH   22  822  553  HOH   HOH A . 
M 7 HOH   23  823  11   HOH   HOH A . 
M 7 HOH   24  824  19   HOH   HOH A . 
M 7 HOH   25  825  1390 HOH   HOH A . 
M 7 HOH   26  826  1    HOH   HOH A . 
M 7 HOH   27  827  266  HOH   HOH A . 
M 7 HOH   28  828  1262 HOH   HOH A . 
M 7 HOH   29  829  236  HOH   HOH A . 
M 7 HOH   30  830  524  HOH   HOH A . 
M 7 HOH   31  831  381  HOH   HOH A . 
M 7 HOH   32  832  1541 HOH   HOH A . 
M 7 HOH   33  833  918  HOH   HOH A . 
M 7 HOH   34  834  1431 HOH   HOH A . 
M 7 HOH   35  835  708  HOH   HOH A . 
M 7 HOH   36  836  148  HOH   HOH A . 
M 7 HOH   37  837  40   HOH   HOH A . 
M 7 HOH   38  838  318  HOH   HOH A . 
M 7 HOH   39  839  341  HOH   HOH A . 
M 7 HOH   40  840  312  HOH   HOH A . 
M 7 HOH   41  841  269  HOH   HOH A . 
M 7 HOH   42  842  1257 HOH   HOH A . 
M 7 HOH   43  843  3    HOH   HOH A . 
M 7 HOH   44  844  1196 HOH   HOH A . 
M 7 HOH   45  845  621  HOH   HOH A . 
M 7 HOH   46  846  1214 HOH   HOH A . 
M 7 HOH   47  847  731  HOH   HOH A . 
M 7 HOH   48  848  1439 HOH   HOH A . 
M 7 HOH   49  849  477  HOH   HOH A . 
M 7 HOH   50  850  75   HOH   HOH A . 
M 7 HOH   51  851  1557 HOH   HOH A . 
M 7 HOH   52  852  1195 HOH   HOH A . 
M 7 HOH   53  853  12   HOH   HOH A . 
M 7 HOH   54  854  1348 HOH   HOH A . 
M 7 HOH   55  855  85   HOH   HOH A . 
M 7 HOH   56  856  425  HOH   HOH A . 
M 7 HOH   57  857  682  HOH   HOH A . 
M 7 HOH   58  858  18   HOH   HOH A . 
M 7 HOH   59  859  421  HOH   HOH A . 
M 7 HOH   60  860  642  HOH   HOH A . 
M 7 HOH   61  861  1428 HOH   HOH A . 
M 7 HOH   62  862  1424 HOH   HOH A . 
M 7 HOH   63  863  558  HOH   HOH A . 
M 7 HOH   64  864  757  HOH   HOH A . 
M 7 HOH   65  865  2    HOH   HOH A . 
M 7 HOH   66  866  250  HOH   HOH A . 
M 7 HOH   67  867  1511 HOH   HOH A . 
M 7 HOH   68  868  17   HOH   HOH A . 
M 7 HOH   69  869  247  HOH   HOH A . 
M 7 HOH   70  870  699  HOH   HOH A . 
M 7 HOH   71  871  738  HOH   HOH A . 
M 7 HOH   72  872  1046 HOH   HOH A . 
M 7 HOH   73  873  859  HOH   HOH A . 
M 7 HOH   74  874  183  HOH   HOH A . 
M 7 HOH   75  875  618  HOH   HOH A . 
M 7 HOH   76  876  397  HOH   HOH A . 
M 7 HOH   77  877  629  HOH   HOH A . 
M 7 HOH   78  878  1324 HOH   HOH A . 
M 7 HOH   79  879  1171 HOH   HOH A . 
M 7 HOH   80  880  1075 HOH   HOH A . 
M 7 HOH   81  881  1210 HOH   HOH A . 
M 7 HOH   82  882  1228 HOH   HOH A . 
M 7 HOH   83  883  1364 HOH   HOH A . 
M 7 HOH   84  884  721  HOH   HOH A . 
M 7 HOH   85  885  371  HOH   HOH A . 
M 7 HOH   86  886  1000 HOH   HOH A . 
M 7 HOH   87  887  902  HOH   HOH A . 
M 7 HOH   88  888  296  HOH   HOH A . 
M 7 HOH   89  889  637  HOH   HOH A . 
M 7 HOH   90  890  108  HOH   HOH A . 
M 7 HOH   91  891  493  HOH   HOH A . 
M 7 HOH   92  892  1121 HOH   HOH A . 
M 7 HOH   93  893  908  HOH   HOH A . 
M 7 HOH   94  894  752  HOH   HOH A . 
M 7 HOH   95  895  607  HOH   HOH A . 
M 7 HOH   96  896  46   HOH   HOH A . 
M 7 HOH   97  897  356  HOH   HOH A . 
M 7 HOH   98  898  181  HOH   HOH A . 
M 7 HOH   99  899  257  HOH   HOH A . 
M 7 HOH   100 900  179  HOH   HOH A . 
M 7 HOH   101 901  589  HOH   HOH A . 
M 7 HOH   102 902  846  HOH   HOH A . 
M 7 HOH   103 903  79   HOH   HOH A . 
M 7 HOH   104 904  1273 HOH   HOH A . 
M 7 HOH   105 905  171  HOH   HOH A . 
M 7 HOH   106 906  401  HOH   HOH A . 
M 7 HOH   107 907  516  HOH   HOH A . 
M 7 HOH   108 908  849  HOH   HOH A . 
M 7 HOH   109 909  330  HOH   HOH A . 
M 7 HOH   110 910  619  HOH   HOH A . 
M 7 HOH   111 911  827  HOH   HOH A . 
M 7 HOH   112 912  663  HOH   HOH A . 
M 7 HOH   113 913  466  HOH   HOH A . 
M 7 HOH   114 914  291  HOH   HOH A . 
M 7 HOH   115 915  392  HOH   HOH A . 
M 7 HOH   116 916  852  HOH   HOH A . 
M 7 HOH   117 917  229  HOH   HOH A . 
M 7 HOH   118 918  614  HOH   HOH A . 
M 7 HOH   119 919  938  HOH   HOH A . 
M 7 HOH   120 920  112  HOH   HOH A . 
M 7 HOH   121 921  56   HOH   HOH A . 
M 7 HOH   122 922  1373 HOH   HOH A . 
M 7 HOH   123 923  670  HOH   HOH A . 
M 7 HOH   124 924  134  HOH   HOH A . 
M 7 HOH   125 925  488  HOH   HOH A . 
M 7 HOH   126 926  321  HOH   HOH A . 
M 7 HOH   127 927  1034 HOH   HOH A . 
M 7 HOH   128 928  185  HOH   HOH A . 
M 7 HOH   129 929  679  HOH   HOH A . 
M 7 HOH   130 930  5    HOH   HOH A . 
M 7 HOH   131 931  484  HOH   HOH A . 
M 7 HOH   132 932  486  HOH   HOH A . 
M 7 HOH   133 933  47   HOH   HOH A . 
M 7 HOH   134 934  88   HOH   HOH A . 
M 7 HOH   135 935  666  HOH   HOH A . 
M 7 HOH   136 936  848  HOH   HOH A . 
M 7 HOH   137 937  1294 HOH   HOH A . 
M 7 HOH   138 938  595  HOH   HOH A . 
M 7 HOH   139 939  1466 HOH   HOH A . 
M 7 HOH   140 940  508  HOH   HOH A . 
M 7 HOH   141 941  499  HOH   HOH A . 
M 7 HOH   142 942  164  HOH   HOH A . 
M 7 HOH   143 943  60   HOH   HOH A . 
M 7 HOH   144 944  202  HOH   HOH A . 
M 7 HOH   145 945  126  HOH   HOH A . 
M 7 HOH   146 946  59   HOH   HOH A . 
M 7 HOH   147 947  511  HOH   HOH A . 
M 7 HOH   148 948  26   HOH   HOH A . 
M 7 HOH   149 949  1370 HOH   HOH A . 
M 7 HOH   150 950  349  HOH   HOH A . 
M 7 HOH   151 951  638  HOH   HOH A . 
M 7 HOH   152 952  643  HOH   HOH A . 
M 7 HOH   153 953  1325 HOH   HOH A . 
M 7 HOH   154 954  533  HOH   HOH A . 
M 7 HOH   155 955  936  HOH   HOH A . 
M 7 HOH   156 956  343  HOH   HOH A . 
M 7 HOH   157 957  549  HOH   HOH A . 
M 7 HOH   158 958  20   HOH   HOH A . 
M 7 HOH   159 959  1405 HOH   HOH A . 
M 7 HOH   160 960  155  HOH   HOH A . 
M 7 HOH   161 961  362  HOH   HOH A . 
M 7 HOH   162 962  187  HOH   HOH A . 
M 7 HOH   163 963  322  HOH   HOH A . 
M 7 HOH   164 964  135  HOH   HOH A . 
M 7 HOH   165 965  823  HOH   HOH A . 
M 7 HOH   166 966  314  HOH   HOH A . 
M 7 HOH   167 967  382  HOH   HOH A . 
M 7 HOH   168 968  610  HOH   HOH A . 
M 7 HOH   169 969  133  HOH   HOH A . 
M 7 HOH   170 970  232  HOH   HOH A . 
M 7 HOH   171 971  55   HOH   HOH A . 
M 7 HOH   172 972  1031 HOH   HOH A . 
M 7 HOH   173 973  816  HOH   HOH A . 
M 7 HOH   174 974  497  HOH   HOH A . 
M 7 HOH   175 975  669  HOH   HOH A . 
M 7 HOH   176 976  1343 HOH   HOH A . 
M 7 HOH   177 977  204  HOH   HOH A . 
M 7 HOH   178 978  168  HOH   HOH A . 
M 7 HOH   179 979  1215 HOH   HOH A . 
M 7 HOH   180 980  225  HOH   HOH A . 
M 7 HOH   181 981  51   HOH   HOH A . 
M 7 HOH   182 982  413  HOH   HOH A . 
M 7 HOH   183 983  1420 HOH   HOH A . 
M 7 HOH   184 984  394  HOH   HOH A . 
M 7 HOH   185 985  138  HOH   HOH A . 
M 7 HOH   186 986  459  HOH   HOH A . 
M 7 HOH   187 987  579  HOH   HOH A . 
M 7 HOH   188 988  219  HOH   HOH A . 
M 7 HOH   189 989  30   HOH   HOH A . 
M 7 HOH   190 990  756  HOH   HOH A . 
M 7 HOH   191 991  226  HOH   HOH A . 
M 7 HOH   192 992  331  HOH   HOH A . 
M 7 HOH   193 993  400  HOH   HOH A . 
M 7 HOH   194 994  213  HOH   HOH A . 
M 7 HOH   195 995  537  HOH   HOH A . 
M 7 HOH   196 996  1296 HOH   HOH A . 
M 7 HOH   197 997  624  HOH   HOH A . 
M 7 HOH   198 998  156  HOH   HOH A . 
M 7 HOH   199 999  200  HOH   HOH A . 
M 7 HOH   200 1000 1009 HOH   HOH A . 
M 7 HOH   201 1001 151  HOH   HOH A . 
M 7 HOH   202 1002 258  HOH   HOH A . 
M 7 HOH   203 1003 152  HOH   HOH A . 
M 7 HOH   204 1004 1278 HOH   HOH A . 
M 7 HOH   205 1005 317  HOH   HOH A . 
M 7 HOH   206 1006 1234 HOH   HOH A . 
M 7 HOH   207 1007 1125 HOH   HOH A . 
M 7 HOH   208 1008 345  HOH   HOH A . 
M 7 HOH   209 1009 1025 HOH   HOH A . 
M 7 HOH   210 1010 143  HOH   HOH A . 
M 7 HOH   211 1011 215  HOH   HOH A . 
M 7 HOH   212 1012 361  HOH   HOH A . 
M 7 HOH   213 1013 1249 HOH   HOH A . 
M 7 HOH   214 1014 32   HOH   HOH A . 
M 7 HOH   215 1015 1191 HOH   HOH A . 
M 7 HOH   216 1016 1479 HOH   HOH A . 
M 7 HOH   217 1017 218  HOH   HOH A . 
M 7 HOH   218 1018 1050 HOH   HOH A . 
M 7 HOH   219 1019 81   HOH   HOH A . 
M 7 HOH   220 1020 193  HOH   HOH A . 
M 7 HOH   221 1021 905  HOH   HOH A . 
M 7 HOH   222 1022 1079 HOH   HOH A . 
M 7 HOH   223 1023 13   HOH   HOH A . 
M 7 HOH   224 1024 605  HOH   HOH A . 
M 7 HOH   225 1025 210  HOH   HOH A . 
M 7 HOH   226 1026 89   HOH   HOH A . 
M 7 HOH   227 1027 14   HOH   HOH A . 
M 7 HOH   228 1028 541  HOH   HOH A . 
M 7 HOH   229 1029 175  HOH   HOH A . 
M 7 HOH   230 1030 1521 HOH   HOH A . 
M 7 HOH   231 1031 10   HOH   HOH A . 
M 7 HOH   232 1032 773  HOH   HOH A . 
M 7 HOH   233 1033 101  HOH   HOH A . 
M 7 HOH   234 1034 789  HOH   HOH A . 
M 7 HOH   235 1035 949  HOH   HOH A . 
M 7 HOH   236 1036 967  HOH   HOH A . 
M 7 HOH   237 1037 1005 HOH   HOH A . 
M 7 HOH   238 1038 1159 HOH   HOH A . 
M 7 HOH   239 1039 197  HOH   HOH A . 
M 7 HOH   240 1040 172  HOH   HOH A . 
M 7 HOH   241 1041 121  HOH   HOH A . 
M 7 HOH   242 1042 784  HOH   HOH A . 
M 7 HOH   243 1043 1318 HOH   HOH A . 
M 7 HOH   244 1044 347  HOH   HOH A . 
M 7 HOH   245 1045 1298 HOH   HOH A . 
M 7 HOH   246 1046 389  HOH   HOH A . 
M 7 HOH   247 1047 169  HOH   HOH A . 
M 7 HOH   248 1048 1004 HOH   HOH A . 
M 7 HOH   249 1049 70   HOH   HOH A . 
M 7 HOH   250 1050 245  HOH   HOH A . 
M 7 HOH   251 1051 1235 HOH   HOH A . 
M 7 HOH   252 1052 1535 HOH   HOH A . 
M 7 HOH   253 1053 78   HOH   HOH A . 
M 7 HOH   254 1054 360  HOH   HOH A . 
M 7 HOH   255 1055 1253 HOH   HOH A . 
M 7 HOH   256 1056 805  HOH   HOH A . 
M 7 HOH   257 1057 837  HOH   HOH A . 
M 7 HOH   258 1058 76   HOH   HOH A . 
M 7 HOH   259 1059 521  HOH   HOH A . 
M 7 HOH   260 1060 36   HOH   HOH A . 
M 7 HOH   261 1061 906  HOH   HOH A . 
M 7 HOH   262 1062 451  HOH   HOH A . 
M 7 HOH   263 1063 211  HOH   HOH A . 
M 7 HOH   264 1064 943  HOH   HOH A . 
M 7 HOH   265 1065 660  HOH   HOH A . 
M 7 HOH   266 1066 333  HOH   HOH A . 
M 7 HOH   267 1067 106  HOH   HOH A . 
M 7 HOH   268 1068 1160 HOH   HOH A . 
M 7 HOH   269 1069 945  HOH   HOH A . 
M 7 HOH   270 1070 72   HOH   HOH A . 
M 7 HOH   271 1071 1149 HOH   HOH A . 
M 7 HOH   272 1072 1330 HOH   HOH A . 
M 7 HOH   273 1073 271  HOH   HOH A . 
M 7 HOH   274 1074 480  HOH   HOH A . 
M 7 HOH   275 1075 363  HOH   HOH A . 
M 7 HOH   276 1076 71   HOH   HOH A . 
M 7 HOH   277 1077 387  HOH   HOH A . 
M 7 HOH   278 1078 885  HOH   HOH A . 
M 7 HOH   279 1079 841  HOH   HOH A . 
M 7 HOH   280 1080 402  HOH   HOH A . 
M 7 HOH   281 1081 406  HOH   HOH A . 
M 7 HOH   282 1082 255  HOH   HOH A . 
M 7 HOH   283 1083 648  HOH   HOH A . 
M 7 HOH   284 1084 810  HOH   HOH A . 
M 7 HOH   285 1085 529  HOH   HOH A . 
M 7 HOH   286 1086 711  HOH   HOH A . 
M 7 HOH   287 1087 216  HOH   HOH A . 
M 7 HOH   288 1088 246  HOH   HOH A . 
M 7 HOH   289 1089 577  HOH   HOH A . 
M 7 HOH   290 1090 692  HOH   HOH A . 
M 7 HOH   291 1091 1097 HOH   HOH A . 
M 7 HOH   292 1092 191  HOH   HOH A . 
M 7 HOH   293 1093 1044 HOH   HOH A . 
M 7 HOH   294 1094 1213 HOH   HOH A . 
M 7 HOH   295 1095 65   HOH   HOH A . 
M 7 HOH   296 1096 1102 HOH   HOH A . 
M 7 HOH   297 1097 25   HOH   HOH A . 
M 7 HOH   298 1098 834  HOH   HOH A . 
M 7 HOH   299 1099 145  HOH   HOH A . 
M 7 HOH   300 1100 681  HOH   HOH A . 
M 7 HOH   301 1101 430  HOH   HOH A . 
M 7 HOH   302 1102 440  HOH   HOH A . 
M 7 HOH   303 1103 274  HOH   HOH A . 
M 7 HOH   304 1104 570  HOH   HOH A . 
M 7 HOH   305 1105 74   HOH   HOH A . 
M 7 HOH   306 1106 426  HOH   HOH A . 
M 7 HOH   307 1107 1216 HOH   HOH A . 
M 7 HOH   308 1108 201  HOH   HOH A . 
M 7 HOH   309 1109 1140 HOH   HOH A . 
M 7 HOH   310 1110 590  HOH   HOH A . 
M 7 HOH   311 1111 365  HOH   HOH A . 
M 7 HOH   312 1112 241  HOH   HOH A . 
M 7 HOH   313 1113 43   HOH   HOH A . 
M 7 HOH   314 1114 388  HOH   HOH A . 
M 7 HOH   315 1115 824  HOH   HOH A . 
M 7 HOH   316 1116 442  HOH   HOH A . 
M 7 HOH   317 1117 457  HOH   HOH A . 
M 7 HOH   318 1118 728  HOH   HOH A . 
M 7 HOH   319 1119 118  HOH   HOH A . 
M 7 HOH   320 1120 344  HOH   HOH A . 
M 7 HOH   321 1121 358  HOH   HOH A . 
M 7 HOH   322 1122 260  HOH   HOH A . 
M 7 HOH   323 1123 1199 HOH   HOH A . 
M 7 HOH   324 1124 927  HOH   HOH A . 
M 7 HOH   325 1125 547  HOH   HOH A . 
M 7 HOH   326 1126 1538 HOH   HOH A . 
M 7 HOH   327 1127 985  HOH   HOH A . 
M 7 HOH   328 1128 791  HOH   HOH A . 
M 7 HOH   329 1129 1051 HOH   HOH A . 
M 7 HOH   330 1130 67   HOH   HOH A . 
M 7 HOH   331 1131 719  HOH   HOH A . 
M 7 HOH   332 1132 178  HOH   HOH A . 
M 7 HOH   333 1133 866  HOH   HOH A . 
M 7 HOH   334 1134 80   HOH   HOH A . 
M 7 HOH   335 1135 412  HOH   HOH A . 
M 7 HOH   336 1136 224  HOH   HOH A . 
M 7 HOH   337 1137 27   HOH   HOH A . 
M 7 HOH   338 1138 424  HOH   HOH A . 
M 7 HOH   339 1139 838  HOH   HOH A . 
M 7 HOH   340 1140 1470 HOH   HOH A . 
M 7 HOH   341 1141 498  HOH   HOH A . 
M 7 HOH   342 1142 228  HOH   HOH A . 
M 7 HOH   343 1143 509  HOH   HOH A . 
M 7 HOH   344 1144 41   HOH   HOH A . 
M 7 HOH   345 1145 190  HOH   HOH A . 
M 7 HOH   346 1146 1416 HOH   HOH A . 
M 7 HOH   347 1147 707  HOH   HOH A . 
M 7 HOH   348 1148 1447 HOH   HOH A . 
M 7 HOH   349 1149 324  HOH   HOH A . 
M 7 HOH   350 1150 997  HOH   HOH A . 
M 7 HOH   351 1151 278  HOH   HOH A . 
M 7 HOH   352 1152 288  HOH   HOH A . 
M 7 HOH   353 1153 1090 HOH   HOH A . 
M 7 HOH   354 1154 867  HOH   HOH A . 
M 7 HOH   355 1155 346  HOH   HOH A . 
M 7 HOH   356 1156 1445 HOH   HOH A . 
M 7 HOH   357 1157 438  HOH   HOH A . 
M 7 HOH   358 1158 510  HOH   HOH A . 
M 7 HOH   359 1159 505  HOH   HOH A . 
M 7 HOH   360 1160 52   HOH   HOH A . 
M 7 HOH   361 1161 414  HOH   HOH A . 
M 7 HOH   362 1162 445  HOH   HOH A . 
M 7 HOH   363 1163 1310 HOH   HOH A . 
M 7 HOH   364 1164 809  HOH   HOH A . 
M 7 HOH   365 1165 1138 HOH   HOH A . 
M 7 HOH   366 1166 620  HOH   HOH A . 
M 7 HOH   367 1167 380  HOH   HOH A . 
M 7 HOH   368 1168 582  HOH   HOH A . 
M 7 HOH   369 1169 491  HOH   HOH A . 
M 7 HOH   370 1170 1378 HOH   HOH A . 
M 7 HOH   371 1171 100  HOH   HOH A . 
M 7 HOH   372 1172 617  HOH   HOH A . 
M 7 HOH   373 1173 404  HOH   HOH A . 
M 7 HOH   374 1174 61   HOH   HOH A . 
M 7 HOH   375 1175 1112 HOH   HOH A . 
M 7 HOH   376 1176 292  HOH   HOH A . 
M 7 HOH   377 1177 658  HOH   HOH A . 
M 7 HOH   378 1178 871  HOH   HOH A . 
M 7 HOH   379 1179 265  HOH   HOH A . 
M 7 HOH   380 1180 192  HOH   HOH A . 
M 7 HOH   381 1181 964  HOH   HOH A . 
M 7 HOH   382 1182 539  HOH   HOH A . 
M 7 HOH   383 1183 1269 HOH   HOH A . 
M 7 HOH   384 1184 16   HOH   HOH A . 
M 7 HOH   385 1185 391  HOH   HOH A . 
M 7 HOH   386 1186 399  HOH   HOH A . 
M 7 HOH   387 1187 1240 HOH   HOH A . 
M 7 HOH   388 1188 289  HOH   HOH A . 
M 7 HOH   389 1189 336  HOH   HOH A . 
M 7 HOH   390 1190 664  HOH   HOH A . 
M 7 HOH   391 1191 1504 HOH   HOH A . 
M 7 HOH   392 1192 696  HOH   HOH A . 
M 7 HOH   393 1193 1528 HOH   HOH A . 
M 7 HOH   394 1194 334  HOH   HOH A . 
M 7 HOH   395 1195 195  HOH   HOH A . 
M 7 HOH   396 1196 159  HOH   HOH A . 
M 7 HOH   397 1197 1380 HOH   HOH A . 
M 7 HOH   398 1198 58   HOH   HOH A . 
M 7 HOH   399 1199 367  HOH   HOH A . 
M 7 HOH   400 1200 234  HOH   HOH A . 
M 7 HOH   401 1201 1327 HOH   HOH A . 
M 7 HOH   402 1202 513  HOH   HOH A . 
M 7 HOH   403 1203 1204 HOH   HOH A . 
M 7 HOH   404 1204 1010 HOH   HOH A . 
M 7 HOH   405 1205 636  HOH   HOH A . 
M 7 HOH   406 1206 386  HOH   HOH A . 
M 7 HOH   407 1207 308  HOH   HOH A . 
M 7 HOH   408 1208 506  HOH   HOH A . 
M 7 HOH   409 1209 1389 HOH   HOH A . 
M 7 HOH   410 1210 38   HOH   HOH A . 
M 7 HOH   411 1211 1220 HOH   HOH A . 
M 7 HOH   412 1212 734  HOH   HOH A . 
M 7 HOH   413 1213 262  HOH   HOH A . 
M 7 HOH   414 1214 909  HOH   HOH A . 
M 7 HOH   415 1215 471  HOH   HOH A . 
M 7 HOH   416 1216 920  HOH   HOH A . 
M 7 HOH   417 1217 1277 HOH   HOH A . 
M 7 HOH   418 1218 820  HOH   HOH A . 
M 7 HOH   419 1219 460  HOH   HOH A . 
M 7 HOH   420 1220 562  HOH   HOH A . 
M 7 HOH   421 1221 650  HOH   HOH A . 
M 7 HOH   422 1222 335  HOH   HOH A . 
M 7 HOH   423 1223 146  HOH   HOH A . 
M 7 HOH   424 1224 373  HOH   HOH A . 
M 7 HOH   425 1225 613  HOH   HOH A . 
M 7 HOH   426 1226 1342 HOH   HOH A . 
M 7 HOH   427 1227 774  HOH   HOH A . 
M 7 HOH   428 1228 1451 HOH   HOH A . 
M 7 HOH   429 1229 99   HOH   HOH A . 
M 7 HOH   430 1230 1189 HOH   HOH A . 
M 7 HOH   431 1231 546  HOH   HOH A . 
M 7 HOH   432 1232 632  HOH   HOH A . 
M 7 HOH   433 1233 1152 HOH   HOH A . 
M 7 HOH   434 1234 1563 HOH   HOH A . 
M 7 HOH   435 1235 415  HOH   HOH A . 
M 7 HOH   436 1236 1460 HOH   HOH A . 
M 7 HOH   437 1237 1341 HOH   HOH A . 
M 7 HOH   438 1238 431  HOH   HOH A . 
M 7 HOH   439 1239 1142 HOH   HOH A . 
M 7 HOH   440 1240 92   HOH   HOH A . 
M 7 HOH   441 1241 194  HOH   HOH A . 
M 7 HOH   442 1242 868  HOH   HOH A . 
M 7 HOH   443 1243 1481 HOH   HOH A . 
M 7 HOH   444 1244 1201 HOH   HOH A . 
M 7 HOH   445 1245 717  HOH   HOH A . 
M 7 HOH   446 1246 1530 HOH   HOH A . 
M 7 HOH   447 1247 956  HOH   HOH A . 
M 7 HOH   448 1248 1013 HOH   HOH A . 
M 7 HOH   449 1249 82   HOH   HOH A . 
M 7 HOH   450 1250 1108 HOH   HOH A . 
M 7 HOH   451 1251 1517 HOH   HOH A . 
M 7 HOH   452 1252 307  HOH   HOH A . 
M 7 HOH   453 1253 1208 HOH   HOH A . 
M 7 HOH   454 1254 662  HOH   HOH A . 
M 7 HOH   455 1255 304  HOH   HOH A . 
M 7 HOH   456 1256 706  HOH   HOH A . 
M 7 HOH   457 1257 417  HOH   HOH A . 
M 7 HOH   458 1258 559  HOH   HOH A . 
M 7 HOH   459 1259 552  HOH   HOH A . 
M 7 HOH   460 1260 1311 HOH   HOH A . 
M 7 HOH   461 1261 1095 HOH   HOH A . 
M 7 HOH   462 1262 1467 HOH   HOH A . 
M 7 HOH   463 1263 766  HOH   HOH A . 
M 7 HOH   464 1264 647  HOH   HOH A . 
M 7 HOH   465 1265 800  HOH   HOH A . 
M 7 HOH   466 1266 1502 HOH   HOH A . 
M 7 HOH   467 1267 803  HOH   HOH A . 
M 7 HOH   468 1268 1103 HOH   HOH A . 
M 7 HOH   469 1269 369  HOH   HOH A . 
M 7 HOH   470 1270 416  HOH   HOH A . 
M 7 HOH   471 1271 1198 HOH   HOH A . 
M 7 HOH   472 1272 951  HOH   HOH A . 
M 7 HOH   473 1273 242  HOH   HOH A . 
M 7 HOH   474 1274 1205 HOH   HOH A . 
M 7 HOH   475 1275 1510 HOH   HOH A . 
M 7 HOH   476 1276 678  HOH   HOH A . 
M 7 HOH   477 1277 1418 HOH   HOH A . 
M 7 HOH   478 1278 161  HOH   HOH A . 
M 7 HOH   479 1279 1543 HOH   HOH A . 
M 7 HOH   480 1280 683  HOH   HOH A . 
M 7 HOH   481 1281 1417 HOH   HOH A . 
M 7 HOH   482 1282 934  HOH   HOH A . 
M 7 HOH   483 1283 1281 HOH   HOH A . 
M 7 HOH   484 1284 199  HOH   HOH A . 
M 7 HOH   485 1285 186  HOH   HOH A . 
M 7 HOH   486 1286 811  HOH   HOH A . 
M 7 HOH   487 1287 566  HOH   HOH A . 
M 7 HOH   488 1288 1019 HOH   HOH A . 
M 7 HOH   489 1289 689  HOH   HOH A . 
M 7 HOH   490 1290 1406 HOH   HOH A . 
M 7 HOH   491 1291 817  HOH   HOH A . 
M 7 HOH   492 1292 1485 HOH   HOH A . 
M 7 HOH   493 1293 641  HOH   HOH A . 
M 7 HOH   494 1294 1170 HOH   HOH A . 
M 7 HOH   495 1295 465  HOH   HOH A . 
M 7 HOH   496 1296 704  HOH   HOH A . 
M 7 HOH   497 1297 364  HOH   HOH A . 
M 7 HOH   498 1298 857  HOH   HOH A . 
M 7 HOH   499 1299 668  HOH   HOH A . 
M 7 HOH   500 1300 561  HOH   HOH A . 
M 7 HOH   501 1301 1290 HOH   HOH A . 
M 7 HOH   502 1302 1224 HOH   HOH A . 
M 7 HOH   503 1303 1098 HOH   HOH A . 
M 7 HOH   504 1304 1476 HOH   HOH A . 
M 7 HOH   505 1305 209  HOH   HOH A . 
M 7 HOH   506 1306 1057 HOH   HOH A . 
M 7 HOH   507 1307 1523 HOH   HOH A . 
M 7 HOH   508 1308 598  HOH   HOH A . 
M 7 HOH   509 1309 1347 HOH   HOH A . 
M 7 HOH   510 1310 1383 HOH   HOH A . 
M 7 HOH   511 1311 969  HOH   HOH A . 
M 7 HOH   512 1312 1209 HOH   HOH A . 
M 7 HOH   513 1313 1375 HOH   HOH A . 
M 7 HOH   514 1314 722  HOH   HOH A . 
M 7 HOH   515 1315 555  HOH   HOH A . 
M 7 HOH   516 1316 1099 HOH   HOH A . 
M 7 HOH   517 1317 1265 HOH   HOH A . 
M 7 HOH   518 1318 1016 HOH   HOH A . 
M 7 HOH   519 1319 597  HOH   HOH A . 
M 7 HOH   520 1320 903  HOH   HOH A . 
M 7 HOH   521 1321 1018 HOH   HOH A . 
M 7 HOH   522 1322 439  HOH   HOH A . 
M 7 HOH   523 1323 1393 HOH   HOH A . 
M 7 HOH   524 1324 863  HOH   HOH A . 
M 7 HOH   525 1325 1300 HOH   HOH A . 
M 7 HOH   526 1326 1361 HOH   HOH A . 
M 7 HOH   527 1327 843  HOH   HOH A . 
M 7 HOH   528 1328 1434 HOH   HOH A . 
M 7 HOH   529 1329 551  HOH   HOH A . 
M 7 HOH   530 1330 110  HOH   HOH A . 
M 7 HOH   531 1331 1559 HOH   HOH A . 
M 7 HOH   532 1332 563  HOH   HOH A . 
M 7 HOH   533 1333 298  HOH   HOH A . 
M 7 HOH   534 1334 786  HOH   HOH A . 
M 7 HOH   535 1335 795  HOH   HOH A . 
M 7 HOH   536 1336 836  HOH   HOH A . 
M 7 HOH   537 1337 1444 HOH   HOH A . 
M 7 HOH   538 1338 1239 HOH   HOH A . 
M 7 HOH   539 1339 813  HOH   HOH A . 
M 7 HOH   540 1340 1320 HOH   HOH A . 
M 7 HOH   541 1341 1055 HOH   HOH A . 
M 7 HOH   542 1342 105  HOH   HOH A . 
M 7 HOH   543 1343 1513 HOH   HOH A . 
M 7 HOH   544 1344 1185 HOH   HOH A . 
M 7 HOH   545 1345 490  HOH   HOH A . 
M 7 HOH   546 1346 1409 HOH   HOH A . 
M 7 HOH   547 1347 502  HOH   HOH A . 
M 7 HOH   548 1348 1427 HOH   HOH A . 
M 7 HOH   549 1349 1464 HOH   HOH A . 
M 7 HOH   550 1350 1027 HOH   HOH A . 
M 7 HOH   551 1351 772  HOH   HOH A . 
M 7 HOH   552 1352 1175 HOH   HOH A . 
M 7 HOH   553 1353 625  HOH   HOH A . 
M 7 HOH   554 1354 917  HOH   HOH A . 
M 7 HOH   555 1355 1073 HOH   HOH A . 
M 7 HOH   556 1356 694  HOH   HOH A . 
M 7 HOH   557 1357 840  HOH   HOH A . 
M 7 HOH   558 1358 1480 HOH   HOH A . 
M 7 HOH   559 1359 472  HOH   HOH A . 
M 7 HOH   560 1360 447  HOH   HOH A . 
M 7 HOH   561 1361 1549 HOH   HOH A . 
M 7 HOH   562 1362 870  HOH   HOH A . 
M 7 HOH   563 1363 1251 HOH   HOH A . 
M 7 HOH   564 1364 1322 HOH   HOH A . 
M 7 HOH   565 1365 1349 HOH   HOH A . 
M 7 HOH   566 1366 776  HOH   HOH A . 
M 7 HOH   567 1367 783  HOH   HOH A . 
M 7 HOH   568 1368 1398 HOH   HOH A . 
M 7 HOH   569 1369 1429 HOH   HOH A . 
M 7 HOH   570 1370 1123 HOH   HOH A . 
M 7 HOH   571 1371 467  HOH   HOH A . 
M 7 HOH   572 1372 925  HOH   HOH A . 
M 7 HOH   573 1373 1314 HOH   HOH A . 
M 7 HOH   574 1374 587  HOH   HOH A . 
M 7 HOH   575 1375 1188 HOH   HOH A . 
M 7 HOH   576 1376 700  HOH   HOH A . 
M 7 HOH   577 1377 910  HOH   HOH A . 
M 7 HOH   578 1378 208  HOH   HOH A . 
M 7 HOH   579 1379 481  HOH   HOH A . 
M 7 HOH   580 1380 1542 HOH   HOH A . 
M 7 HOH   581 1381 1026 HOH   HOH A . 
M 7 HOH   582 1382 724  HOH   HOH A . 
M 7 HOH   583 1383 1433 HOH   HOH A . 
M 7 HOH   584 1384 372  HOH   HOH A . 
M 7 HOH   585 1385 1126 HOH   HOH A . 
M 7 HOH   586 1386 1186 HOH   HOH A . 
M 7 HOH   587 1387 735  HOH   HOH A . 
M 7 HOH   588 1388 616  HOH   HOH A . 
M 7 HOH   589 1389 1134 HOH   HOH A . 
M 7 HOH   590 1390 1533 HOH   HOH A . 
M 7 HOH   591 1391 749  HOH   HOH A . 
M 7 HOH   592 1392 1488 HOH   HOH A . 
M 7 HOH   593 1393 1496 HOH   HOH A . 
M 7 HOH   594 1394 174  HOH   HOH A . 
M 7 HOH   595 1395 851  HOH   HOH A . 
M 7 HOH   596 1396 1162 HOH   HOH A . 
M 7 HOH   597 1397 276  HOH   HOH A . 
M 7 HOH   598 1398 1289 HOH   HOH A . 
M 7 HOH   599 1399 548  HOH   HOH A . 
M 7 HOH   600 1400 1008 HOH   HOH A . 
M 7 HOH   601 1401 1319 HOH   HOH A . 
M 7 HOH   602 1402 1382 HOH   HOH A . 
M 7 HOH   603 1403 494  HOH   HOH A . 
M 7 HOH   604 1404 1124 HOH   HOH A . 
M 7 HOH   605 1405 338  HOH   HOH A . 
M 7 HOH   606 1406 463  HOH   HOH A . 
M 7 HOH   607 1407 954  HOH   HOH A . 
M 7 HOH   608 1408 1483 HOH   HOH A . 
M 7 HOH   609 1409 963  HOH   HOH A . 
M 7 HOH   610 1410 538  HOH   HOH A . 
M 7 HOH   611 1411 1309 HOH   HOH A . 
M 7 HOH   612 1412 1562 HOH   HOH A . 
M 7 HOH   613 1413 1107 HOH   HOH A . 
M 7 HOH   614 1414 939  HOH   HOH A . 
M 7 HOH   615 1415 1554 HOH   HOH A . 
M 7 HOH   616 1416 609  HOH   HOH A . 
M 7 HOH   617 1417 1415 HOH   HOH A . 
M 7 HOH   618 1418 1161 HOH   HOH A . 
M 7 HOH   619 1419 1035 HOH   HOH A . 
M 7 HOH   620 1420 1555 HOH   HOH A . 
M 7 HOH   621 1421 1135 HOH   HOH A . 
M 7 HOH   622 1422 673  HOH   HOH A . 
M 7 HOH   623 1423 517  HOH   HOH A . 
M 7 HOH   624 1424 1315 HOH   HOH A . 
M 7 HOH   625 1425 1068 HOH   HOH A . 
M 7 HOH   626 1426 1250 HOH   HOH A . 
M 7 HOH   627 1427 1487 HOH   HOH A . 
M 7 HOH   628 1428 1540 HOH   HOH A . 
M 7 HOH   629 1429 1372 HOH   HOH A . 
M 7 HOH   630 1430 993  HOH   HOH A . 
M 7 HOH   631 1431 858  HOH   HOH A . 
M 7 HOH   632 1432 622  HOH   HOH A . 
M 7 HOH   633 1433 1200 HOH   HOH A . 
M 7 HOH   634 1434 904  HOH   HOH A . 
M 7 HOH   635 1435 705  HOH   HOH A . 
M 7 HOH   636 1436 921  HOH   HOH A . 
M 7 HOH   637 1437 746  HOH   HOH A . 
M 7 HOH   638 1438 702  HOH   HOH A . 
M 7 HOH   639 1439 1486 HOH   HOH A . 
M 7 HOH   640 1440 1054 HOH   HOH A . 
M 7 HOH   641 1441 1021 HOH   HOH A . 
M 7 HOH   642 1442 434  HOH   HOH A . 
M 7 HOH   643 1443 176  HOH   HOH A . 
M 7 HOH   644 1444 1526 HOH   HOH A . 
M 7 HOH   645 1445 919  HOH   HOH A . 
M 7 HOH   646 1446 165  HOH   HOH A . 
M 7 HOH   647 1447 785  HOH   HOH A . 
M 7 HOH   648 1448 1230 HOH   HOH A . 
M 7 HOH   649 1449 872  HOH   HOH A . 
M 7 HOH   650 1450 941  HOH   HOH A . 
M 7 HOH   651 1451 1002 HOH   HOH A . 
M 7 HOH   652 1452 1374 HOH   HOH A . 
M 7 HOH   653 1453 968  HOH   HOH A . 
M 7 HOH   654 1454 815  HOH   HOH A . 
M 7 HOH   655 1455 653  HOH   HOH A . 
M 7 HOH   656 1456 1537 HOH   HOH A . 
M 7 HOH   657 1457 573  HOH   HOH A . 
M 7 HOH   658 1458 1299 HOH   HOH A . 
M 7 HOH   659 1459 656  HOH   HOH A . 
M 7 HOH   660 1460 206  HOH   HOH A . 
M 7 HOH   661 1461 584  HOH   HOH A . 
M 7 HOH   662 1462 635  HOH   HOH A . 
M 7 HOH   663 1463 1164 HOH   HOH A . 
M 7 HOH   664 1464 714  HOH   HOH A . 
M 7 HOH   665 1465 1033 HOH   HOH A . 
M 7 HOH   666 1466 977  HOH   HOH A . 
M 7 HOH   667 1467 640  HOH   HOH A . 
M 7 HOH   668 1468 716  HOH   HOH A . 
M 7 HOH   669 1469 407  HOH   HOH A . 
M 7 HOH   670 1470 1323 HOH   HOH A . 
M 7 HOH   671 1471 198  HOH   HOH A . 
M 7 HOH   672 1472 869  HOH   HOH A . 
M 7 HOH   673 1473 1425 HOH   HOH A . 
M 7 HOH   674 1474 1326 HOH   HOH A . 
M 7 HOH   675 1475 1082 HOH   HOH A . 
M 7 HOH   676 1476 929  HOH   HOH A . 
M 7 HOH   677 1477 758  HOH   HOH A . 
M 7 HOH   678 1478 1501 HOH   HOH A . 
M 7 HOH   679 1479 1184 HOH   HOH A . 
M 7 HOH   680 1480 998  HOH   HOH A . 
M 7 HOH   681 1481 655  HOH   HOH A . 
M 7 HOH   682 1482 1227 HOH   HOH A . 
M 7 HOH   683 1483 818  HOH   HOH A . 
M 7 HOH   684 1484 1329 HOH   HOH A . 
M 7 HOH   685 1485 990  HOH   HOH A . 
M 7 HOH   686 1486 485  HOH   HOH A . 
M 7 HOH   687 1487 1519 HOH   HOH A . 
M 7 HOH   688 1488 715  HOH   HOH A . 
M 7 HOH   689 1489 657  HOH   HOH A . 
M 7 HOH   690 1490 992  HOH   HOH A . 
M 7 HOH   691 1491 988  HOH   HOH A . 
M 7 HOH   692 1492 890  HOH   HOH A . 
M 7 HOH   693 1493 1336 HOH   HOH A . 
M 7 HOH   694 1494 966  HOH   HOH A . 
M 7 HOH   695 1495 771  HOH   HOH A . 
M 7 HOH   696 1496 1104 HOH   HOH A . 
M 7 HOH   697 1497 474  HOH   HOH A . 
M 7 HOH   698 1498 1058 HOH   HOH A . 
M 7 HOH   699 1499 887  HOH   HOH A . 
M 7 HOH   700 1500 592  HOH   HOH A . 
M 7 HOH   701 1501 1064 HOH   HOH A . 
M 7 HOH   702 1502 737  HOH   HOH A . 
M 7 HOH   703 1503 1414 HOH   HOH A . 
M 7 HOH   704 1504 753  HOH   HOH A . 
M 7 HOH   705 1505 107  HOH   HOH A . 
M 7 HOH   706 1506 383  HOH   HOH A . 
M 7 HOH   707 1507 1089 HOH   HOH A . 
M 7 HOH   708 1508 1536 HOH   HOH A . 
M 7 HOH   709 1509 661  HOH   HOH A . 
M 7 HOH   710 1510 395  HOH   HOH A . 
M 7 HOH   711 1511 1545 HOH   HOH A . 
M 7 HOH   712 1512 1087 HOH   HOH A . 
M 7 HOH   713 1513 924  HOH   HOH A . 
M 7 HOH   714 1514 337  HOH   HOH A . 
M 7 HOH   715 1515 697  HOH   HOH A . 
M 7 HOH   716 1516 144  HOH   HOH A . 
M 7 HOH   717 1517 378  HOH   HOH A . 
M 7 HOH   718 1518 419  HOH   HOH A . 
M 7 HOH   719 1519 1532 HOH   HOH A . 
M 7 HOH   720 1520 575  HOH   HOH A . 
M 7 HOH   721 1521 861  HOH   HOH A . 
M 7 HOH   722 1522 932  HOH   HOH A . 
M 7 HOH   723 1523 95   HOH   HOH A . 
M 7 HOH   724 1524 751  HOH   HOH A . 
M 7 HOH   725 1525 303  HOH   HOH A . 
M 7 HOH   726 1526 1156 HOH   HOH A . 
M 7 HOH   727 1527 970  HOH   HOH A . 
M 7 HOH   728 1528 770  HOH   HOH A . 
M 7 HOH   729 1529 962  HOH   HOH A . 
M 7 HOH   730 1530 608  HOH   HOH A . 
M 7 HOH   731 1531 1069 HOH   HOH A . 
M 7 HOH   732 1532 323  HOH   HOH A . 
M 7 HOH   733 1533 1282 HOH   HOH A . 
M 7 HOH   734 1534 1307 HOH   HOH A . 
M 7 HOH   735 1535 1518 HOH   HOH A . 
M 7 HOH   736 1536 1472 HOH   HOH A . 
M 7 HOH   737 1537 1531 HOH   HOH A . 
M 7 HOH   738 1538 914  HOH   HOH A . 
M 7 HOH   739 1539 319  HOH   HOH A . 
M 7 HOH   740 1540 1442 HOH   HOH A . 
M 7 HOH   741 1541 1332 HOH   HOH A . 
M 7 HOH   742 1542 745  HOH   HOH A . 
M 7 HOH   743 1543 1255 HOH   HOH A . 
M 7 HOH   744 1544 911  HOH   HOH A . 
M 7 HOH   745 1545 1225 HOH   HOH A . 
M 7 HOH   746 1546 1275 HOH   HOH A . 
M 7 HOH   747 1547 955  HOH   HOH A . 
M 7 HOH   748 1548 359  HOH   HOH A . 
M 7 HOH   749 1549 1313 HOH   HOH A . 
M 7 HOH   750 1550 602  HOH   HOH A . 
M 7 HOH   751 1551 821  HOH   HOH A . 
M 7 HOH   752 1552 893  HOH   HOH A . 
M 7 HOH   753 1553 1358 HOH   HOH A . 
M 7 HOH   754 1554 889  HOH   HOH A . 
M 7 HOH   755 1555 897  HOH   HOH A . 
M 7 HOH   756 1556 1052 HOH   HOH A . 
M 7 HOH   757 1557 461  HOH   HOH A . 
M 7 HOH   758 1558 1117 HOH   HOH A . 
M 7 HOH   759 1559 596  HOH   HOH A . 
M 7 HOH   760 1560 762  HOH   HOH A . 
M 7 HOH   761 1561 409  HOH   HOH A . 
M 7 HOH   762 1562 1029 HOH   HOH A . 
M 7 HOH   763 1563 170  HOH   HOH A . 
M 7 HOH   764 1564 1279 HOH   HOH A . 
M 7 HOH   765 1565 1453 HOH   HOH A . 
M 7 HOH   766 1566 1357 HOH   HOH A . 
M 7 HOH   767 1567 612  HOH   HOH A . 
M 7 HOH   768 1568 1032 HOH   HOH A . 
M 7 HOH   769 1569 1534 HOH   HOH A . 
M 7 HOH   770 1570 1001 HOH   HOH A . 
M 7 HOH   771 1571 853  HOH   HOH A . 
M 7 HOH   772 1572 385  HOH   HOH A . 
M 7 HOH   773 1573 403  HOH   HOH A . 
M 7 HOH   774 1574 698  HOH   HOH A . 
M 7 HOH   775 1575 544  HOH   HOH A . 
M 7 HOH   776 1576 1060 HOH   HOH A . 
M 7 HOH   777 1577 747  HOH   HOH A . 
M 7 HOH   778 1578 1059 HOH   HOH A . 
M 7 HOH   779 1579 1183 HOH   HOH A . 
M 7 HOH   780 1580 1147 HOH   HOH A . 
M 7 HOH   781 1581 886  HOH   HOH A . 
M 7 HOH   782 1582 880  HOH   HOH A . 
M 7 HOH   783 1583 1321 HOH   HOH A . 
N 7 HOH   1   801  1558 HOH   HOH B . 
N 7 HOH   2   802  1547 HOH   HOH B . 
N 7 HOH   3   803  1544 HOH   HOH B . 
N 7 HOH   4   804  922  HOH   HOH B . 
N 7 HOH   5   805  1014 HOH   HOH B . 
N 7 HOH   6   806  1474 HOH   HOH B . 
N 7 HOH   7   807  1130 HOH   HOH B . 
N 7 HOH   8   808  495  HOH   HOH B . 
N 7 HOH   9   809  1473 HOH   HOH B . 
N 7 HOH   10  810  390  HOH   HOH B . 
N 7 HOH   11  811  6    HOH   HOH B . 
N 7 HOH   12  812  23   HOH   HOH B . 
N 7 HOH   13  813  1074 HOH   HOH B . 
N 7 HOH   14  814  162  HOH   HOH B . 
N 7 HOH   15  815  1525 HOH   HOH B . 
N 7 HOH   16  816  299  HOH   HOH B . 
N 7 HOH   17  817  611  HOH   HOH B . 
N 7 HOH   18  818  305  HOH   HOH B . 
N 7 HOH   19  819  94   HOH   HOH B . 
N 7 HOH   20  820  31   HOH   HOH B . 
N 7 HOH   21  821  873  HOH   HOH B . 
N 7 HOH   22  822  339  HOH   HOH B . 
N 7 HOH   23  823  742  HOH   HOH B . 
N 7 HOH   24  824  709  HOH   HOH B . 
N 7 HOH   25  825  884  HOH   HOH B . 
N 7 HOH   26  826  740  HOH   HOH B . 
N 7 HOH   27  827  1182 HOH   HOH B . 
N 7 HOH   28  828  1551 HOH   HOH B . 
N 7 HOH   29  829  1308 HOH   HOH B . 
N 7 HOH   30  830  325  HOH   HOH B . 
N 7 HOH   31  831  309  HOH   HOH B . 
N 7 HOH   32  832  1128 HOH   HOH B . 
N 7 HOH   33  833  117  HOH   HOH B . 
N 7 HOH   34  834  248  HOH   HOH B . 
N 7 HOH   35  835  594  HOH   HOH B . 
N 7 HOH   36  836  631  HOH   HOH B . 
N 7 HOH   37  837  119  HOH   HOH B . 
N 7 HOH   38  838  8    HOH   HOH B . 
N 7 HOH   39  839  723  HOH   HOH B . 
N 7 HOH   40  840  408  HOH   HOH B . 
N 7 HOH   41  841  989  HOH   HOH B . 
N 7 HOH   42  842  125  HOH   HOH B . 
N 7 HOH   43  843  150  HOH   HOH B . 
N 7 HOH   44  844  473  HOH   HOH B . 
N 7 HOH   45  845  1286 HOH   HOH B . 
N 7 HOH   46  846  654  HOH   HOH B . 
N 7 HOH   47  847  550  HOH   HOH B . 
N 7 HOH   48  848  1028 HOH   HOH B . 
N 7 HOH   49  849  376  HOH   HOH B . 
N 7 HOH   50  850  180  HOH   HOH B . 
N 7 HOH   51  851  585  HOH   HOH B . 
N 7 HOH   52  852  283  HOH   HOH B . 
N 7 HOH   53  853  545  HOH   HOH B . 
N 7 HOH   54  854  1167 HOH   HOH B . 
N 7 HOH   55  855  158  HOH   HOH B . 
N 7 HOH   56  856  411  HOH   HOH B . 
N 7 HOH   57  857  718  HOH   HOH B . 
N 7 HOH   58  858  1401 HOH   HOH B . 
N 7 HOH   59  859  1180 HOH   HOH B . 
N 7 HOH   60  860  147  HOH   HOH B . 
N 7 HOH   61  861  915  HOH   HOH B . 
N 7 HOH   62  862  96   HOH   HOH B . 
N 7 HOH   63  863  1113 HOH   HOH B . 
N 7 HOH   64  864  1245 HOH   HOH B . 
N 7 HOH   65  865  1197 HOH   HOH B . 
N 7 HOH   66  866  233  HOH   HOH B . 
N 7 HOH   67  867  315  HOH   HOH B . 
N 7 HOH   68  868  883  HOH   HOH B . 
N 7 HOH   69  869  686  HOH   HOH B . 
N 7 HOH   70  870  995  HOH   HOH B . 
N 7 HOH   71  871  767  HOH   HOH B . 
N 7 HOH   72  872  313  HOH   HOH B . 
N 7 HOH   73  873  986  HOH   HOH B . 
N 7 HOH   74  874  253  HOH   HOH B . 
N 7 HOH   75  875  15   HOH   HOH B . 
N 7 HOH   76  876  781  HOH   HOH B . 
N 7 HOH   77  877  729  HOH   HOH B . 
N 7 HOH   78  878  120  HOH   HOH B . 
N 7 HOH   79  879  77   HOH   HOH B . 
N 7 HOH   80  880  203  HOH   HOH B . 
N 7 HOH   81  881  532  HOH   HOH B . 
N 7 HOH   82  882  574  HOH   HOH B . 
N 7 HOH   83  883  1454 HOH   HOH B . 
N 7 HOH   84  884  1312 HOH   HOH B . 
N 7 HOH   85  885  926  HOH   HOH B . 
N 7 HOH   86  886  1368 HOH   HOH B . 
N 7 HOH   87  887  104  HOH   HOH B . 
N 7 HOH   88  888  167  HOH   HOH B . 
N 7 HOH   89  889  50   HOH   HOH B . 
N 7 HOH   90  890  227  HOH   HOH B . 
N 7 HOH   91  891  720  HOH   HOH B . 
N 7 HOH   92  892  311  HOH   HOH B . 
N 7 HOH   93  893  273  HOH   HOH B . 
N 7 HOH   94  894  946  HOH   HOH B . 
N 7 HOH   95  895  240  HOH   HOH B . 
N 7 HOH   96  896  526  HOH   HOH B . 
N 7 HOH   97  897  534  HOH   HOH B . 
N 7 HOH   98  898  53   HOH   HOH B . 
N 7 HOH   99  899  633  HOH   HOH B . 
N 7 HOH   100 900  87   HOH   HOH B . 
N 7 HOH   101 901  93   HOH   HOH B . 
N 7 HOH   102 902  806  HOH   HOH B . 
N 7 HOH   103 903  302  HOH   HOH B . 
N 7 HOH   104 904  24   HOH   HOH B . 
N 7 HOH   105 905  898  HOH   HOH B . 
N 7 HOH   106 906  567  HOH   HOH B . 
N 7 HOH   107 907  983  HOH   HOH B . 
N 7 HOH   108 908  1328 HOH   HOH B . 
N 7 HOH   109 909  9    HOH   HOH B . 
N 7 HOH   110 910  527  HOH   HOH B . 
N 7 HOH   111 911  965  HOH   HOH B . 
N 7 HOH   112 912  948  HOH   HOH B . 
N 7 HOH   113 913  1038 HOH   HOH B . 
N 7 HOH   114 914  864  HOH   HOH B . 
N 7 HOH   115 915  450  HOH   HOH B . 
N 7 HOH   116 916  327  HOH   HOH B . 
N 7 HOH   117 917  1421 HOH   HOH B . 
N 7 HOH   118 918  142  HOH   HOH B . 
N 7 HOH   119 919  556  HOH   HOH B . 
N 7 HOH   120 920  272  HOH   HOH B . 
N 7 HOH   121 921  267  HOH   HOH B . 
N 7 HOH   122 922  787  HOH   HOH B . 
N 7 HOH   123 923  352  HOH   HOH B . 
N 7 HOH   124 924  1258 HOH   HOH B . 
N 7 HOH   125 925  384  HOH   HOH B . 
N 7 HOH   126 926  109  HOH   HOH B . 
N 7 HOH   127 927  141  HOH   HOH B . 
N 7 HOH   128 928  277  HOH   HOH B . 
N 7 HOH   129 929  1012 HOH   HOH B . 
N 7 HOH   130 930  732  HOH   HOH B . 
N 7 HOH   131 931  113  HOH   HOH B . 
N 7 HOH   132 932  196  HOH   HOH B . 
N 7 HOH   133 933  238  HOH   HOH B . 
N 7 HOH   134 934  844  HOH   HOH B . 
N 7 HOH   135 935  1061 HOH   HOH B . 
N 7 HOH   136 936  1465 HOH   HOH B . 
N 7 HOH   137 937  1174 HOH   HOH B . 
N 7 HOH   138 938  263  HOH   HOH B . 
N 7 HOH   139 939  254  HOH   HOH B . 
N 7 HOH   140 940  819  HOH   HOH B . 
N 7 HOH   141 941  514  HOH   HOH B . 
N 7 HOH   142 942  230  HOH   HOH B . 
N 7 HOH   143 943  1015 HOH   HOH B . 
N 7 HOH   144 944  295  HOH   HOH B . 
N 7 HOH   145 945  398  HOH   HOH B . 
N 7 HOH   146 946  212  HOH   HOH B . 
N 7 HOH   147 947  420  HOH   HOH B . 
N 7 HOH   148 948  62   HOH   HOH B . 
N 7 HOH   149 949  294  HOH   HOH B . 
N 7 HOH   150 950  316  HOH   HOH B . 
N 7 HOH   151 951  1173 HOH   HOH B . 
N 7 HOH   152 952  972  HOH   HOH B . 
N 7 HOH   153 953  588  HOH   HOH B . 
N 7 HOH   154 954  504  HOH   HOH B . 
N 7 HOH   155 955  68   HOH   HOH B . 
N 7 HOH   156 956  128  HOH   HOH B . 
N 7 HOH   157 957  1353 HOH   HOH B . 
N 7 HOH   158 958  492  HOH   HOH B . 
N 7 HOH   159 959  163  HOH   HOH B . 
N 7 HOH   160 960  103  HOH   HOH B . 
N 7 HOH   161 961  944  HOH   HOH B . 
N 7 HOH   162 962  942  HOH   HOH B . 
N 7 HOH   163 963  63   HOH   HOH B . 
N 7 HOH   164 964  69   HOH   HOH B . 
N 7 HOH   165 965  1148 HOH   HOH B . 
N 7 HOH   166 966  29   HOH   HOH B . 
N 7 HOH   167 967  149  HOH   HOH B . 
N 7 HOH   168 968  124  HOH   HOH B . 
N 7 HOH   169 969  328  HOH   HOH B . 
N 7 HOH   170 970  799  HOH   HOH B . 
N 7 HOH   171 971  645  HOH   HOH B . 
N 7 HOH   172 972  536  HOH   HOH B . 
N 7 HOH   173 973  644  HOH   HOH B . 
N 7 HOH   174 974  45   HOH   HOH B . 
N 7 HOH   175 975  999  HOH   HOH B . 
N 7 HOH   176 976  1435 HOH   HOH B . 
N 7 HOH   177 977  91   HOH   HOH B . 
N 7 HOH   178 978  37   HOH   HOH B . 
N 7 HOH   179 979  259  HOH   HOH B . 
N 7 HOH   180 980  1231 HOH   HOH B . 
N 7 HOH   181 981  496  HOH   HOH B . 
N 7 HOH   182 982  264  HOH   HOH B . 
N 7 HOH   183 983  455  HOH   HOH B . 
N 7 HOH   184 984  593  HOH   HOH B . 
N 7 HOH   185 985  1446 HOH   HOH B . 
N 7 HOH   186 986  557  HOH   HOH B . 
N 7 HOH   187 987  1094 HOH   HOH B . 
N 7 HOH   188 988  535  HOH   HOH B . 
N 7 HOH   189 989  1303 HOH   HOH B . 
N 7 HOH   190 990  601  HOH   HOH B . 
N 7 HOH   191 991  1080 HOH   HOH B . 
N 7 HOH   192 992  765  HOH   HOH B . 
N 7 HOH   193 993  284  HOH   HOH B . 
N 7 HOH   194 994  48   HOH   HOH B . 
N 7 HOH   195 995  591  HOH   HOH B . 
N 7 HOH   196 996  355  HOH   HOH B . 
N 7 HOH   197 997  280  HOH   HOH B . 
N 7 HOH   198 998  856  HOH   HOH B . 
N 7 HOH   199 999  542  HOH   HOH B . 
N 7 HOH   200 1000 270  HOH   HOH B . 
N 7 HOH   201 1001 1217 HOH   HOH B . 
N 7 HOH   202 1002 830  HOH   HOH B . 
N 7 HOH   203 1003 375  HOH   HOH B . 
N 7 HOH   204 1004 894  HOH   HOH B . 
N 7 HOH   205 1005 651  HOH   HOH B . 
N 7 HOH   206 1006 214  HOH   HOH B . 
N 7 HOH   207 1007 28   HOH   HOH B . 
N 7 HOH   208 1008 33   HOH   HOH B . 
N 7 HOH   209 1009 797  HOH   HOH B . 
N 7 HOH   210 1010 519  HOH   HOH B . 
N 7 HOH   211 1011 1111 HOH   HOH B . 
N 7 HOH   212 1012 1169 HOH   HOH B . 
N 7 HOH   213 1013 712  HOH   HOH B . 
N 7 HOH   214 1014 64   HOH   HOH B . 
N 7 HOH   215 1015 132  HOH   HOH B . 
N 7 HOH   216 1016 90   HOH   HOH B . 
N 7 HOH   217 1017 750  HOH   HOH B . 
N 7 HOH   218 1018 1179 HOH   HOH B . 
N 7 HOH   219 1019 874  HOH   HOH B . 
N 7 HOH   220 1020 1101 HOH   HOH B . 
N 7 HOH   221 1021 1268 HOH   HOH B . 
N 7 HOH   222 1022 748  HOH   HOH B . 
N 7 HOH   223 1023 44   HOH   HOH B . 
N 7 HOH   224 1024 991  HOH   HOH B . 
N 7 HOH   225 1025 792  HOH   HOH B . 
N 7 HOH   226 1026 483  HOH   HOH B . 
N 7 HOH   227 1027 701  HOH   HOH B . 
N 7 HOH   228 1028 1448 HOH   HOH B . 
N 7 HOH   229 1029 54   HOH   HOH B . 
N 7 HOH   230 1030 1246 HOH   HOH B . 
N 7 HOH   231 1031 850  HOH   HOH B . 
N 7 HOH   232 1032 1153 HOH   HOH B . 
N 7 HOH   233 1033 476  HOH   HOH B . 
N 7 HOH   234 1034 154  HOH   HOH B . 
N 7 HOH   235 1035 674  HOH   HOH B . 
N 7 HOH   236 1036 901  HOH   HOH B . 
N 7 HOH   237 1037 354  HOH   HOH B . 
N 7 HOH   238 1038 136  HOH   HOH B . 
N 7 HOH   239 1039 796  HOH   HOH B . 
N 7 HOH   240 1040 518  HOH   HOH B . 
N 7 HOH   241 1041 137  HOH   HOH B . 
N 7 HOH   242 1042 1127 HOH   HOH B . 
N 7 HOH   243 1043 1023 HOH   HOH B . 
N 7 HOH   244 1044 410  HOH   HOH B . 
N 7 HOH   245 1045 123  HOH   HOH B . 
N 7 HOH   246 1046 687  HOH   HOH B . 
N 7 HOH   247 1047 423  HOH   HOH B . 
N 7 HOH   248 1048 847  HOH   HOH B . 
N 7 HOH   249 1049 1263 HOH   HOH B . 
N 7 HOH   250 1050 675  HOH   HOH B . 
N 7 HOH   251 1051 1548 HOH   HOH B . 
N 7 HOH   252 1052 690  HOH   HOH B . 
N 7 HOH   253 1053 1157 HOH   HOH B . 
N 7 HOH   254 1054 454  HOH   HOH B . 
N 7 HOH   255 1055 1233 HOH   HOH B . 
N 7 HOH   256 1056 671  HOH   HOH B . 
N 7 HOH   257 1057 523  HOH   HOH B . 
N 7 HOH   258 1058 1030 HOH   HOH B . 
N 7 HOH   259 1059 931  HOH   HOH B . 
N 7 HOH   260 1060 275  HOH   HOH B . 
N 7 HOH   261 1061 1063 HOH   HOH B . 
N 7 HOH   262 1062 1116 HOH   HOH B . 
N 7 HOH   263 1063 478  HOH   HOH B . 
N 7 HOH   264 1064 221  HOH   HOH B . 
N 7 HOH   265 1065 896  HOH   HOH B . 
N 7 HOH   266 1066 357  HOH   HOH B . 
N 7 HOH   267 1067 1151 HOH   HOH B . 
N 7 HOH   268 1068 501  HOH   HOH B . 
N 7 HOH   269 1069 685  HOH   HOH B . 
N 7 HOH   270 1070 428  HOH   HOH B . 
N 7 HOH   271 1071 279  HOH   HOH B . 
N 7 HOH   272 1072 1132 HOH   HOH B . 
N 7 HOH   273 1073 1203 HOH   HOH B . 
N 7 HOH   274 1074 173  HOH   HOH B . 
N 7 HOH   275 1075 1048 HOH   HOH B . 
N 7 HOH   276 1076 900  HOH   HOH B . 
N 7 HOH   277 1077 98   HOH   HOH B . 
N 7 HOH   278 1078 693  HOH   HOH B . 
N 7 HOH   279 1079 971  HOH   HOH B . 
N 7 HOH   280 1080 73   HOH   HOH B . 
N 7 HOH   281 1081 83   HOH   HOH B . 
N 7 HOH   282 1082 86   HOH   HOH B . 
N 7 HOH   283 1083 1114 HOH   HOH B . 
N 7 HOH   284 1084 286  HOH   HOH B . 
N 7 HOH   285 1085 282  HOH   HOH B . 
N 7 HOH   286 1086 436  HOH   HOH B . 
N 7 HOH   287 1087 987  HOH   HOH B . 
N 7 HOH   288 1088 961  HOH   HOH B . 
N 7 HOH   289 1089 49   HOH   HOH B . 
N 7 HOH   290 1090 628  HOH   HOH B . 
N 7 HOH   291 1091 326  HOH   HOH B . 
N 7 HOH   292 1092 515  HOH   HOH B . 
N 7 HOH   293 1093 646  HOH   HOH B . 
N 7 HOH   294 1094 627  HOH   HOH B . 
N 7 HOH   295 1095 777  HOH   HOH B . 
N 7 HOH   296 1096 21   HOH   HOH B . 
N 7 HOH   297 1097 1272 HOH   HOH B . 
N 7 HOH   298 1098 379  HOH   HOH B . 
N 7 HOH   299 1099 243  HOH   HOH B . 
N 7 HOH   300 1100 512  HOH   HOH B . 
N 7 HOH   301 1101 730  HOH   HOH B . 
N 7 HOH   302 1102 1190 HOH   HOH B . 
N 7 HOH   303 1103 727  HOH   HOH B . 
N 7 HOH   304 1104 1441 HOH   HOH B . 
N 7 HOH   305 1105 639  HOH   HOH B . 
N 7 HOH   306 1106 182  HOH   HOH B . 
N 7 HOH   307 1107 1440 HOH   HOH B . 
N 7 HOH   308 1108 1495 HOH   HOH B . 
N 7 HOH   309 1109 441  HOH   HOH B . 
N 7 HOH   310 1110 188  HOH   HOH B . 
N 7 HOH   311 1111 1469 HOH   HOH B . 
N 7 HOH   312 1112 1304 HOH   HOH B . 
N 7 HOH   313 1113 755  HOH   HOH B . 
N 7 HOH   314 1114 184  HOH   HOH B . 
N 7 HOH   315 1115 4    HOH   HOH B . 
N 7 HOH   316 1116 393  HOH   HOH B . 
N 7 HOH   317 1117 600  HOH   HOH B . 
N 7 HOH   318 1118 340  HOH   HOH B . 
N 7 HOH   319 1119 981  HOH   HOH B . 
N 7 HOH   320 1120 1384 HOH   HOH B . 
N 7 HOH   321 1121 854  HOH   HOH B . 
N 7 HOH   322 1122 503  HOH   HOH B . 
N 7 HOH   323 1123 1006 HOH   HOH B . 
N 7 HOH   324 1124 177  HOH   HOH B . 
N 7 HOH   325 1125 634  HOH   HOH B . 
N 7 HOH   326 1126 140  HOH   HOH B . 
N 7 HOH   327 1127 520  HOH   HOH B . 
N 7 HOH   328 1128 458  HOH   HOH B . 
N 7 HOH   329 1129 913  HOH   HOH B . 
N 7 HOH   330 1130 285  HOH   HOH B . 
N 7 HOH   331 1131 122  HOH   HOH B . 
N 7 HOH   332 1132 1515 HOH   HOH B . 
N 7 HOH   333 1133 659  HOH   HOH B . 
N 7 HOH   334 1134 1338 HOH   HOH B . 
N 7 HOH   335 1135 1455 HOH   HOH B . 
N 7 HOH   336 1136 808  HOH   HOH B . 
N 7 HOH   337 1137 160  HOH   HOH B . 
N 7 HOH   338 1138 1202 HOH   HOH B . 
N 7 HOH   339 1139 235  HOH   HOH B . 
N 7 HOH   340 1140 798  HOH   HOH B . 
N 7 HOH   341 1141 804  HOH   HOH B . 
N 7 HOH   342 1142 34   HOH   HOH B . 
N 7 HOH   343 1143 907  HOH   HOH B . 
N 7 HOH   344 1144 543  HOH   HOH B . 
N 7 HOH   345 1145 680  HOH   HOH B . 
N 7 HOH   346 1146 835  HOH   HOH B . 
N 7 HOH   347 1147 353  HOH   HOH B . 
N 7 HOH   348 1148 531  HOH   HOH B . 
N 7 HOH   349 1149 207  HOH   HOH B . 
N 7 HOH   350 1150 320  HOH   HOH B . 
N 7 HOH   351 1151 453  HOH   HOH B . 
N 7 HOH   352 1152 116  HOH   HOH B . 
N 7 HOH   353 1153 1317 HOH   HOH B . 
N 7 HOH   354 1154 366  HOH   HOH B . 
N 7 HOH   355 1155 530  HOH   HOH B . 
N 7 HOH   356 1156 1221 HOH   HOH B . 
N 7 HOH   357 1157 329  HOH   HOH B . 
N 7 HOH   358 1158 959  HOH   HOH B . 
N 7 HOH   359 1159 1007 HOH   HOH B . 
N 7 HOH   360 1160 1301 HOH   HOH B . 
N 7 HOH   361 1161 97   HOH   HOH B . 
N 7 HOH   362 1162 952  HOH   HOH B . 
N 7 HOH   363 1163 115  HOH   HOH B . 
N 7 HOH   364 1164 860  HOH   HOH B . 
N 7 HOH   365 1165 1367 HOH   HOH B . 
N 7 HOH   366 1166 370  HOH   HOH B . 
N 7 HOH   367 1167 237  HOH   HOH B . 
N 7 HOH   368 1168 102  HOH   HOH B . 
N 7 HOH   369 1169 739  HOH   HOH B . 
N 7 HOH   370 1170 1017 HOH   HOH B . 
N 7 HOH   371 1171 222  HOH   HOH B . 
N 7 HOH   372 1172 1266 HOH   HOH B . 
N 7 HOH   373 1173 865  HOH   HOH B . 
N 7 HOH   374 1174 405  HOH   HOH B . 
N 7 HOH   375 1175 1131 HOH   HOH B . 
N 7 HOH   376 1176 1043 HOH   HOH B . 
N 7 HOH   377 1177 157  HOH   HOH B . 
N 7 HOH   378 1178 976  HOH   HOH B . 
N 7 HOH   379 1179 1076 HOH   HOH B . 
N 7 HOH   380 1180 1490 HOH   HOH B . 
N 7 HOH   381 1181 489  HOH   HOH B . 
N 7 HOH   382 1182 1288 HOH   HOH B . 
N 7 HOH   383 1183 261  HOH   HOH B . 
N 7 HOH   384 1184 111  HOH   HOH B . 
N 7 HOH   385 1185 1083 HOH   HOH B . 
N 7 HOH   386 1186 833  HOH   HOH B . 
N 7 HOH   387 1187 1120 HOH   HOH B . 
N 7 HOH   388 1188 713  HOH   HOH B . 
N 7 HOH   389 1189 779  HOH   HOH B . 
N 7 HOH   390 1190 768  HOH   HOH B . 
N 7 HOH   391 1191 982  HOH   HOH B . 
N 7 HOH   392 1192 1238 HOH   HOH B . 
N 7 HOH   393 1193 1561 HOH   HOH B . 
N 7 HOH   394 1194 377  HOH   HOH B . 
N 7 HOH   395 1195 1306 HOH   HOH B . 
N 7 HOH   396 1196 1283 HOH   HOH B . 
N 7 HOH   397 1197 470  HOH   HOH B . 
N 7 HOH   398 1198 606  HOH   HOH B . 
N 7 HOH   399 1199 736  HOH   HOH B . 
N 7 HOH   400 1200 433  HOH   HOH B . 
N 7 HOH   401 1201 39   HOH   HOH B . 
N 7 HOH   402 1202 1350 HOH   HOH B . 
N 7 HOH   403 1203 933  HOH   HOH B . 
N 7 HOH   404 1204 1222 HOH   HOH B . 
N 7 HOH   405 1205 293  HOH   HOH B . 
N 7 HOH   406 1206 761  HOH   HOH B . 
N 7 HOH   407 1207 239  HOH   HOH B . 
N 7 HOH   408 1208 1129 HOH   HOH B . 
N 7 HOH   409 1209 1045 HOH   HOH B . 
N 7 HOH   410 1210 581  HOH   HOH B . 
N 7 HOH   411 1211 1512 HOH   HOH B . 
N 7 HOH   412 1212 1229 HOH   HOH B . 
N 7 HOH   413 1213 268  HOH   HOH B . 
N 7 HOH   414 1214 432  HOH   HOH B . 
N 7 HOH   415 1215 189  HOH   HOH B . 
N 7 HOH   416 1216 845  HOH   HOH B . 
N 7 HOH   417 1217 1376 HOH   HOH B . 
N 7 HOH   418 1218 1276 HOH   HOH B . 
N 7 HOH   419 1219 287  HOH   HOH B . 
N 7 HOH   420 1220 825  HOH   HOH B . 
N 7 HOH   421 1221 1546 HOH   HOH B . 
N 7 HOH   422 1222 953  HOH   HOH B . 
N 7 HOH   423 1223 1223 HOH   HOH B . 
N 7 HOH   424 1224 1539 HOH   HOH B . 
N 7 HOH   425 1225 665  HOH   HOH B . 
N 7 HOH   426 1226 1305 HOH   HOH B . 
N 7 HOH   427 1227 826  HOH   HOH B . 
N 7 HOH   428 1228 572  HOH   HOH B . 
N 7 HOH   429 1229 223  HOH   HOH B . 
N 7 HOH   430 1230 435  HOH   HOH B . 
N 7 HOH   431 1231 1244 HOH   HOH B . 
N 7 HOH   432 1232 297  HOH   HOH B . 
N 7 HOH   433 1233 733  HOH   HOH B . 
N 7 HOH   434 1234 217  HOH   HOH B . 
N 7 HOH   435 1235 256  HOH   HOH B . 
N 7 HOH   436 1236 1062 HOH   HOH B . 
N 7 HOH   437 1237 703  HOH   HOH B . 
N 7 HOH   438 1238 374  HOH   HOH B . 
N 7 HOH   439 1239 1371 HOH   HOH B . 
N 7 HOH   440 1240 1560 HOH   HOH B . 
N 7 HOH   441 1241 1218 HOH   HOH B . 
N 7 HOH   442 1242 812  HOH   HOH B . 
N 7 HOH   443 1243 1192 HOH   HOH B . 
N 7 HOH   444 1244 130  HOH   HOH B . 
N 7 HOH   445 1245 418  HOH   HOH B . 
N 7 HOH   446 1246 1100 HOH   HOH B . 
N 7 HOH   447 1247 832  HOH   HOH B . 
N 7 HOH   448 1248 1493 HOH   HOH B . 
N 7 HOH   449 1249 487  HOH   HOH B . 
N 7 HOH   450 1250 831  HOH   HOH B . 
N 7 HOH   451 1251 940  HOH   HOH B . 
N 7 HOH   452 1252 1242 HOH   HOH B . 
N 7 HOH   453 1253 1492 HOH   HOH B . 
N 7 HOH   454 1254 1437 HOH   HOH B . 
N 7 HOH   455 1255 1206 HOH   HOH B . 
N 7 HOH   456 1256 1419 HOH   HOH B . 
N 7 HOH   457 1257 790  HOH   HOH B . 
N 7 HOH   458 1258 1078 HOH   HOH B . 
N 7 HOH   459 1259 793  HOH   HOH B . 
N 7 HOH   460 1260 449  HOH   HOH B . 
N 7 HOH   461 1261 1400 HOH   HOH B . 
N 7 HOH   462 1262 446  HOH   HOH B . 
N 7 HOH   463 1263 35   HOH   HOH B . 
N 7 HOH   464 1264 1181 HOH   HOH B . 
N 7 HOH   465 1265 244  HOH   HOH B . 
N 7 HOH   466 1266 764  HOH   HOH B . 
N 7 HOH   467 1267 568  HOH   HOH B . 
N 7 HOH   468 1268 578  HOH   HOH B . 
N 7 HOH   469 1269 427  HOH   HOH B . 
N 7 HOH   470 1270 1410 HOH   HOH B . 
N 7 HOH   471 1271 1335 HOH   HOH B . 
N 7 HOH   472 1272 468  HOH   HOH B . 
N 7 HOH   473 1273 540  HOH   HOH B . 
N 7 HOH   474 1274 1267 HOH   HOH B . 
N 7 HOH   475 1275 801  HOH   HOH B . 
N 7 HOH   476 1276 1144 HOH   HOH B . 
N 7 HOH   477 1277 828  HOH   HOH B . 
N 7 HOH   478 1278 1509 HOH   HOH B . 
N 7 HOH   479 1279 422  HOH   HOH B . 
N 7 HOH   480 1280 1003 HOH   HOH B . 
N 7 HOH   481 1281 1293 HOH   HOH B . 
N 7 HOH   482 1282 1187 HOH   HOH B . 
N 7 HOH   483 1283 1040 HOH   HOH B . 
N 7 HOH   484 1284 626  HOH   HOH B . 
N 7 HOH   485 1285 923  HOH   HOH B . 
N 7 HOH   486 1286 895  HOH   HOH B . 
N 7 HOH   487 1287 1287 HOH   HOH B . 
N 7 HOH   488 1288 1122 HOH   HOH B . 
N 7 HOH   489 1289 475  HOH   HOH B . 
N 7 HOH   490 1290 310  HOH   HOH B . 
N 7 HOH   491 1291 1011 HOH   HOH B . 
N 7 HOH   492 1292 127  HOH   HOH B . 
N 7 HOH   493 1293 1385 HOH   HOH B . 
N 7 HOH   494 1294 1379 HOH   HOH B . 
N 7 HOH   495 1295 1177 HOH   HOH B . 
N 7 HOH   496 1296 1482 HOH   HOH B . 
N 7 HOH   497 1297 1369 HOH   HOH B . 
N 7 HOH   498 1298 842  HOH   HOH B . 
N 7 HOH   499 1299 42   HOH   HOH B . 
N 7 HOH   500 1300 603  HOH   HOH B . 
N 7 HOH   501 1301 139  HOH   HOH B . 
N 7 HOH   502 1302 881  HOH   HOH B . 
N 7 HOH   503 1303 153  HOH   HOH B . 
N 7 HOH   504 1304 975  HOH   HOH B . 
N 7 HOH   505 1305 1165 HOH   HOH B . 
N 7 HOH   506 1306 1143 HOH   HOH B . 
N 7 HOH   507 1307 994  HOH   HOH B . 
N 7 HOH   508 1308 780  HOH   HOH B . 
N 7 HOH   509 1309 1339 HOH   HOH B . 
N 7 HOH   510 1310 1412 HOH   HOH B . 
N 7 HOH   511 1311 1077 HOH   HOH B . 
N 7 HOH   512 1312 1158 HOH   HOH B . 
N 7 HOH   513 1313 1344 HOH   HOH B . 
N 7 HOH   514 1314 300  HOH   HOH B . 
N 7 HOH   515 1315 649  HOH   HOH B . 
N 7 HOH   516 1316 862  HOH   HOH B . 
N 7 HOH   517 1317 996  HOH   HOH B . 
N 7 HOH   518 1318 676  HOH   HOH B . 
N 7 HOH   519 1319 973  HOH   HOH B . 
N 7 HOH   520 1320 1331 HOH   HOH B . 
N 7 HOH   521 1321 814  HOH   HOH B . 
N 7 HOH   522 1322 57   HOH   HOH B . 
N 7 HOH   523 1323 876  HOH   HOH B . 
N 7 HOH   524 1324 855  HOH   HOH B . 
N 7 HOH   525 1325 1086 HOH   HOH B . 
N 7 HOH   526 1326 1507 HOH   HOH B . 
N 7 HOH   527 1327 1494 HOH   HOH B . 
N 7 HOH   528 1328 1053 HOH   HOH B . 
N 7 HOH   529 1329 1247 HOH   HOH B . 
N 7 HOH   530 1330 937  HOH   HOH B . 
N 7 HOH   531 1331 1145 HOH   HOH B . 
N 7 HOH   532 1332 462  HOH   HOH B . 
N 7 HOH   533 1333 652  HOH   HOH B . 
N 7 HOH   534 1334 899  HOH   HOH B . 
N 7 HOH   535 1335 1133 HOH   HOH B . 
N 7 HOH   536 1336 1477 HOH   HOH B . 
N 7 HOH   537 1337 1491 HOH   HOH B . 
N 7 HOH   538 1338 672  HOH   HOH B . 
N 7 HOH   539 1339 1081 HOH   HOH B . 
N 7 HOH   540 1340 1423 HOH   HOH B . 
N 7 HOH   541 1341 695  HOH   HOH B . 
N 7 HOH   542 1342 778  HOH   HOH B . 
N 7 HOH   543 1343 583  HOH   HOH B . 
N 7 HOH   544 1344 754  HOH   HOH B . 
N 7 HOH   545 1345 1443 HOH   HOH B . 
N 7 HOH   546 1346 1252 HOH   HOH B . 
N 7 HOH   547 1347 437  HOH   HOH B . 
N 7 HOH   548 1348 576  HOH   HOH B . 
N 7 HOH   549 1349 1413 HOH   HOH B . 
N 7 HOH   550 1350 1066 HOH   HOH B . 
N 7 HOH   551 1351 960  HOH   HOH B . 
N 7 HOH   552 1352 691  HOH   HOH B . 
N 7 HOH   553 1353 1377 HOH   HOH B . 
N 7 HOH   554 1354 560  HOH   HOH B . 
N 7 HOH   555 1355 231  HOH   HOH B . 
N 7 HOH   556 1356 1150 HOH   HOH B . 
N 7 HOH   557 1357 396  HOH   HOH B . 
N 7 HOH   558 1358 794  HOH   HOH B . 
N 7 HOH   559 1359 525  HOH   HOH B . 
N 7 HOH   560 1360 1020 HOH   HOH B . 
N 7 HOH   561 1361 878  HOH   HOH B . 
N 7 HOH   562 1362 807  HOH   HOH B . 
N 7 HOH   563 1363 565  HOH   HOH B . 
N 7 HOH   564 1364 604  HOH   HOH B . 
N 7 HOH   565 1365 1553 HOH   HOH B . 
N 7 HOH   566 1366 978  HOH   HOH B . 
N 7 HOH   567 1367 131  HOH   HOH B . 
N 7 HOH   568 1368 684  HOH   HOH B . 
N 7 HOH   569 1369 1146 HOH   HOH B . 
N 7 HOH   570 1370 1105 HOH   HOH B . 
N 7 HOH   571 1371 522  HOH   HOH B . 
N 7 HOH   572 1372 1065 HOH   HOH B . 
N 7 HOH   573 1373 1285 HOH   HOH B . 
N 7 HOH   574 1374 875  HOH   HOH B . 
N 7 HOH   575 1375 1211 HOH   HOH B . 
N 7 HOH   576 1376 743  HOH   HOH B . 
N 7 HOH   577 1377 443  HOH   HOH B . 
N 7 HOH   578 1378 1297 HOH   HOH B . 
N 7 HOH   579 1379 586  HOH   HOH B . 
N 7 HOH   580 1380 1459 HOH   HOH B . 
N 7 HOH   581 1381 1163 HOH   HOH B . 
N 7 HOH   582 1382 615  HOH   HOH B . 
N 7 HOH   583 1383 1172 HOH   HOH B . 
N 7 HOH   584 1384 1457 HOH   HOH B . 
N 7 HOH   585 1385 974  HOH   HOH B . 
N 7 HOH   586 1386 482  HOH   HOH B . 
N 7 HOH   587 1387 839  HOH   HOH B . 
N 7 HOH   588 1388 1256 HOH   HOH B . 
N 7 HOH   589 1389 1219 HOH   HOH B . 
N 7 HOH   590 1390 249  HOH   HOH B . 
N 7 HOH   591 1391 1106 HOH   HOH B . 
N 7 HOH   592 1392 950  HOH   HOH B . 
N 7 HOH   593 1393 1463 HOH   HOH B . 
N 7 HOH   594 1394 350  HOH   HOH B . 
N 7 HOH   595 1395 456  HOH   HOH B . 
N 7 HOH   596 1396 1232 HOH   HOH B . 
N 7 HOH   597 1397 444  HOH   HOH B . 
N 7 HOH   598 1398 1484 HOH   HOH B . 
N 7 HOH   599 1399 569  HOH   HOH B . 
N 7 HOH   600 1400 1168 HOH   HOH B . 
N 7 HOH   601 1401 775  HOH   HOH B . 
N 7 HOH   602 1402 129  HOH   HOH B . 
N 7 HOH   603 1403 630  HOH   HOH B . 
N 7 HOH   604 1404 1236 HOH   HOH B . 
N 7 HOH   605 1405 763  HOH   HOH B . 
N 7 HOH   606 1406 469  HOH   HOH B . 
N 7 HOH   607 1407 479  HOH   HOH B . 
N 7 HOH   608 1408 1042 HOH   HOH B . 
N 7 HOH   609 1409 1096 HOH   HOH B . 
N 7 HOH   610 1410 1302 HOH   HOH B . 
N 7 HOH   611 1411 1291 HOH   HOH B . 
N 7 HOH   612 1412 452  HOH   HOH B . 
N 7 HOH   613 1413 1072 HOH   HOH B . 
N 7 HOH   614 1414 916  HOH   HOH B . 
N 7 HOH   615 1415 1022 HOH   HOH B . 
N 7 HOH   616 1416 1274 HOH   HOH B . 
N 7 HOH   617 1417 1352 HOH   HOH B . 
N 7 HOH   618 1418 888  HOH   HOH B . 
N 7 HOH   619 1419 984  HOH   HOH B . 
N 7 HOH   620 1420 1292 HOH   HOH B . 
N 7 HOH   621 1421 205  HOH   HOH B . 
N 7 HOH   622 1422 769  HOH   HOH B . 
N 7 HOH   623 1423 1333 HOH   HOH B . 
N 7 HOH   624 1424 788  HOH   HOH B . 
N 7 HOH   625 1425 1396 HOH   HOH B . 
N 7 HOH   626 1426 1047 HOH   HOH B . 
N 7 HOH   627 1427 829  HOH   HOH B . 
N 7 HOH   628 1428 1550 HOH   HOH B . 
N 7 HOH   629 1429 928  HOH   HOH B . 
N 7 HOH   630 1430 166  HOH   HOH B . 
N 7 HOH   631 1431 667  HOH   HOH B . 
N 7 HOH   632 1432 891  HOH   HOH B . 
N 7 HOH   633 1433 1136 HOH   HOH B . 
N 7 HOH   634 1434 892  HOH   HOH B . 
N 7 HOH   635 1435 332  HOH   HOH B . 
N 7 HOH   636 1436 1207 HOH   HOH B . 
N 7 HOH   637 1437 1388 HOH   HOH B . 
N 7 HOH   638 1438 1402 HOH   HOH B . 
N 7 HOH   639 1439 623  HOH   HOH B . 
N 7 HOH   640 1440 879  HOH   HOH B . 
N 7 HOH   641 1441 688  HOH   HOH B . 
N 7 HOH   642 1442 1270 HOH   HOH B . 
N 7 HOH   643 1443 1478 HOH   HOH B . 
N 7 HOH   644 1444 1391 HOH   HOH B . 
N 7 HOH   645 1445 1119 HOH   HOH B . 
N 7 HOH   646 1446 957  HOH   HOH B . 
N 7 HOH   647 1447 1438 HOH   HOH B . 
N 7 HOH   648 1448 1085 HOH   HOH B . 
N 7 HOH   649 1449 1356 HOH   HOH B . 
N 7 HOH   650 1450 759  HOH   HOH B . 
N 7 HOH   651 1451 1346 HOH   HOH B . 
N 7 HOH   652 1452 1381 HOH   HOH B . 
N 7 HOH   653 1453 912  HOH   HOH B . 
N 7 HOH   654 1454 1155 HOH   HOH B . 
N 7 HOH   655 1455 979  HOH   HOH B . 
N 7 HOH   656 1456 1527 HOH   HOH B . 
N 7 HOH   657 1457 1259 HOH   HOH B . 
N 7 HOH   658 1458 1354 HOH   HOH B . 
N 7 HOH   659 1459 1037 HOH   HOH B . 
N 7 HOH   660 1460 725  HOH   HOH B . 
N 7 HOH   661 1461 947  HOH   HOH B . 
N 7 HOH   662 1462 507  HOH   HOH B . 
N 7 HOH   663 1463 1243 HOH   HOH B . 
N 7 HOH   664 1464 1271 HOH   HOH B . 
N 7 HOH   665 1465 368  HOH   HOH B . 
N 7 HOH   666 1466 1506 HOH   HOH B . 
N 7 HOH   667 1467 348  HOH   HOH B . 
N 7 HOH   668 1468 677  HOH   HOH B . 
N 7 HOH   669 1469 1137 HOH   HOH B . 
N 7 HOH   670 1470 1556 HOH   HOH B . 
N 7 HOH   671 1471 66   HOH   HOH B . 
N 7 HOH   672 1472 1056 HOH   HOH B . 
N 7 HOH   673 1473 935  HOH   HOH B . 
N 7 HOH   674 1474 1241 HOH   HOH B . 
N 7 HOH   675 1475 1067 HOH   HOH B . 
N 7 HOH   676 1476 1468 HOH   HOH B . 
N 7 HOH   677 1477 342  HOH   HOH B . 
N 7 HOH   678 1478 1093 HOH   HOH B . 
N 7 HOH   679 1479 464  HOH   HOH B . 
N 7 HOH   680 1480 1552 HOH   HOH B . 
N 7 HOH   681 1481 1432 HOH   HOH B . 
N 7 HOH   682 1482 1071 HOH   HOH B . 
N 7 HOH   683 1483 1237 HOH   HOH B . 
N 7 HOH   684 1484 448  HOH   HOH B . 
N 7 HOH   685 1485 1248 HOH   HOH B . 
N 7 HOH   686 1486 564  HOH   HOH B . 
N 7 HOH   687 1487 1166 HOH   HOH B . 
N 7 HOH   688 1488 1070 HOH   HOH B . 
N 7 HOH   689 1489 1193 HOH   HOH B . 
N 7 HOH   690 1490 281  HOH   HOH B . 
N 7 HOH   691 1491 306  HOH   HOH B . 
N 7 HOH   692 1492 1452 HOH   HOH B . 
N 7 HOH   693 1493 571  HOH   HOH B . 
N 7 HOH   694 1494 1508 HOH   HOH B . 
N 7 HOH   695 1495 1345 HOH   HOH B . 
N 7 HOH   696 1496 1404 HOH   HOH B . 
N 7 HOH   697 1497 710  HOH   HOH B . 
N 7 HOH   698 1498 1036 HOH   HOH B . 
N 7 HOH   699 1499 1450 HOH   HOH B . 
N 7 HOH   700 1500 1264 HOH   HOH B . 
N 7 HOH   701 1501 1499 HOH   HOH B . 
N 7 HOH   702 1502 1084 HOH   HOH B . 
N 7 HOH   703 1503 290  HOH   HOH B . 
N 7 HOH   704 1504 1092 HOH   HOH B . 
N 7 HOH   705 1505 882  HOH   HOH B . 
N 7 HOH   706 1506 500  HOH   HOH B . 
N 7 HOH   707 1507 1316 HOH   HOH B . 
N 7 HOH   708 1508 958  HOH   HOH B . 
N 7 HOH   709 1509 760  HOH   HOH B . 
N 7 HOH   710 1510 980  HOH   HOH B . 
N 7 HOH   711 1511 726  HOH   HOH B . 
N 7 HOH   712 1512 1115 HOH   HOH B . 
N 7 HOH   713 1513 1520 HOH   HOH B . 
N 7 HOH   714 1514 1091 HOH   HOH B . 
N 7 HOH   715 1515 1340 HOH   HOH B . 
N 7 HOH   716 1516 252  HOH   HOH B . 
N 7 HOH   717 1517 251  HOH   HOH B . 
N 7 HOH   718 1518 1387 HOH   HOH B . 
N 7 HOH   719 1519 1226 HOH   HOH B . 
N 7 HOH   720 1520 1141 HOH   HOH B . 
N 7 HOH   721 1521 301  HOH   HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? CRANK2   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9G7J 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     64.595 
_cell.length_a_esd                 ? 
_cell.length_b                     100.436 
_cell.length_b_esd                 ? 
_cell.length_c                     176.595 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9G7J 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9G7J 
_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             2.16 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.06 
_exptl_crystal.description                  'Irregular polygonal brown crystal.' 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    / 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Crystals were obtained by initial screening at 20 degrees Celsius using the sitting drop method on a 96-Well MRC 2-Drop Crystallization Plates in polystyrene (SWISSCI). The crystallization reservoir contained 90 ul of mother liquor, the crystallization drop contained a mixture of 0.55 ul protein at 8.6 mg.ml-1 and 0.55 ul precipitant. The protein was in 25 mM Tris/HCl buffer pH 7.6, 10 % (v/v) glycerol, and 2 mM dithiothreitol.
The crystal was obtained in a Coy tent under an N2/H2 atmosphere (96:4 %). The crystallization reservoir contained 25% (w/v) PEG 3350, 100 mM BIS-Tris pH 6.5, 200 mM Magnesium chloride hexahydrate. The crystal was soaked in the crystallization solution supplemented with 25 % (v/v) glycerol before freezing in liquid nitrogen.
;
_exptl_crystal_grow.pdbx_pH_range   / 
_exptl_crystal_grow.temp            293.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-04-28 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.21434 
_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                        'SOLEIL BEAMLINE PROXIMA 1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.21434 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'PROXIMA 1' 
_diffrn_source.pdbx_synchrotron_site       SOLEIL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9G7J 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.59 
_reflns.d_resolution_low                               100.44 
_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                                     116033 
_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                           95.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.4 
_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                                0.187 
_reflns.pdbx_Rpim_I_all                                0.072 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.173 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.595 
_reflns_shell.d_res_low                                     1.736 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.6 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5802 
_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                               12.2 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.882 
_reflns_shell.pdbx_Rpim_I_all                               0.746 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.641 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          63.1 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.725 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               19.29 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  
;The last refinement steps were performed by refining with a translation libration screw (TLS) with hydrogens modelled in the riding position. Hydrogens were omitted in the final deposited model.
;
_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                                 9G7J 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.59 
_refine.ls_d_res_low                             50.79 
_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                     115999 
_refine.ls_number_reflns_R_free                  5813 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    75.66 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1624 
_refine.ls_R_factor_R_free                       0.1779 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1616 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          SAD 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 18.25 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.11 
_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.pdbx_number_atoms_protein        9306 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         128 
_refine_hist.number_atoms_solvent             1504 
_refine_hist.number_atoms_total               10938 
_refine_hist.d_res_high                       1.59 
_refine_hist.d_res_low                        50.79 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.011  ? ?    ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.467  ? ?    ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.413 ? 3649 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.096  ? 1455 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.019  ? 1683 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.59 1.61  . . 1   24   0.00   . . . . 0.2295 . . . . . . . . . . . 0.4832 
'X-RAY DIFFRACTION' 1.61 1.63  . . 4   158  3.00   . . . . 0.2774 . . . . . . . . . . . 0.3638 
'X-RAY DIFFRACTION' 1.63 1.65  . . 27  393  8.00   . . . . 0.3033 . . . . . . . . . . . 0.3366 
'X-RAY DIFFRACTION' 1.65 1.67  . . 41  689  15.00  . . . . 0.2912 . . . . . . . . . . . 0.3224 
'X-RAY DIFFRACTION' 1.67 1.69  . . 66  1121 23.00  . . . . 0.2978 . . . . . . . . . . . 0.3571 
'X-RAY DIFFRACTION' 1.69 1.72  . . 98  1550 33.00  . . . . 0.2825 . . . . . . . . . . . 0.2773 
'X-RAY DIFFRACTION' 1.72 1.74  . . 120 2284 47.00  . . . . 0.2749 . . . . . . . . . . . 0.2718 
'X-RAY DIFFRACTION' 1.74 1.77  . . 161 2999 63.00  . . . . 0.2473 . . . . . . . . . . . 0.2697 
'X-RAY DIFFRACTION' 1.77 1.80  . . 175 3321 68.00  . . . . 0.2364 . . . . . . . . . . . 0.2726 
'X-RAY DIFFRACTION' 1.80 1.83  . . 184 3524 73.00  . . . . 0.2222 . . . . . . . . . . . 0.2313 
'X-RAY DIFFRACTION' 1.83 1.86  . . 184 3703 77.00  . . . . 0.2136 . . . . . . . . . . . 0.2476 
'X-RAY DIFFRACTION' 1.86 1.89  . . 214 3844 80.00  . . . . 0.2136 . . . . . . . . . . . 0.2113 
'X-RAY DIFFRACTION' 1.89 1.93  . . 222 4085 84.00  . . . . 0.2037 . . . . . . . . . . . 0.2187 
'X-RAY DIFFRACTION' 1.93 1.97  . . 230 4325 90.00  . . . . 0.1777 . . . . . . . . . . . 0.2019 
'X-RAY DIFFRACTION' 1.97 2.01  . . 223 4702 97.00  . . . . 0.1700 . . . . . . . . . . . 0.2109 
'X-RAY DIFFRACTION' 2.01 2.06  . . 262 4813 100.00 . . . . 0.1719 . . . . . . . . . . . 0.2001 
'X-RAY DIFFRACTION' 2.06 2.11  . . 264 4792 100.00 . . . . 0.1692 . . . . . . . . . . . 0.1852 
'X-RAY DIFFRACTION' 2.11 2.16  . . 261 4859 100.00 . . . . 0.1561 . . . . . . . . . . . 0.1581 
'X-RAY DIFFRACTION' 2.16 2.23  . . 254 4849 100.00 . . . . 0.1531 . . . . . . . . . . . 0.1548 
'X-RAY DIFFRACTION' 2.23 2.30  . . 240 4873 100.00 . . . . 0.1405 . . . . . . . . . . . 0.1589 
'X-RAY DIFFRACTION' 2.30 2.38  . . 255 4838 100.00 . . . . 0.1432 . . . . . . . . . . . 0.1716 
'X-RAY DIFFRACTION' 2.38 2.48  . . 270 4862 100.00 . . . . 0.1509 . . . . . . . . . . . 0.1555 
'X-RAY DIFFRACTION' 2.48 2.59  . . 238 4869 100.00 . . . . 0.1534 . . . . . . . . . . . 0.1629 
'X-RAY DIFFRACTION' 2.59 2.73  . . 260 4873 100.00 . . . . 0.1562 . . . . . . . . . . . 0.1709 
'X-RAY DIFFRACTION' 2.73 2.90  . . 250 4882 100.00 . . . . 0.1535 . . . . . . . . . . . 0.1700 
'X-RAY DIFFRACTION' 2.90 3.12  . . 273 4878 100.00 . . . . 0.1540 . . . . . . . . . . . 0.1685 
'X-RAY DIFFRACTION' 3.12 3.44  . . 241 4943 100.00 . . . . 0.1499 . . . . . . . . . . . 0.1607 
'X-RAY DIFFRACTION' 3.44 3.93  . . 260 4934 100.00 . . . . 0.1328 . . . . . . . . . . . 0.1519 
'X-RAY DIFFRACTION' 3.93 4.95  . . 259 5028 100.00 . . . . 0.1302 . . . . . . . . . . . 0.1462 
'X-RAY DIFFRACTION' 4.95 50.79 . . 276 5171 100.00 . . . . 0.1809 . . . . . . . . . . . 0.1945 
# 
_struct.entry_id                     9G7J 
_struct.title                        
'Crystal structure of the tungsten-dependent aldehyde:ferredoxin oxidoreductase from Clostridium autoethanogenum.' 
_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        9G7J 
_struct_keywords.text            
'Anaerobic metabolism, Metalloenzyme, Tungstopterin, Ethanol production, acetogenic bacteria, iron-sulfur cluster, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 2 ? 
H N N 3 ? 
I N N 6 ? 
J N N 6 ? 
K N N 4 ? 
L N N 4 ? 
M N N 7 ? 
N N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A3M0S906_9CLOT 
_struct_ref.pdbx_db_accession          A0A3M0S906 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MYGYDGKVLRINLKERTCKSENLDLDKAKKFIGCRGLGVKTLFDEIDPKIDALSPENKFIIVTGPLTGAPVPTSGRFMVV
TKAPLTGTIGISNSGGKWGVDLKKAGWDMIIVEDKADSPVYIEIVDDKVEIKDASQLWGKVTSETTKELEKITENKSKVL
CIGPAGERLSLMAAVMNDVDRTAARGGVGAVMGSKNLKAITVKGTGKIALADKEKVKKVSVEKITTLKNDPVAGQGMPTY
GTAILVNIINENGVHPVKNFQESYTNQADKISGETLTANQLVRKNPCYSCPIGCGRWVRLKDGTECGGPEYETLWCFGSD
CGSYDLDAINEANMLCNEYGIDTITCGATIAAAMELYQRGYIKDEEIAGDNLSLKWGDTESMIGWIKRMVYSEGFGAKMT
NGSYRLCEGYGAPEYSMTVKKQEIPAYDPRGIQGHGITYAVNNRGGCHIKGYMINPEILGYPEKLDRFALDGKAAYAKLF
HDLTAVIDSLGLCIFTTFGLGIQDYVDMYNAVVGESTYDADSLLEAGDRIWTLEKLFNLAAGIDSSQDTLPKRLLEEPIP
DGPSKGEVHRLDVLLPEYYSVRGWSKEGIPTEETLKKLGLDEYIGKF
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9G7J A 1 ? 607 ? A0A3M0S906 1 ? 607 ? 1 607 
2 1 9G7J B 1 ? 607 ? A0A3M0S906 1 ? 607 ? 1 607 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,M     
2 1 B,G,H,I,J,K,L,N 
# 
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'             'Monomer population is confirmed' 
2 1 'native gel electrophoresis' 'Monomer population is confirmed' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 24  ? PHE A 31  ? ASP A 24  PHE A 31  1 ? 8  
HELX_P HELX_P2  AA2 GLY A 33  ? ILE A 46  ? GLY A 33  ILE A 46  1 ? 14 
HELX_P HELX_P3  AA3 LYS A 97  ? ALA A 105 ? LYS A 97  ALA A 105 1 ? 9  
HELX_P HELX_P4  AA4 VAL A 141 ? THR A 153 ? VAL A 141 THR A 153 1 ? 13 
HELX_P HELX_P5  AA5 GLY A 163 ? ARG A 168 ? GLY A 163 ARG A 168 1 ? 6  
HELX_P HELX_P6  AA6 ALA A 184 ? GLY A 186 ? ALA A 184 GLY A 186 5 ? 3  
HELX_P HELX_P7  AA7 GLY A 187 ? LYS A 195 ? GLY A 187 LYS A 195 1 ? 9  
HELX_P HELX_P8  AA8 ASP A 212 ? ASP A 230 ? ASP A 212 ASP A 230 1 ? 19 
HELX_P HELX_P9  AA9 ASP A 230 ? GLN A 235 ? ASP A 230 GLN A 235 1 ? 6  
HELX_P HELX_P10 AB1 GLN A 235 ? GLY A 241 ? GLN A 235 GLY A 241 1 ? 7  
HELX_P HELX_P11 AB2 ILE A 244 ? ASN A 252 ? ILE A 244 ASN A 252 1 ? 9  
HELX_P HELX_P12 AB3 GLN A 267 ? ILE A 271 ? GLN A 267 ILE A 271 5 ? 5  
HELX_P HELX_P13 AB4 SER A 272 ? ASN A 279 ? SER A 272 ASN A 279 1 ? 8  
HELX_P HELX_P14 AB5 GLU A 310 ? PHE A 317 ? GLU A 310 PHE A 317 1 ? 8  
HELX_P HELX_P15 AB6 GLY A 318 ? GLY A 322 ? GLY A 318 GLY A 322 5 ? 5  
HELX_P HELX_P16 AB7 ASP A 325 ? GLY A 340 ? ASP A 325 GLY A 340 1 ? 16 
HELX_P HELX_P17 AB8 ASP A 342 ? ARG A 359 ? ASP A 342 ARG A 359 1 ? 18 
HELX_P HELX_P18 AB9 LYS A 363 ? GLY A 369 ? LYS A 363 GLY A 369 1 ? 7  
HELX_P HELX_P19 AC1 ASP A 378 ? TYR A 391 ? ASP A 378 TYR A 391 1 ? 14 
HELX_P HELX_P20 AC2 PHE A 395 ? THR A 400 ? PHE A 395 THR A 400 1 ? 6  
HELX_P HELX_P21 AC3 GLY A 402 ? TYR A 410 ? GLY A 402 TYR A 410 1 ? 9  
HELX_P HELX_P22 AC4 ALA A 412 ? SER A 416 ? ALA A 412 SER A 416 5 ? 5  
HELX_P HELX_P23 AC5 ASP A 428 ? GLY A 431 ? ASP A 428 GLY A 431 5 ? 4  
HELX_P HELX_P24 AC6 ILE A 432 ? ASN A 442 ? ILE A 432 ASN A 442 1 ? 11 
HELX_P HELX_P25 AC7 MET A 453 ? ILE A 458 ? MET A 453 ILE A 458 1 ? 6  
HELX_P HELX_P26 AC8 GLY A 472 ? GLY A 491 ? GLY A 472 GLY A 491 1 ? 20 
HELX_P HELX_P27 AC9 CYS A 493 ? PHE A 498 ? CYS A 493 PHE A 498 5 ? 6  
HELX_P HELX_P28 AD1 GLY A 501 ? GLY A 514 ? GLY A 501 GLY A 514 1 ? 14 
HELX_P HELX_P29 AD2 ASP A 519 ? ALA A 541 ? ASP A 519 ALA A 541 1 ? 23 
HELX_P HELX_P30 AD3 ASP A 544 ? ASP A 548 ? ASP A 544 ASP A 548 5 ? 5  
HELX_P HELX_P31 AD4 PRO A 551 ? GLU A 557 ? PRO A 551 GLU A 557 1 ? 7  
HELX_P HELX_P32 AD5 ARG A 570 ? GLY A 583 ? ARG A 570 GLY A 583 1 ? 14 
HELX_P HELX_P33 AD6 THR A 591 ? LEU A 598 ? THR A 591 LEU A 598 1 ? 8  
HELX_P HELX_P34 AD7 LEU A 600 ? ILE A 604 ? LEU A 600 ILE A 604 5 ? 5  
HELX_P HELX_P35 AD8 ASP B 24  ? PHE B 31  ? ASP B 24  PHE B 31  1 ? 8  
HELX_P HELX_P36 AD9 GLY B 33  ? ILE B 46  ? GLY B 33  ILE B 46  1 ? 14 
HELX_P HELX_P37 AE1 LYS B 97  ? ALA B 105 ? LYS B 97  ALA B 105 1 ? 9  
HELX_P HELX_P38 AE2 VAL B 141 ? ILE B 152 ? VAL B 141 ILE B 152 1 ? 12 
HELX_P HELX_P39 AE3 GLY B 163 ? ARG B 168 ? GLY B 163 ARG B 168 1 ? 6  
HELX_P HELX_P40 AE4 ALA B 184 ? GLY B 186 ? ALA B 184 GLY B 186 5 ? 3  
HELX_P HELX_P41 AE5 GLY B 187 ? LYS B 195 ? GLY B 187 LYS B 195 1 ? 9  
HELX_P HELX_P42 AE6 ASP B 212 ? ASP B 230 ? ASP B 212 ASP B 230 1 ? 19 
HELX_P HELX_P43 AE7 ASP B 230 ? GLN B 235 ? ASP B 230 GLN B 235 1 ? 6  
HELX_P HELX_P44 AE8 GLN B 235 ? GLY B 241 ? GLN B 235 GLY B 241 1 ? 7  
HELX_P HELX_P45 AE9 ILE B 244 ? ASN B 252 ? ILE B 244 ASN B 252 1 ? 9  
HELX_P HELX_P46 AF1 GLN B 267 ? ILE B 271 ? GLN B 267 ILE B 271 5 ? 5  
HELX_P HELX_P47 AF2 SER B 272 ? ASN B 279 ? SER B 272 ASN B 279 1 ? 8  
HELX_P HELX_P48 AF3 GLU B 310 ? PHE B 317 ? GLU B 310 PHE B 317 1 ? 8  
HELX_P HELX_P49 AF4 GLY B 318 ? GLY B 322 ? GLY B 318 GLY B 322 5 ? 5  
HELX_P HELX_P50 AF5 ASP B 325 ? GLY B 340 ? ASP B 325 GLY B 340 1 ? 16 
HELX_P HELX_P51 AF6 ASP B 342 ? ARG B 359 ? ASP B 342 ARG B 359 1 ? 18 
HELX_P HELX_P52 AF7 LYS B 363 ? ALA B 368 ? LYS B 363 ALA B 368 1 ? 6  
HELX_P HELX_P53 AF8 GLY B 369 ? ASN B 371 ? GLY B 369 ASN B 371 5 ? 3  
HELX_P HELX_P54 AF9 ASP B 378 ? TYR B 391 ? ASP B 378 TYR B 391 1 ? 14 
HELX_P HELX_P55 AG1 PHE B 395 ? THR B 400 ? PHE B 395 THR B 400 1 ? 6  
HELX_P HELX_P56 AG2 GLY B 402 ? TYR B 410 ? GLY B 402 TYR B 410 1 ? 9  
HELX_P HELX_P57 AG3 GLY B 411 ? SER B 416 ? GLY B 411 SER B 416 5 ? 6  
HELX_P HELX_P58 AG4 ASP B 428 ? GLY B 431 ? ASP B 428 GLY B 431 5 ? 4  
HELX_P HELX_P59 AG5 ILE B 432 ? ASN B 442 ? ILE B 432 ASN B 442 1 ? 11 
HELX_P HELX_P60 AG6 MET B 453 ? ILE B 458 ? MET B 453 ILE B 458 1 ? 6  
HELX_P HELX_P61 AG7 GLY B 472 ? GLY B 491 ? GLY B 472 GLY B 491 1 ? 20 
HELX_P HELX_P62 AG8 CYS B 493 ? PHE B 498 ? CYS B 493 PHE B 498 5 ? 6  
HELX_P HELX_P63 AG9 GLY B 501 ? GLY B 514 ? GLY B 501 GLY B 514 1 ? 14 
HELX_P HELX_P64 AH1 ASP B 519 ? ALA B 541 ? ASP B 519 ALA B 541 1 ? 23 
HELX_P HELX_P65 AH2 ASP B 544 ? ASP B 548 ? ASP B 544 ASP B 548 5 ? 5  
HELX_P HELX_P66 AH3 PRO B 551 ? GLU B 557 ? PRO B 551 GLU B 557 1 ? 7  
HELX_P HELX_P67 AH4 ARG B 570 ? ARG B 582 ? ARG B 570 ARG B 582 1 ? 13 
HELX_P HELX_P68 AH5 THR B 591 ? GLY B 599 ? THR B 591 GLY B 599 1 ? 9  
HELX_P HELX_P69 AH6 LEU B 600 ? ILE B 604 ? LEU B 600 ILE B 604 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 
metalc1  metalc ? ? A ASN   93  O  ? ? ? 1_555 D A1IJH . MG  ? ? A ASN   93  A A1IJH 702  1_555 ? ? ? ? ? ? ? 2.111 ? ? 
metalc2  metalc ? ? A THR   182 O  ? ? ? 1_555 D A1IJH . MG  ? ? A THR   182 A A1IJH 702  1_555 ? ? ? ? ? ? ? 2.188 ? ? 
metalc3  metalc ? ? A CYS   287 SG ? ? ? 1_555 C SF4   . FE4 ? ? A CYS   287 A SF4   701  1_555 ? ? ? ? ? ? ? 2.404 ? ? 
metalc4  metalc ? ? A CYS   290 SG ? ? ? 1_555 C SF4   . FE3 ? ? A CYS   290 A SF4   701  1_555 ? ? ? ? ? ? ? 2.228 ? ? 
metalc5  metalc ? ? A CYS   294 SG ? ? ? 1_555 C SF4   . FE2 ? ? A CYS   294 A SF4   701  1_555 ? ? ? ? ? ? ? 2.349 ? ? 
metalc6  metalc ? ? A CYS   493 SG ? ? ? 1_555 C SF4   . FE1 ? ? A CYS   493 A SF4   701  1_555 ? ? ? ? ? ? ? 2.384 ? ? 
metalc7  metalc ? ? D A1IJH .   W  ? ? ? 1_555 M HOH   . O   ? ? A A1IJH 702 A HOH   824  1_555 ? ? ? ? ? ? ? 2.231 ? ? 
metalc8  metalc ? ? D A1IJH .   MG ? ? ? 1_555 M HOH   . O   ? ? A A1IJH 702 A HOH   1091 1_555 ? ? ? ? ? ? ? 2.257 ? ? 
metalc9  metalc ? ? D A1IJH .   MG ? ? ? 1_555 M HOH   . O   ? ? A A1IJH 702 A HOH   1097 1_555 ? ? ? ? ? ? ? 2.341 ? ? 
metalc10 metalc ? ? D A1IJH .   W  ? ? ? 1_555 M HOH   . O   ? ? A A1IJH 702 A HOH   1330 1_555 ? ? ? ? ? ? ? 2.183 ? ? 
metalc11 metalc ? ? F MG    .   MG ? ? ? 1_555 M HOH   . O   ? ? A MG    704 A HOH   1293 1_555 ? ? ? ? ? ? ? 2.201 ? ? 
metalc12 metalc ? ? F MG    .   MG ? ? ? 1_555 M HOH   . O   ? ? A MG    704 A HOH   1580 1_555 ? ? ? ? ? ? ? 2.147 ? ? 
metalc13 metalc ? ? F MG    .   MG ? ? ? 1_555 N HOH   . O   B ? A MG    704 B HOH   1010 1_555 ? ? ? ? ? ? ? 2.310 ? ? 
metalc14 metalc ? ? F MG    .   MG ? ? ? 1_555 N HOH   . O   ? ? A MG    704 B HOH   1415 1_555 ? ? ? ? ? ? ? 2.080 ? ? 
metalc15 metalc ? ? F MG    .   MG ? ? ? 1_555 N HOH   . O   B ? A MG    704 B HOH   1506 1_555 ? ? ? ? ? ? ? 2.244 ? ? 
metalc16 metalc ? ? B ASN   93  O  ? ? ? 1_555 H A1IJH . MG  ? ? B ASN   93  B A1IJH 702  1_555 ? ? ? ? ? ? ? 2.117 ? ? 
metalc17 metalc ? ? B THR   182 O  ? ? ? 1_555 H A1IJH . MG  ? ? B THR   182 B A1IJH 702  1_555 ? ? ? ? ? ? ? 2.165 ? ? 
metalc18 metalc ? ? B CYS   287 SG ? ? ? 1_555 G SF4   . FE4 ? ? B CYS   287 B SF4   701  1_555 ? ? ? ? ? ? ? 2.377 ? ? 
metalc19 metalc ? ? B CYS   290 SG ? ? ? 1_555 G SF4   . FE3 ? ? B CYS   290 B SF4   701  1_555 ? ? ? ? ? ? ? 2.210 ? ? 
metalc20 metalc ? ? B CYS   294 SG ? ? ? 1_555 G SF4   . FE2 ? ? B CYS   294 B SF4   701  1_555 ? ? ? ? ? ? ? 2.343 ? ? 
metalc21 metalc ? ? B CYS   493 SG ? ? ? 1_555 G SF4   . FE1 ? ? B CYS   493 B SF4   701  1_555 ? ? ? ? ? ? ? 2.363 ? ? 
metalc22 metalc ? ? H A1IJH .   W  ? ? ? 1_555 N HOH   . O   ? ? B A1IJH 702 B HOH   811  1_555 ? ? ? ? ? ? ? 2.279 ? ? 
metalc23 metalc ? ? H A1IJH .   MG ? ? ? 1_555 N HOH   . O   ? ? B A1IJH 702 B HOH   1115 1_555 ? ? ? ? ? ? ? 2.259 ? ? 
metalc24 metalc ? ? H A1IJH .   MG ? ? ? 1_555 N HOH   . O   ? ? B A1IJH 702 B HOH   1142 1_555 ? ? ? ? ? ? ? 2.330 ? ? 
metalc25 metalc ? ? H A1IJH .   W  ? ? ? 1_555 N HOH   . O   ? ? B A1IJH 702 B HOH   1301 1_555 ? ? ? ? ? ? ? 2.175 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1   O   ? A ASN   93  ? A ASN   93   ? 1_555 MG  ? D A1IJH . ? A A1IJH 702 ? 1_555 O1P ? D A1IJH .   ? A A1IJH 702  ? 1_555 89.4  
? 
2   O   ? A ASN   93  ? A ASN   93   ? 1_555 MG  ? D A1IJH . ? A A1IJH 702 ? 1_555 O5P ? D A1IJH .   ? A A1IJH 702  ? 1_555 90.1  
? 
3   O1P ? D A1IJH .   ? A A1IJH 702  ? 1_555 MG  ? D A1IJH . ? A A1IJH 702 ? 1_555 O5P ? D A1IJH .   ? A A1IJH 702  ? 1_555 176.2 
? 
4   O   ? A ASN   93  ? A ASN   93   ? 1_555 MG  ? D A1IJH . ? A A1IJH 702 ? 1_555 O   ? A THR   182 ? A THR   182  ? 1_555 89.7  
? 
5   O1P ? D A1IJH .   ? A A1IJH 702  ? 1_555 MG  ? D A1IJH . ? A A1IJH 702 ? 1_555 O   ? A THR   182 ? A THR   182  ? 1_555 89.2  
? 
6   O5P ? D A1IJH .   ? A A1IJH 702  ? 1_555 MG  ? D A1IJH . ? A A1IJH 702 ? 1_555 O   ? A THR   182 ? A THR   182  ? 1_555 94.5  
? 
7   O   ? A ASN   93  ? A ASN   93   ? 1_555 MG  ? D A1IJH . ? A A1IJH 702 ? 1_555 O   ? M HOH   .   ? A HOH   1091 ? 1_555 79.4  
? 
8   O1P ? D A1IJH .   ? A A1IJH 702  ? 1_555 MG  ? D A1IJH . ? A A1IJH 702 ? 1_555 O   ? M HOH   .   ? A HOH   1091 ? 1_555 96.3  
? 
9   O5P ? D A1IJH .   ? A A1IJH 702  ? 1_555 MG  ? D A1IJH . ? A A1IJH 702 ? 1_555 O   ? M HOH   .   ? A HOH   1091 ? 1_555 79.9  
? 
10  O   ? A THR   182 ? A THR   182  ? 1_555 MG  ? D A1IJH . ? A A1IJH 702 ? 1_555 O   ? M HOH   .   ? A HOH   1091 ? 1_555 167.7 
? 
11  O   ? A ASN   93  ? A ASN   93   ? 1_555 MG  ? D A1IJH . ? A A1IJH 702 ? 1_555 O   ? M HOH   .   ? A HOH   1097 ? 1_555 176.8 
? 
12  O1P ? D A1IJH .   ? A A1IJH 702  ? 1_555 MG  ? D A1IJH . ? A A1IJH 702 ? 1_555 O   ? M HOH   .   ? A HOH   1097 ? 1_555 87.4  
? 
13  O5P ? D A1IJH .   ? A A1IJH 702  ? 1_555 MG  ? D A1IJH . ? A A1IJH 702 ? 1_555 O   ? M HOH   .   ? A HOH   1097 ? 1_555 93.1  
? 
14  O   ? A THR   182 ? A THR   182  ? 1_555 MG  ? D A1IJH . ? A A1IJH 702 ? 1_555 O   ? M HOH   .   ? A HOH   1097 ? 1_555 90.1  
? 
15  O   ? M HOH   .   ? A HOH   1091 ? 1_555 MG  ? D A1IJH . ? A A1IJH 702 ? 1_555 O   ? M HOH   .   ? A HOH   1097 ? 1_555 101.1 
? 
16  SG  ? A CYS   287 ? A CYS   287  ? 1_555 FE4 ? C SF4   . ? A SF4   701 ? 1_555 S1  ? C SF4   .   ? A SF4   701  ? 1_555 104.9 
? 
17  SG  ? A CYS   287 ? A CYS   287  ? 1_555 FE4 ? C SF4   . ? A SF4   701 ? 1_555 S2  ? C SF4   .   ? A SF4   701  ? 1_555 103.6 
? 
18  S1  ? C SF4   .   ? A SF4   701  ? 1_555 FE4 ? C SF4   . ? A SF4   701 ? 1_555 S2  ? C SF4   .   ? A SF4   701  ? 1_555 108.9 
? 
19  SG  ? A CYS   287 ? A CYS   287  ? 1_555 FE4 ? C SF4   . ? A SF4   701 ? 1_555 S3  ? C SF4   .   ? A SF4   701  ? 1_555 126.0 
? 
20  S1  ? C SF4   .   ? A SF4   701  ? 1_555 FE4 ? C SF4   . ? A SF4   701 ? 1_555 S3  ? C SF4   .   ? A SF4   701  ? 1_555 107.7 
? 
21  S2  ? C SF4   .   ? A SF4   701  ? 1_555 FE4 ? C SF4   . ? A SF4   701 ? 1_555 S3  ? C SF4   .   ? A SF4   701  ? 1_555 105.0 
? 
22  SG  ? A CYS   290 ? A CYS   290  ? 1_555 FE3 ? C SF4   . ? A SF4   701 ? 1_555 S1  ? C SF4   .   ? A SF4   701  ? 1_555 113.9 
? 
23  SG  ? A CYS   290 ? A CYS   290  ? 1_555 FE3 ? C SF4   . ? A SF4   701 ? 1_555 S2  ? C SF4   .   ? A SF4   701  ? 1_555 110.7 
? 
24  S1  ? C SF4   .   ? A SF4   701  ? 1_555 FE3 ? C SF4   . ? A SF4   701 ? 1_555 S2  ? C SF4   .   ? A SF4   701  ? 1_555 108.4 
? 
25  SG  ? A CYS   290 ? A CYS   290  ? 1_555 FE3 ? C SF4   . ? A SF4   701 ? 1_555 S4  ? C SF4   .   ? A SF4   701  ? 1_555 111.4 
? 
26  S1  ? C SF4   .   ? A SF4   701  ? 1_555 FE3 ? C SF4   . ? A SF4   701 ? 1_555 S4  ? C SF4   .   ? A SF4   701  ? 1_555 105.4 
? 
27  S2  ? C SF4   .   ? A SF4   701  ? 1_555 FE3 ? C SF4   . ? A SF4   701 ? 1_555 S4  ? C SF4   .   ? A SF4   701  ? 1_555 106.7 
? 
28  SG  ? A CYS   294 ? A CYS   294  ? 1_555 FE2 ? C SF4   . ? A SF4   701 ? 1_555 S1  ? C SF4   .   ? A SF4   701  ? 1_555 121.4 
? 
29  SG  ? A CYS   294 ? A CYS   294  ? 1_555 FE2 ? C SF4   . ? A SF4   701 ? 1_555 S3  ? C SF4   .   ? A SF4   701  ? 1_555 102.8 
? 
30  S1  ? C SF4   .   ? A SF4   701  ? 1_555 FE2 ? C SF4   . ? A SF4   701 ? 1_555 S3  ? C SF4   .   ? A SF4   701  ? 1_555 107.9 
? 
31  SG  ? A CYS   294 ? A CYS   294  ? 1_555 FE2 ? C SF4   . ? A SF4   701 ? 1_555 S4  ? C SF4   .   ? A SF4   701  ? 1_555 111.2 
? 
32  S1  ? C SF4   .   ? A SF4   701  ? 1_555 FE2 ? C SF4   . ? A SF4   701 ? 1_555 S4  ? C SF4   .   ? A SF4   701  ? 1_555 105.5 
? 
33  S3  ? C SF4   .   ? A SF4   701  ? 1_555 FE2 ? C SF4   . ? A SF4   701 ? 1_555 S4  ? C SF4   .   ? A SF4   701  ? 1_555 107.4 
? 
34  SG  ? A CYS   493 ? A CYS   493  ? 1_555 FE1 ? C SF4   . ? A SF4   701 ? 1_555 S2  ? C SF4   .   ? A SF4   701  ? 1_555 109.7 
? 
35  SG  ? A CYS   493 ? A CYS   493  ? 1_555 FE1 ? C SF4   . ? A SF4   701 ? 1_555 S3  ? C SF4   .   ? A SF4   701  ? 1_555 114.8 
? 
36  S2  ? C SF4   .   ? A SF4   701  ? 1_555 FE1 ? C SF4   . ? A SF4   701 ? 1_555 S3  ? C SF4   .   ? A SF4   701  ? 1_555 105.0 
? 
37  SG  ? A CYS   493 ? A CYS   493  ? 1_555 FE1 ? C SF4   . ? A SF4   701 ? 1_555 S4  ? C SF4   .   ? A SF4   701  ? 1_555 112.4 
? 
38  S2  ? C SF4   .   ? A SF4   701  ? 1_555 FE1 ? C SF4   . ? A SF4   701 ? 1_555 S4  ? C SF4   .   ? A SF4   701  ? 1_555 107.4 
? 
39  S3  ? C SF4   .   ? A SF4   701  ? 1_555 FE1 ? C SF4   . ? A SF4   701 ? 1_555 S4  ? C SF4   .   ? A SF4   701  ? 1_555 107.0 
? 
40  O   ? M HOH   .   ? A HOH   824  ? 1_555 W   ? D A1IJH . ? A A1IJH 702 ? 1_555 S3  ? D A1IJH .   ? A A1IJH 702  ? 1_555 92.0  
? 
41  O   ? M HOH   .   ? A HOH   824  ? 1_555 W   ? D A1IJH . ? A A1IJH 702 ? 1_555 S4  ? D A1IJH .   ? A A1IJH 702  ? 1_555 124.5 
? 
42  S3  ? D A1IJH .   ? A A1IJH 702  ? 1_555 W   ? D A1IJH . ? A A1IJH 702 ? 1_555 S4  ? D A1IJH .   ? A A1IJH 702  ? 1_555 74.2  
? 
43  O   ? M HOH   .   ? A HOH   824  ? 1_555 W   ? D A1IJH . ? A A1IJH 702 ? 1_555 S24 ? D A1IJH .   ? A A1IJH 702  ? 1_555 75.4  
? 
44  S3  ? D A1IJH .   ? A A1IJH 702  ? 1_555 W   ? D A1IJH . ? A A1IJH 702 ? 1_555 S24 ? D A1IJH .   ? A A1IJH 702  ? 1_555 75.9  
? 
45  S4  ? D A1IJH .   ? A A1IJH 702  ? 1_555 W   ? D A1IJH . ? A A1IJH 702 ? 1_555 S24 ? D A1IJH .   ? A A1IJH 702  ? 1_555 144.3 
? 
46  O   ? M HOH   .   ? A HOH   824  ? 1_555 W   ? D A1IJH . ? A A1IJH 702 ? 1_555 S23 ? D A1IJH .   ? A A1IJH 702  ? 1_555 145.3 
? 
47  S3  ? D A1IJH .   ? A A1IJH 702  ? 1_555 W   ? D A1IJH . ? A A1IJH 702 ? 1_555 S23 ? D A1IJH .   ? A A1IJH 702  ? 1_555 96.8  
? 
48  S4  ? D A1IJH .   ? A A1IJH 702  ? 1_555 W   ? D A1IJH . ? A A1IJH 702 ? 1_555 S23 ? D A1IJH .   ? A A1IJH 702  ? 1_555 90.2  
? 
49  S24 ? D A1IJH .   ? A A1IJH 702  ? 1_555 W   ? D A1IJH . ? A A1IJH 702 ? 1_555 S23 ? D A1IJH .   ? A A1IJH 702  ? 1_555 74.4  
? 
50  O   ? M HOH   .   ? A HOH   824  ? 1_555 W   ? D A1IJH . ? A A1IJH 702 ? 1_555 O   ? M HOH   .   ? A HOH   1330 ? 1_555 85.8  
? 
51  S3  ? D A1IJH .   ? A A1IJH 702  ? 1_555 W   ? D A1IJH . ? A A1IJH 702 ? 1_555 O   ? M HOH   .   ? A HOH   1330 ? 1_555 159.9 
? 
52  S4  ? D A1IJH .   ? A A1IJH 702  ? 1_555 W   ? D A1IJH . ? A A1IJH 702 ? 1_555 O   ? M HOH   .   ? A HOH   1330 ? 1_555 90.6  
? 
53  S24 ? D A1IJH .   ? A A1IJH 702  ? 1_555 W   ? D A1IJH . ? A A1IJH 702 ? 1_555 O   ? M HOH   .   ? A HOH   1330 ? 1_555 122.5 
? 
54  S23 ? D A1IJH .   ? A A1IJH 702  ? 1_555 W   ? D A1IJH . ? A A1IJH 702 ? 1_555 O   ? M HOH   .   ? A HOH   1330 ? 1_555 96.2  
? 
55  O   ? M HOH   .   ? A HOH   1293 ? 1_555 MG  ? F MG    . ? A MG    704 ? 1_555 O   ? M HOH   .   ? A HOH   1580 ? 1_555 93.1  
? 
56  O   ? M HOH   .   ? A HOH   1293 ? 1_555 MG  ? F MG    . ? A MG    704 ? 1_555 O   B N HOH   .   ? B HOH   1010 ? 1_555 78.9  
? 
57  O   ? M HOH   .   ? A HOH   1580 ? 1_555 MG  ? F MG    . ? A MG    704 ? 1_555 O   B N HOH   .   ? B HOH   1010 ? 1_555 167.5 
? 
58  O   ? M HOH   .   ? A HOH   1293 ? 1_555 MG  ? F MG    . ? A MG    704 ? 1_555 O   ? N HOH   .   ? B HOH   1415 ? 1_555 95.9  
? 
59  O   ? M HOH   .   ? A HOH   1580 ? 1_555 MG  ? F MG    . ? A MG    704 ? 1_555 O   ? N HOH   .   ? B HOH   1415 ? 1_555 89.7  
? 
60  O   B N HOH   .   ? B HOH   1010 ? 1_555 MG  ? F MG    . ? A MG    704 ? 1_555 O   ? N HOH   .   ? B HOH   1415 ? 1_555 81.7  
? 
61  O   ? M HOH   .   ? A HOH   1293 ? 1_555 MG  ? F MG    . ? A MG    704 ? 1_555 O   B N HOH   .   ? B HOH   1506 ? 1_555 167.4 
? 
62  O   ? M HOH   .   ? A HOH   1580 ? 1_555 MG  ? F MG    . ? A MG    704 ? 1_555 O   B N HOH   .   ? B HOH   1506 ? 1_555 97.4  
? 
63  O   B N HOH   .   ? B HOH   1010 ? 1_555 MG  ? F MG    . ? A MG    704 ? 1_555 O   B N HOH   .   ? B HOH   1506 ? 1_555 91.7  
? 
64  O   ? N HOH   .   ? B HOH   1415 ? 1_555 MG  ? F MG    . ? A MG    704 ? 1_555 O   B N HOH   .   ? B HOH   1506 ? 1_555 91.0  
? 
65  O   ? B ASN   93  ? B ASN   93   ? 1_555 MG  ? H A1IJH . ? B A1IJH 702 ? 1_555 O1P ? H A1IJH .   ? B A1IJH 702  ? 1_555 87.8  
? 
66  O   ? B ASN   93  ? B ASN   93   ? 1_555 MG  ? H A1IJH . ? B A1IJH 702 ? 1_555 O5P ? H A1IJH .   ? B A1IJH 702  ? 1_555 94.1  
? 
67  O1P ? H A1IJH .   ? B A1IJH 702  ? 1_555 MG  ? H A1IJH . ? B A1IJH 702 ? 1_555 O5P ? H A1IJH .   ? B A1IJH 702  ? 1_555 175.9 
? 
68  O   ? B ASN   93  ? B ASN   93   ? 1_555 MG  ? H A1IJH . ? B A1IJH 702 ? 1_555 O   ? B THR   182 ? B THR   182  ? 1_555 91.4  
? 
69  O1P ? H A1IJH .   ? B A1IJH 702  ? 1_555 MG  ? H A1IJH . ? B A1IJH 702 ? 1_555 O   ? B THR   182 ? B THR   182  ? 1_555 88.2  
? 
70  O5P ? H A1IJH .   ? B A1IJH 702  ? 1_555 MG  ? H A1IJH . ? B A1IJH 702 ? 1_555 O   ? B THR   182 ? B THR   182  ? 1_555 95.4  
? 
71  O   ? B ASN   93  ? B ASN   93   ? 1_555 MG  ? H A1IJH . ? B A1IJH 702 ? 1_555 O   ? N HOH   .   ? B HOH   1115 ? 1_555 80.6  
? 
72  O1P ? H A1IJH .   ? B A1IJH 702  ? 1_555 MG  ? H A1IJH . ? B A1IJH 702 ? 1_555 O   ? N HOH   .   ? B HOH   1115 ? 1_555 92.0  
? 
73  O5P ? H A1IJH .   ? B A1IJH 702  ? 1_555 MG  ? H A1IJH . ? B A1IJH 702 ? 1_555 O   ? N HOH   .   ? B HOH   1115 ? 1_555 84.7  
? 
74  O   ? B THR   182 ? B THR   182  ? 1_555 MG  ? H A1IJH . ? B A1IJH 702 ? 1_555 O   ? N HOH   .   ? B HOH   1115 ? 1_555 171.9 
? 
75  O   ? B ASN   93  ? B ASN   93   ? 1_555 MG  ? H A1IJH . ? B A1IJH 702 ? 1_555 O   ? N HOH   .   ? B HOH   1142 ? 1_555 170.0 
? 
76  O1P ? H A1IJH .   ? B A1IJH 702  ? 1_555 MG  ? H A1IJH . ? B A1IJH 702 ? 1_555 O   ? N HOH   .   ? B HOH   1142 ? 1_555 82.6  
? 
77  O5P ? H A1IJH .   ? B A1IJH 702  ? 1_555 MG  ? H A1IJH . ? B A1IJH 702 ? 1_555 O   ? N HOH   .   ? B HOH   1142 ? 1_555 95.3  
? 
78  O   ? B THR   182 ? B THR   182  ? 1_555 MG  ? H A1IJH . ? B A1IJH 702 ? 1_555 O   ? N HOH   .   ? B HOH   1142 ? 1_555 91.1  
? 
79  O   ? N HOH   .   ? B HOH   1115 ? 1_555 MG  ? H A1IJH . ? B A1IJH 702 ? 1_555 O   ? N HOH   .   ? B HOH   1142 ? 1_555 96.9  
? 
80  SG  ? B CYS   287 ? B CYS   287  ? 1_555 FE4 ? G SF4   . ? B SF4   701 ? 1_555 S1  ? G SF4   .   ? B SF4   701  ? 1_555 105.9 
? 
81  SG  ? B CYS   287 ? B CYS   287  ? 1_555 FE4 ? G SF4   . ? B SF4   701 ? 1_555 S2  ? G SF4   .   ? B SF4   701  ? 1_555 104.6 
? 
82  S1  ? G SF4   .   ? B SF4   701  ? 1_555 FE4 ? G SF4   . ? B SF4   701 ? 1_555 S2  ? G SF4   .   ? B SF4   701  ? 1_555 107.6 
? 
83  SG  ? B CYS   287 ? B CYS   287  ? 1_555 FE4 ? G SF4   . ? B SF4   701 ? 1_555 S3  ? G SF4   .   ? B SF4   701  ? 1_555 125.4 
? 
84  S1  ? G SF4   .   ? B SF4   701  ? 1_555 FE4 ? G SF4   . ? B SF4   701 ? 1_555 S3  ? G SF4   .   ? B SF4   701  ? 1_555 106.7 
? 
85  S2  ? G SF4   .   ? B SF4   701  ? 1_555 FE4 ? G SF4   . ? B SF4   701 ? 1_555 S3  ? G SF4   .   ? B SF4   701  ? 1_555 105.6 
? 
86  SG  ? B CYS   290 ? B CYS   290  ? 1_555 FE3 ? G SF4   . ? B SF4   701 ? 1_555 S1  ? G SF4   .   ? B SF4   701  ? 1_555 113.4 
? 
87  SG  ? B CYS   290 ? B CYS   290  ? 1_555 FE3 ? G SF4   . ? B SF4   701 ? 1_555 S2  ? G SF4   .   ? B SF4   701  ? 1_555 109.1 
? 
88  S1  ? G SF4   .   ? B SF4   701  ? 1_555 FE3 ? G SF4   . ? B SF4   701 ? 1_555 S2  ? G SF4   .   ? B SF4   701  ? 1_555 107.8 
? 
89  SG  ? B CYS   290 ? B CYS   290  ? 1_555 FE3 ? G SF4   . ? B SF4   701 ? 1_555 S4  ? G SF4   .   ? B SF4   701  ? 1_555 112.0 
? 
90  S1  ? G SF4   .   ? B SF4   701  ? 1_555 FE3 ? G SF4   . ? B SF4   701 ? 1_555 S4  ? G SF4   .   ? B SF4   701  ? 1_555 106.8 
? 
91  S2  ? G SF4   .   ? B SF4   701  ? 1_555 FE3 ? G SF4   . ? B SF4   701 ? 1_555 S4  ? G SF4   .   ? B SF4   701  ? 1_555 107.5 
? 
92  SG  ? B CYS   294 ? B CYS   294  ? 1_555 FE2 ? G SF4   . ? B SF4   701 ? 1_555 S1  ? G SF4   .   ? B SF4   701  ? 1_555 122.3 
? 
93  SG  ? B CYS   294 ? B CYS   294  ? 1_555 FE2 ? G SF4   . ? B SF4   701 ? 1_555 S3  ? G SF4   .   ? B SF4   701  ? 1_555 101.9 
? 
94  S1  ? G SF4   .   ? B SF4   701  ? 1_555 FE2 ? G SF4   . ? B SF4   701 ? 1_555 S3  ? G SF4   .   ? B SF4   701  ? 1_555 106.8 
? 
95  SG  ? B CYS   294 ? B CYS   294  ? 1_555 FE2 ? G SF4   . ? B SF4   701 ? 1_555 S4  ? G SF4   .   ? B SF4   701  ? 1_555 111.4 
? 
96  S1  ? G SF4   .   ? B SF4   701  ? 1_555 FE2 ? G SF4   . ? B SF4   701 ? 1_555 S4  ? G SF4   .   ? B SF4   701  ? 1_555 106.9 
? 
97  S3  ? G SF4   .   ? B SF4   701  ? 1_555 FE2 ? G SF4   . ? B SF4   701 ? 1_555 S4  ? G SF4   .   ? B SF4   701  ? 1_555 106.4 
? 
98  SG  ? B CYS   493 ? B CYS   493  ? 1_555 FE1 ? G SF4   . ? B SF4   701 ? 1_555 S2  ? G SF4   .   ? B SF4   701  ? 1_555 113.3 
? 
99  SG  ? B CYS   493 ? B CYS   493  ? 1_555 FE1 ? G SF4   . ? B SF4   701 ? 1_555 S3  ? G SF4   .   ? B SF4   701  ? 1_555 113.6 
? 
100 S2  ? G SF4   .   ? B SF4   701  ? 1_555 FE1 ? G SF4   . ? B SF4   701 ? 1_555 S3  ? G SF4   .   ? B SF4   701  ? 1_555 105.8 
? 
101 SG  ? B CYS   493 ? B CYS   493  ? 1_555 FE1 ? G SF4   . ? B SF4   701 ? 1_555 S4  ? G SF4   .   ? B SF4   701  ? 1_555 110.9 
? 
102 S2  ? G SF4   .   ? B SF4   701  ? 1_555 FE1 ? G SF4   . ? B SF4   701 ? 1_555 S4  ? G SF4   .   ? B SF4   701  ? 1_555 106.6 
? 
103 S3  ? G SF4   .   ? B SF4   701  ? 1_555 FE1 ? G SF4   . ? B SF4   701 ? 1_555 S4  ? G SF4   .   ? B SF4   701  ? 1_555 106.1 
? 
104 O   ? N HOH   .   ? B HOH   811  ? 1_555 W   ? H A1IJH . ? B A1IJH 702 ? 1_555 S3  ? H A1IJH .   ? B A1IJH 702  ? 1_555 89.2  
? 
105 O   ? N HOH   .   ? B HOH   811  ? 1_555 W   ? H A1IJH . ? B A1IJH 702 ? 1_555 S4  ? H A1IJH .   ? B A1IJH 702  ? 1_555 120.9 
? 
106 S3  ? H A1IJH .   ? B A1IJH 702  ? 1_555 W   ? H A1IJH . ? B A1IJH 702 ? 1_555 S4  ? H A1IJH .   ? B A1IJH 702  ? 1_555 73.2  
? 
107 O   ? N HOH   .   ? B HOH   811  ? 1_555 W   ? H A1IJH . ? B A1IJH 702 ? 1_555 S24 ? H A1IJH .   ? B A1IJH 702  ? 1_555 72.9  
? 
108 S3  ? H A1IJH .   ? B A1IJH 702  ? 1_555 W   ? H A1IJH . ? B A1IJH 702 ? 1_555 S24 ? H A1IJH .   ? B A1IJH 702  ? 1_555 75.2  
? 
109 S4  ? H A1IJH .   ? B A1IJH 702  ? 1_555 W   ? H A1IJH . ? B A1IJH 702 ? 1_555 S24 ? H A1IJH .   ? B A1IJH 702  ? 1_555 144.9 
? 
110 O   ? N HOH   .   ? B HOH   811  ? 1_555 W   ? H A1IJH . ? B A1IJH 702 ? 1_555 S23 ? H A1IJH .   ? B A1IJH 702  ? 1_555 146.8 
? 
111 S3  ? H A1IJH .   ? B A1IJH 702  ? 1_555 W   ? H A1IJH . ? B A1IJH 702 ? 1_555 S23 ? H A1IJH .   ? B A1IJH 702  ? 1_555 98.7  
? 
112 S4  ? H A1IJH .   ? B A1IJH 702  ? 1_555 W   ? H A1IJH . ? B A1IJH 702 ? 1_555 S23 ? H A1IJH .   ? B A1IJH 702  ? 1_555 92.1  
? 
113 S24 ? H A1IJH .   ? B A1IJH 702  ? 1_555 W   ? H A1IJH . ? B A1IJH 702 ? 1_555 S23 ? H A1IJH .   ? B A1IJH 702  ? 1_555 78.1  
? 
114 O   ? N HOH   .   ? B HOH   811  ? 1_555 W   ? H A1IJH . ? B A1IJH 702 ? 1_555 O   ? N HOH   .   ? B HOH   1301 ? 1_555 89.5  
? 
115 S3  ? H A1IJH .   ? B A1IJH 702  ? 1_555 W   ? H A1IJH . ? B A1IJH 702 ? 1_555 O   ? N HOH   .   ? B HOH   1301 ? 1_555 159.0 
? 
116 S4  ? H A1IJH .   ? B A1IJH 702  ? 1_555 W   ? H A1IJH . ? B A1IJH 702 ? 1_555 O   ? N HOH   .   ? B HOH   1301 ? 1_555 89.6  
? 
117 S24 ? H A1IJH .   ? B A1IJH 702  ? 1_555 W   ? H A1IJH . ? B A1IJH 702 ? 1_555 O   ? N HOH   .   ? B HOH   1301 ? 1_555 124.3 
? 
118 S23 ? H A1IJH .   ? B A1IJH 702  ? 1_555 W   ? H A1IJH . ? B A1IJH 702 ? 1_555 O   ? N HOH   .   ? B HOH   1301 ? 1_555 93.8  
? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 TYR 461 A . ? TYR 461 A PRO 462 A ? PRO 462 A 1 -5.22 
2 TYR 461 B . ? TYR 461 B PRO 462 B ? PRO 462 B 1 -6.20 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 6 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 6 ? 
AA6 ? 6 ? 
AA7 ? 3 ? 
AA8 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? parallel      
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? parallel      
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA8 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 17  ? ASN A 22  ? THR A 17  ASN A 22  
AA1 2 LYS A 7   ? ASN A 12  ? LYS A 7   ASN A 12  
AA1 3 MET A 109 ? GLU A 113 ? MET A 109 GLU A 113 
AA1 4 LYS A 58  ? THR A 63  ? LYS A 58  THR A 63  
AA1 5 PHE A 77  ? LYS A 82  ? PHE A 77  LYS A 82  
AA1 6 ILE A 89  ? SER A 94  ? ILE A 89  SER A 94  
AA2 1 LYS A 128 ? ASP A 133 ? LYS A 128 ASP A 133 
AA2 2 VAL A 120 ? VAL A 125 ? VAL A 120 VAL A 125 
AA2 3 LEU A 197 ? LYS A 203 ? LEU A 197 LYS A 203 
AA2 4 LYS A 158 ? CYS A 161 ? LYS A 158 CYS A 161 
AA2 5 VAL A 175 ? ASN A 177 ? VAL A 175 ASN A 177 
AA2 6 ARG A 181 ? ALA A 183 ? ARG A 181 ALA A 183 
AA3 1 LEU A 281 ? LYS A 284 ? LEU A 281 LYS A 284 
AA3 2 ARG A 296 ? ARG A 299 ? ARG A 296 ARG A 299 
AA3 3 GLU A 305 ? GLY A 307 ? GLU A 305 GLY A 307 
AA4 1 THR A 418 ? VAL A 419 ? THR A 418 VAL A 419 
AA4 2 GLN A 422 ? GLU A 423 ? GLN A 422 GLU A 423 
AA5 1 THR B 17  ? ASN B 22  ? THR B 17  ASN B 22  
AA5 2 LYS B 7   ? ASN B 12  ? LYS B 7   ASN B 12  
AA5 3 MET B 109 ? GLU B 113 ? MET B 109 GLU B 113 
AA5 4 PHE B 59  ? THR B 63  ? PHE B 59  THR B 63  
AA5 5 PHE B 77  ? LYS B 82  ? PHE B 77  LYS B 82  
AA5 6 ILE B 89  ? SER B 94  ? ILE B 89  SER B 94  
AA6 1 LYS B 128 ? ASP B 133 ? LYS B 128 ASP B 133 
AA6 2 VAL B 120 ? VAL B 125 ? VAL B 120 VAL B 125 
AA6 3 LEU B 197 ? LYS B 203 ? LEU B 197 LYS B 203 
AA6 4 LYS B 158 ? CYS B 161 ? LYS B 158 CYS B 161 
AA6 5 VAL B 175 ? ASN B 177 ? VAL B 175 ASN B 177 
AA6 6 ARG B 181 ? ALA B 183 ? ARG B 181 ALA B 183 
AA7 1 LEU B 281 ? LYS B 284 ? LEU B 281 LYS B 284 
AA7 2 ARG B 296 ? ARG B 299 ? ARG B 296 ARG B 299 
AA7 3 GLU B 305 ? GLY B 307 ? GLU B 305 GLY B 307 
AA8 1 THR B 418 ? VAL B 419 ? THR B 418 VAL B 419 
AA8 2 GLN B 422 ? GLU B 423 ? GLN B 422 GLU B 423 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O GLU A 21  ? O GLU A 21  N VAL A 8   ? N VAL A 8   
AA1 2 3 N ILE A 11  ? N ILE A 11  O GLU A 113 ? O GLU A 113 
AA1 3 4 O ILE A 110 ? O ILE A 110 N ILE A 61  ? N ILE A 61  
AA1 4 5 N ILE A 60  ? N ILE A 60  O VAL A 80  ? O VAL A 80  
AA1 5 6 N VAL A 79  ? N VAL A 79  O SER A 92  ? O SER A 92  
AA2 1 2 O GLU A 130 ? O GLU A 130 N GLU A 123 ? N GLU A 123 
AA2 2 3 N ILE A 122 ? N ILE A 122 O THR A 201 ? O THR A 201 
AA2 3 4 O VAL A 202 ? O VAL A 202 N LYS A 158 ? N LYS A 158 
AA2 4 5 N CYS A 161 ? N CYS A 161 O MET A 176 ? O MET A 176 
AA2 5 6 N VAL A 175 ? N VAL A 175 O ALA A 183 ? O ALA A 183 
AA3 1 2 N VAL A 282 ? N VAL A 282 O TRP A 297 ? O TRP A 297 
AA3 2 3 N VAL A 298 ? N VAL A 298 O CYS A 306 ? O CYS A 306 
AA4 1 2 N VAL A 419 ? N VAL A 419 O GLN A 422 ? O GLN A 422 
AA5 1 2 O GLU B 21  ? O GLU B 21  N VAL B 8   ? N VAL B 8   
AA5 2 3 N ILE B 11  ? N ILE B 11  O GLU B 113 ? O GLU B 113 
AA5 3 4 O ILE B 110 ? O ILE B 110 N ILE B 61  ? N ILE B 61  
AA5 4 5 N ILE B 60  ? N ILE B 60  O VAL B 80  ? O VAL B 80  
AA5 5 6 N VAL B 79  ? N VAL B 79  O SER B 92  ? O SER B 92  
AA6 1 2 O LYS B 132 ? O LYS B 132 N TYR B 121 ? N TYR B 121 
AA6 2 3 N VAL B 120 ? N VAL B 120 O LYS B 198 ? O LYS B 198 
AA6 3 4 O VAL B 202 ? O VAL B 202 N LYS B 158 ? N LYS B 158 
AA6 4 5 N CYS B 161 ? N CYS B 161 O MET B 176 ? O MET B 176 
AA6 5 6 N ASN B 177 ? N ASN B 177 O ARG B 181 ? O ARG B 181 
AA7 1 2 N VAL B 282 ? N VAL B 282 O TRP B 297 ? O TRP B 297 
AA7 2 3 N VAL B 298 ? N VAL B 298 O CYS B 306 ? O CYS B 306 
AA8 1 2 N VAL B 419 ? N VAL B 419 O GLN B 422 ? O GLN B 422 
# 
_pdbx_entry_details.entry_id                   9G7J 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   HZ1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   LYS 
_pdbx_validate_close_contact.auth_seq_id_1    218 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    801 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.53 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    HH21 
_pdbx_validate_symm_contact.auth_asym_id_1    B 
_pdbx_validate_symm_contact.auth_comp_id_1    ARG 
_pdbx_validate_symm_contact.auth_seq_id_1     570 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    HH21 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    ARG 
_pdbx_validate_symm_contact.auth_seq_id_2     570 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_556 
_pdbx_validate_symm_contact.dist              0.99 
# 
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 ILE A 32  ? ? 68.08   -54.43  
2  1 CYS A 34  ? ? 32.22   -117.06 
3  1 THR A 73  ? ? 71.98   37.60   
4  1 ASP A 114 ? ? 61.38   -154.14 
5  1 ASP A 126 ? ? 56.47   -122.23 
6  1 LYS A 156 ? ? 80.64   6.29    
7  1 VAL A 179 ? ? 73.55   -46.86  
8  1 ASP A 212 ? ? -152.17 89.29   
9  1 GLN A 235 ? ? -138.31 -58.30  
10 1 ASN A 279 ? ? -130.99 -83.06  
11 1 PRO A 425 ? ? -83.23  -156.77 
12 1 ALA A 426 ? ? -81.58  48.38   
13 1 ARG A 570 ? A -103.17 62.59   
14 1 ARG A 570 ? B -103.71 61.90   
15 1 LEU A 600 ? ? -106.26 42.35   
16 1 ILE B 32  ? ? 67.97   -53.87  
17 1 CYS B 34  ? ? 32.54   -117.40 
18 1 ASP B 114 ? ? 62.35   -150.89 
19 1 ASP B 126 ? ? 53.69   -119.81 
20 1 LYS B 156 ? ? 82.70   2.51    
21 1 VAL B 179 ? ? 71.72   -50.23  
22 1 GLN B 235 ? ? -141.43 -56.38  
23 1 ASN B 279 ? ? -126.33 -83.11  
24 1 PRO B 425 ? ? -80.66  -156.79 
25 1 ARG B 570 ? ? -103.45 57.80   
# 
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 529 ? A 0.167 'SIDE CHAIN' 
2 1 ARG A 570 ? A 0.277 'SIDE CHAIN' 
3 1 ARG B 529 ? A 0.191 'SIDE CHAIN' 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 1378 ? M HOH . 
2 1 A HOH 1399 ? M HOH . 
3 1 A HOH 1444 ? M HOH . 
4 1 A HOH 1581 ? M HOH . 
5 1 B HOH 1470 ? N HOH . 
# 
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 1580 ? 6.01 . 
2 1 O ? A HOH 1581 ? 6.10 . 
3 1 O ? A HOH 1582 ? 6.38 . 
4 1 O ? A HOH 1583 ? 6.67 . 
5 1 O ? B HOH 1519 ? 5.85 . 
6 1 O ? B HOH 1520 ? 5.89 . 
7 1 O ? B HOH 1521 ? 6.43 . 
# 
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 
A1IJH C1   C  N N 1   
A1IJH C2   C  N R 2   
A1IJH C3   C  N N 3   
A1IJH S3   S  N N 4   
A1IJH C4   C  N N 5   
A1IJH S4   S  N N 6   
A1IJH C5   C  N R 7   
A1IJH N6   N  N N 8   
A1IJH C7   C  N N 9   
A1IJH C8   C  N N 10  
A1IJH O8   O  N N 11  
A1IJH N9   N  N N 12  
A1IJH C10  C  N N 13  
A1IJH N10  N  N N 14  
A1IJH N11  N  N N 15  
A1IJH C12  C  N N 16  
A1IJH N13  N  N N 17  
A1IJH C14  C  N R 18  
A1IJH O2   O  N N 19  
A1IJH C21  C  N N 20  
A1IJH C22  C  N R 21  
A1IJH C23  C  N N 22  
A1IJH S23  S  N N 23  
A1IJH C24  C  N N 24  
A1IJH S24  S  N N 25  
A1IJH C25  C  N R 26  
A1IJH N26  N  N N 27  
A1IJH C27  C  N N 28  
A1IJH C28  C  N N 29  
A1IJH O28  O  N N 30  
A1IJH N29  N  N N 31  
A1IJH C30  C  N N 32  
A1IJH N30  N  N N 33  
A1IJH N31  N  N N 34  
A1IJH C32  C  N N 35  
A1IJH N33  N  N N 36  
A1IJH C34  C  N R 37  
A1IJH O22  O  N N 38  
A1IJH P1   P  N N 39  
A1IJH O1P  O  N N 40  
A1IJH O2P  O  N N 41  
A1IJH O3P  O  N N 42  
A1IJH O4P  O  N N 43  
A1IJH P2   P  N N 44  
A1IJH O5P  O  N N 45  
A1IJH O6P  O  N N 46  
A1IJH O7P  O  N N 47  
A1IJH O8P  O  N N 48  
A1IJH MG   MG N N 49  
A1IJH W    W  N N 50  
A1IJH H12  H  N N 51  
A1IJH H11  H  N N 52  
A1IJH H2   H  N N 53  
A1IJH H5   H  N N 54  
A1IJH H6   H  N N 55  
A1IJH H9   H  N N 56  
A1IJH H102 H  N N 57  
A1IJH H101 H  N N 58  
A1IJH H13  H  N N 59  
A1IJH H14  H  N N 60  
A1IJH H211 H  N N 61  
A1IJH H212 H  N N 62  
A1IJH H22  H  N N 63  
A1IJH H25  H  N N 64  
A1IJH H26  H  N N 65  
A1IJH H29  H  N N 66  
A1IJH H301 H  N N 67  
A1IJH H302 H  N N 68  
A1IJH H33  H  N N 69  
A1IJH H34  H  N N 70  
A1IJH H1   H  N N 71  
A1IJH H3   H  N N 72  
ALA   N    N  N N 73  
ALA   CA   C  N S 74  
ALA   C    C  N N 75  
ALA   O    O  N N 76  
ALA   CB   C  N N 77  
ALA   OXT  O  N N 78  
ALA   H    H  N N 79  
ALA   H2   H  N N 80  
ALA   HA   H  N N 81  
ALA   HB1  H  N N 82  
ALA   HB2  H  N N 83  
ALA   HB3  H  N N 84  
ALA   HXT  H  N N 85  
ARG   N    N  N N 86  
ARG   CA   C  N S 87  
ARG   C    C  N N 88  
ARG   O    O  N N 89  
ARG   CB   C  N N 90  
ARG   CG   C  N N 91  
ARG   CD   C  N N 92  
ARG   NE   N  N N 93  
ARG   CZ   C  N N 94  
ARG   NH1  N  N N 95  
ARG   NH2  N  N N 96  
ARG   OXT  O  N N 97  
ARG   H    H  N N 98  
ARG   H2   H  N N 99  
ARG   HA   H  N N 100 
ARG   HB2  H  N N 101 
ARG   HB3  H  N N 102 
ARG   HG2  H  N N 103 
ARG   HG3  H  N N 104 
ARG   HD2  H  N N 105 
ARG   HD3  H  N N 106 
ARG   HE   H  N N 107 
ARG   HH11 H  N N 108 
ARG   HH12 H  N N 109 
ARG   HH21 H  N N 110 
ARG   HH22 H  N N 111 
ARG   HXT  H  N N 112 
ASN   N    N  N N 113 
ASN   CA   C  N S 114 
ASN   C    C  N N 115 
ASN   O    O  N N 116 
ASN   CB   C  N N 117 
ASN   CG   C  N N 118 
ASN   OD1  O  N N 119 
ASN   ND2  N  N N 120 
ASN   OXT  O  N N 121 
ASN   H    H  N N 122 
ASN   H2   H  N N 123 
ASN   HA   H  N N 124 
ASN   HB2  H  N N 125 
ASN   HB3  H  N N 126 
ASN   HD21 H  N N 127 
ASN   HD22 H  N N 128 
ASN   HXT  H  N N 129 
ASP   N    N  N N 130 
ASP   CA   C  N S 131 
ASP   C    C  N N 132 
ASP   O    O  N N 133 
ASP   CB   C  N N 134 
ASP   CG   C  N N 135 
ASP   OD1  O  N N 136 
ASP   OD2  O  N N 137 
ASP   OXT  O  N N 138 
ASP   H    H  N N 139 
ASP   H2   H  N N 140 
ASP   HA   H  N N 141 
ASP   HB2  H  N N 142 
ASP   HB3  H  N N 143 
ASP   HD2  H  N N 144 
ASP   HXT  H  N N 145 
CL    CL   CL N N 146 
CYS   N    N  N N 147 
CYS   CA   C  N R 148 
CYS   C    C  N N 149 
CYS   O    O  N N 150 
CYS   CB   C  N N 151 
CYS   SG   S  N N 152 
CYS   OXT  O  N N 153 
CYS   H    H  N N 154 
CYS   H2   H  N N 155 
CYS   HA   H  N N 156 
CYS   HB2  H  N N 157 
CYS   HB3  H  N N 158 
CYS   HG   H  N N 159 
CYS   HXT  H  N N 160 
EDO   C1   C  N N 161 
EDO   O1   O  N N 162 
EDO   C2   C  N N 163 
EDO   O2   O  N N 164 
EDO   H11  H  N N 165 
EDO   H12  H  N N 166 
EDO   HO1  H  N N 167 
EDO   H21  H  N N 168 
EDO   H22  H  N N 169 
EDO   HO2  H  N N 170 
GLN   N    N  N N 171 
GLN   CA   C  N S 172 
GLN   C    C  N N 173 
GLN   O    O  N N 174 
GLN   CB   C  N N 175 
GLN   CG   C  N N 176 
GLN   CD   C  N N 177 
GLN   OE1  O  N N 178 
GLN   NE2  N  N N 179 
GLN   OXT  O  N N 180 
GLN   H    H  N N 181 
GLN   H2   H  N N 182 
GLN   HA   H  N N 183 
GLN   HB2  H  N N 184 
GLN   HB3  H  N N 185 
GLN   HG2  H  N N 186 
GLN   HG3  H  N N 187 
GLN   HE21 H  N N 188 
GLN   HE22 H  N N 189 
GLN   HXT  H  N N 190 
GLU   N    N  N N 191 
GLU   CA   C  N S 192 
GLU   C    C  N N 193 
GLU   O    O  N N 194 
GLU   CB   C  N N 195 
GLU   CG   C  N N 196 
GLU   CD   C  N N 197 
GLU   OE1  O  N N 198 
GLU   OE2  O  N N 199 
GLU   OXT  O  N N 200 
GLU   H    H  N N 201 
GLU   H2   H  N N 202 
GLU   HA   H  N N 203 
GLU   HB2  H  N N 204 
GLU   HB3  H  N N 205 
GLU   HG2  H  N N 206 
GLU   HG3  H  N N 207 
GLU   HE2  H  N N 208 
GLU   HXT  H  N N 209 
GLY   N    N  N N 210 
GLY   CA   C  N N 211 
GLY   C    C  N N 212 
GLY   O    O  N N 213 
GLY   OXT  O  N N 214 
GLY   H    H  N N 215 
GLY   H2   H  N N 216 
GLY   HA2  H  N N 217 
GLY   HA3  H  N N 218 
GLY   HXT  H  N N 219 
HIS   N    N  N N 220 
HIS   CA   C  N S 221 
HIS   C    C  N N 222 
HIS   O    O  N N 223 
HIS   CB   C  N N 224 
HIS   CG   C  Y N 225 
HIS   ND1  N  Y N 226 
HIS   CD2  C  Y N 227 
HIS   CE1  C  Y N 228 
HIS   NE2  N  Y N 229 
HIS   OXT  O  N N 230 
HIS   H    H  N N 231 
HIS   H2   H  N N 232 
HIS   HA   H  N N 233 
HIS   HB2  H  N N 234 
HIS   HB3  H  N N 235 
HIS   HD1  H  N N 236 
HIS   HD2  H  N N 237 
HIS   HE1  H  N N 238 
HIS   HE2  H  N N 239 
HIS   HXT  H  N N 240 
HOH   O    O  N N 241 
HOH   H1   H  N N 242 
HOH   H2   H  N N 243 
ILE   N    N  N N 244 
ILE   CA   C  N S 245 
ILE   C    C  N N 246 
ILE   O    O  N N 247 
ILE   CB   C  N S 248 
ILE   CG1  C  N N 249 
ILE   CG2  C  N N 250 
ILE   CD1  C  N N 251 
ILE   OXT  O  N N 252 
ILE   H    H  N N 253 
ILE   H2   H  N N 254 
ILE   HA   H  N N 255 
ILE   HB   H  N N 256 
ILE   HG12 H  N N 257 
ILE   HG13 H  N N 258 
ILE   HG21 H  N N 259 
ILE   HG22 H  N N 260 
ILE   HG23 H  N N 261 
ILE   HD11 H  N N 262 
ILE   HD12 H  N N 263 
ILE   HD13 H  N N 264 
ILE   HXT  H  N N 265 
LEU   N    N  N N 266 
LEU   CA   C  N S 267 
LEU   C    C  N N 268 
LEU   O    O  N N 269 
LEU   CB   C  N N 270 
LEU   CG   C  N N 271 
LEU   CD1  C  N N 272 
LEU   CD2  C  N N 273 
LEU   OXT  O  N N 274 
LEU   H    H  N N 275 
LEU   H2   H  N N 276 
LEU   HA   H  N N 277 
LEU   HB2  H  N N 278 
LEU   HB3  H  N N 279 
LEU   HG   H  N N 280 
LEU   HD11 H  N N 281 
LEU   HD12 H  N N 282 
LEU   HD13 H  N N 283 
LEU   HD21 H  N N 284 
LEU   HD22 H  N N 285 
LEU   HD23 H  N N 286 
LEU   HXT  H  N N 287 
LYS   N    N  N N 288 
LYS   CA   C  N S 289 
LYS   C    C  N N 290 
LYS   O    O  N N 291 
LYS   CB   C  N N 292 
LYS   CG   C  N N 293 
LYS   CD   C  N N 294 
LYS   CE   C  N N 295 
LYS   NZ   N  N N 296 
LYS   OXT  O  N N 297 
LYS   H    H  N N 298 
LYS   H2   H  N N 299 
LYS   HA   H  N N 300 
LYS   HB2  H  N N 301 
LYS   HB3  H  N N 302 
LYS   HG2  H  N N 303 
LYS   HG3  H  N N 304 
LYS   HD2  H  N N 305 
LYS   HD3  H  N N 306 
LYS   HE2  H  N N 307 
LYS   HE3  H  N N 308 
LYS   HZ1  H  N N 309 
LYS   HZ2  H  N N 310 
LYS   HZ3  H  N N 311 
LYS   HXT  H  N N 312 
MET   N    N  N N 313 
MET   CA   C  N S 314 
MET   C    C  N N 315 
MET   O    O  N N 316 
MET   CB   C  N N 317 
MET   CG   C  N N 318 
MET   SD   S  N N 319 
MET   CE   C  N N 320 
MET   OXT  O  N N 321 
MET   H    H  N N 322 
MET   H2   H  N N 323 
MET   HA   H  N N 324 
MET   HB2  H  N N 325 
MET   HB3  H  N N 326 
MET   HG2  H  N N 327 
MET   HG3  H  N N 328 
MET   HE1  H  N N 329 
MET   HE2  H  N N 330 
MET   HE3  H  N N 331 
MET   HXT  H  N N 332 
MG    MG   MG N N 333 
PHE   N    N  N N 334 
PHE   CA   C  N S 335 
PHE   C    C  N N 336 
PHE   O    O  N N 337 
PHE   CB   C  N N 338 
PHE   CG   C  Y N 339 
PHE   CD1  C  Y N 340 
PHE   CD2  C  Y N 341 
PHE   CE1  C  Y N 342 
PHE   CE2  C  Y N 343 
PHE   CZ   C  Y N 344 
PHE   OXT  O  N N 345 
PHE   H    H  N N 346 
PHE   H2   H  N N 347 
PHE   HA   H  N N 348 
PHE   HB2  H  N N 349 
PHE   HB3  H  N N 350 
PHE   HD1  H  N N 351 
PHE   HD2  H  N N 352 
PHE   HE1  H  N N 353 
PHE   HE2  H  N N 354 
PHE   HZ   H  N N 355 
PHE   HXT  H  N N 356 
PRO   N    N  N N 357 
PRO   CA   C  N S 358 
PRO   C    C  N N 359 
PRO   O    O  N N 360 
PRO   CB   C  N N 361 
PRO   CG   C  N N 362 
PRO   CD   C  N N 363 
PRO   OXT  O  N N 364 
PRO   H    H  N N 365 
PRO   HA   H  N N 366 
PRO   HB2  H  N N 367 
PRO   HB3  H  N N 368 
PRO   HG2  H  N N 369 
PRO   HG3  H  N N 370 
PRO   HD2  H  N N 371 
PRO   HD3  H  N N 372 
PRO   HXT  H  N N 373 
SER   N    N  N N 374 
SER   CA   C  N S 375 
SER   C    C  N N 376 
SER   O    O  N N 377 
SER   CB   C  N N 378 
SER   OG   O  N N 379 
SER   OXT  O  N N 380 
SER   H    H  N N 381 
SER   H2   H  N N 382 
SER   HA   H  N N 383 
SER   HB2  H  N N 384 
SER   HB3  H  N N 385 
SER   HG   H  N N 386 
SER   HXT  H  N N 387 
SF4   FE1  FE N N 388 
SF4   FE2  FE N N 389 
SF4   FE3  FE N N 390 
SF4   FE4  FE N N 391 
SF4   S1   S  N N 392 
SF4   S2   S  N N 393 
SF4   S3   S  N N 394 
SF4   S4   S  N N 395 
THR   N    N  N N 396 
THR   CA   C  N S 397 
THR   C    C  N N 398 
THR   O    O  N N 399 
THR   CB   C  N R 400 
THR   OG1  O  N N 401 
THR   CG2  C  N N 402 
THR   OXT  O  N N 403 
THR   H    H  N N 404 
THR   H2   H  N N 405 
THR   HA   H  N N 406 
THR   HB   H  N N 407 
THR   HG1  H  N N 408 
THR   HG21 H  N N 409 
THR   HG22 H  N N 410 
THR   HG23 H  N N 411 
THR   HXT  H  N N 412 
TRP   N    N  N N 413 
TRP   CA   C  N S 414 
TRP   C    C  N N 415 
TRP   O    O  N N 416 
TRP   CB   C  N N 417 
TRP   CG   C  Y N 418 
TRP   CD1  C  Y N 419 
TRP   CD2  C  Y N 420 
TRP   NE1  N  Y N 421 
TRP   CE2  C  Y N 422 
TRP   CE3  C  Y N 423 
TRP   CZ2  C  Y N 424 
TRP   CZ3  C  Y N 425 
TRP   CH2  C  Y N 426 
TRP   OXT  O  N N 427 
TRP   H    H  N N 428 
TRP   H2   H  N N 429 
TRP   HA   H  N N 430 
TRP   HB2  H  N N 431 
TRP   HB3  H  N N 432 
TRP   HD1  H  N N 433 
TRP   HE1  H  N N 434 
TRP   HE3  H  N N 435 
TRP   HZ2  H  N N 436 
TRP   HZ3  H  N N 437 
TRP   HH2  H  N N 438 
TRP   HXT  H  N N 439 
TYR   N    N  N N 440 
TYR   CA   C  N S 441 
TYR   C    C  N N 442 
TYR   O    O  N N 443 
TYR   CB   C  N N 444 
TYR   CG   C  Y N 445 
TYR   CD1  C  Y N 446 
TYR   CD2  C  Y N 447 
TYR   CE1  C  Y N 448 
TYR   CE2  C  Y N 449 
TYR   CZ   C  Y N 450 
TYR   OH   O  N N 451 
TYR   OXT  O  N N 452 
TYR   H    H  N N 453 
TYR   H2   H  N N 454 
TYR   HA   H  N N 455 
TYR   HB2  H  N N 456 
TYR   HB3  H  N N 457 
TYR   HD1  H  N N 458 
TYR   HD2  H  N N 459 
TYR   HE1  H  N N 460 
TYR   HE2  H  N N 461 
TYR   HH   H  N N 462 
TYR   HXT  H  N N 463 
VAL   N    N  N N 464 
VAL   CA   C  N S 465 
VAL   C    C  N N 466 
VAL   O    O  N N 467 
VAL   CB   C  N N 468 
VAL   CG1  C  N N 469 
VAL   CG2  C  N N 470 
VAL   OXT  O  N N 471 
VAL   H    H  N N 472 
VAL   H2   H  N N 473 
VAL   HA   H  N N 474 
VAL   HB   H  N N 475 
VAL   HG11 H  N N 476 
VAL   HG12 H  N N 477 
VAL   HG13 H  N N 478 
VAL   HG21 H  N N 479 
VAL   HG22 H  N N 480 
VAL   HG23 H  N N 481 
VAL   HXT  H  N N 482 
# 
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 
A1IJH O2P P1   doub N N 1   
A1IJH O4P P1   sing N N 2   
A1IJH O4P C1   sing N N 3   
A1IJH P1  O3P  sing N N 4   
A1IJH P1  O1P  sing N N 5   
A1IJH C2  C1   sing N N 6   
A1IJH C2  O2   sing N N 7   
A1IJH C2  C3   sing N N 8   
A1IJH C14 N13  sing N N 9   
A1IJH C14 O2   sing N N 10  
A1IJH C14 C5   sing N N 11  
A1IJH N13 C12  sing N N 12  
A1IJH C3  S3   sing N N 13  
A1IJH C3  C4   doub N N 14  
A1IJH O28 C28  doub N N 15  
A1IJH S3  W    sing N N 16  
A1IJH O1P MG   sing N N 17  
A1IJH C4  C5   sing N N 18  
A1IJH C4  S4   sing N N 19  
A1IJH C5  N6   sing N N 20  
A1IJH C12 N11  sing N N 21  
A1IJH C12 C7   doub N N 22  
A1IJH N11 C10  doub N N 23  
A1IJH C28 N29  sing N N 24  
A1IJH C28 C27  sing N N 25  
A1IJH S4  W    sing N N 26  
A1IJH N29 C30  sing N N 27  
A1IJH W   S24  sing N N 28  
A1IJH W   S23  sing N N 29  
A1IJH S24 C24  sing N N 30  
A1IJH N6  C7   sing N N 31  
A1IJH C7  C8   sing N N 32  
A1IJH C10 N10  sing N N 33  
A1IJH C10 N9   sing N N 34  
A1IJH N26 C27  sing N N 35  
A1IJH N26 C25  sing N N 36  
A1IJH MG  O5P  sing N N 37  
A1IJH C27 C32  doub N N 38  
A1IJH C30 N30  sing N N 39  
A1IJH C30 N31  doub N N 40  
A1IJH C24 C25  sing N N 41  
A1IJH C24 C23  doub N N 42  
A1IJH C25 C34  sing N N 43  
A1IJH N9  C8   sing N N 44  
A1IJH C8  O8   doub N N 45  
A1IJH C32 N31  sing N N 46  
A1IJH C32 N33  sing N N 47  
A1IJH S23 C23  sing N N 48  
A1IJH C23 C22  sing N N 49  
A1IJH O5P P2   sing N N 50  
A1IJH C34 N33  sing N N 51  
A1IJH C34 O22  sing N N 52  
A1IJH O22 C22  sing N N 53  
A1IJH C21 C22  sing N N 54  
A1IJH C21 O8P  sing N N 55  
A1IJH O7P P2   doub N N 56  
A1IJH P2  O8P  sing N N 57  
A1IJH P2  O6P  sing N N 58  
A1IJH C1  H12  sing N N 59  
A1IJH C1  H11  sing N N 60  
A1IJH C2  H2   sing N N 61  
A1IJH C5  H5   sing N N 62  
A1IJH N6  H6   sing N N 63  
A1IJH N9  H9   sing N N 64  
A1IJH N10 H102 sing N N 65  
A1IJH N10 H101 sing N N 66  
A1IJH N13 H13  sing N N 67  
A1IJH C14 H14  sing N N 68  
A1IJH C21 H211 sing N N 69  
A1IJH C21 H212 sing N N 70  
A1IJH C22 H22  sing N N 71  
A1IJH C25 H25  sing N N 72  
A1IJH N26 H26  sing N N 73  
A1IJH N29 H29  sing N N 74  
A1IJH N30 H301 sing N N 75  
A1IJH N30 H302 sing N N 76  
A1IJH N33 H33  sing N N 77  
A1IJH C34 H34  sing N N 78  
A1IJH O3P H1   sing N N 79  
A1IJH O6P H3   sing N N 80  
ALA   N   CA   sing N N 81  
ALA   N   H    sing N N 82  
ALA   N   H2   sing N N 83  
ALA   CA  C    sing N N 84  
ALA   CA  CB   sing N N 85  
ALA   CA  HA   sing N N 86  
ALA   C   O    doub N N 87  
ALA   C   OXT  sing N N 88  
ALA   CB  HB1  sing N N 89  
ALA   CB  HB2  sing N N 90  
ALA   CB  HB3  sing N N 91  
ALA   OXT HXT  sing N N 92  
ARG   N   CA   sing N N 93  
ARG   N   H    sing N N 94  
ARG   N   H2   sing N N 95  
ARG   CA  C    sing N N 96  
ARG   CA  CB   sing N N 97  
ARG   CA  HA   sing N N 98  
ARG   C   O    doub N N 99  
ARG   C   OXT  sing N N 100 
ARG   CB  CG   sing N N 101 
ARG   CB  HB2  sing N N 102 
ARG   CB  HB3  sing N N 103 
ARG   CG  CD   sing N N 104 
ARG   CG  HG2  sing N N 105 
ARG   CG  HG3  sing N N 106 
ARG   CD  NE   sing N N 107 
ARG   CD  HD2  sing N N 108 
ARG   CD  HD3  sing N N 109 
ARG   NE  CZ   sing N N 110 
ARG   NE  HE   sing N N 111 
ARG   CZ  NH1  sing N N 112 
ARG   CZ  NH2  doub N N 113 
ARG   NH1 HH11 sing N N 114 
ARG   NH1 HH12 sing N N 115 
ARG   NH2 HH21 sing N N 116 
ARG   NH2 HH22 sing N N 117 
ARG   OXT HXT  sing N N 118 
ASN   N   CA   sing N N 119 
ASN   N   H    sing N N 120 
ASN   N   H2   sing N N 121 
ASN   CA  C    sing N N 122 
ASN   CA  CB   sing N N 123 
ASN   CA  HA   sing N N 124 
ASN   C   O    doub N N 125 
ASN   C   OXT  sing N N 126 
ASN   CB  CG   sing N N 127 
ASN   CB  HB2  sing N N 128 
ASN   CB  HB3  sing N N 129 
ASN   CG  OD1  doub N N 130 
ASN   CG  ND2  sing N N 131 
ASN   ND2 HD21 sing N N 132 
ASN   ND2 HD22 sing N N 133 
ASN   OXT HXT  sing N N 134 
ASP   N   CA   sing N N 135 
ASP   N   H    sing N N 136 
ASP   N   H2   sing N N 137 
ASP   CA  C    sing N N 138 
ASP   CA  CB   sing N N 139 
ASP   CA  HA   sing N N 140 
ASP   C   O    doub N N 141 
ASP   C   OXT  sing N N 142 
ASP   CB  CG   sing N N 143 
ASP   CB  HB2  sing N N 144 
ASP   CB  HB3  sing N N 145 
ASP   CG  OD1  doub N N 146 
ASP   CG  OD2  sing N N 147 
ASP   OD2 HD2  sing N N 148 
ASP   OXT HXT  sing N N 149 
CYS   N   CA   sing N N 150 
CYS   N   H    sing N N 151 
CYS   N   H2   sing N N 152 
CYS   CA  C    sing N N 153 
CYS   CA  CB   sing N N 154 
CYS   CA  HA   sing N N 155 
CYS   C   O    doub N N 156 
CYS   C   OXT  sing N N 157 
CYS   CB  SG   sing N N 158 
CYS   CB  HB2  sing N N 159 
CYS   CB  HB3  sing N N 160 
CYS   SG  HG   sing N N 161 
CYS   OXT HXT  sing N N 162 
EDO   C1  O1   sing N N 163 
EDO   C1  C2   sing N N 164 
EDO   C1  H11  sing N N 165 
EDO   C1  H12  sing N N 166 
EDO   O1  HO1  sing N N 167 
EDO   C2  O2   sing N N 168 
EDO   C2  H21  sing N N 169 
EDO   C2  H22  sing N N 170 
EDO   O2  HO2  sing N N 171 
GLN   N   CA   sing N N 172 
GLN   N   H    sing N N 173 
GLN   N   H2   sing N N 174 
GLN   CA  C    sing N N 175 
GLN   CA  CB   sing N N 176 
GLN   CA  HA   sing N N 177 
GLN   C   O    doub N N 178 
GLN   C   OXT  sing N N 179 
GLN   CB  CG   sing N N 180 
GLN   CB  HB2  sing N N 181 
GLN   CB  HB3  sing N N 182 
GLN   CG  CD   sing N N 183 
GLN   CG  HG2  sing N N 184 
GLN   CG  HG3  sing N N 185 
GLN   CD  OE1  doub N N 186 
GLN   CD  NE2  sing N N 187 
GLN   NE2 HE21 sing N N 188 
GLN   NE2 HE22 sing N N 189 
GLN   OXT HXT  sing N N 190 
GLU   N   CA   sing N N 191 
GLU   N   H    sing N N 192 
GLU   N   H2   sing N N 193 
GLU   CA  C    sing N N 194 
GLU   CA  CB   sing N N 195 
GLU   CA  HA   sing N N 196 
GLU   C   O    doub N N 197 
GLU   C   OXT  sing N N 198 
GLU   CB  CG   sing N N 199 
GLU   CB  HB2  sing N N 200 
GLU   CB  HB3  sing N N 201 
GLU   CG  CD   sing N N 202 
GLU   CG  HG2  sing N N 203 
GLU   CG  HG3  sing N N 204 
GLU   CD  OE1  doub N N 205 
GLU   CD  OE2  sing N N 206 
GLU   OE2 HE2  sing N N 207 
GLU   OXT HXT  sing N N 208 
GLY   N   CA   sing N N 209 
GLY   N   H    sing N N 210 
GLY   N   H2   sing N N 211 
GLY   CA  C    sing N N 212 
GLY   CA  HA2  sing N N 213 
GLY   CA  HA3  sing N N 214 
GLY   C   O    doub N N 215 
GLY   C   OXT  sing N N 216 
GLY   OXT HXT  sing N N 217 
HIS   N   CA   sing N N 218 
HIS   N   H    sing N N 219 
HIS   N   H2   sing N N 220 
HIS   CA  C    sing N N 221 
HIS   CA  CB   sing N N 222 
HIS   CA  HA   sing N N 223 
HIS   C   O    doub N N 224 
HIS   C   OXT  sing N N 225 
HIS   CB  CG   sing N N 226 
HIS   CB  HB2  sing N N 227 
HIS   CB  HB3  sing N N 228 
HIS   CG  ND1  sing Y N 229 
HIS   CG  CD2  doub Y N 230 
HIS   ND1 CE1  doub Y N 231 
HIS   ND1 HD1  sing N N 232 
HIS   CD2 NE2  sing Y N 233 
HIS   CD2 HD2  sing N N 234 
HIS   CE1 NE2  sing Y N 235 
HIS   CE1 HE1  sing N N 236 
HIS   NE2 HE2  sing N N 237 
HIS   OXT HXT  sing N N 238 
HOH   O   H1   sing N N 239 
HOH   O   H2   sing N N 240 
ILE   N   CA   sing N N 241 
ILE   N   H    sing N N 242 
ILE   N   H2   sing N N 243 
ILE   CA  C    sing N N 244 
ILE   CA  CB   sing N N 245 
ILE   CA  HA   sing N N 246 
ILE   C   O    doub N N 247 
ILE   C   OXT  sing N N 248 
ILE   CB  CG1  sing N N 249 
ILE   CB  CG2  sing N N 250 
ILE   CB  HB   sing N N 251 
ILE   CG1 CD1  sing N N 252 
ILE   CG1 HG12 sing N N 253 
ILE   CG1 HG13 sing N N 254 
ILE   CG2 HG21 sing N N 255 
ILE   CG2 HG22 sing N N 256 
ILE   CG2 HG23 sing N N 257 
ILE   CD1 HD11 sing N N 258 
ILE   CD1 HD12 sing N N 259 
ILE   CD1 HD13 sing N N 260 
ILE   OXT HXT  sing N N 261 
LEU   N   CA   sing N N 262 
LEU   N   H    sing N N 263 
LEU   N   H2   sing N N 264 
LEU   CA  C    sing N N 265 
LEU   CA  CB   sing N N 266 
LEU   CA  HA   sing N N 267 
LEU   C   O    doub N N 268 
LEU   C   OXT  sing N N 269 
LEU   CB  CG   sing N N 270 
LEU   CB  HB2  sing N N 271 
LEU   CB  HB3  sing N N 272 
LEU   CG  CD1  sing N N 273 
LEU   CG  CD2  sing N N 274 
LEU   CG  HG   sing N N 275 
LEU   CD1 HD11 sing N N 276 
LEU   CD1 HD12 sing N N 277 
LEU   CD1 HD13 sing N N 278 
LEU   CD2 HD21 sing N N 279 
LEU   CD2 HD22 sing N N 280 
LEU   CD2 HD23 sing N N 281 
LEU   OXT HXT  sing N N 282 
LYS   N   CA   sing N N 283 
LYS   N   H    sing N N 284 
LYS   N   H2   sing N N 285 
LYS   CA  C    sing N N 286 
LYS   CA  CB   sing N N 287 
LYS   CA  HA   sing N N 288 
LYS   C   O    doub N N 289 
LYS   C   OXT  sing N N 290 
LYS   CB  CG   sing N N 291 
LYS   CB  HB2  sing N N 292 
LYS   CB  HB3  sing N N 293 
LYS   CG  CD   sing N N 294 
LYS   CG  HG2  sing N N 295 
LYS   CG  HG3  sing N N 296 
LYS   CD  CE   sing N N 297 
LYS   CD  HD2  sing N N 298 
LYS   CD  HD3  sing N N 299 
LYS   CE  NZ   sing N N 300 
LYS   CE  HE2  sing N N 301 
LYS   CE  HE3  sing N N 302 
LYS   NZ  HZ1  sing N N 303 
LYS   NZ  HZ2  sing N N 304 
LYS   NZ  HZ3  sing N N 305 
LYS   OXT HXT  sing N N 306 
MET   N   CA   sing N N 307 
MET   N   H    sing N N 308 
MET   N   H2   sing N N 309 
MET   CA  C    sing N N 310 
MET   CA  CB   sing N N 311 
MET   CA  HA   sing N N 312 
MET   C   O    doub N N 313 
MET   C   OXT  sing N N 314 
MET   CB  CG   sing N N 315 
MET   CB  HB2  sing N N 316 
MET   CB  HB3  sing N N 317 
MET   CG  SD   sing N N 318 
MET   CG  HG2  sing N N 319 
MET   CG  HG3  sing N N 320 
MET   SD  CE   sing N N 321 
MET   CE  HE1  sing N N 322 
MET   CE  HE2  sing N N 323 
MET   CE  HE3  sing N N 324 
MET   OXT HXT  sing N N 325 
PHE   N   CA   sing N N 326 
PHE   N   H    sing N N 327 
PHE   N   H2   sing N N 328 
PHE   CA  C    sing N N 329 
PHE   CA  CB   sing N N 330 
PHE   CA  HA   sing N N 331 
PHE   C   O    doub N N 332 
PHE   C   OXT  sing N N 333 
PHE   CB  CG   sing N N 334 
PHE   CB  HB2  sing N N 335 
PHE   CB  HB3  sing N N 336 
PHE   CG  CD1  doub Y N 337 
PHE   CG  CD2  sing Y N 338 
PHE   CD1 CE1  sing Y N 339 
PHE   CD1 HD1  sing N N 340 
PHE   CD2 CE2  doub Y N 341 
PHE   CD2 HD2  sing N N 342 
PHE   CE1 CZ   doub Y N 343 
PHE   CE1 HE1  sing N N 344 
PHE   CE2 CZ   sing Y N 345 
PHE   CE2 HE2  sing N N 346 
PHE   CZ  HZ   sing N N 347 
PHE   OXT HXT  sing N N 348 
PRO   N   CA   sing N N 349 
PRO   N   CD   sing N N 350 
PRO   N   H    sing N N 351 
PRO   CA  C    sing N N 352 
PRO   CA  CB   sing N N 353 
PRO   CA  HA   sing N N 354 
PRO   C   O    doub N N 355 
PRO   C   OXT  sing N N 356 
PRO   CB  CG   sing N N 357 
PRO   CB  HB2  sing N N 358 
PRO   CB  HB3  sing N N 359 
PRO   CG  CD   sing N N 360 
PRO   CG  HG2  sing N N 361 
PRO   CG  HG3  sing N N 362 
PRO   CD  HD2  sing N N 363 
PRO   CD  HD3  sing N N 364 
PRO   OXT HXT  sing N N 365 
SER   N   CA   sing N N 366 
SER   N   H    sing N N 367 
SER   N   H2   sing N N 368 
SER   CA  C    sing N N 369 
SER   CA  CB   sing N N 370 
SER   CA  HA   sing N N 371 
SER   C   O    doub N N 372 
SER   C   OXT  sing N N 373 
SER   CB  OG   sing N N 374 
SER   CB  HB2  sing N N 375 
SER   CB  HB3  sing N N 376 
SER   OG  HG   sing N N 377 
SER   OXT HXT  sing N N 378 
SF4   FE1 S2   sing N N 379 
SF4   FE1 S3   sing N N 380 
SF4   FE1 S4   sing N N 381 
SF4   FE2 S1   sing N N 382 
SF4   FE2 S3   sing N N 383 
SF4   FE2 S4   sing N N 384 
SF4   FE3 S1   sing N N 385 
SF4   FE3 S2   sing N N 386 
SF4   FE3 S4   sing N N 387 
SF4   FE4 S1   sing N N 388 
SF4   FE4 S2   sing N N 389 
SF4   FE4 S3   sing N N 390 
THR   N   CA   sing N N 391 
THR   N   H    sing N N 392 
THR   N   H2   sing N N 393 
THR   CA  C    sing N N 394 
THR   CA  CB   sing N N 395 
THR   CA  HA   sing N N 396 
THR   C   O    doub N N 397 
THR   C   OXT  sing N N 398 
THR   CB  OG1  sing N N 399 
THR   CB  CG2  sing N N 400 
THR   CB  HB   sing N N 401 
THR   OG1 HG1  sing N N 402 
THR   CG2 HG21 sing N N 403 
THR   CG2 HG22 sing N N 404 
THR   CG2 HG23 sing N N 405 
THR   OXT HXT  sing N N 406 
TRP   N   CA   sing N N 407 
TRP   N   H    sing N N 408 
TRP   N   H2   sing N N 409 
TRP   CA  C    sing N N 410 
TRP   CA  CB   sing N N 411 
TRP   CA  HA   sing N N 412 
TRP   C   O    doub N N 413 
TRP   C   OXT  sing N N 414 
TRP   CB  CG   sing N N 415 
TRP   CB  HB2  sing N N 416 
TRP   CB  HB3  sing N N 417 
TRP   CG  CD1  doub Y N 418 
TRP   CG  CD2  sing Y N 419 
TRP   CD1 NE1  sing Y N 420 
TRP   CD1 HD1  sing N N 421 
TRP   CD2 CE2  doub Y N 422 
TRP   CD2 CE3  sing Y N 423 
TRP   NE1 CE2  sing Y N 424 
TRP   NE1 HE1  sing N N 425 
TRP   CE2 CZ2  sing Y N 426 
TRP   CE3 CZ3  doub Y N 427 
TRP   CE3 HE3  sing N N 428 
TRP   CZ2 CH2  doub Y N 429 
TRP   CZ2 HZ2  sing N N 430 
TRP   CZ3 CH2  sing Y N 431 
TRP   CZ3 HZ3  sing N N 432 
TRP   CH2 HH2  sing N N 433 
TRP   OXT HXT  sing N N 434 
TYR   N   CA   sing N N 435 
TYR   N   H    sing N N 436 
TYR   N   H2   sing N N 437 
TYR   CA  C    sing N N 438 
TYR   CA  CB   sing N N 439 
TYR   CA  HA   sing N N 440 
TYR   C   O    doub N N 441 
TYR   C   OXT  sing N N 442 
TYR   CB  CG   sing N N 443 
TYR   CB  HB2  sing N N 444 
TYR   CB  HB3  sing N N 445 
TYR   CG  CD1  doub Y N 446 
TYR   CG  CD2  sing Y N 447 
TYR   CD1 CE1  sing Y N 448 
TYR   CD1 HD1  sing N N 449 
TYR   CD2 CE2  doub Y N 450 
TYR   CD2 HD2  sing N N 451 
TYR   CE1 CZ   doub Y N 452 
TYR   CE1 HE1  sing N N 453 
TYR   CE2 CZ   sing Y N 454 
TYR   CE2 HE2  sing N N 455 
TYR   CZ  OH   sing N N 456 
TYR   OH  HH   sing N N 457 
TYR   OXT HXT  sing N N 458 
VAL   N   CA   sing N N 459 
VAL   N   H    sing N N 460 
VAL   N   H2   sing N N 461 
VAL   CA  C    sing N N 462 
VAL   CA  CB   sing N N 463 
VAL   CA  HA   sing N N 464 
VAL   C   O    doub N N 465 
VAL   C   OXT  sing N N 466 
VAL   CB  CG1  sing N N 467 
VAL   CB  CG2  sing N N 468 
VAL   CB  HB   sing N N 469 
VAL   CG1 HG11 sing N N 470 
VAL   CG1 HG12 sing N N 471 
VAL   CG1 HG13 sing N N 472 
VAL   CG2 HG21 sing N N 473 
VAL   CG2 HG22 sing N N 474 
VAL   CG2 HG23 sing N N 475 
VAL   OXT HXT  sing N N 476 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Max Planck Society'               Germany ?                          1 
'German Research Foundation (DFG)' Germany 'DFG-SPP 1927 WA 4053/1-1' 2 
# 
_atom_sites.entry_id                    9G7J 
_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]   0.015481 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009957 
_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]   0.005663 
_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  
CL 
FE 
H  
MG 
N  
O  
P  
S  
W  
# 
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    . MET   A 1 1   ? 28.885 55.818  35.426 1.00 43.28 ? 1    MET   A N    1 
ATOM   2     C  CA   . MET   A 1 1   ? 27.540 56.246  34.955 1.00 42.76 ? 1    MET   A CA   1 
ATOM   3     C  C    . MET   A 1 1   ? 26.468 55.374  35.609 1.00 37.99 ? 1    MET   A C    1 
ATOM   4     O  O    . MET   A 1 1   ? 26.843 54.467  36.374 1.00 35.09 ? 1    MET   A O    1 
ATOM   5     C  CB   . MET   A 1 1   ? 27.435 56.096  33.436 1.00 30.92 ? 1    MET   A CB   1 
ATOM   6     C  CG   . MET   A 1 1   ? 28.690 55.556  32.821 1.00 30.40 ? 1    MET   A CG   1 
ATOM   7     S  SD   . MET   A 1 1   ? 28.620 55.598  31.025 1.00 31.16 ? 1    MET   A SD   1 
ATOM   8     C  CE   . MET   A 1 1   ? 29.742 56.954  30.695 1.00 31.31 ? 1    MET   A CE   1 
ATOM   9     H  H1   . MET   A 1 1   ? 29.507 56.344  35.068 1.00 51.94 ? 1    MET   A H1   1 
ATOM   10    H  H2   . MET   A 1 1   ? 28.922 55.877  36.313 1.00 51.94 ? 1    MET   A H2   1 
ATOM   11    H  H3   . MET   A 1 1   ? 29.032 54.976  35.179 1.00 51.94 ? 1    MET   A H3   1 
ATOM   12    H  HA   . MET   A 1 1   ? 27.410 57.176  35.197 1.00 51.32 ? 1    MET   A HA   1 
ATOM   13    H  HB2  . MET   A 1 1   ? 26.695 55.506  33.223 1.00 37.11 ? 1    MET   A HB2  1 
ATOM   14    H  HB3  . MET   A 1 1   ? 27.232 56.959  33.043 1.00 37.11 ? 1    MET   A HB3  1 
ATOM   15    H  HG2  . MET   A 1 1   ? 29.450 56.074  33.128 1.00 36.48 ? 1    MET   A HG2  1 
ATOM   16    H  HG3  . MET   A 1 1   ? 28.830 54.643  33.119 1.00 36.48 ? 1    MET   A HG3  1 
ATOM   17    H  HE1  . MET   A 1 1   ? 29.805 57.096  29.738 1.00 37.57 ? 1    MET   A HE1  1 
ATOM   18    H  HE2  . MET   A 1 1   ? 29.409 57.760  31.120 1.00 37.57 ? 1    MET   A HE2  1 
ATOM   19    H  HE3  . MET   A 1 1   ? 30.620 56.741  31.049 1.00 37.57 ? 1    MET   A HE3  1 
ATOM   20    N  N    . TYR   A 1 2   ? 25.195 55.601  35.270 1.00 31.26 ? 2    TYR   A N    1 
ATOM   21    C  CA   . TYR   A 1 2   ? 24.112 54.729  35.800 1.00 23.48 ? 2    TYR   A CA   1 
ATOM   22    C  C    . TYR   A 1 2   ? 23.842 53.585  34.814 1.00 20.99 ? 2    TYR   A C    1 
ATOM   23    O  O    . TYR   A 1 2   ? 23.752 53.837  33.604 1.00 18.99 ? 2    TYR   A O    1 
ATOM   24    C  CB   . TYR   A 1 2   ? 22.845 55.537  36.087 1.00 24.56 ? 2    TYR   A CB   1 
ATOM   25    C  CG   . TYR   A 1 2   ? 23.012 56.604  37.137 1.00 26.31 ? 2    TYR   A CG   1 
ATOM   26    C  CD1  . TYR   A 1 2   ? 23.536 56.304  38.382 1.00 24.25 ? 2    TYR   A CD1  1 
ATOM   27    C  CD2  . TYR   A 1 2   ? 22.648 57.915  36.884 1.00 23.86 ? 2    TYR   A CD2  1 
ATOM   28    C  CE1  . TYR   A 1 2   ? 23.691 57.278  39.353 1.00 27.38 ? 2    TYR   A CE1  1 
ATOM   29    C  CE2  . TYR   A 1 2   ? 22.794 58.901  37.844 1.00 27.31 ? 2    TYR   A CE2  1 
ATOM   30    C  CZ   . TYR   A 1 2   ? 23.319 58.582  39.082 1.00 31.21 ? 2    TYR   A CZ   1 
ATOM   31    O  OH   . TYR   A 1 2   ? 23.467 59.558  40.038 1.00 33.84 ? 2    TYR   A OH   1 
ATOM   32    H  H    . TYR   A 1 2   ? 24.932 56.234  34.750 1.00 37.51 ? 2    TYR   A H    1 
ATOM   33    H  HA   . TYR   A 1 2   ? 24.399 54.346  36.644 1.00 28.18 ? 2    TYR   A HA   1 
ATOM   34    H  HB2  . TYR   A 1 2   ? 22.546 55.953  35.263 1.00 29.47 ? 2    TYR   A HB2  1 
ATOM   35    H  HB3  . TYR   A 1 2   ? 22.143 54.929  36.368 1.00 29.47 ? 2    TYR   A HB3  1 
ATOM   36    H  HD1  . TYR   A 1 2   ? 23.789 55.429  38.570 1.00 29.10 ? 2    TYR   A HD1  1 
ATOM   37    H  HD2  . TYR   A 1 2   ? 22.298 58.138  36.052 1.00 28.64 ? 2    TYR   A HD2  1 
ATOM   38    H  HE1  . TYR   A 1 2   ? 24.044 57.056  40.184 1.00 32.86 ? 2    TYR   A HE1  1 
ATOM   39    H  HE2  . TYR   A 1 2   ? 22.540 59.776  37.657 1.00 32.78 ? 2    TYR   A HE2  1 
ATOM   40    H  HH   . TYR   A 1 2   ? 23.202 60.294  39.731 1.00 40.61 ? 2    TYR   A HH   1 
ATOM   41    N  N    . GLY   A 1 3   ? 23.724 52.364  35.339 1.00 20.60 ? 3    GLY   A N    1 
ATOM   42    C  CA   . GLY   A 1 3   ? 23.481 51.227  34.476 1.00 19.36 ? 3    GLY   A CA   1 
ATOM   43    C  C    . GLY   A 1 3   ? 24.754 50.832  33.766 1.00 16.95 ? 3    GLY   A C    1 
ATOM   44    O  O    . GLY   A 1 3   ? 25.439 49.896  34.189 1.00 16.39 ? 3    GLY   A O    1 
ATOM   45    H  H    . GLY   A 1 3   ? 23.781 52.182  36.178 1.00 24.72 ? 3    GLY   A H    1 
ATOM   46    H  HA2  . GLY   A 1 3   ? 23.149 50.480  34.999 1.00 23.24 ? 3    GLY   A HA2  1 
ATOM   47    H  HA3  . GLY   A 1 3   ? 22.795 51.446  33.826 1.00 23.24 ? 3    GLY   A HA3  1 
ATOM   48    N  N    . TYR   A 1 4   ? 25.081 51.575  32.718 1.00 15.42 ? 4    TYR   A N    1 
ATOM   49    C  CA   . TYR   A 1 4   ? 26.384 51.356  32.061 1.00 17.33 ? 4    TYR   A CA   1 
ATOM   50    C  C    . TYR   A 1 4   ? 27.485 51.700  33.067 1.00 15.98 ? 4    TYR   A C    1 
ATOM   51    O  O    . TYR   A 1 4   ? 27.265 52.587  33.900 1.00 18.13 ? 4    TYR   A O    1 
ATOM   52    C  CB   . TYR   A 1 4   ? 26.499 52.250  30.829 1.00 17.60 ? 4    TYR   A CB   1 
ATOM   53    C  CG   . TYR   A 1 4   ? 25.325 52.215  29.884 1.00 17.60 ? 4    TYR   A CG   1 
ATOM   54    C  CD1  . TYR   A 1 4   ? 24.263 53.093  30.025 1.00 17.72 ? 4    TYR   A CD1  1 
ATOM   55    C  CD2  . TYR   A 1 4   ? 25.284 51.316  28.832 1.00 17.56 ? 4    TYR   A CD2  1 
ATOM   56    C  CE1  . TYR   A 1 4   ? 23.186 53.070  29.155 1.00 17.42 ? 4    TYR   A CE1  1 
ATOM   57    C  CE2  . TYR   A 1 4   ? 24.215 51.280  27.953 1.00 18.31 ? 4    TYR   A CE2  1 
ATOM   58    C  CZ   . TYR   A 1 4   ? 23.161 52.161  28.114 1.00 16.31 ? 4    TYR   A CZ   1 
ATOM   59    O  OH   . TYR   A 1 4   ? 22.100 52.125  27.244 1.00 17.79 ? 4    TYR   A OH   1 
ATOM   60    H  H    . TYR   A 1 4   ? 24.590 52.192  32.374 1.00 18.51 ? 4    TYR   A H    1 
ATOM   61    H  HA   . TYR   A 1 4   ? 26.469 50.433  31.776 1.00 20.80 ? 4    TYR   A HA   1 
ATOM   62    H  HB2  . TYR   A 1 4   ? 26.628 53.165  31.124 1.00 21.12 ? 4    TYR   A HB2  1 
ATOM   63    H  HB3  . TYR   A 1 4   ? 27.296 51.995  30.338 1.00 21.12 ? 4    TYR   A HB3  1 
ATOM   64    H  HD1  . TYR   A 1 4   ? 24.274 53.712  30.719 1.00 21.27 ? 4    TYR   A HD1  1 
ATOM   65    H  HD2  . TYR   A 1 4   ? 25.990 50.723  28.713 1.00 21.08 ? 4    TYR   A HD2  1 
ATOM   66    H  HE1  . TYR   A 1 4   ? 22.481 53.665  29.271 1.00 20.90 ? 4    TYR   A HE1  1 
ATOM   67    H  HE2  . TYR   A 1 4   ? 24.206 50.665  27.256 1.00 21.98 ? 4    TYR   A HE2  1 
ATOM   68    H  HH   . TYR   A 1 4   ? 22.077 51.378  26.861 1.00 21.36 ? 4    TYR   A HH   1 
ATOM   69    N  N    . ASP   A 1 5   ? 28.615 50.997  33.002 1.00 17.18 ? 5    ASP   A N    1 
ATOM   70    C  CA   . ASP   A 1 5   ? 29.770 51.305  33.883 1.00 17.74 ? 5    ASP   A CA   1 
ATOM   71    C  C    . ASP   A 1 5   ? 30.523 52.506  33.305 1.00 18.39 ? 5    ASP   A C    1 
ATOM   72    O  O    . ASP   A 1 5   ? 30.944 53.372  34.089 1.00 16.95 ? 5    ASP   A O    1 
ATOM   73    C  CB   . ASP   A 1 5   ? 30.729 50.121  33.970 1.00 15.41 ? 5    ASP   A CB   1 
ATOM   74    C  CG   . ASP   A 1 5   ? 30.238 48.971  34.830 1.00 15.58 ? 5    ASP   A CG   1 
ATOM   75    O  OD1  . ASP   A 1 5   ? 29.310 49.188  35.628 1.00 14.95 ? 5    ASP   A OD1  1 
ATOM   76    O  OD2  . ASP   A 1 5   ? 30.803 47.874  34.697 1.00 15.67 ? 5    ASP   A OD2  1 
ATOM   77    H  H    . ASP   A 1 5   ? 28.743 50.340  32.462 1.00 20.62 ? 5    ASP   A H    1 
ATOM   78    H  HA   . ASP   A 1 5   ? 29.436 51.499  34.773 1.00 21.29 ? 5    ASP   A HA   1 
ATOM   79    H  HB2  . ASP   A 1 5   ? 30.897 49.790  33.074 1.00 18.49 ? 5    ASP   A HB2  1 
ATOM   80    H  HB3  . ASP   A 1 5   ? 31.578 50.433  34.321 1.00 18.49 ? 5    ASP   A HB3  1 
ATOM   81    N  N    . GLY   A 1 6   ? 30.714 52.520  31.987 1.00 17.22 ? 6    GLY   A N    1 
ATOM   82    C  CA   . GLY   A 1 6   ? 31.402 53.649  31.329 1.00 19.44 ? 6    GLY   A CA   1 
ATOM   83    C  C    . GLY   A 1 6   ? 32.782 53.293  30.809 1.00 16.80 ? 6    GLY   A C    1 
ATOM   84    O  O    . GLY   A 1 6   ? 33.465 54.202  30.314 1.00 15.72 ? 6    GLY   A O    1 
ATOM   85    H  H    . GLY   A 1 6   ? 30.458 51.895  31.454 1.00 20.67 ? 6    GLY   A H    1 
ATOM   86    H  HA2  . GLY   A 1 6   ? 30.857 53.965  30.591 1.00 23.33 ? 6    GLY   A HA2  1 
ATOM   87    H  HA3  . GLY   A 1 6   ? 31.480 54.383  31.959 1.00 23.33 ? 6    GLY   A HA3  1 
ATOM   88    N  N    . LYS   A 1 7   ? 33.180 52.020  30.892 1.00 16.85 ? 7    LYS   A N    1 
ATOM   89    C  CA   . LYS   A 1 7   ? 34.566 51.657  30.493 1.00 16.43 ? 7    LYS   A CA   1 
ATOM   90    C  C    . LYS   A 1 7   ? 34.587 50.416  29.595 1.00 15.45 ? 7    LYS   A C    1 
ATOM   91    O  O    . LYS   A 1 7   ? 33.774 49.501  29.824 1.00 14.05 ? 7    LYS   A O    1 
ATOM   92    C  CB   . LYS   A 1 7   ? 35.439 51.430  31.732 1.00 15.97 ? 7    LYS   A CB   1 
ATOM   93    C  CG   . LYS   A 1 7   ? 35.569 52.628  32.663 1.00 18.27 ? 7    LYS   A CG   1 
ATOM   94    C  CD   . LYS   A 1 7   ? 36.393 53.751  32.072 1.00 20.74 ? 7    LYS   A CD   1 
ATOM   95    C  CE   . LYS   A 1 7   ? 36.237 55.057  32.821 1.00 21.53 ? 7    LYS   A CE   1 
ATOM   96    N  NZ   . LYS   A 1 7   ? 37.332 56.004  32.505 1.00 25.57 ? 7    LYS   A NZ   1 
ATOM   97    H  H    . LYS   A 1 7   ? 32.691 51.367  31.165 1.00 20.23 ? 7    LYS   A H    1 
ATOM   98    H  HA   . LYS   A 1 7   ? 34.928 52.399  29.983 1.00 19.72 ? 7    LYS   A HA   1 
ATOM   99    H  HB2  . LYS   A 1 7   ? 35.073 50.686  32.235 1.00 19.17 ? 7    LYS   A HB2  1 
ATOM   100   H  HB3  . LYS   A 1 7   ? 36.326 51.167  31.441 1.00 19.17 ? 7    LYS   A HB3  1 
ATOM   101   H  HG2  . LYS   A 1 7   ? 34.684 52.962  32.878 1.00 21.93 ? 7    LYS   A HG2  1 
ATOM   102   H  HG3  . LYS   A 1 7   ? 35.974 52.341  33.496 1.00 21.93 ? 7    LYS   A HG3  1 
ATOM   103   H  HD2  . LYS   A 1 7   ? 37.328 53.494  32.072 1.00 24.89 ? 7    LYS   A HD2  1 
ATOM   104   H  HD3  . LYS   A 1 7   ? 36.135 53.882  31.146 1.00 24.89 ? 7    LYS   A HD3  1 
ATOM   105   H  HE2  . LYS   A 1 7   ? 35.384 55.460  32.594 1.00 25.84 ? 7    LYS   A HE2  1 
ATOM   106   H  HE3  . LYS   A 1 7   ? 36.224 54.884  33.775 1.00 25.84 ? 7    LYS   A HE3  1 
ATOM   107   H  HZ1  . LYS   A 1 7   ? 37.287 56.704  33.053 1.00 30.68 ? 7    LYS   A HZ1  1 
ATOM   108   H  HZ2  . LYS   A 1 7   ? 38.116 55.597  32.609 1.00 30.68 ? 7    LYS   A HZ2  1 
ATOM   109   H  HZ3  . LYS   A 1 7   ? 37.252 56.281  31.663 1.00 30.68 ? 7    LYS   A HZ3  1 
ATOM   110   N  N    . VAL   A 1 8   ? 35.508 50.393  28.636 1.00 14.22 ? 8    VAL   A N    1 
ATOM   111   C  CA   . VAL   A 1 8   ? 35.644 49.241  27.705 1.00 14.81 ? 8    VAL   A CA   1 
ATOM   112   C  C    . VAL   A 1 8   ? 37.077 48.720  27.812 1.00 18.28 ? 8    VAL   A C    1 
ATOM   113   O  O    . VAL   A 1 8   ? 38.001 49.546  27.860 1.00 16.60 ? 8    VAL   A O    1 
ATOM   114   C  CB   . VAL   A 1 8   ? 35.326 49.642  26.253 1.00 16.14 ? 8    VAL   A CB   1 
ATOM   115   C  CG1  . VAL   A 1 8   ? 35.652 48.528  25.270 1.00 15.96 ? 8    VAL   A CG1  1 
ATOM   116   C  CG2  . VAL   A 1 8   ? 33.887 50.105  26.094 1.00 14.39 ? 8    VAL   A CG2  1 
ATOM   117   H  H    . VAL   A 1 8   ? 36.070 51.029  28.497 1.00 17.07 ? 8    VAL   A H    1 
ATOM   118   H  HA   . VAL   A 1 8   ? 35.008 48.551  27.951 1.00 17.77 ? 8    VAL   A HA   1 
ATOM   119   H  HB   . VAL   A 1 8   ? 35.901 50.394  26.043 1.00 19.37 ? 8    VAL   A HB   1 
ATOM   120   H  HG11 . VAL   A 1 8   ? 35.439 48.818  24.369 1.00 19.16 ? 8    VAL   A HG11 1 
ATOM   121   H  HG12 . VAL   A 1 8   ? 36.596 48.314  25.325 1.00 19.16 ? 8    VAL   A HG12 1 
ATOM   122   H  HG13 . VAL   A 1 8   ? 35.129 47.741  25.488 1.00 19.16 ? 8    VAL   A HG13 1 
ATOM   123   H  HG21 . VAL   A 1 8   ? 33.725 50.348  25.169 1.00 17.27 ? 8    VAL   A HG21 1 
ATOM   124   H  HG22 . VAL   A 1 8   ? 33.286 49.388  26.349 1.00 17.27 ? 8    VAL   A HG22 1 
ATOM   125   H  HG23 . VAL   A 1 8   ? 33.730 50.875  26.662 1.00 17.27 ? 8    VAL   A HG23 1 
ATOM   126   N  N    . LEU   A 1 9   ? 37.239 47.398  27.837 1.00 13.57 ? 9    LEU   A N    1 
ATOM   127   C  CA   . LEU   A 1 9   ? 38.588 46.790  27.951 1.00 13.13 ? 9    LEU   A CA   1 
ATOM   128   C  C    . LEU   A 1 9   ? 39.030 46.313  26.565 1.00 13.38 ? 9    LEU   A C    1 
ATOM   129   O  O    . LEU   A 1 9   ? 38.400 45.389  26.038 1.00 13.86 ? 9    LEU   A O    1 
ATOM   130   C  CB   . LEU   A 1 9   ? 38.518 45.635  28.958 1.00 13.99 ? 9    LEU   A CB   1 
ATOM   131   C  CG   . LEU   A 1 9   ? 39.792 44.807  29.113 1.00 15.97 ? 9    LEU   A CG   1 
ATOM   132   C  CD1  . LEU   A 1 9   ? 40.974 45.692  29.475 1.00 16.20 ? 9    LEU   A CD1  1 
ATOM   133   C  CD2  . LEU   A 1 9   ? 39.598 43.725  30.163 1.00 18.64 ? 9    LEU   A CD2  1 
ATOM   134   H  H    . LEU   A 1 9   ? 36.594 46.831  27.790 1.00 16.29 ? 9    LEU   A H    1 
ATOM   135   H  HA   . LEU   A 1 9   ? 39.241 47.432  28.270 1.00 15.75 ? 9    LEU   A HA   1 
ATOM   136   H  HB2  . LEU   A 1 9   ? 38.282 45.999  29.826 1.00 16.80 ? 9    LEU   A HB2  1 
ATOM   137   H  HB3  . LEU   A 1 9   ? 37.797 45.042  28.694 1.00 16.80 ? 9    LEU   A HB3  1 
ATOM   138   H  HG   . LEU   A 1 9   ? 39.982 44.383  28.262 1.00 19.17 ? 9    LEU   A HG   1 
ATOM   139   H  HD11 . LEU   A 1 9   ? 41.771 45.146  29.568 1.00 19.44 ? 9    LEU   A HD11 1 
ATOM   140   H  HD12 . LEU   A 1 9   ? 41.113 46.349  28.775 1.00 19.44 ? 9    LEU   A HD12 1 
ATOM   141   H  HD13 . LEU   A 1 9   ? 40.794 46.146  30.313 1.00 19.44 ? 9    LEU   A HD13 1 
ATOM   142   H  HD21 . LEU   A 1 9   ? 40.414 43.208  30.250 1.00 22.37 ? 9    LEU   A HD21 1 
ATOM   143   H  HD22 . LEU   A 1 9   ? 39.383 44.136  31.015 1.00 22.37 ? 9    LEU   A HD22 1 
ATOM   144   H  HD23 . LEU   A 1 9   ? 38.872 43.140  29.895 1.00 22.37 ? 9    LEU   A HD23 1 
ATOM   145   N  N    . ARG   A 1 10  ? 40.062 46.946  26.001 1.00 12.41 ? 10   ARG   A N    1 
ATOM   146   C  CA   . ARG   A 1 10  ? 40.577 46.568  24.655 1.00 13.60 ? 10   ARG   A CA   1 
ATOM   147   C  C    . ARG   A 1 10  ? 41.863 45.761  24.832 1.00 14.82 ? 10   ARG   A C    1 
ATOM   148   O  O    . ARG   A 1 10  ? 42.834 46.310  25.371 1.00 13.91 ? 10   ARG   A O    1 
ATOM   149   C  CB   . ARG   A 1 10  ? 40.794 47.793  23.757 1.00 16.87 ? 10   ARG   A CB   1 
ATOM   150   C  CG   . ARG   A 1 10  ? 41.158 47.443  22.322 1.00 15.43 ? 10   ARG   A CG   1 
ATOM   151   C  CD   . ARG   A 1 10  ? 41.273 48.652  21.414 1.00 19.38 ? 10   ARG   A CD   1 
ATOM   152   N  NE   . ARG   A 1 10  ? 40.022 49.385  21.288 1.00 15.72 ? 10   ARG   A NE   1 
ATOM   153   C  CZ   . ARG   A 1 10  ? 39.080 49.124  20.390 1.00 16.49 ? 10   ARG   A CZ   1 
ATOM   154   N  NH1  . ARG   A 1 10  ? 39.211 48.100  19.566 1.00 16.94 ? 10   ARG   A NH1  1 
ATOM   155   N  NH2  . ARG   A 1 10  ? 38.007 49.892  20.319 1.00 17.61 ? 10   ARG   A NH2  1 
ATOM   156   H  H    . ARG   A 1 10  ? 40.485 47.597  26.371 1.00 14.90 ? 10   ARG   A H    1 
ATOM   157   H  HA   . ARG   A 1 10  ? 39.914 46.023  24.203 1.00 16.32 ? 10   ARG   A HA   1 
ATOM   158   H  HB2  . ARG   A 1 10  ? 39.986 48.330  23.755 1.00 20.24 ? 10   ARG   A HB2  1 
ATOM   159   H  HB3  . ARG   A 1 10  ? 41.498 48.341  24.136 1.00 20.24 ? 10   ARG   A HB3  1 
ATOM   160   H  HG2  . ARG   A 1 10  ? 42.001 46.963  22.318 1.00 18.52 ? 10   ARG   A HG2  1 
ATOM   161   H  HG3  . ARG   A 1 10  ? 40.487 46.841  21.964 1.00 18.52 ? 10   ARG   A HG3  1 
ATOM   162   H  HD2  . ARG   A 1 10  ? 41.958 49.246  21.759 1.00 23.26 ? 10   ARG   A HD2  1 
ATOM   163   H  HD3  . ARG   A 1 10  ? 41.564 48.364  20.535 1.00 23.26 ? 10   ARG   A HD3  1 
ATOM   164   H  HE   . ARG   A 1 10  ? 39.883 50.034  21.835 1.00 18.87 ? 10   ARG   A HE   1 
ATOM   165   H  HH11 . ARG   A 1 10  ? 39.909 47.599  19.610 1.00 20.33 ? 10   ARG   A HH11 1 
ATOM   166   H  HH12 . ARG   A 1 10  ? 38.599 47.934  18.986 1.00 20.33 ? 10   ARG   A HH12 1 
ATOM   167   H  HH21 . ARG   A 1 10  ? 37.920 50.560  20.854 1.00 21.14 ? 10   ARG   A HH21 1 
ATOM   168   H  HH22 . ARG   A 1 10  ? 37.396 49.724  19.738 1.00 21.14 ? 10   ARG   A HH22 1 
ATOM   169   N  N    . ILE   A 1 11  ? 41.863 44.519  24.364 1.00 15.38 ? 11   ILE   A N    1 
ATOM   170   C  CA   . ILE   A 1 11  ? 42.984 43.614  24.570 1.00 14.51 ? 11   ILE   A CA   1 
ATOM   171   C  C    . ILE   A 1 11  ? 43.492 43.173  23.207 1.00 13.36 ? 11   ILE   A C    1 
ATOM   172   O  O    . ILE   A 1 11  ? 42.767 42.505  22.457 1.00 16.07 ? 11   ILE   A O    1 
ATOM   173   C  CB   . ILE   A 1 11  ? 42.580 42.403  25.424 1.00 14.33 ? 11   ILE   A CB   1 
ATOM   174   C  CG1  . ILE   A 1 11  ? 42.131 42.871  26.813 1.00 16.14 ? 11   ILE   A CG1  1 
ATOM   175   C  CG2  . ILE   A 1 11  ? 43.739 41.412  25.533 1.00 14.64 ? 11   ILE   A CG2  1 
ATOM   176   C  CD1  . ILE   A 1 11  ? 41.626 41.769  27.706 1.00 17.88 ? 11   ILE   A CD1  1 
ATOM   177   H  H    . ILE   A 1 11  ? 41.212 44.177  23.918 1.00 18.46 ? 11   ILE   A H    1 
ATOM   178   H  HA   . ILE   A 1 11  ? 43.687 44.073  25.055 1.00 17.42 ? 11   ILE   A HA   1 
ATOM   179   H  HB   . ILE   A 1 11  ? 41.838 41.949  24.995 1.00 17.20 ? 11   ILE   A HB   1 
ATOM   180   H  HG12 . ILE   A 1 11  ? 42.876 43.311  27.251 1.00 19.37 ? 11   ILE   A HG12 1 
ATOM   181   H  HG13 . ILE   A 1 11  ? 41.431 43.534  26.708 1.00 19.37 ? 11   ILE   A HG13 1 
ATOM   182   H  HG21 . ILE   A 1 11  ? 43.467 40.655  26.075 1.00 17.57 ? 11   ILE   A HG21 1 
ATOM   183   H  HG22 . ILE   A 1 11  ? 43.986 41.104  24.647 1.00 17.57 ? 11   ILE   A HG22 1 
ATOM   184   H  HG23 . ILE   A 1 11  ? 44.500 41.848  25.947 1.00 17.57 ? 11   ILE   A HG23 1 
ATOM   185   H  HD11 . ILE   A 1 11  ? 41.362 42.141  28.562 1.00 21.46 ? 11   ILE   A HD11 1 
ATOM   186   H  HD12 . ILE   A 1 11  ? 40.861 41.341  27.291 1.00 21.46 ? 11   ILE   A HD12 1 
ATOM   187   H  HD13 . ILE   A 1 11  ? 42.329 41.114  27.841 1.00 21.46 ? 11   ILE   A HD13 1 
ATOM   188   N  N    . ASN   A 1 12  ? 44.728 43.542  22.880 1.00 13.69 ? 12   ASN   A N    1 
ATOM   189   C  CA   . ASN   A 1 12  ? 45.345 43.117  21.630 1.00 14.51 ? 12   ASN   A CA   1 
ATOM   190   C  C    . ASN   A 1 12  ? 46.309 41.976  21.918 1.00 16.83 ? 12   ASN   A C    1 
ATOM   191   O  O    . ASN   A 1 12  ? 47.335 42.176  22.579 1.00 14.53 ? 12   ASN   A O    1 
ATOM   192   C  CB   . ASN   A 1 12  ? 46.077 44.261  20.931 1.00 17.05 ? 12   ASN   A CB   1 
ATOM   193   C  CG   . ASN   A 1 12  ? 46.576 43.855  19.561 1.00 19.33 ? 12   ASN   A CG   1 
ATOM   194   O  OD1  . ASN   A 1 12  ? 47.516 43.069  19.444 1.00 18.41 ? 12   ASN   A OD1  1 
ATOM   195   N  ND2  . ASN   A 1 12  ? 45.918 44.349  18.513 1.00 17.66 ? 12   ASN   A ND2  1 
ATOM   196   H  H    . ASN   A 1 12  ? 45.227 44.041  23.372 1.00 16.43 ? 12   ASN   A H    1 
ATOM   197   H  HA   . ASN   A 1 12  ? 44.643 42.821  21.030 1.00 17.41 ? 12   ASN   A HA   1 
ATOM   198   H  HB2  . ASN   A 1 12  ? 45.481 45.022  20.846 1.00 20.46 ? 12   ASN   A HB2  1 
ATOM   199   H  HB3  . ASN   A 1 12  ? 46.826 44.547  21.477 1.00 20.46 ? 12   ASN   A HB3  1 
ATOM   200   H  HD21 . ASN   A 1 12  ? 46.146 44.120  17.716 1.00 21.20 ? 12   ASN   A HD21 1 
ATOM   201   H  HD22 . ASN   A 1 12  ? 45.266 44.896  18.634 1.00 21.20 ? 12   ASN   A HD22 1 
ATOM   202   N  N    . LEU   A 1 13  ? 45.995 40.787  21.398 1.00 15.54 ? 13   LEU   A N    1 
ATOM   203   C  CA   . LEU   A 1 13  ? 46.757 39.597  21.767 1.00 16.00 ? 13   LEU   A CA   1 
ATOM   204   C  C    . LEU   A 1 13  ? 48.078 39.479  21.023 1.00 17.70 ? 13   LEU   A C    1 
ATOM   205   O  O    . LEU   A 1 13  ? 48.962 38.746  21.483 1.00 16.48 ? 13   LEU   A O    1 
ATOM   206   C  CB   . LEU   A 1 13  ? 45.928 38.337  21.545 1.00 14.54 ? 13   LEU   A CB   1 
ATOM   207   C  CG   . LEU   A 1 13  ? 44.748 38.166  22.510 1.00 14.08 ? 13   LEU   A CG   1 
ATOM   208   C  CD1  . LEU   A 1 13  ? 43.932 36.949  22.131 1.00 16.96 ? 13   LEU   A CD1  1 
ATOM   209   C  CD2  . LEU   A 1 13  ? 45.231 38.079  23.955 1.00 14.36 ? 13   LEU   A CD2  1 
ATOM   210   H  H    . LEU   A 1 13  ? 45.355 40.651  20.840 1.00 18.65 ? 13   LEU   A H    1 
ATOM   211   H  HA   . LEU   A 1 13  ? 46.966 39.692  22.709 1.00 19.20 ? 13   LEU   A HA   1 
ATOM   212   H  HB2  . LEU   A 1 13  ? 45.588 38.344  20.636 1.00 17.45 ? 13   LEU   A HB2  1 
ATOM   213   H  HB3  . LEU   A 1 13  ? 46.509 37.564  21.624 1.00 17.45 ? 13   LEU   A HB3  1 
ATOM   214   H  HG   . LEU   A 1 13  ? 44.178 38.948  22.440 1.00 16.89 ? 13   LEU   A HG   1 
ATOM   215   H  HD11 . LEU   A 1 13  ? 43.190 36.852  22.748 1.00 20.36 ? 13   LEU   A HD11 1 
ATOM   216   H  HD12 . LEU   A 1 13  ? 43.591 37.056  21.229 1.00 20.36 ? 13   LEU   A HD12 1 
ATOM   217   H  HD13 . LEU   A 1 13  ? 44.492 36.158  22.172 1.00 20.36 ? 13   LEU   A HD13 1 
ATOM   218   H  HD21 . LEU   A 1 13  ? 44.469 37.971  24.545 1.00 17.23 ? 13   LEU   A HD21 1 
ATOM   219   H  HD22 . LEU   A 1 13  ? 45.825 37.318  24.053 1.00 17.23 ? 13   LEU   A HD22 1 
ATOM   220   H  HD23 . LEU   A 1 13  ? 45.707 38.892  24.187 1.00 17.23 ? 13   LEU   A HD23 1 
ATOM   221   N  N    . LYS   A 1 14  ? 48.232 40.208  19.921 1.00 16.88 ? 14   LYS   A N    1 
ATOM   222   C  CA   . LYS   A 1 14  ? 49.535 40.196  19.207 1.00 17.67 ? 14   LYS   A CA   1 
ATOM   223   C  C    . LYS   A 1 14  ? 50.527 41.069  19.981 1.00 19.33 ? 14   LYS   A C    1 
ATOM   224   O  O    . LYS   A 1 14  ? 51.661 40.618  20.199 1.00 19.36 ? 14   LYS   A O    1 
ATOM   225   C  CB   . LYS   A 1 14  ? 49.373 40.694  17.769 1.00 20.54 ? 14   LYS   A CB   1 
ATOM   226   C  CG   . LYS   A 1 14  ? 50.669 40.819  16.980 1.00 22.59 ? 14   LYS   A CG   1 
ATOM   227   C  CD   . LYS   A 1 14  ? 50.453 41.202  15.533 1.00 23.43 ? 14   LYS   A CD   1 
ATOM   228   C  CE   . LYS   A 1 14  ? 51.685 41.799  14.887 1.00 31.15 ? 14   LYS   A CE   1 
ATOM   229   N  NZ   . LYS   A 1 14  ? 51.357 43.017  14.109 1.00 39.31 ? 14   LYS   A NZ   1 
ATOM   230   H  H    . LYS   A 1 14  ? 47.624 40.705  19.570 1.00 20.26 ? 14   LYS   A H    1 
ATOM   231   H  HA   . LYS   A 1 14  ? 49.872 39.288  19.160 1.00 21.21 ? 14   LYS   A HA   1 
ATOM   232   H  HB2  . LYS   A 1 14  ? 48.780 40.089  17.297 1.00 24.65 ? 14   LYS   A HB2  1 
ATOM   233   H  HB3  . LYS   A 1 14  ? 48.937 41.560  17.788 1.00 24.65 ? 14   LYS   A HB3  1 
ATOM   234   H  HG2  . LYS   A 1 14  ? 51.235 41.483  17.403 1.00 27.11 ? 14   LYS   A HG2  1 
ATOM   235   H  HG3  . LYS   A 1 14  ? 51.146 39.975  17.017 1.00 27.11 ? 14   LYS   A HG3  1 
ATOM   236   H  HD2  . LYS   A 1 14  ? 50.181 40.416  15.033 1.00 28.12 ? 14   LYS   A HD2  1 
ATOM   237   H  HD3  . LYS   A 1 14  ? 49.724 41.840  15.478 1.00 28.12 ? 14   LYS   A HD3  1 
ATOM   238   H  HE2  . LYS   A 1 14  ? 52.337 42.017  15.572 1.00 37.38 ? 14   LYS   A HE2  1 
ATOM   239   H  HE3  . LYS   A 1 14  ? 52.096 41.142  14.303 1.00 37.38 ? 14   LYS   A HE3  1 
ATOM   240   H  HZ1  . LYS   A 1 14  ? 52.099 43.344  13.742 1.00 47.17 ? 14   LYS   A HZ1  1 
ATOM   241   H  HZ2  . LYS   A 1 14  ? 50.775 42.812  13.468 1.00 47.17 ? 14   LYS   A HZ2  1 
ATOM   242   H  HZ3  . LYS   A 1 14  ? 51.000 43.627  14.649 1.00 47.17 ? 14   LYS   A HZ3  1 
ATOM   243   N  N    . GLU   A 1 15  ? 50.097 42.265  20.386 1.00 20.57 ? 15   GLU   A N    1 
ATOM   244   C  CA   . GLU   A 1 15  ? 50.986 43.201  21.127 1.00 20.26 ? 15   GLU   A CA   1 
ATOM   245   C  C    . GLU   A 1 15  ? 50.954 42.880  22.625 1.00 18.73 ? 15   GLU   A C    1 
ATOM   246   O  O    . GLU   A 1 15  ? 51.789 43.431  23.354 1.00 19.35 ? 15   GLU   A O    1 
ATOM   247   C  CB   . GLU   A 1 15  ? 50.541 44.642  20.877 1.00 18.42 ? 15   GLU   A CB   1 
ATOM   248   C  CG   . GLU   A 1 15  ? 50.464 45.007  19.408 1.00 21.59 ? 15   GLU   A CG   1 
ATOM   249   C  CD   . GLU   A 1 15  ? 51.786 44.897  18.671 1.00 25.37 ? 15   GLU   A CD   1 
ATOM   250   O  OE1  . GLU   A 1 15  ? 52.837 45.036  19.326 1.00 24.62 ? 15   GLU   A OE1  1 
ATOM   251   O  OE2  . GLU   A 1 15  ? 51.761 44.675  17.447 1.00 30.02 ? 15   GLU   A OE2  1 
ATOM   252   H  H    . GLU   A 1 15  ? 49.302 42.562  20.249 1.00 24.69 ? 15   GLU   A H    1 
ATOM   253   H  HA   . GLU   A 1 15  ? 51.897 43.097  20.810 1.00 24.32 ? 15   GLU   A HA   1 
ATOM   254   H  HB2  . GLU   A 1 15  ? 49.671 44.779  21.283 1.00 22.10 ? 15   GLU   A HB2  1 
ATOM   255   H  HB3  . GLU   A 1 15  ? 51.158 45.245  21.320 1.00 22.10 ? 15   GLU   A HB3  1 
ATOM   256   H  HG2  . GLU   A 1 15  ? 49.815 44.431  18.975 1.00 25.91 ? 15   GLU   A HG2  1 
ATOM   257   H  HG3  . GLU   A 1 15  ? 50.135 45.916  19.327 1.00 25.91 ? 15   GLU   A HG3  1 
ATOM   258   N  N    . ARG   A 1 16  ? 50.015 42.037  23.059 1.00 16.79 ? 16   ARG   A N    1 
ATOM   259   C  CA   . ARG   A 1 16  ? 49.867 41.677  24.496 1.00 15.79 ? 16   ARG   A CA   1 
ATOM   260   C  C    . ARG   A 1 16  ? 49.642 42.946  25.323 1.00 18.07 ? 16   ARG   A C    1 
ATOM   261   O  O    . ARG   A 1 16  ? 50.314 43.111  26.352 1.00 16.80 ? 16   ARG   A O    1 
ATOM   262   C  CB   . ARG   A 1 16  ? 51.053 40.834  24.974 1.00 22.14 ? 16   ARG   A CB   1 
ATOM   263   C  CG   . ARG   A 1 16  ? 51.211 39.525  24.212 1.00 22.91 ? 16   ARG   A CG   1 
ATOM   264   C  CD   . ARG   A 1 16  ? 51.590 38.345  25.086 1.00 27.37 ? 16   ARG   A CD   1 
ATOM   265   N  NE   . ARG   A 1 16  ? 51.743 37.112  24.327 1.00 26.08 ? 16   ARG   A NE   1 
ATOM   266   C  CZ   . ARG   A 1 16  ? 51.804 35.900  24.866 1.00 29.32 ? 16   ARG   A CZ   1 
ATOM   267   N  NH1  . ARG   A 1 16  ? 51.838 35.765  26.179 1.00 30.70 ? 16   ARG   A NH1  1 
ATOM   268   N  NH2  . ARG   A 1 16  ? 51.830 34.828  24.093 1.00 29.23 ? 16   ARG   A NH2  1 
ATOM   269   H  H    . ARG   A 1 16  ? 49.444 41.654  22.542 1.00 20.15 ? 16   ARG   A H    1 
ATOM   270   H  HA   . ARG   A 1 16  ? 49.084 41.117  24.618 1.00 18.95 ? 16   ARG   A HA   1 
ATOM   271   H  HB2  . ARG   A 1 16  ? 51.867 41.353  24.884 1.00 26.57 ? 16   ARG   A HB2  1 
ATOM   272   H  HB3  . ARG   A 1 16  ? 50.943 40.640  25.918 1.00 26.57 ? 16   ARG   A HB3  1 
ATOM   273   H  HG2  . ARG   A 1 16  ? 50.379 39.324  23.756 1.00 27.49 ? 16   ARG   A HG2  1 
ATOM   274   H  HG3  . ARG   A 1 16  ? 51.889 39.640  23.527 1.00 27.49 ? 16   ARG   A HG3  1 
ATOM   275   H  HD2  . ARG   A 1 16  ? 52.420 38.542  25.547 1.00 32.85 ? 16   ARG   A HD2  1 
ATOM   276   H  HD3  . ARG   A 1 16  ? 50.910 38.220  25.767 1.00 32.85 ? 16   ARG   A HD3  1 
ATOM   277   H  HE   . ARG   A 1 16  ? 51.798 37.173  23.471 1.00 31.31 ? 16   ARG   A HE   1 
ATOM   278   H  HH11 . ARG   A 1 16  ? 51.821 36.461  26.683 1.00 36.84 ? 16   ARG   A HH11 1 
ATOM   279   H  HH12 . ARG   A 1 16  ? 51.877 34.981  26.530 1.00 36.84 ? 16   ARG   A HH12 1 
ATOM   280   H  HH21 . ARG   A 1 16  ? 51.807 34.914  23.238 1.00 35.08 ? 16   ARG   A HH21 1 
ATOM   281   H  HH22 . ARG   A 1 16  ? 51.870 34.045  24.445 1.00 35.08 ? 16   ARG   A HH22 1 
ATOM   282   N  N    . THR   A 1 17  ? 48.692 43.779  24.897 1.00 17.41 ? 17   THR   A N    1 
ATOM   283   C  CA   . THR   A 1 17  ? 48.361 45.016  25.643 1.00 15.99 ? 17   THR   A CA   1 
ATOM   284   C  C    . THR   A 1 17  ? 46.928 44.940  26.171 1.00 17.04 ? 17   THR   A C    1 
ATOM   285   O  O    . THR   A 1 17  ? 46.073 44.379  25.468 1.00 14.88 ? 17   THR   A O    1 
ATOM   286   C  CB   . THR   A 1 17  ? 48.519 46.250  24.747 1.00 15.50 ? 17   THR   A CB   1 
ATOM   287   O  OG1  . THR   A 1 17  ? 47.679 46.090  23.604 1.00 19.01 ? 17   THR   A OG1  1 
ATOM   288   C  CG2  . THR   A 1 17  ? 49.949 46.471  24.305 1.00 18.91 ? 17   THR   A CG2  1 
ATOM   289   H  H    . THR   A 1 17  ? 48.226 43.655  24.185 1.00 20.90 ? 17   THR   A H    1 
ATOM   290   H  HA   . THR   A 1 17  ? 48.975 45.096  26.390 1.00 19.19 ? 17   THR   A HA   1 
ATOM   291   H  HB   . THR   A 1 17  ? 48.262 47.031  25.262 1.00 18.60 ? 17   THR   A HB   1 
ATOM   292   H  HG1  . THR   A 1 17  ? 47.912 46.632  23.006 1.00 22.82 ? 17   THR   A HG1  1 
ATOM   293   H  HG21 . THR   A 1 17  ? 49.996 47.260  23.743 1.00 22.70 ? 17   THR   A HG21 1 
ATOM   294   H  HG22 . THR   A 1 17  ? 50.513 46.596  25.084 1.00 22.70 ? 17   THR   A HG22 1 
ATOM   295   H  HG23 . THR   A 1 17  ? 50.256 45.699  23.804 1.00 22.70 ? 17   THR   A HG23 1 
ATOM   296   N  N    . CYS   A 1 18  ? 46.693 45.475  27.364 1.00 14.78 ? 18   CYS   A N    1 
ATOM   297   C  CA   . CYS   A 1 18  ? 45.327 45.532  27.936 1.00 17.13 ? 18   CYS   A CA   1 
ATOM   298   C  C    . CYS   A 1 18  ? 45.067 46.999  28.271 1.00 16.57 ? 18   CYS   A C    1 
ATOM   299   O  O    . CYS   A 1 18  ? 45.742 47.519  29.174 1.00 18.81 ? 18   CYS   A O    1 
ATOM   300   C  CB   . CYS   A 1 18  ? 45.226 44.665  29.183 1.00 19.85 ? 18   CYS   A CB   1 
ATOM   301   S  SG   . CYS   A 1 18  ? 45.616 42.923  28.870 1.00 17.98 ? 18   CYS   A SG   1 
ATOM   302   H  H    . CYS   A 1 18  ? 47.303 45.813  27.867 1.00 17.74 ? 18   CYS   A H    1 
ATOM   303   H  HA   . CYS   A 1 18  ? 44.669 45.193  27.309 1.00 20.56 ? 18   CYS   A HA   1 
ATOM   304   H  HB2  . CYS   A 1 18  ? 45.829 45.010  29.860 1.00 23.82 ? 18   CYS   A HB2  1 
ATOM   305   H  HB3  . CYS   A 1 18  ? 44.328 44.730  29.544 1.00 23.82 ? 18   CYS   A HB3  1 
ATOM   306   H  HG   . CYS   A 1 18  ? 45.889 42.776  27.711 1.00 21.58 ? 18   CYS   A HG   1 
ATOM   307   N  N    . LYS   A 1 19  ? 44.139 47.644  27.561 1.00 12.24 ? 19   LYS   A N    1 
ATOM   308   C  CA   . LYS   A 1 19  ? 43.959 49.102  27.772 1.00 14.28 ? 19   LYS   A CA   1 
ATOM   309   C  C    . LYS   A 1 19  ? 42.505 49.446  28.099 1.00 15.20 ? 19   LYS   A C    1 
ATOM   310   O  O    . LYS   A 1 19  ? 41.605 48.739  27.613 1.00 16.01 ? 19   LYS   A O    1 
ATOM   311   C  CB   . LYS   A 1 19  ? 44.424 49.845  26.519 1.00 16.73 ? 19   LYS   A CB   1 
ATOM   312   C  CG   . LYS   A 1 19  ? 45.925 49.800  26.273 1.00 20.48 ? 19   LYS   A CG   1 
ATOM   313   C  CD   . LYS   A 1 19  ? 46.370 50.624  25.086 1.00 21.48 ? 19   LYS   A CD   1 
ATOM   314   C  CE   . LYS   A 1 19  ? 47.871 50.613  24.893 1.00 20.82 ? 19   LYS   A CE   1 
ATOM   315   N  NZ   . LYS   A 1 19  ? 48.311 51.670  23.954 1.00 21.04 ? 19   LYS   A NZ   1 
ATOM   316   H  H    . LYS   A 1 19  ? 43.621 47.285  26.976 1.00 14.69 ? 19   LYS   A H    1 
ATOM   317   H  HA   . LYS   A 1 19  ? 44.493 49.378  28.533 1.00 17.14 ? 19   LYS   A HA   1 
ATOM   318   H  HB2  . LYS   A 1 19  ? 43.971 49.469  25.748 1.00 20.08 ? 19   LYS   A HB2  1 
ATOM   319   H  HB3  . LYS   A 1 19  ? 44.147 50.772  26.586 1.00 20.08 ? 19   LYS   A HB3  1 
ATOM   320   H  HG2  . LYS   A 1 19  ? 46.385 50.116  27.067 1.00 24.58 ? 19   LYS   A HG2  1 
ATOM   321   H  HG3  . LYS   A 1 19  ? 46.195 48.878  26.137 1.00 24.58 ? 19   LYS   A HG3  1 
ATOM   322   H  HD2  . LYS   A 1 19  ? 45.943 50.285  24.284 1.00 25.78 ? 19   LYS   A HD2  1 
ATOM   323   H  HD3  . LYS   A 1 19  ? 46.070 51.539  25.202 1.00 25.78 ? 19   LYS   A HD3  1 
ATOM   324   H  HE2  . LYS   A 1 19  ? 48.308 50.738  25.750 1.00 24.99 ? 19   LYS   A HE2  1 
ATOM   325   H  HE3  . LYS   A 1 19  ? 48.148 49.746  24.557 1.00 24.99 ? 19   LYS   A HE3  1 
ATOM   326   H  HZ1  . LYS   A 1 19  ? 49.195 51.763  24.004 1.00 25.25 ? 19   LYS   A HZ1  1 
ATOM   327   H  HZ2  . LYS   A 1 19  ? 48.084 51.443  23.124 1.00 25.25 ? 19   LYS   A HZ2  1 
ATOM   328   H  HZ3  . LYS   A 1 19  ? 47.919 52.440  24.169 1.00 25.25 ? 19   LYS   A HZ3  1 
ATOM   329   N  N    . SER   A 1 20  ? 42.301 50.487  28.903 1.00 13.08 ? 20   SER   A N    1 
ATOM   330   C  CA   . SER   A 1 20  ? 40.930 50.955  29.208 1.00 14.86 ? 20   SER   A CA   1 
ATOM   331   C  C    . SER   A 1 20  ? 40.536 52.052  28.220 1.00 17.83 ? 20   SER   A C    1 
ATOM   332   O  O    . SER   A 1 20  ? 41.400 52.875  27.878 1.00 18.23 ? 20   SER   A O    1 
ATOM   333   C  CB   . SER   A 1 20  ? 40.802 51.458  30.617 1.00 17.33 ? 20   SER   A CB   1 
ATOM   334   O  OG   . SER   A 1 20  ? 39.498 51.957  30.864 1.00 17.64 ? 20   SER   A OG   1 
ATOM   335   H  H    . SER   A 1 20  ? 42.928 50.937  29.282 1.00 15.70 ? 20   SER   A H    1 
ATOM   336   H  HA   . SER   A 1 20  ? 40.331 50.197  29.120 1.00 17.84 ? 20   SER   A HA   1 
ATOM   337   H  HB2  . SER   A 1 20  ? 41.000 50.741  31.239 1.00 20.80 ? 20   SER   A HB2  1 
ATOM   338   H  HB3  . SER   A 1 20  ? 41.455 52.158  30.774 1.00 20.80 ? 20   SER   A HB3  1 
ATOM   339   H  HG   . SER   A 1 20  ? 38.971 51.315  30.986 1.00 21.17 ? 20   SER   A HG   1 
ATOM   340   N  N    . GLU   A 1 21  ? 39.284 52.032  27.769 1.00 16.59 ? 21   GLU   A N    1 
ATOM   341   C  CA   . GLU   A 1 21  ? 38.772 53.114  26.893 1.00 16.15 ? 21   GLU   A CA   1 
ATOM   342   C  C    . GLU   A 1 21  ? 37.446 53.578  27.500 1.00 15.85 ? 21   GLU   A C    1 
ATOM   343   O  O    . GLU   A 1 21  ? 36.803 52.785  28.204 1.00 16.86 ? 21   GLU   A O    1 
ATOM   344   C  CB   . GLU   A 1 21  ? 38.578 52.627  25.459 1.00 17.80 ? 21   GLU   A CB   1 
ATOM   345   C  CG   . GLU   A 1 21  ? 39.862 52.293  24.728 1.00 20.69 ? 21   GLU   A CG   1 
ATOM   346   C  CD   . GLU   A 1 21  ? 39.644 51.948  23.266 1.00 19.23 ? 21   GLU   A CD   1 
ATOM   347   O  OE1  . GLU   A 1 21  ? 38.478 51.756  22.877 1.00 21.73 ? 21   GLU   A OE1  1 
ATOM   348   O  OE2  . GLU   A 1 21  ? 40.634 51.884  22.519 1.00 23.34 ? 21   GLU   A OE2  1 
ATOM   349   H  H    . GLU   A 1 21  ? 38.713 51.414  27.949 1.00 19.91 ? 21   GLU   A H    1 
ATOM   350   H  HA   . GLU   A 1 21  ? 39.408 53.845  26.846 1.00 19.39 ? 21   GLU   A HA   1 
ATOM   351   H  HB2  . GLU   A 1 21  ? 38.012 51.839  25.471 1.00 21.36 ? 21   GLU   A HB2  1 
ATOM   352   H  HB3  . GLU   A 1 21  ? 38.103 53.310  24.959 1.00 21.36 ? 21   GLU   A HB3  1 
ATOM   353   H  HG2  . GLU   A 1 21  ? 40.468 53.048  24.789 1.00 24.83 ? 21   GLU   A HG2  1 
ATOM   354   H  HG3  . GLU   A 1 21  ? 40.294 51.545  25.170 1.00 24.83 ? 21   GLU   A HG3  1 
ATOM   355   N  N    . ASN   A 1 22  ? 37.061 54.822  27.241 1.00 16.13 ? 22   ASN   A N    1 
ATOM   356   C  CA   . ASN   A 1 22  ? 35.757 55.311  27.744 1.00 17.55 ? 22   ASN   A CA   1 
ATOM   357   C  C    . ASN   A 1 22  ? 34.646 54.808  26.819 1.00 18.63 ? 22   ASN   A C    1 
ATOM   358   O  O    . ASN   A 1 22  ? 34.828 54.848  25.596 1.00 19.13 ? 22   ASN   A O    1 
ATOM   359   C  CB   . ASN   A 1 22  ? 35.716 56.834  27.868 1.00 18.24 ? 22   ASN   A CB   1 
ATOM   360   C  CG   . ASN   A 1 22  ? 36.397 57.335  29.123 1.00 19.77 ? 22   ASN   A CG   1 
ATOM   361   O  OD1  . ASN   A 1 22  ? 36.994 56.558  29.862 1.00 19.22 ? 22   ASN   A OD1  1 
ATOM   362   N  ND2  . ASN   A 1 22  ? 36.313 58.632  29.371 1.00 20.87 ? 22   ASN   A ND2  1 
ATOM   363   H  H    . ASN   A 1 22  ? 37.518 55.394  26.789 1.00 19.36 ? 22   ASN   A H    1 
ATOM   364   H  HA   . ASN   A 1 22  ? 35.624 54.961  28.639 1.00 21.07 ? 22   ASN   A HA   1 
ATOM   365   H  HB2  . ASN   A 1 22  ? 36.143 57.230  27.092 1.00 21.90 ? 22   ASN   A HB2  1 
ATOM   366   H  HB3  . ASN   A 1 22  ? 34.792 57.130  27.865 1.00 21.90 ? 22   ASN   A HB3  1 
ATOM   367   H  HD21 . ASN   A 1 22  ? 36.685 58.961  30.073 1.00 25.05 ? 22   ASN   A HD21 1 
ATOM   368   H  HD22 . ASN   A 1 22  ? 35.886 59.146  28.830 1.00 25.05 ? 22   ASN   A HD22 1 
ATOM   369   N  N    . LEU   A 1 23  ? 33.547 54.351  27.411 1.00 17.91 ? 23   LEU   A N    1 
ATOM   370   C  CA   . LEU   A 1 23  ? 32.389 53.896  26.605 1.00 16.84 ? 23   LEU   A CA   1 
ATOM   371   C  C    . LEU   A 1 23  ? 31.786 55.094  25.872 1.00 19.94 ? 23   LEU   A C    1 
ATOM   372   O  O    . LEU   A 1 23  ? 31.767 56.185  26.459 1.00 20.32 ? 23   LEU   A O    1 
ATOM   373   C  CB   . LEU   A 1 23  ? 31.359 53.274  27.550 1.00 18.59 ? 23   LEU   A CB   1 
ATOM   374   C  CG   . LEU   A 1 23  ? 30.040 52.846  26.906 1.00 19.06 ? 23   LEU   A CG   1 
ATOM   375   C  CD1  . LEU   A 1 23  ? 30.196 51.511  26.197 1.00 16.67 ? 23   LEU   A CD1  1 
ATOM   376   C  CD2  . LEU   A 1 23  ? 28.933 52.770  27.944 1.00 19.86 ? 23   LEU   A CD2  1 
ATOM   377   H  H    . LEU   A 1 23  ? 33.441 54.292  28.262 1.00 21.50 ? 23   LEU   A H    1 
ATOM   378   H  HA   . LEU   A 1 23  ? 32.665 53.237  25.949 1.00 20.21 ? 23   LEU   A HA   1 
ATOM   379   H  HB2  . LEU   A 1 23  ? 31.760 52.499  27.973 1.00 22.31 ? 23   LEU   A HB2  1 
ATOM   380   H  HB3  . LEU   A 1 23  ? 31.164 53.912  28.254 1.00 22.31 ? 23   LEU   A HB3  1 
ATOM   381   H  HG   . LEU   A 1 23  ? 29.796 53.515  26.248 1.00 22.88 ? 23   LEU   A HG   1 
ATOM   382   H  HD11 . LEU   A 1 23  ? 29.350 51.257  25.796 1.00 20.01 ? 23   LEU   A HD11 1 
ATOM   383   H  HD12 . LEU   A 1 23  ? 30.871 51.589  25.505 1.00 20.01 ? 23   LEU   A HD12 1 
ATOM   384   H  HD13 . LEU   A 1 23  ? 30.466 50.834  26.837 1.00 20.01 ? 23   LEU   A HD13 1 
ATOM   385   H  HD21 . LEU   A 1 23  ? 28.106 52.497  27.516 1.00 23.83 ? 23   LEU   A HD21 1 
ATOM   386   H  HD22 . LEU   A 1 23  ? 29.172 52.123  28.626 1.00 23.83 ? 23   LEU   A HD22 1 
ATOM   387   H  HD23 . LEU   A 1 23  ? 28.813 53.641  28.353 1.00 23.83 ? 23   LEU   A HD23 1 
ATOM   388   N  N    . ASP   A 1 24  ? 31.341 54.893  24.630 1.00 21.94 ? 24   ASP   A N    1 
ATOM   389   C  CA   . ASP   A 1 24  ? 30.612 55.971  23.914 1.00 19.52 ? 24   ASP   A CA   1 
ATOM   390   C  C    . ASP   A 1 24  ? 29.163 55.873  24.393 1.00 21.56 ? 24   ASP   A C    1 
ATOM   391   O  O    . ASP   A 1 24  ? 28.444 54.995  23.887 1.00 18.94 ? 24   ASP   A O    1 
ATOM   392   C  CB   . ASP   A 1 24  ? 30.746 55.804  22.402 1.00 20.89 ? 24   ASP   A CB   1 
ATOM   393   C  CG   . ASP   A 1 24  ? 30.008 56.852  21.586 1.00 24.77 ? 24   ASP   A CG   1 
ATOM   394   O  OD1  . ASP   A 1 24  ? 29.021 57.408  22.096 1.00 22.53 ? 24   ASP   A OD1  1 
ATOM   395   O  OD2  . ASP   A 1 24  ? 30.427 57.093  20.440 1.00 29.24 ? 24   ASP   A OD2  1 
ATOM   396   H  H    . ASP   A 1 24  ? 31.442 54.164  24.186 1.00 26.33 ? 24   ASP   A H    1 
ATOM   397   H  HA   . ASP   A 1 24  ? 30.973 56.851  24.105 1.00 23.43 ? 24   ASP   A HA   1 
ATOM   398   H  HB2  . ASP   A 1 24  ? 31.687 55.831  22.167 1.00 25.07 ? 24   ASP   A HB2  1 
ATOM   399   H  HB3  . ASP   A 1 24  ? 30.416 54.926  22.154 1.00 25.07 ? 24   ASP   A HB3  1 
ATOM   400   N  N    . LEU   A 1 25  ? 28.759 56.709  25.349 1.00 19.86 ? 25   LEU   A N    1 
ATOM   401   C  CA   . LEU   A 1 25  ? 27.401 56.566  25.943 1.00 20.33 ? 25   LEU   A CA   1 
ATOM   402   C  C    . LEU   A 1 25  ? 26.327 56.827  24.879 1.00 19.77 ? 25   LEU   A C    1 
ATOM   403   O  O    . LEU   A 1 25  ? 25.280 56.170  24.925 1.00 19.20 ? 25   LEU   A O    1 
ATOM   404   C  CB   . LEU   A 1 25  ? 27.266 57.538  27.115 1.00 21.48 ? 25   LEU   A CB   1 
ATOM   405   C  CG   . LEU   A 1 25  ? 26.019 57.361  27.981 1.00 23.15 ? 25   LEU   A CG   1 
ATOM   406   C  CD1  . LEU   A 1 25  ? 25.901 55.928  28.477 1.00 23.63 ? 25   LEU   A CD1  1 
ATOM   407   C  CD2  . LEU   A 1 25  ? 26.037 58.330  29.153 1.00 28.18 ? 25   LEU   A CD2  1 
ATOM   408   H  H    . LEU   A 1 25  ? 29.232 57.352  25.669 1.00 23.84 ? 25   LEU   A H    1 
ATOM   409   H  HA   . LEU   A 1 25  ? 27.277 55.661  26.270 1.00 24.40 ? 25   LEU   A HA   1 
ATOM   410   H  HB2  . LEU   A 1 25  ? 28.049 57.447  27.681 1.00 25.78 ? 25   LEU   A HB2  1 
ATOM   411   H  HB3  . LEU   A 1 25  ? 27.272 58.443  26.766 1.00 25.78 ? 25   LEU   A HB3  1 
ATOM   412   H  HG   . LEU   A 1 25  ? 25.243 57.557  27.433 1.00 27.78 ? 25   LEU   A HG   1 
ATOM   413   H  HD11 . LEU   A 1 25  ? 25.104 55.839  29.023 1.00 28.37 ? 25   LEU   A HD11 1 
ATOM   414   H  HD12 . LEU   A 1 25  ? 25.841 55.327  27.718 1.00 28.37 ? 25   LEU   A HD12 1 
ATOM   415   H  HD13 . LEU   A 1 25  ? 26.682 55.703  29.006 1.00 28.37 ? 25   LEU   A HD13 1 
ATOM   416   H  HD21 . LEU   A 1 25  ? 25.239 58.203  29.690 1.00 33.82 ? 25   LEU   A HD21 1 
ATOM   417   H  HD22 . LEU   A 1 25  ? 26.823 58.165  29.697 1.00 33.82 ? 25   LEU   A HD22 1 
ATOM   418   H  HD23 . LEU   A 1 25  ? 26.060 59.241  28.820 1.00 33.82 ? 25   LEU   A HD23 1 
ATOM   419   N  N    . ASP   A 1 26  ? 26.593 57.755  23.961 1.00 22.06 ? 26   ASP   A N    1 
ATOM   420   C  CA   . ASP   A 1 26  ? 25.614 58.074  22.892 1.00 23.51 ? 26   ASP   A CA   1 
ATOM   421   C  C    . ASP   A 1 26  ? 25.318 56.794  22.103 1.00 19.21 ? 26   ASP   A C    1 
ATOM   422   O  O    . ASP   A 1 26  ? 24.129 56.480  21.920 1.00 21.17 ? 26   ASP   A O    1 
ATOM   423   C  CB   . ASP   A 1 26  ? 26.127 59.190  21.980 1.00 20.18 ? 26   ASP   A CB   1 
ATOM   424   C  CG   . ASP   A 1 26  ? 25.935 60.580  22.561 1.00 32.14 ? 26   ASP   A CG   1 
ATOM   425   O  OD1  . ASP   A 1 26  ? 25.317 60.685  23.636 1.00 29.61 ? 26   ASP   A OD1  1 
ATOM   426   O  OD2  . ASP   A 1 26  ? 26.402 61.544  21.929 1.00 36.15 ? 26   ASP   A OD2  1 
ATOM   427   H  H    . ASP   A 1 26  ? 27.321 58.211  23.930 1.00 26.47 ? 26   ASP   A H    1 
ATOM   428   H  HA   . ASP   A 1 26  ? 24.793 58.402  23.292 1.00 28.22 ? 26   ASP   A HA   1 
ATOM   429   H  HB2  . ASP   A 1 26  ? 27.070 59.047  21.805 1.00 24.22 ? 26   ASP   A HB2  1 
ATOM   430   H  HB3  . ASP   A 1 26  ? 25.669 59.137  21.127 1.00 24.22 ? 26   ASP   A HB3  1 
ATOM   431   N  N    . LYS   A 1 27  ? 26.361 56.093  21.658 1.00 17.35 ? 27   LYS   A N    1 
ATOM   432   C  CA   . LYS   A 1 27  ? 26.175 54.853  20.855 1.00 20.47 ? 27   LYS   A CA   1 
ATOM   433   C  C    . LYS   A 1 27  ? 25.549 53.768  21.738 1.00 17.12 ? 27   LYS   A C    1 
ATOM   434   O  O    . LYS   A 1 27  ? 24.652 53.058  21.254 1.00 17.97 ? 27   LYS   A O    1 
ATOM   435   C  CB   . LYS   A 1 27  ? 27.512 54.379  20.281 1.00 23.32 ? 27   LYS   A CB   1 
ATOM   436   C  CG   . LYS   A 1 27  ? 27.461 53.057  19.528 1.00 26.71 ? 27   LYS   A CG   1 
ATOM   437   C  CD   . LYS   A 1 27  ? 28.814 52.602  19.028 1.00 32.16 ? 27   LYS   A CD   1 
ATOM   438   C  CE   . LYS   A 1 27  ? 29.948 52.994  19.951 1.00 31.86 ? 27   LYS   A CE   1 
ATOM   439   N  NZ   . LYS   A 1 27  ? 31.242 53.065  19.234 1.00 35.84 ? 27   LYS   A NZ   1 
ATOM   440   H  H    . LYS   A 1 27  ? 27.182 56.306  21.802 1.00 20.82 ? 27   LYS   A H    1 
ATOM   441   H  HA   . LYS   A 1 27  ? 25.582 55.039  20.111 1.00 24.56 ? 27   LYS   A HA   1 
ATOM   442   H  HB2  . LYS   A 1 27  ? 27.852 55.063  19.683 1.00 27.98 ? 27   LYS   A HB2  1 
ATOM   443   H  HB3  . LYS   A 1 27  ? 28.149 54.296  21.008 1.00 27.98 ? 27   LYS   A HB3  1 
ATOM   444   H  HG2  . LYS   A 1 27  ? 27.092 52.374  20.110 1.00 32.06 ? 27   LYS   A HG2  1 
ATOM   445   H  HG3  . LYS   A 1 27  ? 26.857 53.144  18.774 1.00 32.06 ? 27   LYS   A HG3  1 
ATOM   446   H  HD2  . LYS   A 1 27  ? 28.807 51.638  18.924 1.00 38.60 ? 27   LYS   A HD2  1 
ATOM   447   H  HD3  . LYS   A 1 27  ? 28.973 52.981  18.149 1.00 38.60 ? 27   LYS   A HD3  1 
ATOM   448   H  HE2  . LYS   A 1 27  ? 29.754 53.855  20.354 1.00 38.24 ? 27   LYS   A HE2  1 
ATOM   449   H  HE3  . LYS   A 1 27  ? 30.014 52.351  20.674 1.00 38.24 ? 27   LYS   A HE3  1 
ATOM   450   H  HZ1  . LYS   A 1 27  ? 31.874 52.674  19.723 1.00 43.01 ? 27   LYS   A HZ1  1 
ATOM   451   H  HZ2  . LYS   A 1 27  ? 31.171 52.647  18.452 1.00 43.01 ? 27   LYS   A HZ2  1 
ATOM   452   H  HZ3  . LYS   A 1 27  ? 31.459 53.917  19.096 1.00 43.01 ? 27   LYS   A HZ3  1 
ATOM   453   N  N    . ALA   A 1 28  ? 26.014 53.654  22.984 1.00 14.13 ? 28   ALA   A N    1 
ATOM   454   C  CA   . ALA   A 1 28  ? 25.493 52.612  23.897 1.00 16.72 ? 28   ALA   A CA   1 
ATOM   455   C  C    . ALA   A 1 28  ? 23.991 52.814  24.122 1.00 16.20 ? 28   ALA   A C    1 
ATOM   456   O  O    . ALA   A 1 28  ? 23.269 51.814  24.221 1.00 15.24 ? 28   ALA   A O    1 
ATOM   457   C  CB   . ALA   A 1 28  ? 26.265 52.640  25.193 1.00 17.99 ? 28   ALA   A CB   1 
ATOM   458   H  H    . ALA   A 1 28  ? 26.622 54.159  23.323 1.00 16.96 ? 28   ALA   A H    1 
ATOM   459   H  HA   . ALA   A 1 28  ? 25.613 51.736  23.498 1.00 20.06 ? 28   ALA   A HA   1 
ATOM   460   H  HB1  . ALA   A 1 28  ? 25.922 51.956  25.789 1.00 21.59 ? 28   ALA   A HB1  1 
ATOM   461   H  HB2  . ALA   A 1 28  ? 27.203 52.471  25.015 1.00 21.59 ? 28   ALA   A HB2  1 
ATOM   462   H  HB3  . ALA   A 1 28  ? 26.167 53.511  25.609 1.00 21.59 ? 28   ALA   A HB3  1 
ATOM   463   N  N    . LYS   A 1 29  ? 23.549 54.070  24.204 1.00 16.93 ? 29   LYS   A N    1 
ATOM   464   C  CA   . LYS   A 1 29  ? 22.099 54.352  24.383 1.00 16.86 ? 29   LYS   A CA   1 
ATOM   465   C  C    . LYS   A 1 29  ? 21.369 54.125  23.053 1.00 18.34 ? 29   LYS   A C    1 
ATOM   466   O  O    . LYS   A 1 29  ? 20.302 53.496  23.070 1.00 16.29 ? 29   LYS   A O    1 
ATOM   467   C  CB   . LYS   A 1 29  ? 21.888 55.775  24.911 1.00 19.68 ? 29   LYS   A CB   1 
ATOM   468   C  CG   . LYS   A 1 29  ? 22.189 55.955  26.393 1.00 24.00 ? 29   LYS   A CG   1 
ATOM   469   C  CD   . LYS   A 1 29  ? 22.200 57.401  26.836 1.00 23.13 ? 29   LYS   A CD   1 
ATOM   470   C  CE   . LYS   A 1 29  ? 22.108 57.556  28.339 1.00 34.02 ? 29   LYS   A CE   1 
ATOM   471   N  NZ   . LYS   A 1 29  ? 22.129 58.981  28.747 1.00 37.17 ? 29   LYS   A NZ   1 
ATOM   472   H  H    . LYS   A 1 29  ? 24.051 54.767  24.161 1.00 20.32 ? 29   LYS   A H    1 
ATOM   473   H  HA   . LYS   A 1 29  ? 21.728 53.745  25.043 1.00 20.24 ? 29   LYS   A HA   1 
ATOM   474   H  HB2  . LYS   A 1 29  ? 22.449 56.382  24.403 1.00 23.62 ? 29   LYS   A HB2  1 
ATOM   475   H  HB3  . LYS   A 1 29  ? 20.968 56.035  24.746 1.00 23.62 ? 29   LYS   A HB3  1 
ATOM   476   H  HG2  . LYS   A 1 29  ? 21.527 55.471  26.911 1.00 28.81 ? 29   LYS   A HG2  1 
ATOM   477   H  HG3  . LYS   A 1 29  ? 23.051 55.557  26.591 1.00 28.81 ? 29   LYS   A HG3  1 
ATOM   478   H  HD2  . LYS   A 1 29  ? 23.013 57.825  26.521 1.00 27.76 ? 29   LYS   A HD2  1 
ATOM   479   H  HD3  . LYS   A 1 29  ? 21.458 57.868  26.421 1.00 27.76 ? 29   LYS   A HD3  1 
ATOM   480   H  HE2  . LYS   A 1 29  ? 21.292 57.140  28.658 1.00 40.82 ? 29   LYS   A HE2  1 
ATOM   481   H  HE3  . LYS   A 1 29  ? 22.847 57.088  28.758 1.00 40.82 ? 29   LYS   A HE3  1 
ATOM   482   H  HZ1  . LYS   A 1 29  ? 22.118 59.036  29.635 1.00 44.61 ? 29   LYS   A HZ1  1 
ATOM   483   H  HZ2  . LYS   A 1 29  ? 22.867 59.368  28.436 1.00 44.61 ? 29   LYS   A HZ2  1 
ATOM   484   H  HZ3  . LYS   A 1 29  ? 21.415 59.396  28.415 1.00 44.61 ? 29   LYS   A HZ3  1 
ATOM   485   N  N    . LYS   A 1 30  ? 21.935 54.619  21.953 1.00 15.72 ? 30   LYS   A N    1 
ATOM   486   C  CA   . LYS   A 1 30  ? 21.285 54.477  20.624 1.00 16.47 ? 30   LYS   A CA   1 
ATOM   487   C  C    . LYS   A 1 30  ? 21.077 52.992  20.302 1.00 17.74 ? 30   LYS   A C    1 
ATOM   488   O  O    . LYS   A 1 30  ? 20.036 52.657  19.725 1.00 15.25 ? 30   LYS   A O    1 
ATOM   489   C  CB   . LYS   A 1 30  ? 22.124 55.163  19.540 1.00 17.78 ? 30   LYS   A CB   1 
ATOM   490   C  CG   . LYS   A 1 30  ? 21.521 55.130  18.143 1.00 18.54 ? 30   LYS   A CG   1 
ATOM   491   C  CD   . LYS   A 1 30  ? 22.256 56.003  17.152 1.00 20.88 ? 30   LYS   A CD   1 
ATOM   492   C  CE   . LYS   A 1 30  ? 21.586 56.044  15.796 1.00 22.25 ? 30   LYS   A CE   1 
ATOM   493   N  NZ   . LYS   A 1 30  ? 22.315 56.919  14.849 1.00 19.77 ? 30   LYS   A NZ   1 
ATOM   494   H  H    . LYS   A 1 30  ? 22.686 55.037  21.942 1.00 18.87 ? 30   LYS   A H    1 
ATOM   495   H  HA   . LYS   A 1 30  ? 20.418 54.911  20.647 1.00 19.77 ? 30   LYS   A HA   1 
ATOM   496   H  HB2  . LYS   A 1 30  ? 22.264 56.088  19.795 1.00 21.34 ? 30   LYS   A HB2  1 
ATOM   497   H  HB3  . LYS   A 1 30  ? 22.997 54.742  19.511 1.00 21.34 ? 30   LYS   A HB3  1 
ATOM   498   H  HG2  . LYS   A 1 30  ? 21.520 54.215  17.820 1.00 22.25 ? 30   LYS   A HG2  1 
ATOM   499   H  HG3  . LYS   A 1 30  ? 20.595 55.415  18.191 1.00 22.25 ? 30   LYS   A HG3  1 
ATOM   500   H  HD2  . LYS   A 1 30  ? 22.318 56.904  17.505 1.00 25.06 ? 30   LYS   A HD2  1 
ATOM   501   H  HD3  . LYS   A 1 30  ? 23.163 55.676  17.050 1.00 25.06 ? 30   LYS   A HD3  1 
ATOM   502   H  HE2  . LYS   A 1 30  ? 21.535 55.146  15.433 1.00 26.70 ? 30   LYS   A HE2  1 
ATOM   503   H  HE3  . LYS   A 1 30  ? 20.675 56.362  15.895 1.00 26.70 ? 30   LYS   A HE3  1 
ATOM   504   H  HZ1  . LYS   A 1 30  ? 21.904 56.910  14.059 1.00 23.72 ? 30   LYS   A HZ1  1 
ATOM   505   H  HZ2  . LYS   A 1 30  ? 22.331 57.751  15.165 1.00 23.72 ? 30   LYS   A HZ2  1 
ATOM   506   H  HZ3  . LYS   A 1 30  ? 23.149 56.623  14.753 1.00 23.72 ? 30   LYS   A HZ3  1 
ATOM   507   N  N    . PHE   A 1 31  ? 22.048 52.152  20.662 1.00 15.44 ? 31   PHE   A N    1 
ATOM   508   C  CA   . PHE   A 1 31  ? 21.943 50.695  20.379 1.00 13.44 ? 31   PHE   A CA   1 
ATOM   509   C  C    . PHE   A 1 31  ? 21.625 49.945  21.682 1.00 15.38 ? 31   PHE   A C    1 
ATOM   510   O  O    . PHE   A 1 31  ? 21.850 48.722  21.708 1.00 14.29 ? 31   PHE   A O    1 
ATOM   511   C  CB   . PHE   A 1 31  ? 23.186 50.231  19.613 1.00 17.48 ? 31   PHE   A CB   1 
ATOM   512   C  CG   . PHE   A 1 31  ? 23.354 50.901  18.273 1.00 13.18 ? 31   PHE   A CG   1 
ATOM   513   C  CD1  . PHE   A 1 31  ? 22.750 50.383  17.139 1.00 14.68 ? 31   PHE   A CD1  1 
ATOM   514   C  CD2  . PHE   A 1 31  ? 24.094 52.066  18.147 1.00 17.60 ? 31   PHE   A CD2  1 
ATOM   515   C  CE1  . PHE   A 1 31  ? 22.898 51.003  15.908 1.00 15.74 ? 31   PHE   A CE1  1 
ATOM   516   C  CE2  . PHE   A 1 31  ? 24.238 52.686  16.917 1.00 18.32 ? 31   PHE   A CE2  1 
ATOM   517   C  CZ   . PHE   A 1 31  ? 23.640 52.155  15.800 1.00 19.27 ? 31   PHE   A CZ   1 
ATOM   518   H  H    . PHE   A 1 31  ? 22.770 52.389  21.065 1.00 18.53 ? 31   PHE   A H    1 
ATOM   519   H  HA   . PHE   A 1 31  ? 21.202 50.488  19.788 1.00 16.13 ? 31   PHE   A HA   1 
ATOM   520   H  HB2  . PHE   A 1 31  ? 23.973 50.404  20.153 1.00 20.98 ? 31   PHE   A HB2  1 
ATOM   521   H  HB3  . PHE   A 1 31  ? 23.137 49.271  19.482 1.00 20.98 ? 31   PHE   A HB3  1 
ATOM   522   H  HD1  . PHE   A 1 31  ? 22.238 49.609  17.204 1.00 17.61 ? 31   PHE   A HD1  1 
ATOM   523   H  HD2  . PHE   A 1 31  ? 24.499 52.436  18.898 1.00 21.13 ? 31   PHE   A HD2  1 
ATOM   524   H  HE1  . PHE   A 1 31  ? 22.494 50.639  15.154 1.00 18.89 ? 31   PHE   A HE1  1 
ATOM   525   H  HE2  . PHE   A 1 31  ? 24.741 53.465  16.847 1.00 21.99 ? 31   PHE   A HE2  1 
ATOM   526   H  HZ   . PHE   A 1 31  ? 23.737 52.573  14.975 1.00 23.13 ? 31   PHE   A HZ   1 
ATOM   527   N  N    . ILE   A 1 32  ? 21.134 50.649  22.707 1.00 12.45 ? 32   ILE   A N    1 
ATOM   528   C  CA   . ILE   A 1 32  ? 20.668 50.031  23.988 1.00 13.21 ? 32   ILE   A CA   1 
ATOM   529   C  C    . ILE   A 1 32  ? 21.827 49.433  24.792 1.00 17.45 ? 32   ILE   A C    1 
ATOM   530   O  O    . ILE   A 1 32  ? 21.947 49.776  25.979 1.00 15.78 ? 32   ILE   A O    1 
ATOM   531   C  CB   . ILE   A 1 32  ? 19.570 48.981  23.724 1.00 13.11 ? 32   ILE   A CB   1 
ATOM   532   C  CG1  . ILE   A 1 32  ? 18.427 49.562  22.889 1.00 14.66 ? 32   ILE   A CG1  1 
ATOM   533   C  CG2  . ILE   A 1 32  ? 19.068 48.395  25.034 1.00 14.71 ? 32   ILE   A CG2  1 
ATOM   534   C  CD1  . ILE   A 1 32  ? 17.336 48.569  22.565 1.00 14.26 ? 32   ILE   A CD1  1 
ATOM   535   H  H    . ILE   A 1 32  ? 21.056 51.505  22.691 1.00 14.95 ? 32   ILE   A H    1 
ATOM   536   H  HA   . ILE   A 1 32  ? 20.285 50.740  24.529 1.00 15.86 ? 32   ILE   A HA   1 
ATOM   537   H  HB   . ILE   A 1 32  ? 19.960 48.261  23.204 1.00 15.74 ? 32   ILE   A HB   1 
ATOM   538   H  HG12 . ILE   A 1 32  ? 18.038 50.311  23.367 1.00 17.60 ? 32   ILE   A HG12 1 
ATOM   539   H  HG13 . ILE   A 1 32  ? 18.790 49.912  22.060 1.00 17.60 ? 32   ILE   A HG13 1 
ATOM   540   H  HG21 . ILE   A 1 32  ? 18.379 47.737  24.851 1.00 17.66 ? 32   ILE   A HG21 1 
ATOM   541   H  HG22 . ILE   A 1 32  ? 19.804 47.970  25.502 1.00 17.66 ? 32   ILE   A HG22 1 
ATOM   542   H  HG23 . ILE   A 1 32  ? 18.700 49.103  25.586 1.00 17.66 ? 32   ILE   A HG23 1 
ATOM   543   H  HD11 . ILE   A 1 32  ? 16.649 49.004  22.037 1.00 17.12 ? 32   ILE   A HD11 1 
ATOM   544   H  HD12 . ILE   A 1 32  ? 17.711 47.829  22.061 1.00 17.12 ? 32   ILE   A HD12 1 
ATOM   545   H  HD13 . ILE   A 1 32  ? 16.947 48.235  23.389 1.00 17.12 ? 32   ILE   A HD13 1 
ATOM   546   N  N    . GLY   A 1 33  ? 22.597 48.562  24.177 1.00 13.81 ? 33   GLY   A N    1 
ATOM   547   C  CA   . GLY   A 1 33  ? 23.642 47.842  24.925 1.00 14.23 ? 33   GLY   A CA   1 
ATOM   548   C  C    . GLY   A 1 33  ? 23.840 46.419  24.424 1.00 12.87 ? 33   GLY   A C    1 
ATOM   549   O  O    . GLY   A 1 33  ? 23.363 46.122  23.356 1.00 13.06 ? 33   GLY   A O    1 
ATOM   550   H  H    . GLY   A 1 33  ? 22.544 48.365  23.341 1.00 16.58 ? 33   GLY   A H    1 
ATOM   551   H  HA2  . GLY   A 1 33  ? 24.479 48.327  24.853 1.00 17.08 ? 33   GLY   A HA2  1 
ATOM   552   H  HA3  . GLY   A 1 33  ? 23.406 47.821  25.866 1.00 17.08 ? 33   GLY   A HA3  1 
ATOM   553   N  N    . CYS   A 1 34  ? 24.602 45.623  25.157 1.00 11.72 ? 34   CYS   A N    1 
ATOM   554   C  CA   . CYS   A 1 34  ? 24.835 44.195  24.838 1.00 12.15 ? 34   CYS   A CA   1 
ATOM   555   C  C    . CYS   A 1 34  ? 24.818 43.961  23.321 1.00 10.54 ? 34   CYS   A C    1 
ATOM   556   O  O    . CYS   A 1 34  ? 25.654 44.487  22.640 1.00 12.50 ? 34   CYS   A O    1 
ATOM   557   C  CB   . CYS   A 1 34  ? 23.805 43.417  25.645 1.00 11.68 ? 34   CYS   A CB   1 
ATOM   558   S  SG   . CYS   A 1 34  ? 24.190 41.655  25.865 1.00 11.86 ? 34   CYS   A SG   1 
ATOM   559   H  H    . CYS   A 1 34  ? 25.010 45.888  25.866 1.00 14.07 ? 34   CYS   A H    1 
ATOM   560   H  HA   . CYS   A 1 34  ? 25.717 43.881  25.092 1.00 14.59 ? 34   CYS   A HA   1 
ATOM   561   H  HB2  . CYS   A 1 34  ? 23.718 43.829  26.519 1.00 14.01 ? 34   CYS   A HB2  1 
ATOM   562   H  HB3  . CYS   A 1 34  ? 22.943 43.495  25.208 1.00 14.01 ? 34   CYS   A HB3  1 
ATOM   563   H  HG   . CYS   A 1 34  ? 25.343 41.532  26.172 1.00 14.24 ? 34   CYS   A HG   1 
ATOM   564   N  N    . ARG   A 1 35  ? 23.857 43.159  22.840 1.00 11.53 ? 35   ARG   A N    1 
ATOM   565   C  CA   . ARG   A 1 35  ? 23.777 42.811  21.396 1.00 12.79 ? 35   ARG   A CA   1 
ATOM   566   C  C    . ARG   A 1 35  ? 24.021 44.017  20.472 1.00 11.44 ? 35   ARG   A C    1 
ATOM   567   O  O    . ARG   A 1 35  ? 24.928 43.970  19.685 1.00 10.84 ? 35   ARG   A O    1 
ATOM   568   C  CB   . ARG   A 1 35  ? 22.369 42.255  21.129 1.00 10.81 ? 35   ARG   A CB   1 
ATOM   569   C  CG   . ARG   A 1 35  ? 22.129 41.778  19.705 1.00 9.26  ? 35   ARG   A CG   1 
ATOM   570   C  CD   . ARG   A 1 35  ? 20.806 41.032  19.633 1.00 11.10 ? 35   ARG   A CD   1 
ATOM   571   N  NE   . ARG   A 1 35  ? 20.349 40.724  18.286 1.00 11.59 ? 35   ARG   A NE   1 
ATOM   572   C  CZ   . ARG   A 1 35  ? 19.139 40.256  18.004 1.00 12.87 ? 35   ARG   A CZ   1 
ATOM   573   N  NH1  . ARG   A 1 35  ? 18.343 39.852  18.976 1.00 11.51 ? 35   ARG   A NH1  1 
ATOM   574   N  NH2  . ARG   A 1 35  ? 18.733 40.191  16.751 1.00 11.35 ? 35   ARG   A NH2  1 
ATOM   575   H  H    . ARG   A 1 35  ? 23.242 42.804  23.325 1.00 13.84 ? 35   ARG   A H    1 
ATOM   576   H  HA   . ARG   A 1 35  ? 24.472 42.163  21.202 1.00 15.35 ? 35   ARG   A HA   1 
ATOM   577   H  HB2  . ARG   A 1 35  ? 22.207 41.516  21.736 1.00 12.98 ? 35   ARG   A HB2  1 
ATOM   578   H  HB3  . ARG   A 1 35  ? 21.718 42.943  21.340 1.00 12.98 ? 35   ARG   A HB3  1 
ATOM   579   H  HG2  . ARG   A 1 35  ? 22.118 42.535  19.098 1.00 11.11 ? 35   ARG   A HG2  1 
ATOM   580   H  HG3  . ARG   A 1 35  ? 22.853 41.198  19.422 1.00 11.11 ? 35   ARG   A HG3  1 
ATOM   581   H  HD2  . ARG   A 1 35  ? 20.890 40.203  20.130 1.00 13.33 ? 35   ARG   A HD2  1 
ATOM   582   H  HD3  . ARG   A 1 35  ? 20.126 41.562  20.078 1.00 13.33 ? 35   ARG   A HD3  1 
ATOM   583   H  HE   . ARG   A 1 35  ? 20.895 40.853  17.634 1.00 13.91 ? 35   ARG   A HE   1 
ATOM   584   H  HH11 . ARG   A 1 35  ? 18.608 39.892  19.793 1.00 13.82 ? 35   ARG   A HH11 1 
ATOM   585   H  HH12 . ARG   A 1 35  ? 17.559 39.549  18.792 1.00 13.82 ? 35   ARG   A HH12 1 
ATOM   586   H  HH21 . ARG   A 1 35  ? 19.252 40.452  16.117 1.00 13.62 ? 35   ARG   A HH21 1 
ATOM   587   H  HH22 . ARG   A 1 35  ? 17.949 39.888  16.568 1.00 13.62 ? 35   ARG   A HH22 1 
ATOM   588   N  N    . GLY   A 1 36  ? 23.140 45.021  20.586 1.00 11.99 ? 36   GLY   A N    1 
ATOM   589   C  CA   . GLY   A 1 36  ? 23.240 46.173  19.668 1.00 12.94 ? 36   GLY   A CA   1 
ATOM   590   C  C    . GLY   A 1 36  ? 24.571 46.899  19.755 1.00 12.81 ? 36   GLY   A C    1 
ATOM   591   O  O    . GLY   A 1 36  ? 25.122 47.253  18.706 1.00 11.80 ? 36   GLY   A O    1 
ATOM   592   H  H    . GLY   A 1 36  ? 22.502 45.059  21.161 1.00 14.39 ? 36   GLY   A H    1 
ATOM   593   H  HA2  . GLY   A 1 36  ? 23.106 45.865  18.758 1.00 15.53 ? 36   GLY   A HA2  1 
ATOM   594   H  HA3  . GLY   A 1 36  ? 22.525 46.798  19.865 1.00 15.53 ? 36   GLY   A HA3  1 
ATOM   595   N  N    . LEU   A 1 37  ? 25.056 47.119  20.976 1.00 13.79 ? 37   LEU   A N    1 
ATOM   596   C  CA   . LEU   A 1 37  ? 26.360 47.811  21.163 1.00 12.29 ? 37   LEU   A CA   1 
ATOM   597   C  C    . LEU   A 1 37  ? 27.473 46.953  20.551 1.00 12.05 ? 37   LEU   A C    1 
ATOM   598   O  O    . LEU   A 1 37  ? 28.342 47.507  19.870 1.00 13.51 ? 37   LEU   A O    1 
ATOM   599   C  CB   . LEU   A 1 37  ? 26.584 48.059  22.659 1.00 12.77 ? 37   LEU   A CB   1 
ATOM   600   C  CG   . LEU   A 1 37  ? 27.980 48.534  23.052 1.00 13.96 ? 37   LEU   A CG   1 
ATOM   601   C  CD1  . LEU   A 1 37  ? 28.285 49.887  22.429 1.00 12.69 ? 37   LEU   A CD1  1 
ATOM   602   C  CD2  . LEU   A 1 37  ? 28.120 48.599  24.564 1.00 12.86 ? 37   LEU   A CD2  1 
ATOM   603   H  H    . LEU   A 1 37  ? 24.663 46.885  21.704 1.00 16.56 ? 37   LEU   A H    1 
ATOM   604   H  HA   . LEU   A 1 37  ? 26.364 48.671  20.714 1.00 14.75 ? 37   LEU   A HA   1 
ATOM   605   H  HB2  . LEU   A 1 37  ? 25.940 48.719  22.960 1.00 15.32 ? 37   LEU   A HB2  1 
ATOM   606   H  HB3  . LEU   A 1 37  ? 26.394 47.237  23.138 1.00 15.32 ? 37   LEU   A HB3  1 
ATOM   607   H  HG   . LEU   A 1 37  ? 28.623 47.892  22.713 1.00 16.75 ? 37   LEU   A HG   1 
ATOM   608   H  HD11 . LEU   A 1 37  ? 29.175 50.171  22.690 1.00 15.23 ? 37   LEU   A HD11 1 
ATOM   609   H  HD12 . LEU   A 1 37  ? 28.240 49.816  21.463 1.00 15.23 ? 37   LEU   A HD12 1 
ATOM   610   H  HD13 . LEU   A 1 37  ? 27.635 50.539  22.736 1.00 15.23 ? 37   LEU   A HD13 1 
ATOM   611   H  HD21 . LEU   A 1 37  ? 29.012 48.902  24.794 1.00 15.44 ? 37   LEU   A HD21 1 
ATOM   612   H  HD22 . LEU   A 1 37  ? 27.466 49.218  24.923 1.00 15.44 ? 37   LEU   A HD22 1 
ATOM   613   H  HD23 . LEU   A 1 37  ? 27.971 47.718  24.941 1.00 15.44 ? 37   LEU   A HD23 1 
ATOM   614   N  N    . GLY   A 1 38  ? 27.428 45.640  20.766 1.00 10.52 ? 38   GLY   A N    1 
ATOM   615   C  CA   . GLY   A 1 38  ? 28.470 44.757  20.217 1.00 10.30 ? 38   GLY   A CA   1 
ATOM   616   C  C    . GLY   A 1 38  ? 28.481 44.746  18.696 1.00 12.99 ? 38   GLY   A C    1 
ATOM   617   O  O    . GLY   A 1 38  ? 29.569 44.780  18.113 1.00 12.28 ? 38   GLY   A O    1 
ATOM   618   H  H    . GLY   A 1 38  ? 26.815 45.241  21.219 1.00 12.62 ? 38   GLY   A H    1 
ATOM   619   H  HA2  . GLY   A 1 38  ? 29.338 45.044  20.542 1.00 12.36 ? 38   GLY   A HA2  1 
ATOM   620   H  HA3  . GLY   A 1 38  ? 28.330 43.854  20.543 1.00 12.36 ? 38   GLY   A HA3  1 
ATOM   621   N  N    . VAL   A 1 39  ? 27.299 44.670  18.076 1.00 11.84 ? 39   VAL   A N    1 
ATOM   622   C  CA   . VAL   A 1 39  ? 27.235 44.567  16.589 1.00 10.54 ? 39   VAL   A CA   1 
ATOM   623   C  C    . VAL   A 1 39  ? 27.760 45.867  15.970 1.00 9.27  ? 39   VAL   A C    1 
ATOM   624   O  O    . VAL   A 1 39  ? 28.510 45.798  14.996 1.00 13.38 ? 39   VAL   A O    1 
ATOM   625   C  CB   . VAL   A 1 39  ? 25.802 44.263  16.107 1.00 10.95 ? 39   VAL   A CB   1 
ATOM   626   C  CG1  . VAL   A 1 39  ? 25.687 44.347  14.593 1.00 13.56 ? 39   VAL   A CG1  1 
ATOM   627   C  CG2  . VAL   A 1 39  ? 25.318 42.910  16.608 1.00 11.34 ? 39   VAL   A CG2  1 
ATOM   628   H  H    . VAL   A 1 39  ? 26.537 44.675  18.474 1.00 14.22 ? 39   VAL   A H    1 
ATOM   629   H  HA   . VAL   A 1 39  ? 27.793 43.828  16.301 1.00 12.66 ? 39   VAL   A HA   1 
ATOM   630   H  HB   . VAL   A 1 39  ? 25.227 44.946  16.487 1.00 13.14 ? 39   VAL   A HB   1 
ATOM   631   H  HG11 . VAL   A 1 39  ? 24.775 44.151  14.326 1.00 16.28 ? 39   VAL   A HG11 1 
ATOM   632   H  HG12 . VAL   A 1 39  ? 25.924 45.241  14.299 1.00 16.28 ? 39   VAL   A HG12 1 
ATOM   633   H  HG13 . VAL   A 1 39  ? 26.288 43.703  14.186 1.00 16.28 ? 39   VAL   A HG13 1 
ATOM   634   H  HG21 . VAL   A 1 39  ? 24.416 42.750  16.288 1.00 13.61 ? 39   VAL   A HG21 1 
ATOM   635   H  HG22 . VAL   A 1 39  ? 25.906 42.213  16.278 1.00 13.61 ? 39   VAL   A HG22 1 
ATOM   636   H  HG23 . VAL   A 1 39  ? 25.322 42.903  17.578 1.00 13.61 ? 39   VAL   A HG23 1 
ATOM   637   N  N    . LYS   A 1 40  ? 27.344 47.001  16.524 1.00 13.13 ? 40   LYS   A N    1 
ATOM   638   C  CA   . LYS   A 1 40  ? 27.790 48.314  15.990 1.00 12.97 ? 40   LYS   A CA   1 
ATOM   639   C  C    . LYS   A 1 40  ? 29.309 48.429  16.152 1.00 12.28 ? 40   LYS   A C    1 
ATOM   640   O  O    . LYS   A 1 40  ? 29.974 48.887  15.218 1.00 12.41 ? 40   LYS   A O    1 
ATOM   641   C  CB   . LYS   A 1 40  ? 27.082 49.447  16.735 1.00 14.82 ? 40   LYS   A CB   1 
ATOM   642   C  CG   . LYS   A 1 40  ? 27.453 50.852  16.283 1.00 16.15 ? 40   LYS   A CG   1 
ATOM   643   C  CD   . LYS   A 1 40  ? 27.185 51.101  14.814 1.00 19.88 ? 40   LYS   A CD   1 
ATOM   644   C  CE   . LYS   A 1 40  ? 27.277 52.565  14.438 1.00 26.04 ? 40   LYS   A CE   1 
ATOM   645   N  NZ   . LYS   A 1 40  ? 28.004 52.763  13.164 1.00 27.68 ? 40   LYS   A NZ   1 
ATOM   646   H  H    . LYS   A 1 40  ? 26.812 47.047  17.199 1.00 15.76 ? 40   LYS   A H    1 
ATOM   647   H  HA   . LYS   A 1 40  ? 27.564 48.381  15.049 1.00 15.57 ? 40   LYS   A HA   1 
ATOM   648   H  HB2  . LYS   A 1 40  ? 26.124 49.333  16.633 1.00 17.78 ? 40   LYS   A HB2  1 
ATOM   649   H  HB3  . LYS   A 1 40  ? 27.279 49.365  17.681 1.00 17.78 ? 40   LYS   A HB3  1 
ATOM   650   H  HG2  . LYS   A 1 40  ? 26.954 51.496  16.810 1.00 19.38 ? 40   LYS   A HG2  1 
ATOM   651   H  HG3  . LYS   A 1 40  ? 28.394 51.005  16.464 1.00 19.38 ? 40   LYS   A HG3  1 
ATOM   652   H  HD2  . LYS   A 1 40  ? 27.820 50.595  14.284 1.00 23.86 ? 40   LYS   A HD2  1 
ATOM   653   H  HD3  . LYS   A 1 40  ? 26.301 50.769  14.590 1.00 23.86 ? 40   LYS   A HD3  1 
ATOM   654   H  HE2  . LYS   A 1 40  ? 26.384 52.936  14.361 1.00 31.25 ? 40   LYS   A HE2  1 
ATOM   655   H  HE3  . LYS   A 1 40  ? 27.727 53.053  15.146 1.00 31.25 ? 40   LYS   A HE3  1 
ATOM   656   H  HZ1  . LYS   A 1 40  ? 28.103 53.634  13.011 1.00 33.22 ? 40   LYS   A HZ1  1 
ATOM   657   H  HZ2  . LYS   A 1 40  ? 28.805 52.379  13.216 1.00 33.22 ? 40   LYS   A HZ2  1 
ATOM   658   H  HZ3  . LYS   A 1 40  ? 27.542 52.395  12.498 1.00 33.22 ? 40   LYS   A HZ3  1 
ATOM   659   N  N    . THR   A 1 41  ? 29.810 48.022  17.317 1.00 12.96 ? 41   THR   A N    1 
ATOM   660   C  CA   . THR   A 1 41  ? 31.272 48.069  17.575 1.00 13.74 ? 41   THR   A CA   1 
ATOM   661   C  C    . THR   A 1 41  ? 31.992 47.209  16.528 1.00 11.67 ? 41   THR   A C    1 
ATOM   662   O  O    . THR   A 1 41  ? 32.965 47.691  15.930 1.00 13.63 ? 41   THR   A O    1 
ATOM   663   C  CB   . THR   A 1 41  ? 31.573 47.653  19.024 1.00 13.10 ? 41   THR   A CB   1 
ATOM   664   O  OG1  . THR   A 1 41  ? 30.856 48.505  19.916 1.00 14.19 ? 41   THR   A OG1  1 
ATOM   665   C  CG2  . THR   A 1 41  ? 33.051 47.694  19.346 1.00 15.35 ? 41   THR   A CG2  1 
ATOM   666   H  H    . THR   A 1 41  ? 29.338 47.718  17.969 1.00 15.56 ? 41   THR   A H    1 
ATOM   667   H  HA   . THR   A 1 41  ? 31.607 48.975  17.484 1.00 16.49 ? 41   THR   A HA   1 
ATOM   668   H  HB   . THR   A 1 41  ? 31.287 46.732  19.132 1.00 15.73 ? 41   THR   A HB   1 
ATOM   669   H  HG1  . THR   A 1 41  ? 30.057 48.249  19.967 1.00 17.03 ? 41   THR   A HG1  1 
ATOM   670   H  HG21 . THR   A 1 41  ? 33.189 47.424  20.267 1.00 18.42 ? 41   THR   A HG21 1 
ATOM   671   H  HG22 . THR   A 1 41  ? 33.528 47.088  18.757 1.00 18.42 ? 41   THR   A HG22 1 
ATOM   672   H  HG23 . THR   A 1 41  ? 33.385 48.596  19.220 1.00 18.42 ? 41   THR   A HG23 1 
ATOM   673   N  N    . LEU   A 1 42  ? 31.514 45.983  16.316 1.00 11.91 ? 42   LEU   A N    1 
ATOM   674   C  CA   . LEU   A 1 42  ? 32.190 45.067  15.360 1.00 11.74 ? 42   LEU   A CA   1 
ATOM   675   C  C    . LEU   A 1 42  ? 32.100 45.650  13.944 1.00 13.53 ? 42   LEU   A C    1 
ATOM   676   O  O    . LEU   A 1 42  ? 33.122 45.662  13.245 1.00 13.37 ? 42   LEU   A O    1 
ATOM   677   C  CB   . LEU   A 1 42  ? 31.506 43.695  15.417 1.00 12.17 ? 42   LEU   A CB   1 
ATOM   678   C  CG   . LEU   A 1 42  ? 32.132 42.606  14.547 1.00 11.00 ? 42   LEU   A CG   1 
ATOM   679   C  CD1  . LEU   A 1 42  ? 33.424 42.097  15.166 1.00 14.57 ? 42   LEU   A CD1  1 
ATOM   680   C  CD2  . LEU   A 1 42  ? 31.158 41.456  14.336 1.00 12.86 ? 42   LEU   A CD2  1 
ATOM   681   H  H    . LEU   A 1 42  ? 30.817 45.658  16.700 1.00 14.30 ? 42   LEU   A H    1 
ATOM   682   H  HA   . LEU   A 1 42  ? 33.125 44.968  15.597 1.00 14.10 ? 42   LEU   A HA   1 
ATOM   683   H  HB2  . LEU   A 1 42  ? 31.506 43.390  16.338 1.00 14.61 ? 42   LEU   A HB2  1 
ATOM   684   H  HB3  . LEU   A 1 42  ? 30.579 43.803  15.154 1.00 14.61 ? 42   LEU   A HB3  1 
ATOM   685   H  HG   . LEU   A 1 42  ? 32.338 42.996  13.683 1.00 13.20 ? 42   LEU   A HG   1 
ATOM   686   H  HD11 . LEU   A 1 42  ? 33.805 41.408  14.600 1.00 17.49 ? 42   LEU   A HD11 1 
ATOM   687   H  HD12 . LEU   A 1 42  ? 34.054 42.830  15.250 1.00 17.49 ? 42   LEU   A HD12 1 
ATOM   688   H  HD13 . LEU   A 1 42  ? 33.239 41.728  16.044 1.00 17.49 ? 42   LEU   A HD13 1 
ATOM   689   H  HD21 . LEU   A 1 42  ? 31.574 40.777  13.782 1.00 15.44 ? 42   LEU   A HD21 1 
ATOM   690   H  HD22 . LEU   A 1 42  ? 30.920 41.072  15.194 1.00 15.44 ? 42   LEU   A HD22 1 
ATOM   691   H  HD23 . LEU   A 1 42  ? 30.358 41.785  13.897 1.00 15.44 ? 42   LEU   A HD23 1 
ATOM   692   N  N    . PHE   A 1 43  ? 30.901 46.088  13.548 1.00 12.19 ? 43   PHE   A N    1 
ATOM   693   C  CA   . PHE   A 1 43  ? 30.689 46.619  12.175 1.00 12.66 ? 43   PHE   A CA   1 
ATOM   694   C  C    . PHE   A 1 43  ? 31.628 47.807  11.941 1.00 14.27 ? 43   PHE   A C    1 
ATOM   695   O  O    . PHE   A 1 43  ? 32.174 47.951  10.839 1.00 15.89 ? 43   PHE   A O    1 
ATOM   696   C  CB   . PHE   A 1 43  ? 29.218 47.013  12.011 1.00 13.60 ? 43   PHE   A CB   1 
ATOM   697   C  CG   . PHE   A 1 43  ? 28.686 47.059  10.601 1.00 17.30 ? 43   PHE   A CG   1 
ATOM   698   C  CD1  . PHE   A 1 43  ? 29.521 46.874  9.513  1.00 14.75 ? 43   PHE   A CD1  1 
ATOM   699   C  CD2  . PHE   A 1 43  ? 27.341 47.293  10.366 1.00 15.84 ? 43   PHE   A CD2  1 
ATOM   700   C  CE1  . PHE   A 1 43  ? 29.023 46.924  8.221  1.00 17.31 ? 43   PHE   A CE1  1 
ATOM   701   C  CE2  . PHE   A 1 43  ? 26.843 47.341  9.074  1.00 14.33 ? 43   PHE   A CE2  1 
ATOM   702   C  CZ   . PHE   A 1 43  ? 27.685 47.157  8.004  1.00 15.59 ? 43   PHE   A CZ   1 
ATOM   703   H  H    . PHE   A 1 43  ? 30.199 46.091  14.045 1.00 14.63 ? 43   PHE   A H    1 
ATOM   704   H  HA   . PHE   A 1 43  ? 30.894 45.943  11.511 1.00 15.19 ? 43   PHE   A HA   1 
ATOM   705   H  HB2  . PHE   A 1 43  ? 28.678 46.387  12.519 1.00 16.33 ? 43   PHE   A HB2  1 
ATOM   706   H  HB3  . PHE   A 1 43  ? 29.092 47.887  12.412 1.00 16.33 ? 43   PHE   A HB3  1 
ATOM   707   H  HD1  . PHE   A 1 43  ? 30.427 46.714  9.651  1.00 17.70 ? 43   PHE   A HD1  1 
ATOM   708   H  HD2  . PHE   A 1 43  ? 26.765 47.420  11.085 1.00 19.01 ? 43   PHE   A HD2  1 
ATOM   709   H  HE1  . PHE   A 1 43  ? 29.595 46.800  7.498  1.00 20.78 ? 43   PHE   A HE1  1 
ATOM   710   H  HE2  . PHE   A 1 43  ? 25.938 47.498  8.931  1.00 17.20 ? 43   PHE   A HE2  1 
ATOM   711   H  HZ   . PHE   A 1 43  ? 27.352 47.190  7.136  1.00 18.71 ? 43   PHE   A HZ   1 
ATOM   712   N  N    . ASP   A 1 44  ? 31.811 48.621  12.972 1.00 17.06 ? 44   ASP   A N    1 
ATOM   713   C  CA   . ASP   A 1 44  ? 32.663 49.829  12.842 1.00 15.53 ? 44   ASP   A CA   1 
ATOM   714   C  C    . ASP   A 1 44  ? 34.148 49.469  12.803 1.00 17.29 ? 44   ASP   A C    1 
ATOM   715   O  O    . ASP   A 1 44  ? 34.920 50.286  12.296 1.00 18.23 ? 44   ASP   A O    1 
ATOM   716   C  CB   . ASP   A 1 44  ? 32.442 50.772  14.023 1.00 15.99 ? 44   ASP   A CB   1 
ATOM   717   C  CG   . ASP   A 1 44  ? 31.123 51.522  13.988 1.00 17.69 ? 44   ASP   A CG   1 
ATOM   718   O  OD1  . ASP   A 1 44  ? 30.487 51.532  12.922 1.00 18.89 ? 44   ASP   A OD1  1 
ATOM   719   O  OD2  . ASP   A 1 44  ? 30.751 52.092  15.028 1.00 18.57 ? 44   ASP   A OD2  1 
ATOM   720   H  H    . ASP   A 1 44  ? 31.463 48.506  13.750 1.00 20.48 ? 44   ASP   A H    1 
ATOM   721   H  HA   . ASP   A 1 44  ? 32.411 50.259  12.010 1.00 18.64 ? 44   ASP   A HA   1 
ATOM   722   H  HB2  . ASP   A 1 44  ? 32.488 50.259  14.845 1.00 19.19 ? 44   ASP   A HB2  1 
ATOM   723   H  HB3  . ASP   A 1 44  ? 33.167 51.416  14.049 1.00 19.19 ? 44   ASP   A HB3  1 
ATOM   724   N  N    . GLU   A 1 45  ? 34.530 48.292  13.296 1.00 15.89 ? 45   GLU   A N    1 
ATOM   725   C  CA   . GLU   A 1 45  ? 35.985 47.996  13.420 1.00 17.10 ? 45   GLU   A CA   1 
ATOM   726   C  C    . GLU   A 1 45  ? 36.450 46.852  12.511 1.00 17.92 ? 45   GLU   A C    1 
ATOM   727   O  O    . GLU   A 1 45  ? 37.657 46.586  12.503 1.00 20.99 ? 45   GLU   A O    1 
ATOM   728   C  CB   . GLU   A 1 45  ? 36.308 47.667  14.880 1.00 16.67 ? 45   GLU   A CB   1 
ATOM   729   C  CG   . GLU   A 1 45  ? 35.927 48.774  15.845 1.00 18.83 ? 45   GLU   A CG   1 
ATOM   730   C  CD   . GLU   A 1 45  ? 36.525 48.646  17.236 1.00 18.85 ? 45   GLU   A CD   1 
ATOM   731   O  OE1  . GLU   A 1 45  ? 37.251 47.665  17.477 1.00 16.78 ? 45   GLU   A OE1  1 
ATOM   732   O  OE2  . GLU   A 1 45  ? 36.259 49.527  18.072 1.00 18.54 ? 45   GLU   A OE2  1 
ATOM   733   H  H    . GLU   A 1 45  ? 34.000 47.667  13.558 1.00 19.07 ? 45   GLU   A H    1 
ATOM   734   H  HA   . GLU   A 1 45  ? 36.465 48.788  13.132 1.00 20.52 ? 45   GLU   A HA   1 
ATOM   735   H  HB2  . GLU   A 1 45  ? 35.844 46.853  15.132 1.00 20.01 ? 45   GLU   A HB2  1 
ATOM   736   H  HB3  . GLU   A 1 45  ? 37.258 47.488  14.962 1.00 20.01 ? 45   GLU   A HB3  1 
ATOM   737   H  HG2  . GLU   A 1 45  ? 36.202 49.624  15.466 1.00 22.60 ? 45   GLU   A HG2  1 
ATOM   738   H  HG3  . GLU   A 1 45  ? 34.961 48.798  15.924 1.00 22.60 ? 45   GLU   A HG3  1 
ATOM   739   N  N    . ILE   A 1 46  ? 35.552 46.191  11.782 1.00 14.90 ? 46   ILE   A N    1 
ATOM   740   C  CA   . ILE   A 1 46  ? 36.076 45.131  10.875 1.00 15.08 ? 46   ILE   A CA   1 
ATOM   741   C  C    . ILE   A 1 46  ? 35.439 45.213  9.486  1.00 18.14 ? 46   ILE   A C    1 
ATOM   742   O  O    . ILE   A 1 46  ? 34.376 45.846  9.354  1.00 14.69 ? 46   ILE   A O    1 
ATOM   743   C  CB   . ILE   A 1 46  ? 35.865 43.719  11.467 1.00 17.53 ? 46   ILE   A CB   1 
ATOM   744   C  CG1  . ILE   A 1 46  ? 34.406 43.272  11.346 1.00 17.80 ? 46   ILE   A CG1  1 
ATOM   745   C  CG2  . ILE   A 1 46  ? 36.365 43.635  12.900 1.00 16.45 ? 46   ILE   A CG2  1 
ATOM   746   C  CD1  . ILE   A 1 46  ? 34.231 41.776  11.243 1.00 17.06 ? 46   ILE   A CD1  1 
ATOM   747   H  H    . ILE   A 1 46  ? 34.701 46.315  11.783 1.00 17.89 ? 46   ILE   A H    1 
ATOM   748   H  HA   . ILE   A 1 46  ? 37.029 45.288  10.786 1.00 18.10 ? 46   ILE   A HA   1 
ATOM   749   H  HB   . ILE   A 1 46  ? 36.397 43.101  10.942 1.00 21.04 ? 46   ILE   A HB   1 
ATOM   750   H  HG12 . ILE   A 1 46  ? 33.913 43.594  12.117 1.00 21.37 ? 46   ILE   A HG12 1 
ATOM   751   H  HG13 . ILE   A 1 46  ? 34.013 43.689  10.564 1.00 21.37 ? 46   ILE   A HG13 1 
ATOM   752   H  HG21 . ILE   A 1 46  ? 36.219 42.739  13.242 1.00 19.75 ? 46   ILE   A HG21 1 
ATOM   753   H  HG22 . ILE   A 1 46  ? 37.313 43.839  12.925 1.00 19.75 ? 46   ILE   A HG22 1 
ATOM   754   H  HG23 . ILE   A 1 46  ? 35.883 44.273  13.449 1.00 19.75 ? 46   ILE   A HG23 1 
ATOM   755   H  HD11 . ILE   A 1 46  ? 33.287 41.565  11.170 1.00 20.48 ? 46   ILE   A HD11 1 
ATOM   756   H  HD12 . ILE   A 1 46  ? 34.697 41.449  10.458 1.00 20.48 ? 46   ILE   A HD12 1 
ATOM   757   H  HD13 . ILE   A 1 46  ? 34.596 41.352  12.035 1.00 20.48 ? 46   ILE   A HD13 1 
ATOM   758   N  N    . ASP   A 1 47  ? 36.105 44.626  8.496  1.00 16.54 ? 47   ASP   A N    1 
ATOM   759   C  CA   . ASP   A 1 47  ? 35.500 44.492  7.152  1.00 18.09 ? 47   ASP   A CA   1 
ATOM   760   C  C    . ASP   A 1 47  ? 34.731 43.169  7.182  1.00 18.34 ? 47   ASP   A C    1 
ATOM   761   O  O    . ASP   A 1 47  ? 35.377 42.123  7.298  1.00 14.98 ? 47   ASP   A O    1 
ATOM   762   C  CB   . ASP   A 1 47  ? 36.572 44.526  6.067  1.00 18.72 ? 47   ASP   A CB   1 
ATOM   763   C  CG   . ASP   A 1 47  ? 36.148 43.887  4.754  1.00 19.38 ? 47   ASP   A CG   1 
ATOM   764   O  OD1  . ASP   A 1 47  ? 34.937 43.860  4.476  1.00 21.31 ? 47   ASP   A OD1  1 
ATOM   765   O  OD2  . ASP   A 1 47  ? 37.038 43.423  4.020  1.00 26.98 ? 47   ASP   A OD2  1 
ATOM   766   H  H    . ASP   A 1 47  ? 36.897 44.300  8.570  1.00 19.85 ? 47   ASP   A H    1 
ATOM   767   H  HA   . ASP   A 1 47  ? 34.904 45.227  6.940  1.00 21.71 ? 47   ASP   A HA   1 
ATOM   768   H  HB2  . ASP   A 1 47  ? 36.821 45.449  5.901  1.00 22.47 ? 47   ASP   A HB2  1 
ATOM   769   H  HB3  . ASP   A 1 47  ? 37.365 44.073  6.395  1.00 22.47 ? 47   ASP   A HB3  1 
ATOM   770   N  N    . PRO   A 1 48  ? 33.386 43.176  7.138  1.00 17.17 ? 48   PRO   A N    1 
ATOM   771   C  CA   . PRO   A 1 48  ? 32.601 41.936  7.284  1.00 15.76 ? 48   PRO   A CA   1 
ATOM   772   C  C    . PRO   A 1 48  ? 32.905 40.796  6.296  1.00 16.46 ? 48   PRO   A C    1 
ATOM   773   O  O    . PRO   A 1 48  ? 32.470 39.700  6.544  1.00 15.68 ? 48   PRO   A O    1 
ATOM   774   C  CB   . PRO   A 1 48  ? 31.160 42.440  7.090  1.00 15.89 ? 48   PRO   A CB   1 
ATOM   775   C  CG   . PRO   A 1 48  ? 31.219 43.898  7.475  1.00 19.42 ? 48   PRO   A CG   1 
ATOM   776   C  CD   . PRO   A 1 48  ? 32.554 44.361  6.934  1.00 17.36 ? 48   PRO   A CD   1 
ATOM   777   H  HA   . PRO   A 1 48  ? 32.804 41.517  8.135  1.00 18.92 ? 48   PRO   A HA   1 
ATOM   778   H  HB2  . PRO   A 1 48  ? 30.866 42.328  6.172  1.00 19.07 ? 48   PRO   A HB2  1 
ATOM   779   H  HB3  . PRO   A 1 48  ? 30.536 41.951  7.649  1.00 19.07 ? 48   PRO   A HB3  1 
ATOM   780   H  HG2  . PRO   A 1 48  ? 30.485 44.399  7.087  1.00 23.30 ? 48   PRO   A HG2  1 
ATOM   781   H  HG3  . PRO   A 1 48  ? 31.165 44.015  8.436  1.00 23.30 ? 48   PRO   A HG3  1 
ATOM   782   H  HD2  . PRO   A 1 48  ? 32.500 44.611  5.998  1.00 20.84 ? 48   PRO   A HD2  1 
ATOM   783   H  HD3  . PRO   A 1 48  ? 32.894 45.132  7.415  1.00 20.84 ? 48   PRO   A HD3  1 
ATOM   784   N  N    . LYS   A 1 49  ? 33.653 41.081  5.228  1.00 16.93 ? 49   LYS   A N    1 
ATOM   785   C  CA   . LYS   A 1 49  ? 33.979 40.051  4.207  1.00 19.16 ? 49   LYS   A CA   1 
ATOM   786   C  C    . LYS   A 1 49  ? 35.111 39.150  4.705  1.00 18.78 ? 49   LYS   A C    1 
ATOM   787   O  O    . LYS   A 1 49  ? 35.354 38.111  4.074  1.00 21.35 ? 49   LYS   A O    1 
ATOM   788   C  CB   . LYS   A 1 49  ? 34.431 40.721  2.907  1.00 19.58 ? 49   LYS   A CB   1 
ATOM   789   C  CG   . LYS   A 1 49  ? 33.383 41.580  2.216  1.00 22.09 ? 49   LYS   A CG   1 
ATOM   790   C  CD   . LYS   A 1 49  ? 33.765 41.955  0.802  1.00 24.36 ? 49   LYS   A CD   1 
ATOM   791   C  CE   . LYS   A 1 49  ? 35.221 42.348  0.662  1.00 24.18 ? 49   LYS   A CE   1 
ATOM   792   N  NZ   . LYS   A 1 49  ? 35.482 43.693  1.225  1.00 22.77 ? 49   LYS   A NZ   1 
ATOM   793   H  H    . LYS   A 1 49  ? 33.985 41.858  5.067  1.00 20.31 ? 49   LYS   A H    1 
ATOM   794   H  HA   . LYS   A 1 49  ? 33.182 39.522  4.048  1.00 22.99 ? 49   LYS   A HA   1 
ATOM   795   H  HB2  . LYS   A 1 49  ? 35.205 41.273  3.098  1.00 23.50 ? 49   LYS   A HB2  1 
ATOM   796   H  HB3  . LYS   A 1 49  ? 34.720 40.031  2.289  1.00 23.50 ? 49   LYS   A HB3  1 
ATOM   797   H  HG2  . LYS   A 1 49  ? 32.539 41.102  2.202  1.00 26.51 ? 49   LYS   A HG2  1 
ATOM   798   H  HG3  . LYS   A 1 49  ? 33.243 42.389  2.733  1.00 26.51 ? 49   LYS   A HG3  1 
ATOM   799   H  HD2  . LYS   A 1 49  ? 33.580 41.206  0.214  1.00 29.24 ? 49   LYS   A HD2  1 
ATOM   800   H  HD3  . LYS   A 1 49  ? 33.207 42.692  0.507  1.00 29.24 ? 49   LYS   A HD3  1 
ATOM   801   H  HE2  . LYS   A 1 49  ? 35.778 41.694  1.113  1.00 29.02 ? 49   LYS   A HE2  1 
ATOM   802   H  HE3  . LYS   A 1 49  ? 35.471 42.335  -0.275 1.00 29.02 ? 49   LYS   A HE3  1 
ATOM   803   H  HZ1  . LYS   A 1 49  ? 35.990 44.158  0.661  1.00 27.33 ? 49   LYS   A HZ1  1 
ATOM   804   H  HZ2  . LYS   A 1 49  ? 34.710 44.119  1.348  1.00 27.33 ? 49   LYS   A HZ2  1 
ATOM   805   H  HZ3  . LYS   A 1 49  ? 35.903 43.612  2.005  1.00 27.33 ? 49   LYS   A HZ3  1 
ATOM   806   N  N    . ILE   A 1 50  ? 35.775 39.536  5.791  1.00 17.22 ? 50   ILE   A N    1 
ATOM   807   C  CA   . ILE   A 1 50  ? 36.972 38.770  6.246  1.00 16.27 ? 50   ILE   A CA   1 
ATOM   808   C  C    . ILE   A 1 50  ? 36.606 37.346  6.668  1.00 15.05 ? 50   ILE   A C    1 
ATOM   809   O  O    . ILE   A 1 50  ? 35.436 37.115  7.007  1.00 15.07 ? 50   ILE   A O    1 
ATOM   810   C  CB   . ILE   A 1 50  ? 37.664 39.499  7.412  1.00 18.08 ? 50   ILE   A CB   1 
ATOM   811   C  CG1  . ILE   A 1 50  ? 36.727 39.648  8.613  1.00 18.02 ? 50   ILE   A CG1  1 
ATOM   812   C  CG2  . ILE   A 1 50  ? 38.226 40.838  6.962  1.00 22.57 ? 50   ILE   A CG2  1 
ATOM   813   C  CD1  . ILE   A 1 50  ? 37.415 40.104  9.876  1.00 23.43 ? 50   ILE   A CD1  1 
ATOM   814   H  H    . ILE   A 1 50  ? 35.569 40.216  6.276  1.00 20.67 ? 50   ILE   A H    1 
ATOM   815   H  HA   . ILE   A 1 50  ? 37.583 38.712  5.495  1.00 19.52 ? 50   ILE   A HA   1 
ATOM   816   H  HB   . ILE   A 1 50  ? 38.412 38.954  7.702  1.00 21.70 ? 50   ILE   A HB   1 
ATOM   817   H  HG12 . ILE   A 1 50  ? 36.028 40.282  8.389  1.00 21.63 ? 50   ILE   A HG12 1 
ATOM   818   H  HG13 . ILE   A 1 50  ? 36.294 38.796  8.781  1.00 21.63 ? 50   ILE   A HG13 1 
ATOM   819   H  HG21 . ILE   A 1 50  ? 38.656 41.277  7.712  1.00 27.09 ? 50   ILE   A HG21 1 
ATOM   820   H  HG22 . ILE   A 1 50  ? 38.875 40.696  6.256  1.00 27.09 ? 50   ILE   A HG22 1 
ATOM   821   H  HG23 . ILE   A 1 50  ? 37.506 41.397  6.630  1.00 27.09 ? 50   ILE   A HG23 1 
ATOM   822   H  HD11 . ILE   A 1 50  ? 36.764 40.176  10.591 1.00 28.12 ? 50   ILE   A HD11 1 
ATOM   823   H  HD12 . ILE   A 1 50  ? 38.097 39.460  10.124 1.00 28.12 ? 50   ILE   A HD12 1 
ATOM   824   H  HD13 . ILE   A 1 50  ? 37.827 40.969  9.726  1.00 28.12 ? 50   ILE   A HD13 1 
ATOM   825   N  N    . ASP   A 1 51  ? 37.591 36.450  6.655  1.00 16.69 ? 51   ASP   A N    1 
ATOM   826   C  CA   . ASP   A 1 51  ? 37.386 35.080  7.184  1.00 17.62 ? 51   ASP   A CA   1 
ATOM   827   C  C    . ASP   A 1 51  ? 37.232 35.207  8.703  1.00 15.63 ? 51   ASP   A C    1 
ATOM   828   O  O    . ASP   A 1 51  ? 38.068 35.888  9.316  1.00 15.89 ? 51   ASP   A O    1 
ATOM   829   C  CB   . ASP   A 1 51  ? 38.553 34.188  6.766  1.00 20.07 ? 51   ASP   A CB   1 
ATOM   830   C  CG   . ASP   A 1 51  ? 38.542 32.789  7.353  1.00 24.27 ? 51   ASP   A CG   1 
ATOM   831   O  OD1  . ASP   A 1 51  ? 37.664 32.502  8.180  1.00 18.79 ? 51   ASP   A OD1  1 
ATOM   832   O  OD2  . ASP   A 1 51  ? 39.442 32.009  6.996  1.00 33.20 ? 51   ASP   A OD2  1 
ATOM   833   H  H    . ASP   A 1 51  ? 38.380 36.603  6.350  1.00 20.04 ? 51   ASP   A H    1 
ATOM   834   H  HA   . ASP   A 1 51  ? 36.589 34.660  6.825  1.00 21.15 ? 51   ASP   A HA   1 
ATOM   835   H  HB2  . ASP   A 1 51  ? 38.556 34.117  5.799  1.00 24.09 ? 51   ASP   A HB2  1 
ATOM   836   H  HB3  . ASP   A 1 51  ? 39.381 34.623  7.021  1.00 24.09 ? 51   ASP   A HB3  1 
ATOM   837   N  N    . ALA   A 1 52  ? 36.207 34.579  9.280  1.00 15.49 ? 52   ALA   A N    1 
ATOM   838   C  CA   . ALA   A 1 52  ? 35.927 34.728  10.727 1.00 17.27 ? 52   ALA   A CA   1 
ATOM   839   C  C    . ALA   A 1 52  ? 37.040 34.124  11.596 1.00 12.66 ? 52   ALA   A C    1 
ATOM   840   O  O    . ALA   A 1 52  ? 37.080 34.438  12.794 1.00 11.61 ? 52   ALA   A O    1 
ATOM   841   C  CB   . ALA   A 1 52  ? 34.597 34.091  11.038 1.00 12.98 ? 52   ALA   A CB   1 
ATOM   842   H  H    . ALA   A 1 52  ? 35.660 34.064  8.862  1.00 18.59 ? 52   ALA   A H    1 
ATOM   843   H  HA   . ALA   A 1 52  ? 35.895 35.674  10.938 1.00 20.73 ? 52   ALA   A HA   1 
ATOM   844   H  HB1  . ALA   A 1 52  ? 34.407 34.185  11.985 1.00 15.58 ? 52   ALA   A HB1  1 
ATOM   845   H  HB2  . ALA   A 1 52  ? 33.900 34.528  10.524 1.00 15.58 ? 52   ALA   A HB2  1 
ATOM   846   H  HB3  . ALA   A 1 52  ? 34.627 33.150  10.806 1.00 15.58 ? 52   ALA   A HB3  1 
ATOM   847   N  N    . LEU   A 1 53  ? 37.887 33.280  11.011 1.00 14.28 ? 53   LEU   A N    1 
ATOM   848   C  CA   . LEU   A 1 53  ? 38.993 32.649  11.784 1.00 16.15 ? 53   LEU   A CA   1 
ATOM   849   C  C    . LEU   A 1 53  ? 40.298 33.421  11.547 1.00 14.90 ? 53   LEU   A C    1 
ATOM   850   O  O    . LEU   A 1 53  ? 41.316 33.022  12.121 1.00 14.95 ? 53   LEU   A O    1 
ATOM   851   C  CB   . LEU   A 1 53  ? 39.109 31.175  11.389 1.00 14.89 ? 53   LEU   A CB   1 
ATOM   852   C  CG   . LEU   A 1 53  ? 37.876 30.335  11.720 1.00 15.36 ? 53   LEU   A CG   1 
ATOM   853   C  CD1  . LEU   A 1 53  ? 38.083 28.878  11.341 1.00 16.77 ? 53   LEU   A CD1  1 
ATOM   854   C  CD2  . LEU   A 1 53  ? 37.517 30.459  13.191 1.00 13.07 ? 53   LEU   A CD2  1 
ATOM   855   H  H    . LEU   A 1 53  ? 37.852 33.054  10.182 1.00 17.14 ? 53   LEU   A H    1 
ATOM   856   H  HA   . LEU   A 1 53  ? 38.805 32.686  12.735 1.00 19.39 ? 53   LEU   A HA   1 
ATOM   857   H  HB2  . LEU   A 1 53  ? 39.279 31.119  10.436 1.00 17.87 ? 53   LEU   A HB2  1 
ATOM   858   H  HB3  . LEU   A 1 53  ? 39.879 30.791  11.837 1.00 17.87 ? 53   LEU   A HB3  1 
ATOM   859   H  HG   . LEU   A 1 53  ? 37.136 30.678  11.194 1.00 18.44 ? 53   LEU   A HG   1 
ATOM   860   H  HD11 . LEU   A 1 53  ? 37.287 28.370  11.562 1.00 20.13 ? 53   LEU   A HD11 1 
ATOM   861   H  HD12 . LEU   A 1 53  ? 38.254 28.812  10.389 1.00 20.13 ? 53   LEU   A HD12 1 
ATOM   862   H  HD13 . LEU   A 1 53  ? 38.840 28.521  11.831 1.00 20.13 ? 53   LEU   A HD13 1 
ATOM   863   H  HD21 . LEU   A 1 53  ? 36.733 29.919  13.380 1.00 15.69 ? 53   LEU   A HD21 1 
ATOM   864   H  HD22 . LEU   A 1 53  ? 38.260 30.150  13.733 1.00 15.69 ? 53   LEU   A HD22 1 
ATOM   865   H  HD23 . LEU   A 1 53  ? 37.328 31.387  13.401 1.00 15.69 ? 53   LEU   A HD23 1 
ATOM   866   N  N    . SER   A 1 54  ? 40.252 34.484  10.744 1.00 14.65 ? 54   SER   A N    1 
ATOM   867   C  CA   . SER   A 1 54  ? 41.447 35.344  10.536 1.00 14.64 ? 54   SER   A CA   1 
ATOM   868   C  C    . SER   A 1 54  ? 41.668 36.193  11.789 1.00 14.39 ? 54   SER   A C    1 
ATOM   869   O  O    . SER   A 1 54  ? 40.691 36.514  12.471 1.00 14.76 ? 54   SER   A O    1 
ATOM   870   C  CB   . SER   A 1 54  ? 41.278 36.231  9.323  1.00 16.02 ? 54   SER   A CB   1 
ATOM   871   O  OG   . SER   A 1 54  ? 40.407 37.312  9.603  1.00 17.97 ? 54   SER   A OG   1 
ATOM   872   H  H    . SER   A 1 54  ? 39.552 34.732  10.310 1.00 17.59 ? 54   SER   A H    1 
ATOM   873   H  HA   . SER   A 1 54  ? 42.220 34.779  10.379 1.00 17.57 ? 54   SER   A HA   1 
ATOM   874   H  HB2  . SER   A 1 54  ? 42.142 36.571  9.044  1.00 19.23 ? 54   SER   A HB2  1 
ATOM   875   H  HB3  . SER   A 1 54  ? 40.926 35.711  8.584  1.00 19.23 ? 54   SER   A HB3  1 
ATOM   876   H  HG   . SER   A 1 54  ? 39.610 37.049  9.557  1.00 21.56 ? 54   SER   A HG   1 
ATOM   877   N  N    . PRO   A 1 55  ? 42.922 36.569  12.107 1.00 14.23 ? 55   PRO   A N    1 
ATOM   878   C  CA   . PRO   A 1 55  ? 43.200 37.400  13.272 1.00 16.83 ? 55   PRO   A CA   1 
ATOM   879   C  C    . PRO   A 1 55  ? 42.439 38.732  13.211 1.00 17.16 ? 55   PRO   A C    1 
ATOM   880   O  O    . PRO   A 1 55  ? 42.284 39.352  14.234 1.00 16.03 ? 55   PRO   A O    1 
ATOM   881   C  CB   . PRO   A 1 55  ? 44.710 37.658  13.158 1.00 17.33 ? 55   PRO   A CB   1 
ATOM   882   C  CG   . PRO   A 1 55  ? 45.229 36.473  12.380 1.00 20.08 ? 55   PRO   A CG   1 
ATOM   883   C  CD   . PRO   A 1 55  ? 44.132 36.181  11.381 1.00 21.79 ? 55   PRO   A CD   1 
ATOM   884   H  HA   . PRO   A 1 55  ? 42.930 36.977  14.102 1.00 20.20 ? 55   PRO   A HA   1 
ATOM   885   H  HB2  . PRO   A 1 55  ? 44.894 38.492  12.698 1.00 20.80 ? 55   PRO   A HB2  1 
ATOM   886   H  HB3  . PRO   A 1 55  ? 45.126 37.718  14.032 1.00 20.80 ? 55   PRO   A HB3  1 
ATOM   887   H  HG2  . PRO   A 1 55  ? 46.067 36.679  11.937 1.00 24.10 ? 55   PRO   A HG2  1 
ATOM   888   H  HG3  . PRO   A 1 55  ? 45.393 35.712  12.959 1.00 24.10 ? 55   PRO   A HG3  1 
ATOM   889   H  HD2  . PRO   A 1 55  ? 44.242 36.694  10.565 1.00 26.15 ? 55   PRO   A HD2  1 
ATOM   890   H  HD3  . PRO   A 1 55  ? 44.115 35.245  11.128 1.00 26.15 ? 55   PRO   A HD3  1 
ATOM   891   N  N    . GLU   A 1 56  ? 42.003 39.140  12.014 1.00 15.61 ? 56   GLU   A N    1 
ATOM   892   C  CA   . GLU   A 1 56  ? 41.349 40.468  11.846 1.00 18.80 ? 56   GLU   A CA   1 
ATOM   893   C  C    . GLU   A 1 56  ? 39.926 40.447  12.412 1.00 17.15 ? 56   GLU   A C    1 
ATOM   894   O  O    . GLU   A 1 56  ? 39.364 41.528  12.616 1.00 15.41 ? 56   GLU   A O    1 
ATOM   895   C  CB   . GLU   A 1 56  ? 41.376 40.900  10.378 1.00 17.28 ? 56   GLU   A CB   1 
ATOM   896   C  CG   . GLU   A 1 56  ? 42.759 41.293  9.899  1.00 21.10 ? 56   GLU   A CG   1 
ATOM   897   C  CD   . GLU   A 1 56  ? 43.767 40.157  9.900  1.00 22.91 ? 56   GLU   A CD   1 
ATOM   898   O  OE1  . GLU   A 1 56  ? 43.439 39.078  9.376  1.00 20.63 ? 56   GLU   A OE1  1 
ATOM   899   O  OE2  . GLU   A 1 56  ? 44.874 40.356  10.430 1.00 20.74 ? 56   GLU   A OE2  1 
ATOM   900   H  H    . GLU   A 1 56  ? 42.070 38.679  11.291 1.00 18.74 ? 56   GLU   A H    1 
ATOM   901   H  HA   . GLU   A 1 56  ? 41.849 41.128  12.351 1.00 22.57 ? 56   GLU   A HA   1 
ATOM   902   H  HB2  . GLU   A 1 56  ? 41.043 40.175  9.827  1.00 20.74 ? 56   GLU   A HB2  1 
ATOM   903   H  HB3  . GLU   A 1 56  ? 40.772 41.649  10.256 1.00 20.74 ? 56   GLU   A HB3  1 
ATOM   904   H  HG2  . GLU   A 1 56  ? 42.689 41.649  8.999  1.00 25.32 ? 56   GLU   A HG2  1 
ATOM   905   H  HG3  . GLU   A 1 56  ? 43.093 42.009  10.462 1.00 25.32 ? 56   GLU   A HG3  1 
ATOM   906   N  N    . ASN   A 1 57  ? 39.379 39.258  12.658 1.00 15.29 ? 57   ASN   A N    1 
ATOM   907   C  CA   . ASN   A 1 57  ? 38.057 39.197  13.329 1.00 15.89 ? 57   ASN   A CA   1 
ATOM   908   C  C    . ASN   A 1 57  ? 38.223 39.768  14.739 1.00 15.50 ? 57   ASN   A C    1 
ATOM   909   O  O    . ASN   A 1 57  ? 39.353 39.755  15.245 1.00 15.22 ? 57   ASN   A O    1 
ATOM   910   C  CB   . ASN   A 1 57  ? 37.494 37.773  13.349 1.00 14.16 ? 57   ASN   A CB   1 
ATOM   911   C  CG   . ASN   A 1 57  ? 36.023 37.706  13.701 1.00 12.81 ? 57   ASN   A CG   1 
ATOM   912   O  OD1  . ASN   A 1 57  ? 35.387 38.729  13.937 1.00 12.68 ? 57   ASN   A OD1  1 
ATOM   913   N  ND2  . ASN   A 1 57  ? 35.479 36.502  13.744 1.00 12.36 ? 57   ASN   A ND2  1 
ATOM   914   H  H    . ASN   A 1 57  ? 39.730 38.499  12.459 1.00 18.35 ? 57   ASN   A H    1 
ATOM   915   H  HA   . ASN   A 1 57  ? 37.410 39.725  12.835 1.00 19.07 ? 57   ASN   A HA   1 
ATOM   916   H  HB2  . ASN   A 1 57  ? 37.629 37.368  12.478 1.00 17.00 ? 57   ASN   A HB2  1 
ATOM   917   H  HB3  . ASN   A 1 57  ? 37.996 37.244  13.989 1.00 17.00 ? 57   ASN   A HB3  1 
ATOM   918   H  HD21 . ASN   A 1 57  ? 34.647 36.413  13.944 1.00 14.84 ? 57   ASN   A HD21 1 
ATOM   919   H  HD22 . ASN   A 1 57  ? 35.957 35.808  13.572 1.00 14.84 ? 57   ASN   A HD22 1 
ATOM   920   N  N    . LYS   A 1 58  ? 37.144 40.282  15.326 1.00 13.93 ? 58   LYS   A N    1 
ATOM   921   C  CA   . LYS   A 1 58  ? 37.214 40.759  16.730 1.00 12.72 ? 58   LYS   A CA   1 
ATOM   922   C  C    . LYS   A 1 58  ? 36.282 39.900  17.585 1.00 11.15 ? 58   LYS   A C    1 
ATOM   923   O  O    . LYS   A 1 58  ? 35.162 39.623  17.135 1.00 13.34 ? 58   LYS   A O    1 
ATOM   924   C  CB   . LYS   A 1 58  ? 36.882 42.250  16.835 1.00 14.48 ? 58   LYS   A CB   1 
ATOM   925   C  CG   . LYS   A 1 58  ? 37.728 43.149  15.943 1.00 17.04 ? 58   LYS   A CG   1 
ATOM   926   C  CD   . LYS   A 1 58  ? 38.268 44.381  16.632 1.00 16.94 ? 58   LYS   A CD   1 
ATOM   927   C  CE   . LYS   A 1 58  ? 39.250 45.148  15.771 1.00 16.63 ? 58   LYS   A CE   1 
ATOM   928   N  NZ   . LYS   A 1 58  ? 39.467 46.525  16.272 1.00 21.79 ? 58   LYS   A NZ   1 
ATOM   929   H  H    . LYS   A 1 58  ? 36.375 40.367  14.950 1.00 16.72 ? 58   LYS   A H    1 
ATOM   930   H  HA   . LYS   A 1 58  ? 38.121 40.665  17.060 1.00 15.26 ? 58   LYS   A HA   1 
ATOM   931   H  HB2  . LYS   A 1 58  ? 35.947 42.378  16.611 1.00 17.37 ? 58   LYS   A HB2  1 
ATOM   932   H  HB3  . LYS   A 1 58  ? 36.994 42.531  17.757 1.00 17.37 ? 58   LYS   A HB3  1 
ATOM   933   H  HG2  . LYS   A 1 58  ? 38.473 42.633  15.596 1.00 20.46 ? 58   LYS   A HG2  1 
ATOM   934   H  HG3  . LYS   A 1 58  ? 37.194 43.425  15.181 1.00 20.46 ? 58   LYS   A HG3  1 
ATOM   935   H  HD2  . LYS   A 1 58  ? 37.530 44.963  16.871 1.00 20.33 ? 58   LYS   A HD2  1 
ATOM   936   H  HD3  . LYS   A 1 58  ? 38.703 44.120  17.459 1.00 20.33 ? 58   LYS   A HD3  1 
ATOM   937   H  HE2  . LYS   A 1 58  ? 40.097 44.676  15.748 1.00 19.96 ? 58   LYS   A HE2  1 
ATOM   938   H  HE3  . LYS   A 1 58  ? 38.921 45.184  14.859 1.00 19.96 ? 58   LYS   A HE3  1 
ATOM   939   H  HZ1  . LYS   A 1 58  ? 39.799 47.030  15.618 1.00 26.16 ? 58   LYS   A HZ1  1 
ATOM   940   H  HZ2  . LYS   A 1 58  ? 38.692 46.867  16.547 1.00 26.16 ? 58   LYS   A HZ2  1 
ATOM   941   H  HZ3  . LYS   A 1 58  ? 40.041 46.507  16.952 1.00 26.16 ? 58   LYS   A HZ3  1 
ATOM   942   N  N    . PHE   A 1 59  ? 36.755 39.497  18.760 1.00 11.53 ? 59   PHE   A N    1 
ATOM   943   C  CA   . PHE   A 1 59  ? 35.946 38.661  19.678 1.00 12.45 ? 59   PHE   A CA   1 
ATOM   944   C  C    . PHE   A 1 59  ? 35.434 39.589  20.774 1.00 11.78 ? 59   PHE   A C    1 
ATOM   945   O  O    . PHE   A 1 59  ? 36.222 40.009  21.633 1.00 12.30 ? 59   PHE   A O    1 
ATOM   946   C  CB   . PHE   A 1 59  ? 36.791 37.499  20.204 1.00 13.58 ? 59   PHE   A CB   1 
ATOM   947   C  CG   . PHE   A 1 59  ? 36.046 36.505  21.055 1.00 11.80 ? 59   PHE   A CG   1 
ATOM   948   C  CD1  . PHE   A 1 59  ? 35.194 35.578  20.479 1.00 10.77 ? 59   PHE   A CD1  1 
ATOM   949   C  CD2  . PHE   A 1 59  ? 36.201 36.493  22.431 1.00 12.10 ? 59   PHE   A CD2  1 
ATOM   950   C  CE1  . PHE   A 1 59  ? 34.511 34.663  21.263 1.00 12.98 ? 59   PHE   A CE1  1 
ATOM   951   C  CE2  . PHE   A 1 59  ? 35.514 35.579  23.212 1.00 15.32 ? 59   PHE   A CE2  1 
ATOM   952   C  CZ   . PHE   A 1 59  ? 34.669 34.667  22.627 1.00 13.16 ? 59   PHE   A CZ   1 
ATOM   953   H  H    . PHE   A 1 59  ? 37.540 39.691  19.054 1.00 13.84 ? 59   PHE   A H    1 
ATOM   954   H  HA   . PHE   A 1 59  ? 35.187 38.249  19.237 1.00 14.95 ? 59   PHE   A HA   1 
ATOM   955   H  HB2  . PHE   A 1 59  ? 37.179 37.031  19.448 1.00 16.30 ? 59   PHE   A HB2  1 
ATOM   956   H  HB3  . PHE   A 1 59  ? 37.527 37.861  20.722 1.00 16.30 ? 59   PHE   A HB3  1 
ATOM   957   H  HD1  . PHE   A 1 59  ? 35.079 35.570  19.556 1.00 12.93 ? 59   PHE   A HD1  1 
ATOM   958   H  HD2  . PHE   A 1 59  ? 36.773 37.105  22.835 1.00 14.52 ? 59   PHE   A HD2  1 
ATOM   959   H  HE1  . PHE   A 1 59  ? 33.943 34.044  20.864 1.00 15.58 ? 59   PHE   A HE1  1 
ATOM   960   H  HE2  . PHE   A 1 59  ? 35.625 35.582  24.135 1.00 18.39 ? 59   PHE   A HE2  1 
ATOM   961   H  HZ   . PHE   A 1 59  ? 34.206 34.055  23.153 1.00 15.80 ? 59   PHE   A HZ   1 
ATOM   962   N  N    . ILE   A 1 60  ? 34.148 39.927  20.728 1.00 10.23 ? 60   ILE   A N    1 
ATOM   963   C  CA   . ILE   A 1 60  ? 33.621 40.925  21.698 1.00 11.25 ? 60   ILE   A CA   1 
ATOM   964   C  C    . ILE   A 1 60  ? 32.743 40.244  22.748 1.00 12.79 ? 60   ILE   A C    1 
ATOM   965   O  O    . ILE   A 1 60  ? 31.873 39.447  22.363 1.00 11.84 ? 60   ILE   A O    1 
ATOM   966   C  CB   . ILE   A 1 60  ? 32.850 42.042  20.964 1.00 10.48 ? 60   ILE   A CB   1 
ATOM   967   C  CG1  . ILE   A 1 60  ? 33.744 42.776  19.961 1.00 11.09 ? 60   ILE   A CG1  1 
ATOM   968   C  CG2  . ILE   A 1 60  ? 32.202 42.994  21.956 1.00 11.14 ? 60   ILE   A CG2  1 
ATOM   969   C  CD1  . ILE   A 1 60  ? 33.001 43.733  19.058 1.00 15.80 ? 60   ILE   A CD1  1 
ATOM   970   H  H    . ILE   A 1 60  ? 33.573 39.612  20.171 1.00 12.28 ? 60   ILE   A H    1 
ATOM   971   H  HA   . ILE   A 1 60  ? 34.371 41.334  22.157 1.00 13.51 ? 60   ILE   A HA   1 
ATOM   972   H  HB   . ILE   A 1 60  ? 32.138 41.628  20.451 1.00 12.57 ? 60   ILE   A HB   1 
ATOM   973   H  HG12 . ILE   A 1 60  ? 34.424 43.268  20.448 1.00 13.31 ? 60   ILE   A HG12 1 
ATOM   974   H  HG13 . ILE   A 1 60  ? 34.205 42.121  19.413 1.00 13.31 ? 60   ILE   A HG13 1 
ATOM   975   H  HG21 . ILE   A 1 60  ? 31.724 43.687  21.475 1.00 13.37 ? 60   ILE   A HG21 1 
ATOM   976   H  HG22 . ILE   A 1 60  ? 31.581 42.504  22.517 1.00 13.37 ? 60   ILE   A HG22 1 
ATOM   977   H  HG23 . ILE   A 1 60  ? 32.887 43.400  22.510 1.00 13.37 ? 60   ILE   A HG23 1 
ATOM   978   H  HD11 . ILE   A 1 60  ? 33.628 44.159  18.453 1.00 18.96 ? 60   ILE   A HD11 1 
ATOM   979   H  HD12 . ILE   A 1 60  ? 32.338 43.245  18.545 1.00 18.96 ? 60   ILE   A HD12 1 
ATOM   980   H  HD13 . ILE   A 1 60  ? 32.560 44.409  19.596 1.00 18.96 ? 60   ILE   A HD13 1 
ATOM   981   N  N    . ILE   A 1 61  ? 33.007 40.528  24.023 1.00 11.24 ? 61   ILE   A N    1 
ATOM   982   C  CA   . ILE   A 1 61  ? 32.115 40.033  25.105 1.00 10.97 ? 61   ILE   A CA   1 
ATOM   983   C  C    . ILE   A 1 61  ? 31.470 41.300  25.657 1.00 9.12  ? 61   ILE   A C    1 
ATOM   984   O  O    . ILE   A 1 61  ? 32.215 42.184  26.106 1.00 10.94 ? 61   ILE   A O    1 
ATOM   985   C  CB   . ILE   A 1 61  ? 32.881 39.230  26.170 1.00 11.39 ? 61   ILE   A CB   1 
ATOM   986   C  CG1  . ILE   A 1 61  ? 33.582 38.013  25.564 1.00 13.11 ? 61   ILE   A CG1  1 
ATOM   987   C  CG2  . ILE   A 1 61  ? 31.957 38.839  27.312 1.00 14.87 ? 61   ILE   A CG2  1 
ATOM   988   C  CD1  . ILE   A 1 61  ? 34.731 37.497  26.397 1.00 18.87 ? 61   ILE   A CD1  1 
ATOM   989   H  H    . ILE   A 1 61  ? 33.679 40.994  24.290 1.00 13.49 ? 61   ILE   A H    1 
ATOM   990   H  HA   . ILE   A 1 61  ? 31.452 39.402  24.784 1.00 13.17 ? 61   ILE   A HA   1 
ATOM   991   H  HB   . ILE   A 1 61  ? 33.577 39.800  26.532 1.00 13.67 ? 61   ILE   A HB   1 
ATOM   992   H  HG12 . ILE   A 1 61  ? 32.933 37.302  25.446 1.00 15.74 ? 61   ILE   A HG12 1 
ATOM   993   H  HG13 . ILE   A 1 61  ? 33.911 38.246  24.682 1.00 15.74 ? 61   ILE   A HG13 1 
ATOM   994   H  HG21 . ILE   A 1 61  ? 32.455 38.334  27.973 1.00 17.85 ? 61   ILE   A HG21 1 
ATOM   995   H  HG22 . ILE   A 1 61  ? 31.594 39.639  27.723 1.00 17.85 ? 61   ILE   A HG22 1 
ATOM   996   H  HG23 . ILE   A 1 61  ? 31.231 38.294  26.969 1.00 17.85 ? 61   ILE   A HG23 1 
ATOM   997   H  HD11 . ILE   A 1 61  ? 35.130 36.729  25.959 1.00 22.65 ? 61   ILE   A HD11 1 
ATOM   998   H  HD12 . ILE   A 1 61  ? 35.398 38.194  26.496 1.00 22.65 ? 61   ILE   A HD12 1 
ATOM   999   H  HD13 . ILE   A 1 61  ? 34.405 37.236  27.272 1.00 22.65 ? 61   ILE   A HD13 1 
ATOM   1000  N  N    . VAL   A 1 62  ? 30.147 41.393  25.587 1.00 10.06 ? 62   VAL   A N    1 
ATOM   1001  C  CA   . VAL   A 1 62  ? 29.499 42.681  25.954 1.00 11.60 ? 62   VAL   A CA   1 
ATOM   1002  C  C    . VAL   A 1 62  ? 28.343 42.453  26.922 1.00 10.54 ? 62   VAL   A C    1 
ATOM   1003  O  O    . VAL   A 1 62  ? 27.620 41.456  26.773 1.00 11.14 ? 62   VAL   A O    1 
ATOM   1004  C  CB   . VAL   A 1 62  ? 29.031 43.422  24.685 1.00 13.16 ? 62   VAL   A CB   1 
ATOM   1005  C  CG1  . VAL   A 1 62  ? 28.117 42.554  23.832 1.00 11.56 ? 62   VAL   A CG1  1 
ATOM   1006  C  CG2  . VAL   A 1 62  ? 28.368 44.752  25.007 1.00 12.32 ? 62   VAL   A CG2  1 
ATOM   1007  H  H    . VAL   A 1 62  ? 29.615 40.763  25.343 1.00 12.07 ? 62   VAL   A H    1 
ATOM   1008  H  HA   . VAL   A 1 62  ? 30.151 43.238  26.407 1.00 13.92 ? 62   VAL   A HA   1 
ATOM   1009  H  HB   . VAL   A 1 62  ? 29.829 43.614  24.169 1.00 15.79 ? 62   VAL   A HB   1 
ATOM   1010  H  HG11 . VAL   A 1 62  ? 27.842 43.049  23.045 1.00 13.88 ? 62   VAL   A HG11 1 
ATOM   1011  H  HG12 . VAL   A 1 62  ? 28.592 41.753  23.560 1.00 13.88 ? 62   VAL   A HG12 1 
ATOM   1012  H  HG13 . VAL   A 1 62  ? 27.333 42.305  24.347 1.00 13.88 ? 62   VAL   A HG13 1 
ATOM   1013  H  HG21 . VAL   A 1 62  ? 28.090 45.183  24.184 1.00 14.78 ? 62   VAL   A HG21 1 
ATOM   1014  H  HG22 . VAL   A 1 62  ? 27.593 44.599  25.569 1.00 14.78 ? 62   VAL   A HG22 1 
ATOM   1015  H  HG23 . VAL   A 1 62  ? 28.998 45.323  25.474 1.00 14.78 ? 62   VAL   A HG23 1 
ATOM   1016  N  N    . THR   A 1 63  ? 28.196 43.367  27.875 1.00 12.30 ? 63   THR   A N    1 
ATOM   1017  C  CA   . THR   A 1 63  ? 27.068 43.287  28.827 1.00 12.93 ? 63   THR   A CA   1 
ATOM   1018  C  C    . THR   A 1 63  ? 26.010 44.326  28.459 1.00 11.82 ? 63   THR   A C    1 
ATOM   1019  O  O    . THR   A 1 63  ? 26.241 45.101  27.522 1.00 12.88 ? 63   THR   A O    1 
ATOM   1020  C  CB   . THR   A 1 63  ? 27.545 43.593  30.248 1.00 14.14 ? 63   THR   A CB   1 
ATOM   1021  O  OG1  . THR   A 1 63  ? 27.948 44.962  30.269 1.00 14.37 ? 63   THR   A OG1  1 
ATOM   1022  C  CG2  . THR   A 1 63  ? 28.694 42.715  30.692 1.00 15.10 ? 63   THR   A CG2  1 
ATOM   1023  H  H    . THR   A 1 63  ? 28.724 44.035  27.995 1.00 14.76 ? 63   THR   A H    1 
ATOM   1024  H  HA   . THR   A 1 63  ? 26.701 42.390  28.785 1.00 15.52 ? 63   THR   A HA   1 
ATOM   1025  H  HB   . THR   A 1 63  ? 26.818 43.415  30.866 1.00 16.98 ? 63   THR   A HB   1 
ATOM   1026  H  HG1  . THR   A 1 63  ? 28.635 45.059  29.796 1.00 17.25 ? 63   THR   A HG1  1 
ATOM   1027  H  HG21 . THR   A 1 63  ? 28.953 42.953  31.596 1.00 18.12 ? 63   THR   A HG21 1 
ATOM   1028  H  HG22 . THR   A 1 63  ? 28.419 41.785  30.669 1.00 18.12 ? 63   THR   A HG22 1 
ATOM   1029  H  HG23 . THR   A 1 63  ? 29.448 42.843  30.096 1.00 18.12 ? 63   THR   A HG23 1 
ATOM   1030  N  N    . GLY   A 1 64  ? 24.896 44.322  29.184 1.00 14.03 ? 64   GLY   A N    1 
ATOM   1031  C  CA   . GLY   A 1 64  ? 23.861 45.345  28.980 1.00 13.51 ? 64   GLY   A CA   1 
ATOM   1032  C  C    . GLY   A 1 64  ? 23.823 46.281  30.177 1.00 13.27 ? 64   GLY   A C    1 
ATOM   1033  O  O    . GLY   A 1 64  ? 24.376 45.935  31.228 1.00 14.48 ? 64   GLY   A O    1 
ATOM   1034  H  H    . GLY   A 1 64  ? 24.716 43.744  29.795 1.00 16.84 ? 64   GLY   A H    1 
ATOM   1035  H  HA2  . GLY   A 1 64  ? 24.046 45.848  28.171 1.00 16.22 ? 64   GLY   A HA2  1 
ATOM   1036  H  HA3  . GLY   A 1 64  ? 22.996 44.923  28.861 1.00 16.22 ? 64   GLY   A HA3  1 
ATOM   1037  N  N    . PRO   A 1 65  ? 23.171 47.450  30.057 1.00 13.01 ? 65   PRO   A N    1 
ATOM   1038  C  CA   . PRO   A 1 65  ? 23.077 48.395  31.170 1.00 15.75 ? 65   PRO   A CA   1 
ATOM   1039  C  C    . PRO   A 1 65  ? 22.412 47.779  32.409 1.00 13.41 ? 65   PRO   A C    1 
ATOM   1040  O  O    . PRO   A 1 65  ? 22.704 48.194  33.498 1.00 13.83 ? 65   PRO   A O    1 
ATOM   1041  C  CB   . PRO   A 1 65  ? 22.213 49.531  30.600 1.00 16.05 ? 65   PRO   A CB   1 
ATOM   1042  C  CG   . PRO   A 1 65  ? 21.506 48.923  29.409 1.00 16.35 ? 65   PRO   A CG   1 
ATOM   1043  C  CD   . PRO   A 1 65  ? 22.487 47.916  28.852 1.00 15.37 ? 65   PRO   A CD   1 
ATOM   1044  H  HA   . PRO   A 1 65  ? 23.951 48.684  31.475 1.00 18.91 ? 65   PRO   A HA   1 
ATOM   1045  H  HB2  . PRO   A 1 65  ? 21.578 49.854  31.258 1.00 19.27 ? 65   PRO   A HB2  1 
ATOM   1046  H  HB3  . PRO   A 1 65  ? 22.758 50.289  30.336 1.00 19.27 ? 65   PRO   A HB3  1 
ATOM   1047  H  HG2  . PRO   A 1 65  ? 20.675 48.497  29.672 1.00 19.63 ? 65   PRO   A HG2  1 
ATOM   1048  H  HG3  . PRO   A 1 65  ? 21.282 49.598  28.750 1.00 19.63 ? 65   PRO   A HG3  1 
ATOM   1049  H  HD2  . PRO   A 1 65  ? 22.038 47.192  28.387 1.00 18.44 ? 65   PRO   A HD2  1 
ATOM   1050  H  HD3  . PRO   A 1 65  ? 23.102 48.321  28.220 1.00 18.44 ? 65   PRO   A HD3  1 
ATOM   1051  N  N    . LEU   A 1 66  ? 21.531 46.799  32.203 1.00 15.05 ? 66   LEU   A N    1 
ATOM   1052  C  CA   . LEU   A 1 66  ? 20.814 46.175  33.345 1.00 15.83 ? 66   LEU   A CA   1 
ATOM   1053  C  C    . LEU   A 1 66  ? 21.587 44.952  33.863 1.00 15.39 ? 66   LEU   A C    1 
ATOM   1054  O  O    . LEU   A 1 66  ? 21.250 44.470  34.949 1.00 12.71 ? 66   LEU   A O    1 
ATOM   1055  C  CB   . LEU   A 1 66  ? 19.402 45.792  32.892 1.00 16.30 ? 66   LEU   A CB   1 
ATOM   1056  C  CG   . LEU   A 1 66  ? 18.538 46.950  32.394 1.00 16.35 ? 66   LEU   A CG   1 
ATOM   1057  C  CD1  . LEU   A 1 66  ? 17.081 46.532  32.282 1.00 19.67 ? 66   LEU   A CD1  1 
ATOM   1058  C  CD2  . LEU   A 1 66  ? 18.672 48.158  33.307 1.00 19.24 ? 66   LEU   A CD2  1 
ATOM   1059  H  H    . LEU   A 1 66  ? 21.330 46.479  31.430 1.00 18.07 ? 66   LEU   A H    1 
ATOM   1060  H  HA   . LEU   A 1 66  ? 20.750 46.806  34.079 1.00 18.99 ? 66   LEU   A HA   1 
ATOM   1061  H  HB2  . LEU   A 1 66  ? 19.473 45.133  32.183 1.00 19.57 ? 66   LEU   A HB2  1 
ATOM   1062  H  HB3  . LEU   A 1 66  ? 18.946 45.363  33.633 1.00 19.57 ? 66   LEU   A HB3  1 
ATOM   1063  H  HG   . LEU   A 1 66  ? 18.854 47.197  31.511 1.00 19.62 ? 66   LEU   A HG   1 
ATOM   1064  H  HD11 . LEU   A 1 66  ? 16.553 47.281  31.965 1.00 23.61 ? 66   LEU   A HD11 1 
ATOM   1065  H  HD12 . LEU   A 1 66  ? 17.003 45.794  31.657 1.00 23.61 ? 66   LEU   A HD12 1 
ATOM   1066  H  HD13 . LEU   A 1 66  ? 16.756 46.253  33.153 1.00 23.61 ? 66   LEU   A HD13 1 
ATOM   1067  H  HD21 . LEU   A 1 66  ? 18.116 48.880  32.973 1.00 23.09 ? 66   LEU   A HD21 1 
ATOM   1068  H  HD22 . LEU   A 1 66  ? 18.387 47.920  34.203 1.00 23.09 ? 66   LEU   A HD22 1 
ATOM   1069  H  HD23 . LEU   A 1 66  ? 19.598 48.447  33.328 1.00 23.09 ? 66   LEU   A HD23 1 
ATOM   1070  N  N    . THR   A 1 67  ? 22.579 44.478  33.105 1.00 14.59 ? 67   THR   A N    1 
ATOM   1071  C  CA   . THR   A 1 67  ? 23.400 43.340  33.591 1.00 15.57 ? 67   THR   A CA   1 
ATOM   1072  C  C    . THR   A 1 67  ? 23.975 43.688  34.970 1.00 14.25 ? 67   THR   A C    1 
ATOM   1073  O  O    . THR   A 1 67  ? 24.657 44.719  35.073 1.00 13.43 ? 67   THR   A O    1 
ATOM   1074  C  CB   . THR   A 1 67  ? 24.489 42.955  32.580 1.00 12.75 ? 67   THR   A CB   1 
ATOM   1075  O  OG1  . THR   A 1 67  ? 23.879 42.604  31.339 1.00 13.44 ? 67   THR   A OG1  1 
ATOM   1076  C  CG2  . THR   A 1 67  ? 25.356 41.813  33.064 1.00 15.05 ? 67   THR   A CG2  1 
ATOM   1077  H  H    . THR   A 1 67  ? 22.795 44.783  32.330 1.00 17.52 ? 67   THR   A H    1 
ATOM   1078  H  HA   . THR   A 1 67  ? 22.838 42.555  33.683 1.00 18.68 ? 67   THR   A HA   1 
ATOM   1079  H  HB   . THR   A 1 67  ? 25.068 43.725  32.468 1.00 15.30 ? 67   THR   A HB   1 
ATOM   1080  H  HG1  . THR   A 1 67  ? 23.968 41.779  31.206 1.00 16.13 ? 67   THR   A HG1  1 
ATOM   1081  H  HG21 . THR   A 1 67  ? 26.026 41.608  32.393 1.00 18.06 ? 67   THR   A HG21 1 
ATOM   1082  H  HG22 . THR   A 1 67  ? 25.795 42.067  33.891 1.00 18.06 ? 67   THR   A HG22 1 
ATOM   1083  H  HG23 . THR   A 1 67  ? 24.804 41.030  33.219 1.00 18.06 ? 67   THR   A HG23 1 
ATOM   1084  N  N    . GLY   A 1 68  ? 23.698 42.860  35.980 1.00 14.18 ? 68   GLY   A N    1 
ATOM   1085  C  CA   . GLY   A 1 68  ? 24.269 43.076  37.325 1.00 13.61 ? 68   GLY   A CA   1 
ATOM   1086  C  C    . GLY   A 1 68  ? 23.428 43.968  38.223 1.00 17.53 ? 68   GLY   A C    1 
ATOM   1087  O  O    . GLY   A 1 68  ? 23.748 44.050  39.419 1.00 15.84 ? 68   GLY   A O    1 
ATOM   1088  H  H    . GLY   A 1 68  ? 23.187 42.172  35.914 1.00 17.02 ? 68   GLY   A H    1 
ATOM   1089  H  HA2  . GLY   A 1 68  ? 24.385 42.216  37.758 1.00 16.34 ? 68   GLY   A HA2  1 
ATOM   1090  H  HA3  . GLY   A 1 68  ? 25.151 43.468  37.232 1.00 16.34 ? 68   GLY   A HA3  1 
ATOM   1091  N  N    . ALA   A 1 69  ? 22.410 44.629  37.669 1.00 16.60 ? 69   ALA   A N    1 
ATOM   1092  C  CA   . ALA   A 1 69  ? 21.506 45.475  38.480 1.00 16.00 ? 69   ALA   A CA   1 
ATOM   1093  C  C    . ALA   A 1 69  ? 20.517 44.594  39.248 1.00 15.18 ? 69   ALA   A C    1 
ATOM   1094  O  O    . ALA   A 1 69  ? 20.217 43.486  38.786 1.00 15.76 ? 69   ALA   A O    1 
ATOM   1095  C  CB   . ALA   A 1 69  ? 20.786 46.460  37.597 1.00 15.62 ? 69   ALA   A CB   1 
ATOM   1096  H  H    . ALA   A 1 69  ? 22.220 44.606  36.831 1.00 19.93 ? 69   ALA   A H    1 
ATOM   1097  H  HA   . ALA   A 1 69  ? 22.029 45.977  39.124 1.00 19.21 ? 69   ALA   A HA   1 
ATOM   1098  H  HB1  . ALA   A 1 69  ? 20.197 47.009  38.138 1.00 18.75 ? 69   ALA   A HB1  1 
ATOM   1099  H  HB2  . ALA   A 1 69  ? 21.433 47.026  37.148 1.00 18.75 ? 69   ALA   A HB2  1 
ATOM   1100  H  HB3  . ALA   A 1 69  ? 20.263 45.980  36.935 1.00 18.75 ? 69   ALA   A HB3  1 
ATOM   1101  N  N    . PRO   A 1 70  ? 20.004 45.051  40.409 1.00 18.95 ? 70   PRO   A N    1 
ATOM   1102  C  CA   . PRO   A 1 70  ? 19.069 44.259  41.211 1.00 16.71 ? 70   PRO   A CA   1 
ATOM   1103  C  C    . PRO   A 1 70  ? 17.679 44.223  40.564 1.00 16.32 ? 70   PRO   A C    1 
ATOM   1104  O  O    . PRO   A 1 70  ? 16.745 44.727  41.153 1.00 17.30 ? 70   PRO   A O    1 
ATOM   1105  C  CB   . PRO   A 1 70  ? 19.074 44.981  42.570 1.00 19.05 ? 70   PRO   A CB   1 
ATOM   1106  C  CG   . PRO   A 1 70  ? 19.395 46.415  42.223 1.00 20.88 ? 70   PRO   A CG   1 
ATOM   1107  C  CD   . PRO   A 1 70  ? 20.329 46.336  41.034 1.00 20.00 ? 70   PRO   A CD   1 
ATOM   1108  H  HA   . PRO   A 1 70  ? 19.319 43.325  41.293 1.00 20.06 ? 70   PRO   A HA   1 
ATOM   1109  H  HB2  . PRO   A 1 70  ? 18.215 44.907  43.014 1.00 22.86 ? 70   PRO   A HB2  1 
ATOM   1110  H  HB3  . PRO   A 1 70  ? 19.737 44.604  43.170 1.00 22.86 ? 70   PRO   A HB3  1 
ATOM   1111  H  HG2  . PRO   A 1 70  ? 18.591 46.911  42.004 1.00 25.07 ? 70   PRO   A HG2  1 
ATOM   1112  H  HG3  . PRO   A 1 70  ? 19.815 46.870  42.969 1.00 25.07 ? 70   PRO   A HG3  1 
ATOM   1113  H  HD2  . PRO   A 1 70  ? 20.187 47.074  40.421 1.00 24.01 ? 70   PRO   A HD2  1 
ATOM   1114  H  HD3  . PRO   A 1 70  ? 21.258 46.371  41.310 1.00 24.01 ? 70   PRO   A HD3  1 
ATOM   1115  N  N    . VAL   A 1 71  ? 17.594 43.641  39.366 1.00 16.05 ? 71   VAL   A N    1 
ATOM   1116  C  CA   . VAL   A 1 71  ? 16.292 43.484  38.659 1.00 15.91 ? 71   VAL   A CA   1 
ATOM   1117  C  C    . VAL   A 1 71  ? 16.233 42.029  38.186 1.00 14.37 ? 71   VAL   A C    1 
ATOM   1118  O  O    . VAL   A 1 71  ? 17.290 41.385  38.137 1.00 12.98 ? 71   VAL   A O    1 
ATOM   1119  C  CB   . VAL   A 1 71  ? 16.168 44.466  37.480 1.00 16.67 ? 71   VAL   A CB   1 
ATOM   1120  C  CG1  . VAL   A 1 71  ? 16.098 45.909  37.954 1.00 20.71 ? 71   VAL   A CG1  1 
ATOM   1121  C  CG2  . VAL   A 1 71  ? 17.294 44.284  36.475 1.00 20.48 ? 71   VAL   A CG2  1 
ATOM   1122  H  H    . VAL   A 1 71  ? 18.270 43.327  38.937 1.00 19.27 ? 71   VAL   A H    1 
ATOM   1123  H  HA   . VAL   A 1 71  ? 15.550 43.688  39.249 1.00 19.09 ? 71   VAL   A HA   1 
ATOM   1124  H  HB   . VAL   A 1 71  ? 15.333 44.260  37.031 1.00 20.01 ? 71   VAL   A HB   1 
ATOM   1125  H  HG11 . VAL   A 1 71  ? 16.021 46.498  37.187 1.00 24.85 ? 71   VAL   A HG11 1 
ATOM   1126  H  HG12 . VAL   A 1 71  ? 15.325 46.024  38.529 1.00 24.85 ? 71   VAL   A HG12 1 
ATOM   1127  H  HG13 . VAL   A 1 71  ? 16.904 46.127  38.449 1.00 24.85 ? 71   VAL   A HG13 1 
ATOM   1128  H  HG21 . VAL   A 1 71  ? 17.185 44.917  35.748 1.00 24.58 ? 71   VAL   A HG21 1 
ATOM   1129  H  HG22 . VAL   A 1 71  ? 18.146 44.438  36.912 1.00 24.58 ? 71   VAL   A HG22 1 
ATOM   1130  H  HG23 . VAL   A 1 71  ? 17.271 43.380  36.123 1.00 24.58 ? 71   VAL   A HG23 1 
ATOM   1131  N  N    . PRO   A 1 72  ? 15.050 41.475  37.857 1.00 15.02 ? 72   PRO   A N    1 
ATOM   1132  C  CA   . PRO   A 1 72  ? 14.964 40.053  37.499 1.00 14.07 ? 72   PRO   A CA   1 
ATOM   1133  C  C    . PRO   A 1 72  ? 15.712 39.622  36.222 1.00 13.32 ? 72   PRO   A C    1 
ATOM   1134  O  O    . PRO   A 1 72  ? 15.546 40.279  35.221 1.00 12.74 ? 72   PRO   A O    1 
ATOM   1135  C  CB   . PRO   A 1 72  ? 13.446 39.831  37.368 1.00 18.16 ? 72   PRO   A CB   1 
ATOM   1136  C  CG   . PRO   A 1 72  ? 12.875 41.201  37.083 1.00 13.34 ? 72   PRO   A CG   1 
ATOM   1137  C  CD   . PRO   A 1 72  ? 13.756 42.158  37.855 1.00 14.50 ? 72   PRO   A CD   1 
ATOM   1138  H  HA   . PRO   A 1 72  ? 15.406 39.509  38.169 1.00 16.89 ? 72   PRO   A HA   1 
ATOM   1139  H  HB2  . PRO   A 1 72  ? 13.242 39.209  36.652 1.00 21.80 ? 72   PRO   A HB2  1 
ATOM   1140  H  HB3  . PRO   A 1 72  ? 13.074 39.458  38.182 1.00 21.80 ? 72   PRO   A HB3  1 
ATOM   1141  H  HG2  . PRO   A 1 72  ? 12.890 41.398  36.133 1.00 16.01 ? 72   PRO   A HG2  1 
ATOM   1142  H  HG3  . PRO   A 1 72  ? 11.951 41.264  37.371 1.00 16.01 ? 72   PRO   A HG3  1 
ATOM   1143  H  HD2  . PRO   A 1 72  ? 13.808 43.026  37.426 1.00 17.40 ? 72   PRO   A HD2  1 
ATOM   1144  H  HD3  . PRO   A 1 72  ? 13.425 42.306  38.755 1.00 17.40 ? 72   PRO   A HD3  1 
ATOM   1145  N  N    . THR   A 1 73  ? 16.539 38.571  36.311 1.00 14.34 ? 73   THR   A N    1 
ATOM   1146  C  CA   . THR   A 1 73  ? 17.246 37.984  35.133 1.00 14.29 ? 73   THR   A CA   1 
ATOM   1147  C  C    . THR   A 1 73  ? 18.375 38.889  34.618 1.00 12.76 ? 73   THR   A C    1 
ATOM   1148  O  O    . THR   A 1 73  ? 18.599 38.888  33.404 1.00 13.53 ? 73   THR   A O    1 
ATOM   1149  C  CB   . THR   A 1 73  ? 16.247 37.575  34.038 1.00 13.78 ? 73   THR   A CB   1 
ATOM   1150  O  OG1  . THR   A 1 73  ? 15.821 38.728  33.311 1.00 14.18 ? 73   THR   A OG1  1 
ATOM   1151  C  CG2  . THR   A 1 73  ? 15.047 36.842  34.597 1.00 14.28 ? 73   THR   A CG2  1 
ATOM   1152  H  H    . THR   A 1 73  ? 16.713 38.171  37.052 1.00 17.22 ? 73   THR   A H    1 
ATOM   1153  H  HA   . THR   A 1 73  ? 17.686 37.171  35.427 1.00 17.15 ? 73   THR   A HA   1 
ATOM   1154  H  HB   . THR   A 1 73  ? 16.706 36.962  33.443 1.00 16.53 ? 73   THR   A HB   1 
ATOM   1155  H  HG1  . THR   A 1 73  ? 15.944 39.415  33.778 1.00 17.02 ? 73   THR   A HG1  1 
ATOM   1156  H  HG21 . THR   A 1 73  ? 14.446 36.605  33.873 1.00 17.14 ? 73   THR   A HG21 1 
ATOM   1157  H  HG22 . THR   A 1 73  ? 15.342 36.036  35.049 1.00 17.14 ? 73   THR   A HG22 1 
ATOM   1158  H  HG23 . THR   A 1 73  ? 14.582 37.415  35.227 1.00 17.14 ? 73   THR   A HG23 1 
ATOM   1159  N  N    . SER   A 1 74  ? 19.105 39.555  35.518 1.00 11.85 ? 74   SER   A N    1 
ATOM   1160  C  CA   . SER   A 1 74  ? 20.159 40.521  35.104 1.00 12.89 ? 74   SER   A CA   1 
ATOM   1161  C  C    . SER   A 1 74  ? 21.537 39.865  34.926 1.00 12.50 ? 74   SER   A C    1 
ATOM   1162  O  O    . SER   A 1 74  ? 22.537 40.593  34.956 1.00 12.37 ? 74   SER   A O    1 
ATOM   1163  C  CB   . SER   A 1 74  ? 20.236 41.660  36.090 1.00 14.43 ? 74   SER   A CB   1 
ATOM   1164  O  OG   . SER   A 1 74  ? 20.602 41.186  37.376 1.00 15.38 ? 74   SER   A OG   1 
ATOM   1165  H  H    . SER   A 1 74  ? 19.014 39.470  36.369 1.00 14.22 ? 74   SER   A H    1 
ATOM   1166  H  HA   . SER   A 1 74  ? 19.903 40.863  34.233 1.00 15.47 ? 74   SER   A HA   1 
ATOM   1167  H  HB2  . SER   A 1 74  ? 20.884 42.315  35.785 1.00 17.31 ? 74   SER   A HB2  1 
ATOM   1168  H  HB3  . SER   A 1 74  ? 19.378 42.111  36.138 1.00 17.31 ? 74   SER   A HB3  1 
ATOM   1169  H  HG   . SER   A 1 74  ? 20.531 41.809  37.935 1.00 18.46 ? 74   SER   A HG   1 
ATOM   1170  N  N    . GLY   A 1 75  ? 21.583 38.550  34.708 1.00 12.45 ? 75   GLY   A N    1 
ATOM   1171  C  CA   . GLY   A 1 75  ? 22.878 37.860  34.567 1.00 12.69 ? 75   GLY   A CA   1 
ATOM   1172  C  C    . GLY   A 1 75  ? 23.264 37.640  33.114 1.00 12.31 ? 75   GLY   A C    1 
ATOM   1173  O  O    . GLY   A 1 75  ? 24.293 37.003  32.886 1.00 14.69 ? 75   GLY   A O    1 
ATOM   1174  H  H    . GLY   A 1 75  ? 20.892 38.043  34.639 1.00 14.94 ? 75   GLY   A H    1 
ATOM   1175  H  HA2  . GLY   A 1 75  ? 23.568 38.381  35.007 1.00 15.23 ? 75   GLY   A HA2  1 
ATOM   1176  H  HA3  . GLY   A 1 75  ? 22.836 37.004  35.021 1.00 15.23 ? 75   GLY   A HA3  1 
ATOM   1177  N  N    . ARG   A 1 76  ? 22.498 38.196  32.169 1.00 11.08 ? 76   ARG   A N    1 
ATOM   1178  C  CA   . ARG   A 1 76  ? 22.733 37.903  30.727 1.00 10.40 ? 76   ARG   A CA   1 
ATOM   1179  C  C    . ARG   A 1 76  ? 23.816 38.783  30.089 1.00 11.93 ? 76   ARG   A C    1 
ATOM   1180  O  O    . ARG   A 1 76  ? 23.886 39.974  30.417 1.00 11.96 ? 76   ARG   A O    1 
ATOM   1181  C  CB   . ARG   A 1 76  ? 21.426 38.046  29.938 1.00 12.06 ? 76   ARG   A CB   1 
ATOM   1182  C  CG   . ARG   A 1 76  ? 20.270 37.221  30.485 1.00 10.41 ? 76   ARG   A CG   1 
ATOM   1183  C  CD   . ARG   A 1 76  ? 20.593 35.751  30.672 1.00 13.77 ? 76   ARG   A CD   1 
ATOM   1184  N  NE   . ARG   A 1 76  ? 20.912 35.084  29.419 1.00 10.56 ? 76   ARG   A NE   1 
ATOM   1185  C  CZ   . ARG   A 1 76  ? 20.812 33.777  29.211 1.00 10.03 ? 76   ARG   A CZ   1 
ATOM   1186  N  NH1  . ARG   A 1 76  ? 20.262 33.000  30.128 1.00 11.88 ? 76   ARG   A NH1  1 
ATOM   1187  N  NH2  . ARG   A 1 76  ? 21.263 33.251  28.086 1.00 12.80 ? 76   ARG   A NH2  1 
ATOM   1188  H  H    . ARG   A 1 76  ? 21.847 38.736  32.326 1.00 13.30 ? 76   ARG   A H    1 
ATOM   1189  H  HA   . ARG   A 1 76  ? 23.055 36.989  30.687 1.00 12.49 ? 76   ARG   A HA   1 
ATOM   1190  H  HB2  . ARG   A 1 76  ? 21.167 38.981  29.929 1.00 14.47 ? 76   ARG   A HB2  1 
ATOM   1191  H  HB3  . ARG   A 1 76  ? 21.587 37.787  29.017 1.00 14.47 ? 76   ARG   A HB3  1 
ATOM   1192  H  HG2  . ARG   A 1 76  ? 19.995 37.593  31.338 1.00 12.50 ? 76   ARG   A HG2  1 
ATOM   1193  H  HG3  . ARG   A 1 76  ? 19.514 37.302  29.883 1.00 12.50 ? 76   ARG   A HG3  1 
ATOM   1194  H  HD2  . ARG   A 1 76  ? 21.343 35.663  31.281 1.00 16.53 ? 76   ARG   A HD2  1 
ATOM   1195  H  HD3  . ARG   A 1 76  ? 19.837 35.308  31.087 1.00 16.53 ? 76   ARG   A HD3  1 
ATOM   1196  H  HE   . ARG   A 1 76  ? 21.185 35.572  28.766 1.00 12.68 ? 76   ARG   A HE   1 
ATOM   1197  H  HH11 . ARG   A 1 76  ? 19.968 33.341  30.861 1.00 14.26 ? 76   ARG   A HH11 1 
ATOM   1198  H  HH12 . ARG   A 1 76  ? 20.198 32.153  29.992 1.00 14.26 ? 76   ARG   A HH12 1 
ATOM   1199  H  HH21 . ARG   A 1 76  ? 21.621 33.756  27.489 1.00 15.36 ? 76   ARG   A HH21 1 
ATOM   1200  H  HH22 . ARG   A 1 76  ? 21.198 32.404  27.951 1.00 15.36 ? 76   ARG   A HH22 1 
ATOM   1201  N  N    . PHE   A 1 77  ? 24.622 38.185  29.210 1.00 11.39 ? 77   PHE   A N    1 
ATOM   1202  C  CA   . PHE   A 1 77  ? 25.654 38.933  28.452 1.00 10.92 ? 77   PHE   A CA   1 
ATOM   1203  C  C    . PHE   A 1 77  ? 25.765 38.235  27.097 1.00 10.38 ? 77   PHE   A C    1 
ATOM   1204  O  O    . PHE   A 1 77  ? 25.087 37.210  26.914 1.00 8.92  ? 77   PHE   A O    1 
ATOM   1205  C  CB   . PHE   A 1 77  ? 26.993 38.960  29.199 1.00 9.89  ? 77   PHE   A CB   1 
ATOM   1206  C  CG   . PHE   A 1 77  ? 27.693 37.633  29.330 1.00 10.96 ? 77   PHE   A CG   1 
ATOM   1207  C  CD1  . PHE   A 1 77  ? 27.276 36.701  30.265 1.00 10.04 ? 77   PHE   A CD1  1 
ATOM   1208  C  CD2  . PHE   A 1 77  ? 28.781 37.323  28.532 1.00 11.77 ? 77   PHE   A CD2  1 
ATOM   1209  C  CE1  . PHE   A 1 77  ? 27.923 35.483  30.389 1.00 11.19 ? 77   PHE   A CE1  1 
ATOM   1210  C  CE2  . PHE   A 1 77  ? 29.428 36.104  28.656 1.00 11.22 ? 77   PHE   A CE2  1 
ATOM   1211  C  CZ   . PHE   A 1 77  ? 28.998 35.187  29.586 1.00 11.13 ? 77   PHE   A CZ   1 
ATOM   1212  H  H    . PHE   A 1 77  ? 24.594 37.344  29.032 1.00 13.67 ? 77   PHE   A H    1 
ATOM   1213  H  HA   . PHE   A 1 77  ? 25.407 39.865  28.342 1.00 13.11 ? 77   PHE   A HA   1 
ATOM   1214  H  HB2  . PHE   A 1 77  ? 27.587 39.577  28.743 1.00 11.87 ? 77   PHE   A HB2  1 
ATOM   1215  H  HB3  . PHE   A 1 77  ? 26.842 39.317  30.088 1.00 11.87 ? 77   PHE   A HB3  1 
ATOM   1216  H  HD1  . PHE   A 1 77  ? 26.553 36.895  30.816 1.00 12.05 ? 77   PHE   A HD1  1 
ATOM   1217  H  HD2  . PHE   A 1 77  ? 29.081 37.941  27.905 1.00 14.12 ? 77   PHE   A HD2  1 
ATOM   1218  H  HE1  . PHE   A 1 77  ? 27.629 34.864  31.017 1.00 13.43 ? 77   PHE   A HE1  1 
ATOM   1219  H  HE2  . PHE   A 1 77  ? 30.154 35.906  28.110 1.00 13.46 ? 77   PHE   A HE2  1 
ATOM   1220  H  HZ   . PHE   A 1 77  ? 29.433 34.370  29.671 1.00 13.36 ? 77   PHE   A HZ   1 
ATOM   1221  N  N    . MET   A 1 78  ? 26.579 38.752  26.184 1.00 10.40 ? 78   MET   A N    1 
ATOM   1222  C  CA   . MET   A 1 78  ? 26.596 38.113  24.848 1.00 10.23 ? 78   MET   A CA   1 
ATOM   1223  C  C    . MET   A 1 78  ? 27.998 38.101  24.248 1.00 8.14  ? 78   MET   A C    1 
ATOM   1224  O  O    . MET   A 1 78  ? 28.830 38.917  24.668 1.00 11.33 ? 78   MET   A O    1 
ATOM   1225  C  CB   . MET   A 1 78  ? 25.653 38.831  23.871 1.00 9.59  ? 78   MET   A CB   1 
ATOM   1226  C  CG   . MET   A 1 78  ? 24.190 38.588  24.176 1.00 12.90 ? 78   MET   A CG   1 
ATOM   1227  S  SD   . MET   A 1 78  ? 23.076 39.321  22.956 1.00 13.98 ? 78   MET   A SD   1 
ATOM   1228  C  CE   . MET   A 1 78  ? 23.608 38.458  21.479 1.00 13.14 ? 78   MET   A CE   1 
ATOM   1229  H  H    . MET   A 1 78  ? 27.101 39.427  26.293 1.00 12.48 ? 78   MET   A H    1 
ATOM   1230  H  HA   . MET   A 1 78  ? 26.295 37.200  24.979 1.00 12.28 ? 78   MET   A HA   1 
ATOM   1231  H  HB2  . MET   A 1 78  ? 25.830 39.784  23.899 1.00 11.51 ? 78   MET   A HB2  1 
ATOM   1232  H  HB3  . MET   A 1 78  ? 25.844 38.534  22.968 1.00 11.51 ? 78   MET   A HB3  1 
ATOM   1233  H  HG2  . MET   A 1 78  ? 24.029 37.632  24.219 1.00 15.48 ? 78   MET   A HG2  1 
ATOM   1234  H  HG3  . MET   A 1 78  ? 23.984 38.950  25.052 1.00 15.48 ? 78   MET   A HG3  1 
ATOM   1235  H  HE1  . MET   A 1 78  ? 23.082 38.759  20.721 1.00 15.78 ? 78   MET   A HE1  1 
ATOM   1236  H  HE2  . MET   A 1 78  ? 24.546 38.644  21.315 1.00 15.78 ? 78   MET   A HE2  1 
ATOM   1237  H  HE3  . MET   A 1 78  ? 23.484 37.503  21.599 1.00 15.78 ? 78   MET   A HE3  1 
ATOM   1238  N  N    . VAL   A 1 79  ? 28.230 37.158  23.344 1.00 9.27  ? 79   VAL   A N    1 
ATOM   1239  C  CA   . VAL   A 1 79  ? 29.501 37.140  22.578 1.00 10.78 ? 79   VAL   A CA   1 
ATOM   1240  C  C    . VAL   A 1 79  ? 29.123 37.645  21.184 1.00 11.31 ? 79   VAL   A C    1 
ATOM   1241  O  O    . VAL   A 1 79  ? 28.137 37.138  20.629 1.00 9.04  ? 79   VAL   A O    1 
ATOM   1242  C  CB   . VAL   A 1 79  ? 30.120 35.732  22.524 1.00 11.36 ? 79   VAL   A CB   1 
ATOM   1243  C  CG1  . VAL   A 1 79  ? 31.150 35.607  21.413 1.00 11.36 ? 79   VAL   A CG1  1 
ATOM   1244  C  CG2  . VAL   A 1 79  ? 30.709 35.321  23.863 1.00 9.49  ? 79   VAL   A CG2  1 
ATOM   1245  H  H    . VAL   A 1 79  ? 27.683 36.523  23.151 1.00 11.13 ? 79   VAL   A H    1 
ATOM   1246  H  HA   . VAL   A 1 79  ? 30.180 37.694  22.994 1.00 12.94 ? 79   VAL   A HA   1 
ATOM   1247  H  HB   . VAL   A 1 79  ? 29.396 35.118  22.322 1.00 13.64 ? 79   VAL   A HB   1 
ATOM   1248  H  HG11 . VAL   A 1 79  ? 31.516 34.709  21.411 1.00 13.63 ? 79   VAL   A HG11 1 
ATOM   1249  H  HG12 . VAL   A 1 79  ? 30.728 35.786  20.558 1.00 13.63 ? 79   VAL   A HG12 1 
ATOM   1250  H  HG13 . VAL   A 1 79  ? 31.864 36.247  21.560 1.00 13.63 ? 79   VAL   A HG13 1 
ATOM   1251  H  HG21 . VAL   A 1 79  ? 31.089 34.431  23.790 1.00 11.39 ? 79   VAL   A HG21 1 
ATOM   1252  H  HG22 . VAL   A 1 79  ? 31.403 35.949  24.118 1.00 11.39 ? 79   VAL   A HG22 1 
ATOM   1253  H  HG23 . VAL   A 1 79  ? 30.011 35.320  24.537 1.00 11.39 ? 79   VAL   A HG23 1 
ATOM   1254  N  N    . VAL   A 1 80  ? 29.846 38.643  20.681 1.00 11.54 ? 80   VAL   A N    1 
ATOM   1255  C  CA   . VAL   A 1 80  ? 29.558 39.198  19.329 1.00 10.29 ? 80   VAL   A CA   1 
ATOM   1256  C  C    . VAL   A 1 80  ? 30.842 39.127  18.498 1.00 9.26  ? 80   VAL   A C    1 
ATOM   1257  O  O    . VAL   A 1 80  ? 31.883 39.585  18.986 1.00 12.74 ? 80   VAL   A O    1 
ATOM   1258  C  CB   . VAL   A 1 80  ? 28.983 40.625  19.403 1.00 10.61 ? 80   VAL   A CB   1 
ATOM   1259  C  CG1  . VAL   A 1 80  ? 28.689 41.176  18.016 1.00 13.29 ? 80   VAL   A CG1  1 
ATOM   1260  C  CG2  . VAL   A 1 80  ? 27.740 40.691  20.276 1.00 11.42 ? 80   VAL   A CG2  1 
ATOM   1261  H  H    . VAL   A 1 80  ? 30.503 39.018  21.090 1.00 13.85 ? 80   VAL   A H    1 
ATOM   1262  H  HA   . VAL   A 1 80  ? 28.870 38.668  18.898 1.00 12.35 ? 80   VAL   A HA   1 
ATOM   1263  H  HB   . VAL   A 1 80  ? 29.663 41.181  19.815 1.00 12.74 ? 80   VAL   A HB   1 
ATOM   1264  H  HG11 . VAL   A 1 80  ? 28.329 42.073  18.094 1.00 15.95 ? 80   VAL   A HG11 1 
ATOM   1265  H  HG12 . VAL   A 1 80  ? 29.508 41.200  17.497 1.00 15.95 ? 80   VAL   A HG12 1 
ATOM   1266  H  HG13 . VAL   A 1 80  ? 28.042 40.606  17.572 1.00 15.95 ? 80   VAL   A HG13 1 
ATOM   1267  H  HG21 . VAL   A 1 80  ? 27.408 41.602  20.298 1.00 13.71 ? 80   VAL   A HG21 1 
ATOM   1268  H  HG22 . VAL   A 1 80  ? 27.057 40.107  19.911 1.00 13.71 ? 80   VAL   A HG22 1 
ATOM   1269  H  HG23 . VAL   A 1 80  ? 27.961 40.406  21.176 1.00 13.71 ? 80   VAL   A HG23 1 
ATOM   1270  N  N    . THR   A 1 81  ? 30.750 38.552  17.301 1.00 10.16 ? 81   THR   A N    1 
ATOM   1271  C  CA   . THR   A 1 81  ? 31.930 38.378  16.421 1.00 8.97  ? 81   THR   A CA   1 
ATOM   1272  C  C    . THR   A 1 81  ? 31.416 37.859  15.082 1.00 10.04 ? 81   THR   A C    1 
ATOM   1273  O  O    . THR   A 1 81  ? 30.237 37.490  15.023 1.00 12.29 ? 81   THR   A O    1 
ATOM   1274  C  CB   . THR   A 1 81  ? 32.919 37.364  17.009 1.00 9.50  ? 81   THR   A CB   1 
ATOM   1275  O  OG1  . THR   A 1 81  ? 34.095 37.321  16.202 1.00 14.91 ? 81   THR   A OG1  1 
ATOM   1276  C  CG2  . THR   A 1 81  ? 32.326 35.975  17.114 1.00 12.01 ? 81   THR   A CG2  1 
ATOM   1277  H  H    . THR   A 1 81  ? 30.015 38.252  16.970 1.00 12.20 ? 81   THR   A H    1 
ATOM   1278  H  HA   . THR   A 1 81  ? 32.397 39.223  16.326 1.00 10.76 ? 81   THR   A HA   1 
ATOM   1279  H  HB   . THR   A 1 81  ? 33.136 37.657  17.908 1.00 11.41 ? 81   THR   A HB   1 
ATOM   1280  H  HG1  . THR   A 1 81  ? 34.578 37.987  16.374 1.00 17.89 ? 81   THR   A HG1  1 
ATOM   1281  H  HG21 . THR   A 1 81  ? 32.984 35.369  17.489 1.00 14.42 ? 81   THR   A HG21 1 
ATOM   1282  H  HG22 . THR   A 1 81  ? 31.545 35.999  17.688 1.00 14.42 ? 81   THR   A HG22 1 
ATOM   1283  H  HG23 . THR   A 1 81  ? 32.069 35.665  16.232 1.00 14.42 ? 81   THR   A HG23 1 
ATOM   1284  N  N    . LYS   A 1 82  ? 32.264 37.830  14.054 1.00 12.82 ? 82   LYS   A N    1 
ATOM   1285  C  CA   . LYS   A 1 82  ? 31.783 37.194  12.800 1.00 14.63 ? 82   LYS   A CA   1 
ATOM   1286  C  C    . LYS   A 1 82  ? 31.658 35.692  13.076 1.00 13.84 ? 82   LYS   A C    1 
ATOM   1287  O  O    . LYS   A 1 82  ? 32.598 35.121  13.656 1.00 11.29 ? 82   LYS   A O    1 
ATOM   1288  C  CB   . LYS   A 1 82  ? 32.660 37.482  11.578 1.00 12.15 ? 82   LYS   A CB   1 
ATOM   1289  C  CG   . LYS   A 1 82  ? 32.066 36.948  10.281 1.00 12.79 ? 82   LYS   A CG   1 
ATOM   1290  C  CD   . LYS   A 1 82  ? 32.780 37.373  9.019  1.00 14.54 ? 82   LYS   A CD   1 
ATOM   1291  C  CE   . LYS   A 1 82  ? 32.056 36.894  7.778  1.00 10.91 ? 82   LYS   A CE   1 
ATOM   1292  N  NZ   . LYS   A 1 82  ? 32.859 37.094  6.549  1.00 14.81 ? 82   LYS   A NZ   1 
ATOM   1293  H  H    . LYS   A 1 82  ? 33.065 38.144  14.045 1.00 15.38 ? 82   LYS   A H    1 
ATOM   1294  H  HA   . LYS   A 1 82  ? 30.925 37.578  12.562 1.00 17.56 ? 82   LYS   A HA   1 
ATOM   1295  H  HB2  . LYS   A 1 82  ? 32.790 38.440  11.498 1.00 14.59 ? 82   LYS   A HB2  1 
ATOM   1296  H  HB3  . LYS   A 1 82  ? 33.535 37.087  11.714 1.00 14.59 ? 82   LYS   A HB3  1 
ATOM   1297  H  HG2  . LYS   A 1 82  ? 32.060 35.979  10.321 1.00 15.35 ? 82   LYS   A HG2  1 
ATOM   1298  H  HG3  . LYS   A 1 82  ? 31.141 37.235  10.224 1.00 15.35 ? 82   LYS   A HG3  1 
ATOM   1299  H  HD2  . LYS   A 1 82  ? 32.853 38.340  8.998  1.00 17.46 ? 82   LYS   A HD2  1 
ATOM   1300  H  HD3  . LYS   A 1 82  ? 33.684 37.020  9.023  1.00 17.46 ? 82   LYS   A HD3  1 
ATOM   1301  H  HE2  . LYS   A 1 82  ? 31.843 35.953  7.873  1.00 13.10 ? 82   LYS   A HE2  1 
ATOM   1302  H  HE3  . LYS   A 1 82  ? 31.214 37.369  7.693  1.00 13.10 ? 82   LYS   A HE3  1 
ATOM   1303  H  HZ1  . LYS   A 1 82  ? 32.527 36.593  5.892  1.00 17.77 ? 82   LYS   A HZ1  1 
ATOM   1304  H  HZ2  . LYS   A 1 82  ? 32.830 37.951  6.311  1.00 17.77 ? 82   LYS   A HZ2  1 
ATOM   1305  H  HZ3  . LYS   A 1 82  ? 33.703 36.858  6.704  1.00 17.77 ? 82   LYS   A HZ3  1 
ATOM   1306  N  N    . ALA   A 1 83  ? 30.535 35.095  12.678 1.00 10.98 ? 83   ALA   A N    1 
ATOM   1307  C  CA   . ALA   A 1 83  ? 30.260 33.666  12.957 1.00 10.81 ? 83   ALA   A CA   1 
ATOM   1308  C  C    . ALA   A 1 83  ? 30.841 32.781  11.853 1.00 12.25 ? 83   ALA   A C    1 
ATOM   1309  O  O    . ALA   A 1 83  ? 30.406 32.887  10.699 1.00 10.40 ? 83   ALA   A O    1 
ATOM   1310  C  CB   . ALA   A 1 83  ? 28.771 33.463  13.085 1.00 11.12 ? 83   ALA   A CB   1 
ATOM   1311  H  H    . ALA   A 1 83  ? 29.911 35.495  12.242 1.00 13.18 ? 83   ALA   A H    1 
ATOM   1312  H  HA   . ALA   A 1 83  ? 30.686 33.412  13.791 1.00 12.97 ? 83   ALA   A HA   1 
ATOM   1313  H  HB1  . ALA   A 1 83  ? 28.586 32.528  13.268 1.00 13.35 ? 83   ALA   A HB1  1 
ATOM   1314  H  HB2  . ALA   A 1 83  ? 28.431 34.008  13.812 1.00 13.35 ? 83   ALA   A HB2  1 
ATOM   1315  H  HB3  . ALA   A 1 83  ? 28.337 33.722  12.257 1.00 13.35 ? 83   ALA   A HB3  1 
ATOM   1316  N  N    . PRO   A 1 84  ? 31.810 31.907  12.183 1.00 10.51 ? 84   PRO   A N    1 
ATOM   1317  C  CA   . PRO   A 1 84  ? 32.445 31.057  11.175 1.00 12.46 ? 84   PRO   A CA   1 
ATOM   1318  C  C    . PRO   A 1 84  ? 31.581 29.897  10.642 1.00 12.67 ? 84   PRO   A C    1 
ATOM   1319  O  O    . PRO   A 1 84  ? 31.842 29.458  9.545  1.00 12.79 ? 84   PRO   A O    1 
ATOM   1320  C  CB   . PRO   A 1 84  ? 33.664 30.488  11.917 1.00 14.91 ? 84   PRO   A CB   1 
ATOM   1321  C  CG   . PRO   A 1 84  ? 33.300 30.589  13.376 1.00 14.42 ? 84   PRO   A CG   1 
ATOM   1322  C  CD   . PRO   A 1 84  ? 32.371 31.769  13.520 1.00 11.06 ? 84   PRO   A CD   1 
ATOM   1323  H  HA   . PRO   A 1 84  ? 32.638 31.579  10.380 1.00 14.96 ? 84   PRO   A HA   1 
ATOM   1324  H  HB2  . PRO   A 1 84  ? 33.837 29.569  11.659 1.00 17.90 ? 84   PRO   A HB2  1 
ATOM   1325  H  HB3  . PRO   A 1 84  ? 34.467 30.995  11.718 1.00 17.90 ? 84   PRO   A HB3  1 
ATOM   1326  H  HG2  . PRO   A 1 84  ? 32.869 29.774  13.679 1.00 17.31 ? 84   PRO   A HG2  1 
ATOM   1327  H  HG3  . PRO   A 1 84  ? 34.094 30.709  13.920 1.00 17.31 ? 84   PRO   A HG3  1 
ATOM   1328  H  HD2  . PRO   A 1 84  ? 31.683 31.606  14.184 1.00 13.28 ? 84   PRO   A HD2  1 
ATOM   1329  H  HD3  . PRO   A 1 84  ? 32.846 32.569  13.795 1.00 13.28 ? 84   PRO   A HD3  1 
ATOM   1330  N  N    . LEU   A 1 85  ? 30.589 29.443  11.413 1.00 11.19 ? 85   LEU   A N    1 
ATOM   1331  C  CA   . LEU   A 1 85  ? 29.718 28.356  10.894 1.00 9.63  ? 85   LEU   A CA   1 
ATOM   1332  C  C    . LEU   A 1 85  ? 28.814 28.897  9.783  1.00 10.63 ? 85   LEU   A C    1 
ATOM   1333  O  O    . LEU   A 1 85  ? 28.609 28.178  8.799  1.00 10.18 ? 85   LEU   A O    1 
ATOM   1334  C  CB   . LEU   A 1 85  ? 28.860 27.824  12.045 1.00 10.18 ? 85   LEU   A CB   1 
ATOM   1335  C  CG   . LEU   A 1 85  ? 27.825 26.764  11.672 1.00 11.29 ? 85   LEU   A CG   1 
ATOM   1336  C  CD1  . LEU   A 1 85  ? 28.498 25.445  11.328 1.00 9.88  ? 85   LEU   A CD1  1 
ATOM   1337  C  CD2  . LEU   A 1 85  ? 26.818 26.569  12.795 1.00 11.90 ? 85   LEU   A CD2  1 
ATOM   1338  H  H    . LEU   A 1 85  ? 30.401 29.728  12.203 1.00 13.43 ? 85   LEU   A H    1 
ATOM   1339  H  HA   . LEU   A 1 85  ? 30.265 27.642  10.531 1.00 11.56 ? 85   LEU   A HA   1 
ATOM   1340  H  HB2  . LEU   A 1 85  ? 29.449 27.452  12.720 1.00 12.22 ? 85   LEU   A HB2  1 
ATOM   1341  H  HB3  . LEU   A 1 85  ? 28.398 28.573  12.454 1.00 12.22 ? 85   LEU   A HB3  1 
ATOM   1342  H  HG   . LEU   A 1 85  ? 27.349 27.078  10.887 1.00 13.56 ? 85   LEU   A HG   1 
ATOM   1343  H  HD11 . LEU   A 1 85  ? 27.823 24.788  11.095 1.00 11.85 ? 85   LEU   A HD11 1 
ATOM   1344  H  HD12 . LEU   A 1 85  ? 29.097 25.574  10.576 1.00 11.85 ? 85   LEU   A HD12 1 
ATOM   1345  H  HD13 . LEU   A 1 85  ? 29.004 25.130  12.093 1.00 11.85 ? 85   LEU   A HD13 1 
ATOM   1346  H  HD21 . LEU   A 1 85  ? 26.172 25.893  12.537 1.00 14.28 ? 85   LEU   A HD21 1 
ATOM   1347  H  HD22 . LEU   A 1 85  ? 27.280 26.284  13.599 1.00 14.28 ? 85   LEU   A HD22 1 
ATOM   1348  H  HD23 . LEU   A 1 85  ? 26.359 27.406  12.967 1.00 14.28 ? 85   LEU   A HD23 1 
ATOM   1349  N  N    . THR   A 1 86  ? 28.327 30.127  9.933  1.00 11.38 ? 86   THR   A N    1 
ATOM   1350  C  CA   . THR   A 1 86  ? 27.323 30.664  8.980  1.00 9.46  ? 86   THR   A CA   1 
ATOM   1351  C  C    . THR   A 1 86  ? 27.885 31.729  8.035  1.00 10.91 ? 86   THR   A C    1 
ATOM   1352  O  O    . THR   A 1 86  ? 27.301 31.905  6.961  1.00 12.79 ? 86   THR   A O    1 
ATOM   1353  C  CB   . THR   A 1 86  ? 26.191 31.310  9.779  1.00 12.07 ? 86   THR   A CB   1 
ATOM   1354  O  OG1  . THR   A 1 86  ? 26.768 32.340  10.580 1.00 11.27 ? 86   THR   A OG1  1 
ATOM   1355  C  CG2  . THR   A 1 86  ? 25.460 30.324  10.663 1.00 8.37  ? 86   THR   A CG2  1 
ATOM   1356  H  H    . THR   A 1 86  ? 28.552 30.666  10.564 1.00 13.66 ? 86   THR   A H    1 
ATOM   1357  H  HA   . THR   A 1 86  ? 27.024 29.916  8.439  1.00 11.35 ? 86   THR   A HA   1 
ATOM   1358  H  HB   . THR   A 1 86  ? 25.533 31.661  9.159  1.00 14.48 ? 86   THR   A HB   1 
ATOM   1359  H  HG1  . THR   A 1 86  ? 26.260 33.009  10.586 1.00 13.53 ? 86   THR   A HG1  1 
ATOM   1360  H  HG21 . THR   A 1 86  ? 24.755 30.783  11.146 1.00 10.05 ? 86   THR   A HG21 1 
ATOM   1361  H  HG22 . THR   A 1 86  ? 25.073 29.623  10.115 1.00 10.05 ? 86   THR   A HG22 1 
ATOM   1362  H  HG23 . THR   A 1 86  ? 26.083 29.933  11.296 1.00 10.05 ? 86   THR   A HG23 1 
ATOM   1363  N  N    . GLY   A 1 87  ? 28.961 32.412  8.419  1.00 11.31 ? 87   GLY   A N    1 
ATOM   1364  C  CA   . GLY   A 1 87  ? 29.434 33.548  7.605  1.00 10.53 ? 87   GLY   A CA   1 
ATOM   1365  C  C    . GLY   A 1 87  ? 28.625 34.796  7.918  1.00 13.20 ? 87   GLY   A C    1 
ATOM   1366  O  O    . GLY   A 1 87  ? 28.843 35.824  7.258  1.00 13.76 ? 87   GLY   A O    1 
ATOM   1367  H  H    . GLY   A 1 87  ? 29.424 32.246  9.125  1.00 13.57 ? 87   GLY   A H    1 
ATOM   1368  H  HA2  . GLY   A 1 87  ? 30.374 33.711  7.782  1.00 12.64 ? 87   GLY   A HA2  1 
ATOM   1369  H  HA3  . GLY   A 1 87  ? 29.356 33.333  6.662  1.00 12.64 ? 87   GLY   A HA3  1 
ATOM   1370  N  N    . THR   A 1 88  ? 27.724 34.708  8.898  1.00 10.63 ? 88   THR   A N    1 
ATOM   1371  C  CA   . THR   A 1 88  ? 26.868 35.857  9.274  1.00 11.06 ? 88   THR   A CA   1 
ATOM   1372  C  C    . THR   A 1 88  ? 27.376 36.546  10.539 1.00 12.38 ? 88   THR   A C    1 
ATOM   1373  O  O    . THR   A 1 88  ? 28.452 36.176  11.034 1.00 9.68  ? 88   THR   A O    1 
ATOM   1374  C  CB   . THR   A 1 88  ? 25.440 35.408  9.609  1.00 12.52 ? 88   THR   A CB   1 
ATOM   1375  O  OG1  . THR   A 1 88  ? 25.473 34.685  10.840 1.00 11.33 ? 88   THR   A OG1  1 
ATOM   1376  C  CG2  . THR   A 1 88  ? 24.816 34.557  8.524  1.00 13.83 ? 88   THR   A CG2  1 
ATOM   1377  H  H    . THR   A 1 88  ? 27.587 33.997  9.361  1.00 12.75 ? 88   THR   A H    1 
ATOM   1378  H  HA   . THR   A 1 88  ? 26.888 36.453  8.509  1.00 13.28 ? 88   THR   A HA   1 
ATOM   1379  H  HB   . THR   A 1 88  ? 24.886 36.201  9.684  1.00 15.02 ? 88   THR   A HB   1 
ATOM   1380  H  HG1  . THR   A 1 88  ? 24.784 34.209  10.904 1.00 13.60 ? 88   THR   A HG1  1 
ATOM   1381  H  HG21 . THR   A 1 88  ? 23.918 34.303  8.788  1.00 16.59 ? 88   THR   A HG21 1 
ATOM   1382  H  HG22 . THR   A 1 88  ? 24.779 35.063  7.697  1.00 16.59 ? 88   THR   A HG22 1 
ATOM   1383  H  HG23 . THR   A 1 88  ? 25.351 33.759  8.390  1.00 16.59 ? 88   THR   A HG23 1 
ATOM   1384  N  N    . ILE   A 1 89  ? 26.620 37.530  11.019 1.00 11.40 ? 89   ILE   A N    1 
ATOM   1385  C  CA   . ILE   A 1 89  ? 26.962 38.141  12.329 1.00 11.38 ? 89   ILE   A CA   1 
ATOM   1386  C  C    . ILE   A 1 89  ? 26.828 37.041  13.380 1.00 9.00  ? 89   ILE   A C    1 
ATOM   1387  O  O    . ILE   A 1 89  ? 25.926 36.199  13.233 1.00 9.78  ? 89   ILE   A O    1 
ATOM   1388  C  CB   . ILE   A 1 89  ? 26.014 39.312  12.650 1.00 11.86 ? 89   ILE   A CB   1 
ATOM   1389  C  CG1  . ILE   A 1 89  ? 26.332 39.954  14.003 1.00 12.50 ? 89   ILE   A CG1  1 
ATOM   1390  C  CG2  . ILE   A 1 89  ? 24.561 38.868  12.569 1.00 13.91 ? 89   ILE   A CG2  1 
ATOM   1391  C  CD1  . ILE   A 1 89  ? 27.643 40.701  14.031 1.00 10.31 ? 89   ILE   A CD1  1 
ATOM   1392  H  H    . ILE   A 1 89  ? 25.927 37.857  10.628 1.00 13.69 ? 89   ILE   A H    1 
ATOM   1393  H  HA   . ILE   A 1 89  ? 27.863 38.500  12.315 1.00 13.66 ? 89   ILE   A HA   1 
ATOM   1394  H  HB   . ILE   A 1 89  ? 26.157 39.996  11.977 1.00 14.24 ? 89   ILE   A HB   1 
ATOM   1395  H  HG12 . ILE   A 1 89  ? 25.616 40.565  14.237 1.00 15.00 ? 89   ILE   A HG12 1 
ATOM   1396  H  HG13 . ILE   A 1 89  ? 26.349 39.263  14.683 1.00 15.00 ? 89   ILE   A HG13 1 
ATOM   1397  H  HG21 . ILE   A 1 89  ? 23.981 39.618  12.774 1.00 16.70 ? 89   ILE   A HG21 1 
ATOM   1398  H  HG22 . ILE   A 1 89  ? 24.370 38.547  11.674 1.00 16.70 ? 89   ILE   A HG22 1 
ATOM   1399  H  HG23 . ILE   A 1 89  ? 24.404 38.155  13.208 1.00 16.70 ? 89   ILE   A HG23 1 
ATOM   1400  H  HD11 . ILE   A 1 89  ? 27.781 41.080  14.913 1.00 12.38 ? 89   ILE   A HD11 1 
ATOM   1401  H  HD12 . ILE   A 1 89  ? 28.368 40.090  13.825 1.00 12.38 ? 89   ILE   A HD12 1 
ATOM   1402  H  HD13 . ILE   A 1 89  ? 27.624 41.413  13.373 1.00 12.38 ? 89   ILE   A HD13 1 
ATOM   1403  N  N    . GLY   A 1 90  ? 27.687 37.031  14.379 1.00 10.43 ? 90   GLY   A N    1 
ATOM   1404  C  CA   . GLY   A 1 90  ? 27.540 36.102  15.508 1.00 8.70  ? 90   GLY   A CA   1 
ATOM   1405  C  C    . GLY   A 1 90  ? 27.013 36.821  16.729 1.00 9.91  ? 90   GLY   A C    1 
ATOM   1406  O  O    . GLY   A 1 90  ? 27.609 37.788  17.127 1.00 10.77 ? 90   GLY   A O    1 
ATOM   1407  H  H    . GLY   A 1 90  ? 28.369 37.552  14.433 1.00 12.51 ? 90   GLY   A H    1 
ATOM   1408  H  HA2  . GLY   A 1 90  ? 26.936 35.383  15.265 1.00 10.45 ? 90   GLY   A HA2  1 
ATOM   1409  H  HA3  . GLY   A 1 90  ? 28.397 35.695  15.711 1.00 10.45 ? 90   GLY   A HA3  1 
ATOM   1410  N  N    . ILE   A 1 91  ? 25.898 36.341  17.260 1.00 8.14  ? 91   ILE   A N    1 
ATOM   1411  C  CA   . ILE   A 1 91  ? 25.245 36.974  18.421 1.00 9.23  ? 91   ILE   A CA   1 
ATOM   1412  C  C    . ILE   A 1 91  ? 24.758 35.839  19.333 1.00 9.39  ? 91   ILE   A C    1 
ATOM   1413  O  O    . ILE   A 1 91  ? 23.646 35.396  19.159 1.00 10.66 ? 91   ILE   A O    1 
ATOM   1414  C  CB   . ILE   A 1 91  ? 24.110 37.914  17.979 1.00 7.57  ? 91   ILE   A CB   1 
ATOM   1415  C  CG1  . ILE   A 1 91  ? 23.403 37.363  16.742 1.00 9.23  ? 91   ILE   A CG1  1 
ATOM   1416  C  CG2  . ILE   A 1 91  ? 24.645 39.314  17.729 1.00 10.25 ? 91   ILE   A CG2  1 
ATOM   1417  C  CD1  . ILE   A 1 91  ? 22.090 38.048  16.455 1.00 10.60 ? 91   ILE   A CD1  1 
ATOM   1418  H  H    . ILE   A 1 91  ? 25.492 35.642  16.966 1.00 9.78  ? 91   ILE   A H    1 
ATOM   1419  H  HA   . ILE   A 1 91  ? 25.865 37.539  18.908 1.00 11.08 ? 91   ILE   A HA   1 
ATOM   1420  H  HB   . ILE   A 1 91  ? 23.457 37.966  18.694 1.00 9.08  ? 91   ILE   A HB   1 
ATOM   1421  H  HG12 . ILE   A 1 91  ? 23.986 37.459  15.973 1.00 11.08 ? 91   ILE   A HG12 1 
ATOM   1422  H  HG13 . ILE   A 1 91  ? 23.246 36.413  16.862 1.00 11.08 ? 91   ILE   A HG13 1 
ATOM   1423  H  HG21 . ILE   A 1 91  ? 23.918 39.894  17.452 1.00 12.31 ? 91   ILE   A HG21 1 
ATOM   1424  H  HG22 . ILE   A 1 91  ? 25.041 39.660  18.544 1.00 12.31 ? 91   ILE   A HG22 1 
ATOM   1425  H  HG23 . ILE   A 1 91  ? 25.318 39.284  17.031 1.00 12.31 ? 91   ILE   A HG23 1 
ATOM   1426  H  HD11 . ILE   A 1 91  ? 21.688 37.659  15.663 1.00 12.73 ? 91   ILE   A HD11 1 
ATOM   1427  H  HD12 . ILE   A 1 91  ? 21.492 37.932  17.210 1.00 12.73 ? 91   ILE   A HD12 1 
ATOM   1428  H  HD13 . ILE   A 1 91  ? 22.244 38.994  16.307 1.00 12.73 ? 91   ILE   A HD13 1 
ATOM   1429  N  N    . SER   A 1 92  ? 25.600 35.432  20.276 1.00 8.39  ? 92   SER   A N    1 
ATOM   1430  C  CA   . SER   A 1 92  ? 25.304 34.287  21.162 1.00 8.25  ? 92   SER   A CA   1 
ATOM   1431  C  C    . SER   A 1 92  ? 25.167 34.761  22.611 1.00 8.92  ? 92   SER   A C    1 
ATOM   1432  O  O    . SER   A 1 92  ? 26.004 35.536  23.045 1.00 10.70 ? 92   SER   A O    1 
ATOM   1433  C  CB   . SER   A 1 92  ? 26.303 33.186  20.964 1.00 9.98  ? 92   SER   A CB   1 
ATOM   1434  O  OG   . SER   A 1 92  ? 26.529 32.939  19.588 1.00 13.22 ? 92   SER   A OG   1 
ATOM   1435  H  H    . SER   A 1 92  ? 26.360 35.805  20.428 1.00 10.07 ? 92   SER   A H    1 
ATOM   1436  H  HA   . SER   A 1 92  ? 24.447 33.900  20.925 1.00 9.90  ? 92   SER   A HA   1 
ATOM   1437  H  HB2  . SER   A 1 92  ? 27.139 33.424  21.394 1.00 11.98 ? 92   SER   A HB2  1 
ATOM   1438  H  HB3  . SER   A 1 92  ? 25.984 32.376  21.392 1.00 11.98 ? 92   SER   A HB3  1 
ATOM   1439  H  HG   . SER   A 1 92  ? 26.733 32.132  19.478 1.00 15.86 ? 92   SER   A HG   1 
ATOM   1440  N  N    . ASN   A 1 93  ? 24.119 34.299  23.291 1.00 9.93  ? 93   ASN   A N    1 
ATOM   1441  C  CA   . ASN   A 1 93  ? 23.791 34.840  24.634 1.00 7.38  ? 93   ASN   A CA   1 
ATOM   1442  C  C    . ASN   A 1 93  ? 24.106 33.811  25.723 1.00 9.93  ? 93   ASN   A C    1 
ATOM   1443  O  O    . ASN   A 1 93  ? 23.994 32.615  25.462 1.00 9.72  ? 93   ASN   A O    1 
ATOM   1444  C  CB   . ASN   A 1 93  ? 22.327 35.295  24.658 1.00 10.01 ? 93   ASN   A CB   1 
ATOM   1445  C  CG   . ASN   A 1 93  ? 21.944 36.136  25.857 1.00 8.26  ? 93   ASN   A CG   1 
ATOM   1446  O  OD1  . ASN   A 1 93  ? 21.979 35.665  26.989 1.00 10.45 ? 93   ASN   A OD1  1 
ATOM   1447  N  ND2  . ASN   A 1 93  ? 21.548 37.373  25.609 1.00 11.18 ? 93   ASN   A ND2  1 
ATOM   1448  H  H    . ASN   A 1 93  ? 23.588 33.684  23.009 1.00 11.92 ? 93   ASN   A H    1 
ATOM   1449  H  HA   . ASN   A 1 93  ? 24.344 35.615  24.820 1.00 8.86  ? 93   ASN   A HA   1 
ATOM   1450  H  HB2  . ASN   A 1 93  ? 22.146 35.803  23.851 1.00 12.02 ? 93   ASN   A HB2  1 
ATOM   1451  H  HB3  . ASN   A 1 93  ? 21.757 34.510  24.634 1.00 12.02 ? 93   ASN   A HB3  1 
ATOM   1452  H  HD21 . ASN   A 1 93  ? 21.301 37.883  26.256 1.00 13.42 ? 93   ASN   A HD21 1 
ATOM   1453  H  HD22 . ASN   A 1 93  ? 21.537 37.667  24.801 1.00 13.42 ? 93   ASN   A HD22 1 
ATOM   1454  N  N    . SER   A 1 94  ? 24.498 34.298  26.902 1.00 9.72  ? 94   SER   A N    1 
ATOM   1455  C  CA   . SER   A 1 94  ? 24.767 33.383  28.039 1.00 9.13  ? 94   SER   A CA   1 
ATOM   1456  C  C    . SER   A 1 94  ? 24.316 34.012  29.359 1.00 9.58  ? 94   SER   A C    1 
ATOM   1457  O  O    . SER   A 1 94  ? 24.228 35.243  29.437 1.00 9.98  ? 94   SER   A O    1 
ATOM   1458  C  CB   . SER   A 1 94  ? 26.220 32.983  28.112 1.00 8.65  ? 94   SER   A CB   1 
ATOM   1459  O  OG   . SER   A 1 94  ? 26.385 31.840  28.933 1.00 9.00  ? 94   SER   A OG   1 
ATOM   1460  H  H    . SER   A 1 94  ? 24.615 35.133  27.071 1.00 11.67 ? 94   SER   A H    1 
ATOM   1461  H  HA   . SER   A 1 94  ? 24.251 32.576  27.886 1.00 10.96 ? 94   SER   A HA   1 
ATOM   1462  H  HB2  . SER   A 1 94  ? 26.554 32.797  27.220 1.00 10.39 ? 94   SER   A HB2  1 
ATOM   1463  H  HB3  . SER   A 1 94  ? 26.745 33.718  28.464 1.00 10.39 ? 94   SER   A HB3  1 
ATOM   1464  H  HG   . SER   A 1 94  ? 27.177 31.806  29.211 1.00 10.80 ? 94   SER   A HG   1 
ATOM   1465  N  N    . GLY   A 1 95  ? 24.047 33.165  30.351 1.00 11.68 ? 95   GLY   A N    1 
ATOM   1466  C  CA   . GLY   A 1 95  ? 23.647 33.664  31.676 1.00 10.28 ? 95   GLY   A CA   1 
ATOM   1467  C  C    . GLY   A 1 95  ? 24.651 33.221  32.721 1.00 9.37  ? 95   GLY   A C    1 
ATOM   1468  O  O    . GLY   A 1 95  ? 25.853 33.391  32.487 1.00 10.98 ? 95   GLY   A O    1 
ATOM   1469  H  H    . GLY   A 1 95  ? 24.088 32.309  30.284 1.00 14.01 ? 95   GLY   A H    1 
ATOM   1470  H  HA2  . GLY   A 1 95  ? 23.590 34.632  31.662 1.00 12.34 ? 95   GLY   A HA2  1 
ATOM   1471  H  HA3  . GLY   A 1 95  ? 22.765 33.331  31.903 1.00 12.34 ? 95   GLY   A HA3  1 
ATOM   1472  N  N    . GLY   A 1 96  ? 24.163 32.663  33.825 1.00 11.99 ? 96   GLY   A N    1 
ATOM   1473  C  CA   . GLY   A 1 96  ? 25.054 32.260  34.924 1.00 12.68 ? 96   GLY   A CA   1 
ATOM   1474  C  C    . GLY   A 1 96  ? 25.482 33.444  35.778 1.00 13.02 ? 96   GLY   A C    1 
ATOM   1475  O  O    . GLY   A 1 96  ? 24.599 34.184  36.227 1.00 13.77 ? 96   GLY   A O    1 
ATOM   1476  H  H    . GLY   A 1 96  ? 23.328 32.508  33.962 1.00 14.39 ? 96   GLY   A H    1 
ATOM   1477  H  HA2  . GLY   A 1 96  ? 24.603 31.607  35.482 1.00 15.22 ? 96   GLY   A HA2  1 
ATOM   1478  H  HA3  . GLY   A 1 96  ? 25.840 31.826  34.558 1.00 15.22 ? 96   GLY   A HA3  1 
ATOM   1479  N  N    . LYS   A 1 97  ? 26.794 33.619  35.969 1.00 10.60 ? 97   LYS   A N    1 
ATOM   1480  C  CA   . LYS   A 1 97  ? 27.302 34.691  36.865 1.00 10.78 ? 97   LYS   A CA   1 
ATOM   1481  C  C    . LYS   A 1 97  ? 28.477 35.454  36.241 1.00 9.97  ? 97   LYS   A C    1 
ATOM   1482  O  O    . LYS   A 1 97  ? 28.680 36.608  36.634 1.00 10.94 ? 97   LYS   A O    1 
ATOM   1483  C  CB   . LYS   A 1 97  ? 27.817 34.055  38.159 1.00 15.24 ? 97   LYS   A CB   1 
ATOM   1484  C  CG   . LYS   A 1 97  ? 26.823 33.215  38.946 1.00 18.92 ? 97   LYS   A CG   1 
ATOM   1485  C  CD   . LYS   A 1 97  ? 27.471 32.545  40.138 1.00 27.45 ? 97   LYS   A CD   1 
ATOM   1486  C  CE   . LYS   A 1 97  ? 26.497 32.209  41.245 1.00 32.68 ? 97   LYS   A CE   1 
ATOM   1487  N  NZ   . LYS   A 1 97  ? 25.513 31.191  40.809 1.00 32.73 ? 97   LYS   A NZ   1 
ATOM   1488  H  H    . LYS   A 1 97  ? 27.405 33.140  35.599 1.00 12.73 ? 97   LYS   A H    1 
ATOM   1489  H  HA   . LYS   A 1 97  ? 26.569 35.306  37.023 1.00 12.94 ? 97   LYS   A HA   1 
ATOM   1490  H  HB2  . LYS   A 1 97  ? 28.580 33.497  37.940 1.00 18.29 ? 97   LYS   A HB2  1 
ATOM   1491  H  HB3  . LYS   A 1 97  ? 28.141 34.763  38.737 1.00 18.29 ? 97   LYS   A HB3  1 
ATOM   1492  H  HG2  . LYS   A 1 97  ? 26.093 33.777  39.249 1.00 22.71 ? 97   LYS   A HG2  1 
ATOM   1493  H  HG3  . LYS   A 1 97  ? 26.439 32.540  38.365 1.00 22.71 ? 97   LYS   A HG3  1 
ATOM   1494  H  HD2  . LYS   A 1 97  ? 27.909 31.731  39.844 1.00 32.95 ? 97   LYS   A HD2  1 
ATOM   1495  H  HD3  . LYS   A 1 97  ? 28.162 33.127  40.491 1.00 32.95 ? 97   LYS   A HD3  1 
ATOM   1496  H  HE2  . LYS   A 1 97  ? 26.983 31.881  42.018 1.00 39.22 ? 97   LYS   A HE2  1 
ATOM   1497  H  HE3  . LYS   A 1 97  ? 26.031 33.013  41.523 1.00 39.22 ? 97   LYS   A HE3  1 
ATOM   1498  H  HZ1  . LYS   A 1 97  ? 25.119 30.834  41.523 1.00 39.28 ? 97   LYS   A HZ1  1 
ATOM   1499  H  HZ2  . LYS   A 1 97  ? 24.898 31.574  40.292 1.00 39.28 ? 97   LYS   A HZ2  1 
ATOM   1500  H  HZ3  . LYS   A 1 97  ? 25.930 30.553  40.350 1.00 39.28 ? 97   LYS   A HZ3  1 
ATOM   1501  N  N    . TRP   A 1 98  ? 29.227 34.828  35.335 1.00 11.27 ? 98   TRP   A N    1 
ATOM   1502  C  CA   . TRP   A 1 98  ? 30.461 35.452  34.774 1.00 13.60 ? 98   TRP   A CA   1 
ATOM   1503  C  C    . TRP   A 1 98  ? 30.243 36.907  34.344 1.00 13.64 ? 98   TRP   A C    1 
ATOM   1504  O  O    . TRP   A 1 98  ? 31.046 37.759  34.745 1.00 12.78 ? 98   TRP   A O    1 
ATOM   1505  C  CB   . TRP   A 1 98  ? 30.983 34.610  33.601 1.00 9.71  ? 98   TRP   A CB   1 
ATOM   1506  C  CG   . TRP   A 1 98  ? 32.341 34.999  33.105 1.00 12.06 ? 98   TRP   A CG   1 
ATOM   1507  C  CD1  . TRP   A 1 98  ? 33.534 34.431  33.442 1.00 10.84 ? 98   TRP   A CD1  1 
ATOM   1508  C  CD2  . TRP   A 1 98  ? 32.647 36.039  32.160 1.00 11.64 ? 98   TRP   A CD2  1 
ATOM   1509  N  NE1  . TRP   A 1 98  ? 34.560 35.050  32.782 1.00 12.25 ? 98   TRP   A NE1  1 
ATOM   1510  C  CE2  . TRP   A 1 98  ? 34.047 36.040  31.987 1.00 10.36 ? 98   TRP   A CE2  1 
ATOM   1511  C  CE3  . TRP   A 1 98  ? 31.879 36.967  31.448 1.00 9.96  ? 98   TRP   A CE3  1 
ATOM   1512  C  CZ2  . TRP   A 1 98  ? 34.689 36.936  31.136 1.00 10.91 ? 98   TRP   A CZ2  1 
ATOM   1513  C  CZ3  . TRP   A 1 98  ? 32.516 37.852  30.609 1.00 9.79  ? 98   TRP   A CZ3  1 
ATOM   1514  C  CH2  . TRP   A 1 98  ? 33.901 37.835  30.455 1.00 12.10 ? 98   TRP   A CH2  1 
ATOM   1515  H  H    . TRP   A 1 98  ? 29.052 34.045  35.025 1.00 13.53 ? 98   TRP   A H    1 
ATOM   1516  H  HA   . TRP   A 1 98  ? 31.126 35.470  35.480 1.00 16.33 ? 98   TRP   A HA   1 
ATOM   1517  H  HB2  . TRP   A 1 98  ? 31.006 33.679  33.872 1.00 11.65 ? 98   TRP   A HB2  1 
ATOM   1518  H  HB3  . TRP   A 1 98  ? 30.353 34.676  32.866 1.00 11.65 ? 98   TRP   A HB3  1 
ATOM   1519  H  HD1  . TRP   A 1 98  ? 33.636 33.723  34.036 1.00 13.02 ? 98   TRP   A HD1  1 
ATOM   1520  H  HE1  . TRP   A 1 98  ? 35.393 34.850  32.855 1.00 14.71 ? 98   TRP   A HE1  1 
ATOM   1521  H  HE3  . TRP   A 1 98  ? 30.954 36.985  31.540 1.00 11.95 ? 98   TRP   A HE3  1 
ATOM   1522  H  HZ2  . TRP   A 1 98  ? 35.613 36.927  31.032 1.00 13.10 ? 98   TRP   A HZ2  1 
ATOM   1523  H  HZ3  . TRP   A 1 98  ? 32.012 38.474  30.135 1.00 11.75 ? 98   TRP   A HZ3  1 
ATOM   1524  H  HH2  . TRP   A 1 98  ? 34.302 38.445  29.879 1.00 14.53 ? 98   TRP   A HH2  1 
ATOM   1525  N  N    . GLY   A 1 99  ? 29.215 37.170  33.539 1.00 14.36 ? 99   GLY   A N    1 
ATOM   1526  C  CA   . GLY   A 1 99  ? 29.003 38.528  32.999 1.00 12.45 ? 99   GLY   A CA   1 
ATOM   1527  C  C    . GLY   A 1 99  ? 28.714 39.547  34.084 1.00 13.56 ? 99   GLY   A C    1 
ATOM   1528  O  O    . GLY   A 1 99  ? 28.983 40.734  33.865 1.00 12.94 ? 99   GLY   A O    1 
ATOM   1529  H  H    . GLY   A 1 99  ? 28.631 36.589  33.292 1.00 17.23 ? 99   GLY   A H    1 
ATOM   1530  H  HA2  . GLY   A 1 99  ? 29.791 38.802  32.504 1.00 14.94 ? 99   GLY   A HA2  1 
ATOM   1531  H  HA3  . GLY   A 1 99  ? 28.264 38.511  32.371 1.00 14.94 ? 99   GLY   A HA3  1 
ATOM   1532  N  N    . VAL   A 1 100 ? 28.184 39.092  35.215 1.00 12.73 ? 100  VAL   A N    1 
ATOM   1533  C  CA   . VAL   A 1 100 ? 27.881 40.017  36.340 1.00 11.33 ? 100  VAL   A CA   1 
ATOM   1534  C  C    . VAL   A 1 100 ? 29.202 40.375  37.033 1.00 13.25 ? 100  VAL   A C    1 
ATOM   1535  O  O    . VAL   A 1 100 ? 29.369 41.534  37.420 1.00 15.94 ? 100  VAL   A O    1 
ATOM   1536  C  CB   . VAL   A 1 100 ? 26.853 39.406  37.312 1.00 12.79 ? 100  VAL   A CB   1 
ATOM   1537  C  CG1  . VAL   A 1 100 ? 26.667 40.265  38.551 1.00 14.42 ? 100  VAL   A CG1  1 
ATOM   1538  C  CG2  . VAL   A 1 100 ? 25.517 39.166  36.626 1.00 14.38 ? 100  VAL   A CG2  1 
ATOM   1539  H  H    . VAL   A 1 100 ? 27.990 38.267  35.363 1.00 15.28 ? 100  VAL   A H    1 
ATOM   1540  H  HA   . VAL   A 1 100 ? 27.470 40.828  36.003 1.00 13.60 ? 100  VAL   A HA   1 
ATOM   1541  H  HB   . VAL   A 1 100 ? 27.209 38.549  37.596 1.00 15.35 ? 100  VAL   A HB   1 
ATOM   1542  H  HG11 . VAL   A 1 100 ? 26.015 39.850  39.138 1.00 17.31 ? 100  VAL   A HG11 1 
ATOM   1543  H  HG12 . VAL   A 1 100 ? 27.514 40.349  39.017 1.00 17.31 ? 100  VAL   A HG12 1 
ATOM   1544  H  HG13 . VAL   A 1 100 ? 26.353 41.145  38.291 1.00 17.31 ? 100  VAL   A HG13 1 
ATOM   1545  H  HG21 . VAL   A 1 100 ? 24.892 38.782  37.260 1.00 17.26 ? 100  VAL   A HG21 1 
ATOM   1546  H  HG22 . VAL   A 1 100 ? 25.166 40.008  36.296 1.00 17.26 ? 100  VAL   A HG22 1 
ATOM   1547  H  HG23 . VAL   A 1 100 ? 25.640 38.554  35.883 1.00 17.26 ? 100  VAL   A HG23 1 
ATOM   1548  N  N    . ASP   A 1 101 ? 30.117 39.412  37.138 1.00 14.29 ? 101  ASP   A N    1 
ATOM   1549  C  CA   . ASP   A 1 101 ? 31.442 39.739  37.729 1.00 12.69 ? 101  ASP   A CA   1 
ATOM   1550  C  C    . ASP   A 1 101 ? 32.182 40.726  36.816 1.00 12.57 ? 101  ASP   A C    1 
ATOM   1551  O  O    . ASP   A 1 101 ? 32.830 41.640  37.336 1.00 13.04 ? 101  ASP   A O    1 
ATOM   1552  C  CB   . ASP   A 1 101 ? 32.270 38.484  38.011 1.00 14.23 ? 101  ASP   A CB   1 
ATOM   1553  C  CG   . ASP   A 1 101 ? 32.144 38.019  39.451 1.00 16.17 ? 101  ASP   A CG   1 
ATOM   1554  O  OD1  . ASP   A 1 101 ? 32.932 38.492  40.288 1.00 16.23 ? 101  ASP   A OD1  1 
ATOM   1555  O  OD2  . ASP   A 1 101 ? 31.245 37.203  39.725 1.00 17.30 ? 101  ASP   A OD2  1 
ATOM   1556  H  H    . ASP   A 1 101 ? 30.011 38.596  36.889 1.00 17.15 ? 101  ASP   A H    1 
ATOM   1557  H  HA   . ASP   A 1 101 ? 31.301 40.162  38.590 1.00 15.23 ? 101  ASP   A HA   1 
ATOM   1558  H  HB2  . ASP   A 1 101 ? 31.985 37.772  37.418 1.00 17.08 ? 101  ASP   A HB2  1 
ATOM   1559  H  HB3  . ASP   A 1 101 ? 33.202 38.663  37.812 1.00 17.08 ? 101  ASP   A HB3  1 
ATOM   1560  N  N    . LEU   A 1 102 ? 32.085 40.533  35.501 1.00 14.54 ? 102  LEU   A N    1 
ATOM   1561  C  CA   . LEU   A 1 102 ? 32.725 41.485  34.553 1.00 12.13 ? 102  LEU   A CA   1 
ATOM   1562  C  C    . LEU   A 1 102 ? 32.151 42.889  34.786 1.00 12.61 ? 102  LEU   A C    1 
ATOM   1563  O  O    . LEU   A 1 102 ? 32.929 43.846  34.875 1.00 12.56 ? 102  LEU   A O    1 
ATOM   1564  C  CB   . LEU   A 1 102 ? 32.476 41.010  33.118 1.00 12.30 ? 102  LEU   A CB   1 
ATOM   1565  C  CG   . LEU   A 1 102 ? 33.043 41.922  32.033 1.00 12.36 ? 102  LEU   A CG   1 
ATOM   1566  C  CD1  . LEU   A 1 102 ? 34.562 41.915  32.072 1.00 12.73 ? 102  LEU   A CD1  1 
ATOM   1567  C  CD2  . LEU   A 1 102 ? 32.541 41.511  30.659 1.00 11.47 ? 102  LEU   A CD2  1 
ATOM   1568  H  H    . LEU   A 1 102 ? 31.667 39.878  35.133 1.00 17.45 ? 102  LEU   A H    1 
ATOM   1569  H  HA   . LEU   A 1 102 ? 33.683 41.520  34.700 1.00 14.56 ? 102  LEU   A HA   1 
ATOM   1570  H  HB2  . LEU   A 1 102 ? 32.860 40.126  33.012 1.00 14.77 ? 102  LEU   A HB2  1 
ATOM   1571  H  HB3  . LEU   A 1 102 ? 31.520 40.922  32.981 1.00 14.77 ? 102  LEU   A HB3  1 
ATOM   1572  H  HG   . LEU   A 1 102 ? 32.735 42.825  32.207 1.00 14.84 ? 102  LEU   A HG   1 
ATOM   1573  H  HD11 . LEU   A 1 102 ? 34.906 42.498  31.378 1.00 15.28 ? 102  LEU   A HD11 1 
ATOM   1574  H  HD12 . LEU   A 1 102 ? 34.865 42.230  32.938 1.00 15.28 ? 102  LEU   A HD12 1 
ATOM   1575  H  HD13 . LEU   A 1 102 ? 34.886 41.012  31.925 1.00 15.28 ? 102  LEU   A HD13 1 
ATOM   1576  H  HD21 . LEU   A 1 102 ? 32.914 42.104  29.988 1.00 13.77 ? 102  LEU   A HD21 1 
ATOM   1577  H  HD22 . LEU   A 1 102 ? 32.815 40.599  30.473 1.00 13.77 ? 102  LEU   A HD22 1 
ATOM   1578  H  HD23 . LEU   A 1 102 ? 31.573 41.567  30.638 1.00 13.77 ? 102  LEU   A HD23 1 
ATOM   1579  N  N    . LYS   A 1 103 ? 30.828 42.994  34.871 1.00 11.89 ? 103  LYS   A N    1 
ATOM   1580  C  CA   . LYS   A 1 103 ? 30.176 44.311  35.074 1.00 13.28 ? 103  LYS   A CA   1 
ATOM   1581  C  C    . LYS   A 1 103 ? 30.566 44.858  36.454 1.00 13.57 ? 103  LYS   A C    1 
ATOM   1582  O  O    . LYS   A 1 103 ? 30.827 46.063  36.564 1.00 14.85 ? 103  LYS   A O    1 
ATOM   1583  C  CB   . LYS   A 1 103 ? 28.660 44.164  34.925 1.00 15.27 ? 103  LYS   A CB   1 
ATOM   1584  C  CG   . LYS   A 1 103 ? 27.873 45.466  34.928 1.00 14.50 ? 103  LYS   A CG   1 
ATOM   1585  C  CD   . LYS   A 1 103 ? 27.827 46.132  33.573 1.00 14.34 ? 103  LYS   A CD   1 
ATOM   1586  C  CE   . LYS   A 1 103 ? 26.990 47.392  33.569 1.00 16.25 ? 103  LYS   A CE   1 
ATOM   1587  N  NZ   . LYS   A 1 103 ? 25.544 47.094  33.688 1.00 15.72 ? 103  LYS   A NZ   1 
ATOM   1588  H  H    . LYS   A 1 103 ? 30.285 42.329  34.816 1.00 14.28 ? 103  LYS   A H    1 
ATOM   1589  H  HA   . LYS   A 1 103 ? 30.476 44.944  34.403 1.00 15.93 ? 103  LYS   A HA   1 
ATOM   1590  H  HB2  . LYS   A 1 103 ? 28.476 43.695  34.096 1.00 18.32 ? 103  LYS   A HB2  1 
ATOM   1591  H  HB3  . LYS   A 1 103 ? 28.332 43.604  35.646 1.00 18.32 ? 103  LYS   A HB3  1 
ATOM   1592  H  HG2  . LYS   A 1 103 ? 26.967 45.290  35.227 1.00 17.40 ? 103  LYS   A HG2  1 
ATOM   1593  H  HG3  . LYS   A 1 103 ? 28.270 46.076  35.569 1.00 17.40 ? 103  LYS   A HG3  1 
ATOM   1594  H  HD2  . LYS   A 1 103 ? 28.730 46.347  33.292 1.00 17.22 ? 103  LYS   A HD2  1 
ATOM   1595  H  HD3  . LYS   A 1 103 ? 27.469 45.508  32.922 1.00 17.22 ? 103  LYS   A HD3  1 
ATOM   1596  H  HE2  . LYS   A 1 103 ? 27.264 47.964  34.303 1.00 19.50 ? 103  LYS   A HE2  1 
ATOM   1597  H  HE3  . LYS   A 1 103 ? 27.152 47.885  32.750 1.00 19.50 ? 103  LYS   A HE3  1 
ATOM   1598  H  HZ1  . LYS   A 1 103 ? 25.107 47.831  33.928 1.00 18.87 ? 103  LYS   A HZ1  1 
ATOM   1599  H  HZ2  . LYS   A 1 103 ? 25.234 46.808  32.904 1.00 18.87 ? 103  LYS   A HZ2  1 
ATOM   1600  H  HZ3  . LYS   A 1 103 ? 25.420 46.463  34.303 1.00 18.87 ? 103  LYS   A HZ3  1 
ATOM   1601  N  N    . LYS   A 1 104 ? 30.653 43.997  37.465 1.00 12.85 ? 104  LYS   A N    1 
ATOM   1602  C  CA   . LYS   A 1 104 ? 31.040 44.460  38.827 1.00 14.38 ? 104  LYS   A CA   1 
ATOM   1603  C  C    . LYS   A 1 104 ? 32.539 44.787  38.870 1.00 16.83 ? 104  LYS   A C    1 
ATOM   1604  O  O    . LYS   A 1 104 ? 32.959 45.453  39.824 1.00 18.02 ? 104  LYS   A O    1 
ATOM   1605  C  CB   . LYS   A 1 104 ? 30.646 43.424  39.883 1.00 16.59 ? 104  LYS   A CB   1 
ATOM   1606  C  CG   . LYS   A 1 104 ? 29.152 43.303  40.145 1.00 16.40 ? 104  LYS   A CG   1 
ATOM   1607  C  CD   . LYS   A 1 104 ? 28.806 42.286  41.211 1.00 15.42 ? 104  LYS   A CD   1 
ATOM   1608  C  CE   . LYS   A 1 104 ? 27.353 42.348  41.631 1.00 19.34 ? 104  LYS   A CE   1 
ATOM   1609  N  NZ   . LYS   A 1 104 ? 26.999 41.256  42.567 1.00 23.20 ? 104  LYS   A NZ   1 
ATOM   1610  H  H    . LYS   A 1 104 ? 30.498 43.154  37.400 1.00 15.43 ? 104  LYS   A H    1 
ATOM   1611  H  HA   . LYS   A 1 104 ? 30.556 45.275  39.034 1.00 17.26 ? 104  LYS   A HA   1 
ATOM   1612  H  HB2  . LYS   A 1 104 ? 30.983 42.557  39.607 1.00 19.91 ? 104  LYS   A HB2  1 
ATOM   1613  H  HB3  . LYS   A 1 104 ? 31.089 43.648  40.716 1.00 19.91 ? 104  LYS   A HB3  1 
ATOM   1614  H  HG2  . LYS   A 1 104 ? 28.806 44.170  40.411 1.00 19.68 ? 104  LYS   A HG2  1 
ATOM   1615  H  HG3  . LYS   A 1 104 ? 28.705 43.060  39.319 1.00 19.68 ? 104  LYS   A HG3  1 
ATOM   1616  H  HD2  . LYS   A 1 104 ? 29.005 41.396  40.880 1.00 18.51 ? 104  LYS   A HD2  1 
ATOM   1617  H  HD3  . LYS   A 1 104 ? 29.369 42.433  41.987 1.00 18.51 ? 104  LYS   A HD3  1 
ATOM   1618  H  HE2  . LYS   A 1 104 ? 27.175 43.204  42.052 1.00 23.22 ? 104  LYS   A HE2  1 
ATOM   1619  H  HE3  . LYS   A 1 104 ? 26.787 42.295  40.845 1.00 23.22 ? 104  LYS   A HE3  1 
ATOM   1620  H  HZ1  . LYS   A 1 104 ? 26.120 41.120  42.546 1.00 27.85 ? 104  LYS   A HZ1  1 
ATOM   1621  H  HZ2  . LYS   A 1 104 ? 27.420 40.510  42.326 1.00 27.85 ? 104  LYS   A HZ2  1 
ATOM   1622  H  HZ3  . LYS   A 1 104 ? 27.244 41.481  43.392 1.00 27.85 ? 104  LYS   A HZ3  1 
ATOM   1623  N  N    . ALA   A 1 105 ? 33.302 44.342  37.874 1.00 16.12 ? 105  ALA   A N    1 
ATOM   1624  C  CA   . ALA   A 1 105 ? 34.751 44.661  37.814 1.00 13.57 ? 105  ALA   A CA   1 
ATOM   1625  C  C    . ALA   A 1 105 ? 34.959 46.032  37.161 1.00 14.99 ? 105  ALA   A C    1 
ATOM   1626  O  O    . ALA   A 1 105 ? 36.107 46.480  37.111 1.00 15.83 ? 105  ALA   A O    1 
ATOM   1627  C  CB   . ALA   A 1 105 ? 35.498 43.580  37.073 1.00 13.93 ? 105  ALA   A CB   1 
ATOM   1628  H  H    . ALA   A 1 105 ? 33.014 43.858  37.224 1.00 19.35 ? 105  ALA   A H    1 
ATOM   1629  H  HA   . ALA   A 1 105 ? 35.106 44.699  38.716 1.00 16.29 ? 105  ALA   A HA   1 
ATOM   1630  H  HB1  . ALA   A 1 105 ? 36.442 43.802  37.042 1.00 16.71 ? 105  ALA   A HB1  1 
ATOM   1631  H  HB2  . ALA   A 1 105 ? 35.380 42.733  37.531 1.00 16.71 ? 105  ALA   A HB2  1 
ATOM   1632  H  HB3  . ALA   A 1 105 ? 35.153 43.509  36.169 1.00 16.71 ? 105  ALA   A HB3  1 
ATOM   1633  N  N    . GLY   A 1 106 ? 33.888 46.652  36.656 1.00 15.81 ? 106  GLY   A N    1 
ATOM   1634  C  CA   . GLY   A 1 106 ? 33.984 48.012  36.087 1.00 16.49 ? 106  GLY   A CA   1 
ATOM   1635  C  C    . GLY   A 1 106 ? 33.980 48.038  34.568 1.00 16.34 ? 106  GLY   A C    1 
ATOM   1636  O  O    . GLY   A 1 106 ? 34.205 49.121  34.006 1.00 15.39 ? 106  GLY   A O    1 
ATOM   1637  H  H    . GLY   A 1 106 ? 33.100 46.309  36.631 1.00 18.97 ? 106  GLY   A H    1 
ATOM   1638  H  HA2  . GLY   A 1 106 ? 33.242 48.544  36.414 1.00 19.79 ? 106  GLY   A HA2  1 
ATOM   1639  H  HA3  . GLY   A 1 106 ? 34.797 48.432  36.408 1.00 19.79 ? 106  GLY   A HA3  1 
ATOM   1640  N  N    . TRP   A 1 107 ? 33.719 46.898  33.925 1.00 14.26 ? 107  TRP   A N    1 
ATOM   1641  C  CA   . TRP   A 1 107 ? 33.789 46.825  32.441 1.00 13.29 ? 107  TRP   A CA   1 
ATOM   1642  C  C    . TRP   A 1 107 ? 32.416 46.535  31.829 1.00 14.18 ? 107  TRP   A C    1 
ATOM   1643  O  O    . TRP   A 1 107 ? 31.748 45.603  32.288 1.00 13.57 ? 107  TRP   A O    1 
ATOM   1644  C  CB   . TRP   A 1 107 ? 34.794 45.759  32.004 1.00 14.41 ? 107  TRP   A CB   1 
ATOM   1645  C  CG   . TRP   A 1 107 ? 36.133 45.883  32.661 1.00 16.11 ? 107  TRP   A CG   1 
ATOM   1646  C  CD1  . TRP   A 1 107 ? 36.628 45.122  33.679 1.00 16.31 ? 107  TRP   A CD1  1 
ATOM   1647  C  CD2  . TRP   A 1 107 ? 37.157 46.838  32.337 1.00 14.67 ? 107  TRP   A CD2  1 
ATOM   1648  N  NE1  . TRP   A 1 107 ? 37.889 45.537  34.012 1.00 14.99 ? 107  TRP   A NE1  1 
ATOM   1649  C  CE2  . TRP   A 1 107 ? 38.241 46.587  33.205 1.00 16.58 ? 107  TRP   A CE2  1 
ATOM   1650  C  CE3  . TRP   A 1 107 ? 37.263 47.875  31.405 1.00 16.58 ? 107  TRP   A CE3  1 
ATOM   1651  C  CZ2  . TRP   A 1 107 ? 39.414 47.337  33.163 1.00 18.13 ? 107  TRP   A CZ2  1 
ATOM   1652  C  CZ3  . TRP   A 1 107 ? 38.423 48.614  31.363 1.00 16.52 ? 107  TRP   A CZ3  1 
ATOM   1653  C  CH2  . TRP   A 1 107 ? 39.481 48.347  32.232 1.00 21.19 ? 107  TRP   A CH2  1 
ATOM   1654  H  H    . TRP   A 1 107 ? 33.502 46.161  34.312 1.00 17.12 ? 107  TRP   A H    1 
ATOM   1655  H  HA   . TRP   A 1 107 ? 34.085 47.691  32.118 1.00 15.95 ? 107  TRP   A HA   1 
ATOM   1656  H  HB2  . TRP   A 1 107 ? 34.428 44.882  32.199 1.00 17.30 ? 107  TRP   A HB2  1 
ATOM   1657  H  HB3  . TRP   A 1 107 ? 34.909 45.811  31.042 1.00 17.30 ? 107  TRP   A HB3  1 
ATOM   1658  H  HD1  . TRP   A 1 107 ? 36.174 44.421  34.088 1.00 19.57 ? 107  TRP   A HD1  1 
ATOM   1659  H  HE1  . TRP   A 1 107 ? 38.381 45.194  34.628 1.00 17.99 ? 107  TRP   A HE1  1 
ATOM   1660  H  HE3  . TRP   A 1 107 ? 36.562 48.062  30.824 1.00 19.90 ? 107  TRP   A HE3  1 
ATOM   1661  H  HZ2  . TRP   A 1 107 ? 40.122 47.162  33.740 1.00 21.76 ? 107  TRP   A HZ2  1 
ATOM   1662  H  HZ3  . TRP   A 1 107 ? 38.503 49.304  30.744 1.00 19.83 ? 107  TRP   A HZ3  1 
ATOM   1663  H  HH2  . TRP   A 1 107 ? 40.251 48.865  32.180 1.00 25.43 ? 107  TRP   A HH2  1 
ATOM   1664  N  N    . ASP   A 1 108 ? 32.045 47.304  30.808 1.00 13.39 ? 108  ASP   A N    1 
ATOM   1665  C  CA   . ASP   A 1 108 ? 30.774 47.042  30.090 1.00 13.63 ? 108  ASP   A CA   1 
ATOM   1666  C  C    . ASP   A 1 108 ? 31.039 46.061  28.953 1.00 13.60 ? 108  ASP   A C    1 
ATOM   1667  O  O    . ASP   A 1 108 ? 30.104 45.340  28.569 1.00 11.71 ? 108  ASP   A O    1 
ATOM   1668  C  CB   . ASP   A 1 108 ? 30.240 48.319  29.444 1.00 14.44 ? 108  ASP   A CB   1 
ATOM   1669  C  CG   . ASP   A 1 108 ? 29.799 49.374  30.440 1.00 14.80 ? 108  ASP   A CG   1 
ATOM   1670  O  OD1  . ASP   A 1 108 ? 28.885 49.081  31.227 1.00 14.58 ? 108  ASP   A OD1  1 
ATOM   1671  O  OD2  . ASP   A 1 108 ? 30.371 50.478  30.410 1.00 17.67 ? 108  ASP   A OD2  1 
ATOM   1672  H  H    . ASP   A 1 108 ? 32.498 47.972  30.512 1.00 16.07 ? 108  ASP   A H    1 
ATOM   1673  H  HA   . ASP   A 1 108 ? 30.135 46.695  30.732 1.00 16.36 ? 108  ASP   A HA   1 
ATOM   1674  H  HB2  . ASP   A 1 108 ? 30.928 48.694  28.873 1.00 17.33 ? 108  ASP   A HB2  1 
ATOM   1675  H  HB3  . ASP   A 1 108 ? 29.490 48.092  28.873 1.00 17.33 ? 108  ASP   A HB3  1 
ATOM   1676  N  N    . MET   A 1 109 ? 32.275 46.020  28.462 1.00 12.51 ? 109  MET   A N    1 
ATOM   1677  C  CA   . MET   A 1 109 ? 32.543 45.216  27.249 1.00 11.55 ? 109  MET   A CA   1 
ATOM   1678  C  C    . MET   A 1 109 ? 34.035 44.910  27.117 1.00 13.22 ? 109  MET   A C    1 
ATOM   1679  O  O    . MET   A 1 109 ? 34.844 45.719  27.597 1.00 12.65 ? 109  MET   A O    1 
ATOM   1680  C  CB   . MET   A 1 109 ? 32.088 46.034  26.034 1.00 11.90 ? 109  MET   A CB   1 
ATOM   1681  C  CG   . MET   A 1 109 ? 32.549 45.523  24.686 1.00 14.35 ? 109  MET   A CG   1 
ATOM   1682  S  SD   . MET   A 1 109 ? 31.582 46.279  23.339 1.00 14.93 ? 109  MET   A SD   1 
ATOM   1683  C  CE   . MET   A 1 109 ? 32.075 47.996  23.482 1.00 14.86 ? 109  MET   A CE   1 
ATOM   1684  H  H    . MET   A 1 109 ? 32.954 46.430  28.794 1.00 15.02 ? 109  MET   A H    1 
ATOM   1685  H  HA   . MET   A 1 109 ? 32.065 44.374  27.305 1.00 13.87 ? 109  MET   A HA   1 
ATOM   1686  H  HB2  . MET   A 1 109 ? 31.119 46.069  26.033 1.00 14.28 ? 109  MET   A HB2  1 
ATOM   1687  H  HB3  . MET   A 1 109 ? 32.405 46.945  26.141 1.00 14.28 ? 109  MET   A HB3  1 
ATOM   1688  H  HG2  . MET   A 1 109 ? 33.490 45.723  24.565 1.00 17.23 ? 109  MET   A HG2  1 
ATOM   1689  H  HG3  . MET   A 1 109 ? 32.457 44.558  24.653 1.00 17.23 ? 109  MET   A HG3  1 
ATOM   1690  H  HE1  . MET   A 1 109 ? 31.620 48.521  22.805 1.00 17.84 ? 109  MET   A HE1  1 
ATOM   1691  H  HE2  . MET   A 1 109 ? 31.838 48.329  24.362 1.00 17.84 ? 109  MET   A HE2  1 
ATOM   1692  H  HE3  . MET   A 1 109 ? 33.034 48.069  23.357 1.00 17.84 ? 109  MET   A HE3  1 
ATOM   1693  N  N    . ILE   A 1 110 ? 34.367 43.765  26.524 1.00 11.39 ? 110  ILE   A N    1 
ATOM   1694  C  CA   . ILE   A 1 110 ? 35.789 43.433  26.245 1.00 10.96 ? 110  ILE   A CA   1 
ATOM   1695  C  C    . ILE   A 1 110 ? 35.923 43.268  24.732 1.00 12.68 ? 110  ILE   A C    1 
ATOM   1696  O  O    . ILE   A 1 110 ? 35.095 42.552  24.151 1.00 13.48 ? 110  ILE   A O    1 
ATOM   1697  C  CB   . ILE   A 1 110 ? 36.223 42.142  26.963 1.00 12.44 ? 110  ILE   A CB   1 
ATOM   1698  C  CG1  . ILE   A 1 110 ? 35.929 42.176  28.464 1.00 13.35 ? 110  ILE   A CG1  1 
ATOM   1699  C  CG2  . ILE   A 1 110 ? 37.689 41.842  26.683 1.00 11.89 ? 110  ILE   A CG2  1 
ATOM   1700  C  CD1  . ILE   A 1 110 ? 36.321 40.904  29.179 1.00 14.42 ? 110  ILE   A CD1  1 
ATOM   1701  H  H    . ILE   A 1 110 ? 33.802 43.167  26.274 1.00 13.67 ? 110  ILE   A H    1 
ATOM   1702  H  HA   . ILE   A 1 110 ? 36.364 44.141  26.574 1.00 13.16 ? 110  ILE   A HA   1 
ATOM   1703  H  HB   . ILE   A 1 110 ? 35.689 41.417  26.602 1.00 14.93 ? 110  ILE   A HB   1 
ATOM   1704  H  HG12 . ILE   A 1 110 ? 36.402 42.923  28.863 1.00 16.03 ? 110  ILE   A HG12 1 
ATOM   1705  H  HG13 . ILE   A 1 110 ? 34.982 42.336  28.598 1.00 16.03 ? 110  ILE   A HG13 1 
ATOM   1706  H  HG21 . ILE   A 1 110 ? 37.946 41.027  27.142 1.00 14.27 ? 110  ILE   A HG21 1 
ATOM   1707  H  HG22 . ILE   A 1 110 ? 37.820 41.730  25.728 1.00 14.27 ? 110  ILE   A HG22 1 
ATOM   1708  H  HG23 . ILE   A 1 110 ? 38.236 42.577  27.000 1.00 14.27 ? 110  ILE   A HG23 1 
ATOM   1709  H  HD11 . ILE   A 1 110 ? 36.111 40.985  30.123 1.00 17.31 ? 110  ILE   A HD11 1 
ATOM   1710  H  HD12 . ILE   A 1 110 ? 35.831 40.157  28.802 1.00 17.31 ? 110  ILE   A HD12 1 
ATOM   1711  H  HD13 . ILE   A 1 110 ? 37.273 40.752  29.072 1.00 17.31 ? 110  ILE   A HD13 1 
ATOM   1712  N  N    . ILE   A 1 111 ? 36.902 43.934  24.120 1.00 11.49 ? 111  ILE   A N    1 
ATOM   1713  C  CA   . ILE   A 1 111 ? 37.168 43.730  22.669 1.00 12.94 ? 111  ILE   A CA   1 
ATOM   1714  C  C    . ILE   A 1 111 ? 38.520 43.019  22.558 1.00 12.70 ? 111  ILE   A C    1 
ATOM   1715  O  O    . ILE   A 1 111 ? 39.527 43.609  22.974 1.00 12.74 ? 111  ILE   A O    1 
ATOM   1716  C  CB   . ILE   A 1 111 ? 37.145 45.061  21.890 1.00 9.79  ? 111  ILE   A CB   1 
ATOM   1717  C  CG1  . ILE   A 1 111 ? 35.848 45.838  22.130 1.00 10.21 ? 111  ILE   A CG1  1 
ATOM   1718  C  CG2  . ILE   A 1 111 ? 37.394 44.818  20.410 1.00 9.68  ? 111  ILE   A CG2  1 
ATOM   1719  C  CD1  . ILE   A 1 111 ? 35.891 47.264  21.632 1.00 15.32 ? 111  ILE   A CD1  1 
ATOM   1720  H  H    . ILE   A 1 111 ? 37.421 44.500  24.507 1.00 13.79 ? 111  ILE   A H    1 
ATOM   1721  H  HA   . ILE   A 1 111 ? 36.471 43.188  22.268 1.00 15.53 ? 111  ILE   A HA   1 
ATOM   1722  H  HB   . ILE   A 1 111 ? 37.866 45.616  22.226 1.00 11.75 ? 111  ILE   A HB   1 
ATOM   1723  H  HG12 . ILE   A 1 111 ? 35.117 45.374  21.693 1.00 12.26 ? 111  ILE   A HG12 1 
ATOM   1724  H  HG13 . ILE   A 1 111 ? 35.654 45.842  23.080 1.00 12.26 ? 111  ILE   A HG13 1 
ATOM   1725  H  HG21 . ILE   A 1 111 ? 37.376 45.664  19.936 1.00 11.62 ? 111  ILE   A HG21 1 
ATOM   1726  H  HG22 . ILE   A 1 111 ? 38.261 44.400  20.292 1.00 11.62 ? 111  ILE   A HG22 1 
ATOM   1727  H  HG23 . ILE   A 1 111 ? 36.704 44.235  20.057 1.00 11.62 ? 111  ILE   A HG23 1 
ATOM   1728  H  HD11 . ILE   A 1 111 ? 35.042 47.696  21.815 1.00 18.38 ? 111  ILE   A HD11 1 
ATOM   1729  H  HD12 . ILE   A 1 111 ? 36.602 47.744  22.085 1.00 18.38 ? 111  ILE   A HD12 1 
ATOM   1730  H  HD13 . ILE   A 1 111 ? 36.056 47.268  20.676 1.00 18.38 ? 111  ILE   A HD13 1 
ATOM   1731  N  N    . VAL   A 1 112 ? 38.520 41.788  22.055 1.00 11.72 ? 112  VAL   A N    1 
ATOM   1732  C  CA   . VAL   A 1 112 ? 39.753 41.017  21.909 1.00 12.45 ? 112  VAL   A CA   1 
ATOM   1733  C  C    . VAL   A 1 112 ? 40.174 41.039  20.448 1.00 11.64 ? 112  VAL   A C    1 
ATOM   1734  O  O    . VAL   A 1 112 ? 39.394 40.645  19.567 1.00 13.63 ? 112  VAL   A O    1 
ATOM   1735  C  CB   . VAL   A 1 112 ? 39.576 39.570  22.405 1.00 11.55 ? 112  VAL   A CB   1 
ATOM   1736  C  CG1  . VAL   A 1 112 ? 40.898 38.817  22.301 1.00 12.44 ? 112  VAL   A CG1  1 
ATOM   1737  C  CG2  . VAL   A 1 112 ? 39.058 39.544  23.843 1.00 11.74 ? 112  VAL   A CG2  1 
ATOM   1738  H  H    . VAL   A 1 112 ? 37.812 41.378  21.790 1.00 14.06 ? 112  VAL   A H    1 
ATOM   1739  H  HA   . VAL   A 1 112 ? 40.445 41.421  22.456 1.00 14.94 ? 112  VAL   A HA   1 
ATOM   1740  H  HB   . VAL   A 1 112 ? 38.919 39.132  21.842 1.00 13.86 ? 112  VAL   A HB   1 
ATOM   1741  H  HG11 . VAL   A 1 112 ? 40.778 37.907  22.615 1.00 14.93 ? 112  VAL   A HG11 1 
ATOM   1742  H  HG12 . VAL   A 1 112 ? 41.191 38.803  21.376 1.00 14.93 ? 112  VAL   A HG12 1 
ATOM   1743  H  HG13 . VAL   A 1 112 ? 41.567 39.261  22.845 1.00 14.93 ? 112  VAL   A HG13 1 
ATOM   1744  H  HG21 . VAL   A 1 112 ? 38.954 38.624  24.133 1.00 14.09 ? 112  VAL   A HG21 1 
ATOM   1745  H  HG22 . VAL   A 1 112 ? 39.690 39.997  24.423 1.00 14.09 ? 112  VAL   A HG22 1 
ATOM   1746  H  HG23 . VAL   A 1 112 ? 38.200 39.995  23.886 1.00 14.09 ? 112  VAL   A HG23 1 
ATOM   1747  N  N    . GLU   A 1 113 ? 41.413 41.484  20.216 1.00 12.31 ? 113  GLU   A N    1 
ATOM   1748  C  CA   . GLU   A 1 113 ? 41.887 41.668  18.825 1.00 12.77 ? 113  GLU   A CA   1 
ATOM   1749  C  C    . GLU   A 1 113 ? 43.066 40.769  18.457 1.00 14.49 ? 113  GLU   A C    1 
ATOM   1750  O  O    . GLU   A 1 113 ? 43.822 40.381  19.364 1.00 15.00 ? 113  GLU   A O    1 
ATOM   1751  C  CB   . GLU   A 1 113 ? 42.402 43.097  18.639 1.00 15.89 ? 113  GLU   A CB   1 
ATOM   1752  C  CG   . GLU   A 1 113 ? 41.404 44.181  18.996 1.00 15.59 ? 113  GLU   A CG   1 
ATOM   1753  C  CD   . GLU   A 1 113 ? 41.987 45.582  18.929 1.00 19.98 ? 113  GLU   A CD   1 
ATOM   1754  O  OE1  . GLU   A 1 113 ? 43.179 45.738  19.259 1.00 17.49 ? 113  GLU   A OE1  1 
ATOM   1755  O  OE2  . GLU   A 1 113 ? 41.251 46.510  18.544 1.00 17.18 ? 113  GLU   A OE2  1 
ATOM   1756  H  H    . GLU   A 1 113 ? 41.985 41.682  20.827 1.00 14.78 ? 113  GLU   A H    1 
ATOM   1757  H  HA   . GLU   A 1 113 ? 41.123 41.454  18.266 1.00 15.32 ? 113  GLU   A HA   1 
ATOM   1758  H  HB2  . GLU   A 1 113 ? 43.197 43.215  19.182 1.00 19.08 ? 113  GLU   A HB2  1 
ATOM   1759  H  HB3  . GLU   A 1 113 ? 42.671 43.213  17.714 1.00 19.08 ? 113  GLU   A HB3  1 
ATOM   1760  H  HG2  . GLU   A 1 113 ? 40.646 44.124  18.394 1.00 18.72 ? 113  GLU   A HG2  1 
ATOM   1761  H  HG3  . GLU   A 1 113 ? 41.068 44.020  19.892 1.00 18.72 ? 113  GLU   A HG3  1 
ATOM   1762  N  N    . ASP   A 1 114 ? 43.189 40.455  17.171 1.00 13.35 ? 114  ASP   A N    1 
ATOM   1763  C  CA   . ASP   A 1 114 ? 44.365 39.710  16.655 1.00 15.44 ? 114  ASP   A CA   1 
ATOM   1764  C  C    . ASP   A 1 114 ? 44.505 38.320  17.278 1.00 14.63 ? 114  ASP   A C    1 
ATOM   1765  O  O    . ASP   A 1 114 ? 43.498 37.747  17.700 1.00 13.21 ? 114  ASP   A O    1 
ATOM   1766  C  CB   . ASP   A 1 114 ? 45.632 40.557  16.811 1.00 15.90 ? 114  ASP   A CB   1 
ATOM   1767  C  CG   . ASP   A 1 114 ? 46.600 40.371  15.656 1.00 21.08 ? 114  ASP   A CG   1 
ATOM   1768  O  OD1  . ASP   A 1 114 ? 47.085 39.240  15.483 1.00 19.70 ? 114  ASP   A OD1  1 
ATOM   1769  O  OD2  . ASP   A 1 114 ? 46.850 41.354  14.937 1.00 20.19 ? 114  ASP   A OD2  1 
ATOM   1770  H  H    . ASP   A 1 114 ? 42.608 40.659  16.571 1.00 16.03 ? 114  ASP   A H    1 
ATOM   1771  H  HA   . ASP   A 1 114 ? 44.225 39.549  15.709 1.00 18.53 ? 114  ASP   A HA   1 
ATOM   1772  H  HB2  . ASP   A 1 114 ? 45.386 41.493  16.876 1.00 19.09 ? 114  ASP   A HB2  1 
ATOM   1773  H  HB3  . ASP   A 1 114 ? 46.075 40.322  17.641 1.00 19.09 ? 114  ASP   A HB3  1 
ATOM   1774  N  N    . LYS   A 1 115 ? 45.735 37.814  17.308 1.00 15.64 ? 115  LYS   A N    1 
ATOM   1775  C  CA   . LYS   A 1 115 ? 45.956 36.434  17.801 1.00 16.63 ? 115  LYS   A CA   1 
ATOM   1776  C  C    . LYS   A 1 115 ? 47.248 36.363  18.616 1.00 16.68 ? 115  LYS   A C    1 
ATOM   1777  O  O    . LYS   A 1 115 ? 48.248 36.957  18.191 1.00 18.43 ? 115  LYS   A O    1 
ATOM   1778  C  CB   . LYS   A 1 115 ? 46.058 35.474  16.617 1.00 14.67 ? 115  LYS   A CB   1 
ATOM   1779  C  CG   . LYS   A 1 115 ? 46.409 34.036  16.964 1.00 18.07 ? 115  LYS   A CG   1 
ATOM   1780  C  CD   . LYS   A 1 115 ? 46.757 33.219  15.743 1.00 20.67 ? 115  LYS   A CD   1 
ATOM   1781  C  CE   . LYS   A 1 115 ? 47.013 31.763  16.066 1.00 22.66 ? 115  LYS   A CE   1 
ATOM   1782  N  NZ   . LYS   A 1 115 ? 47.168 30.952  14.836 1.00 28.62 ? 115  LYS   A NZ   1 
ATOM   1783  H  H    . LYS   A 1 115 ? 46.444 38.231  17.057 1.00 18.77 ? 115  LYS   A H    1 
ATOM   1784  H  HA   . LYS   A 1 115 ? 45.208 36.182  18.365 1.00 19.95 ? 115  LYS   A HA   1 
ATOM   1785  H  HB2  . LYS   A 1 115 ? 45.211 35.478  16.144 1.00 17.61 ? 115  LYS   A HB2  1 
ATOM   1786  H  HB3  . LYS   A 1 115 ? 46.727 35.814  16.003 1.00 17.61 ? 115  LYS   A HB3  1 
ATOM   1787  H  HG2  . LYS   A 1 115 ? 47.158 34.028  17.580 1.00 21.68 ? 115  LYS   A HG2  1 
ATOM   1788  H  HG3  . LYS   A 1 115 ? 45.660 33.624  17.423 1.00 21.68 ? 115  LYS   A HG3  1 
ATOM   1789  H  HD2  . LYS   A 1 115 ? 46.033 33.281  15.100 1.00 24.80 ? 115  LYS   A HD2  1 
ATOM   1790  H  HD3  . LYS   A 1 115 ? 47.545 33.596  15.320 1.00 24.80 ? 115  LYS   A HD3  1 
ATOM   1791  H  HE2  . LYS   A 1 115 ? 47.814 31.687  16.608 1.00 27.19 ? 115  LYS   A HE2  1 
ATOM   1792  H  HE3  . LYS   A 1 115 ? 46.278 31.414  16.595 1.00 27.19 ? 115  LYS   A HE3  1 
ATOM   1793  H  HZ1  . LYS   A 1 115 ? 47.459 30.139  15.051 1.00 34.35 ? 115  LYS   A HZ1  1 
ATOM   1794  H  HZ2  . LYS   A 1 115 ? 46.383 30.886  14.423 1.00 34.35 ? 115  LYS   A HZ2  1 
ATOM   1795  H  HZ3  . LYS   A 1 115 ? 47.756 31.343  14.294 1.00 34.35 ? 115  LYS   A HZ3  1 
ATOM   1796  N  N    . ALA   A 1 116 ? 47.208 35.657  19.739 1.00 16.48 ? 116  ALA   A N    1 
ATOM   1797  C  CA   . ALA   A 1 116 ? 48.425 35.449  20.556 1.00 15.00 ? 116  ALA   A CA   1 
ATOM   1798  C  C    . ALA   A 1 116 ? 49.301 34.405  19.861 1.00 18.57 ? 116  ALA   A C    1 
ATOM   1799  O  O    . ALA   A 1 116 ? 48.752 33.514  19.196 1.00 17.89 ? 116  ALA   A O    1 
ATOM   1800  C  CB   . ALA   A 1 116 ? 48.057 35.017  21.950 1.00 18.34 ? 116  ALA   A CB   1 
ATOM   1801  H  H    . ALA   A 1 116 ? 46.498 35.288  20.053 1.00 19.78 ? 116  ALA   A H    1 
ATOM   1802  H  HA   . ALA   A 1 116 ? 48.920 36.279  20.636 1.00 18.01 ? 116  ALA   A HA   1 
ATOM   1803  H  HB1  . ALA   A 1 116 ? 48.864 34.885  22.472 1.00 22.02 ? 116  ALA   A HB1  1 
ATOM   1804  H  HB2  . ALA   A 1 116 ? 47.511 35.701  22.367 1.00 22.02 ? 116  ALA   A HB2  1 
ATOM   1805  H  HB3  . ALA   A 1 116 ? 47.559 34.186  21.910 1.00 22.02 ? 116  ALA   A HB3  1 
ATOM   1806  N  N    . ASP   A 1 117 ? 50.622 34.529  20.003 1.00 19.13 ? 117  ASP   A N    1 
ATOM   1807  C  CA   . ASP   A 1 117 ? 51.538 33.607  19.281 1.00 23.32 ? 117  ASP   A CA   1 
ATOM   1808  C  C    . ASP   A 1 117 ? 51.569 32.250  19.990 1.00 22.86 ? 117  ASP   A C    1 
ATOM   1809  O  O    . ASP   A 1 117 ? 52.143 31.311  19.425 1.00 26.31 ? 117  ASP   A O    1 
ATOM   1810  C  CB   . ASP   A 1 117 ? 52.927 34.229  19.126 1.00 23.13 ? 117  ASP   A CB   1 
ATOM   1811  C  CG   . ASP   A 1 117 ? 53.511 34.754  20.425 1.00 26.79 ? 117  ASP   A CG   1 
ATOM   1812  O  OD1  . ASP   A 1 117 ? 52.955 34.435  21.491 1.00 25.94 ? 117  ASP   A OD1  1 
ATOM   1813  O  OD2  . ASP   A 1 117 ? 54.520 35.482  20.357 1.00 39.98 ? 117  ASP   A OD2  1 
ATOM   1814  H  H    . ASP   A 1 117 ? 51.009 35.119  20.495 1.00 22.96 ? 117  ASP   A H    1 
ATOM   1815  H  HA   . ASP   A 1 117 ? 51.207 33.458  18.382 1.00 27.99 ? 117  ASP   A HA   1 
ATOM   1816  H  HB2  . ASP   A 1 117 ? 53.530 33.566  18.755 1.00 27.76 ? 117  ASP   A HB2  1 
ATOM   1817  H  HB3  . ASP   A 1 117 ? 52.877 34.956  18.486 1.00 27.76 ? 117  ASP   A HB3  1 
ATOM   1818  N  N    . SER   A 1 118 ? 50.966 32.166  21.172 1.00 19.14 ? 118  SER   A N    1 
ATOM   1819  C  CA   . SER   A 1 118 ? 50.887 30.885  21.915 1.00 20.15 ? 118  SER   A CA   1 
ATOM   1820  C  C    . SER   A 1 118 ? 49.646 30.924  22.813 1.00 18.43 ? 118  SER   A C    1 
ATOM   1821  O  O    . SER   A 1 118 ? 49.191 32.033  23.133 1.00 17.19 ? 118  SER   A O    1 
ATOM   1822  C  CB   . SER   A 1 118 ? 52.152 30.635  22.716 1.00 23.90 ? 118  SER   A CB   1 
ATOM   1823  O  OG   . SER   A 1 118 ? 52.230 31.505  23.834 1.00 28.19 ? 118  SER   A OG   1 
ATOM   1824  H  H    . SER   A 1 118 ? 50.594 32.831  21.570 1.00 22.97 ? 118  SER   A H    1 
ATOM   1825  H  HA   . SER   A 1 118 ? 50.809 30.147  21.291 1.00 24.18 ? 118  SER   A HA   1 
ATOM   1826  H  HB2  . SER   A 1 118 ? 52.170 29.713  23.018 1.00 28.68 ? 118  SER   A HB2  1 
ATOM   1827  H  HB3  . SER   A 1 118 ? 52.928 30.763  22.148 1.00 28.68 ? 118  SER   A HB3  1 
ATOM   1828  H  HG   . SER   A 1 118 ? 52.901 32.004  23.755 1.00 33.83 ? 118  SER   A HG   1 
ATOM   1829  N  N    . PRO   A 1 119 ? 49.079 29.769  23.227 1.00 19.82 ? 119  PRO   A N    1 
ATOM   1830  C  CA   . PRO   A 1 119 ? 47.852 29.766  24.023 1.00 14.41 ? 119  PRO   A CA   1 
ATOM   1831  C  C    . PRO   A 1 119 ? 48.011 30.633  25.278 1.00 15.46 ? 119  PRO   A C    1 
ATOM   1832  O  O    . PRO   A 1 119 ? 48.999 30.493  25.969 1.00 16.45 ? 119  PRO   A O    1 
ATOM   1833  C  CB   . PRO   A 1 119 ? 47.675 28.296  24.424 1.00 15.83 ? 119  PRO   A CB   1 
ATOM   1834  C  CG   . PRO   A 1 119 ? 48.408 27.536  23.344 1.00 19.37 ? 119  PRO   A CG   1 
ATOM   1835  C  CD   . PRO   A 1 119 ? 49.575 28.415  22.962 1.00 20.06 ? 119  PRO   A CD   1 
ATOM   1836  H  HA   . PRO   A 1 119 ? 47.095 30.124  23.533 1.00 17.29 ? 119  PRO   A HA   1 
ATOM   1837  H  HB2  . PRO   A 1 119 ? 48.050 28.119  25.301 1.00 19.00 ? 119  PRO   A HB2  1 
ATOM   1838  H  HB3  . PRO   A 1 119 ? 46.738 28.047  24.461 1.00 19.00 ? 119  PRO   A HB3  1 
ATOM   1839  H  HG2  . PRO   A 1 119 ? 48.711 26.673  23.667 1.00 23.25 ? 119  PRO   A HG2  1 
ATOM   1840  H  HG3  . PRO   A 1 119 ? 47.832 27.368  22.582 1.00 23.25 ? 119  PRO   A HG3  1 
ATOM   1841  H  HD2  . PRO   A 1 119 ? 50.363 28.213  23.490 1.00 24.07 ? 119  PRO   A HD2  1 
ATOM   1842  H  HD3  . PRO   A 1 119 ? 49.820 28.300  22.031 1.00 24.07 ? 119  PRO   A HD3  1 
ATOM   1843  N  N    . VAL   A 1 120 ? 47.033 31.502  25.535 1.00 13.83 ? 120  VAL   A N    1 
ATOM   1844  C  CA   . VAL   A 1 120 ? 47.084 32.371  26.740 1.00 14.15 ? 120  VAL   A CA   1 
ATOM   1845  C  C    . VAL   A 1 120 ? 45.711 32.420  27.409 1.00 13.68 ? 120  VAL   A C    1 
ATOM   1846  O  O    . VAL   A 1 120 ? 44.747 31.900  26.826 1.00 13.12 ? 120  VAL   A O    1 
ATOM   1847  C  CB   . VAL   A 1 120 ? 47.522 33.802  26.378 1.00 16.73 ? 120  VAL   A CB   1 
ATOM   1848  C  CG1  . VAL   A 1 120 ? 48.902 33.835  25.741 1.00 15.67 ? 120  VAL   A CG1  1 
ATOM   1849  C  CG2  . VAL   A 1 120 ? 46.500 34.493  25.489 1.00 14.63 ? 120  VAL   A CG2  1 
ATOM   1850  H  H    . VAL   A 1 120 ? 46.338 31.611  25.040 1.00 16.60 ? 120  VAL   A H    1 
ATOM   1851  H  HA   . VAL   A 1 120 ? 47.735 31.992  27.351 1.00 16.99 ? 120  VAL   A HA   1 
ATOM   1852  H  HB   . VAL   A 1 120 ? 47.575 34.294  27.212 1.00 20.07 ? 120  VAL   A HB   1 
ATOM   1853  H  HG11 . VAL   A 1 120 ? 49.139 34.751  25.529 1.00 18.80 ? 120  VAL   A HG11 1 
ATOM   1854  H  HG12 . VAL   A 1 120 ? 49.553 33.468  26.359 1.00 18.80 ? 120  VAL   A HG12 1 
ATOM   1855  H  HG13 . VAL   A 1 120 ? 48.896 33.307  24.927 1.00 18.80 ? 120  VAL   A HG13 1 
ATOM   1856  H  HG21 . VAL   A 1 120 ? 46.806 35.390  25.280 1.00 17.55 ? 120  VAL   A HG21 1 
ATOM   1857  H  HG22 . VAL   A 1 120 ? 46.392 33.989  24.667 1.00 17.55 ? 120  VAL   A HG22 1 
ATOM   1858  H  HG23 . VAL   A 1 120 ? 45.649 34.542  25.952 1.00 17.55 ? 120  VAL   A HG23 1 
ATOM   1859  N  N    . TYR   A 1 121 ? 45.651 33.000  28.603 1.00 13.36 ? 121  TYR   A N    1 
ATOM   1860  C  CA   . TYR   A 1 121 ? 44.345 33.238  29.263 1.00 13.81 ? 121  TYR   A CA   1 
ATOM   1861  C  C    . TYR   A 1 121 ? 44.390 34.672  29.809 1.00 14.23 ? 121  TYR   A C    1 
ATOM   1862  O  O    . TYR   A 1 121 ? 45.493 35.206  30.009 1.00 14.76 ? 121  TYR   A O    1 
ATOM   1863  C  CB   . TYR   A 1 121 ? 44.015 32.183  30.321 1.00 14.52 ? 121  TYR   A CB   1 
ATOM   1864  C  CG   . TYR   A 1 121 ? 44.901 32.142  31.540 1.00 13.97 ? 121  TYR   A CG   1 
ATOM   1865  C  CD1  . TYR   A 1 121 ? 46.035 31.349  31.565 1.00 16.22 ? 121  TYR   A CD1  1 
ATOM   1866  C  CD2  . TYR   A 1 121 ? 44.581 32.852  32.684 1.00 15.23 ? 121  TYR   A CD2  1 
ATOM   1867  C  CE1  . TYR   A 1 121 ? 46.844 31.282  32.686 1.00 19.04 ? 121  TYR   A CE1  1 
ATOM   1868  C  CE2  . TYR   A 1 121 ? 45.379 32.797  33.814 1.00 16.31 ? 121  TYR   A CE2  1 
ATOM   1869  C  CZ   . TYR   A 1 121 ? 46.514 32.006  33.815 1.00 19.69 ? 121  TYR   A CZ   1 
ATOM   1870  O  OH   . TYR   A 1 121 ? 47.317 31.939  34.926 1.00 22.21 ? 121  TYR   A OH   1 
ATOM   1871  H  H    . TYR   A 1 121 ? 46.336 33.264  29.051 1.00 16.04 ? 121  TYR   A H    1 
ATOM   1872  H  HA   . TYR   A 1 121 ? 43.615 33.150  28.630 1.00 16.58 ? 121  TYR   A HA   1 
ATOM   1873  H  HB2  . TYR   A 1 121 ? 43.102 32.326  30.616 1.00 17.42 ? 121  TYR   A HB2  1 
ATOM   1874  H  HB3  . TYR   A 1 121 ? 44.043 31.311  29.897 1.00 17.42 ? 121  TYR   A HB3  1 
ATOM   1875  H  HD1  . TYR   A 1 121 ? 46.258 30.850  30.812 1.00 19.47 ? 121  TYR   A HD1  1 
ATOM   1876  H  HD2  . TYR   A 1 121 ? 43.814 33.377  32.694 1.00 18.28 ? 121  TYR   A HD2  1 
ATOM   1877  H  HE1  . TYR   A 1 121 ? 47.608 30.751  32.679 1.00 22.85 ? 121  TYR   A HE1  1 
ATOM   1878  H  HE2  . TYR   A 1 121 ? 45.153 33.290  34.570 1.00 19.57 ? 121  TYR   A HE2  1 
ATOM   1879  H  HH   . TYR   A 1 121 ? 46.977 32.394  35.545 1.00 26.66 ? 121  TYR   A HH   1 
ATOM   1880  N  N    . ILE   A 1 122 ? 43.223 35.283  29.998 1.00 13.13 ? 122  ILE   A N    1 
ATOM   1881  C  CA   . ILE   A 1 122 ? 43.164 36.676  30.520 1.00 12.44 ? 122  ILE   A CA   1 
ATOM   1882  C  C    . ILE   A 1 122 ? 42.652 36.627  31.962 1.00 12.49 ? 122  ILE   A C    1 
ATOM   1883  O  O    . ILE   A 1 122 ? 41.648 35.942  32.210 1.00 12.86 ? 122  ILE   A O    1 
ATOM   1884  C  CB   . ILE   A 1 122 ? 42.297 37.568  29.609 1.00 14.24 ? 122  ILE   A CB   1 
ATOM   1885  C  CG1  . ILE   A 1 122 ? 42.912 37.718  28.216 1.00 14.18 ? 122  ILE   A CG1  1 
ATOM   1886  C  CG2  . ILE   A 1 122 ? 42.035 38.915  30.262 1.00 12.61 ? 122  ILE   A CG2  1 
ATOM   1887  C  CD1  . ILE   A 1 122 ? 41.924 38.132  27.151 1.00 11.93 ? 122  ILE   A CD1  1 
ATOM   1888  H  H    . ILE   A 1 122 ? 42.457 34.926  29.837 1.00 15.75 ? 122  ILE   A H    1 
ATOM   1889  H  HA   . ILE   A 1 122 ? 44.047 37.077  30.520 1.00 14.93 ? 122  ILE   A HA   1 
ATOM   1890  H  HB   . ILE   A 1 122 ? 41.440 37.129  29.490 1.00 17.09 ? 122  ILE   A HB   1 
ATOM   1891  H  HG12 . ILE   A 1 122 ? 43.625 38.375  28.256 1.00 17.02 ? 122  ILE   A HG12 1 
ATOM   1892  H  HG13 . ILE   A 1 122 ? 43.317 36.875  27.959 1.00 17.02 ? 122  ILE   A HG13 1 
ATOM   1893  H  HG21 . ILE   A 1 122 ? 41.489 39.459  29.673 1.00 15.14 ? 122  ILE   A HG21 1 
ATOM   1894  H  HG22 . ILE   A 1 122 ? 41.570 38.782  31.103 1.00 15.14 ? 122  ILE   A HG22 1 
ATOM   1895  H  HG23 . ILE   A 1 122 ? 42.879 39.364  30.427 1.00 15.14 ? 122  ILE   A HG23 1 
ATOM   1896  H  HD11 . ILE   A 1 122 ? 42.380 38.208  26.298 1.00 14.32 ? 122  ILE   A HD11 1 
ATOM   1897  H  HD12 . ILE   A 1 122 ? 41.222 37.466  27.084 1.00 14.32 ? 122  ILE   A HD12 1 
ATOM   1898  H  HD13 . ILE   A 1 122 ? 41.535 38.989  27.386 1.00 14.32 ? 122  ILE   A HD13 1 
ATOM   1899  N  N    . GLU   A 1 123 ? 43.348 37.311  32.870 1.00 13.21 ? 123  GLU   A N    1 
ATOM   1900  C  CA   . GLU   A 1 123 ? 42.977 37.296  34.307 1.00 13.45 ? 123  GLU   A CA   1 
ATOM   1901  C  C    . GLU   A 1 123 ? 42.545 38.701  34.734 1.00 13.86 ? 123  GLU   A C    1 
ATOM   1902  O  O    . GLU   A 1 123 ? 43.378 39.613  34.676 1.00 14.19 ? 123  GLU   A O    1 
ATOM   1903  C  CB   . GLU   A 1 123 ? 44.164 36.816  35.139 1.00 15.63 ? 123  GLU   A CB   1 
ATOM   1904  C  CG   . GLU   A 1 123 ? 43.827 36.585  36.597 1.00 14.76 ? 123  GLU   A CG   1 
ATOM   1905  C  CD   . GLU   A 1 123 ? 44.982 36.016  37.400 1.00 19.68 ? 123  GLU   A CD   1 
ATOM   1906  O  OE1  . GLU   A 1 123 ? 45.955 35.554  36.782 1.00 21.54 ? 123  GLU   A OE1  1 
ATOM   1907  O  OE2  . GLU   A 1 123 ? 44.899 36.038  38.636 1.00 21.16 ? 123  GLU   A OE2  1 
ATOM   1908  H  H    . GLU   A 1 123 ? 44.037 37.791  32.686 1.00 15.86 ? 123  GLU   A H    1 
ATOM   1909  H  HA   . GLU   A 1 123 ? 42.236 36.686  34.450 1.00 16.15 ? 123  GLU   A HA   1 
ATOM   1910  H  HB2  . GLU   A 1 123 ? 44.504 35.991  34.759 1.00 18.75 ? 123  GLU   A HB2  1 
ATOM   1911  H  HB3  . GLU   A 1 123 ? 44.877 37.471  35.079 1.00 18.75 ? 123  GLU   A HB3  1 
ATOM   1912  H  HG2  . GLU   A 1 123 ? 43.548 37.425  36.995 1.00 17.71 ? 123  GLU   A HG2  1 
ATOM   1913  H  HG3  . GLU   A 1 123 ? 43.072 35.979  36.655 1.00 17.71 ? 123  GLU   A HG3  1 
ATOM   1914  N  N    . ILE   A 1 124 ? 41.288 38.848  35.154 1.00 14.47 ? 124  ILE   A N    1 
ATOM   1915  C  CA   . ILE   A 1 124 ? 40.763 40.195  35.506 1.00 12.90 ? 124  ILE   A CA   1 
ATOM   1916  C  C    . ILE   A 1 124 ? 40.325 40.235  36.966 1.00 14.17 ? 124  ILE   A C    1 
ATOM   1917  O  O    . ILE   A 1 124 ? 39.556 39.349  37.374 1.00 14.04 ? 124  ILE   A O    1 
ATOM   1918  C  CB   . ILE   A 1 124 ? 39.579 40.588  34.598 1.00 14.60 ? 124  ILE   A CB   1 
ATOM   1919  C  CG1  . ILE   A 1 124 ? 39.958 40.582  33.116 1.00 16.03 ? 124  ILE   A CG1  1 
ATOM   1920  C  CG2  . ILE   A 1 124 ? 38.997 41.926  35.028 1.00 12.95 ? 124  ILE   A CG2  1 
ATOM   1921  C  CD1  . ILE   A 1 124 ? 38.765 40.584  32.189 1.00 13.43 ? 124  ILE   A CD1  1 
ATOM   1922  H  H    . ILE   A 1 124 ? 40.725 38.204  35.244 1.00 17.37 ? 124  ILE   A H    1 
ATOM   1923  H  HA   . ILE   A 1 124 ? 41.481 40.833  35.371 1.00 15.49 ? 124  ILE   A HA   1 
ATOM   1924  H  HB   . ILE   A 1 124 ? 38.891 39.913  34.704 1.00 17.53 ? 124  ILE   A HB   1 
ATOM   1925  H  HG12 . ILE   A 1 124 ? 40.507 41.359  32.927 1.00 19.24 ? 124  ILE   A HG12 1 
ATOM   1926  H  HG13 . ILE   A 1 124 ? 40.501 39.800  32.931 1.00 19.24 ? 124  ILE   A HG13 1 
ATOM   1927  H  HG21 . ILE   A 1 124 ? 38.255 42.158  34.448 1.00 15.54 ? 124  ILE   A HG21 1 
ATOM   1928  H  HG22 . ILE   A 1 124 ? 38.684 41.863  35.944 1.00 15.54 ? 124  ILE   A HG22 1 
ATOM   1929  H  HG23 . ILE   A 1 124 ? 39.681 42.611  34.967 1.00 15.54 ? 124  ILE   A HG23 1 
ATOM   1930  H  HD11 . ILE   A 1 124 ? 39.070 40.580  31.268 1.00 16.11 ? 124  ILE   A HD11 1 
ATOM   1931  H  HD12 . ILE   A 1 124 ? 38.226 39.795  32.354 1.00 16.11 ? 124  ILE   A HD12 1 
ATOM   1932  H  HD13 . ILE   A 1 124 ? 38.232 41.379  32.349 1.00 16.11 ? 124  ILE   A HD13 1 
ATOM   1933  N  N    . VAL   A 1 125 ? 40.824 41.215  37.713 1.00 13.76 ? 125  VAL   A N    1 
ATOM   1934  C  CA   . VAL   A 1 125 ? 40.322 41.448  39.091 1.00 15.94 ? 125  VAL   A CA   1 
ATOM   1935  C  C    . VAL   A 1 125 ? 40.039 42.949  39.133 1.00 17.11 ? 125  VAL   A C    1 
ATOM   1936  O  O    . VAL   A 1 125 ? 41.006 43.720  39.227 1.00 16.28 ? 125  VAL   A O    1 
ATOM   1937  C  CB   . VAL   A 1 125 ? 41.312 41.000  40.182 1.00 17.13 ? 125  VAL   A CB   1 
ATOM   1938  C  CG1  . VAL   A 1 125 ? 40.769 41.301  41.570 1.00 22.99 ? 125  VAL   A CG1  1 
ATOM   1939  C  CG2  . VAL   A 1 125 ? 41.651 39.524  40.057 1.00 18.45 ? 125  VAL   A CG2  1 
ATOM   1940  H  H    . VAL   A 1 125 ? 41.443 41.754  37.458 1.00 16.52 ? 125  VAL   A H    1 
ATOM   1941  H  HA   . VAL   A 1 125 ? 39.532 40.918  39.281 1.00 19.13 ? 125  VAL   A HA   1 
ATOM   1942  H  HB   . VAL   A 1 125 ? 42.129 41.507  40.054 1.00 20.56 ? 125  VAL   A HB   1 
ATOM   1943  H  HG11 . VAL   A 1 125 ? 41.409 41.010  42.238 1.00 27.59 ? 125  VAL   A HG11 1 
ATOM   1944  H  HG12 . VAL   A 1 125 ? 40.620 42.255  41.659 1.00 27.59 ? 125  VAL   A HG12 1 
ATOM   1945  H  HG13 . VAL   A 1 125 ? 39.931 40.830  41.699 1.00 27.59 ? 125  VAL   A HG13 1 
ATOM   1946  H  HG21 . VAL   A 1 125 ? 42.275 39.275  40.757 1.00 22.15 ? 125  VAL   A HG21 1 
ATOM   1947  H  HG22 . VAL   A 1 125 ? 40.841 38.997  40.144 1.00 22.15 ? 125  VAL   A HG22 1 
ATOM   1948  H  HG23 . VAL   A 1 125 ? 42.054 39.357  39.191 1.00 22.15 ? 125  VAL   A HG23 1 
ATOM   1949  N  N    . ASP   A 1 126 ? 38.773 43.333  38.998 1.00 14.63 ? 126  ASP   A N    1 
ATOM   1950  C  CA   . ASP   A 1 126 ? 38.427 44.775  38.910 1.00 16.04 ? 126  ASP   A CA   1 
ATOM   1951  C  C    . ASP   A 1 126 ? 39.210 45.385  37.739 1.00 16.24 ? 126  ASP   A C    1 
ATOM   1952  O  O    . ASP   A 1 126 ? 39.076 44.881  36.617 1.00 14.24 ? 126  ASP   A O    1 
ATOM   1953  C  CB   . ASP   A 1 126 ? 38.623 45.472  40.260 1.00 17.08 ? 126  ASP   A CB   1 
ATOM   1954  C  CG   . ASP   A 1 126 ? 37.593 45.055  41.295 1.00 19.65 ? 126  ASP   A CG   1 
ATOM   1955  O  OD1  . ASP   A 1 126 ? 36.441 44.788  40.901 1.00 18.96 ? 126  ASP   A OD1  1 
ATOM   1956  O  OD2  . ASP   A 1 126 ? 37.949 44.996  42.485 1.00 19.92 ? 126  ASP   A OD2  1 
ATOM   1957  H  H    . ASP   A 1 126 ? 38.103 42.796  38.955 1.00 17.55 ? 126  ASP   A H    1 
ATOM   1958  H  HA   . ASP   A 1 126 ? 37.485 44.903  38.718 1.00 19.25 ? 126  ASP   A HA   1 
ATOM   1959  H  HB2  . ASP   A 1 126 ? 39.511 45.273  40.596 1.00 20.50 ? 126  ASP   A HB2  1 
ATOM   1960  H  HB3  . ASP   A 1 126 ? 38.576 46.432  40.133 1.00 20.50 ? 126  ASP   A HB3  1 
ATOM   1961  N  N    . ASP   A 1 127 ? 40.023 46.414  38.000 1.00 17.04 ? 127  ASP   A N    1 
ATOM   1962  C  CA   . ASP   A 1 127 ? 40.744 47.103  36.896 1.00 16.34 ? 127  ASP   A CA   1 
ATOM   1963  C  C    . ASP   A 1 127 ? 42.101 46.446  36.608 1.00 18.75 ? 127  ASP   A C    1 
ATOM   1964  O  O    . ASP   A 1 127 ? 42.781 46.901  35.682 1.00 21.15 ? 127  ASP   A O    1 
ATOM   1965  C  CB   . ASP   A 1 127 ? 40.928 48.587  37.213 1.00 23.25 ? 127  ASP   A CB   1 
ATOM   1966  C  CG   . ASP   A 1 127 ? 41.832 48.813  38.409 1.00 29.05 ? 127  ASP   A CG   1 
ATOM   1967  O  OD1  . ASP   A 1 127 ? 41.502 48.295  39.491 1.00 28.67 ? 127  ASP   A OD1  1 
ATOM   1968  O  OD2  . ASP   A 1 127 ? 42.861 49.493  38.244 1.00 38.23 ? 127  ASP   A OD2  1 
ATOM   1969  H  H    . ASP   A 1 127 ? 40.175 46.729  38.786 1.00 20.46 ? 127  ASP   A H    1 
ATOM   1970  H  HA   . ASP   A 1 127 ? 40.199 47.020  36.098 1.00 19.61 ? 127  ASP   A HA   1 
ATOM   1971  H  HB2  . ASP   A 1 127 ? 41.301 49.037  36.439 1.00 27.90 ? 127  ASP   A HB2  1 
ATOM   1972  H  HB3  . ASP   A 1 127 ? 40.062 48.989  37.385 1.00 27.90 ? 127  ASP   A HB3  1 
ATOM   1973  N  N    . LYS   A 1 128 ? 42.471 45.420  37.374 1.00 19.06 ? 128  LYS   A N    1 
ATOM   1974  C  CA   . LYS   A 1 128 ? 43.751 44.703  37.123 1.00 19.75 ? 128  LYS   A CA   1 
ATOM   1975  C  C    . LYS   A 1 128 ? 43.541 43.642  36.038 1.00 18.58 ? 128  LYS   A C    1 
ATOM   1976  O  O    . LYS   A 1 128 ? 42.723 42.738  36.257 1.00 15.87 ? 128  LYS   A O    1 
ATOM   1977  C  CB   . LYS   A 1 128 ? 44.288 44.053  38.402 1.00 21.74 ? 128  LYS   A CB   1 
ATOM   1978  C  CG   . LYS   A 1 128 ? 45.696 43.484  38.288 1.00 26.21 ? 128  LYS   A CG   1 
ATOM   1979  C  CD   . LYS   A 1 128 ? 46.037 42.492  39.377 1.00 36.59 ? 128  LYS   A CD   1 
ATOM   1980  C  CE   . LYS   A 1 128 ? 47.440 41.937  39.248 1.00 41.35 ? 128  LYS   A CE   1 
ATOM   1981  N  NZ   . LYS   A 1 128 ? 47.836 41.162  40.448 1.00 47.86 ? 128  LYS   A NZ   1 
ATOM   1982  H  H    . LYS   A 1 128 ? 42.012 45.118  38.036 1.00 22.88 ? 128  LYS   A H    1 
ATOM   1983  H  HA   . LYS   A 1 128 ? 44.409 45.349  36.822 1.00 23.70 ? 128  LYS   A HA   1 
ATOM   1984  H  HB2  . LYS   A 1 128 ? 44.276 44.712  39.114 1.00 26.09 ? 128  LYS   A HB2  1 
ATOM   1985  H  HB3  . LYS   A 1 128 ? 43.685 43.340  38.665 1.00 26.09 ? 128  LYS   A HB3  1 
ATOM   1986  H  HG2  . LYS   A 1 128 ? 45.793 43.052  37.425 1.00 31.46 ? 128  LYS   A HG2  1 
ATOM   1987  H  HG3  . LYS   A 1 128 ? 46.335 44.214  38.314 1.00 31.46 ? 128  LYS   A HG3  1 
ATOM   1988  H  HD2  . LYS   A 1 128 ? 45.942 42.922  40.241 1.00 43.91 ? 128  LYS   A HD2  1 
ATOM   1989  H  HD3  . LYS   A 1 128 ? 45.401 41.760  39.353 1.00 43.91 ? 128  LYS   A HD3  1 
ATOM   1990  H  HE2  . LYS   A 1 128 ? 47.493 41.369  38.464 1.00 49.62 ? 128  LYS   A HE2  1 
ATOM   1991  H  HE3  . LYS   A 1 128 ? 48.065 42.666  39.112 1.00 49.62 ? 128  LYS   A HE3  1 
ATOM   1992  H  HZ1  . LYS   A 1 128 ? 48.690 41.325  40.638 1.00 57.43 ? 128  LYS   A HZ1  1 
ATOM   1993  H  HZ2  . LYS   A 1 128 ? 47.328 41.403  41.138 1.00 57.43 ? 128  LYS   A HZ2  1 
ATOM   1994  H  HZ3  . LYS   A 1 128 ? 47.728 40.293  40.289 1.00 57.43 ? 128  LYS   A HZ3  1 
ATOM   1995  N  N    . VAL   A 1 129 ? 44.267 43.753  34.927 1.00 16.38 ? 129  VAL   A N    1 
ATOM   1996  C  CA   . VAL   A 1 129 ? 44.098 42.803  33.792 1.00 15.28 ? 129  VAL   A CA   1 
ATOM   1997  C  C    . VAL   A 1 129 ? 45.478 42.295  33.369 1.00 17.84 ? 129  VAL   A C    1 
ATOM   1998  O  O    . VAL   A 1 129 ? 46.370 43.129  33.138 1.00 16.78 ? 129  VAL   A O    1 
ATOM   1999  C  CB   . VAL   A 1 129 ? 43.359 43.463  32.611 1.00 15.87 ? 129  VAL   A CB   1 
ATOM   2000  C  CG1  . VAL   A 1 129 ? 43.071 42.471  31.495 1.00 16.75 ? 129  VAL   A CG1  1 
ATOM   2001  C  CG2  . VAL   A 1 129 ? 42.084 44.158  33.060 1.00 16.50 ? 129  VAL   A CG2  1 
ATOM   2002  H  H    . VAL   A 1 129 ? 44.861 44.361  34.798 1.00 19.65 ? 129  VAL   A H    1 
ATOM   2003  H  HA   . VAL   A 1 129 ? 43.551 42.055  34.078 1.00 18.34 ? 129  VAL   A HA   1 
ATOM   2004  H  HB   . VAL   A 1 129 ? 43.955 44.140  32.255 1.00 19.04 ? 129  VAL   A HB   1 
ATOM   2005  H  HG11 . VAL   A 1 129 ? 42.607 42.922  30.773 1.00 20.11 ? 129  VAL   A HG11 1 
ATOM   2006  H  HG12 . VAL   A 1 129 ? 43.906 42.105  31.164 1.00 20.11 ? 129  VAL   A HG12 1 
ATOM   2007  H  HG13 . VAL   A 1 129 ? 42.516 41.752  31.836 1.00 20.11 ? 129  VAL   A HG13 1 
ATOM   2008  H  HG21 . VAL   A 1 129 ? 41.647 44.560  32.293 1.00 19.81 ? 129  VAL   A HG21 1 
ATOM   2009  H  HG22 . VAL   A 1 129 ? 41.488 43.510  33.468 1.00 19.81 ? 129  VAL   A HG22 1 
ATOM   2010  H  HG23 . VAL   A 1 129 ? 42.302 44.848  33.706 1.00 19.81 ? 129  VAL   A HG23 1 
ATOM   2011  N  N    . GLU   A 1 130 ? 45.627 40.977  33.256 1.00 15.83 ? 130  GLU   A N    1 
ATOM   2012  C  CA   . GLU   A 1 130 ? 46.923 40.397  32.829 1.00 16.52 ? 130  GLU   A CA   1 
ATOM   2013  C  C    . GLU   A 1 130 ? 46.727 39.304  31.782 1.00 16.69 ? 130  GLU   A C    1 
ATOM   2014  O  O    . GLU   A 1 130 ? 45.685 38.624  31.826 1.00 16.65 ? 130  GLU   A O    1 
ATOM   2015  C  CB   . GLU   A 1 130 ? 47.661 39.772  34.014 1.00 17.37 ? 130  GLU   A CB   1 
ATOM   2016  C  CG   . GLU   A 1 130 ? 47.650 40.626  35.265 1.00 20.88 ? 130  GLU   A CG   1 
ATOM   2017  C  CD   . GLU   A 1 130 ? 48.301 39.955  36.462 1.00 30.17 ? 130  GLU   A CD   1 
ATOM   2018  O  OE1  . GLU   A 1 130 ? 47.591 39.247  37.198 1.00 30.44 ? 130  GLU   A OE1  1 
ATOM   2019  O  OE2  . GLU   A 1 130 ? 49.518 40.135  36.647 1.00 34.12 ? 130  GLU   A OE2  1 
ATOM   2020  H  H    . GLU   A 1 130 ? 45.008 40.402  33.416 1.00 19.00 ? 130  GLU   A H    1 
ATOM   2021  H  HA   . GLU   A 1 130 ? 47.440 41.127  32.454 1.00 19.83 ? 130  GLU   A HA   1 
ATOM   2022  H  HB2  . GLU   A 1 130 ? 47.260 38.912  34.217 1.00 20.85 ? 130  GLU   A HB2  1 
ATOM   2023  H  HB3  . GLU   A 1 130 ? 48.581 39.602  33.757 1.00 20.85 ? 130  GLU   A HB3  1 
ATOM   2024  H  HG2  . GLU   A 1 130 ? 48.109 41.461  35.082 1.00 25.06 ? 130  GLU   A HG2  1 
ATOM   2025  H  HG3  . GLU   A 1 130 ? 46.733 40.849  35.488 1.00 25.06 ? 130  GLU   A HG3  1 
ATOM   2026  N  N    . ILE   A 1 131 ? 47.685 39.170  30.869 1.00 16.40 ? 131  ILE   A N    1 
ATOM   2027  C  CA   . ILE   A 1 131 ? 47.667 38.053  29.884 1.00 16.01 ? 131  ILE   A CA   1 
ATOM   2028  C  C    . ILE   A 1 131 ? 48.706 37.046  30.384 1.00 16.82 ? 131  ILE   A C    1 
ATOM   2029  O  O    . ILE   A 1 131 ? 49.823 37.482  30.703 1.00 17.82 ? 131  ILE   A O    1 
ATOM   2030  C  CB   . ILE   A 1 131 ? 47.988 38.550  28.463 1.00 16.06 ? 131  ILE   A CB   1 
ATOM   2031  C  CG1  . ILE   A 1 131 ? 46.946 39.558  27.970 1.00 16.28 ? 131  ILE   A CG1  1 
ATOM   2032  C  CG2  . ILE   A 1 131 ? 48.140 37.381  27.503 1.00 17.38 ? 131  ILE   A CG2  1 
ATOM   2033  C  CD1  . ILE   A 1 131 ? 47.399 40.375  26.786 1.00 16.38 ? 131  ILE   A CD1  1 
ATOM   2034  H  H    . ILE   A 1 131 ? 48.355 39.703  30.792 1.00 19.69 ? 131  ILE   A H    1 
ATOM   2035  H  HA   . ILE   A 1 131 ? 46.788 37.647  29.821 1.00 19.22 ? 131  ILE   A HA   1 
ATOM   2036  H  HB   . ILE   A 1 131 ? 48.838 39.017  28.496 1.00 19.27 ? 131  ILE   A HB   1 
ATOM   2037  H  HG12 . ILE   A 1 131 ? 46.135 39.082  27.732 1.00 19.54 ? 131  ILE   A HG12 1 
ATOM   2038  H  HG13 . ILE   A 1 131 ? 46.719 40.158  28.698 1.00 19.54 ? 131  ILE   A HG13 1 
ATOM   2039  H  HG21 . ILE   A 1 131 ? 48.342 37.715  26.615 1.00 20.86 ? 131  ILE   A HG21 1 
ATOM   2040  H  HG22 . ILE   A 1 131 ? 48.862 36.807  27.804 1.00 20.86 ? 131  ILE   A HG22 1 
ATOM   2041  H  HG23 . ILE   A 1 131 ? 47.314 36.874  27.477 1.00 20.86 ? 131  ILE   A HG23 1 
ATOM   2042  H  HD11 . ILE   A 1 131 ? 46.694 40.989  26.528 1.00 19.65 ? 131  ILE   A HD11 1 
ATOM   2043  H  HD12 . ILE   A 1 131 ? 48.194 40.877  27.024 1.00 19.65 ? 131  ILE   A HD12 1 
ATOM   2044  H  HD13 . ILE   A 1 131 ? 47.601 39.785  26.043 1.00 19.65 ? 131  ILE   A HD13 1 
ATOM   2045  N  N    . LYS   A 1 132 ? 48.348 35.763  30.460 1.00 17.54 ? 132  LYS   A N    1 
ATOM   2046  C  CA   . LYS   A 1 132 ? 49.278 34.767  31.056 1.00 18.17 ? 132  LYS   A CA   1 
ATOM   2047  C  C    . LYS   A 1 132 ? 49.361 33.510  30.189 1.00 17.94 ? 132  LYS   A C    1 
ATOM   2048  O  O    . LYS   A 1 132 ? 48.422 33.255  29.423 1.00 15.92 ? 132  LYS   A O    1 
ATOM   2049  C  CB   . LYS   A 1 132 ? 48.828 34.419  32.476 1.00 19.30 ? 132  LYS   A CB   1 
ATOM   2050  C  CG   . LYS   A 1 132 ? 49.029 35.533  33.495 1.00 23.03 ? 132  LYS   A CG   1 
ATOM   2051  C  CD   . LYS   A 1 132 ? 48.723 35.128  34.919 1.00 23.72 ? 132  LYS   A CD   1 
ATOM   2052  C  CE   . LYS   A 1 132 ? 49.112 36.190  35.926 1.00 29.85 ? 132  LYS   A CE   1 
ATOM   2053  N  NZ   . LYS   A 1 132 ? 48.850 35.754  37.317 1.00 33.58 ? 132  LYS   A NZ   1 
ATOM   2054  H  H    . LYS   A 1 132 ? 47.598 35.445  30.185 1.00 21.05 ? 132  LYS   A H    1 
ATOM   2055  H  HA   . LYS   A 1 132 ? 50.165 35.157  31.096 1.00 21.80 ? 132  LYS   A HA   1 
ATOM   2056  H  HB2  . LYS   A 1 132 ? 47.888 34.181  32.456 1.00 23.16 ? 132  LYS   A HB2  1 
ATOM   2057  H  HB3  . LYS   A 1 132 ? 49.313 33.633  32.773 1.00 23.16 ? 132  LYS   A HB3  1 
ATOM   2058  H  HG2  . LYS   A 1 132 ? 49.948 35.841  33.447 1.00 27.64 ? 132  LYS   A HG2  1 
ATOM   2059  H  HG3  . LYS   A 1 132 ? 48.465 36.284  33.254 1.00 27.64 ? 132  LYS   A HG3  1 
ATOM   2060  H  HD2  . LYS   A 1 132 ? 47.775 34.942  35.001 1.00 28.47 ? 132  LYS   A HD2  1 
ATOM   2061  H  HD3  . LYS   A 1 132 ? 49.193 34.305  35.125 1.00 28.47 ? 132  LYS   A HD3  1 
ATOM   2062  H  HE2  . LYS   A 1 132 ? 50.053 36.401  35.825 1.00 35.82 ? 132  LYS   A HE2  1 
ATOM   2063  H  HE3  . LYS   A 1 132 ? 48.618 37.004  35.744 1.00 35.82 ? 132  LYS   A HE3  1 
ATOM   2064  H  HZ1  . LYS   A 1 132 ? 49.116 36.388  37.882 1.00 40.30 ? 132  LYS   A HZ1  1 
ATOM   2065  H  HZ2  . LYS   A 1 132 ? 47.978 35.609  37.424 1.00 40.30 ? 132  LYS   A HZ2  1 
ATOM   2066  H  HZ3  . LYS   A 1 132 ? 49.298 35.003  37.482 1.00 40.30 ? 132  LYS   A HZ3  1 
ATOM   2067  N  N    . ASP   A 1 133 ? 50.439 32.746  30.353 1.00 17.82 ? 133  ASP   A N    1 
ATOM   2068  C  CA   . ASP   A 1 133 ? 50.655 31.518  29.547 1.00 20.23 ? 133  ASP   A CA   1 
ATOM   2069  C  C    . ASP   A 1 133 ? 49.607 30.463  29.912 1.00 16.85 ? 133  ASP   A C    1 
ATOM   2070  O  O    . ASP   A 1 133 ? 49.434 30.196  31.104 1.00 17.33 ? 133  ASP   A O    1 
ATOM   2071  C  CB   . ASP   A 1 133 ? 52.076 30.989  29.749 1.00 24.89 ? 133  ASP   A CB   1 
ATOM   2072  C  CG   . ASP   A 1 133 ? 52.487 29.904  28.769 1.00 29.64 ? 133  ASP   A CG   1 
ATOM   2073  O  OD1  . ASP   A 1 133 ? 51.595 29.244  28.214 1.00 27.26 ? 133  ASP   A OD1  1 
ATOM   2074  O  OD2  . ASP   A 1 133 ? 53.703 29.731  28.576 1.00 36.27 ? 133  ASP   A OD2  1 
ATOM   2075  H  H    . ASP   A 1 133 ? 51.062 32.912  30.922 1.00 21.39 ? 133  ASP   A H    1 
ATOM   2076  H  HA   . ASP   A 1 133 ? 50.553 31.732  28.606 1.00 24.28 ? 133  ASP   A HA   1 
ATOM   2077  H  HB2  . ASP   A 1 133 ? 52.698 31.729  29.675 1.00 29.87 ? 133  ASP   A HB2  1 
ATOM   2078  H  HB3  . ASP   A 1 133 ? 52.155 30.641  30.651 1.00 29.87 ? 133  ASP   A HB3  1 
ATOM   2079  N  N    . ALA   A 1 134 ? 48.967 29.874  28.900 1.00 15.98 ? 134  ALA   A N    1 
ATOM   2080  C  CA   . ALA   A 1 134 ? 47.920 28.852  29.144 1.00 15.93 ? 134  ALA   A CA   1 
ATOM   2081  C  C    . ALA   A 1 134 ? 48.361 27.486  28.607 1.00 17.79 ? 134  ALA   A C    1 
ATOM   2082  O  O    . ALA   A 1 134 ? 47.493 26.635  28.383 1.00 14.60 ? 134  ALA   A O    1 
ATOM   2083  C  CB   . ALA   A 1 134 ? 46.630 29.292  28.495 1.00 15.52 ? 134  ALA   A CB   1 
ATOM   2084  H  H    . ALA   A 1 134 ? 49.116 30.044  28.070 1.00 19.18 ? 134  ALA   A H    1 
ATOM   2085  H  HA   . ALA   A 1 134 ? 47.779 28.762  30.100 1.00 19.12 ? 134  ALA   A HA   1 
ATOM   2086  H  HB1  . ALA   A 1 134 ? 45.944 28.625  28.653 1.00 18.63 ? 134  ALA   A HB1  1 
ATOM   2087  H  HB2  . ALA   A 1 134 ? 46.350 30.140  28.874 1.00 18.63 ? 134  ALA   A HB2  1 
ATOM   2088  H  HB3  . ALA   A 1 134 ? 46.766 29.394  27.540 1.00 18.63 ? 134  ALA   A HB3  1 
ATOM   2089  N  N    . SER   A 1 135 ? 49.669 27.282  28.430 1.00 17.57 ? 135  SER   A N    1 
ATOM   2090  C  CA   . SER   A 1 135 ? 50.176 26.016  27.840 1.00 21.16 ? 135  SER   A CA   1 
ATOM   2091  C  C    . SER   A 1 135 ? 49.772 24.804  28.692 1.00 22.99 ? 135  SER   A C    1 
ATOM   2092  O  O    . SER   A 1 135 ? 49.611 23.715  28.117 1.00 22.81 ? 135  SER   A O    1 
ATOM   2093  C  CB   . SER   A 1 135 ? 51.671 26.079  27.664 1.00 21.05 ? 135  SER   A CB   1 
ATOM   2094  O  OG   . SER   A 1 135 ? 52.309 26.265  28.917 1.00 23.94 ? 135  SER   A OG   1 
ATOM   2095  H  H    . SER   A 1 135 ? 50.280 27.850  28.639 1.00 21.09 ? 135  SER   A H    1 
ATOM   2096  H  HA   . SER   A 1 135 ? 49.770 25.907  26.966 1.00 25.40 ? 135  SER   A HA   1 
ATOM   2097  H  HB2  . SER   A 1 135 ? 51.989 25.261  27.251 1.00 25.27 ? 135  SER   A HB2  1 
ATOM   2098  H  HB3  . SER   A 1 135 ? 51.902 26.807  27.066 1.00 25.27 ? 135  SER   A HB3  1 
ATOM   2099  H  HG   . SER   A 1 135 ? 52.402 25.522  29.297 1.00 28.73 ? 135  SER   A HG   1 
ATOM   2100  N  N    . GLN   A 1 136 ? 49.627 24.987  30.004 1.00 17.82 ? 136  GLN   A N    1 
ATOM   2101  C  CA   . GLN   A 1 136 ? 49.301 23.847  30.902 1.00 21.40 ? 136  GLN   A CA   1 
ATOM   2102  C  C    . GLN   A 1 136 ? 47.783 23.637  30.976 1.00 20.99 ? 136  GLN   A C    1 
ATOM   2103  O  O    . GLN   A 1 136 ? 47.360 22.657  31.604 1.00 20.96 ? 136  GLN   A O    1 
ATOM   2104  C  CB   . GLN   A 1 136 ? 49.880 24.084  32.298 1.00 25.31 ? 136  GLN   A CB   1 
ATOM   2105  C  CG   . GLN   A 1 136 ? 51.390 24.272  32.304 1.00 27.27 ? 136  GLN   A CG   1 
ATOM   2106  C  CD   . GLN   A 1 136 ? 52.105 23.200  31.520 1.00 36.17 ? 136  GLN   A CD   1 
ATOM   2107  O  OE1  . GLN   A 1 136 ? 52.741 23.466  30.503 1.00 34.20 ? 136  GLN   A OE1  1 
ATOM   2108  N  NE2  . GLN   A 1 136 ? 52.007 21.969  31.994 1.00 33.95 ? 136  GLN   A NE2  1 
ATOM   2109  H  H    . GLN   A 1 136 ? 49.709 25.746  30.400 1.00 21.39 ? 136  GLN   A H    1 
ATOM   2110  H  HA   . GLN   A 1 136 ? 49.702 23.043  30.536 1.00 25.69 ? 136  GLN   A HA   1 
ATOM   2111  H  HB2  . GLN   A 1 136 ? 49.462 24.869  32.685 1.00 30.38 ? 136  GLN   A HB2  1 
ATOM   2112  H  HB3  . GLN   A 1 136 ? 49.652 23.332  32.867 1.00 30.38 ? 136  GLN   A HB3  1 
ATOM   2113  H  HG2  . GLN   A 1 136 ? 51.607 25.141  31.931 1.00 32.73 ? 136  GLN   A HG2  1 
ATOM   2114  H  HG3  . GLN   A 1 136 ? 51.710 24.268  33.220 1.00 32.73 ? 136  GLN   A HG3  1 
ATOM   2115  H  HE21 . GLN   A 1 136 ? 51.553 21.818  32.709 1.00 40.75 ? 136  GLN   A HE21 1 
ATOM   2116  H  HE22 . GLN   A 1 136 ? 52.397 21.319  31.587 1.00 40.75 ? 136  GLN   A HE22 1 
ATOM   2117  N  N    . LEU   A 1 137 ? 47.006 24.536  30.369 1.00 16.97 ? 137  LEU   A N    1 
ATOM   2118  C  CA   . LEU   A 1 137 ? 45.527 24.384  30.353 1.00 16.07 ? 137  LEU   A CA   1 
ATOM   2119  C  C    . LEU   A 1 137 ? 45.080 23.870  28.979 1.00 14.47 ? 137  LEU   A C    1 
ATOM   2120  O  O    . LEU   A 1 137 ? 44.079 23.138  28.922 1.00 16.49 ? 137  LEU   A O    1 
ATOM   2121  C  CB   . LEU   A 1 137 ? 44.892 25.747  30.649 1.00 16.90 ? 137  LEU   A CB   1 
ATOM   2122  C  CG   . LEU   A 1 137 ? 45.286 26.389  31.976 1.00 19.03 ? 137  LEU   A CG   1 
ATOM   2123  C  CD1  . LEU   A 1 137 ? 44.866 27.850  32.010 1.00 17.84 ? 137  LEU   A CD1  1 
ATOM   2124  C  CD2  . LEU   A 1 137 ? 44.674 25.631  33.142 1.00 19.50 ? 137  LEU   A CD2  1 
ATOM   2125  H  H    . LEU   A 1 137 ? 47.300 25.235  29.963 1.00 20.36 ? 137  LEU   A H    1 
ATOM   2126  H  HA   . LEU   A 1 137 ? 45.246 23.745  31.027 1.00 19.29 ? 137  LEU   A HA   1 
ATOM   2127  H  HB2  . LEU   A 1 137 ? 45.126 26.357  29.932 1.00 20.28 ? 137  LEU   A HB2  1 
ATOM   2128  H  HB3  . LEU   A 1 137 ? 43.927 25.646  30.632 1.00 20.28 ? 137  LEU   A HB3  1 
ATOM   2129  H  HG   . LEU   A 1 137 ? 46.252 26.347  32.058 1.00 22.84 ? 137  LEU   A HG   1 
ATOM   2130  H  HD11 . LEU   A 1 137 ? 45.124 28.241  32.859 1.00 21.41 ? 137  LEU   A HD11 1 
ATOM   2131  H  HD12 . LEU   A 1 137 ? 45.302 28.329  31.288 1.00 21.41 ? 137  LEU   A HD12 1 
ATOM   2132  H  HD13 . LEU   A 1 137 ? 43.904 27.913  31.905 1.00 21.41 ? 137  LEU   A HD13 1 
ATOM   2133  H  HD21 . LEU   A 1 137 ? 44.935 26.053  33.975 1.00 23.40 ? 137  LEU   A HD21 1 
ATOM   2134  H  HD22 . LEU   A 1 137 ? 43.707 25.642  33.064 1.00 23.40 ? 137  LEU   A HD22 1 
ATOM   2135  H  HD23 . LEU   A 1 137 ? 44.988 24.713  33.132 1.00 23.40 ? 137  LEU   A HD23 1 
ATOM   2136  N  N    . TRP   A 1 138 ? 45.798 24.252  27.920 1.00 14.17 ? 138  TRP   A N    1 
ATOM   2137  C  CA   . TRP   A 1 138 ? 45.409 23.862  26.538 1.00 17.75 ? 138  TRP   A CA   1 
ATOM   2138  C  C    . TRP   A 1 138 ? 45.122 22.359  26.462 1.00 16.75 ? 138  TRP   A C    1 
ATOM   2139  O  O    . TRP   A 1 138 ? 45.986 21.575  26.885 1.00 14.62 ? 138  TRP   A O    1 
ATOM   2140  C  CB   . TRP   A 1 138 ? 46.498 24.285  25.546 1.00 16.39 ? 138  TRP   A CB   1 
ATOM   2141  C  CG   . TRP   A 1 138 ? 46.019 24.518  24.146 1.00 15.99 ? 138  TRP   A CG   1 
ATOM   2142  C  CD1  . TRP   A 1 138 ? 46.270 23.738  23.055 1.00 19.00 ? 138  TRP   A CD1  1 
ATOM   2143  C  CD2  . TRP   A 1 138 ? 45.221 25.619  23.674 1.00 16.34 ? 138  TRP   A CD2  1 
ATOM   2144  N  NE1  . TRP   A 1 138 ? 45.681 24.272  21.941 1.00 20.01 ? 138  TRP   A NE1  1 
ATOM   2145  C  CE2  . TRP   A 1 138 ? 45.031 25.426  22.290 1.00 19.32 ? 138  TRP   A CE2  1 
ATOM   2146  C  CE3  . TRP   A 1 138 ? 44.649 26.741  24.282 1.00 15.40 ? 138  TRP   A CE3  1 
ATOM   2147  C  CZ2  . TRP   A 1 138 ? 44.294 26.315  21.509 1.00 18.36 ? 138  TRP   A CZ2  1 
ATOM   2148  C  CZ3  . TRP   A 1 138 ? 43.922 27.620  23.510 1.00 15.61 ? 138  TRP   A CZ3  1 
ATOM   2149  C  CH2  . TRP   A 1 138 ? 43.746 27.406  22.143 1.00 16.82 ? 138  TRP   A CH2  1 
ATOM   2150  H  H    . TRP   A 1 138 ? 46.509 24.733  27.968 1.00 17.01 ? 138  TRP   A H    1 
ATOM   2151  H  HA   . TRP   A 1 138 ? 44.591 24.324  26.296 1.00 21.30 ? 138  TRP   A HA   1 
ATOM   2152  H  HB2  . TRP   A 1 138 ? 46.915 25.098  25.871 1.00 19.67 ? 138  TRP   A HB2  1 
ATOM   2153  H  HB3  . TRP   A 1 138 ? 47.185 23.601  25.529 1.00 19.67 ? 138  TRP   A HB3  1 
ATOM   2154  H  HD1  . TRP   A 1 138 ? 46.771 22.954  23.067 1.00 22.80 ? 138  TRP   A HD1  1 
ATOM   2155  H  HE1  . TRP   A 1 138 ? 45.714 23.937  21.150 1.00 24.01 ? 138  TRP   A HE1  1 
ATOM   2156  H  HE3  . TRP   A 1 138 ? 44.758 26.891  25.193 1.00 18.49 ? 138  TRP   A HE3  1 
ATOM   2157  H  HZ2  . TRP   A 1 138 ? 44.178 26.176  20.597 1.00 22.03 ? 138  TRP   A HZ2  1 
ATOM   2158  H  HZ3  . TRP   A 1 138 ? 43.542 28.370  23.907 1.00 18.73 ? 138  TRP   A HZ3  1 
ATOM   2159  H  HH2  . TRP   A 1 138 ? 43.247 28.015  21.649 1.00 20.19 ? 138  TRP   A HH2  1 
ATOM   2160  N  N    . GLY   A 1 139 ? 43.949 21.986  25.941 1.00 14.23 ? 139  GLY   A N    1 
ATOM   2161  C  CA   . GLY   A 1 139 ? 43.594 20.562  25.786 1.00 13.45 ? 139  GLY   A CA   1 
ATOM   2162  C  C    . GLY   A 1 139 ? 42.611 20.088  26.842 1.00 15.03 ? 139  GLY   A C    1 
ATOM   2163  O  O    . GLY   A 1 139 ? 42.033 19.006  26.659 1.00 16.35 ? 139  GLY   A O    1 
ATOM   2164  H  H    . GLY   A 1 139 ? 43.345 22.536  25.671 1.00 17.08 ? 139  GLY   A H    1 
ATOM   2165  H  HA2  . GLY   A 1 139 ? 43.211 20.421  24.906 1.00 16.15 ? 139  GLY   A HA2  1 
ATOM   2166  H  HA3  . GLY   A 1 139 ? 44.400 20.024  25.834 1.00 16.15 ? 139  GLY   A HA3  1 
ATOM   2167  N  N    . LYS   A 1 140 ? 42.398 20.882  27.889 1.00 16.28 ? 140  LYS   A N    1 
ATOM   2168  C  CA   . LYS   A 1 140 ? 41.543 20.427  29.016 1.00 15.66 ? 140  LYS   A CA   1 
ATOM   2169  C  C    . LYS   A 1 140 ? 40.066 20.758  28.775 1.00 14.55 ? 140  LYS   A C    1 
ATOM   2170  O  O    . LYS   A 1 140 ? 39.786 21.793  28.160 1.00 12.95 ? 140  LYS   A O    1 
ATOM   2171  C  CB   . LYS   A 1 140 ? 42.017 21.049  30.335 1.00 14.19 ? 140  LYS   A CB   1 
ATOM   2172  C  CG   . LYS   A 1 140 ? 43.357 20.522  30.836 1.00 15.30 ? 140  LYS   A CG   1 
ATOM   2173  C  CD   . LYS   A 1 140 ? 43.785 21.115  32.159 1.00 17.76 ? 140  LYS   A CD   1 
ATOM   2174  C  CE   . LYS   A 1 140 ? 44.944 20.375  32.792 1.00 25.78 ? 140  LYS   A CE   1 
ATOM   2175  N  NZ   . LYS   A 1 140 ? 45.863 19.819  31.773 1.00 34.46 ? 140  LYS   A NZ   1 
ATOM   2176  H  H    . LYS   A 1 140 ? 42.726 21.672  27.977 1.00 19.53 ? 140  LYS   A H    1 
ATOM   2177  H  HA   . LYS   A 1 140 ? 41.625 19.462  29.074 1.00 18.80 ? 140  LYS   A HA   1 
ATOM   2178  H  HB2  . LYS   A 1 140 ? 42.082 22.010  30.221 1.00 17.03 ? 140  LYS   A HB2  1 
ATOM   2179  H  HB3  . LYS   A 1 140 ? 41.344 20.889  31.015 1.00 17.03 ? 140  LYS   A HB3  1 
ATOM   2180  H  HG2  . LYS   A 1 140 ? 43.304 19.558  30.925 1.00 18.37 ? 140  LYS   A HG2  1 
ATOM   2181  H  HG3  . LYS   A 1 140 ? 44.038 20.709  30.171 1.00 18.37 ? 140  LYS   A HG3  1 
ATOM   2182  H  HD2  . LYS   A 1 140 ? 44.034 22.043  32.026 1.00 21.32 ? 140  LYS   A HD2  1 
ATOM   2183  H  HD3  . LYS   A 1 140 ? 43.031 21.108  32.770 1.00 21.32 ? 140  LYS   A HD3  1 
ATOM   2184  H  HE2  . LYS   A 1 140 ? 45.433 20.977  33.374 1.00 30.94 ? 140  LYS   A HE2  1 
ATOM   2185  H  HE3  . LYS   A 1 140 ? 44.604 19.656  33.348 1.00 30.94 ? 140  LYS   A HE3  1 
ATOM   2186  H  HZ1  . LYS   A 1 140 ? 46.635 19.600  32.157 1.00 41.35 ? 140  LYS   A HZ1  1 
ATOM   2187  H  HZ2  . LYS   A 1 140 ? 45.498 19.094  31.407 1.00 41.35 ? 140  LYS   A HZ2  1 
ATOM   2188  H  HZ3  . LYS   A 1 140 ? 46.009 20.428  31.141 1.00 41.35 ? 140  LYS   A HZ3  1 
ATOM   2189  N  N    . VAL   A 1 141 ? 39.176 19.906  29.289 1.00 16.02 ? 141  VAL   A N    1 
ATOM   2190  C  CA   . VAL   A 1 141 ? 37.711 20.144  29.163 1.00 12.53 ? 141  VAL   A CA   1 
ATOM   2191  C  C    . VAL   A 1 141 ? 37.310 21.318  30.064 1.00 12.49 ? 141  VAL   A C    1 
ATOM   2192  O  O    . VAL   A 1 141 ? 38.114 21.709  30.921 1.00 13.55 ? 141  VAL   A O    1 
ATOM   2193  C  CB   . VAL   A 1 141 ? 36.910 18.871  29.503 1.00 15.27 ? 141  VAL   A CB   1 
ATOM   2194  C  CG1  . VAL   A 1 141 ? 37.075 17.809  28.428 1.00 13.78 ? 141  VAL   A CG1  1 
ATOM   2195  C  CG2  . VAL   A 1 141 ? 37.282 18.316  30.868 1.00 17.63 ? 141  VAL   A CG2  1 
ATOM   2196  H  H    . VAL   A 1 141 ? 39.386 19.188  29.713 1.00 19.23 ? 141  VAL   A H    1 
ATOM   2197  H  HA   . VAL   A 1 141 ? 37.502 20.370  28.243 1.00 15.04 ? 141  VAL   A HA   1 
ATOM   2198  H  HB   . VAL   A 1 141 ? 35.975 19.126  29.535 1.00 18.33 ? 141  VAL   A HB   1 
ATOM   2199  H  HG11 . VAL   A 1 141 ? 36.561 17.022  28.669 1.00 16.53 ? 141  VAL   A HG11 1 
ATOM   2200  H  HG12 . VAL   A 1 141 ? 36.757 18.155  27.579 1.00 16.53 ? 141  VAL   A HG12 1 
ATOM   2201  H  HG13 . VAL   A 1 141 ? 38.012 17.571  28.349 1.00 16.53 ? 141  VAL   A HG13 1 
ATOM   2202  H  HG21 . VAL   A 1 141 ? 36.760 17.518  31.047 1.00 21.16 ? 141  VAL   A HG21 1 
ATOM   2203  H  HG22 . VAL   A 1 141 ? 38.226 18.093  30.881 1.00 21.16 ? 141  VAL   A HG22 1 
ATOM   2204  H  HG23 . VAL   A 1 141 ? 37.098 18.982  31.549 1.00 21.16 ? 141  VAL   A HG23 1 
ATOM   2205  N  N    . THR   A 1 142 ? 36.088 21.822  29.895 1.00 11.62 ? 142  THR   A N    1 
ATOM   2206  C  CA   . THR   A 1 142 ? 35.617 23.013  30.651 1.00 14.05 ? 142  THR   A CA   1 
ATOM   2207  C  C    . THR   A 1 142 ? 35.831 22.851  32.162 1.00 13.34 ? 142  THR   A C    1 
ATOM   2208  O  O    . THR   A 1 142 ? 36.400 23.767  32.768 1.00 14.13 ? 142  THR   A O    1 
ATOM   2209  C  CB   . THR   A 1 142 ? 34.144 23.294  30.314 1.00 12.82 ? 142  THR   A CB   1 
ATOM   2210  O  OG1  . THR   A 1 142 ? 34.022 23.344  28.892 1.00 12.55 ? 142  THR   A OG1  1 
ATOM   2211  C  CG2  . THR   A 1 142 ? 33.628 24.574  30.932 1.00 12.17 ? 142  THR   A CG2  1 
ATOM   2212  H  H    . THR   A 1 142 ? 35.508 21.497  29.350 1.00 13.95 ? 142  THR   A H    1 
ATOM   2213  H  HA   . THR   A 1 142 ? 36.148 23.778  30.379 1.00 16.87 ? 142  THR   A HA   1 
ATOM   2214  H  HB   . THR   A 1 142 ? 33.602 22.582  30.689 1.00 15.38 ? 142  THR   A HB   1 
ATOM   2215  H  HG1  . THR   A 1 142 ? 33.306 22.971  28.659 1.00 15.06 ? 142  THR   A HG1  1 
ATOM   2216  H  HG21 . THR   A 1 142 ? 32.698 24.700  30.687 1.00 14.60 ? 142  THR   A HG21 1 
ATOM   2217  H  HG22 . THR   A 1 142 ? 33.703 24.521  31.898 1.00 14.60 ? 142  THR   A HG22 1 
ATOM   2218  H  HG23 . THR   A 1 142 ? 34.151 25.324  30.608 1.00 14.60 ? 142  THR   A HG23 1 
ATOM   2219  N  N    . SER   A 1 143 ? 35.375 21.741  32.742 1.00 13.41 ? 143  SER   A N    1 
ATOM   2220  C  CA   . SER   A 1 143 ? 35.447 21.563  34.220 1.00 13.30 ? 143  SER   A CA   1 
ATOM   2221  C  C    . SER   A 1 143 ? 36.901 21.567  34.708 1.00 15.94 ? 143  SER   A C    1 
ATOM   2222  O  O    . SER   A 1 143 ? 37.167 22.206  35.734 1.00 14.25 ? 143  SER   A O    1 
ATOM   2223  C  CB   . SER   A 1 143 ? 34.725 20.299  34.652 1.00 13.23 ? 143  SER   A CB   1 
ATOM   2224  O  OG   . SER   A 1 143 ? 35.370 19.147  34.136 1.00 14.52 ? 143  SER   A OG   1 
ATOM   2225  H  H    . SER   A 1 143 ? 35.023 21.081  32.317 1.00 16.10 ? 143  SER   A H    1 
ATOM   2226  H  HA   . SER   A 1 143 ? 34.997 22.317  34.633 1.00 15.97 ? 143  SER   A HA   1 
ATOM   2227  H  HB2  . SER   A 1 143 ? 34.698 20.253  35.621 1.00 15.87 ? 143  SER   A HB2  1 
ATOM   2228  H  HB3  . SER   A 1 143 ? 33.806 20.325  34.343 1.00 15.87 ? 143  SER   A HB3  1 
ATOM   2229  H  HG   . SER   A 1 143 ? 34.863 18.765  33.585 1.00 17.42 ? 143  SER   A HG   1 
ATOM   2230  N  N    . GLU   A 1 144 ? 37.783 20.866  33.999 1.00 14.89 ? 144  GLU   A N    1 
ATOM   2231  C  CA   . GLU   A 1 144 ? 39.203 20.766  34.421 1.00 14.54 ? 144  GLU   A CA   1 
ATOM   2232  C  C    . GLU   A 1 144 ? 39.870 22.120  34.189 1.00 13.70 ? 144  GLU   A C    1 
ATOM   2233  O  O    . GLU   A 1 144 ? 40.661 22.549  35.045 1.00 15.25 ? 144  GLU   A O    1 
ATOM   2234  C  CB   . GLU   A 1 144 ? 39.906 19.659  33.637 1.00 18.48 ? 144  GLU   A CB   1 
ATOM   2235  C  CG   . GLU   A 1 144 ? 39.423 18.269  34.004 1.00 20.83 ? 144  GLU   A CG   1 
ATOM   2236  C  CD   . GLU   A 1 144 ? 40.109 17.153  33.239 1.00 34.43 ? 144  GLU   A CD   1 
ATOM   2237  O  OE1  . GLU   A 1 144 ? 41.164 17.420  32.634 1.00 33.12 ? 144  GLU   A OE1  1 
ATOM   2238  O  OE2  . GLU   A 1 144 ? 39.585 16.022  33.250 1.00 38.52 ? 144  GLU   A OE2  1 
ATOM   2239  H  H    . GLU   A 1 144 ? 37.593 20.441  33.276 1.00 17.87 ? 144  GLU   A H    1 
ATOM   2240  H  HA   . GLU   A 1 144 ? 39.262 20.539  35.362 1.00 17.45 ? 144  GLU   A HA   1 
ATOM   2241  H  HB2  . GLU   A 1 144 ? 39.766 19.804  32.688 1.00 22.18 ? 144  GLU   A HB2  1 
ATOM   2242  H  HB3  . GLU   A 1 144 ? 40.861 19.715  33.795 1.00 22.18 ? 144  GLU   A HB3  1 
ATOM   2243  H  HG2  . GLU   A 1 144 ? 39.561 18.129  34.954 1.00 25.00 ? 144  GLU   A HG2  1 
ATOM   2244  H  HG3  . GLU   A 1 144 ? 38.467 18.217  33.846 1.00 25.00 ? 144  GLU   A HG3  1 
ATOM   2245  N  N    . THR   A 1 145 ? 39.565 22.756  33.061 1.00 12.67 ? 145  THR   A N    1 
ATOM   2246  C  CA   . THR   A 1 145 ? 40.100 24.119  32.817 1.00 13.80 ? 145  THR   A CA   1 
ATOM   2247  C  C    . THR   A 1 145 ? 39.698 25.008  33.997 1.00 12.68 ? 145  THR   A C    1 
ATOM   2248  O  O    . THR   A 1 145 ? 40.553 25.755  34.495 1.00 13.87 ? 145  THR   A O    1 
ATOM   2249  C  CB   . THR   A 1 145 ? 39.594 24.679  31.479 1.00 11.65 ? 145  THR   A CB   1 
ATOM   2250  O  OG1  . THR   A 1 145 ? 40.112 23.880  30.416 1.00 13.95 ? 145  THR   A OG1  1 
ATOM   2251  C  CG2  . THR   A 1 145 ? 39.979 26.128  31.270 1.00 12.75 ? 145  THR   A CG2  1 
ATOM   2252  H  H    . THR   A 1 145 ? 39.067 22.439  32.436 1.00 15.21 ? 145  THR   A H    1 
ATOM   2253  H  HA   . THR   A 1 145 ? 41.067 24.092  32.752 1.00 16.56 ? 145  THR   A HA   1 
ATOM   2254  H  HB   . THR   A 1 145 ? 38.625 24.645  31.491 1.00 13.99 ? 145  THR   A HB   1 
ATOM   2255  H  HG1  . THR   A 1 145 ? 39.675 23.165  30.364 1.00 16.75 ? 145  THR   A HG1  1 
ATOM   2256  H  HG21 . THR   A 1 145 ? 39.638 26.434  30.415 1.00 15.30 ? 145  THR   A HG21 1 
ATOM   2257  H  HG22 . THR   A 1 145 ? 39.601 26.669  31.981 1.00 15.30 ? 145  THR   A HG22 1 
ATOM   2258  H  HG23 . THR   A 1 145 ? 40.945 26.211  31.280 1.00 15.30 ? 145  THR   A HG23 1 
ATOM   2259  N  N    . THR   A 1 146 ? 38.440 24.912  34.430 1.00 11.52 ? 146  THR   A N    1 
ATOM   2260  C  CA   . THR   A 1 146 ? 37.938 25.786  35.522 1.00 12.82 ? 146  THR   A CA   1 
ATOM   2261  C  C    . THR   A 1 146 ? 38.655 25.445  36.838 1.00 15.55 ? 146  THR   A C    1 
ATOM   2262  O  O    . THR   A 1 146 ? 39.059 26.374  37.548 1.00 15.11 ? 146  THR   A O    1 
ATOM   2263  C  CB   . THR   A 1 146 ? 36.411 25.685  35.629 1.00 14.48 ? 146  THR   A CB   1 
ATOM   2264  O  OG1  . THR   A 1 146 ? 35.861 26.035  34.359 1.00 16.12 ? 146  THR   A OG1  1 
ATOM   2265  C  CG2  . THR   A 1 146 ? 35.828 26.570  36.709 1.00 13.78 ? 146  THR   A CG2  1 
ATOM   2266  H  H    . THR   A 1 146 ? 37.861 24.359  34.117 1.00 13.83 ? 146  THR   A H    1 
ATOM   2267  H  HA   . THR   A 1 146 ? 38.140 26.713  35.320 1.00 15.39 ? 146  THR   A HA   1 
ATOM   2268  H  HB   . THR   A 1 146 ? 36.183 24.776  35.878 1.00 17.37 ? 146  THR   A HB   1 
ATOM   2269  H  HG1  . THR   A 1 146 ? 35.970 25.399  33.821 1.00 19.34 ? 146  THR   A HG1  1 
ATOM   2270  H  HG21 . THR   A 1 146 ? 34.864 26.464  36.729 1.00 16.54 ? 146  THR   A HG21 1 
ATOM   2271  H  HG22 . THR   A 1 146 ? 36.199 26.318  37.569 1.00 16.54 ? 146  THR   A HG22 1 
ATOM   2272  H  HG23 . THR   A 1 146 ? 36.047 27.496  36.522 1.00 16.54 ? 146  THR   A HG23 1 
ATOM   2273  N  N    . LYS   A 1 147 ? 38.780 24.155  37.148 1.00 16.33 ? 147  LYS   A N    1 
ATOM   2274  C  CA   . LYS   A 1 147 ? 39.404 23.750  38.434 1.00 15.20 ? 147  LYS   A CA   1 
ATOM   2275  C  C    . LYS   A 1 147 ? 40.865 24.207  38.458 1.00 16.12 ? 147  LYS   A C    1 
ATOM   2276  O  O    . LYS   A 1 147 ? 41.309 24.699  39.499 1.00 16.72 ? 147  LYS   A O    1 
ATOM   2277  C  CB   . LYS   A 1 147 ? 39.309 22.233  38.612 1.00 16.27 ? 147  LYS   A CB   1 
ATOM   2278  C  CG   . LYS   A 1 147 ? 37.920 21.702  38.936 1.00 21.74 ? 147  LYS   A CG   1 
ATOM   2279  C  CD   . LYS   A 1 147 ? 37.212 22.481  40.023 1.00 19.46 ? 147  LYS   A CD   1 
ATOM   2280  C  CE   . LYS   A 1 147 ? 35.985 21.768  40.551 1.00 24.73 ? 147  LYS   A CE   1 
ATOM   2281  N  NZ   . LYS   A 1 147 ? 35.202 22.624  41.471 1.00 23.92 ? 147  LYS   A NZ   1 
ATOM   2282  H  H    . LYS   A 1 147 ? 38.520 23.505  36.649 1.00 19.60 ? 147  LYS   A H    1 
ATOM   2283  H  HA   . LYS   A 1 147 ? 38.931 24.171  39.169 1.00 18.25 ? 147  LYS   A HA   1 
ATOM   2284  H  HB2  . LYS   A 1 147 ? 39.621 21.807  37.798 1.00 19.53 ? 147  LYS   A HB2  1 
ATOM   2285  H  HB3  . LYS   A 1 147 ? 39.915 21.967  39.321 1.00 19.53 ? 147  LYS   A HB3  1 
ATOM   2286  H  HG2  . LYS   A 1 147 ? 37.379 21.720  38.131 1.00 26.09 ? 147  LYS   A HG2  1 
ATOM   2287  H  HG3  . LYS   A 1 147 ? 37.992 20.774  39.208 1.00 26.09 ? 147  LYS   A HG3  1 
ATOM   2288  H  HD2  . LYS   A 1 147 ? 37.828 22.640  40.755 1.00 23.35 ? 147  LYS   A HD2  1 
ATOM   2289  H  HD3  . LYS   A 1 147 ? 36.953 23.349  39.676 1.00 23.35 ? 147  LYS   A HD3  1 
ATOM   2290  H  HE2  . LYS   A 1 147 ? 35.425 21.496  39.808 1.00 29.68 ? 147  LYS   A HE2  1 
ATOM   2291  H  HE3  . LYS   A 1 147 ? 36.255 20.959  41.014 1.00 29.68 ? 147  LYS   A HE3  1 
ATOM   2292  H  HZ1  . LYS   A 1 147 ? 34.440 22.215  41.681 1.00 28.70 ? 147  LYS   A HZ1  1 
ATOM   2293  H  HZ2  . LYS   A 1 147 ? 35.673 22.773  42.211 1.00 28.70 ? 147  LYS   A HZ2  1 
ATOM   2294  H  HZ3  . LYS   A 1 147 ? 35.022 23.400  41.074 1.00 28.70 ? 147  LYS   A HZ3  1 
ATOM   2295  N  N    . GLU   A 1 148 ? 41.575 24.023  37.347 1.00 15.83 ? 148  GLU   A N    1 
ATOM   2296  C  CA   . GLU   A 1 148 ? 43.010 24.401  37.295 1.00 15.33 ? 148  GLU   A CA   1 
ATOM   2297  C  C    . GLU   A 1 148 ? 43.150 25.917  37.498 1.00 14.53 ? 148  GLU   A C    1 
ATOM   2298  O  O    . GLU   A 1 148 ? 44.091 26.342  38.194 1.00 15.00 ? 148  GLU   A O    1 
ATOM   2299  C  CB   . GLU   A 1 148 ? 43.633 23.933  35.979 1.00 17.27 ? 148  GLU   A CB   1 
ATOM   2300  C  CG   . GLU   A 1 148 ? 43.786 22.425  35.885 1.00 17.20 ? 148  GLU   A CG   1 
ATOM   2301  C  CD   . GLU   A 1 148 ? 44.712 21.798  36.915 1.00 24.94 ? 148  GLU   A CD   1 
ATOM   2302  O  OE1  . GLU   A 1 148 ? 45.596 22.509  37.426 1.00 23.29 ? 148  GLU   A OE1  1 
ATOM   2303  O  OE2  . GLU   A 1 148 ? 44.546 20.597  37.197 1.00 25.86 ? 148  GLU   A OE2  1 
ATOM   2304  H  H    . GLU   A 1 148 ? 41.262 23.688  36.619 1.00 18.99 ? 148  GLU   A H    1 
ATOM   2305  H  HA   . GLU   A 1 148 ? 43.493 23.960  38.011 1.00 18.40 ? 148  GLU   A HA   1 
ATOM   2306  H  HB2  . GLU   A 1 148 ? 43.084 24.242  35.241 1.00 20.73 ? 148  GLU   A HB2  1 
ATOM   2307  H  HB3  . GLU   A 1 148 ? 44.504 24.347  35.877 1.00 20.73 ? 148  GLU   A HB3  1 
ATOM   2308  H  HG2  . GLU   A 1 148 ? 42.909 22.020  35.972 1.00 20.65 ? 148  GLU   A HG2  1 
ATOM   2309  H  HG3  . GLU   A 1 148 ? 44.114 22.203  35.000 1.00 20.65 ? 148  GLU   A HG3  1 
ATOM   2310  N  N    . LEU   A 1 149 ? 42.241 26.699  36.913 1.00 14.58 ? 149  LEU   A N    1 
ATOM   2311  C  CA   . LEU   A 1 149 ? 42.336 28.179  37.025 1.00 13.08 ? 149  LEU   A CA   1 
ATOM   2312  C  C    . LEU   A 1 149 ? 41.965 28.604  38.450 1.00 15.74 ? 149  LEU   A C    1 
ATOM   2313  O  O    . LEU   A 1 149 ? 42.519 29.602  38.928 1.00 16.01 ? 149  LEU   A O    1 
ATOM   2314  C  CB   . LEU   A 1 149 ? 41.419 28.832  35.984 1.00 14.06 ? 149  LEU   A CB   1 
ATOM   2315  C  CG   . LEU   A 1 149 ? 42.029 28.962  34.590 1.00 14.97 ? 149  LEU   A CG   1 
ATOM   2316  C  CD1  . LEU   A 1 149 ? 40.981 29.388  33.575 1.00 13.97 ? 149  LEU   A CD1  1 
ATOM   2317  C  CD2  . LEU   A 1 149 ? 43.192 29.940  34.603 1.00 16.62 ? 149  LEU   A CD2  1 
ATOM   2318  H  H    . LEU   A 1 149 ? 41.572 26.412  36.455 1.00 17.50 ? 149  LEU   A H    1 
ATOM   2319  H  HA   . LEU   A 1 149 ? 43.244 28.472  36.849 1.00 15.69 ? 149  LEU   A HA   1 
ATOM   2320  H  HB2  . LEU   A 1 149 ? 40.602 28.313  35.919 1.00 16.87 ? 149  LEU   A HB2  1 
ATOM   2321  H  HB3  . LEU   A 1 149 ? 41.170 29.715  36.299 1.00 16.87 ? 149  LEU   A HB3  1 
ATOM   2322  H  HG   . LEU   A 1 149 ? 42.365 28.091  34.327 1.00 17.97 ? 149  LEU   A HG   1 
ATOM   2323  H  HD11 . LEU   A 1 149 ? 41.391 29.464  32.699 1.00 16.77 ? 149  LEU   A HD11 1 
ATOM   2324  H  HD12 . LEU   A 1 149 ? 40.272 28.726  33.544 1.00 16.77 ? 149  LEU   A HD12 1 
ATOM   2325  H  HD13 . LEU   A 1 149 ? 40.610 30.246  33.833 1.00 16.77 ? 149  LEU   A HD13 1 
ATOM   2326  H  HD21 . LEU   A 1 149 ? 43.566 30.010  33.711 1.00 19.95 ? 149  LEU   A HD21 1 
ATOM   2327  H  HD22 . LEU   A 1 149 ? 42.879 30.812  34.891 1.00 19.95 ? 149  LEU   A HD22 1 
ATOM   2328  H  HD23 . LEU   A 1 149 ? 43.874 29.624  35.216 1.00 19.95 ? 149  LEU   A HD23 1 
ATOM   2329  N  N    . GLU   A 1 150 ? 41.069 27.856  39.097 1.00 16.97 ? 150  GLU   A N    1 
ATOM   2330  C  CA   . GLU   A 1 150 ? 40.664 28.181  40.491 1.00 18.14 ? 150  GLU   A CA   1 
ATOM   2331  C  C    . GLU   A 1 150 ? 41.879 28.041  41.419 1.00 15.10 ? 150  GLU   A C    1 
ATOM   2332  O  O    . GLU   A 1 150 ? 41.917 28.715  42.451 1.00 17.23 ? 150  GLU   A O    1 
ATOM   2333  C  CB   . GLU   A 1 150 ? 39.496 27.290  40.922 1.00 20.13 ? 150  GLU   A CB   1 
ATOM   2334  C  CG   . GLU   A 1 150 ? 38.188 27.677  40.259 1.00 16.92 ? 150  GLU   A CG   1 
ATOM   2335  C  CD   . GLU   A 1 150 ? 36.980 26.840  40.640 1.00 19.59 ? 150  GLU   A CD   1 
ATOM   2336  O  OE1  . GLU   A 1 150 ? 37.155 25.845  41.366 1.00 19.12 ? 150  GLU   A OE1  1 
ATOM   2337  O  OE2  . GLU   A 1 150 ? 35.866 27.192  40.211 1.00 22.89 ? 150  GLU   A OE2  1 
ATOM   2338  H  H    . GLU   A 1 150 ? 40.683 27.164  38.762 1.00 20.37 ? 150  GLU   A H    1 
ATOM   2339  H  HA   . GLU   A 1 150 ? 40.354 29.099  40.544 1.00 21.77 ? 150  GLU   A HA   1 
ATOM   2340  H  HB2  . GLU   A 1 150 ? 39.702 26.367  40.707 1.00 24.16 ? 150  GLU   A HB2  1 
ATOM   2341  H  HB3  . GLU   A 1 150 ? 39.393 27.341  41.885 1.00 24.16 ? 150  GLU   A HB3  1 
ATOM   2342  H  HG2  . GLU   A 1 150 ? 37.998 28.604  40.473 1.00 20.31 ? 150  GLU   A HG2  1 
ATOM   2343  H  HG3  . GLU   A 1 150 ? 38.305 27.626  39.297 1.00 20.31 ? 150  GLU   A HG3  1 
ATOM   2344  N  N    . LYS   A 1 151 ? 42.833 27.193  41.043 1.00 17.58 ? 151  LYS   A N    1 
ATOM   2345  C  CA   . LYS   A 1 151 ? 44.021 26.971  41.907 1.00 18.19 ? 151  LYS   A CA   1 
ATOM   2346  C  C    . LYS   A 1 151 ? 44.966 28.169  41.805 1.00 16.80 ? 151  LYS   A C    1 
ATOM   2347  O  O    . LYS   A 1 151 ? 45.724 28.394  42.761 1.00 18.64 ? 151  LYS   A O    1 
ATOM   2348  C  CB   . LYS   A 1 151 ? 44.789 25.715  41.483 1.00 18.52 ? 151  LYS   A CB   1 
ATOM   2349  C  CG   . LYS   A 1 151 ? 44.063 24.394  41.689 1.00 18.30 ? 151  LYS   A CG   1 
ATOM   2350  C  CD   . LYS   A 1 151 ? 44.825 23.209  41.135 1.00 24.66 ? 151  LYS   A CD   1 
ATOM   2351  C  CE   . LYS   A 1 151 ? 44.065 21.905  41.259 1.00 25.90 ? 151  LYS   A CE   1 
ATOM   2352  N  NZ   . LYS   A 1 151 ? 44.787 20.788  40.607 1.00 39.33 ? 151  LYS   A NZ   1 
ATOM   2353  H  H    . LYS   A 1 151 ? 42.825 26.741  40.312 1.00 21.10 ? 151  LYS   A H    1 
ATOM   2354  H  HA   . LYS   A 1 151 ? 43.706 26.860  42.818 1.00 21.84 ? 151  LYS   A HA   1 
ATOM   2355  H  HB2  . LYS   A 1 151 ? 45.016 25.797  40.543 1.00 22.23 ? 151  LYS   A HB2  1 
ATOM   2356  H  HB3  . LYS   A 1 151 ? 45.624 25.686  41.975 1.00 22.23 ? 151  LYS   A HB3  1 
ATOM   2357  H  HG2  . LYS   A 1 151 ? 43.910 24.259  42.637 1.00 21.97 ? 151  LYS   A HG2  1 
ATOM   2358  H  HG3  . LYS   A 1 151 ? 43.192 24.439  41.264 1.00 21.97 ? 151  LYS   A HG3  1 
ATOM   2359  H  HD2  . LYS   A 1 151 ? 45.029 23.371  40.201 1.00 29.59 ? 151  LYS   A HD2  1 
ATOM   2360  H  HD3  . LYS   A 1 151 ? 45.672 23.129  41.601 1.00 29.59 ? 151  LYS   A HD3  1 
ATOM   2361  H  HE2  . LYS   A 1 151 ? 43.927 21.698  42.197 1.00 31.08 ? 151  LYS   A HE2  1 
ATOM   2362  H  HE3  . LYS   A 1 151 ? 43.187 22.002  40.858 1.00 31.08 ? 151  LYS   A HE3  1 
ATOM   2363  H  HZ1  . LYS   A 1 151 ? 44.298 20.471  39.934 1.00 47.19 ? 151  LYS   A HZ1  1 
ATOM   2364  H  HZ2  . LYS   A 1 151 ? 45.567 21.081  40.294 1.00 47.19 ? 151  LYS   A HZ2  1 
ATOM   2365  H  HZ3  . LYS   A 1 151 ? 44.930 20.140  41.200 1.00 47.19 ? 151  LYS   A HZ3  1 
ATOM   2366  N  N    . ILE   A 1 152 ? 44.897 28.928  40.713 1.00 16.05 ? 152  ILE   A N    1 
ATOM   2367  C  CA   . ILE   A 1 152 ? 45.918 30.002  40.516 1.00 17.22 ? 152  ILE   A CA   1 
ATOM   2368  C  C    . ILE   A 1 152 ? 45.267 31.371  40.284 1.00 18.16 ? 152  ILE   A C    1 
ATOM   2369  O  O    . ILE   A 1 152 ? 45.971 32.274  39.806 1.00 16.87 ? 152  ILE   A O    1 
ATOM   2370  C  CB   . ILE   A 1 152 ? 46.837 29.605  39.344 1.00 18.38 ? 152  ILE   A CB   1 
ATOM   2371  C  CG1  . ILE   A 1 152 ? 46.044 29.399  38.052 1.00 16.88 ? 152  ILE   A CG1  1 
ATOM   2372  C  CG2  . ILE   A 1 152 ? 47.659 28.377  39.699 1.00 19.53 ? 152  ILE   A CG2  1 
ATOM   2373  C  CD1  . ILE   A 1 152 ? 46.857 28.823  36.920 1.00 22.62 ? 152  ILE   A CD1  1 
ATOM   2374  H  H    . ILE   A 1 152 ? 44.305 28.857  40.093 1.00 19.27 ? 152  ILE   A H    1 
ATOM   2375  H  HA   . ILE   A 1 152 ? 46.448 30.088  41.324 1.00 20.67 ? 152  ILE   A HA   1 
ATOM   2376  H  HB   . ILE   A 1 152 ? 47.451 30.338  39.184 1.00 22.06 ? 152  ILE   A HB   1 
ATOM   2377  H  HG12 . ILE   A 1 152 ? 45.295 28.809  38.233 1.00 20.26 ? 152  ILE   A HG12 1 
ATOM   2378  H  HG13 . ILE   A 1 152 ? 45.673 30.250  37.771 1.00 20.26 ? 152  ILE   A HG13 1 
ATOM   2379  H  HG21 . ILE   A 1 152 ? 48.230 28.142  38.951 1.00 23.44 ? 152  ILE   A HG21 1 
ATOM   2380  H  HG22 . ILE   A 1 152 ? 48.207 28.568  40.476 1.00 23.44 ? 152  ILE   A HG22 1 
ATOM   2381  H  HG23 . ILE   A 1 152 ? 47.065 27.636  39.897 1.00 23.44 ? 152  ILE   A HG23 1 
ATOM   2382  H  HD11 . ILE   A 1 152 ? 46.294 28.720  36.137 1.00 27.14 ? 152  ILE   A HD11 1 
ATOM   2383  H  HD12 . ILE   A 1 152 ? 47.592 29.421  36.713 1.00 27.14 ? 152  ILE   A HD12 1 
ATOM   2384  H  HD13 . ILE   A 1 152 ? 47.208 27.958  37.181 1.00 27.14 ? 152  ILE   A HD13 1 
ATOM   2385  N  N    . THR   A 1 153 ? 43.990 31.520  40.631 1.00 16.73 ? 153  THR   A N    1 
ATOM   2386  C  CA   . THR   A 1 153 ? 43.314 32.836  40.495 1.00 16.85 ? 153  THR   A CA   1 
ATOM   2387  C  C    . THR   A 1 153 ? 42.685 33.225  41.833 1.00 15.77 ? 153  THR   A C    1 
ATOM   2388  O  O    . THR   A 1 153 ? 42.577 32.361  42.714 1.00 15.00 ? 153  THR   A O    1 
ATOM   2389  C  CB   . THR   A 1 153 ? 42.270 32.838  39.366 1.00 16.25 ? 153  THR   A CB   1 
ATOM   2390  O  OG1  . THR   A 1 153 ? 41.353 31.768  39.589 1.00 17.20 ? 153  THR   A OG1  1 
ATOM   2391  C  CG2  . THR   A 1 153 ? 42.892 32.705  37.994 1.00 19.05 ? 153  THR   A CG2  1 
ATOM   2392  H  H    . THR   A 1 153 ? 43.495 30.890  40.943 1.00 20.08 ? 153  THR   A H    1 
ATOM   2393  H  HA   . THR   A 1 153 ? 43.981 33.497  40.251 1.00 20.22 ? 153  THR   A HA   1 
ATOM   2394  H  HB   . THR   A 1 153 ? 41.814 33.694  39.383 1.00 19.51 ? 153  THR   A HB   1 
ATOM   2395  H  HG1  . THR   A 1 153 ? 41.732 31.036  39.429 1.00 20.64 ? 153  THR   A HG1  1 
ATOM   2396  H  HG21 . THR   A 1 153 ? 42.194 32.712  37.320 1.00 22.86 ? 153  THR   A HG21 1 
ATOM   2397  H  HG22 . THR   A 1 153 ? 43.497 33.447  37.839 1.00 22.86 ? 153  THR   A HG22 1 
ATOM   2398  H  HG23 . THR   A 1 153 ? 43.384 31.871  37.941 1.00 22.86 ? 153  THR   A HG23 1 
ATOM   2399  N  N    . GLU   A 1 154 ? 42.283 34.487  41.952 1.00 16.27 ? 154  GLU   A N    1 
ATOM   2400  C  CA   . GLU   A 1 154 ? 41.710 34.976  43.229 1.00 17.25 ? 154  GLU   A CA   1 
ATOM   2401  C  C    . GLU   A 1 154 ? 40.409 34.236  43.526 1.00 15.52 ? 154  GLU   A C    1 
ATOM   2402  O  O    . GLU   A 1 154 ? 39.629 34.004  42.592 1.00 17.31 ? 154  GLU   A O    1 
ATOM   2403  C  CB   . GLU   A 1 154 ? 41.438 36.478  43.176 1.00 20.25 ? 154  GLU   A CB   1 
ATOM   2404  C  CG   . GLU   A 1 154 ? 42.505 37.314  43.852 1.00 26.68 ? 154  GLU   A CG   1 
ATOM   2405  C  CD   . GLU   A 1 154 ? 42.071 38.730  44.190 1.00 27.50 ? 154  GLU   A CD   1 
ATOM   2406  O  OE1  . GLU   A 1 154 ? 40.973 38.895  44.754 1.00 29.41 ? 154  GLU   A OE1  1 
ATOM   2407  O  OE2  . GLU   A 1 154 ? 42.835 39.661  43.890 1.00 39.44 ? 154  GLU   A OE2  1 
ATOM   2408  H  H    . GLU   A 1 154 ? 42.327 35.074  41.325 1.00 19.53 ? 154  GLU   A H    1 
ATOM   2409  H  HA   . GLU   A 1 154 ? 42.356 34.807  43.932 1.00 20.71 ? 154  GLU   A HA   1 
ATOM   2410  H  HB2  . GLU   A 1 154 ? 41.363 36.752  42.249 1.00 24.30 ? 154  GLU   A HB2  1 
ATOM   2411  H  HB3  . GLU   A 1 154 ? 40.582 36.659  43.596 1.00 24.30 ? 154  GLU   A HB3  1 
ATOM   2412  H  HG2  . GLU   A 1 154 ? 42.781 36.868  44.668 1.00 32.03 ? 154  GLU   A HG2  1 
ATOM   2413  H  HG3  . GLU   A 1 154 ? 43.283 37.355  43.274 1.00 32.03 ? 154  GLU   A HG3  1 
ATOM   2414  N  N    . ASN   A 1 155 ? 40.199 33.900  44.793 1.00 15.32 ? 155  ASN   A N    1 
ATOM   2415  C  CA   . ASN   A 1 155 ? 38.941 33.226  45.194 1.00 17.13 ? 155  ASN   A CA   1 
ATOM   2416  C  C    . ASN   A 1 155 ? 37.748 34.025  44.655 1.00 15.68 ? 155  ASN   A C    1 
ATOM   2417  O  O    . ASN   A 1 155 ? 37.861 35.258  44.601 1.00 16.31 ? 155  ASN   A O    1 
ATOM   2418  C  CB   . ASN   A 1 155 ? 38.881 33.018  46.710 1.00 17.18 ? 155  ASN   A CB   1 
ATOM   2419  C  CG   . ASN   A 1 155 ? 39.962 32.086  47.218 1.00 21.24 ? 155  ASN   A CG   1 
ATOM   2420  O  OD1  . ASN   A 1 155 ? 40.710 31.509  46.433 1.00 18.43 ? 155  ASN   A OD1  1 
ATOM   2421  N  ND2  . ASN   A 1 155 ? 40.052 31.932  48.528 1.00 16.01 ? 155  ASN   A ND2  1 
ATOM   2422  H  H    . ASN   A 1 155 ? 40.753 34.045  45.434 1.00 18.39 ? 155  ASN   A H    1 
ATOM   2423  H  HA   . ASN   A 1 155 ? 38.908 32.338  44.805 1.00 20.56 ? 155  ASN   A HA   1 
ATOM   2424  H  HB2  . ASN   A 1 155 ? 38.965 33.876  47.154 1.00 20.62 ? 155  ASN   A HB2  1 
ATOM   2425  H  HB3  . ASN   A 1 155 ? 38.012 32.659  46.949 1.00 20.62 ? 155  ASN   A HB3  1 
ATOM   2426  H  HD21 . ASN   A 1 155 ? 40.651 31.412  48.860 1.00 19.21 ? 155  ASN   A HD21 1 
ATOM   2427  H  HD22 . ASN   A 1 155 ? 39.511 32.352  49.048 1.00 19.21 ? 155  ASN   A HD22 1 
ATOM   2428  N  N    . LYS   A 1 156 ? 36.679 33.332  44.253 1.00 15.63 ? 156  LYS   A N    1 
ATOM   2429  C  CA   . LYS   A 1 156 ? 35.423 33.981  43.777 1.00 18.49 ? 156  LYS   A CA   1 
ATOM   2430  C  C    . LYS   A 1 156 ? 35.530 34.436  42.315 1.00 16.49 ? 156  LYS   A C    1 
ATOM   2431  O  O    . LYS   A 1 156 ? 34.583 35.078  41.839 1.00 17.73 ? 156  LYS   A O    1 
ATOM   2432  C  CB   . LYS   A 1 156 ? 35.023 35.128  44.711 1.00 19.01 ? 156  LYS   A CB   1 
ATOM   2433  C  CG   . LYS   A 1 156 ? 34.799 34.727  46.163 1.00 21.88 ? 156  LYS   A CG   1 
ATOM   2434  C  CD   . LYS   A 1 156 ? 33.884 35.669  46.913 1.00 27.66 ? 156  LYS   A CD   1 
ATOM   2435  C  CE   . LYS   A 1 156 ? 32.517 35.798  46.275 1.00 36.33 ? 156  LYS   A CE   1 
ATOM   2436  N  NZ   . LYS   A 1 156 ? 31.754 36.937  46.837 1.00 44.76 ? 156  LYS   A NZ   1 
ATOM   2437  H  H    . LYS   A 1 156 ? 36.650 32.473  44.244 1.00 18.76 ? 156  LYS   A H    1 
ATOM   2438  H  HA   . LYS   A 1 156 ? 34.716 33.318  43.803 1.00 22.19 ? 156  LYS   A HA   1 
ATOM   2439  H  HB2  . LYS   A 1 156 ? 35.714 35.808  44.680 1.00 22.81 ? 156  LYS   A HB2  1 
ATOM   2440  H  HB3  . LYS   A 1 156 ? 34.210 35.534  44.373 1.00 22.81 ? 156  LYS   A HB3  1 
ATOM   2441  H  HG2  . LYS   A 1 156 ? 34.424 33.833  46.190 1.00 26.26 ? 156  LYS   A HG2  1 
ATOM   2442  H  HG3  . LYS   A 1 156 ? 35.655 34.689  46.617 1.00 26.26 ? 156  LYS   A HG3  1 
ATOM   2443  H  HD2  . LYS   A 1 156 ? 33.782 35.355  47.825 1.00 33.20 ? 156  LYS   A HD2  1 
ATOM   2444  H  HD3  . LYS   A 1 156 ? 34.298 36.545  46.960 1.00 33.20 ? 156  LYS   A HD3  1 
ATOM   2445  H  HE2  . LYS   A 1 156 ? 32.617 35.916  45.317 1.00 43.60 ? 156  LYS   A HE2  1 
ATOM   2446  H  HE3  . LYS   A 1 156 ? 32.018 34.977  46.409 1.00 43.60 ? 156  LYS   A HE3  1 
ATOM   2447  H  HZ1  . LYS   A 1 156 ? 30.958 36.985  46.442 1.00 53.71 ? 156  LYS   A HZ1  1 
ATOM   2448  H  HZ2  . LYS   A 1 156 ? 31.644 36.818  47.712 1.00 53.71 ? 156  LYS   A HZ2  1 
ATOM   2449  H  HZ3  . LYS   A 1 156 ? 32.201 37.693  46.695 1.00 53.71 ? 156  LYS   A HZ3  1 
ATOM   2450  N  N    . SER   A 1 157 ? 36.623 34.098  41.635 1.00 13.16 ? 157  SER   A N    1 
ATOM   2451  C  CA   . SER   A 1 157 ? 36.736 34.440  40.196 1.00 16.08 ? 157  SER   A CA   1 
ATOM   2452  C  C    . SER   A 1 157 ? 35.807 33.528  39.385 1.00 12.61 ? 157  SER   A C    1 
ATOM   2453  O  O    . SER   A 1 157 ? 35.671 32.351  39.756 1.00 17.50 ? 157  SER   A O    1 
ATOM   2454  C  CB   . SER   A 1 157 ? 38.163 34.346  39.727 1.00 14.72 ? 157  SER   A CB   1 
ATOM   2455  O  OG   . SER   A 1 157 ? 38.946 35.394  40.274 1.00 15.58 ? 157  SER   A OG   1 
ATOM   2456  H  H    . SER   A 1 157 ? 37.299 33.682  41.967 1.00 15.80 ? 157  SER   A H    1 
ATOM   2457  H  HA   . SER   A 1 157 ? 36.460 35.360  40.062 1.00 19.30 ? 157  SER   A HA   1 
ATOM   2458  H  HB2  . SER   A 1 157 ? 38.537 33.489  39.986 1.00 17.66 ? 157  SER   A HB2  1 
ATOM   2459  H  HB3  . SER   A 1 157 ? 38.192 34.387  38.758 1.00 17.66 ? 157  SER   A HB3  1 
ATOM   2460  H  HG   . SER   A 1 157 ? 39.267 35.149  41.010 1.00 18.69 ? 157  SER   A HG   1 
ATOM   2461  N  N    . LYS   A 1 158 ? 35.160 34.070  38.353 1.00 13.26 ? 158  LYS   A N    1 
ATOM   2462  C  CA   . LYS   A 1 158 ? 34.310 33.238  37.460 1.00 11.17 ? 158  LYS   A CA   1 
ATOM   2463  C  C    . LYS   A 1 158 ? 35.124 32.902  36.208 1.00 13.61 ? 158  LYS   A C    1 
ATOM   2464  O  O    . LYS   A 1 158 ? 35.991 33.706  35.833 1.00 12.09 ? 158  LYS   A O    1 
ATOM   2465  C  CB   . LYS   A 1 158 ? 33.005 33.962  37.123 1.00 14.28 ? 158  LYS   A CB   1 
ATOM   2466  C  CG   . LYS   A 1 158 ? 32.225 34.480  38.323 1.00 16.94 ? 158  LYS   A CG   1 
ATOM   2467  C  CD   . LYS   A 1 158 ? 31.882 33.395  39.318 1.00 17.27 ? 158  LYS   A CD   1 
ATOM   2468  C  CE   . LYS   A 1 158 ? 31.037 33.900  40.468 1.00 15.53 ? 158  LYS   A CE   1 
ATOM   2469  N  NZ   . LYS   A 1 158 ? 31.793 34.836  41.333 1.00 16.29 ? 158  LYS   A NZ   1 
ATOM   2470  H  H    . LYS   A 1 158 ? 35.191 34.904  38.145 1.00 15.92 ? 158  LYS   A H    1 
ATOM   2471  H  HA   . LYS   A 1 158 ? 34.056 32.414  37.904 1.00 13.41 ? 158  LYS   A HA   1 
ATOM   2472  H  HB2  . LYS   A 1 158 ? 33.208 34.710  36.539 1.00 17.14 ? 158  LYS   A HB2  1 
ATOM   2473  H  HB3  . LYS   A 1 158 ? 32.436 33.357  36.622 1.00 17.14 ? 158  LYS   A HB3  1 
ATOM   2474  H  HG2  . LYS   A 1 158 ? 32.745 35.167  38.768 1.00 20.33 ? 158  LYS   A HG2  1 
ATOM   2475  H  HG3  . LYS   A 1 158 ? 31.407 34.899  38.014 1.00 20.33 ? 158  LYS   A HG3  1 
ATOM   2476  H  HD2  . LYS   A 1 158 ? 31.408 32.682  38.862 1.00 20.72 ? 158  LYS   A HD2  1 
ATOM   2477  H  HD3  . LYS   A 1 158 ? 32.702 33.012  39.668 1.00 20.72 ? 158  LYS   A HD3  1 
ATOM   2478  H  HE2  . LYS   A 1 158 ? 30.249 34.346  40.120 1.00 18.64 ? 158  LYS   A HE2  1 
ATOM   2479  H  HE3  . LYS   A 1 158 ? 30.727 33.148  40.997 1.00 18.64 ? 158  LYS   A HE3  1 
ATOM   2480  H  HZ1  . LYS   A 1 158 ? 31.375 34.922  42.114 1.00 19.56 ? 158  LYS   A HZ1  1 
ATOM   2481  H  HZ2  . LYS   A 1 158 ? 32.613 34.518  41.469 1.00 19.56 ? 158  LYS   A HZ2  1 
ATOM   2482  H  HZ3  . LYS   A 1 158 ? 31.845 35.631  40.936 1.00 19.56 ? 158  LYS   A HZ3  1 
ATOM   2483  N  N    . VAL   A 1 159 ? 34.837 31.759  35.583 1.00 12.08 ? 159  VAL   A N    1 
ATOM   2484  C  CA   . VAL   A 1 159 ? 35.683 31.317  34.438 1.00 13.41 ? 159  VAL   A CA   1 
ATOM   2485  C  C    . VAL   A 1 159 ? 34.879 31.221  33.141 1.00 11.73 ? 159  VAL   A C    1 
ATOM   2486  O  O    . VAL   A 1 159 ? 33.836 30.555  33.142 1.00 11.36 ? 159  VAL   A O    1 
ATOM   2487  C  CB   . VAL   A 1 159 ? 36.370 29.970  34.733 1.00 12.73 ? 159  VAL   A CB   1 
ATOM   2488  C  CG1  . VAL   A 1 159 ? 37.071 29.412  33.505 1.00 13.06 ? 159  VAL   A CG1  1 
ATOM   2489  C  CG2  . VAL   A 1 159 ? 37.337 30.074  35.902 1.00 13.15 ? 159  VAL   A CG2  1 
ATOM   2490  H  H    . VAL   A 1 159 ? 34.186 31.234  35.786 1.00 14.50 ? 159  VAL   A H    1 
ATOM   2491  H  HA   . VAL   A 1 159 ? 36.367 31.994  34.320 1.00 16.09 ? 159  VAL   A HA   1 
ATOM   2492  H  HB   . VAL   A 1 159 ? 35.668 29.349  34.982 1.00 15.28 ? 159  VAL   A HB   1 
ATOM   2493  H  HG11 . VAL   A 1 159 ? 37.491 28.566  33.728 1.00 15.67 ? 159  VAL   A HG11 1 
ATOM   2494  H  HG12 . VAL   A 1 159 ? 36.423 29.274  32.797 1.00 15.67 ? 159  VAL   A HG12 1 
ATOM   2495  H  HG13 . VAL   A 1 159 ? 37.748 30.039  33.205 1.00 15.67 ? 159  VAL   A HG13 1 
ATOM   2496  H  HG21 . VAL   A 1 159 ? 37.750 29.210  36.059 1.00 15.79 ? 159  VAL   A HG21 1 
ATOM   2497  H  HG22 . VAL   A 1 159 ? 38.024 30.728  35.697 1.00 15.79 ? 159  VAL   A HG22 1 
ATOM   2498  H  HG23 . VAL   A 1 159 ? 36.855 30.351  36.697 1.00 15.79 ? 159  VAL   A HG23 1 
ATOM   2499  N  N    . LEU   A 1 160 ? 35.366 31.877  32.093 1.00 11.04 ? 160  LEU   A N    1 
ATOM   2500  C  CA   . LEU   A 1 160 ? 34.755 31.734  30.751 1.00 9.94  ? 160  LEU   A CA   1 
ATOM   2501  C  C    . LEU   A 1 160 ? 35.839 31.070  29.906 1.00 12.21 ? 160  LEU   A C    1 
ATOM   2502  O  O    . LEU   A 1 160 ? 36.999 31.495  30.010 1.00 13.40 ? 160  LEU   A O    1 
ATOM   2503  C  CB   . LEU   A 1 160 ? 34.405 33.118  30.203 1.00 11.54 ? 160  LEU   A CB   1 
ATOM   2504  C  CG   . LEU   A 1 160 ? 33.937 33.169  28.750 1.00 8.61  ? 160  LEU   A CG   1 
ATOM   2505  C  CD1  . LEU   A 1 160 ? 32.865 34.233  28.576 1.00 12.44 ? 160  LEU   A CD1  1 
ATOM   2506  C  CD2  . LEU   A 1 160 ? 35.104 33.442  27.813 1.00 10.29 ? 160  LEU   A CD2  1 
ATOM   2507  H  H    . LEU   A 1 160 ? 36.042 32.407  32.125 1.00 13.26 ? 160  LEU   A H    1 
ATOM   2508  H  HA   . LEU   A 1 160 ? 33.936 31.215  30.757 1.00 11.94 ? 160  LEU   A HA   1 
ATOM   2509  H  HB2  . LEU   A 1 160 ? 33.710 33.500  30.761 1.00 13.86 ? 160  LEU   A HB2  1 
ATOM   2510  H  HB3  . LEU   A 1 160 ? 35.185 33.688  30.292 1.00 13.86 ? 160  LEU   A HB3  1 
ATOM   2511  H  HG   . LEU   A 1 160 ? 33.560 32.304  28.524 1.00 10.34 ? 160  LEU   A HG   1 
ATOM   2512  H  HD11 . LEU   A 1 160 ? 32.577 34.254  27.650 1.00 14.93 ? 160  LEU   A HD11 1 
ATOM   2513  H  HD12 . LEU   A 1 160 ? 32.107 34.025  29.145 1.00 14.93 ? 160  LEU   A HD12 1 
ATOM   2514  H  HD13 . LEU   A 1 160 ? 33.226 35.099  28.822 1.00 14.93 ? 160  LEU   A HD13 1 
ATOM   2515  H  HD21 . LEU   A 1 160 ? 34.785 33.470  26.898 1.00 12.35 ? 160  LEU   A HD21 1 
ATOM   2516  H  HD22 . LEU   A 1 160 ? 35.509 34.294  28.040 1.00 12.35 ? 160  LEU   A HD22 1 
ATOM   2517  H  HD23 . LEU   A 1 160 ? 35.764 32.737  27.903 1.00 12.35 ? 160  LEU   A HD23 1 
ATOM   2518  N  N    . CYS   A 1 161 ? 35.488 30.047  29.133 1.00 11.35 ? 161  CYS   A N    1 
ATOM   2519  C  CA   . CYS   A 1 161 ? 36.572 29.344  28.417 1.00 10.28 ? 161  CYS   A CA   1 
ATOM   2520  C  C    . CYS   A 1 161 ? 36.056 28.546  27.225 1.00 10.12 ? 161  CYS   A C    1 
ATOM   2521  O  O    . CYS   A 1 161 ? 34.832 28.447  27.050 1.00 13.01 ? 161  CYS   A O    1 
ATOM   2522  C  CB   . CYS   A 1 161 ? 37.286 28.383  29.360 1.00 8.64  ? 161  CYS   A CB   1 
ATOM   2523  S  SG   . CYS   A 1 161 ? 36.245 27.018  29.946 1.00 12.19 ? 161  CYS   A SG   1 
ATOM   2524  H  H    . CYS   A 1 161 ? 34.690 29.753  29.008 1.00 13.63 ? 161  CYS   A H    1 
ATOM   2525  H  HA   . CYS   A 1 161 ? 37.180 30.027  28.093 1.00 12.33 ? 161  CYS   A HA   1 
ATOM   2526  H  HB2  . CYS   A 1 161 ? 38.061 28.015  28.907 1.00 10.37 ? 161  CYS   A HB2  1 
ATOM   2527  H  HB3  . CYS   A 1 161 ? 37.614 28.880  30.126 1.00 10.37 ? 161  CYS   A HB3  1 
ATOM   2528  H  HG   . CYS   A 1 161 ? 36.884 26.313  30.677 1.00 14.64 ? 161  CYS   A HG   1 
ATOM   2529  N  N    . ILE   A 1 162 ? 36.986 28.047  26.420 1.00 12.38 ? 162  ILE   A N    1 
ATOM   2530  C  CA   . ILE   A 1 162 ? 36.603 27.138  25.310 1.00 10.69 ? 162  ILE   A CA   1 
ATOM   2531  C  C    . ILE   A 1 162 ? 37.106 25.749  25.702 1.00 12.73 ? 162  ILE   A C    1 
ATOM   2532  O  O    . ILE   A 1 162 ? 37.980 25.657  26.577 1.00 13.11 ? 162  ILE   A O    1 
ATOM   2533  C  CB   . ILE   A 1 162 ? 37.203 27.598  23.968 1.00 14.60 ? 162  ILE   A CB   1 
ATOM   2534  C  CG1  . ILE   A 1 162 ? 38.695 27.914  24.110 1.00 13.80 ? 162  ILE   A CG1  1 
ATOM   2535  C  CG2  . ILE   A 1 162 ? 36.427 28.774  23.403 1.00 12.46 ? 162  ILE   A CG2  1 
ATOM   2536  C  CD1  . ILE   A 1 162 ? 39.504 27.664  22.861 1.00 14.29 ? 162  ILE   A CD1  1 
ATOM   2537  H  H    . ILE   A 1 162 ? 37.828 28.209  26.485 1.00 14.86 ? 162  ILE   A H    1 
ATOM   2538  H  HA   . ILE   A 1 162 ? 35.642 27.136  25.179 1.00 12.84 ? 162  ILE   A HA   1 
ATOM   2539  H  HB   . ILE   A 1 162 ? 37.124 26.868  23.335 1.00 17.53 ? 162  ILE   A HB   1 
ATOM   2540  H  HG12 . ILE   A 1 162 ? 38.795 28.844  24.367 1.00 16.57 ? 162  ILE   A HG12 1 
ATOM   2541  H  HG13 . ILE   A 1 162 ? 39.061 27.380  24.832 1.00 16.57 ? 162  ILE   A HG13 1 
ATOM   2542  H  HG21 . ILE   A 1 162 ? 36.821 29.047  22.560 1.00 14.96 ? 162  ILE   A HG21 1 
ATOM   2543  H  HG22 . ILE   A 1 162 ? 35.504 28.513  23.259 1.00 14.96 ? 162  ILE   A HG22 1 
ATOM   2544  H  HG23 . ILE   A 1 162 ? 36.460 29.514  24.029 1.00 14.96 ? 162  ILE   A HG23 1 
ATOM   2545  H  HD11 . ILE   A 1 162 ? 40.434 27.886  23.028 1.00 17.16 ? 162  ILE   A HD11 1 
ATOM   2546  H  HD12 . ILE   A 1 162 ? 39.435 26.729  22.612 1.00 17.16 ? 162  ILE   A HD12 1 
ATOM   2547  H  HD13 . ILE   A 1 162 ? 39.165 28.216  22.139 1.00 17.16 ? 162  ILE   A HD13 1 
ATOM   2548  N  N    . GLY   A 1 163 ? 36.536 24.713  25.102 1.00 12.04 ? 163  GLY   A N    1 
ATOM   2549  C  CA   . GLY   A 1 163 ? 37.058 23.361  25.343 1.00 12.35 ? 163  GLY   A CA   1 
ATOM   2550  C  C    . GLY   A 1 163 ? 37.935 22.930  24.186 1.00 11.84 ? 163  GLY   A C    1 
ATOM   2551  O  O    . GLY   A 1 163 ? 38.247 23.764  23.324 1.00 12.64 ? 163  GLY   A O    1 
ATOM   2552  H  H    . GLY   A 1 163 ? 35.865 24.760  24.566 1.00 14.45 ? 163  GLY   A H    1 
ATOM   2553  H  HA2  . GLY   A 1 163 ? 37.568 23.345  26.168 1.00 14.83 ? 163  GLY   A HA2  1 
ATOM   2554  H  HA3  . GLY   A 1 163 ? 36.323 22.737  25.452 1.00 14.83 ? 163  GLY   A HA3  1 
ATOM   2555  N  N    . PRO   A 1 164 ? 38.334 21.647  24.127 1.00 12.88 ? 164  PRO   A N    1 
ATOM   2556  C  CA   . PRO   A 1 164 ? 39.131 21.143  23.008 1.00 16.44 ? 164  PRO   A CA   1 
ATOM   2557  C  C    . PRO   A 1 164 ? 38.529 21.466  21.629 1.00 13.30 ? 164  PRO   A C    1 
ATOM   2558  O  O    . PRO   A 1 164 ? 39.266 21.685  20.702 1.00 12.81 ? 164  PRO   A O    1 
ATOM   2559  C  CB   . PRO   A 1 164 ? 39.107 19.626  23.255 1.00 16.42 ? 164  PRO   A CB   1 
ATOM   2560  C  CG   . PRO   A 1 164 ? 38.952 19.490  24.750 1.00 16.16 ? 164  PRO   A CG   1 
ATOM   2561  C  CD   . PRO   A 1 164 ? 38.038 20.630  25.137 1.00 16.82 ? 164  PRO   A CD   1 
ATOM   2562  H  HA   . PRO   A 1 164 ? 40.014 21.544  22.981 1.00 19.73 ? 164  PRO   A HA   1 
ATOM   2563  H  HB2  . PRO   A 1 164 ? 38.372 19.203  22.784 1.00 19.70 ? 164  PRO   A HB2  1 
ATOM   2564  H  HB3  . PRO   A 1 164 ? 39.924 19.204  22.945 1.00 19.70 ? 164  PRO   A HB3  1 
ATOM   2565  H  HG2  . PRO   A 1 164 ? 38.568 18.632  24.989 1.00 19.39 ? 164  PRO   A HG2  1 
ATOM   2566  H  HG3  . PRO   A 1 164 ? 39.808 19.554  25.202 1.00 19.39 ? 164  PRO   A HG3  1 
ATOM   2567  H  HD2  . PRO   A 1 164 ? 37.105 20.365  25.117 1.00 20.19 ? 164  PRO   A HD2  1 
ATOM   2568  H  HD3  . PRO   A 1 164 ? 38.223 20.950  26.034 1.00 20.19 ? 164  PRO   A HD3  1 
ATOM   2569  N  N    . ALA   A 1 165 ? 37.198 21.477  21.532 1.00 12.25 ? 165  ALA   A N    1 
ATOM   2570  C  CA   . ALA   A 1 165 ? 36.550 21.730  20.224 1.00 10.05 ? 165  ALA   A CA   1 
ATOM   2571  C  C    . ALA   A 1 165 ? 36.912 23.128  19.712 1.00 10.84 ? 165  ALA   A C    1 
ATOM   2572  O  O    . ALA   A 1 165 ? 37.197 23.266  18.518 1.00 12.23 ? 165  ALA   A O    1 
ATOM   2573  C  CB   . ALA   A 1 165 ? 35.057 21.572  20.350 1.00 11.96 ? 165  ALA   A CB   1 
ATOM   2574  H  H    . ALA   A 1 165 ? 36.658 21.345  22.188 1.00 14.70 ? 165  ALA   A H    1 
ATOM   2575  H  HA   . ALA   A 1 165 ? 36.873 21.081  19.580 1.00 12.07 ? 165  ALA   A HA   1 
ATOM   2576  H  HB1  . ALA   A 1 165 ? 34.640 21.739  19.490 1.00 14.36 ? 165  ALA   A HB1  1 
ATOM   2577  H  HB2  . ALA   A 1 165 ? 34.850 20.670  20.639 1.00 14.36 ? 165  ALA   A HB2  1 
ATOM   2578  H  HB3  . ALA   A 1 165 ? 34.718 22.206  21.002 1.00 14.36 ? 165  ALA   A HB3  1 
ATOM   2579  N  N    . GLY   A 1 166 ? 36.843 24.126  20.590 1.00 9.85  ? 166  GLY   A N    1 
ATOM   2580  C  CA   . GLY   A 1 166 ? 37.211 25.497  20.195 1.00 11.91 ? 166  GLY   A CA   1 
ATOM   2581  C  C    . GLY   A 1 166 ? 38.692 25.596  19.867 1.00 9.70  ? 166  GLY   A C    1 
ATOM   2582  O  O    . GLY   A 1 166 ? 39.044 26.359  18.956 1.00 13.05 ? 166  GLY   A O    1 
ATOM   2583  H  H    . GLY   A 1 166 ? 36.591 24.039  21.408 1.00 11.82 ? 166  GLY   A H    1 
ATOM   2584  H  HA2  . GLY   A 1 166 ? 36.688 25.765  19.424 1.00 14.29 ? 166  GLY   A HA2  1 
ATOM   2585  H  HA3  . GLY   A 1 166 ? 36.994 26.112  20.913 1.00 14.29 ? 166  GLY   A HA3  1 
ATOM   2586  N  N    . GLU   A 1 167 ? 39.524 24.856  20.602 1.00 12.57 ? 167  GLU   A N    1 
ATOM   2587  C  CA   . GLU   A 1 167 ? 40.986 24.852  20.333 1.00 13.06 ? 167  GLU   A CA   1 
ATOM   2588  C  C    . GLU   A 1 167 ? 41.237 24.311  18.924 1.00 15.41 ? 167  GLU   A C    1 
ATOM   2589  O  O    . GLU   A 1 167 ? 42.187 24.780  18.274 1.00 12.77 ? 167  GLU   A O    1 
ATOM   2590  C  CB   . GLU   A 1 167 ? 41.700 23.987  21.373 1.00 12.92 ? 167  GLU   A CB   1 
ATOM   2591  C  CG   . GLU   A 1 167 ? 41.496 24.442  22.804 1.00 15.19 ? 167  GLU   A CG   1 
ATOM   2592  C  CD   . GLU   A 1 167 ? 42.063 23.473  23.827 1.00 15.63 ? 167  GLU   A CD   1 
ATOM   2593  O  OE1  . GLU   A 1 167 ? 42.427 22.354  23.429 1.00 15.23 ? 167  GLU   A OE1  1 
ATOM   2594  O  OE2  . GLU   A 1 167 ? 42.141 23.842  25.011 1.00 12.61 ? 167  GLU   A OE2  1 
ATOM   2595  H  H    . GLU   A 1 167 ? 39.277 24.353  21.254 1.00 15.08 ? 167  GLU   A H    1 
ATOM   2596  H  HA   . GLU   A 1 167 ? 41.334 25.756  20.392 1.00 15.68 ? 167  GLU   A HA   1 
ATOM   2597  H  HB2  . GLU   A 1 167 ? 41.388 23.072  21.287 1.00 15.51 ? 167  GLU   A HB2  1 
ATOM   2598  H  HB3  . GLU   A 1 167 ? 42.650 23.982  21.178 1.00 15.51 ? 167  GLU   A HB3  1 
ATOM   2599  H  HG2  . GLU   A 1 167 ? 41.913 25.310  22.924 1.00 18.23 ? 167  GLU   A HG2  1 
ATOM   2600  H  HG3  . GLU   A 1 167 ? 40.547 24.558  22.968 1.00 18.23 ? 167  GLU   A HG3  1 
ATOM   2601  N  N    . ARG   A 1 168 ? 40.408 23.363  18.481 1.00 13.66 ? 168  ARG   A N    1 
ATOM   2602  C  CA   . ARG   A 1 168 ? 40.598 22.728  17.148 1.00 16.85 ? 168  ARG   A CA   1 
ATOM   2603  C  C    . ARG   A 1 168 ? 39.815 23.480  16.063 1.00 11.94 ? 168  ARG   A C    1 
ATOM   2604  O  O    . ARG   A 1 168 ? 39.813 22.998  14.926 1.00 14.70 ? 168  ARG   A O    1 
ATOM   2605  C  CB   . ARG   A 1 168 ? 40.213 21.247  17.222 1.00 15.59 ? 168  ARG   A CB   1 
ATOM   2606  C  CG   . ARG   A 1 168 ? 41.201 20.420  18.032 1.00 18.58 ? 168  ARG   A CG   1 
ATOM   2607  C  CD   . ARG   A 1 168 ? 40.621 19.163  18.646 1.00 18.79 ? 168  ARG   A CD   1 
ATOM   2608  N  NE   . ARG   A 1 168 ? 41.610 18.457  19.446 1.00 23.44 ? 168  ARG   A NE   1 
ATOM   2609  C  CZ   . ARG   A 1 168 ? 42.511 17.613  18.957 1.00 28.41 ? 168  ARG   A CZ   1 
ATOM   2610  N  NH1  . ARG   A 1 168 ? 42.417 17.197  17.707 1.00 28.06 ? 168  ARG   A NH1  1 
ATOM   2611  N  NH2  . ARG   A 1 168 ? 43.501 17.185  19.721 1.00 29.65 ? 168  ARG   A NH2  1 
ATOM   2612  H  H    . ARG   A 1 168 ? 39.732 23.068  18.924 1.00 16.40 ? 168  ARG   A H    1 
ATOM   2613  H  HA   . ARG   A 1 168 ? 41.534 22.781  16.899 1.00 20.23 ? 168  ARG   A HA   1 
ATOM   2614  H  HB2  . ARG   A 1 168 ? 39.330 21.166  17.616 1.00 18.72 ? 168  ARG   A HB2  1 
ATOM   2615  H  HB3  . ARG   A 1 168 ? 40.156 20.887  16.323 1.00 18.72 ? 168  ARG   A HB3  1 
ATOM   2616  H  HG2  . ARG   A 1 168 ? 41.943 20.172  17.459 1.00 22.30 ? 168  ARG   A HG2  1 
ATOM   2617  H  HG3  . ARG   A 1 168 ? 41.563 20.974  18.741 1.00 22.30 ? 168  ARG   A HG3  1 
ATOM   2618  H  HD2  . ARG   A 1 168 ? 39.859 19.394  19.200 1.00 22.55 ? 168  ARG   A HD2  1 
ATOM   2619  H  HD3  . ARG   A 1 168 ? 40.294 18.579  17.944 1.00 22.55 ? 168  ARG   A HD3  1 
ATOM   2620  H  HE   . ARG   A 1 168 ? 41.611 18.596  20.295 1.00 28.13 ? 168  ARG   A HE   1 
ATOM   2621  H  HH11 . ARG   A 1 168 ? 41.772 17.473  17.209 1.00 33.67 ? 168  ARG   A HH11 1 
ATOM   2622  H  HH12 . ARG   A 1 168 ? 43.001 16.650  17.391 1.00 33.67 ? 168  ARG   A HH12 1 
ATOM   2623  H  HH21 . ARG   A 1 168 ? 43.562 17.453  20.536 1.00 35.59 ? 168  ARG   A HH21 1 
ATOM   2624  H  HH22 . ARG   A 1 168 ? 44.084 16.638  19.403 1.00 35.59 ? 168  ARG   A HH22 1 
ATOM   2625  N  N    . LEU   A 1 169 ? 39.175 24.597  16.412 1.00 13.72 ? 169  LEU   A N    1 
ATOM   2626  C  CA   . LEU   A 1 169 ? 38.490 25.450  15.400 1.00 11.13 ? 169  LEU   A CA   1 
ATOM   2627  C  C    . LEU   A 1 169 ? 37.276 24.729  14.806 1.00 13.54 ? 169  LEU   A C    1 
ATOM   2628  O  O    . LEU   A 1 169 ? 36.939 25.027  13.653 1.00 11.83 ? 169  LEU   A O    1 
ATOM   2629  C  CB   . LEU   A 1 169 ? 39.492 25.837  14.306 1.00 12.53 ? 169  LEU   A CB   1 
ATOM   2630  C  CG   . LEU   A 1 169 ? 40.807 26.435  14.806 1.00 15.17 ? 169  LEU   A CG   1 
ATOM   2631  C  CD1  . LEU   A 1 169 ? 41.599 27.043  13.659 1.00 19.71 ? 169  LEU   A CD1  1 
ATOM   2632  C  CD2  . LEU   A 1 169 ? 40.559 27.474  15.888 1.00 13.74 ? 169  LEU   A CD2  1 
ATOM   2633  H  H    . LEU   A 1 169 ? 39.119 24.887  17.220 1.00 16.47 ? 169  LEU   A H    1 
ATOM   2634  H  HA   . LEU   A 1 169 ? 38.163 26.256  15.830 1.00 13.36 ? 169  LEU   A HA   1 
ATOM   2635  H  HB2  . LEU   A 1 169 ? 39.693 25.048  13.778 1.00 15.04 ? 169  LEU   A HB2  1 
ATOM   2636  H  HB3  . LEU   A 1 169 ? 39.069 26.476  13.712 1.00 15.04 ? 169  LEU   A HB3  1 
ATOM   2637  H  HG   . LEU   A 1 169 ? 41.330 25.715  15.191 1.00 18.20 ? 169  LEU   A HG   1 
ATOM   2638  H  HD11 . LEU   A 1 169 ? 42.427 27.415  13.999 1.00 23.65 ? 169  LEU   A HD11 1 
ATOM   2639  H  HD12 . LEU   A 1 169 ? 41.799 26.356  13.004 1.00 23.65 ? 169  LEU   A HD12 1 
ATOM   2640  H  HD13 . LEU   A 1 169 ? 41.077 27.746  13.241 1.00 23.65 ? 169  LEU   A HD13 1 
ATOM   2641  H  HD21 . LEU   A 1 169 ? 41.407 27.838  16.188 1.00 16.49 ? 169  LEU   A HD21 1 
ATOM   2642  H  HD22 . LEU   A 1 169 ? 40.009 28.189  15.531 1.00 16.49 ? 169  LEU   A HD22 1 
ATOM   2643  H  HD23 . LEU   A 1 169 ? 40.103 27.059  16.637 1.00 16.49 ? 169  LEU   A HD23 1 
ATOM   2644  N  N    . SER   A 1 170 ? 36.650 23.832  15.572 1.00 14.40 ? 170  SER   A N    1 
ATOM   2645  C  CA   . SER   A 1 170 ? 35.401 23.184  15.095 1.00 12.30 ? 170  SER   A CA   1 
ATOM   2646  C  C    . SER   A 1 170 ? 34.325 24.260  14.904 1.00 10.75 ? 170  SER   A C    1 
ATOM   2647  O  O    . SER   A 1 170 ? 34.189 25.121  15.783 1.00 9.12  ? 170  SER   A O    1 
ATOM   2648  C  CB   . SER   A 1 170 ? 34.928 22.125  16.054 1.00 11.39 ? 170  SER   A CB   1 
ATOM   2649  O  OG   . SER   A 1 170 ? 33.571 21.789  15.814 1.00 11.41 ? 170  SER   A OG   1 
ATOM   2650  H  H    . SER   A 1 170 ? 36.915 23.584  16.351 1.00 17.28 ? 170  SER   A H    1 
ATOM   2651  H  HA   . SER   A 1 170 ? 35.579 22.744  14.249 1.00 14.77 ? 170  SER   A HA   1 
ATOM   2652  H  HB2  . SER   A 1 170 ? 35.481 21.333  15.965 1.00 13.68 ? 170  SER   A HB2  1 
ATOM   2653  H  HB3  . SER   A 1 170 ? 35.030 22.441  16.965 1.00 13.68 ? 170  SER   A HB3  1 
ATOM   2654  H  HG   . SER   A 1 170 ? 33.512 21.353  15.099 1.00 13.69 ? 170  SER   A HG   1 
ATOM   2655  N  N    . LEU   A 1 171 ? 33.576 24.189  13.799 1.00 12.01 ? 171  LEU   A N    1 
ATOM   2656  C  CA   . LEU   A 1 171 ? 32.571 25.247  13.515 1.00 10.07 ? 171  LEU   A CA   1 
ATOM   2657  C  C    . LEU   A 1 171 ? 31.331 25.075  14.403 1.00 12.28 ? 171  LEU   A C    1 
ATOM   2658  O  O    . LEU   A 1 171 ? 30.417 25.899  14.268 1.00 12.03 ? 171  LEU   A O    1 
ATOM   2659  C  CB   . LEU   A 1 171 ? 32.227 25.228  12.022 1.00 10.92 ? 171  LEU   A CB   1 
ATOM   2660  C  CG   . LEU   A 1 171 ? 33.392 25.536  11.084 1.00 12.78 ? 171  LEU   A CG   1 
ATOM   2661  C  CD1  . LEU   A 1 171 ? 32.905 25.710  9.654  1.00 13.37 ? 171  LEU   A CD1  1 
ATOM   2662  C  CD2  . LEU   A 1 171 ? 34.142 26.776  11.544 1.00 14.86 ? 171  LEU   A CD2  1 
ATOM   2663  H  H    . LEU   A 1 171 ? 33.624 23.562  13.213 1.00 14.42 ? 171  LEU   A H    1 
ATOM   2664  H  HA   . LEU   A 1 171 ? 32.942 26.118  13.728 1.00 12.08 ? 171  LEU   A HA   1 
ATOM   2665  H  HB2  . LEU   A 1 171 ? 31.872 24.354  11.797 1.00 13.11 ? 171  LEU   A HB2  1 
ATOM   2666  H  HB3  . LEU   A 1 171 ? 31.520 25.872  11.859 1.00 13.11 ? 171  LEU   A HB3  1 
ATOM   2667  H  HG   . LEU   A 1 171 ? 34.002 24.782  11.108 1.00 15.34 ? 171  LEU   A HG   1 
ATOM   2668  H  HD11 . LEU   A 1 171 ? 33.660 25.905  9.076  1.00 16.05 ? 171  LEU   A HD11 1 
ATOM   2669  H  HD12 . LEU   A 1 171 ? 32.473 24.894  9.357  1.00 16.05 ? 171  LEU   A HD12 1 
ATOM   2670  H  HD13 . LEU   A 1 171 ? 32.271 26.443  9.615  1.00 16.05 ? 171  LEU   A HD13 1 
ATOM   2671  H  HD21 . LEU   A 1 171 ? 34.877 26.954  10.936 1.00 17.84 ? 171  LEU   A HD21 1 
ATOM   2672  H  HD22 . LEU   A 1 171 ? 33.538 27.535  11.552 1.00 17.84 ? 171  LEU   A HD22 1 
ATOM   2673  H  HD23 . LEU   A 1 171 ? 34.490 26.631  12.438 1.00 17.84 ? 171  LEU   A HD23 1 
ATOM   2674  N  N    . MET   A 1 172 ? 31.307 24.067  15.277 1.00 9.44  ? 172  MET   A N    1 
ATOM   2675  C  CA   . MET   A 1 172 ? 30.193 23.967  16.260 1.00 9.48  ? 172  MET   A CA   1 
ATOM   2676  C  C    . MET   A 1 172 ? 30.738 24.226  17.672 1.00 9.73  ? 172  MET   A C    1 
ATOM   2677  O  O    . MET   A 1 172 ? 30.063 23.876  18.644 1.00 10.37 ? 172  MET   A O    1 
ATOM   2678  C  CB   . MET   A 1 172 ? 29.484 22.609  16.221 1.00 9.31  ? 172  MET   A CB   1 
ATOM   2679  C  CG   . MET   A 1 172 ? 30.371 21.430  16.538 1.00 10.50 ? 172  MET   A CG   1 
ATOM   2680  S  SD   . MET   A 1 172 ? 29.380 19.915  16.568 1.00 13.59 ? 172  MET   A SD   1 
ATOM   2681  C  CE   . MET   A 1 172 ? 29.111 19.665  14.814 1.00 14.99 ? 172  MET   A CE   1 
ATOM   2682  H  H    . MET   A 1 172 ? 31.899 23.445  15.327 1.00 11.33 ? 172  MET   A H    1 
ATOM   2683  H  HA   . MET   A 1 172 ? 29.534 24.637  16.019 1.00 11.38 ? 172  MET   A HA   1 
ATOM   2684  H  HB2  . MET   A 1 172 ? 28.747 22.624  16.852 1.00 11.17 ? 172  MET   A HB2  1 
ATOM   2685  H  HB3  . MET   A 1 172 ? 29.100 22.483  15.339 1.00 11.17 ? 172  MET   A HB3  1 
ATOM   2686  H  HG2  . MET   A 1 172 ? 31.074 21.355  15.874 1.00 12.61 ? 172  MET   A HG2  1 
ATOM   2687  H  HG3  . MET   A 1 172 ? 30.804 21.561  17.396 1.00 12.61 ? 172  MET   A HG3  1 
ATOM   2688  H  HE1  . MET   A 1 172 ? 28.579 18.865  14.679 1.00 17.99 ? 172  MET   A HE1  1 
ATOM   2689  H  HE2  . MET   A 1 172 ? 28.643 20.431  14.446 1.00 17.99 ? 172  MET   A HE2  1 
ATOM   2690  H  HE3  . MET   A 1 172 ? 29.966 19.564  14.367 1.00 17.99 ? 172  MET   A HE3  1 
ATOM   2691  N  N    . ALA   A 1 173 ? 31.911 24.855  17.758 1.00 9.30  ? 173  ALA   A N    1 
ATOM   2692  C  CA   . ALA   A 1 173 ? 32.524 25.125  19.079 1.00 9.11  ? 173  ALA   A CA   1 
ATOM   2693  C  C    . ALA   A 1 173 ? 31.778 26.244  19.807 1.00 9.93  ? 173  ALA   A C    1 
ATOM   2694  O  O    . ALA   A 1 173 ? 31.400 27.229  19.152 1.00 10.94 ? 173  ALA   A O    1 
ATOM   2695  C  CB   . ALA   A 1 173 ? 33.981 25.461  18.910 1.00 13.70 ? 173  ALA   A CB   1 
ATOM   2696  H  H    . ALA   A 1 173 ? 32.367 25.132  17.083 1.00 11.16 ? 173  ALA   A H    1 
ATOM   2697  H  HA   . ALA   A 1 173 ? 32.455 24.326  19.625 1.00 10.94 ? 173  ALA   A HA   1 
ATOM   2698  H  HB1  . ALA   A 1 173 ? 34.376 25.637  19.779 1.00 16.44 ? 173  ALA   A HB1  1 
ATOM   2699  H  HB2  . ALA   A 1 173 ? 34.439 24.715  18.492 1.00 16.44 ? 173  ALA   A HB2  1 
ATOM   2700  H  HB3  . ALA   A 1 173 ? 34.069 26.248  18.350 1.00 16.44 ? 173  ALA   A HB3  1 
ATOM   2701  N  N    . ALA   A 1 174 ? 31.615 26.101  21.120 1.00 12.16 ? 174  ALA   A N    1 
ATOM   2702  C  CA   . ALA   A 1 174 ? 30.851 27.082  21.914 1.00 11.97 ? 174  ALA   A CA   1 
ATOM   2703  C  C    . ALA   A 1 174 ? 31.752 27.834  22.894 1.00 12.11 ? 174  ALA   A C    1 
ATOM   2704  O  O    . ALA   A 1 174 ? 32.905 27.412  23.080 1.00 12.41 ? 174  ALA   A O    1 
ATOM   2705  C  CB   . ALA   A 1 174 ? 29.794 26.354  22.695 1.00 11.17 ? 174  ALA   A CB   1 
ATOM   2706  H  H    . ALA   A 1 174 ? 31.936 25.446  21.576 1.00 14.60 ? 174  ALA   A H    1 
ATOM   2707  H  HA   . ALA   A 1 174 ? 30.456 27.725  21.305 1.00 14.36 ? 174  ALA   A HA   1 
ATOM   2708  H  HB1  . ALA   A 1 174 ? 29.285 26.990  23.222 1.00 13.41 ? 174  ALA   A HB1  1 
ATOM   2709  H  HB2  . ALA   A 1 174 ? 29.200 25.892  22.083 1.00 13.41 ? 174  ALA   A HB2  1 
ATOM   2710  H  HB3  . ALA   A 1 174 ? 30.214 25.709  23.285 1.00 13.41 ? 174  ALA   A HB3  1 
ATOM   2711  N  N    . VAL   A 1 175 ? 31.223 28.908  23.478 1.00 10.86 ? 175  VAL   A N    1 
ATOM   2712  C  CA   . VAL   A 1 175 ? 31.964 29.648  24.538 1.00 8.89  ? 175  VAL   A CA   1 
ATOM   2713  C  C    . VAL   A 1 175 ? 31.297 29.274  25.862 1.00 13.46 ? 175  VAL   A C    1 
ATOM   2714  O  O    . VAL   A 1 175 ? 30.095 29.525  26.010 1.00 10.99 ? 175  VAL   A O    1 
ATOM   2715  C  CB   . VAL   A 1 175 ? 31.965 31.168  24.297 1.00 12.06 ? 175  VAL   A CB   1 
ATOM   2716  C  CG1  . VAL   A 1 175 ? 32.570 31.917  25.475 1.00 10.58 ? 175  VAL   A CG1  1 
ATOM   2717  C  CG2  . VAL   A 1 175 ? 32.689 31.525  23.008 1.00 12.97 ? 175  VAL   A CG2  1 
ATOM   2718  H  H    . VAL   A 1 175 ? 30.449 29.231  23.288 1.00 13.04 ? 175  VAL   A H    1 
ATOM   2719  H  HA   . VAL   A 1 175 ? 32.902 29.400  24.540 1.00 10.68 ? 175  VAL   A HA   1 
ATOM   2720  H  HB   . VAL   A 1 175 ? 31.039 31.444  24.209 1.00 14.48 ? 175  VAL   A HB   1 
ATOM   2721  H  HG11 . VAL   A 1 175 ? 32.557 32.870  25.294 1.00 12.70 ? 175  VAL   A HG11 1 
ATOM   2722  H  HG12 . VAL   A 1 175 ? 32.054 31.733  26.275 1.00 12.70 ? 175  VAL   A HG12 1 
ATOM   2723  H  HG13 . VAL   A 1 175 ? 33.486 31.626  25.608 1.00 12.70 ? 175  VAL   A HG13 1 
ATOM   2724  H  HG21 . VAL   A 1 175 ? 32.673 32.487  22.883 1.00 15.57 ? 175  VAL   A HG21 1 
ATOM   2725  H  HG22 . VAL   A 1 175 ? 33.609 31.221  23.058 1.00 15.57 ? 175  VAL   A HG22 1 
ATOM   2726  H  HG23 . VAL   A 1 175 ? 32.247 31.095  22.259 1.00 15.57 ? 175  VAL   A HG23 1 
ATOM   2727  N  N    . MET   A 1 176 ? 32.062 28.683  26.777 1.00 11.51 ? 176  MET   A N    1 
ATOM   2728  C  CA   . MET   A 1 176 ? 31.463 28.185  28.036 1.00 11.08 ? 176  MET   A CA   1 
ATOM   2729  C  C    . MET   A 1 176 ? 31.746 29.154  29.180 1.00 9.11  ? 176  MET   A C    1 
ATOM   2730  O  O    . MET   A 1 176 ? 32.777 29.825  29.136 1.00 11.11 ? 176  MET   A O    1 
ATOM   2731  C  CB   . MET   A 1 176 ? 32.065 26.821  28.396 1.00 10.26 ? 176  MET   A CB   1 
ATOM   2732  C  CG   . MET   A 1 176 ? 32.003 25.801  27.278 1.00 12.83 ? 176  MET   A CG   1 
ATOM   2733  S  SD   . MET   A 1 176 ? 30.313 25.451  26.722 1.00 12.28 ? 176  MET   A SD   1 
ATOM   2734  C  CE   . MET   A 1 176 ? 29.517 25.057  28.278 1.00 12.36 ? 176  MET   A CE   1 
ATOM   2735  H  H    . MET   A 1 176 ? 32.909 28.558  26.701 1.00 13.82 ? 176  MET   A H    1 
ATOM   2736  H  HA   . MET   A 1 176 ? 30.505 28.105  27.905 1.00 13.30 ? 176  MET   A HA   1 
ATOM   2737  H  HB2  . MET   A 1 176 ? 32.991 26.946  28.655 1.00 12.31 ? 176  MET   A HB2  1 
ATOM   2738  H  HB3  . MET   A 1 176 ? 31.599 26.467  29.170 1.00 12.31 ? 176  MET   A HB3  1 
ATOM   2739  H  HG2  . MET   A 1 176 ? 32.524 26.122  26.526 1.00 15.40 ? 176  MET   A HG2  1 
ATOM   2740  H  HG3  . MET   A 1 176 ? 32.416 24.976  27.578 1.00 15.40 ? 176  MET   A HG3  1 
ATOM   2741  H  HE1  . MET   A 1 176 ? 28.584 24.845  28.120 1.00 14.84 ? 176  MET   A HE1  1 
ATOM   2742  H  HE2  . MET   A 1 176 ? 29.957 24.293  28.683 1.00 14.84 ? 176  MET   A HE2  1 
ATOM   2743  H  HE3  . MET   A 1 176 ? 29.578 25.819  28.875 1.00 14.84 ? 176  MET   A HE3  1 
ATOM   2744  N  N    . ASN   A 1 177 ? 30.836 29.214  30.148 1.00 10.26 ? 177  ASN   A N    1 
ATOM   2745  C  CA   . ASN   A 1 177 ? 31.085 30.033  31.360 1.00 10.33 ? 177  ASN   A CA   1 
ATOM   2746  C  C    . ASN   A 1 177 ? 30.370 29.371  32.539 1.00 10.30 ? 177  ASN   A C    1 
ATOM   2747  O  O    . ASN   A 1 177 ? 29.291 28.805  32.329 1.00 10.73 ? 177  ASN   A O    1 
ATOM   2748  C  CB   . ASN   A 1 177 ? 30.687 31.500  31.178 1.00 10.06 ? 177  ASN   A CB   1 
ATOM   2749  C  CG   . ASN   A 1 177 ? 29.230 31.700  30.827 1.00 9.71  ? 177  ASN   A CG   1 
ATOM   2750  O  OD1  . ASN   A 1 177 ? 28.859 31.635  29.659 1.00 11.81 ? 177  ASN   A OD1  1 
ATOM   2751  N  ND2  . ASN   A 1 177 ? 28.408 31.965  31.829 1.00 11.22 ? 177  ASN   A ND2  1 
ATOM   2752  H  H    . ASN   A 1 177 ? 30.081 28.802  30.135 1.00 12.32 ? 177  ASN   A H    1 
ATOM   2753  H  HA   . ASN   A 1 177 ? 32.039 30.061  31.536 1.00 12.39 ? 177  ASN   A HA   1 
ATOM   2754  H  HB2  . ASN   A 1 177 ? 30.883 31.983  31.996 1.00 12.07 ? 177  ASN   A HB2  1 
ATOM   2755  H  HB3  . ASN   A 1 177 ? 31.235 31.891  30.480 1.00 12.07 ? 177  ASN   A HB3  1 
ATOM   2756  H  HD21 . ASN   A 1 177 ? 27.573 32.101  31.676 1.00 13.46 ? 177  ASN   A HD21 1 
ATOM   2757  H  HD22 . ASN   A 1 177 ? 28.709 32.001  32.634 1.00 13.46 ? 177  ASN   A HD22 1 
ATOM   2758  N  N    . ASP   A 1 178 ? 30.971 29.444  33.726 1.00 8.52  ? 178  ASP   A N    1 
ATOM   2759  C  CA   . ASP   A 1 178 ? 30.344 28.853  34.937 1.00 10.86 ? 178  ASP   A CA   1 
ATOM   2760  C  C    . ASP   A 1 178 ? 30.133 27.349  34.706 1.00 10.67 ? 178  ASP   A C    1 
ATOM   2761  O  O    . ASP   A 1 178 ? 29.111 26.831  35.182 1.00 11.84 ? 178  ASP   A O    1 
ATOM   2762  C  CB   . ASP   A 1 178 ? 29.103 29.655  35.341 1.00 10.50 ? 178  ASP   A CB   1 
ATOM   2763  C  CG   . ASP   A 1 178 ? 29.398 31.133  35.546 1.00 11.15 ? 178  ASP   A CG   1 
ATOM   2764  O  OD1  . ASP   A 1 178 ? 30.203 31.447  36.440 1.00 14.93 ? 178  ASP   A OD1  1 
ATOM   2765  O  OD2  . ASP   A 1 178 ? 28.823 31.955  34.810 1.00 11.30 ? 178  ASP   A OD2  1 
ATOM   2766  H  H    . ASP   A 1 178 ? 31.731 29.823  33.862 1.00 10.23 ? 178  ASP   A H    1 
ATOM   2767  H  HA   . ASP   A 1 178 ? 30.924 28.917  35.712 1.00 13.04 ? 178  ASP   A HA   1 
ATOM   2768  H  HB2  . ASP   A 1 178 ? 28.423 29.557  34.657 1.00 12.60 ? 178  ASP   A HB2  1 
ATOM   2769  H  HB3  . ASP   A 1 178 ? 28.737 29.286  36.160 1.00 12.60 ? 178  ASP   A HB3  1 
ATOM   2770  N  N    . VAL   A 1 179 ? 31.051 26.700  33.983 1.00 11.79 ? 179  VAL   A N    1 
ATOM   2771  C  CA   . VAL   A 1 179 ? 31.035 25.216  33.780 1.00 11.47 ? 179  VAL   A CA   1 
ATOM   2772  C  C    . VAL   A 1 179 ? 29.944 24.730  32.815 1.00 11.55 ? 179  VAL   A C    1 
ATOM   2773  O  O    . VAL   A 1 179 ? 30.276 23.912  31.947 1.00 12.57 ? 179  VAL   A O    1 
ATOM   2774  C  CB   . VAL   A 1 179 ? 30.923 24.471  35.127 1.00 13.54 ? 179  VAL   A CB   1 
ATOM   2775  C  CG1  . VAL   A 1 179 ? 31.055 22.968  34.941 1.00 15.89 ? 179  VAL   A CG1  1 
ATOM   2776  C  CG2  . VAL   A 1 179 ? 31.946 24.973  36.136 1.00 13.36 ? 179  VAL   A CG2  1 
ATOM   2777  H  H    . VAL   A 1 179 ? 31.706 27.095  33.591 1.00 14.15 ? 179  VAL   A H    1 
ATOM   2778  H  HA   . VAL   A 1 179 ? 31.885 25.005  33.362 1.00 13.76 ? 179  VAL   A HA   1 
ATOM   2779  H  HB   . VAL   A 1 179 ? 30.039 24.658  35.480 1.00 16.26 ? 179  VAL   A HB   1 
ATOM   2780  H  HG11 . VAL   A 1 179 ? 30.981 22.527  35.802 1.00 19.07 ? 179  VAL   A HG11 1 
ATOM   2781  H  HG12 . VAL   A 1 179 ? 30.350 22.651  34.354 1.00 19.07 ? 179  VAL   A HG12 1 
ATOM   2782  H  HG13 . VAL   A 1 179 ? 31.918 22.765  34.548 1.00 19.07 ? 179  VAL   A HG13 1 
ATOM   2783  H  HG21 . VAL   A 1 179 ? 31.847 24.484  36.968 1.00 16.04 ? 179  VAL   A HG21 1 
ATOM   2784  H  HG22 . VAL   A 1 179 ? 32.840 24.836  35.786 1.00 16.04 ? 179  VAL   A HG22 1 
ATOM   2785  H  HG23 . VAL   A 1 179 ? 31.804 25.919  36.298 1.00 16.04 ? 179  VAL   A HG23 1 
ATOM   2786  N  N    . ASP   A 1 180 ? 28.708 25.202  32.968 1.00 10.40 ? 180  ASP   A N    1 
ATOM   2787  C  CA   . ASP   A 1 180 ? 27.608 24.604  32.162 1.00 12.10 ? 180  ASP   A CA   1 
ATOM   2788  C  C    . ASP   A 1 180 ? 26.692 25.644  31.504 1.00 11.43 ? 180  ASP   A C    1 
ATOM   2789  O  O    . ASP   A 1 180 ? 25.628 25.241  31.006 1.00 12.70 ? 180  ASP   A O    1 
ATOM   2790  C  CB   . ASP   A 1 180 ? 26.789 23.663  33.046 1.00 13.45 ? 180  ASP   A CB   1 
ATOM   2791  C  CG   . ASP   A 1 180 ? 26.479 24.258  34.408 1.00 15.10 ? 180  ASP   A CG   1 
ATOM   2792  O  OD1  . ASP   A 1 180 ? 25.799 25.296  34.447 1.00 12.99 ? 180  ASP   A OD1  1 
ATOM   2793  O  OD2  . ASP   A 1 180 ? 26.923 23.677  35.415 1.00 18.13 ? 180  ASP   A OD2  1 
ATOM   2794  H  H    . ASP   A 1 180 ? 28.479 25.836  33.502 1.00 12.49 ? 180  ASP   A H    1 
ATOM   2795  H  HA   . ASP   A 1 180 ? 28.023 24.115  31.434 1.00 14.53 ? 180  ASP   A HA   1 
ATOM   2796  H  HB2  . ASP   A 1 180 ? 25.958 23.445  32.596 1.00 16.15 ? 180  ASP   A HB2  1 
ATOM   2797  H  HB3  . ASP   A 1 180 ? 27.275 22.832  33.164 1.00 16.15 ? 180  ASP   A HB3  1 
ATOM   2798  N  N    . ARG   A 1 181 ? 27.077 26.915  31.493 1.00 10.54 ? 181  ARG   A N    1 
ATOM   2799  C  CA   . ARG   A 1 181 ? 26.286 27.942  30.761 1.00 11.30 ? 181  ARG   A CA   1 
ATOM   2800  C  C    . ARG   A 1 181 ? 27.057 28.250  29.466 1.00 11.11 ? 181  ARG   A C    1 
ATOM   2801  O  O    . ARG   A 1 181 ? 28.253 28.036  29.447 1.00 11.52 ? 181  ARG   A O    1 
ATOM   2802  C  CB   . ARG   A 1 181 ? 26.019 29.165  31.639 1.00 9.68  ? 181  ARG   A CB   1 
ATOM   2803  C  CG   . ARG   A 1 181 ? 25.439 28.849  33.011 1.00 9.78  ? 181  ARG   A CG   1 
ATOM   2804  C  CD   . ARG   A 1 181 ? 24.169 28.018  32.992 1.00 12.32 ? 181  ARG   A CD   1 
ATOM   2805  N  NE   . ARG   A 1 181 ? 23.044 28.716  32.392 1.00 9.74  ? 181  ARG   A NE   1 
ATOM   2806  C  CZ   . ARG   A 1 181 ? 21.776 28.336  32.493 1.00 10.75 ? 181  ARG   A CZ   1 
ATOM   2807  N  NH1  . ARG   A 1 181 ? 21.453 27.263  33.188 1.00 12.32 ? 181  ARG   A NH1  1 
ATOM   2808  N  NH2  . ARG   A 1 181 ? 20.829 29.043  31.908 1.00 11.65 ? 181  ARG   A NH2  1 
ATOM   2809  H  H    . ARG   A 1 181 ? 27.778 27.214  31.891 1.00 12.65 ? 181  ARG   A H    1 
ATOM   2810  H  HA   . ARG   A 1 181 ? 25.400 27.622  30.530 1.00 13.57 ? 181  ARG   A HA   1 
ATOM   2811  H  HB2  . ARG   A 1 181 ? 26.850 29.651  31.757 1.00 11.62 ? 181  ARG   A HB2  1 
ATOM   2812  H  HB3  . ARG   A 1 181 ? 25.408 29.756  31.172 1.00 11.62 ? 181  ARG   A HB3  1 
ATOM   2813  H  HG2  . ARG   A 1 181 ? 26.110 28.379  33.531 1.00 11.74 ? 181  ARG   A HG2  1 
ATOM   2814  H  HG3  . ARG   A 1 181 ? 25.257 29.683  33.471 1.00 11.74 ? 181  ARG   A HG3  1 
ATOM   2815  H  HD2  . ARG   A 1 181 ? 24.333 27.197  32.502 1.00 14.79 ? 181  ARG   A HD2  1 
ATOM   2816  H  HD3  . ARG   A 1 181 ? 23.940 27.765  33.900 1.00 14.79 ? 181  ARG   A HD3  1 
ATOM   2817  H  HE   . ARG   A 1 181 ? 23.212 29.427  31.938 1.00 11.69 ? 181  ARG   A HE   1 
ATOM   2818  H  HH11 . ARG   A 1 181 ? 22.066 26.804  33.580 1.00 14.79 ? 181  ARG   A HH11 1 
ATOM   2819  H  HH12 . ARG   A 1 181 ? 20.630 27.022  33.249 1.00 14.79 ? 181  ARG   A HH12 1 
ATOM   2820  H  HH21 . ARG   A 1 181 ? 21.033 29.749  31.462 1.00 13.99 ? 181  ARG   A HH21 1 
ATOM   2821  H  HH22 . ARG   A 1 181 ? 20.007 28.798  31.973 1.00 13.99 ? 181  ARG   A HH22 1 
ATOM   2822  N  N    . THR   A 1 182 ? 26.373 28.737  28.425 1.00 8.69  ? 182  THR   A N    1 
ATOM   2823  C  CA   . THR   A 1 182 ? 27.152 28.909  27.176 1.00 10.29 ? 182  THR   A CA   1 
ATOM   2824  C  C    . THR   A 1 182 ? 26.589 29.890  26.152 1.00 8.95  ? 182  THR   A C    1 
ATOM   2825  O  O    . THR   A 1 182 ? 25.360 29.967  26.027 1.00 7.97  ? 182  THR   A O    1 
ATOM   2826  C  CB   . THR   A 1 182 ? 27.281 27.585  26.410 1.00 10.04 ? 182  THR   A CB   1 
ATOM   2827  O  OG1  . THR   A 1 182 ? 27.920 27.842  25.160 1.00 9.65  ? 182  THR   A OG1  1 
ATOM   2828  C  CG2  . THR   A 1 182 ? 25.950 26.902  26.179 1.00 10.79 ? 182  THR   A CG2  1 
ATOM   2829  H  H    . THR   A 1 182 ? 25.542 28.957  28.406 1.00 10.43 ? 182  THR   A H    1 
ATOM   2830  H  HA   . THR   A 1 182 ? 27.992 29.257  27.515 1.00 12.35 ? 182  THR   A HA   1 
ATOM   2831  H  HB   . THR   A 1 182 ? 27.809 26.979  26.953 1.00 12.05 ? 182  THR   A HB   1 
ATOM   2832  H  HG1  . THR   A 1 182 ? 28.587 28.338  25.283 1.00 11.58 ? 182  THR   A HG1  1 
ATOM   2833  H  HG21 . THR   A 1 182 ? 26.091 26.074  25.693 1.00 12.95 ? 182  THR   A HG21 1 
ATOM   2834  H  HG22 . THR   A 1 182 ? 25.533 26.708  27.033 1.00 12.95 ? 182  THR   A HG22 1 
ATOM   2835  H  HG23 . THR   A 1 182 ? 25.372 27.485  25.663 1.00 12.95 ? 182  THR   A HG23 1 
ATOM   2836  N  N    . ALA   A 1 183 ? 27.478 30.671  25.540 1.00 9.39  ? 183  ALA   A N    1 
ATOM   2837  C  CA   . ALA   A 1 183 ? 27.111 31.454  24.345 1.00 9.32  ? 183  ALA   A CA   1 
ATOM   2838  C  C    . ALA   A 1 183 ? 27.522 30.409  23.315 1.00 11.02 ? 183  ALA   A C    1 
ATOM   2839  O  O    . ALA   A 1 183 ? 28.716 30.307  23.021 1.00 9.41  ? 183  ALA   A O    1 
ATOM   2840  C  CB   . ALA   A 1 183 ? 27.928 32.709  24.287 1.00 10.62 ? 183  ALA   A CB   1 
ATOM   2841  H  H    . ALA   A 1 183 ? 28.294 30.765  25.794 1.00 11.27 ? 183  ALA   A H    1 
ATOM   2842  H  HA   . ALA   A 1 183 ? 26.201 31.779  24.263 1.00 11.19 ? 183  ALA   A HA   1 
ATOM   2843  H  HB1  . ALA   A 1 183 ? 27.682 33.219  23.500 1.00 12.75 ? 183  ALA   A HB1  1 
ATOM   2844  H  HB2  . ALA   A 1 183 ? 27.762 33.241  25.081 1.00 12.75 ? 183  ALA   A HB2  1 
ATOM   2845  H  HB3  . ALA   A 1 183 ? 28.870 32.481  24.243 1.00 12.75 ? 183  ALA   A HB3  1 
ATOM   2846  N  N    . ALA   A 1 184 ? 26.569 29.630  22.808 1.00 9.07  ? 184  ALA   A N    1 
ATOM   2847  C  CA   . ALA   A 1 184 ? 26.957 28.409  22.059 1.00 9.21  ? 184  ALA   A CA   1 
ATOM   2848  C  C    . ALA   A 1 184 ? 26.946 28.396  20.531 1.00 9.34  ? 184  ALA   A C    1 
ATOM   2849  O  O    . ALA   A 1 184 ? 27.806 27.711  19.965 1.00 9.72  ? 184  ALA   A O    1 
ATOM   2850  C  CB   . ALA   A 1 184 ? 26.006 27.323  22.512 1.00 9.29  ? 184  ALA   A CB   1 
ATOM   2851  H  H    . ALA   A 1 184 ? 25.723 29.772  22.876 1.00 10.89 ? 184  ALA   A H    1 
ATOM   2852  H  HA   . ALA   A 1 184 ? 27.900 28.308  22.265 1.00 11.05 ? 184  ALA   A HA   1 
ATOM   2853  H  HB1  . ALA   A 1 184 ? 26.216 26.496  22.051 1.00 11.15 ? 184  ALA   A HB1  1 
ATOM   2854  H  HB2  . ALA   A 1 184 ? 26.097 27.191  23.469 1.00 11.15 ? 184  ALA   A HB2  1 
ATOM   2855  H  HB3  . ALA   A 1 184 ? 25.095 27.585  22.308 1.00 11.15 ? 184  ALA   A HB3  1 
ATOM   2856  N  N    . ARG   A 1 185 ? 25.997 29.070  19.890 1.00 12.35 ? 185  ARG   A N    1 
ATOM   2857  C  CA   . ARG   A 1 185 ? 25.852 28.831  18.426 1.00 10.31 ? 185  ARG   A CA   1 
ATOM   2858  C  C    . ARG   A 1 185 ? 26.726 29.705  17.516 1.00 11.33 ? 185  ARG   A C    1 
ATOM   2859  O  O    . ARG   A 1 185 ? 27.283 30.705  17.987 1.00 10.02 ? 185  ARG   A O    1 
ATOM   2860  C  CB   . ARG   A 1 185 ? 24.363 28.908  18.059 1.00 10.79 ? 185  ARG   A CB   1 
ATOM   2861  C  CG   . ARG   A 1 185 ? 23.456 28.198  19.055 1.00 12.92 ? 185  ARG   A CG   1 
ATOM   2862  C  CD   . ARG   A 1 185 ? 22.172 27.684  18.432 1.00 9.26  ? 185  ARG   A CD   1 
ATOM   2863  N  NE   . ARG   A 1 185 ? 22.386 26.525  17.580 1.00 9.62  ? 185  ARG   A NE   1 
ATOM   2864  C  CZ   . ARG   A 1 185 ? 21.614 26.193  16.552 1.00 10.13 ? 185  ARG   A CZ   1 
ATOM   2865  N  NH1  . ARG   A 1 185 ? 20.490 26.849  16.330 1.00 9.37  ? 185  ARG   A NH1  1 
ATOM   2866  N  NH2  . ARG   A 1 185 ? 21.969 25.204  15.752 1.00 8.32  ? 185  ARG   A NH2  1 
ATOM   2867  H  H    . ARG   A 1 185 ? 25.453 29.636  20.241 1.00 14.82 ? 185  ARG   A H    1 
ATOM   2868  H  HA   . ARG   A 1 185 ? 26.198 27.941  18.254 1.00 12.38 ? 185  ARG   A HA   1 
ATOM   2869  H  HB2  . ARG   A 1 185 ? 24.099 29.840  17.999 1.00 12.95 ? 185  ARG   A HB2  1 
ATOM   2870  H  HB3  . ARG   A 1 185 ? 24.233 28.519  17.180 1.00 12.95 ? 185  ARG   A HB3  1 
ATOM   2871  H  HG2  . ARG   A 1 185 ? 23.938 27.454  19.449 1.00 15.51 ? 185  ARG   A HG2  1 
ATOM   2872  H  HG3  . ARG   A 1 185 ? 23.237 28.808  19.776 1.00 15.51 ? 185  ARG   A HG3  1 
ATOM   2873  H  HD2  . ARG   A 1 185 ? 21.546 27.452  19.136 1.00 11.12 ? 185  ARG   A HD2  1 
ATOM   2874  H  HD3  . ARG   A 1 185 ? 21.763 28.393  17.911 1.00 11.12 ? 185  ARG   A HD3  1 
ATOM   2875  H  HE   . ARG   A 1 185 ? 23.060 26.019  17.754 1.00 11.55 ? 185  ARG   A HE   1 
ATOM   2876  H  HH11 . ARG   A 1 185 ? 20.257 27.492  16.851 1.00 11.25 ? 185  ARG   A HH11 1 
ATOM   2877  H  HH12 . ARG   A 1 185 ? 19.991 26.633  15.664 1.00 11.25 ? 185  ARG   A HH12 1 
ATOM   2878  H  HH21 . ARG   A 1 185 ? 22.700 24.775  15.897 1.00 9.99  ? 185  ARG   A HH21 1 
ATOM   2879  H  HH22 . ARG   A 1 185 ? 21.469 24.989  15.086 1.00 9.99  ? 185  ARG   A HH22 1 
ATOM   2880  N  N    . GLY   A 1 186 ? 26.837 29.291  16.249 1.00 10.88 ? 186  GLY   A N    1 
ATOM   2881  C  CA   . GLY   A 1 186 ? 27.588 30.077  15.250 1.00 11.71 ? 186  GLY   A CA   1 
ATOM   2882  C  C    . GLY   A 1 186 ? 29.054 29.698  15.146 1.00 9.72  ? 186  GLY   A C    1 
ATOM   2883  O  O    . GLY   A 1 186 ? 29.728 30.231  14.255 1.00 10.36 ? 186  GLY   A O    1 
ATOM   2884  H  H    . GLY   A 1 186 ? 26.490 28.565  15.946 1.00 13.06 ? 186  GLY   A H    1 
ATOM   2885  H  HA2  . GLY   A 1 186 ? 27.171 29.963  14.382 1.00 14.06 ? 186  GLY   A HA2  1 
ATOM   2886  H  HA3  . GLY   A 1 186 ? 27.521 31.018  15.475 1.00 14.06 ? 186  GLY   A HA3  1 
ATOM   2887  N  N    . GLY   A 1 187 ? 29.527 28.815  16.024 1.00 11.46 ? 187  GLY   A N    1 
ATOM   2888  C  CA   . GLY   A 1 187 ? 30.966 28.485  16.046 1.00 10.40 ? 187  GLY   A CA   1 
ATOM   2889  C  C    . GLY   A 1 187 ? 31.771 29.590  16.714 1.00 10.54 ? 187  GLY   A C    1 
ATOM   2890  O  O    . GLY   A 1 187 ? 32.968 29.708  16.417 1.00 11.97 ? 187  GLY   A O    1 
ATOM   2891  H  H    . GLY   A 1 187 ? 29.049 28.400  16.606 1.00 13.75 ? 187  GLY   A H    1 
ATOM   2892  H  HA2  . GLY   A 1 187 ? 31.102 27.650  16.520 1.00 12.49 ? 187  GLY   A HA2  1 
ATOM   2893  H  HA3  . GLY   A 1 187 ? 31.284 28.352  15.139 1.00 12.49 ? 187  GLY   A HA3  1 
ATOM   2894  N  N    . VAL   A 1 188 ? 31.139 30.366  17.590 1.00 10.48 ? 188  VAL   A N    1 
ATOM   2895  C  CA   . VAL   A 1 188 ? 31.836 31.538  18.200 1.00 11.69 ? 188  VAL   A CA   1 
ATOM   2896  C  C    . VAL   A 1 188 ? 33.039 31.047  19.016 1.00 11.35 ? 188  VAL   A C    1 
ATOM   2897  O  O    . VAL   A 1 188 ? 33.992 31.819  19.186 1.00 10.43 ? 188  VAL   A O    1 
ATOM   2898  C  CB   . VAL   A 1 188 ? 30.869 32.381  19.050 1.00 9.61  ? 188  VAL   A CB   1 
ATOM   2899  C  CG1  . VAL   A 1 188 ? 29.883 33.143  18.178 1.00 14.39 ? 188  VAL   A CG1  1 
ATOM   2900  C  CG2  . VAL   A 1 188 ? 30.133 31.530  20.073 1.00 13.13 ? 188  VAL   A CG2  1 
ATOM   2901  H  H    . VAL   A 1 188 ? 30.328 30.249  17.850 1.00 12.58 ? 188  VAL   A H    1 
ATOM   2902  H  HA   . VAL   A 1 188 ? 32.161 32.119  17.495 1.00 14.03 ? 188  VAL   A HA   1 
ATOM   2903  H  HB   . VAL   A 1 188 ? 31.407 33.028  19.533 1.00 11.54 ? 188  VAL   A HB   1 
ATOM   2904  H  HG11 . VAL   A 1 188 ? 29.288 33.664  18.740 1.00 17.28 ? 188  VAL   A HG11 1 
ATOM   2905  H  HG12 . VAL   A 1 188 ? 30.368 33.737  17.584 1.00 17.28 ? 188  VAL   A HG12 1 
ATOM   2906  H  HG13 . VAL   A 1 188 ? 29.363 32.515  17.653 1.00 17.28 ? 188  VAL   A HG13 1 
ATOM   2907  H  HG21 . VAL   A 1 188 ? 29.534 32.091  20.590 1.00 15.75 ? 188  VAL   A HG21 1 
ATOM   2908  H  HG22 . VAL   A 1 188 ? 29.620 30.845  19.616 1.00 15.75 ? 188  VAL   A HG22 1 
ATOM   2909  H  HG23 . VAL   A 1 188 ? 30.775 31.110  20.667 1.00 15.75 ? 188  VAL   A HG23 1 
ATOM   2910  N  N    . GLY   A 1 189 ? 32.980 29.807  19.497 1.00 11.71 ? 189  GLY   A N    1 
ATOM   2911  C  CA   . GLY   A 1 189 ? 34.106 29.256  20.274 1.00 11.63 ? 189  GLY   A CA   1 
ATOM   2912  C  C    . GLY   A 1 189 ? 35.344 29.065  19.413 1.00 13.90 ? 189  GLY   A C    1 
ATOM   2913  O  O    . GLY   A 1 189 ? 36.455 29.121  19.947 1.00 10.59 ? 189  GLY   A O    1 
ATOM   2914  H  H    . GLY   A 1 189 ? 32.314 29.273  19.391 1.00 14.06 ? 189  GLY   A H    1 
ATOM   2915  H  HA2  . GLY   A 1 189 ? 34.313 29.852  21.011 1.00 13.95 ? 189  GLY   A HA2  1 
ATOM   2916  H  HA3  . GLY   A 1 189 ? 33.847 28.405  20.661 1.00 13.95 ? 189  GLY   A HA3  1 
ATOM   2917  N  N    . ALA   A 1 190 ? 35.145 28.831  18.118 1.00 12.93 ? 190  ALA   A N    1 
ATOM   2918  C  CA   . ALA   A 1 190 ? 36.293 28.650  17.202 1.00 9.82  ? 190  ALA   A CA   1 
ATOM   2919  C  C    . ALA   A 1 190 ? 36.997 29.994  16.985 1.00 10.06 ? 190  ALA   A C    1 
ATOM   2920  O  O    . ALA   A 1 190 ? 38.200 29.994  16.721 1.00 10.65 ? 190  ALA   A O    1 
ATOM   2921  C  CB   . ALA   A 1 190 ? 35.834 28.056  15.899 1.00 11.72 ? 190  ALA   A CB   1 
ATOM   2922  H  H    . ALA   A 1 190 ? 34.372 28.772  17.746 1.00 15.52 ? 190  ALA   A H    1 
ATOM   2923  H  HA   . ALA   A 1 190 ? 36.928 28.033  17.599 1.00 11.78 ? 190  ALA   A HA   1 
ATOM   2924  H  HB1  . ALA   A 1 190 ? 36.595 27.943  15.309 1.00 14.06 ? 190  ALA   A HB1  1 
ATOM   2925  H  HB2  . ALA   A 1 190 ? 35.422 27.193  16.064 1.00 14.06 ? 190  ALA   A HB2  1 
ATOM   2926  H  HB3  . ALA   A 1 190 ? 35.188 28.648  15.483 1.00 14.06 ? 190  ALA   A HB3  1 
ATOM   2927  N  N    . VAL   A 1 191 ? 36.258 31.094  17.108 1.00 9.75  ? 191  VAL   A N    1 
ATOM   2928  C  CA   . VAL   A 1 191 ? 36.901 32.431  16.974 1.00 10.29 ? 191  VAL   A CA   1 
ATOM   2929  C  C    . VAL   A 1 191 ? 37.865 32.590  18.153 1.00 10.59 ? 191  VAL   A C    1 
ATOM   2930  O  O    . VAL   A 1 191 ? 39.022 32.969  17.935 1.00 11.99 ? 191  VAL   A O    1 
ATOM   2931  C  CB   . VAL   A 1 191 ? 35.866 33.571  16.914 1.00 11.37 ? 191  VAL   A CB   1 
ATOM   2932  C  CG1  . VAL   A 1 191 ? 36.540 34.935  16.871 1.00 13.51 ? 191  VAL   A CG1  1 
ATOM   2933  C  CG2  . VAL   A 1 191 ? 34.926 33.408  15.730 1.00 11.33 ? 191  VAL   A CG2  1 
ATOM   2934  H  H    . VAL   A 1 191 ? 35.412 31.105  17.263 1.00 11.71 ? 191  VAL   A H    1 
ATOM   2935  H  HA   . VAL   A 1 191 ? 37.385 32.486  16.135 1.00 12.36 ? 191  VAL   A HA   1 
ATOM   2936  H  HB   . VAL   A 1 191 ? 35.340 33.519  17.728 1.00 13.65 ? 191  VAL   A HB   1 
ATOM   2937  H  HG11 . VAL   A 1 191 ? 35.864 35.629  16.834 1.00 16.22 ? 191  VAL   A HG11 1 
ATOM   2938  H  HG12 . VAL   A 1 191 ? 37.081 35.054  17.667 1.00 16.22 ? 191  VAL   A HG12 1 
ATOM   2939  H  HG13 . VAL   A 1 191 ? 37.105 34.992  16.085 1.00 16.22 ? 191  VAL   A HG13 1 
ATOM   2940  H  HG21 . VAL   A 1 191 ? 34.288 34.139  15.720 1.00 13.60 ? 191  VAL   A HG21 1 
ATOM   2941  H  HG22 . VAL   A 1 191 ? 35.438 33.415  14.906 1.00 13.60 ? 191  VAL   A HG22 1 
ATOM   2942  H  HG23 . VAL   A 1 191 ? 34.451 32.566  15.807 1.00 13.60 ? 191  VAL   A HG23 1 
ATOM   2943  N  N    . MET   A 1 192 ? 37.386 32.279  19.356 1.00 10.74 ? 192  MET   A N    1 
ATOM   2944  C  CA   . MET   A 1 192 ? 38.261 32.362  20.553 1.00 12.56 ? 192  MET   A CA   1 
ATOM   2945  C  C    . MET   A 1 192 ? 39.485 31.465  20.334 1.00 13.87 ? 192  MET   A C    1 
ATOM   2946  O  O    . MET   A 1 192 ? 40.607 31.928  20.587 1.00 13.00 ? 192  MET   A O    1 
ATOM   2947  C  CB   . MET   A 1 192 ? 37.498 31.915  21.803 1.00 14.71 ? 192  MET   A CB   1 
ATOM   2948  C  CG   . MET   A 1 192 ? 37.975 32.570  23.079 1.00 17.81 ? 192  MET   A CG   1 
ATOM   2949  S  SD   . MET   A 1 192 ? 36.773 32.343  24.413 1.00 13.26 ? 192  MET   A SD   1 
ATOM   2950  C  CE   . MET   A 1 192 ? 37.875 31.985  25.781 1.00 13.25 ? 192  MET   A CE   1 
ATOM   2951  H  H    . MET   A 1 192 ? 36.580 32.023  19.511 1.00 12.89 ? 192  MET   A H    1 
ATOM   2952  H  HA   . MET   A 1 192 ? 38.546 33.280  20.683 1.00 15.07 ? 192  MET   A HA   1 
ATOM   2953  H  HB2  . MET   A 1 192 ? 36.555 32.110  21.683 1.00 17.65 ? 192  MET   A HB2  1 
ATOM   2954  H  HB3  . MET   A 1 192 ? 37.579 30.953  21.894 1.00 17.65 ? 192  MET   A HB3  1 
ATOM   2955  H  HG2  . MET   A 1 192 ? 38.829 32.192  23.341 1.00 21.37 ? 192  MET   A HG2  1 
ATOM   2956  H  HG3  . MET   A 1 192 ? 38.119 33.517  22.926 1.00 21.37 ? 192  MET   A HG3  1 
ATOM   2957  H  HE1  . MET   A 1 192 ? 37.354 31.837  26.586 1.00 15.91 ? 192  MET   A HE1  1 
ATOM   2958  H  HE2  . MET   A 1 192 ? 38.392 31.189  25.580 1.00 15.91 ? 192  MET   A HE2  1 
ATOM   2959  H  HE3  . MET   A 1 192 ? 38.475 32.735  25.918 1.00 15.91 ? 192  MET   A HE3  1 
ATOM   2960  N  N    . GLY   A 1 193 ? 39.266 30.231  19.876 1.00 13.73 ? 193  GLY   A N    1 
ATOM   2961  C  CA   . GLY   A 1 193 ? 40.385 29.305  19.622 1.00 12.34 ? 193  GLY   A CA   1 
ATOM   2962  C  C    . GLY   A 1 193 ? 41.332 29.846  18.565 1.00 11.94 ? 193  GLY   A C    1 
ATOM   2963  O  O    . GLY   A 1 193 ? 42.545 29.656  18.713 1.00 14.96 ? 193  GLY   A O    1 
ATOM   2964  H  H    . GLY   A 1 193 ? 38.487 29.909  19.706 1.00 16.48 ? 193  GLY   A H    1 
ATOM   2965  H  HA2  . GLY   A 1 193 ? 40.873 29.152  20.446 1.00 14.81 ? 193  GLY   A HA2  1 
ATOM   2966  H  HA3  . GLY   A 1 193 ? 40.036 28.446  19.336 1.00 14.81 ? 193  GLY   A HA3  1 
ATOM   2967  N  N    . SER   A 1 194 ? 40.786 30.487  17.530 1.00 12.83 ? 194  SER   A N    1 
ATOM   2968  C  CA   . SER   A 1 194 ? 41.620 31.063  16.444 1.00 11.56 ? 194  SER   A CA   1 
ATOM   2969  C  C    . SER   A 1 194 ? 42.542 32.154  17.001 1.00 14.05 ? 194  SER   A C    1 
ATOM   2970  O  O    . SER   A 1 194 ? 43.501 32.515  16.307 1.00 14.28 ? 194  SER   A O    1 
ATOM   2971  C  CB   . SER   A 1 194 ? 40.752 31.612  15.333 1.00 12.98 ? 194  SER   A CB   1 
ATOM   2972  O  OG   . SER   A 1 194 ? 40.136 32.830  15.714 1.00 13.38 ? 194  SER   A OG   1 
ATOM   2973  H  H    . SER   A 1 194 ? 39.940 30.604  17.429 1.00 15.40 ? 194  SER   A H    1 
ATOM   2974  H  HA   . SER   A 1 194 ? 42.170 30.355  16.073 1.00 13.88 ? 194  SER   A HA   1 
ATOM   2975  H  HB2  . SER   A 1 194 ? 41.291 31.754  14.539 1.00 15.58 ? 194  SER   A HB2  1 
ATOM   2976  H  HB3  . SER   A 1 194 ? 40.071 30.962  15.101 1.00 15.58 ? 194  SER   A HB3  1 
ATOM   2977  H  HG   . SER   A 1 194 ? 39.944 32.804  16.531 1.00 16.06 ? 194  SER   A HG   1 
ATOM   2978  N  N    . LYS   A 1 195 ? 42.239 32.668  18.193 1.00 13.23 ? 195  LYS   A N    1 
ATOM   2979  C  CA   . LYS   A 1 195 ? 43.040 33.781  18.769 1.00 14.44 ? 195  LYS   A CA   1 
ATOM   2980  C  C    . LYS   A 1 195 ? 44.017 33.218  19.803 1.00 14.78 ? 195  LYS   A C    1 
ATOM   2981  O  O    . LYS   A 1 195 ? 44.718 34.018  20.437 1.00 14.27 ? 195  LYS   A O    1 
ATOM   2982  C  CB   . LYS   A 1 195 ? 42.117 34.820  19.408 1.00 12.49 ? 195  LYS   A CB   1 
ATOM   2983  C  CG   . LYS   A 1 195 ? 41.210 35.552  18.429 1.00 11.22 ? 195  LYS   A CG   1 
ATOM   2984  C  CD   . LYS   A 1 195 ? 40.663 36.860  18.956 1.00 13.85 ? 195  LYS   A CD   1 
ATOM   2985  C  CE   . LYS   A 1 195 ? 40.008 37.695  17.877 1.00 15.19 ? 195  LYS   A CE   1 
ATOM   2986  N  NZ   . LYS   A 1 195 ? 40.875 37.820  16.682 1.00 14.99 ? 195  LYS   A NZ   1 
ATOM   2987  H  H    . LYS   A 1 195 ? 41.587 32.400  18.686 1.00 15.87 ? 195  LYS   A H    1 
ATOM   2988  H  HA   . LYS   A 1 195 ? 43.543 34.218  18.064 1.00 17.33 ? 195  LYS   A HA   1 
ATOM   2989  H  HB2  . LYS   A 1 195 ? 41.566 34.379  20.073 1.00 14.99 ? 195  LYS   A HB2  1 
ATOM   2990  H  HB3  . LYS   A 1 195 ? 42.660 35.473  19.877 1.00 14.99 ? 195  LYS   A HB3  1 
ATOM   2991  H  HG2  . LYS   A 1 195 ? 41.704 35.724  17.612 1.00 13.46 ? 195  LYS   A HG2  1 
ATOM   2992  H  HG3  . LYS   A 1 195 ? 40.468 34.973  18.195 1.00 13.46 ? 195  LYS   A HG3  1 
ATOM   2993  H  HD2  . LYS   A 1 195 ? 40.017 36.678  19.656 1.00 16.63 ? 195  LYS   A HD2  1 
ATOM   2994  H  HD3  . LYS   A 1 195 ? 41.383 37.368  19.361 1.00 16.63 ? 195  LYS   A HD3  1 
ATOM   2995  H  HE2  . LYS   A 1 195 ? 39.163 37.292  17.624 1.00 18.23 ? 195  LYS   A HE2  1 
ATOM   2996  H  HE3  . LYS   A 1 195 ? 39.808 38.578  18.226 1.00 18.23 ? 195  LYS   A HE3  1 
ATOM   2997  H  HZ1  . LYS   A 1 195 ? 40.627 38.532  16.208 1.00 17.99 ? 195  LYS   A HZ1  1 
ATOM   2998  H  HZ2  . LYS   A 1 195 ? 41.722 37.915  16.938 1.00 17.99 ? 195  LYS   A HZ2  1 
ATOM   2999  H  HZ3  . LYS   A 1 195 ? 40.797 37.089  16.181 1.00 17.99 ? 195  LYS   A HZ3  1 
ATOM   3000  N  N    . ASN   A 1 196 ? 44.046 31.894  19.948 1.00 14.53 ? 196  ASN   A N    1 
ATOM   3001  C  CA   . ASN   A 1 196 ? 44.909 31.259  20.978 1.00 13.96 ? 196  ASN   A CA   1 
ATOM   3002  C  C    . ASN   A 1 196 ? 44.456 31.707  22.371 1.00 16.03 ? 196  ASN   A C    1 
ATOM   3003  O  O    . ASN   A 1 196 ? 45.303 31.757  23.274 1.00 14.72 ? 196  ASN   A O    1 
ATOM   3004  C  CB   . ASN   A 1 196 ? 46.390 31.559  20.741 1.00 14.45 ? 196  ASN   A CB   1 
ATOM   3005  C  CG   . ASN   A 1 196 ? 47.112 30.405  20.080 1.00 19.39 ? 196  ASN   A CG   1 
ATOM   3006  O  OD1  . ASN   A 1 196 ? 46.710 29.254  20.225 1.00 17.85 ? 196  ASN   A OD1  1 
ATOM   3007  N  ND2  . ASN   A 1 196 ? 48.169 30.704  19.343 1.00 18.41 ? 196  ASN   A ND2  1 
ATOM   3008  H  H    . ASN   A 1 196 ? 43.586 31.344  19.474 1.00 17.43 ? 196  ASN   A H    1 
ATOM   3009  H  HA   . ASN   A 1 196 ? 44.812 30.296  20.913 1.00 16.75 ? 196  ASN   A HA   1 
ATOM   3010  H  HB2  . ASN   A 1 196 ? 46.473 32.350  20.186 1.00 17.35 ? 196  ASN   A HB2  1 
ATOM   3011  H  HB3  . ASN   A 1 196 ? 46.816 31.762  21.588 1.00 17.35 ? 196  ASN   A HB3  1 
ATOM   3012  H  HD21 . ASN   A 1 196 ? 48.604 30.080  18.942 1.00 22.09 ? 196  ASN   A HD21 1 
ATOM   3013  H  HD22 . ASN   A 1 196 ? 48.421 31.523  19.265 1.00 22.09 ? 196  ASN   A HD22 1 
ATOM   3014  N  N    . LEU   A 1 197 ? 43.167 32.015  22.527 1.00 14.09 ? 197  LEU   A N    1 
ATOM   3015  C  CA   . LEU   A 1 197 ? 42.628 32.421  23.853 1.00 13.03 ? 197  LEU   A CA   1 
ATOM   3016  C  C    . LEU   A 1 197 ? 41.872 31.237  24.466 1.00 13.50 ? 197  LEU   A C    1 
ATOM   3017  O  O    . LEU   A 1 197 ? 40.833 30.853  23.911 1.00 12.66 ? 197  LEU   A O    1 
ATOM   3018  C  CB   . LEU   A 1 197 ? 41.728 33.652  23.710 1.00 14.99 ? 197  LEU   A CB   1 
ATOM   3019  C  CG   . LEU   A 1 197 ? 41.192 34.234  25.016 1.00 11.27 ? 197  LEU   A CG   1 
ATOM   3020  C  CD1  . LEU   A 1 197 ? 42.332 34.628  25.942 1.00 12.43 ? 197  LEU   A CD1  1 
ATOM   3021  C  CD2  . LEU   A 1 197 ? 40.292 35.428  24.741 1.00 14.65 ? 197  LEU   A CD2  1 
ATOM   3022  H  H    . LEU   A 1 197 ? 42.586 31.999  21.893 1.00 16.91 ? 197  LEU   A H    1 
ATOM   3023  H  HA   . LEU   A 1 197 ? 43.356 32.666  24.445 1.00 15.64 ? 197  LEU   A HA   1 
ATOM   3024  H  HB2  . LEU   A 1 197 ? 42.225 34.344  23.246 1.00 17.99 ? 197  LEU   A HB2  1 
ATOM   3025  H  HB3  . LEU   A 1 197 ? 40.974 33.418  23.146 1.00 17.99 ? 197  LEU   A HB3  1 
ATOM   3026  H  HG   . LEU   A 1 197 ? 40.666 33.549  25.457 1.00 13.53 ? 197  LEU   A HG   1 
ATOM   3027  H  HD11 . LEU   A 1 197 ? 41.970 34.995  26.764 1.00 14.92 ? 197  LEU   A HD11 1 
ATOM   3028  H  HD12 . LEU   A 1 197 ? 42.868 33.846  26.146 1.00 14.92 ? 197  LEU   A HD12 1 
ATOM   3029  H  HD13 . LEU   A 1 197 ? 42.886 35.295  25.508 1.00 14.92 ? 197  LEU   A HD13 1 
ATOM   3030  H  HD21 . LEU   A 1 197 ? 39.961 35.784  25.580 1.00 17.58 ? 197  LEU   A HD21 1 
ATOM   3031  H  HD22 . LEU   A 1 197 ? 40.797 36.113  24.276 1.00 17.58 ? 197  LEU   A HD22 1 
ATOM   3032  H  HD23 . LEU   A 1 197 ? 39.543 35.149  24.191 1.00 17.58 ? 197  LEU   A HD23 1 
ATOM   3033  N  N    . LYS   A 1 198 ? 42.394 30.700  25.571 1.00 11.88 ? 198  LYS   A N    1 
ATOM   3034  C  CA   . LYS   A 1 198 ? 41.780 29.513  26.217 1.00 12.69 ? 198  LYS   A CA   1 
ATOM   3035  C  C    . LYS   A 1 198 ? 40.717 29.941  27.227 1.00 11.84 ? 198  LYS   A C    1 
ATOM   3036  O  O    . LYS   A 1 198 ? 39.719 29.224  27.363 1.00 12.08 ? 198  LYS   A O    1 
ATOM   3037  C  CB   . LYS   A 1 198 ? 42.868 28.737  26.966 1.00 13.31 ? 198  LYS   A CB   1 
ATOM   3038  C  CG   . LYS   A 1 198 ? 42.375 27.587  27.834 1.00 11.38 ? 198  LYS   A CG   1 
ATOM   3039  C  CD   . LYS   A 1 198 ? 41.672 26.500  27.049 1.00 12.31 ? 198  LYS   A CD   1 
ATOM   3040  C  CE   . LYS   A 1 198 ? 41.481 25.231  27.851 1.00 11.12 ? 198  LYS   A CE   1 
ATOM   3041  N  NZ   . LYS   A 1 198 ? 40.550 24.292  27.183 1.00 13.73 ? 198  LYS   A NZ   1 
ATOM   3042  H  H    . LYS   A 1 198 ? 43.097 30.998  25.966 1.00 14.26 ? 198  LYS   A H    1 
ATOM   3043  H  HA   . LYS   A 1 198 ? 41.370 28.963  25.531 1.00 15.24 ? 198  LYS   A HA   1 
ATOM   3044  H  HB2  . LYS   A 1 198 ? 43.497 28.385  26.317 1.00 15.98 ? 198  LYS   A HB2  1 
ATOM   3045  H  HB3  . LYS   A 1 198 ? 43.358 29.358  27.527 1.00 15.98 ? 198  LYS   A HB3  1 
ATOM   3046  H  HG2  . LYS   A 1 198 ? 43.129 27.200  28.305 1.00 13.66 ? 198  LYS   A HG2  1 
ATOM   3047  H  HG3  . LYS   A 1 198 ? 41.769 27.935  28.506 1.00 13.66 ? 198  LYS   A HG3  1 
ATOM   3048  H  HD2  . LYS   A 1 198 ? 40.807 26.826  26.756 1.00 14.78 ? 198  LYS   A HD2  1 
ATOM   3049  H  HD3  . LYS   A 1 198 ? 42.185 26.299  26.251 1.00 14.78 ? 198  LYS   A HD3  1 
ATOM   3050  H  HE2  . LYS   A 1 198 ? 42.339 24.798  27.980 1.00 13.34 ? 198  LYS   A HE2  1 
ATOM   3051  H  HE3  . LYS   A 1 198 ? 41.140 25.453  28.731 1.00 13.34 ? 198  LYS   A HE3  1 
ATOM   3052  H  HZ1  . LYS   A 1 198 ? 40.415 23.585  27.706 1.00 16.47 ? 198  LYS   A HZ1  1 
ATOM   3053  H  HZ2  . LYS   A 1 198 ? 39.774 24.701  27.031 1.00 16.47 ? 198  LYS   A HZ2  1 
ATOM   3054  H  HZ3  . LYS   A 1 198 ? 40.901 24.026  26.410 1.00 16.47 ? 198  LYS   A HZ3  1 
ATOM   3055  N  N    . ALA   A 1 199 ? 40.929 31.073  27.900 1.00 12.46 ? 199  ALA   A N    1 
ATOM   3056  C  CA   . ALA   A 1 199 ? 39.979 31.430  28.973 1.00 11.10 ? 199  ALA   A CA   1 
ATOM   3057  C  C    . ALA   A 1 199 ? 40.098 32.884  29.426 1.00 12.71 ? 199  ALA   A C    1 
ATOM   3058  O  O    . ALA   A 1 199 ? 41.134 33.510  29.162 1.00 12.33 ? 199  ALA   A O    1 
ATOM   3059  C  CB   . ALA   A 1 199 ? 40.217 30.514  30.152 1.00 14.94 ? 199  ALA   A CB   1 
ATOM   3060  H  H    . ALA   A 1 199 ? 41.576 31.624  27.767 1.00 14.96 ? 199  ALA   A H    1 
ATOM   3061  H  HA   . ALA   A 1 199 ? 39.083 31.324  28.616 1.00 13.33 ? 199  ALA   A HA   1 
ATOM   3062  H  HB1  . ALA   A 1 199 ? 39.599 30.737  30.866 1.00 17.93 ? 199  ALA   A HB1  1 
ATOM   3063  H  HB2  . ALA   A 1 199 ? 40.077 29.593  29.880 1.00 17.93 ? 199  ALA   A HB2  1 
ATOM   3064  H  HB3  . ALA   A 1 199 ? 41.128 30.623  30.468 1.00 17.93 ? 199  ALA   A HB3  1 
ATOM   3065  N  N    . ILE   A 1 200 ? 39.038 33.387  30.052 1.00 11.53 ? 200  ILE   A N    1 
ATOM   3066  C  CA   . ILE   A 1 200 ? 39.081 34.734  30.675 1.00 12.09 ? 200  ILE   A CA   1 
ATOM   3067  C  C    . ILE   A 1 200 ? 38.509 34.544  32.082 1.00 14.63 ? 200  ILE   A C    1 
ATOM   3068  O  O    . ILE   A 1 200 ? 37.362 34.088  32.194 1.00 13.47 ? 200  ILE   A O    1 
ATOM   3069  C  CB   . ILE   A 1 200 ? 38.278 35.765  29.860 1.00 11.02 ? 200  ILE   A CB   1 
ATOM   3070  C  CG1  . ILE   A 1 200 ? 38.661 35.742  28.379 1.00 13.74 ? 200  ILE   A CG1  1 
ATOM   3071  C  CG2  . ILE   A 1 200 ? 38.431 37.154  30.460 1.00 10.60 ? 200  ILE   A CG2  1 
ATOM   3072  C  CD1  . ILE   A 1 200 ? 37.986 36.816  27.562 1.00 14.84 ? 200  ILE   A CD1  1 
ATOM   3073  H  H    . ILE   A 1 200 ? 38.286 32.978  30.133 1.00 13.84 ? 200  ILE   A H    1 
ATOM   3074  H  HA   . ILE   A 1 200 ? 39.984 35.088  30.704 1.00 14.51 ? 200  ILE   A HA   1 
ATOM   3075  H  HB   . ILE   A 1 200 ? 37.341 35.519  29.908 1.00 13.23 ? 200  ILE   A HB   1 
ATOM   3076  H  HG12 . ILE   A 1 200 ? 39.623 35.843  28.300 1.00 16.49 ? 200  ILE   A HG12 1 
ATOM   3077  H  HG13 . ILE   A 1 200 ? 38.435 34.875  28.008 1.00 16.49 ? 200  ILE   A HG13 1 
ATOM   3078  H  HG21 . ILE   A 1 200 ? 37.920 37.791  29.936 1.00 12.73 ? 200  ILE   A HG21 1 
ATOM   3079  H  HG22 . ILE   A 1 200 ? 38.103 37.150  31.373 1.00 12.73 ? 200  ILE   A HG22 1 
ATOM   3080  H  HG23 . ILE   A 1 200 ? 39.367 37.408  30.454 1.00 12.73 ? 200  ILE   A HG23 1 
ATOM   3081  H  HD11 . ILE   A 1 200 ? 38.270 36.746  26.637 1.00 17.81 ? 200  ILE   A HD11 1 
ATOM   3082  H  HD12 . ILE   A 1 200 ? 37.024 36.705  27.613 1.00 17.81 ? 200  ILE   A HD12 1 
ATOM   3083  H  HD13 . ILE   A 1 200 ? 38.229 37.688  27.910 1.00 17.81 ? 200  ILE   A HD13 1 
ATOM   3084  N  N    . THR   A 1 201 ? 39.306 34.827  33.114 1.00 14.32 ? 201  THR   A N    1 
ATOM   3085  C  CA   . THR   A 1 201 ? 38.778 34.758  34.499 1.00 12.94 ? 201  THR   A CA   1 
ATOM   3086  C  C    . THR   A 1 201 ? 38.405 36.177  34.936 1.00 15.14 ? 201  THR   A C    1 
ATOM   3087  O  O    . THR   A 1 201 ? 39.069 37.124  34.481 1.00 13.32 ? 201  THR   A O    1 
ATOM   3088  C  CB   . THR   A 1 201 ? 39.778 34.079  35.444 1.00 15.57 ? 201  THR   A CB   1 
ATOM   3089  O  OG1  . THR   A 1 201 ? 40.792 35.026  35.782 1.00 15.14 ? 201  THR   A OG1  1 
ATOM   3090  C  CG2  . THR   A 1 201 ? 40.409 32.845  34.839 1.00 15.63 ? 201  THR   A CG2  1 
ATOM   3091  H  H    . THR   A 1 201 ? 40.132 35.055  33.048 1.00 17.19 ? 201  THR   A H    1 
ATOM   3092  H  HA   . THR   A 1 201 ? 37.982 34.205  34.532 1.00 15.53 ? 201  THR   A HA   1 
ATOM   3093  H  HB   . THR   A 1 201 ? 39.296 33.786  36.233 1.00 18.69 ? 201  THR   A HB   1 
ATOM   3094  H  HG1  . THR   A 1 201 ? 40.555 35.460  36.461 1.00 18.17 ? 201  THR   A HG1  1 
ATOM   3095  H  HG21 . THR   A 1 201 ? 41.030 32.455  35.473 1.00 18.76 ? 201  THR   A HG21 1 
ATOM   3096  H  HG22 . THR   A 1 201 ? 39.717 32.199  34.626 1.00 18.76 ? 201  THR   A HG22 1 
ATOM   3097  H  HG23 . THR   A 1 201 ? 40.885 33.088  34.029 1.00 18.76 ? 201  THR   A HG23 1 
ATOM   3098  N  N    . VAL   A 1 202 ? 37.365 36.304  35.758 1.00 12.65 ? 202  VAL   A N    1 
ATOM   3099  C  CA   . VAL   A 1 202 ? 36.917 37.670  36.142 1.00 13.20 ? 202  VAL   A CA   1 
ATOM   3100  C  C    . VAL   A 1 202 ? 36.392 37.697  37.580 1.00 13.78 ? 202  VAL   A C    1 
ATOM   3101  O  O    . VAL   A 1 202 ? 35.615 36.808  37.953 1.00 13.97 ? 202  VAL   A O    1 
ATOM   3102  C  CB   . VAL   A 1 202 ? 35.883 38.235  35.147 1.00 14.13 ? 202  VAL   A CB   1 
ATOM   3103  C  CG1  . VAL   A 1 202 ? 34.551 37.508  35.225 1.00 12.41 ? 202  VAL   A CG1  1 
ATOM   3104  C  CG2  . VAL   A 1 202 ? 35.696 39.732  35.334 1.00 15.63 ? 202  VAL   A CG2  1 
ATOM   3105  H  H    . VAL   A 1 202 ? 36.916 35.654  36.097 1.00 15.19 ? 202  VAL   A H    1 
ATOM   3106  H  HA   . VAL   A 1 202 ? 37.692 38.251  36.103 1.00 15.85 ? 202  VAL   A HA   1 
ATOM   3107  H  HB   . VAL   A 1 202 ? 36.240 38.083  34.258 1.00 16.95 ? 202  VAL   A HB   1 
ATOM   3108  H  HG11 . VAL   A 1 202 ? 33.933 37.895  34.585 1.00 14.90 ? 202  VAL   A HG11 1 
ATOM   3109  H  HG12 . VAL   A 1 202 ? 34.682 36.569  35.021 1.00 14.90 ? 202  VAL   A HG12 1 
ATOM   3110  H  HG13 . VAL   A 1 202 ? 34.186 37.596  36.119 1.00 14.90 ? 202  VAL   A HG13 1 
ATOM   3111  H  HG21 . VAL   A 1 202 ? 35.042 40.059  34.697 1.00 18.75 ? 202  VAL   A HG21 1 
ATOM   3112  H  HG22 . VAL   A 1 202 ? 35.385 39.909  36.235 1.00 18.75 ? 202  VAL   A HG22 1 
ATOM   3113  H  HG23 . VAL   A 1 202 ? 36.542 40.184  35.189 1.00 18.75 ? 202  VAL   A HG23 1 
ATOM   3114  N  N    . LYS   A 1 203 ? 36.862 38.669  38.364 1.00 11.61 ? 203  LYS   A N    1 
ATOM   3115  C  CA   . LYS   A 1 203 ? 36.336 38.880  39.733 1.00 13.55 ? 203  LYS   A CA   1 
ATOM   3116  C  C    . LYS   A 1 203 ? 35.967 40.362  39.835 1.00 13.36 ? 203  LYS   A C    1 
ATOM   3117  O  O    . LYS   A 1 203 ? 36.829 41.197  39.528 1.00 15.83 ? 203  LYS   A O    1 
ATOM   3118  C  CB   . LYS   A 1 203 ? 37.382 38.511  40.788 1.00 14.51 ? 203  LYS   A CB   1 
ATOM   3119  C  CG   . LYS   A 1 203 ? 37.008 38.891  42.215 1.00 18.28 ? 203  LYS   A CG   1 
ATOM   3120  C  CD   . LYS   A 1 203 ? 37.892 38.256  43.264 1.00 19.03 ? 203  LYS   A CD   1 
ATOM   3121  C  CE   . LYS   A 1 203 ? 37.480 38.619  44.675 1.00 17.06 ? 203  LYS   A CE   1 
ATOM   3122  N  NZ   . LYS   A 1 203 ? 38.318 37.931  45.684 1.00 21.16 ? 203  LYS   A NZ   1 
ATOM   3123  H  H    . LYS   A 1 203 ? 37.482 39.218  38.131 1.00 13.93 ? 203  LYS   A H    1 
ATOM   3124  H  HA   . LYS   A 1 203 ? 35.565 38.314  39.896 1.00 16.26 ? 203  LYS   A HA   1 
ATOM   3125  H  HB2  . LYS   A 1 203 ? 37.537 37.554  40.751 1.00 17.42 ? 203  LYS   A HB2  1 
ATOM   3126  H  HB3  . LYS   A 1 203 ? 38.220 38.943  40.560 1.00 17.42 ? 203  LYS   A HB3  1 
ATOM   3127  H  HG2  . LYS   A 1 203 ? 37.053 39.856  42.307 1.00 21.94 ? 203  LYS   A HG2  1 
ATOM   3128  H  HG3  . LYS   A 1 203 ? 36.088 38.633  42.379 1.00 21.94 ? 203  LYS   A HG3  1 
ATOM   3129  H  HD2  . LYS   A 1 203 ? 37.867 37.292  43.162 1.00 22.84 ? 203  LYS   A HD2  1 
ATOM   3130  H  HD3  . LYS   A 1 203 ? 38.810 38.533  43.118 1.00 22.84 ? 203  LYS   A HD3  1 
ATOM   3131  H  HE2  . LYS   A 1 203 ? 37.550 39.579  44.796 1.00 20.47 ? 203  LYS   A HE2  1 
ATOM   3132  H  HE3  . LYS   A 1 203 ? 36.549 38.383  44.812 1.00 20.47 ? 203  LYS   A HE3  1 
ATOM   3133  H  HZ1  . LYS   A 1 203 ? 38.024 38.130  46.500 1.00 25.40 ? 203  LYS   A HZ1  1 
ATOM   3134  H  HZ2  . LYS   A 1 203 ? 38.271 37.051  45.559 1.00 25.40 ? 203  LYS   A HZ2  1 
ATOM   3135  H  HZ3  . LYS   A 1 203 ? 39.163 38.198  45.600 1.00 25.40 ? 203  LYS   A HZ3  1 
ATOM   3136  N  N    . GLY   A 1 204 ? 34.733 40.662  40.234 1.00 15.01 ? 204  GLY   A N    1 
ATOM   3137  C  CA   . GLY   A 1 204 ? 34.283 42.058  40.379 1.00 17.31 ? 204  GLY   A CA   1 
ATOM   3138  C  C    . GLY   A 1 204 ? 33.864 42.352  41.808 1.00 16.55 ? 204  GLY   A C    1 
ATOM   3139  O  O    . GLY   A 1 204 ? 33.096 41.558  42.370 1.00 16.12 ? 204  GLY   A O    1 
ATOM   3140  H  H    . GLY   A 1 204 ? 34.135 40.075  40.428 1.00 18.02 ? 204  GLY   A H    1 
ATOM   3141  H  HA2  . GLY   A 1 204 ? 34.998 42.660  40.118 1.00 20.78 ? 204  GLY   A HA2  1 
ATOM   3142  H  HA3  . GLY   A 1 204 ? 33.539 42.225  39.780 1.00 20.78 ? 204  GLY   A HA3  1 
ATOM   3143  N  N    . THR   A 1 205 ? 34.364 43.452  42.377 1.00 18.64 ? 205  THR   A N    1 
ATOM   3144  C  CA   . THR   A 1 205 ? 34.048 43.794  43.787 1.00 21.58 ? 205  THR   A CA   1 
ATOM   3145  C  C    . THR   A 1 205 ? 33.113 45.004  43.827 1.00 21.73 ? 205  THR   A C    1 
ATOM   3146  O  O    . THR   A 1 205 ? 32.693 45.380  44.930 1.00 23.13 ? 205  THR   A O    1 
ATOM   3147  C  CB   . THR   A 1 205 ? 35.329 44.064  44.587 1.00 21.97 ? 205  THR   A CB   1 
ATOM   3148  O  OG1  . THR   A 1 205 ? 35.935 45.251  44.079 1.00 20.35 ? 205  THR   A OG1  1 
ATOM   3149  C  CG2  . THR   A 1 205 ? 36.309 42.913  44.529 1.00 24.51 ? 205  THR   A CG2  1 
ATOM   3150  H  H    . THR   A 1 205 ? 34.881 44.011  41.978 1.00 22.37 ? 205  THR   A H    1 
ATOM   3151  H  HA   . THR   A 1 205 ? 33.600 43.039  44.199 1.00 25.90 ? 205  THR   A HA   1 
ATOM   3152  H  HB   . THR   A 1 205 ? 35.087 44.171  45.520 1.00 26.37 ? 205  THR   A HB   1 
ATOM   3153  H  HG1  . THR   A 1 205 ? 36.712 45.077  43.812 1.00 24.43 ? 205  THR   A HG1  1 
ATOM   3154  H  HG21 . THR   A 1 205 ? 37.098 43.133  45.048 1.00 29.41 ? 205  THR   A HG21 1 
ATOM   3155  H  HG22 . THR   A 1 205 ? 35.894 42.116  44.894 1.00 29.41 ? 205  THR   A HG22 1 
ATOM   3156  H  HG23 . THR   A 1 205 ? 36.564 42.751  43.607 1.00 29.41 ? 205  THR   A HG23 1 
ATOM   3157  N  N    . GLY   A 1 206 ? 32.775 45.556  42.663 1.00 20.24 ? 206  GLY   A N    1 
ATOM   3158  C  CA   . GLY   A 1 206 ? 31.960 46.780  42.624 1.00 22.79 ? 206  GLY   A CA   1 
ATOM   3159  C  C    . GLY   A 1 206 ? 30.468 46.522  42.587 1.00 21.77 ? 206  GLY   A C    1 
ATOM   3160  O  O    . GLY   A 1 206 ? 30.056 45.358  42.725 1.00 21.83 ? 206  GLY   A O    1 
ATOM   3161  H  H    . GLY   A 1 206 ? 33.001 45.247  41.893 1.00 24.30 ? 206  GLY   A H    1 
ATOM   3162  H  HA2  . GLY   A 1 206 ? 32.167 47.321  43.402 1.00 27.35 ? 206  GLY   A HA2  1 
ATOM   3163  H  HA3  . GLY   A 1 206 ? 32.209 47.299  41.844 1.00 27.35 ? 206  GLY   A HA3  1 
ATOM   3164  N  N    . LYS   A 1 207 ? 29.694 47.595  42.454 1.00 22.57 ? 207  LYS   A N    1 
ATOM   3165  C  CA   . LYS   A 1 207 ? 28.219 47.480  42.376 1.00 24.87 ? 207  LYS   A CA   1 
ATOM   3166  C  C    . LYS   A 1 207 ? 27.787 48.247  41.128 1.00 26.16 ? 207  LYS   A C    1 
ATOM   3167  O  O    . LYS   A 1 207 ? 28.522 49.153  40.712 1.00 26.04 ? 207  LYS   A O    1 
ATOM   3168  C  CB   . LYS   A 1 207 ? 27.568 48.078  43.625 1.00 34.56 ? 207  LYS   A CB   1 
ATOM   3169  C  CG   . LYS   A 1 207 ? 27.778 49.573  43.819 1.00 49.57 ? 207  LYS   A CG   1 
ATOM   3170  C  CD   . LYS   A 1 207 ? 27.094 50.115  45.055 1.00 57.07 ? 207  LYS   A CD   1 
ATOM   3171  C  CE   . LYS   A 1 207 ? 27.306 51.602  45.244 1.00 58.42 ? 207  LYS   A CE   1 
ATOM   3172  N  NZ   . LYS   A 1 207 ? 26.625 52.106  46.461 1.00 62.39 ? 207  LYS   A NZ   1 
ATOM   3173  H  H    . LYS   A 1 207 ? 29.992 48.400  42.406 1.00 27.09 ? 207  LYS   A H    1 
ATOM   3174  H  HA   . LYS   A 1 207 ? 27.944 46.551  42.326 1.00 29.85 ? 207  LYS   A HA   1 
ATOM   3175  H  HB2  . LYS   A 1 207 ? 26.615 47.903  43.590 1.00 41.48 ? 207  LYS   A HB2  1 
ATOM   3176  H  HB3  . LYS   A 1 207 ? 27.913 47.615  44.404 1.00 41.48 ? 207  LYS   A HB3  1 
ATOM   3177  H  HG2  . LYS   A 1 207 ? 28.729 49.755  43.876 1.00 59.49 ? 207  LYS   A HG2  1 
ATOM   3178  H  HG3  . LYS   A 1 207 ? 27.445 50.044  43.039 1.00 59.49 ? 207  LYS   A HG3  1 
ATOM   3179  H  HD2  . LYS   A 1 207 ? 26.143 49.934  44.998 1.00 68.48 ? 207  LYS   A HD2  1 
ATOM   3180  H  HD3  . LYS   A 1 207 ? 27.426 49.644  45.835 1.00 68.48 ? 207  LYS   A HD3  1 
ATOM   3181  H  HE2  . LYS   A 1 207 ? 28.256 51.788  45.305 1.00 70.11 ? 207  LYS   A HE2  1 
ATOM   3182  H  HE3  . LYS   A 1 207 ? 26.973 52.077  44.467 1.00 70.11 ? 207  LYS   A HE3  1 
ATOM   3183  H  HZ1  . LYS   A 1 207 ? 26.770 52.980  46.542 1.00 74.87 ? 207  LYS   A HZ1  1 
ATOM   3184  H  HZ2  . LYS   A 1 207 ? 25.750 51.955  46.396 1.00 74.87 ? 207  LYS   A HZ2  1 
ATOM   3185  H  HZ3  . LYS   A 1 207 ? 26.946 51.685  47.177 1.00 74.87 ? 207  LYS   A HZ3  1 
ATOM   3186  N  N    . ILE   A 1 208 ? 26.643 47.884  40.562 1.00 20.07 ? 208  ILE   A N    1 
ATOM   3187  C  CA   . ILE   A 1 208 ? 26.130 48.633  39.384 1.00 21.99 ? 208  ILE   A CA   1 
ATOM   3188  C  C    . ILE   A 1 208 ? 25.495 49.926  39.907 1.00 20.74 ? 208  ILE   A C    1 
ATOM   3189  O  O    . ILE   A 1 208 ? 24.689 49.846  40.845 1.00 19.86 ? 208  ILE   A O    1 
ATOM   3190  C  CB   . ILE   A 1 208 ? 25.144 47.770  38.568 1.00 18.71 ? 208  ILE   A CB   1 
ATOM   3191  C  CG1  . ILE   A 1 208 ? 25.873 46.795  37.640 1.00 18.49 ? 208  ILE   A CG1  1 
ATOM   3192  C  CG2  . ILE   A 1 208 ? 24.172 48.647  37.796 1.00 18.38 ? 208  ILE   A CG2  1 
ATOM   3193  C  CD1  . ILE   A 1 208 ? 26.709 45.755  38.351 1.00 16.13 ? 208  ILE   A CD1  1 
ATOM   3194  H  H    . ILE   A 1 208 ? 26.151 47.229  40.824 1.00 24.09 ? 208  ILE   A H    1 
ATOM   3195  H  HA   . ILE   A 1 208 ? 26.848 48.855  38.771 1.00 26.39 ? 208  ILE   A HA   1 
ATOM   3196  H  HB   . ILE   A 1 208 ? 24.634 47.235  39.196 1.00 22.45 ? 208  ILE   A HB   1 
ATOM   3197  H  HG12 . ILE   A 1 208 ? 25.218 46.343  37.086 1.00 22.19 ? 208  ILE   A HG12 1 
ATOM   3198  H  HG13 . ILE   A 1 208 ? 26.447 47.302  37.044 1.00 22.19 ? 208  ILE   A HG13 1 
ATOM   3199  H  HG21 . ILE   A 1 208 ? 23.562 48.087  37.291 1.00 22.06 ? 208  ILE   A HG21 1 
ATOM   3200  H  HG22 . ILE   A 1 208 ? 23.668 49.196  38.417 1.00 22.06 ? 208  ILE   A HG22 1 
ATOM   3201  H  HG23 . ILE   A 1 208 ? 24.665 49.219  37.187 1.00 22.06 ? 208  ILE   A HG23 1 
ATOM   3202  H  HD11 . ILE   A 1 208 ? 27.135 45.180  37.697 1.00 19.36 ? 208  ILE   A HD11 1 
ATOM   3203  H  HD12 . ILE   A 1 208 ? 27.388 46.196  38.885 1.00 19.36 ? 208  ILE   A HD12 1 
ATOM   3204  H  HD13 . ILE   A 1 208 ? 26.140 45.222  38.928 1.00 19.36 ? 208  ILE   A HD13 1 
ATOM   3205  N  N    . ALA   A 1 209 ? 25.881 51.065  39.332 1.00 22.06 ? 209  ALA   A N    1 
ATOM   3206  C  CA   . ALA   A 1 209 ? 25.341 52.365  39.790 1.00 23.23 ? 209  ALA   A CA   1 
ATOM   3207  C  C    . ALA   A 1 209 ? 23.872 52.486  39.377 1.00 22.16 ? 209  ALA   A C    1 
ATOM   3208  O  O    . ALA   A 1 209 ? 23.571 52.258  38.199 1.00 23.00 ? 209  ALA   A O    1 
ATOM   3209  C  CB   . ALA   A 1 209 ? 26.161 53.502  39.232 1.00 24.73 ? 209  ALA   A CB   1 
ATOM   3210  H  H    . ALA   A 1 209 ? 26.445 51.116  38.685 1.00 26.48 ? 209  ALA   A H    1 
ATOM   3211  H  HA   . ALA   A 1 209 ? 25.393 52.411  40.757 1.00 27.88 ? 209  ALA   A HA   1 
ATOM   3212  H  HB1  . ALA   A 1 209 ? 25.796 54.346  39.540 1.00 29.68 ? 209  ALA   A HB1  1 
ATOM   3213  H  HB2  . ALA   A 1 209 ? 27.079 53.418  39.534 1.00 29.68 ? 209  ALA   A HB2  1 
ATOM   3214  H  HB3  . ALA   A 1 209 ? 26.136 53.474  38.263 1.00 29.68 ? 209  ALA   A HB3  1 
ATOM   3215  N  N    . LEU   A 1 210 ? 23.010 52.843  40.330 1.00 21.11 ? 210  LEU   A N    1 
ATOM   3216  C  CA   . LEU   A 1 210 ? 21.563 53.010  40.041 1.00 26.86 ? 210  LEU   A CA   1 
ATOM   3217  C  C    . LEU   A 1 210 ? 21.191 54.492  40.164 1.00 26.18 ? 210  LEU   A C    1 
ATOM   3218  O  O    . LEU   A 1 210 ? 21.559 55.106  41.175 1.00 24.04 ? 210  LEU   A O    1 
ATOM   3219  C  CB   . LEU   A 1 210 ? 20.768 52.160  41.033 1.00 22.94 ? 210  LEU   A CB   1 
ATOM   3220  C  CG   . LEU   A 1 210 ? 21.197 50.699  41.134 1.00 23.35 ? 210  LEU   A CG   1 
ATOM   3221  C  CD1  . LEU   A 1 210 ? 20.444 49.994  42.249 1.00 24.67 ? 210  LEU   A CD1  1 
ATOM   3222  C  CD2  . LEU   A 1 210 ? 20.987 49.981  39.809 1.00 18.99 ? 210  LEU   A CD2  1 
ATOM   3223  H  H    . LEU   A 1 210 ? 23.231 52.994  41.147 1.00 25.34 ? 210  LEU   A H    1 
ATOM   3224  H  HA   . LEU   A 1 210 ? 21.356 52.719  39.139 1.00 32.23 ? 210  LEU   A HA   1 
ATOM   3225  H  HB2  . LEU   A 1 210 ? 20.840 52.564  41.912 1.00 27.53 ? 210  LEU   A HB2  1 
ATOM   3226  H  HB3  . LEU   A 1 210 ? 19.831 52.190  40.783 1.00 27.53 ? 210  LEU   A HB3  1 
ATOM   3227  H  HG   . LEU   A 1 210 ? 22.144 50.677  41.344 1.00 28.02 ? 210  LEU   A HG   1 
ATOM   3228  H  HD11 . LEU   A 1 210 ? 20.730 49.068  42.298 1.00 29.61 ? 210  LEU   A HD11 1 
ATOM   3229  H  HD12 . LEU   A 1 210 ? 20.629 50.434  43.093 1.00 29.61 ? 210  LEU   A HD12 1 
ATOM   3230  H  HD13 . LEU   A 1 210 ? 19.491 50.029  42.069 1.00 29.61 ? 210  LEU   A HD13 1 
ATOM   3231  H  HD21 . LEU   A 1 210 ? 21.265 49.056  39.894 1.00 22.79 ? 210  LEU   A HD21 1 
ATOM   3232  H  HD22 . LEU   A 1 210 ? 20.048 50.015  39.568 1.00 22.79 ? 210  LEU   A HD22 1 
ATOM   3233  H  HD23 . LEU   A 1 210 ? 21.514 50.414  39.119 1.00 22.79 ? 210  LEU   A HD23 1 
ATOM   3234  N  N    . ALA   A 1 211 ? 20.489 55.027  39.165 1.00 25.28 ? 211  ALA   A N    1 
ATOM   3235  C  CA   . ALA   A 1 211 ? 20.050 56.439  39.203 1.00 28.16 ? 211  ALA   A CA   1 
ATOM   3236  C  C    . ALA   A 1 211 ? 19.119 56.662  40.401 1.00 31.05 ? 211  ALA   A C    1 
ATOM   3237  O  O    . ALA   A 1 211 ? 19.114 57.784  40.940 1.00 30.53 ? 211  ALA   A O    1 
ATOM   3238  C  CB   . ALA   A 1 211 ? 19.382 56.793  37.897 1.00 31.04 ? 211  ALA   A CB   1 
ATOM   3239  H  H    . ALA   A 1 211 ? 20.254 54.599  38.457 1.00 30.35 ? 211  ALA   A H    1 
ATOM   3240  H  HA   . ALA   A 1 211 ? 20.816 57.024  39.315 1.00 33.79 ? 211  ALA   A HA   1 
ATOM   3241  H  HB1  . ALA   A 1 211 ? 19.094 57.719  37.921 1.00 37.25 ? 211  ALA   A HB1  1 
ATOM   3242  H  HB2  . ALA   A 1 211 ? 20.010 56.669  37.168 1.00 37.25 ? 211  ALA   A HB2  1 
ATOM   3243  H  HB3  . ALA   A 1 211 ? 18.612 56.219  37.761 1.00 37.25 ? 211  ALA   A HB3  1 
ATOM   3244  N  N    . ASP   A 1 212 ? 18.374 55.633  40.807 1.00 28.01 ? 212  ASP   A N    1 
ATOM   3245  C  CA   . ASP   A 1 212 ? 17.428 55.755  41.945 1.00 32.11 ? 212  ASP   A CA   1 
ATOM   3246  C  C    . ASP   A 1 212 ? 17.269 54.383  42.599 1.00 33.69 ? 212  ASP   A C    1 
ATOM   3247  O  O    . ASP   A 1 212 ? 16.354 53.643  42.202 1.00 31.93 ? 212  ASP   A O    1 
ATOM   3248  C  CB   . ASP   A 1 212 ? 16.100 56.358  41.485 1.00 39.62 ? 212  ASP   A CB   1 
ATOM   3249  C  CG   . ASP   A 1 212 ? 15.146 56.679  42.622 1.00 40.36 ? 212  ASP   A CG   1 
ATOM   3250  O  OD1  . ASP   A 1 212 ? 15.346 56.142  43.728 1.00 40.29 ? 212  ASP   A OD1  1 
ATOM   3251  O  OD2  . ASP   A 1 212 ? 14.208 57.463  42.385 1.00 44.59 ? 212  ASP   A OD2  1 
ATOM   3252  H  H    . ASP   A 1 212 ? 18.394 54.854  40.444 1.00 33.62 ? 212  ASP   A H    1 
ATOM   3253  H  HA   . ASP   A 1 212 ? 17.778 56.366  42.612 1.00 38.53 ? 212  ASP   A HA   1 
ATOM   3254  H  HB2  . ASP   A 1 212 ? 16.279 57.170  40.985 1.00 47.54 ? 212  ASP   A HB2  1 
ATOM   3255  H  HB3  . ASP   A 1 212 ? 15.667 55.739  40.876 1.00 47.54 ? 212  ASP   A HB3  1 
ATOM   3256  N  N    . LYS   A 1 213 ? 18.123 54.086  43.571 1.00 32.75 ? 213  LYS   A N    1 
ATOM   3257  C  CA   . LYS   A 1 213 ? 18.120 52.768  44.246 1.00 35.36 ? 213  LYS   A CA   1 
ATOM   3258  C  C    . LYS   A 1 213 ? 16.711 52.373  44.697 1.00 33.71 ? 213  LYS   A C    1 
ATOM   3259  O  O    . LYS   A 1 213 ? 16.278 51.262  44.363 1.00 28.76 ? 213  LYS   A O    1 
ATOM   3260  C  CB   . LYS   A 1 213 ? 19.074 52.874  45.438 1.00 37.78 ? 213  LYS   A CB   1 
ATOM   3261  C  CG   . LYS   A 1 213 ? 19.272 51.617  46.267 1.00 50.17 ? 213  LYS   A CG   1 
ATOM   3262  C  CD   . LYS   A 1 213 ? 20.266 51.840  47.382 1.00 61.58 ? 213  LYS   A CD   1 
ATOM   3263  C  CE   . LYS   A 1 213 ? 19.899 51.100  48.651 1.00 60.80 ? 213  LYS   A CE   1 
ATOM   3264  N  NZ   . LYS   A 1 213 ? 20.811 49.959  48.905 1.00 57.03 ? 213  LYS   A NZ   1 
ATOM   3265  H  H    . LYS   A 1 213 ? 18.721 54.631  43.864 1.00 39.31 ? 213  LYS   A H    1 
ATOM   3266  H  HA   . LYS   A 1 213 ? 18.412 52.074  43.635 1.00 42.43 ? 213  LYS   A HA   1 
ATOM   3267  H  HB2  . LYS   A 1 213 ? 19.941 53.159  45.108 1.00 45.34 ? 213  LYS   A HB2  1 
ATOM   3268  H  HB3  . LYS   A 1 213 ? 18.749 53.575  46.024 1.00 45.34 ? 213  LYS   A HB3  1 
ATOM   3269  H  HG2  . LYS   A 1 213 ? 18.422 51.337  46.641 1.00 60.21 ? 213  LYS   A HG2  1 
ATOM   3270  H  HG3  . LYS   A 1 213 ? 19.581 50.897  45.696 1.00 60.21 ? 213  LYS   A HG3  1 
ATOM   3271  H  HD2  . LYS   A 1 213 ? 21.145 51.554  47.088 1.00 73.90 ? 213  LYS   A HD2  1 
ATOM   3272  H  HD3  . LYS   A 1 213 ? 20.326 52.789  47.572 1.00 73.90 ? 213  LYS   A HD3  1 
ATOM   3273  H  HE2  . LYS   A 1 213 ? 19.929 51.712  49.403 1.00 72.96 ? 213  LYS   A HE2  1 
ATOM   3274  H  HE3  . LYS   A 1 213 ? 18.987 50.777  48.585 1.00 72.96 ? 213  LYS   A HE3  1 
ATOM   3275  H  HZ1  . LYS   A 1 213 ? 20.569 49.547  49.656 1.00 68.43 ? 213  LYS   A HZ1  1 
ATOM   3276  H  HZ2  . LYS   A 1 213 ? 20.767 49.387  48.225 1.00 68.43 ? 213  LYS   A HZ2  1 
ATOM   3277  H  HZ3  . LYS   A 1 213 ? 21.645 50.258  48.987 1.00 68.43 ? 213  LYS   A HZ3  1 
ATOM   3278  N  N    . GLU   A 1 214 ? 16.022 53.255  45.421 1.00 34.13 ? 214  GLU   A N    1 
ATOM   3279  C  CA   . GLU   A 1 214 ? 14.706 52.859  45.999 1.00 33.76 ? 214  GLU   A CA   1 
ATOM   3280  C  C    . GLU   A 1 214 ? 13.668 52.655  44.885 1.00 35.15 ? 214  GLU   A C    1 
ATOM   3281  O  O    . GLU   A 1 214 ? 12.841 51.742  45.023 1.00 35.51 ? 214  GLU   A O    1 
ATOM   3282  C  CB   . GLU   A 1 214 ? 14.248 53.875  47.049 1.00 35.84 ? 214  GLU   A CB   1 
ATOM   3283  C  CG   . GLU   A 1 214 ? 15.129 53.901  48.281 1.00 37.22 ? 214  GLU   A CG   1 
ATOM   3284  C  CD   . GLU   A 1 214 ? 16.331 54.823  48.179 1.00 43.28 ? 214  GLU   A CD   1 
ATOM   3285  O  OE1  . GLU   A 1 214 ? 16.431 55.557  47.178 1.00 41.04 ? 214  GLU   A OE1  1 
ATOM   3286  O  OE2  . GLU   A 1 214 ? 17.163 54.803  49.103 1.00 49.17 ? 214  GLU   A OE2  1 
ATOM   3287  H  H    . GLU   A 1 214 ? 16.274 54.059  45.592 1.00 40.95 ? 214  GLU   A H    1 
ATOM   3288  H  HA   . GLU   A 1 214 ? 14.804 52.009  46.455 1.00 40.52 ? 214  GLU   A HA   1 
ATOM   3289  H  HB2  . GLU   A 1 214 ? 14.234 54.759  46.650 1.00 43.01 ? 214  GLU   A HB2  1 
ATOM   3290  H  HB3  . GLU   A 1 214 ? 13.338 53.669  47.314 1.00 43.01 ? 214  GLU   A HB3  1 
ATOM   3291  H  HG2  . GLU   A 1 214 ? 14.592 54.172  49.042 1.00 44.67 ? 214  GLU   A HG2  1 
ATOM   3292  H  HG3  . GLU   A 1 214 ? 15.441 53.000  48.460 1.00 44.67 ? 214  GLU   A HG3  1 
ATOM   3293  N  N    . LYS   A 1 215 ? 13.714 53.465  43.829 1.00 31.68 ? 215  LYS   A N    1 
ATOM   3294  C  CA   . LYS   A 1 215 ? 12.778 53.269  42.694 1.00 31.13 ? 215  LYS   A CA   1 
ATOM   3295  C  C    . LYS   A 1 215 ? 13.085 51.941  41.992 1.00 29.69 ? 215  LYS   A C    1 
ATOM   3296  O  O    . LYS   A 1 215 ? 12.141 51.220  41.625 1.00 27.67 ? 215  LYS   A O    1 
ATOM   3297  C  CB   . LYS   A 1 215 ? 12.901 54.402  41.678 1.00 36.36 ? 215  LYS   A CB   1 
ATOM   3298  C  CG   . LYS   A 1 215 ? 11.835 54.398  40.591 1.00 41.20 ? 215  LYS   A CG   1 
ATOM   3299  C  CD   . LYS   A 1 215 ? 12.348 54.831  39.240 1.00 44.59 ? 215  LYS   A CD   1 
ATOM   3300  C  CE   . LYS   A 1 215 ? 12.564 56.324  39.137 1.00 44.06 ? 215  LYS   A CE   1 
ATOM   3301  N  NZ   . LYS   A 1 215 ? 13.583 56.657  38.114 1.00 47.71 ? 215  LYS   A NZ   1 
ATOM   3302  H  H    . LYS   A 1 215 ? 14.262 54.122  43.740 1.00 38.02 ? 215  LYS   A H    1 
ATOM   3303  H  HA   . LYS   A 1 215 ? 11.875 53.261  43.049 1.00 37.36 ? 215  LYS   A HA   1 
ATOM   3304  H  HB2  . LYS   A 1 215 ? 12.862 55.249  42.149 1.00 43.63 ? 215  LYS   A HB2  1 
ATOM   3305  H  HB3  . LYS   A 1 215 ? 13.774 54.351  41.258 1.00 43.63 ? 215  LYS   A HB3  1 
ATOM   3306  H  HG2  . LYS   A 1 215 ? 11.463 53.505  40.516 1.00 49.44 ? 215  LYS   A HG2  1 
ATOM   3307  H  HG3  . LYS   A 1 215 ? 11.110 54.986  40.857 1.00 49.44 ? 215  LYS   A HG3  1 
ATOM   3308  H  HD2  . LYS   A 1 215 ? 13.185 54.375  39.057 1.00 53.52 ? 215  LYS   A HD2  1 
ATOM   3309  H  HD3  . LYS   A 1 215 ? 11.718 54.553  38.557 1.00 53.52 ? 215  LYS   A HD3  1 
ATOM   3310  H  HE2  . LYS   A 1 215 ? 11.726 56.759  38.914 1.00 52.87 ? 215  LYS   A HE2  1 
ATOM   3311  H  HE3  . LYS   A 1 215 ? 12.843 56.672  39.998 1.00 52.87 ? 215  LYS   A HE3  1 
ATOM   3312  H  HZ1  . LYS   A 1 215 ? 13.762 57.528  38.146 1.00 57.26 ? 215  LYS   A HZ1  1 
ATOM   3313  H  HZ2  . LYS   A 1 215 ? 14.327 56.195  38.274 1.00 57.26 ? 215  LYS   A HZ2  1 
ATOM   3314  H  HZ3  . LYS   A 1 215 ? 13.273 56.448  37.306 1.00 57.26 ? 215  LYS   A HZ3  1 
ATOM   3315  N  N    . VAL   A 1 216 ? 14.369 51.655  41.798 1.00 26.63 ? 216  VAL   A N    1 
ATOM   3316  C  CA   . VAL   A 1 216 ? 14.759 50.386  41.122 1.00 25.71 ? 216  VAL   A CA   1 
ATOM   3317  C  C    . VAL   A 1 216 ? 14.197 49.241  41.967 1.00 25.60 ? 216  VAL   A C    1 
ATOM   3318  O  O    . VAL   A 1 216 ? 13.653 48.285  41.392 1.00 23.22 ? 216  VAL   A O    1 
ATOM   3319  C  CB   . VAL   A 1 216 ? 16.286 50.281  40.958 1.00 22.88 ? 216  VAL   A CB   1 
ATOM   3320  C  CG1  . VAL   A 1 216 ? 16.722 48.864  40.618 1.00 23.89 ? 216  VAL   A CG1  1 
ATOM   3321  C  CG2  . VAL   A 1 216 ? 16.813 51.267  39.930 1.00 24.20 ? 216  VAL   A CG2  1 
ATOM   3322  H  H    . VAL   A 1 216 ? 15.024 52.158  42.038 1.00 31.96 ? 216  VAL   A H    1 
ATOM   3323  H  HA   . VAL   A 1 216 ? 14.396 50.351  40.223 1.00 30.85 ? 216  VAL   A HA   1 
ATOM   3324  H  HB   . VAL   A 1 216 ? 16.674 50.513  41.817 1.00 27.46 ? 216  VAL   A HB   1 
ATOM   3325  H  HG11 . VAL   A 1 216 ? 17.687 48.836  40.523 1.00 28.67 ? 216  VAL   A HG11 1 
ATOM   3326  H  HG12 . VAL   A 1 216 ? 16.450 48.262  41.329 1.00 28.67 ? 216  VAL   A HG12 1 
ATOM   3327  H  HG13 . VAL   A 1 216 ? 16.307 48.589  39.786 1.00 28.67 ? 216  VAL   A HG13 1 
ATOM   3328  H  HG21 . VAL   A 1 216 ? 17.775 51.172  39.854 1.00 29.04 ? 216  VAL   A HG21 1 
ATOM   3329  H  HG22 . VAL   A 1 216 ? 16.402 51.089  39.070 1.00 29.04 ? 216  VAL   A HG22 1 
ATOM   3330  H  HG23 . VAL   A 1 216 ? 16.599 52.171  40.209 1.00 29.04 ? 216  VAL   A HG23 1 
ATOM   3331  N  N    . LYS   A 1 217 ? 14.311 49.364  43.289 1.00 26.29 ? 217  LYS   A N    1 
ATOM   3332  C  CA   . LYS   A 1 217 ? 13.819 48.284  44.186 1.00 27.01 ? 217  LYS   A CA   1 
ATOM   3333  C  C    . LYS   A 1 217 ? 12.304 48.135  44.026 1.00 23.99 ? 217  LYS   A C    1 
ATOM   3334  O  O    . LYS   A 1 217 ? 11.814 46.996  44.029 1.00 23.81 ? 217  LYS   A O    1 
ATOM   3335  C  CB   . LYS   A 1 217 ? 14.164 48.571  45.650 1.00 27.30 ? 217  LYS   A CB   1 
ATOM   3336  C  CG   . LYS   A 1 217 ? 13.512 47.645  46.666 1.00 33.95 ? 217  LYS   A CG   1 
ATOM   3337  C  CD   . LYS   A 1 217 ? 14.286 46.366  46.893 1.00 36.11 ? 217  LYS   A CD   1 
ATOM   3338  C  CE   . LYS   A 1 217 ? 13.450 45.271  47.520 1.00 41.41 ? 217  LYS   A CE   1 
ATOM   3339  N  NZ   . LYS   A 1 217 ? 14.203 44.000  47.631 1.00 47.70 ? 217  LYS   A NZ   1 
ATOM   3340  H  H    . LYS   A 1 217 ? 14.659 50.041  43.690 1.00 31.55 ? 217  LYS   A H    1 
ATOM   3341  H  HA   . LYS   A 1 217 ? 14.259 47.457  43.934 1.00 32.41 ? 217  LYS   A HA   1 
ATOM   3342  H  HB2  . LYS   A 1 217 ? 15.127 48.517  45.756 1.00 32.76 ? 217  LYS   A HB2  1 
ATOM   3343  H  HB3  . LYS   A 1 217 ? 13.907 49.484  45.855 1.00 32.76 ? 217  LYS   A HB3  1 
ATOM   3344  H  HG2  . LYS   A 1 217 ? 13.421 48.114  47.510 1.00 40.74 ? 217  LYS   A HG2  1 
ATOM   3345  H  HG3  . LYS   A 1 217 ? 12.616 47.425  46.365 1.00 40.74 ? 217  LYS   A HG3  1 
ATOM   3346  H  HD2  . LYS   A 1 217 ? 14.638 46.052  46.045 1.00 43.33 ? 217  LYS   A HD2  1 
ATOM   3347  H  HD3  . LYS   A 1 217 ? 15.047 46.552  47.465 1.00 43.33 ? 217  LYS   A HD3  1 
ATOM   3348  H  HE2  . LYS   A 1 217 ? 13.157 45.552  48.401 1.00 49.69 ? 217  LYS   A HE2  1 
ATOM   3349  H  HE3  . LYS   A 1 217 ? 12.652 45.129  46.988 1.00 49.69 ? 217  LYS   A HE3  1 
ATOM   3350  H  HZ1  . LYS   A 1 217 ? 13.685 43.379  48.002 1.00 57.24 ? 217  LYS   A HZ1  1 
ATOM   3351  H  HZ2  . LYS   A 1 217 ? 14.453 43.731  46.820 1.00 57.24 ? 217  LYS   A HZ2  1 
ATOM   3352  H  HZ3  . LYS   A 1 217 ? 14.924 44.125  48.137 1.00 57.24 ? 217  LYS   A HZ3  1 
ATOM   3353  N  N    . LYS   A 1 218 ? 11.601 49.259  43.909 1.00 25.78 ? 218  LYS   A N    1 
ATOM   3354  C  CA   . LYS   A 1 218 ? 10.120 49.207  43.809 1.00 25.75 ? 218  LYS   A CA   1 
ATOM   3355  C  C    . LYS   A 1 218 ? 9.749  48.553  42.477 1.00 24.39 ? 218  LYS   A C    1 
ATOM   3356  O  O    . LYS   A 1 218 ? 8.903  47.646  42.477 1.00 24.13 ? 218  LYS   A O    1 
ATOM   3357  C  CB   . LYS   A 1 218 ? 9.550  50.625  43.916 1.00 27.33 ? 218  LYS   A CB   1 
ATOM   3358  C  CG   . LYS   A 1 218 ? 8.048  50.750  43.712 1.00 28.24 ? 218  LYS   A CG   1 
ATOM   3359  C  CD   . LYS   A 1 218 ? 7.509  52.100  44.130 1.00 30.09 ? 218  LYS   A CD   1 
ATOM   3360  C  CE   . LYS   A 1 218 ? 6.027  52.255  43.868 1.00 31.00 ? 218  LYS   A CE   1 
ATOM   3361  N  NZ   . LYS   A 1 218 ? 5.217  51.646  44.949 1.00 31.94 ? 218  LYS   A NZ   1 
ATOM   3362  H  H    . LYS   A 1 218 ? 11.941 50.049  43.885 1.00 30.95 ? 218  LYS   A H    1 
ATOM   3363  H  HA   . LYS   A 1 218 ? 9.743  48.682  44.532 1.00 30.90 ? 218  LYS   A HA   1 
ATOM   3364  H  HB2  . LYS   A 1 218 ? 9.771  50.979  44.791 1.00 32.80 ? 218  LYS   A HB2  1 
ATOM   3365  H  HB3  . LYS   A 1 218 ? 9.996  51.185  43.262 1.00 32.80 ? 218  LYS   A HB3  1 
ATOM   3366  H  HG2  . LYS   A 1 218 ? 7.839  50.599  42.777 1.00 33.89 ? 218  LYS   A HG2  1 
ATOM   3367  H  HG3  . LYS   A 1 218 ? 7.598  50.056  44.219 1.00 33.89 ? 218  LYS   A HG3  1 
ATOM   3368  H  HD2  . LYS   A 1 218 ? 7.680  52.232  45.076 1.00 36.12 ? 218  LYS   A HD2  1 
ATOM   3369  H  HD3  . LYS   A 1 218 ? 7.990  52.795  43.655 1.00 36.12 ? 218  LYS   A HD3  1 
ATOM   3370  H  HE2  . LYS   A 1 218 ? 5.808  53.197  43.790 1.00 37.20 ? 218  LYS   A HE2  1 
ATOM   3371  H  HE3  . LYS   A 1 218 ? 5.802  51.840  43.021 1.00 37.20 ? 218  LYS   A HE3  1 
ATOM   3372  H  HZ1  . LYS   A 1 218 ? 4.454  52.096  45.038 1.00 38.33 ? 218  LYS   A HZ1  1 
ATOM   3373  H  HZ2  . LYS   A 1 218 ? 5.039  50.798  44.745 1.00 38.33 ? 218  LYS   A HZ2  1 
ATOM   3374  H  HZ3  . LYS   A 1 218 ? 5.671  51.678  45.714 1.00 38.33 ? 218  LYS   A HZ3  1 
ATOM   3375  N  N    . VAL   A 1 219 ? 10.394 48.981  41.394 1.00 23.62 ? 219  VAL   A N    1 
ATOM   3376  C  CA   . VAL   A 1 219 ? 10.121 48.403  40.045 1.00 22.44 ? 219  VAL   A CA   1 
ATOM   3377  C  C    . VAL   A 1 219 ? 10.448 46.903  40.058 1.00 22.68 ? 219  VAL   A C    1 
ATOM   3378  O  O    . VAL   A 1 219 ? 9.623  46.113  39.578 1.00 23.25 ? 219  VAL   A O    1 
ATOM   3379  C  CB   . VAL   A 1 219 ? 10.927 49.131  38.956 1.00 22.08 ? 219  VAL   A CB   1 
ATOM   3380  C  CG1  . VAL   A 1 219 ? 10.846 48.409  37.621 1.00 24.06 ? 219  VAL   A CG1  1 
ATOM   3381  C  CG2  . VAL   A 1 219 ? 10.493 50.581  38.807 1.00 23.74 ? 219  VAL   A CG2  1 
ATOM   3382  H  H    . VAL   A 1 219 ? 10.991 49.600  41.403 1.00 28.35 ? 219  VAL   A H    1 
ATOM   3383  H  HA   . VAL   A 1 219 ? 9.181  48.522  39.836 1.00 26.93 ? 219  VAL   A HA   1 
ATOM   3384  H  HB   . VAL   A 1 219 ? 11.853 49.126  39.244 1.00 26.51 ? 219  VAL   A HB   1 
ATOM   3385  H  HG11 . VAL   A 1 219 ? 11.364 48.893  36.959 1.00 28.87 ? 219  VAL   A HG11 1 
ATOM   3386  H  HG12 . VAL   A 1 219 ? 11.202 47.512  37.716 1.00 28.87 ? 219  VAL   A HG12 1 
ATOM   3387  H  HG13 . VAL   A 1 219 ? 9.920  48.360  37.335 1.00 28.87 ? 219  VAL   A HG13 1 
ATOM   3388  H  HG21 . VAL   A 1 219 ? 11.021 51.007  38.114 1.00 28.49 ? 219  VAL   A HG21 1 
ATOM   3389  H  HG22 . VAL   A 1 219 ? 9.554  50.615  38.565 1.00 28.49 ? 219  VAL   A HG22 1 
ATOM   3390  H  HG23 . VAL   A 1 219 ? 10.627 51.047  39.647 1.00 28.49 ? 219  VAL   A HG23 1 
ATOM   3391  N  N    . SER   A 1 220 ? 11.623 46.538  40.572 1.00 21.85 ? 220  SER   A N    1 
ATOM   3392  C  CA   . SER   A 1 220 ? 12.035 45.113  40.584 1.00 23.27 ? 220  SER   A CA   1 
ATOM   3393  C  C    . SER   A 1 220 ? 10.993 44.274  41.333 1.00 23.26 ? 220  SER   A C    1 
ATOM   3394  O  O    . SER   A 1 220 ? 10.588 43.228  40.801 1.00 22.37 ? 220  SER   A O    1 
ATOM   3395  C  CB   . SER   A 1 220 ? 13.410 44.949  41.183 1.00 24.28 ? 220  SER   A CB   1 
ATOM   3396  O  OG   . SER   A 1 220 ? 13.684 43.589  41.476 1.00 25.88 ? 220  SER   A OG   1 
ATOM   3397  H  H    . SER   A 1 220 ? 12.194 47.082  40.915 1.00 26.22 ? 220  SER   A H    1 
ATOM   3398  H  HA   . SER   A 1 220 ? 12.083 44.795  39.669 1.00 27.93 ? 220  SER   A HA   1 
ATOM   3399  H  HB2  . SER   A 1 220 ? 14.077 45.290  40.567 1.00 29.14 ? 220  SER   A HB2  1 
ATOM   3400  H  HB3  . SER   A 1 220 ? 13.477 45.477  41.994 1.00 29.14 ? 220  SER   A HB3  1 
ATOM   3401  H  HG   . SER   A 1 220 ? 14.515 43.465  41.482 1.00 31.06 ? 220  SER   A HG   1 
ATOM   3402  N  N    . VAL   A 1 221 ? 10.576 44.723  42.519 1.00 21.89 ? 221  VAL   A N    1 
ATOM   3403  C  CA   . VAL   A 1 221 ? 9.640  43.913  43.354 1.00 21.83 ? 221  VAL   A CA   1 
ATOM   3404  C  C    . VAL   A 1 221 ? 8.329  43.707  42.589 1.00 25.98 ? 221  VAL   A C    1 
ATOM   3405  O  O    . VAL   A 1 221 ? 7.738  42.622  42.714 1.00 25.91 ? 221  VAL   A O    1 
ATOM   3406  C  CB   . VAL   A 1 221 ? 9.397  44.576  44.723 1.00 24.73 ? 221  VAL   A CB   1 
ATOM   3407  C  CG1  . VAL   A 1 221 ? 8.143  44.038  45.395 1.00 25.86 ? 221  VAL   A CG1  1 
ATOM   3408  C  CG2  . VAL   A 1 221 ? 10.602 44.427  45.636 1.00 27.20 ? 221  VAL   A CG2  1 
ATOM   3409  H  H    . VAL   A 1 221 ? 10.810 45.475  42.864 1.00 26.27 ? 221  VAL   A H    1 
ATOM   3410  H  HA   . VAL   A 1 221 ? 10.040 43.047  43.530 1.00 26.20 ? 221  VAL   A HA   1 
ATOM   3411  H  HB   . VAL   A 1 221 ? 9.261  45.522  44.558 1.00 29.69 ? 221  VAL   A HB   1 
ATOM   3412  H  HG11 . VAL   A 1 221 ? 8.021  44.476  46.252 1.00 31.03 ? 221  VAL   A HG11 1 
ATOM   3413  H  HG12 . VAL   A 1 221 ? 7.373  44.212  44.831 1.00 31.03 ? 221  VAL   A HG12 1 
ATOM   3414  H  HG13 . VAL   A 1 221 ? 8.233  43.082  45.531 1.00 31.03 ? 221  VAL   A HG13 1 
ATOM   3415  H  HG21 . VAL   A 1 221 ? 10.418 44.854  46.487 1.00 32.64 ? 221  VAL   A HG21 1 
ATOM   3416  H  HG22 . VAL   A 1 221 ? 10.785 43.485  45.780 1.00 32.64 ? 221  VAL   A HG22 1 
ATOM   3417  H  HG23 . VAL   A 1 221 ? 11.374 44.847  45.225 1.00 32.64 ? 221  VAL   A HG23 1 
ATOM   3418  N  N    . GLU   A 1 222 ? 7.905  44.706  41.818 1.00 22.12 ? 222  GLU   A N    1 
ATOM   3419  C  CA   . GLU   A 1 222 ? 6.650  44.591  41.032 1.00 23.98 ? 222  GLU   A CA   1 
ATOM   3420  C  C    . GLU   A 1 222 ? 6.813  43.543  39.923 1.00 24.21 ? 222  GLU   A C    1 
ATOM   3421  O  O    . GLU   A 1 222 ? 5.933  42.675  39.800 1.00 23.10 ? 222  GLU   A O    1 
ATOM   3422  C  CB   . GLU   A 1 222 ? 6.283  45.954  40.444 1.00 28.44 ? 222  GLU   A CB   1 
ATOM   3423  C  CG   . GLU   A 1 222 ? 5.292  45.872  39.300 1.00 32.86 ? 222  GLU   A CG   1 
ATOM   3424  C  CD   . GLU   A 1 222 ? 5.241  47.120  38.437 1.00 40.08 ? 222  GLU   A CD   1 
ATOM   3425  O  OE1  . GLU   A 1 222 ? 5.701  48.178  38.907 1.00 41.12 ? 222  GLU   A OE1  1 
ATOM   3426  O  OE2  . GLU   A 1 222 ? 4.744  47.029  37.300 1.00 43.90 ? 222  GLU   A OE2  1 
ATOM   3427  H  H    . GLU   A 1 222 ? 8.316  45.456  41.729 1.00 26.55 ? 222  GLU   A H    1 
ATOM   3428  H  HA   . GLU   A 1 222 ? 5.931  44.302  41.616 1.00 28.78 ? 222  GLU   A HA   1 
ATOM   3429  H  HB2  . GLU   A 1 222 ? 5.911  46.511  41.145 1.00 34.13 ? 222  GLU   A HB2  1 
ATOM   3430  H  HB3  . GLU   A 1 222 ? 7.090  46.392  40.132 1.00 34.13 ? 222  GLU   A HB3  1 
ATOM   3431  H  HG2  . GLU   A 1 222 ? 5.519  45.112  38.741 1.00 39.44 ? 222  GLU   A HG2  1 
ATOM   3432  H  HG3  . GLU   A 1 222 ? 4.408  45.704  39.662 1.00 39.44 ? 222  GLU   A HG3  1 
ATOM   3433  N  N    . LYS   A 1 223 ? 7.896  43.626  39.151 1.00 21.03 ? 223  LYS   A N    1 
ATOM   3434  C  CA   . LYS   A 1 223 ? 8.085  42.700  38.000 1.00 20.27 ? 223  LYS   A CA   1 
ATOM   3435  C  C    . LYS   A 1 223 ? 8.235  41.261  38.508 1.00 20.91 ? 223  LYS   A C    1 
ATOM   3436  O  O    . LYS   A 1 223 ? 7.696  40.348  37.865 1.00 17.98 ? 223  LYS   A O    1 
ATOM   3437  C  CB   . LYS   A 1 223 ? 9.294  43.141  37.170 1.00 17.49 ? 223  LYS   A CB   1 
ATOM   3438  C  CG   . LYS   A 1 223 ? 9.325  44.615  36.787 1.00 18.27 ? 223  LYS   A CG   1 
ATOM   3439  C  CD   . LYS   A 1 223 ? 8.029  45.119  36.189 1.00 23.28 ? 223  LYS   A CD   1 
ATOM   3440  C  CE   . LYS   A 1 223 ? 8.134  46.541  35.678 1.00 21.68 ? 223  LYS   A CE   1 
ATOM   3441  N  NZ   . LYS   A 1 223 ? 6.809  47.103  35.325 1.00 21.40 ? 223  LYS   A NZ   1 
ATOM   3442  H  H    . LYS   A 1 223 ? 8.530  44.196  39.263 1.00 25.24 ? 223  LYS   A H    1 
ATOM   3443  H  HA   . LYS   A 1 223 ? 7.305  42.729  37.424 1.00 24.33 ? 223  LYS   A HA   1 
ATOM   3444  H  HB2  . LYS   A 1 223 ? 10.101 42.935  37.668 1.00 20.99 ? 223  LYS   A HB2  1 
ATOM   3445  H  HB3  . LYS   A 1 223 ? 9.319  42.611  36.358 1.00 20.99 ? 223  LYS   A HB3  1 
ATOM   3446  H  HG2  . LYS   A 1 223 ? 9.534  45.141  37.575 1.00 21.93 ? 223  LYS   A HG2  1 
ATOM   3447  H  HG3  . LYS   A 1 223 ? 10.043 44.760  36.151 1.00 21.93 ? 223  LYS   A HG3  1 
ATOM   3448  H  HD2  . LYS   A 1 223 ? 7.766  44.536  35.460 1.00 27.94 ? 223  LYS   A HD2  1 
ATOM   3449  H  HD3  . LYS   A 1 223 ? 7.328  45.071  36.858 1.00 27.94 ? 223  LYS   A HD3  1 
ATOM   3450  H  HE2  . LYS   A 1 223 ? 8.550  47.097  36.355 1.00 26.02 ? 223  LYS   A HE2  1 
ATOM   3451  H  HE3  . LYS   A 1 223 ? 8.711  46.562  34.899 1.00 26.02 ? 223  LYS   A HE3  1 
ATOM   3452  H  HZ1  . LYS   A 1 223 ? 6.900  47.959  35.099 1.00 25.68 ? 223  LYS   A HZ1  1 
ATOM   3453  H  HZ2  . LYS   A 1 223 ? 6.467  46.650  34.639 1.00 25.68 ? 223  LYS   A HZ2  1 
ATOM   3454  H  HZ3  . LYS   A 1 223 ? 6.263  47.038  36.025 1.00 25.68 ? 223  LYS   A HZ3  1 
ATOM   3455  N  N    . ILE   A 1 224 ? 8.940  41.082  39.626 1.00 17.80 ? 224  ILE   A N    1 
ATOM   3456  C  CA   . ILE   A 1 224 ? 9.148  39.717  40.194 1.00 19.89 ? 224  ILE   A CA   1 
ATOM   3457  C  C    . ILE   A 1 224 ? 7.791  39.143  40.618 1.00 20.88 ? 224  ILE   A C    1 
ATOM   3458  O  O    . ILE   A 1 224 ? 7.556  37.950  40.396 1.00 20.09 ? 224  ILE   A O    1 
ATOM   3459  C  CB   . ILE   A 1 224 ? 10.156 39.754  41.358 1.00 22.15 ? 224  ILE   A CB   1 
ATOM   3460  C  CG1  . ILE   A 1 224 ? 11.559 40.115  40.863 1.00 20.73 ? 224  ILE   A CG1  1 
ATOM   3461  C  CG2  . ILE   A 1 224 ? 10.149 38.443  42.125 1.00 22.25 ? 224  ILE   A CG2  1 
ATOM   3462  C  CD1  . ILE   A 1 224 ? 12.494 40.585  41.951 1.00 26.59 ? 224  ILE   A CD1  1 
ATOM   3463  H  H    . ILE   A 1 224 ? 9.306  41.718  40.075 1.00 21.36 ? 224  ILE   A H    1 
ATOM   3464  H  HA   . ILE   A 1 224 ? 9.531  39.134  39.520 1.00 23.87 ? 224  ILE   A HA   1 
ATOM   3465  H  HB   . ILE   A 1 224 ? 9.880  40.452  41.973 1.00 26.59 ? 224  ILE   A HB   1 
ATOM   3466  H  HG12 . ILE   A 1 224 ? 11.948 39.340  40.428 1.00 24.88 ? 224  ILE   A HG12 1 
ATOM   3467  H  HG13 . ILE   A 1 224 ? 11.485 40.810  40.190 1.00 24.88 ? 224  ILE   A HG13 1 
ATOM   3468  H  HG21 . ILE   A 1 224 ? 10.790 38.490  42.852 1.00 26.70 ? 224  ILE   A HG21 1 
ATOM   3469  H  HG22 . ILE   A 1 224 ? 9.263  38.284  42.486 1.00 26.70 ? 224  ILE   A HG22 1 
ATOM   3470  H  HG23 . ILE   A 1 224 ? 10.390 37.717  41.528 1.00 26.70 ? 224  ILE   A HG23 1 
ATOM   3471  H  HD11 . ILE   A 1 224 ? 13.359 40.795  41.566 1.00 31.91 ? 224  ILE   A HD11 1 
ATOM   3472  H  HD12 . ILE   A 1 224 ? 12.127 41.378  42.373 1.00 31.91 ? 224  ILE   A HD12 1 
ATOM   3473  H  HD13 . ILE   A 1 224 ? 12.597 39.885  42.614 1.00 31.91 ? 224  ILE   A HD13 1 
ATOM   3474  N  N    . THR   A 1 225 ? 6.940  39.981  41.212 1.00 19.65 ? 225  THR   A N    1 
ATOM   3475  C  CA   . THR   A 1 225 ? 5.600  39.516  41.649 1.00 22.19 ? 225  THR   A CA   1 
ATOM   3476  C  C    . THR   A 1 225 ? 4.837  39.005  40.422 1.00 23.10 ? 225  THR   A C    1 
ATOM   3477  O  O    . THR   A 1 225 ? 4.244  37.920  40.505 1.00 21.94 ? 225  THR   A O    1 
ATOM   3478  C  CB   . THR   A 1 225 ? 4.853  40.636  42.385 1.00 23.92 ? 225  THR   A CB   1 
ATOM   3479  O  OG1  . THR   A 1 225 ? 5.545  40.922  43.602 1.00 22.17 ? 225  THR   A OG1  1 
ATOM   3480  C  CG2  . THR   A 1 225 ? 3.413  40.283  42.685 1.00 26.48 ? 225  THR   A CG2  1 
ATOM   3481  H  H    . THR   A 1 225 ? 7.106  40.809  41.373 1.00 23.58 ? 225  THR   A H    1 
ATOM   3482  H  HA   . THR   A 1 225 ? 5.684  38.786  42.282 1.00 26.63 ? 225  THR   A HA   1 
ATOM   3483  H  HB   . THR   A 1 225 ? 4.833  41.413  41.804 1.00 28.70 ? 225  THR   A HB   1 
ATOM   3484  H  HG1  . THR   A 1 225 ? 6.173  41.458  43.448 1.00 26.60 ? 225  THR   A HG1  1 
ATOM   3485  H  HG21 . THR   A 1 225 ? 2.988  41.022  43.149 1.00 31.79 ? 225  THR   A HG21 1 
ATOM   3486  H  HG22 . THR   A 1 225 ? 2.942  40.110  41.855 1.00 31.79 ? 225  THR   A HG22 1 
ATOM   3487  H  HG23 . THR   A 1 225 ? 3.384  39.491  43.244 1.00 31.79 ? 225  THR   A HG23 1 
ATOM   3488  N  N    . THR   A 1 226 ? 4.864  39.772  39.331 1.00 21.67 ? 226  THR   A N    1 
ATOM   3489  C  CA   . THR   A 1 226 ? 4.165  39.367  38.083 1.00 20.66 ? 226  THR   A CA   1 
ATOM   3490  C  C    . THR   A 1 226 ? 4.733  38.033  37.585 1.00 20.51 ? 226  THR   A C    1 
ATOM   3491  O  O    . THR   A 1 226 ? 3.948  37.141  37.230 1.00 16.94 ? 226  THR   A O    1 
ATOM   3492  C  CB   . THR   A 1 226 ? 4.288  40.457  37.011 1.00 18.45 ? 226  THR   A CB   1 
ATOM   3493  O  OG1  . THR   A 1 226 ? 3.836  41.689  37.572 1.00 19.60 ? 226  THR   A OG1  1 
ATOM   3494  C  CG2  . THR   A 1 226 ? 3.520  40.131  35.749 1.00 19.03 ? 226  THR   A CG2  1 
ATOM   3495  H  H    . THR   A 1 226 ? 5.275  40.526  39.282 1.00 26.01 ? 226  THR   A H    1 
ATOM   3496  H  HA   . THR   A 1 226 ? 3.221  39.251  38.272 1.00 24.80 ? 226  THR   A HA   1 
ATOM   3497  H  HB   . THR   A 1 226 ? 5.219  40.522  36.746 1.00 22.14 ? 226  THR   A HB   1 
ATOM   3498  H  HG1  . THR   A 1 226 ? 4.167  42.331  37.143 1.00 23.52 ? 226  THR   A HG1  1 
ATOM   3499  H  HG21 . THR   A 1 226 ? 3.631  40.850  35.107 1.00 22.84 ? 226  THR   A HG21 1 
ATOM   3500  H  HG22 . THR   A 1 226 ? 3.857  39.304  35.369 1.00 22.84 ? 226  THR   A HG22 1 
ATOM   3501  H  HG23 . THR   A 1 226 ? 2.579  40.029  35.960 1.00 22.84 ? 226  THR   A HG23 1 
ATOM   3502  N  N    . LEU   A 1 227 ? 6.061  37.920  37.559 1.00 16.46 ? 227  LEU   A N    1 
ATOM   3503  C  CA   . LEU   A 1 227 ? 6.688  36.673  37.053 1.00 19.80 ? 227  LEU   A CA   1 
ATOM   3504  C  C    . LEU   A 1 227 ? 6.299  35.509  37.969 1.00 19.38 ? 227  LEU   A C    1 
ATOM   3505  O  O    . LEU   A 1 227 ? 5.970  34.433  37.451 1.00 16.36 ? 227  LEU   A O    1 
ATOM   3506  C  CB   . LEU   A 1 227 ? 8.208  36.868  37.017 1.00 16.37 ? 227  LEU   A CB   1 
ATOM   3507  C  CG   . LEU   A 1 227 ? 8.714  37.808  35.925 1.00 20.57 ? 227  LEU   A CG   1 
ATOM   3508  C  CD1  . LEU   A 1 227 ? 10.205 38.061  36.075 1.00 16.39 ? 227  LEU   A CD1  1 
ATOM   3509  C  CD2  . LEU   A 1 227 ? 8.405  37.247  34.546 1.00 17.91 ? 227  LEU   A CD2  1 
ATOM   3510  H  H    . LEU   A 1 227 ? 6.611  38.528  37.819 1.00 19.75 ? 227  LEU   A H    1 
ATOM   3511  H  HA   . LEU   A 1 227 ? 6.379  36.470  36.156 1.00 23.76 ? 227  LEU   A HA   1 
ATOM   3512  H  HB2  . LEU   A 1 227 ? 8.497  37.209  37.878 1.00 19.64 ? 227  LEU   A HB2  1 
ATOM   3513  H  HB3  . LEU   A 1 227 ? 8.629  36.002  36.900 1.00 19.64 ? 227  LEU   A HB3  1 
ATOM   3514  H  HG   . LEU   A 1 227 ? 8.252  38.655  36.022 1.00 24.69 ? 227  LEU   A HG   1 
ATOM   3515  H  HD11 . LEU   A 1 227 ? 10.504 38.659  35.373 1.00 19.67 ? 227  LEU   A HD11 1 
ATOM   3516  H  HD12 . LEU   A 1 227 ? 10.379 38.465  36.939 1.00 19.67 ? 227  LEU   A HD12 1 
ATOM   3517  H  HD13 . LEU   A 1 227 ? 10.684 37.220  36.009 1.00 19.67 ? 227  LEU   A HD13 1 
ATOM   3518  H  HD21 . LEU   A 1 227 ? 8.733  37.857  33.867 1.00 21.50 ? 227  LEU   A HD21 1 
ATOM   3519  H  HD22 . LEU   A 1 227 ? 8.838  36.385  34.443 1.00 21.50 ? 227  LEU   A HD22 1 
ATOM   3520  H  HD23 . LEU   A 1 227 ? 7.446  37.140  34.447 1.00 21.50 ? 227  LEU   A HD23 1 
ATOM   3521  N  N    . LYS   A 1 228 ? 6.337  35.730  39.282 1.00 19.52 ? 228  LYS   A N    1 
ATOM   3522  C  CA   . LYS   A 1 228 ? 6.048  34.634  40.242 1.00 18.25 ? 228  LYS   A CA   1 
ATOM   3523  C  C    . LYS   A 1 228 ? 4.569  34.246  40.137 1.00 21.72 ? 228  LYS   A C    1 
ATOM   3524  O  O    . LYS   A 1 228 ? 4.246  33.081  40.420 1.00 20.17 ? 228  LYS   A O    1 
ATOM   3525  C  CB   . LYS   A 1 228 ? 6.410  35.066  41.665 1.00 20.84 ? 228  LYS   A CB   1 
ATOM   3526  C  CG   . LYS   A 1 228 ? 7.896  35.076  41.993 1.00 24.91 ? 228  LYS   A CG   1 
ATOM   3527  C  CD   . LYS   A 1 228 ? 8.178  35.417  43.441 1.00 26.40 ? 228  LYS   A CD   1 
ATOM   3528  C  CE   . LYS   A 1 228 ? 9.656  35.483  43.764 1.00 31.91 ? 228  LYS   A CE   1 
ATOM   3529  N  NZ   . LYS   A 1 228 ? 10.139 34.227  44.382 1.00 28.78 ? 228  LYS   A NZ   1 
ATOM   3530  H  H    . LYS   A 1 228 ? 6.523  36.488  39.643 1.00 23.43 ? 228  LYS   A H    1 
ATOM   3531  H  HA   . LYS   A 1 228 ? 6.588  33.858  40.025 1.00 21.91 ? 228  LYS   A HA   1 
ATOM   3532  H  HB2  . LYS   A 1 228 ? 6.056  35.957  41.815 1.00 25.02 ? 228  LYS   A HB2  1 
ATOM   3533  H  HB3  . LYS   A 1 228 ? 5.962  34.474  42.289 1.00 25.02 ? 228  LYS   A HB3  1 
ATOM   3534  H  HG2  . LYS   A 1 228 ? 8.273  34.205  41.791 1.00 29.89 ? 228  LYS   A HG2  1 
ATOM   3535  H  HG3  . LYS   A 1 228 ? 8.344  35.718  41.421 1.00 29.89 ? 228  LYS   A HG3  1 
ATOM   3536  H  HD2  . LYS   A 1 228 ? 7.769  36.271  43.651 1.00 31.68 ? 228  LYS   A HD2  1 
ATOM   3537  H  HD3  . LYS   A 1 228 ? 7.758  34.754  44.011 1.00 31.68 ? 228  LYS   A HD3  1 
ATOM   3538  H  HE2  . LYS   A 1 228 ? 10.157 35.658  42.952 1.00 38.30 ? 228  LYS   A HE2  1 
ATOM   3539  H  HE3  . LYS   A 1 228 ? 9.823  36.225  44.366 1.00 38.30 ? 228  LYS   A HE3  1 
ATOM   3540  H  HZ1  . LYS   A 1 228 ? 10.948 34.359  44.729 1.00 34.54 ? 228  LYS   A HZ1  1 
ATOM   3541  H  HZ2  . LYS   A 1 228 ? 9.578  33.978  45.026 1.00 34.54 ? 228  LYS   A HZ2  1 
ATOM   3542  H  HZ3  . LYS   A 1 228 ? 10.182 33.589  43.763 1.00 34.54 ? 228  LYS   A HZ3  1 
ATOM   3543  N  N    . ASN   A 1 229 ? 3.711  35.166  39.702 1.00 19.50 ? 229  ASN   A N    1 
ATOM   3544  C  CA   . ASN   A 1 229 ? 2.259  34.871  39.588 1.00 21.11 ? 229  ASN   A CA   1 
ATOM   3545  C  C    . ASN   A 1 229 ? 1.929  34.267  38.214 1.00 21.85 ? 229  ASN   A C    1 
ATOM   3546  O  O    . ASN   A 1 229 ? 0.799  33.794  38.040 1.00 18.92 ? 229  ASN   A O    1 
ATOM   3547  C  CB   . ASN   A 1 229 ? 1.408  36.113  39.859 1.00 22.14 ? 229  ASN   A CB   1 
ATOM   3548  C  CG   . ASN   A 1 229 ? 1.359  36.470  41.328 1.00 29.26 ? 229  ASN   A CG   1 
ATOM   3549  O  OD1  . ASN   A 1 229 ? 1.451  35.594  42.184 1.00 33.84 ? 229  ASN   A OD1  1 
ATOM   3550  N  ND2  . ASN   A 1 229 ? 1.229  37.751  41.628 1.00 36.00 ? 229  ASN   A ND2  1 
ATOM   3551  H  H    . ASN   A 1 229 ? 3.934  35.963  39.467 1.00 23.41 ? 229  ASN   A H    1 
ATOM   3552  H  HA   . ASN   A 1 229 ? 2.040  34.215  40.268 1.00 25.33 ? 229  ASN   A HA   1 
ATOM   3553  H  HB2  . ASN   A 1 229 ? 1.766  36.863  39.358 1.00 26.57 ? 229  ASN   A HB2  1 
ATOM   3554  H  HB3  . ASN   A 1 229 ? 0.506  35.961  39.536 1.00 26.57 ? 229  ASN   A HB3  1 
ATOM   3555  H  HD21 . ASN   A 1 229 ? 1.206  38.000  42.451 1.00 43.21 ? 229  ASN   A HD21 1 
ATOM   3556  H  HD22 . ASN   A 1 229 ? 1.167  38.336  41.000 1.00 43.21 ? 229  ASN   A HD22 1 
ATOM   3557  N  N    . ASP   A 1 230 ? 2.879  34.297  37.277 1.00 19.21 ? 230  ASP   A N    1 
ATOM   3558  C  CA   . ASP   A 1 230 ? 2.635  33.759  35.914 1.00 19.91 ? 230  ASP   A CA   1 
ATOM   3559  C  C    . ASP   A 1 230 ? 2.741  32.231  35.932 1.00 18.70 ? 230  ASP   A C    1 
ATOM   3560  O  O    . ASP   A 1 230 ? 3.665  31.705  36.559 1.00 18.83 ? 230  ASP   A O    1 
ATOM   3561  C  CB   . ASP   A 1 230 ? 3.600  34.356  34.890 1.00 18.92 ? 230  ASP   A CB   1 
ATOM   3562  C  CG   . ASP   A 1 230 ? 3.360  33.825  33.488 1.00 18.69 ? 230  ASP   A CG   1 
ATOM   3563  O  OD1  . ASP   A 1 230 ? 2.456  34.350  32.813 1.00 17.78 ? 230  ASP   A OD1  1 
ATOM   3564  O  OD2  . ASP   A 1 230 ? 4.067  32.882  33.092 1.00 18.02 ? 230  ASP   A OD2  1 
ATOM   3565  H  H    . ASP   A 1 230 ? 3.667  34.619  37.399 1.00 23.05 ? 230  ASP   A H    1 
ATOM   3566  H  HA   . ASP   A 1 230 ? 1.738  34.013  35.645 1.00 23.90 ? 230  ASP   A HA   1 
ATOM   3567  H  HB2  . ASP   A 1 230 ? 3.508  35.322  34.887 1.00 22.70 ? 230  ASP   A HB2  1 
ATOM   3568  H  HB3  . ASP   A 1 230 ? 4.512  34.159  35.156 1.00 22.70 ? 230  ASP   A HB3  1 
ATOM   3569  N  N    . PRO   A 1 231 ? 1.814  31.504  35.277 1.00 20.49 ? 231  PRO   A N    1 
ATOM   3570  C  CA   . PRO   A 1 231 ? 1.831  30.041  35.289 1.00 21.85 ? 231  PRO   A CA   1 
ATOM   3571  C  C    . PRO   A 1 231 ? 3.140  29.447  34.739 1.00 15.25 ? 231  PRO   A C    1 
ATOM   3572  O  O    . PRO   A 1 231 ? 3.566  28.429  35.230 1.00 19.92 ? 231  PRO   A O    1 
ATOM   3573  C  CB   . PRO   A 1 231 ? 0.652  29.665  34.380 1.00 25.28 ? 231  PRO   A CB   1 
ATOM   3574  C  CG   . PRO   A 1 231 ? -0.261 30.866  34.437 1.00 24.93 ? 231  PRO   A CG   1 
ATOM   3575  C  CD   . PRO   A 1 231 ? 0.676  32.050  34.535 1.00 19.78 ? 231  PRO   A CD   1 
ATOM   3576  H  HA   . PRO   A 1 231 ? 1.764  29.693  36.192 1.00 26.22 ? 231  PRO   A HA   1 
ATOM   3577  H  HB2  . PRO   A 1 231 ? 0.947  29.487  33.473 1.00 30.34 ? 231  PRO   A HB2  1 
ATOM   3578  H  HB3  . PRO   A 1 231 ? 0.204  28.864  34.695 1.00 30.34 ? 231  PRO   A HB3  1 
ATOM   3579  H  HG2  . PRO   A 1 231 ? -0.820 30.923  33.646 1.00 29.92 ? 231  PRO   A HG2  1 
ATOM   3580  H  HG3  . PRO   A 1 231 ? -0.856 30.822  35.202 1.00 29.92 ? 231  PRO   A HG3  1 
ATOM   3581  H  HD2  . PRO   A 1 231 ? 0.939  32.374  33.659 1.00 23.74 ? 231  PRO   A HD2  1 
ATOM   3582  H  HD3  . PRO   A 1 231 ? 0.266  32.795  35.002 1.00 23.74 ? 231  PRO   A HD3  1 
ATOM   3583  N  N    . VAL   A 1 232 ? 3.730  30.089  33.733 1.00 14.07 ? 232  VAL   A N    1 
ATOM   3584  C  CA   . VAL   A 1 232 ? 4.983  29.545  33.126 1.00 14.92 ? 232  VAL   A CA   1 
ATOM   3585  C  C    . VAL   A 1 232 ? 6.184  30.019  33.954 1.00 15.08 ? 232  VAL   A C    1 
ATOM   3586  O  O    . VAL   A 1 232 ? 6.944  29.165  34.430 1.00 16.98 ? 232  VAL   A O    1 
ATOM   3587  C  CB   . VAL   A 1 232 ? 5.129  29.942  31.643 1.00 13.41 ? 232  VAL   A CB   1 
ATOM   3588  C  CG1  . VAL   A 1 232 ? 6.427  29.423  31.045 1.00 14.59 ? 232  VAL   A CG1  1 
ATOM   3589  C  CG2  . VAL   A 1 232 ? 3.937  29.480  30.821 1.00 20.06 ? 232  VAL   A CG2  1 
ATOM   3590  H  H    . VAL   A 1 232 ? 3.444  30.821  33.384 1.00 16.89 ? 232  VAL   A H    1 
ATOM   3591  H  HA   . VAL   A 1 232 ? 4.942  28.576  33.142 1.00 17.90 ? 232  VAL   A HA   1 
ATOM   3592  H  HB   . VAL   A 1 232 ? 5.156  30.911  31.613 1.00 16.10 ? 232  VAL   A HB   1 
ATOM   3593  H  HG11 . VAL   A 1 232 ? 6.485  29.691  30.114 1.00 17.51 ? 232  VAL   A HG11 1 
ATOM   3594  H  HG12 . VAL   A 1 232 ? 7.179  29.792  31.534 1.00 17.51 ? 232  VAL   A HG12 1 
ATOM   3595  H  HG13 . VAL   A 1 232 ? 6.447  28.455  31.104 1.00 17.51 ? 232  VAL   A HG13 1 
ATOM   3596  H  HG21 . VAL   A 1 232 ? 4.060  29.745  29.896 1.00 24.07 ? 232  VAL   A HG21 1 
ATOM   3597  H  HG22 . VAL   A 1 232 ? 3.862  28.514  30.874 1.00 24.07 ? 232  VAL   A HG22 1 
ATOM   3598  H  HG23 . VAL   A 1 232 ? 3.127  29.886  31.168 1.00 24.07 ? 232  VAL   A HG23 1 
ATOM   3599  N  N    . ALA   A 1 233 ? 6.334  31.330  34.123 1.00 15.70 ? 233  ALA   A N    1 
ATOM   3600  C  CA   . ALA   A 1 233 ? 7.528  31.861  34.826 1.00 15.44 ? 233  ALA   A CA   1 
ATOM   3601  C  C    . ALA   A 1 233 ? 7.487  31.512  36.316 1.00 16.14 ? 233  ALA   A C    1 
ATOM   3602  O  O    . ALA   A 1 233 ? 8.564  31.346  36.901 1.00 19.55 ? 233  ALA   A O    1 
ATOM   3603  C  CB   . ALA   A 1 233 ? 7.612  33.354  34.639 1.00 16.51 ? 233  ALA   A CB   1 
ATOM   3604  H  H    . ALA   A 1 233 ? 5.777  31.926  33.850 1.00 18.85 ? 233  ALA   A H    1 
ATOM   3605  H  HA   . ALA   A 1 233 ? 8.318  31.449  34.444 1.00 18.53 ? 233  ALA   A HA   1 
ATOM   3606  H  HB1  . ALA   A 1 233 ? 8.394  33.695  35.101 1.00 19.82 ? 233  ALA   A HB1  1 
ATOM   3607  H  HB2  . ALA   A 1 233 ? 7.681  33.559  33.693 1.00 19.82 ? 233  ALA   A HB2  1 
ATOM   3608  H  HB3  . ALA   A 1 233 ? 6.815  33.771  35.003 1.00 19.82 ? 233  ALA   A HB3  1 
ATOM   3609  N  N    . GLY   A 1 234 ? 6.290  31.412  36.898 1.00 17.30 ? 234  GLY   A N    1 
ATOM   3610  C  CA   . GLY   A 1 234 ? 6.176  31.192  38.354 1.00 20.11 ? 234  GLY   A CA   1 
ATOM   3611  C  C    . GLY   A 1 234 ? 6.053  29.733  38.761 1.00 22.61 ? 234  GLY   A C    1 
ATOM   3612  O  O    . GLY   A 1 234 ? 6.265  29.450  39.947 1.00 18.60 ? 234  GLY   A O    1 
ATOM   3613  H  H    . GLY   A 1 234 ? 5.540  31.467  36.481 1.00 20.76 ? 234  GLY   A H    1 
ATOM   3614  H  HA2  . GLY   A 1 234 ? 6.954  31.573  38.790 1.00 24.14 ? 234  GLY   A HA2  1 
ATOM   3615  H  HA3  . GLY   A 1 234 ? 5.402  31.675  38.683 1.00 24.14 ? 234  GLY   A HA3  1 
ATOM   3616  N  N    . GLN   A 1 235 ? 5.723  28.837  37.827 1.00 17.27 ? 235  GLN   A N    1 
ATOM   3617  C  CA   . GLN   A 1 235 ? 5.496  27.422  38.216 1.00 20.31 ? 235  GLN   A CA   1 
ATOM   3618  C  C    . GLN   A 1 235 ? 6.115  26.451  37.209 1.00 15.73 ? 235  GLN   A C    1 
ATOM   3619  O  O    . GLN   A 1 235 ? 6.945  25.628  37.621 1.00 15.40 ? 235  GLN   A O    1 
ATOM   3620  C  CB   . GLN   A 1 235 ? 3.992  27.165  38.327 1.00 21.27 ? 235  GLN   A CB   1 
ATOM   3621  C  CG   . GLN   A 1 235 ? 3.336  27.859  39.510 1.00 29.27 ? 235  GLN   A CG   1 
ATOM   3622  C  CD   . GLN   A 1 235 ? 3.802  27.290  40.827 1.00 35.15 ? 235  GLN   A CD   1 
ATOM   3623  O  OE1  . GLN   A 1 235 ? 4.279  26.160  40.903 1.00 33.34 ? 235  GLN   A OE1  1 
ATOM   3624  N  NE2  . GLN   A 1 235 ? 3.668  28.076  41.882 1.00 44.66 ? 235  GLN   A NE2  1 
ATOM   3625  H  H    . GLN   A 1 235 ? 5.626  29.010  36.990 1.00 20.73 ? 235  GLN   A H    1 
ATOM   3626  H  HA   . GLN   A 1 235 ? 5.926  27.270  39.072 1.00 24.38 ? 235  GLN   A HA   1 
ATOM   3627  H  HB2  . GLN   A 1 235 ? 3.561  27.460  37.510 1.00 25.53 ? 235  GLN   A HB2  1 
ATOM   3628  H  HB3  . GLN   A 1 235 ? 3.840  26.210  38.398 1.00 25.53 ? 235  GLN   A HB3  1 
ATOM   3629  H  HG2  . GLN   A 1 235 ? 3.536  28.808  39.479 1.00 35.13 ? 235  GLN   A HG2  1 
ATOM   3630  H  HG3  . GLN   A 1 235 ? 2.372  27.770  39.443 1.00 35.13 ? 235  GLN   A HG3  1 
ATOM   3631  H  HE21 . GLN   A 1 235 ? 3.330  28.862  41.793 1.00 53.59 ? 235  GLN   A HE21 1 
ATOM   3632  H  HE22 . GLN   A 1 235 ? 3.919  27.801  42.657 1.00 53.59 ? 235  GLN   A HE22 1 
ATOM   3633  N  N    . GLY   A 1 236 ? 5.708  26.534  35.944 1.00 16.05 ? 236  GLY   A N    1 
ATOM   3634  C  CA   . GLY   A 1 236 ? 6.173  25.546  34.958 1.00 16.25 ? 236  GLY   A CA   1 
ATOM   3635  C  C    . GLY   A 1 236 ? 7.678  25.522  34.794 1.00 14.89 ? 236  GLY   A C    1 
ATOM   3636  O  O    . GLY   A 1 236 ? 8.256  24.430  34.778 1.00 16.25 ? 236  GLY   A O    1 
ATOM   3637  H  H    . GLY   A 1 236 ? 5.177  27.136  35.637 1.00 19.27 ? 236  GLY   A H    1 
ATOM   3638  H  HA2  . GLY   A 1 236 ? 5.870  24.664  35.226 1.00 19.50 ? 236  GLY   A HA2  1 
ATOM   3639  H  HA3  . GLY   A 1 236 ? 5.764  25.738  34.100 1.00 19.50 ? 236  GLY   A HA3  1 
ATOM   3640  N  N    A MET   A 1 237 ? 8.289  26.691  34.584 0.48 14.75 ? 237  MET   A N    1 
ATOM   3641  N  N    B MET   A 1 237 ? 8.290  26.692  34.582 0.52 14.75 ? 237  MET   A N    1 
ATOM   3642  C  CA   A MET   A 1 237 ? 9.757  26.744  34.334 0.48 15.75 ? 237  MET   A CA   1 
ATOM   3643  C  CA   B MET   A 1 237 ? 9.759  26.746  34.333 0.52 15.75 ? 237  MET   A CA   1 
ATOM   3644  C  C    A MET   A 1 237 ? 10.545 26.303  35.575 0.48 14.33 ? 237  MET   A C    1 
ATOM   3645  C  C    B MET   A 1 237 ? 10.543 26.301  35.575 0.52 14.32 ? 237  MET   A C    1 
ATOM   3646  O  O    A MET   A 1 237 ? 11.538 25.576  35.414 0.48 14.36 ? 237  MET   A O    1 
ATOM   3647  O  O    B MET   A 1 237 ? 11.541 25.580  35.413 0.52 14.36 ? 237  MET   A O    1 
ATOM   3648  C  CB   A MET   A 1 237 ? 10.194 28.147  33.902 0.48 15.79 ? 237  MET   A CB   1 
ATOM   3649  C  CB   B MET   A 1 237 ? 10.213 28.149  33.913 0.52 15.79 ? 237  MET   A CB   1 
ATOM   3650  C  CG   A MET   A 1 237 ? 9.644  28.544  32.554 0.48 17.64 ? 237  MET   A CG   1 
ATOM   3651  C  CG   B MET   A 1 237 ? 9.484  28.695  32.706 0.52 17.87 ? 237  MET   A CG   1 
ATOM   3652  S  SD   A MET   A 1 237 ? 10.500 27.665  31.231 0.48 17.55 ? 237  MET   A SD   1 
ATOM   3653  S  SD   B MET   A 1 237 ? 10.633 29.225  31.415 0.52 18.68 ? 237  MET   A SD   1 
ATOM   3654  C  CE   A MET   A 1 237 ? 11.666 28.925  30.722 0.48 16.87 ? 237  MET   A CE   1 
ATOM   3655  C  CE   B MET   A 1 237 ? 11.128 27.628  30.774 0.52 19.01 ? 237  MET   A CE   1 
ATOM   3656  H  H    A MET   A 1 237 ? 7.893  27.454  34.580 0.48 17.71 ? 237  MET   A H    1 
ATOM   3657  H  H    B MET   A 1 237 ? 7.893  27.455  34.576 0.52 17.70 ? 237  MET   A H    1 
ATOM   3658  H  HA   A MET   A 1 237 ? 9.951  26.127  33.611 0.48 18.90 ? 237  MET   A HA   1 
ATOM   3659  H  HA   B MET   A 1 237 ? 9.944  26.134  33.603 0.52 18.90 ? 237  MET   A HA   1 
ATOM   3660  H  HB2  A MET   A 1 237 ? 9.903  28.790  34.567 0.48 18.95 ? 237  MET   A HB2  1 
ATOM   3661  H  HB2  B MET   A 1 237 ? 10.086 28.757  34.658 0.52 18.96 ? 237  MET   A HB2  1 
ATOM   3662  H  HB3  A MET   A 1 237 ? 11.163 28.185  33.875 0.48 18.95 ? 237  MET   A HB3  1 
ATOM   3663  H  HB3  B MET   A 1 237 ? 11.164 28.128  33.723 0.52 18.96 ? 237  MET   A HB3  1 
ATOM   3664  H  HG2  A MET   A 1 237 ? 8.695  28.349  32.517 0.48 21.17 ? 237  MET   A HG2  1 
ATOM   3665  H  HG2  B MET   A 1 237 ? 8.890  28.015  32.352 0.52 21.45 ? 237  MET   A HG2  1 
ATOM   3666  H  HG3  A MET   A 1 237 ? 9.742  29.501  32.429 0.48 21.17 ? 237  MET   A HG3  1 
ATOM   3667  H  HG3  B MET   A 1 237 ? 8.930  29.445  32.974 0.52 21.45 ? 237  MET   A HG3  1 
ATOM   3668  H  HE1  A MET   A 1 237 ? 12.212 28.586  29.995 0.48 20.25 ? 237  MET   A HE1  1 
ATOM   3669  H  HE1  B MET   A 1 237 ? 11.764 27.752  30.052 0.52 22.82 ? 237  MET   A HE1  1 
ATOM   3670  H  HE2  A MET   A 1 237 ? 11.183 29.712  30.424 0.48 20.25 ? 237  MET   A HE2  1 
ATOM   3671  H  HE2  B MET   A 1 237 ? 11.541 27.109  31.482 0.52 22.82 ? 237  MET   A HE2  1 
ATOM   3672  H  HE3  A MET   A 1 237 ? 12.236 29.161  31.471 0.48 20.25 ? 237  MET   A HE3  1 
ATOM   3673  H  HE3  B MET   A 1 237 ? 10.348 27.157  30.441 0.52 22.82 ? 237  MET   A HE3  1 
ATOM   3674  N  N    . PRO   A 1 238 ? 10.233 26.810  36.787 1.00 15.35 ? 238  PRO   A N    1 
ATOM   3675  C  CA   . PRO   A 1 238 ? 11.028 26.447  37.955 1.00 14.75 ? 238  PRO   A CA   1 
ATOM   3676  C  C    . PRO   A 1 238 ? 10.913 24.934  38.200 1.00 16.71 ? 238  PRO   A C    1 
ATOM   3677  O  O    . PRO   A 1 238 ? 11.899 24.309  38.503 1.00 16.33 ? 238  PRO   A O    1 
ATOM   3678  C  CB   . PRO   A 1 238 ? 10.427 27.278  39.102 1.00 18.38 ? 238  PRO   A CB   1 
ATOM   3679  C  CG   . PRO   A 1 238 ? 9.255  28.016  38.490 1.00 17.20 ? 238  PRO   A CG   1 
ATOM   3680  C  CD   . PRO   A 1 238 ? 9.574  28.096  37.015 1.00 16.88 ? 238  PRO   A CD   1 
ATOM   3681  H  HA   . PRO   A 1 238 ? 11.976 26.630  37.857 1.00 17.71 ? 238  PRO   A HA   1 
ATOM   3682  H  HB2  . PRO   A 1 238 ? 10.139 26.709  39.833 1.00 22.06 ? 238  PRO   A HB2  1 
ATOM   3683  H  HB3  . PRO   A 1 238 ? 11.080 27.897  39.465 1.00 22.06 ? 238  PRO   A HB3  1 
ATOM   3684  H  HG2  . PRO   A 1 238 ? 8.422  27.543  38.645 1.00 20.64 ? 238  PRO   A HG2  1 
ATOM   3685  H  HG3  . PRO   A 1 238 ? 9.155  28.900  38.877 1.00 20.64 ? 238  PRO   A HG3  1 
ATOM   3686  H  HD2  . PRO   A 1 238 ? 8.775  28.197  36.474 1.00 20.26 ? 238  PRO   A HD2  1 
ATOM   3687  H  HD3  . PRO   A 1 238 ? 10.154 28.845  36.807 1.00 20.26 ? 238  PRO   A HD3  1 
ATOM   3688  N  N    . THR   A 1 239 ? 9.718  24.380  38.013 1.00 14.73 ? 239  THR   A N    1 
ATOM   3689  C  CA   . THR   A 1 239 ? 9.500  22.944  38.322 1.00 13.55 ? 239  THR   A CA   1 
ATOM   3690  C  C    . THR   A 1 239 ? 10.054 22.027  37.227 1.00 12.90 ? 239  THR   A C    1 
ATOM   3691  O  O    . THR   A 1 239 ? 10.701 21.032  37.579 1.00 14.79 ? 239  THR   A O    1 
ATOM   3692  C  CB   . THR   A 1 239 ? 8.000  22.666  38.505 1.00 15.48 ? 239  THR   A CB   1 
ATOM   3693  O  OG1  . THR   A 1 239 ? 7.472  23.579  39.467 1.00 16.61 ? 239  THR   A OG1  1 
ATOM   3694  C  CG2  . THR   A 1 239 ? 7.713  21.243  38.930 1.00 18.95 ? 239  THR   A CG2  1 
ATOM   3695  H  H    . THR   A 1 239 ? 9.027  24.797  37.715 1.00 17.68 ? 239  THR   A H    1 
ATOM   3696  H  HA   . THR   A 1 239 ? 9.978  22.752  39.144 1.00 16.27 ? 239  THR   A HA   1 
ATOM   3697  H  HB   . THR   A 1 239 ? 7.571  22.790  37.644 1.00 18.58 ? 239  THR   A HB   1 
ATOM   3698  H  HG1  . THR   A 1 239 ? 7.247  24.292  39.083 1.00 19.94 ? 239  THR   A HG1  1 
ATOM   3699  H  HG21 . THR   A 1 239 ? 6.756  21.122  39.031 1.00 22.74 ? 239  THR   A HG21 1 
ATOM   3700  H  HG22 . THR   A 1 239 ? 8.047  20.630  38.256 1.00 22.74 ? 239  THR   A HG22 1 
ATOM   3701  H  HG23 . THR   A 1 239 ? 8.152  21.063  39.776 1.00 22.74 ? 239  THR   A HG23 1 
ATOM   3702  N  N    . TYR   A 1 240 ? 9.828  22.355  35.950 1.00 14.23 ? 240  TYR   A N    1 
ATOM   3703  C  CA   . TYR   A 1 240 ? 10.200 21.407  34.863 1.00 15.69 ? 240  TYR   A CA   1 
ATOM   3704  C  C    . TYR   A 1 240 ? 11.291 21.950  33.931 1.00 15.81 ? 240  TYR   A C    1 
ATOM   3705  O  O    . TYR   A 1 240 ? 11.801 21.163  33.119 1.00 14.02 ? 240  TYR   A O    1 
ATOM   3706  C  CB   . TYR   A 1 240 ? 8.947  21.048  34.061 1.00 15.89 ? 240  TYR   A CB   1 
ATOM   3707  C  CG   . TYR   A 1 240 ? 7.849  20.461  34.909 1.00 17.22 ? 240  TYR   A CG   1 
ATOM   3708  C  CD1  . TYR   A 1 240 ? 7.989  19.207  35.473 1.00 17.75 ? 240  TYR   A CD1  1 
ATOM   3709  C  CD2  . TYR   A 1 240 ? 6.689  21.168  35.172 1.00 17.50 ? 240  TYR   A CD2  1 
ATOM   3710  C  CE1  . TYR   A 1 240 ? 6.997  18.659  36.267 1.00 20.08 ? 240  TYR   A CE1  1 
ATOM   3711  C  CE2  . TYR   A 1 240 ? 5.685  20.634  35.963 1.00 19.38 ? 240  TYR   A CE2  1 
ATOM   3712  C  CZ   . TYR   A 1 240 ? 5.840  19.373  36.511 1.00 21.62 ? 240  TYR   A CZ   1 
ATOM   3713  O  OH   . TYR   A 1 240 ? 4.858  18.827  37.297 1.00 24.07 ? 240  TYR   A OH   1 
ATOM   3714  H  H    . TYR   A 1 240 ? 9.473  23.093  35.688 1.00 17.08 ? 240  TYR   A H    1 
ATOM   3715  H  HA   . TYR   A 1 240 ? 10.574 20.617  35.283 1.00 18.83 ? 240  TYR   A HA   1 
ATOM   3716  H  HB2  . TYR   A 1 240 ? 8.615  21.844  33.617 1.00 19.07 ? 240  TYR   A HB2  1 
ATOM   3717  H  HB3  . TYR   A 1 240 ? 9.185  20.414  33.366 1.00 19.07 ? 240  TYR   A HB3  1 
ATOM   3718  H  HD1  . TYR   A 1 240 ? 8.766  18.721  35.316 1.00 21.30 ? 240  TYR   A HD1  1 
ATOM   3719  H  HD2  . TYR   A 1 240 ? 6.581  22.018  34.811 1.00 21.00 ? 240  TYR   A HD2  1 
ATOM   3720  H  HE1  . TYR   A 1 240 ? 7.109  17.812  36.635 1.00 24.10 ? 240  TYR   A HE1  1 
ATOM   3721  H  HE2  . TYR   A 1 240 ? 4.910  21.121  36.125 1.00 23.26 ? 240  TYR   A HE2  1 
ATOM   3722  H  HH   . TYR   A 1 240 ? 5.208  18.334  37.880 1.00 28.89 ? 240  TYR   A HH   1 
ATOM   3723  N  N    . GLY   A 1 241 ? 11.630 23.232  34.053 1.00 15.09 ? 241  GLY   A N    1 
ATOM   3724  C  CA   . GLY   A 1 241 ? 12.658 23.836  33.184 1.00 13.79 ? 241  GLY   A CA   1 
ATOM   3725  C  C    . GLY   A 1 241 ? 12.154 24.058  31.768 1.00 13.81 ? 241  GLY   A C    1 
ATOM   3726  O  O    . GLY   A 1 241 ? 10.954 23.859  31.534 1.00 14.72 ? 241  GLY   A O    1 
ATOM   3727  H  H    . GLY   A 1 241 ? 11.283 23.771  34.626 1.00 18.11 ? 241  GLY   A H    1 
ATOM   3728  H  HA2  . GLY   A 1 241 ? 12.941 24.684  33.561 1.00 16.56 ? 241  GLY   A HA2  1 
ATOM   3729  H  HA3  . GLY   A 1 241 ? 13.439 23.261  33.161 1.00 16.56 ? 241  GLY   A HA3  1 
ATOM   3730  N  N    . THR   A 1 242 ? 13.036 24.496  30.865 1.00 10.38 ? 242  THR   A N    1 
ATOM   3731  C  CA   . THR   A 1 242 ? 12.602 24.618  29.476 1.00 11.08 ? 242  THR   A CA   1 
ATOM   3732  C  C    . THR   A 1 242 ? 12.080 23.287  28.959 1.00 12.36 ? 242  THR   A C    1 
ATOM   3733  O  O    . THR   A 1 242 ? 11.269 23.260  28.024 1.00 12.41 ? 242  THR   A O    1 
ATOM   3734  C  CB   . THR   A 1 242 ? 13.739 25.111  28.583 1.00 12.02 ? 242  THR   A CB   1 
ATOM   3735  O  OG1  . THR   A 1 242 ? 14.837 24.195  28.651 1.00 9.69  ? 242  THR   A OG1  1 
ATOM   3736  C  CG2  . THR   A 1 242 ? 14.206 26.512  29.020 1.00 13.06 ? 242  THR   A CG2  1 
ATOM   3737  H  H    . THR   A 1 242 ? 13.851 24.717  31.026 1.00 12.45 ? 242  THR   A H    1 
ATOM   3738  H  HA   . THR   A 1 242 ? 11.885 25.271  29.449 1.00 13.30 ? 242  THR   A HA   1 
ATOM   3739  H  HB   . THR   A 1 242 ? 13.414 25.164  27.670 1.00 14.42 ? 242  THR   A HB   1 
ATOM   3740  H  HG1  . THR   A 1 242 ? 15.533 24.608  28.876 1.00 11.63 ? 242  THR   A HG1  1 
ATOM   3741  H  HG21 . THR   A 1 242 ? 14.927 26.808  28.442 1.00 15.68 ? 242  THR   A HG21 1 
ATOM   3742  H  HG22 . THR   A 1 242 ? 13.465 27.135  28.956 1.00 15.68 ? 242  THR   A HG22 1 
ATOM   3743  H  HG23 . THR   A 1 242 ? 14.520 26.477  29.937 1.00 15.68 ? 242  THR   A HG23 1 
ATOM   3744  N  N    . ALA   A 1 243 ? 12.527 22.182  29.568 1.00 9.05  ? 243  ALA   A N    1 
ATOM   3745  C  CA   . ALA   A 1 243 ? 12.089 20.826  29.255 1.00 9.90  ? 243  ALA   A CA   1 
ATOM   3746  C  C    . ALA   A 1 243 ? 10.578 20.662  29.333 1.00 12.74 ? 243  ALA   A C    1 
ATOM   3747  O  O    . ALA   A 1 243 ? 10.022 19.684  28.814 1.00 12.64 ? 243  ALA   A O    1 
ATOM   3748  C  CB   . ALA   A 1 243 ? 12.778 19.834  30.201 1.00 9.48  ? 243  ALA   A CB   1 
ATOM   3749  H  H    . ALA   A 1 243 ? 13.114 22.208  30.196 1.00 10.86 ? 243  ALA   A H    1 
ATOM   3750  H  HA   . ALA   A 1 243 ? 12.342 20.644  28.337 1.00 11.88 ? 243  ALA   A HA   1 
ATOM   3751  H  HB1  . ALA   A 1 243 ? 12.487 18.932  29.993 1.00 11.38 ? 243  ALA   A HB1  1 
ATOM   3752  H  HB2  . ALA   A 1 243 ? 13.740 19.896  30.091 1.00 11.38 ? 243  ALA   A HB2  1 
ATOM   3753  H  HB3  . ALA   A 1 243 ? 12.544 20.045  31.118 1.00 11.38 ? 243  ALA   A HB3  1 
ATOM   3754  N  N    . ILE   A 1 244 ? 9.897  21.616  29.972 1.00 11.83 ? 244  ILE   A N    1 
ATOM   3755  C  CA   . ILE   A 1 244 ? 8.436  21.612  29.973 1.00 12.14 ? 244  ILE   A CA   1 
ATOM   3756  C  C    . ILE   A 1 244 ? 7.876  21.604  28.553 1.00 12.85 ? 244  ILE   A C    1 
ATOM   3757  O  O    . ILE   A 1 244 ? 6.751  21.139  28.325 1.00 12.74 ? 244  ILE   A O    1 
ATOM   3758  C  CB   . ILE   A 1 244 ? 7.922  22.829  30.779 1.00 13.13 ? 244  ILE   A CB   1 
ATOM   3759  C  CG1  . ILE   A 1 244 ? 6.438  22.671  31.122 1.00 16.74 ? 244  ILE   A CG1  1 
ATOM   3760  C  CG2  . ILE   A 1 244 ? 8.180  24.145  30.019 1.00 14.74 ? 244  ILE   A CG2  1 
ATOM   3761  C  CD1  . ILE   A 1 244 ? 5.888  23.818  31.948 1.00 16.72 ? 244  ILE   A CD1  1 
ATOM   3762  H  H    . ILE   A 1 244 ? 10.258 22.265  30.405 1.00 14.20 ? 244  ILE   A H    1 
ATOM   3763  H  HA   . ILE   A 1 244 ? 8.124  20.798  30.399 1.00 14.57 ? 244  ILE   A HA   1 
ATOM   3764  H  HB   . ILE   A 1 244 ? 8.417  22.867  31.612 1.00 15.76 ? 244  ILE   A HB   1 
ATOM   3765  H  HG12 . ILE   A 1 244 ? 5.928  22.599  30.300 1.00 20.09 ? 244  ILE   A HG12 1 
ATOM   3766  H  HG13 . ILE   A 1 244 ? 6.311  21.841  31.608 1.00 20.09 ? 244  ILE   A HG13 1 
ATOM   3767  H  HG21 . ILE   A 1 244 ? 7.850  24.892  30.543 1.00 17.70 ? 244  ILE   A HG21 1 
ATOM   3768  H  HG22 . ILE   A 1 244 ? 9.133  24.251  29.870 1.00 17.70 ? 244  ILE   A HG22 1 
ATOM   3769  H  HG23 . ILE   A 1 244 ? 7.720  24.121  29.165 1.00 17.70 ? 244  ILE   A HG23 1 
ATOM   3770  H  HD11 . ILE   A 1 244 ? 4.949  23.663  32.133 1.00 20.07 ? 244  ILE   A HD11 1 
ATOM   3771  H  HD12 . ILE   A 1 244 ? 6.376  23.878  32.784 1.00 20.07 ? 244  ILE   A HD12 1 
ATOM   3772  H  HD13 . ILE   A 1 244 ? 5.987  24.648  31.456 1.00 20.07 ? 244  ILE   A HD13 1 
ATOM   3773  N  N    . LEU   A 1 245 ? 8.662  22.040  27.568 1.00 10.00 ? 245  LEU   A N    1 
ATOM   3774  C  CA   . LEU   A 1 245 ? 8.127  22.177  26.184 1.00 11.36 ? 245  LEU   A CA   1 
ATOM   3775  C  C    . LEU   A 1 245 ? 7.979  20.833  25.460 1.00 11.41 ? 245  LEU   A C    1 
ATOM   3776  O  O    . LEU   A 1 245 ? 7.253  20.799  24.457 1.00 11.77 ? 245  LEU   A O    1 
ATOM   3777  C  CB   . LEU   A 1 245 ? 9.081  23.084  25.399 1.00 12.01 ? 245  LEU   A CB   1 
ATOM   3778  C  CG   . LEU   A 1 245 ? 9.045  24.561  25.785 1.00 11.94 ? 245  LEU   A CG   1 
ATOM   3779  C  CD1  . LEU   A 1 245 ? 10.346 25.247  25.401 1.00 11.34 ? 245  LEU   A CD1  1 
ATOM   3780  C  CD2  . LEU   A 1 245 ? 7.862  25.261  25.137 1.00 13.84 ? 245  LEU   A CD2  1 
ATOM   3781  H  H    . LEU   A 1 245 ? 9.488  22.260  27.663 1.00 12.01 ? 245  LEU   A H    1 
ATOM   3782  H  HA   . LEU   A 1 245 ? 7.236  22.556  26.240 1.00 13.63 ? 245  LEU   A HA   1 
ATOM   3783  H  HB2  . LEU   A 1 245 ? 9.986  22.756  25.518 1.00 14.42 ? 245  LEU   A HB2  1 
ATOM   3784  H  HB3  . LEU   A 1 245 ? 8.873  23.007  24.455 1.00 14.42 ? 245  LEU   A HB3  1 
ATOM   3785  H  HG   . LEU   A 1 245 ? 8.941  24.618  26.748 1.00 14.33 ? 245  LEU   A HG   1 
ATOM   3786  H  HD11 . LEU   A 1 245 ? 10.305 26.183  25.653 1.00 13.61 ? 245  LEU   A HD11 1 
ATOM   3787  H  HD12 . LEU   A 1 245 ? 11.085 24.820  25.862 1.00 13.61 ? 245  LEU   A HD12 1 
ATOM   3788  H  HD13 . LEU   A 1 245 ? 10.479 25.176  24.443 1.00 13.61 ? 245  LEU   A HD13 1 
ATOM   3789  H  HD21 . LEU   A 1 245 ? 7.858  26.196  25.395 1.00 16.61 ? 245  LEU   A HD21 1 
ATOM   3790  H  HD22 . LEU   A 1 245 ? 7.934  25.192  24.172 1.00 16.61 ? 245  LEU   A HD22 1 
ATOM   3791  H  HD23 . LEU   A 1 245 ? 7.038  24.842  25.430 1.00 16.61 ? 245  LEU   A HD23 1 
ATOM   3792  N  N    . VAL   A 1 246 ? 8.638  19.775  25.929 1.00 11.61 ? 246  VAL   A N    1 
ATOM   3793  C  CA   . VAL   A 1 246 ? 8.632  18.490  25.166 1.00 12.56 ? 246  VAL   A CA   1 
ATOM   3794  C  C    . VAL   A 1 246 ? 7.193  18.077  24.839 1.00 11.46 ? 246  VAL   A C    1 
ATOM   3795  O  O    . VAL   A 1 246 ? 6.866  17.968  23.652 1.00 11.05 ? 246  VAL   A O    1 
ATOM   3796  C  CB   . VAL   A 1 246 ? 9.364  17.376  25.939 1.00 11.86 ? 246  VAL   A CB   1 
ATOM   3797  C  CG1  . VAL   A 1 246 ? 9.109  16.006  25.331 1.00 15.18 ? 246  VAL   A CG1  1 
ATOM   3798  C  CG2  . VAL   A 1 246 ? 10.857 17.646  26.041 1.00 11.26 ? 246  VAL   A CG2  1 
ATOM   3799  H  H    . VAL   A 1 246 ? 9.086  19.762  26.663 1.00 13.94 ? 246  VAL   A H    1 
ATOM   3800  H  HA   . VAL   A 1 246 ? 9.111  18.628  24.334 1.00 15.08 ? 246  VAL   A HA   1 
ATOM   3801  H  HB   . VAL   A 1 246 ? 8.999  17.377  26.838 1.00 14.23 ? 246  VAL   A HB   1 
ATOM   3802  H  HG11 . VAL   A 1 246 ? 9.584  15.332  25.842 1.00 18.22 ? 246  VAL   A HG11 1 
ATOM   3803  H  HG12 . VAL   A 1 246 ? 8.158  15.815  25.350 1.00 18.22 ? 246  VAL   A HG12 1 
ATOM   3804  H  HG13 . VAL   A 1 246 ? 9.422  15.996  24.413 1.00 18.22 ? 246  VAL   A HG13 1 
ATOM   3805  H  HG21 . VAL   A 1 246 ? 11.283 16.926  26.532 1.00 13.51 ? 246  VAL   A HG21 1 
ATOM   3806  H  HG22 . VAL   A 1 246 ? 11.238 17.699  25.151 1.00 13.51 ? 246  VAL   A HG22 1 
ATOM   3807  H  HG23 . VAL   A 1 246 ? 11.003 18.485  26.505 1.00 13.51 ? 246  VAL   A HG23 1 
ATOM   3808  N  N    . ASN   A 1 247 ? 6.377  17.872  25.868 1.00 12.06 ? 247  ASN   A N    1 
ATOM   3809  C  CA   . ASN   A 1 247 ? 5.000  17.360  25.631 1.00 14.42 ? 247  ASN   A CA   1 
ATOM   3810  C  C    . ASN   A 1 247 ? 4.146  18.419  24.927 1.00 13.55 ? 247  ASN   A C    1 
ATOM   3811  O  O    . ASN   A 1 247 ? 3.249  18.038  24.177 1.00 13.25 ? 247  ASN   A O    1 
ATOM   3812  C  CB   . ASN   A 1 247 ? 4.360  16.862  26.930 1.00 17.16 ? 247  ASN   A CB   1 
ATOM   3813  C  CG   . ASN   A 1 247 ? 4.984  15.572  27.421 1.00 17.95 ? 247  ASN   A CG   1 
ATOM   3814  O  OD1  . ASN   A 1 247 ? 5.500  14.788  26.630 1.00 19.16 ? 247  ASN   A OD1  1 
ATOM   3815  N  ND2  . ASN   A 1 247 ? 4.947  15.344  28.723 1.00 20.40 ? 247  ASN   A ND2  1 
ATOM   3816  H  H    . ASN   A 1 247 ? 6.579  18.014  26.692 1.00 14.47 ? 247  ASN   A H    1 
ATOM   3817  H  HA   . ASN   A 1 247 ? 5.054  16.593  25.039 1.00 17.31 ? 247  ASN   A HA   1 
ATOM   3818  H  HB2  . ASN   A 1 247 ? 4.450  17.543  27.614 1.00 20.60 ? 247  ASN   A HB2  1 
ATOM   3819  H  HB3  . ASN   A 1 247 ? 3.410  16.726  26.789 1.00 20.60 ? 247  ASN   A HB3  1 
ATOM   3820  H  HD21 . ASN   A 1 247 ? 5.293  14.625  29.044 1.00 24.48 ? 247  ASN   A HD21 1 
ATOM   3821  H  HD22 . ASN   A 1 247 ? 4.577  15.915  29.249 1.00 24.48 ? 247  ASN   A HD22 1 
ATOM   3822  N  N    . ILE   A 1 248 ? 4.420  19.698  25.182 1.00 15.28 ? 248  ILE   A N    1 
ATOM   3823  C  CA   . ILE   A 1 248 ? 3.616  20.792  24.563 1.00 15.42 ? 248  ILE   A CA   1 
ATOM   3824  C  C    . ILE   A 1 248 ? 3.833  20.767  23.046 1.00 13.74 ? 248  ILE   A C    1 
ATOM   3825  O  O    . ILE   A 1 248 ? 2.844  20.709  22.299 1.00 14.45 ? 248  ILE   A O    1 
ATOM   3826  C  CB   . ILE   A 1 248 ? 3.998  22.155  25.178 1.00 13.82 ? 248  ILE   A CB   1 
ATOM   3827  C  CG1  . ILE   A 1 248 ? 3.664  22.206  26.670 1.00 14.54 ? 248  ILE   A CG1  1 
ATOM   3828  C  CG2  . ILE   A 1 248 ? 3.342  23.293  24.414 1.00 16.50 ? 248  ILE   A CG2  1 
ATOM   3829  C  CD1  . ILE   A 1 248 ? 4.053  23.501  27.339 1.00 15.41 ? 248  ILE   A CD1  1 
ATOM   3830  H  H    . ILE   A 1 248 ? 5.053  19.965  25.699 1.00 18.34 ? 248  ILE   A H    1 
ATOM   3831  H  HA   . ILE   A 1 248 ? 2.672  20.656  24.742 1.00 18.51 ? 248  ILE   A HA   1 
ATOM   3832  H  HB   . ILE   A 1 248 ? 4.959  22.263  25.099 1.00 16.59 ? 248  ILE   A HB   1 
ATOM   3833  H  HG12 . ILE   A 1 248 ? 2.711  22.067  26.784 1.00 17.45 ? 248  ILE   A HG12 1 
ATOM   3834  H  HG13 . ILE   A 1 248 ? 4.113  21.473  27.118 1.00 17.45 ? 248  ILE   A HG13 1 
ATOM   3835  H  HG21 . ILE   A 1 248 ? 3.594  24.140  24.815 1.00 19.81 ? 248  ILE   A HG21 1 
ATOM   3836  H  HG22 . ILE   A 1 248 ? 3.635  23.274  23.490 1.00 19.81 ? 248  ILE   A HG22 1 
ATOM   3837  H  HG23 . ILE   A 1 248 ? 2.378  23.193  24.449 1.00 19.81 ? 248  ILE   A HG23 1 
ATOM   3838  H  HD11 . ILE   A 1 248 ? 3.814  23.465  28.278 1.00 18.49 ? 248  ILE   A HD11 1 
ATOM   3839  H  HD12 . ILE   A 1 248 ? 5.010  23.634  27.254 1.00 18.49 ? 248  ILE   A HD12 1 
ATOM   3840  H  HD13 . ILE   A 1 248 ? 3.586  24.238  26.915 1.00 18.49 ? 248  ILE   A HD13 1 
ATOM   3841  N  N    . ILE   A 1 249 ? 5.094  20.824  22.619 1.00 13.10 ? 249  ILE   A N    1 
ATOM   3842  C  CA   . ILE   A 1 249 ? 5.388  20.870  21.160 1.00 10.64 ? 249  ILE   A CA   1 
ATOM   3843  C  C    . ILE   A 1 249 ? 4.956  19.541  20.519 1.00 12.11 ? 249  ILE   A C    1 
ATOM   3844  O  O    . ILE   A 1 249 ? 4.418  19.571  19.406 1.00 12.15 ? 249  ILE   A O    1 
ATOM   3845  C  CB   . ILE   A 1 249 ? 6.878  21.185  20.925 1.00 12.22 ? 249  ILE   A CB   1 
ATOM   3846  C  CG1  . ILE   A 1 249 ? 7.302  22.471  21.638 1.00 12.06 ? 249  ILE   A CG1  1 
ATOM   3847  C  CG2  . ILE   A 1 249 ? 7.193  21.236  19.439 1.00 12.15 ? 249  ILE   A CG2  1 
ATOM   3848  C  CD1  . ILE   A 1 249 ? 6.390  23.645  21.370 1.00 11.08 ? 249  ILE   A CD1  1 
ATOM   3849  H  H    . ILE   A 1 249 ? 5.785  20.837  23.131 1.00 15.72 ? 249  ILE   A H    1 
ATOM   3850  H  HA   . ILE   A 1 249 ? 4.884  21.583  20.737 1.00 12.77 ? 249  ILE   A HA   1 
ATOM   3851  H  HB   . ILE   A 1 249 ? 7.398  20.464  21.312 1.00 14.66 ? 249  ILE   A HB   1 
ATOM   3852  H  HG12 . ILE   A 1 249 ? 7.332  22.307  22.594 1.00 14.47 ? 249  ILE   A HG12 1 
ATOM   3853  H  HG13 . ILE   A 1 249 ? 8.203  22.702  21.362 1.00 14.47 ? 249  ILE   A HG13 1 
ATOM   3854  H  HG21 . ILE   A 1 249 ? 8.134  21.435  19.314 1.00 14.58 ? 249  ILE   A HG21 1 
ATOM   3855  H  HG22 . ILE   A 1 249 ? 6.988  20.378  19.035 1.00 14.58 ? 249  ILE   A HG22 1 
ATOM   3856  H  HG23 . ILE   A 1 249 ? 6.658  21.927  19.018 1.00 14.58 ? 249  ILE   A HG23 1 
ATOM   3857  H  HD11 . ILE   A 1 249 ? 6.715  24.423  21.850 1.00 13.30 ? 249  ILE   A HD11 1 
ATOM   3858  H  HD12 . ILE   A 1 249 ? 6.377  23.834  20.419 1.00 13.30 ? 249  ILE   A HD12 1 
ATOM   3859  H  HD13 . ILE   A 1 249 ? 5.492  23.432  21.669 1.00 13.30 ? 249  ILE   A HD13 1 
ATOM   3860  N  N    . ASN   A 1 250 ? 5.189  18.419  21.201 1.00 11.56 ? 250  ASN   A N    1 
ATOM   3861  C  CA   . ASN   A 1 250 ? 4.782  17.096  20.654 1.00 11.51 ? 250  ASN   A CA   1 
ATOM   3862  C  C    . ASN   A 1 250 ? 3.256  17.023  20.501 1.00 16.56 ? 250  ASN   A C    1 
ATOM   3863  O  O    . ASN   A 1 250 ? 2.797  16.494  19.476 1.00 14.69 ? 250  ASN   A O    1 
ATOM   3864  C  CB   . ASN   A 1 250 ? 5.304  15.927  21.495 1.00 12.29 ? 250  ASN   A CB   1 
ATOM   3865  C  CG   . ASN   A 1 250 ? 5.140  14.589  20.807 1.00 15.27 ? 250  ASN   A CG   1 
ATOM   3866  O  OD1  . ASN   A 1 250 ? 5.678  14.371  19.726 1.00 13.50 ? 250  ASN   A OD1  1 
ATOM   3867  N  ND2  . ASN   A 1 250 ? 4.400  13.687  21.430 1.00 16.13 ? 250  ASN   A ND2  1 
ATOM   3868  H  H    . ASN   A 1 250 ? 5.574  18.389  21.970 1.00 13.88 ? 250  ASN   A H    1 
ATOM   3869  H  HA   . ASN   A 1 250 ? 5.189  17.012  19.778 1.00 13.81 ? 250  ASN   A HA   1 
ATOM   3870  H  HB2  . ASN   A 1 250 ? 6.243  16.071  21.694 1.00 14.75 ? 250  ASN   A HB2  1 
ATOM   3871  H  HB3  . ASN   A 1 250 ? 4.834  15.909  22.343 1.00 14.75 ? 250  ASN   A HB3  1 
ATOM   3872  H  HD21 . ASN   A 1 250 ? 4.280  12.911  21.078 1.00 19.35 ? 250  ASN   A HD21 1 
ATOM   3873  H  HD22 . ASN   A 1 250 ? 4.038  13.876  22.187 1.00 19.35 ? 250  ASN   A HD22 1 
ATOM   3874  N  N    . GLU   A 1 251 ? 2.506  17.515  21.488 1.00 17.12 ? 251  GLU   A N    1 
ATOM   3875  C  CA   . GLU   A 1 251 ? 1.021  17.405  21.427 1.00 15.48 ? 251  GLU   A CA   1 
ATOM   3876  C  C    . GLU   A 1 251 ? 0.470  18.232  20.258 1.00 15.61 ? 251  GLU   A C    1 
ATOM   3877  O  O    . GLU   A 1 251 ? -0.637 17.925  19.802 1.00 15.04 ? 251  GLU   A O    1 
ATOM   3878  C  CB   . GLU   A 1 251 ? 0.394  17.823  22.756 1.00 19.37 ? 251  GLU   A CB   1 
ATOM   3879  C  CG   . GLU   A 1 251 ? 0.325  16.692  23.766 1.00 32.48 ? 251  GLU   A CG   1 
ATOM   3880  C  CD   . GLU   A 1 251 ? -0.102 17.122  25.159 1.00 37.62 ? 251  GLU   A CD   1 
ATOM   3881  O  OE1  . GLU   A 1 251 ? -0.868 18.098  25.262 1.00 33.06 ? 251  GLU   A OE1  1 
ATOM   3882  O  OE2  . GLU   A 1 251 ? 0.338  16.482  26.134 1.00 37.22 ? 251  GLU   A OE2  1 
ATOM   3883  H  H    . GLU   A 1 251 ? 2.814  17.908  22.188 1.00 20.55 ? 251  GLU   A H    1 
ATOM   3884  H  HA   . GLU   A 1 251 ? 0.784  16.478  21.271 1.00 18.58 ? 251  GLU   A HA   1 
ATOM   3885  H  HB2  . GLU   A 1 251 ? 0.907  18.555  23.133 1.00 23.24 ? 251  GLU   A HB2  1 
ATOM   3886  H  HB3  . GLU   A 1 251 ? -0.501 18.159  22.593 1.00 23.24 ? 251  GLU   A HB3  1 
ATOM   3887  H  HG2  . GLU   A 1 251 ? -0.296 16.021  23.442 1.00 38.98 ? 251  GLU   A HG2  1 
ATOM   3888  H  HG3  . GLU   A 1 251 ? 1.196  16.269  23.822 1.00 38.98 ? 251  GLU   A HG3  1 
ATOM   3889  N  N    . ASN   A 1 252 ? 1.218  19.236  19.795 1.00 12.71 ? 252  ASN   A N    1 
ATOM   3890  C  CA   . ASN   A 1 252 ? 0.786  20.074  18.640 1.00 14.91 ? 252  ASN   A CA   1 
ATOM   3891  C  C    . ASN   A 1 252 ? 1.281  19.458  17.324 1.00 14.49 ? 252  ASN   A C    1 
ATOM   3892  O  O    . ASN   A 1 252 ? 0.965  20.014  16.268 1.00 16.70 ? 252  ASN   A O    1 
ATOM   3893  C  CB   . ASN   A 1 252 ? 1.255  21.526  18.786 1.00 16.80 ? 252  ASN   A CB   1 
ATOM   3894  C  CG   . ASN   A 1 252 ? 0.413  22.334  19.750 1.00 19.39 ? 252  ASN   A CG   1 
ATOM   3895  O  OD1  . ASN   A 1 252 ? -0.612 22.891  19.366 1.00 22.44 ? 252  ASN   A OD1  1 
ATOM   3896  N  ND2  . ASN   A 1 252 ? 0.841  22.414  20.998 1.00 16.27 ? 252  ASN   A ND2  1 
ATOM   3897  H  H    . ASN   A 1 252 ? 1.980  19.458  20.127 1.00 15.26 ? 252  ASN   A H    1 
ATOM   3898  H  HA   . ASN   A 1 252 ? -0.184 20.091  18.627 1.00 17.90 ? 252  ASN   A HA   1 
ATOM   3899  H  HB2  . ASN   A 1 252 ? 2.177  21.533  19.088 1.00 20.17 ? 252  ASN   A HB2  1 
ATOM   3900  H  HB3  . ASN   A 1 252 ? 1.239  21.954  17.915 1.00 20.17 ? 252  ASN   A HB3  1 
ATOM   3901  H  HD21 . ASN   A 1 252 ? 0.397  22.870  21.577 1.00 19.52 ? 252  ASN   A HD21 1 
ATOM   3902  H  HD22 . ASN   A 1 252 ? 1.564  22.011  21.231 1.00 19.52 ? 252  ASN   A HD22 1 
ATOM   3903  N  N    . GLY   A 1 253 ? 2.034  18.360  17.392 1.00 13.28 ? 253  GLY   A N    1 
ATOM   3904  C  CA   . GLY   A 1 253 ? 2.479  17.665  16.169 1.00 13.53 ? 253  GLY   A CA   1 
ATOM   3905  C  C    . GLY   A 1 253 ? 3.528  18.442  15.394 1.00 11.98 ? 253  GLY   A C    1 
ATOM   3906  O  O    . GLY   A 1 253 ? 3.557  18.323  14.166 1.00 10.62 ? 253  GLY   A O    1 
ATOM   3907  H  H    . GLY   A 1 253 ? 2.299  18.000  18.127 1.00 15.93 ? 253  GLY   A H    1 
ATOM   3908  H  HA2  . GLY   A 1 253 ? 2.839  16.797  16.409 1.00 16.24 ? 253  GLY   A HA2  1 
ATOM   3909  H  HA3  . GLY   A 1 253 ? 1.713  17.506  15.596 1.00 16.24 ? 253  GLY   A HA3  1 
ATOM   3910  N  N    . VAL   A 1 254 ? 4.367  19.201  16.103 1.00 11.76 ? 254  VAL   A N    1 
ATOM   3911  C  CA   . VAL   A 1 254 ? 5.433  20.014  15.447 1.00 10.84 ? 254  VAL   A CA   1 
ATOM   3912  C  C    . VAL   A 1 254 ? 6.762  19.739  16.163 1.00 10.98 ? 254  VAL   A C    1 
ATOM   3913  O  O    . VAL   A 1 254 ? 7.612  20.637  16.190 1.00 11.40 ? 254  VAL   A O    1 
ATOM   3914  C  CB   . VAL   A 1 254 ? 5.075  21.511  15.447 1.00 12.47 ? 254  VAL   A CB   1 
ATOM   3915  C  CG1  . VAL   A 1 254 ? 4.099  21.839  14.328 1.00 12.67 ? 254  VAL   A CG1  1 
ATOM   3916  C  CG2  . VAL   A 1 254 ? 4.511  21.953  16.787 1.00 12.99 ? 254  VAL   A CG2  1 
ATOM   3917  H  H    . VAL   A 1 254 ? 4.346  19.267  16.960 1.00 14.12 ? 254  VAL   A H    1 
ATOM   3918  H  HA   . VAL   A 1 254 ? 5.516  19.758  14.515 1.00 13.01 ? 254  VAL   A HA   1 
ATOM   3919  H  HB   . VAL   A 1 254 ? 5.897  22.002  15.293 1.00 14.97 ? 254  VAL   A HB   1 
ATOM   3920  H  HG11 . VAL   A 1 254 ? 3.889  22.786  14.349 1.00 15.20 ? 254  VAL   A HG11 1 
ATOM   3921  H  HG12 . VAL   A 1 254 ? 4.499  21.616  13.473 1.00 15.20 ? 254  VAL   A HG12 1 
ATOM   3922  H  HG13 . VAL   A 1 254 ? 3.285  21.325  14.447 1.00 15.20 ? 254  VAL   A HG13 1 
ATOM   3923  H  HG21 . VAL   A 1 254 ? 4.297  22.898  16.752 1.00 15.59 ? 254  VAL   A HG21 1 
ATOM   3924  H  HG22 . VAL   A 1 254 ? 3.707  21.447  16.983 1.00 15.59 ? 254  VAL   A HG22 1 
ATOM   3925  H  HG23 . VAL   A 1 254 ? 5.169  21.796  17.483 1.00 15.59 ? 254  VAL   A HG23 1 
ATOM   3926  N  N    . HIS   A 1 255 ? 6.905  18.539  16.726 1.00 11.27 ? 255  HIS   A N    1 
ATOM   3927  C  CA   . HIS   A 1 255 ? 8.169  18.139  17.398 1.00 11.09 ? 255  HIS   A CA   1 
ATOM   3928  C  C    . HIS   A 1 255 ? 8.968  17.306  16.398 1.00 10.76 ? 255  HIS   A C    1 
ATOM   3929  O  O    . HIS   A 1 255 ? 8.577  16.165  16.110 1.00 10.01 ? 255  HIS   A O    1 
ATOM   3930  C  CB   . HIS   A 1 255 ? 7.848  17.383  18.689 1.00 11.47 ? 255  HIS   A CB   1 
ATOM   3931  C  CG   . HIS   A 1 255 ? 9.044  16.943  19.461 1.00 10.75 ? 255  HIS   A CG   1 
ATOM   3932  N  ND1  . HIS   A 1 255 ? 9.792  17.805  20.232 1.00 13.76 ? 255  HIS   A ND1  1 
ATOM   3933  C  CD2  . HIS   A 1 255 ? 9.613  15.740  19.591 1.00 12.19 ? 255  HIS   A CD2  1 
ATOM   3934  C  CE1  . HIS   A 1 255 ? 10.782 17.134  20.800 1.00 12.43 ? 255  HIS   A CE1  1 
ATOM   3935  N  NE2  . HIS   A 1 255 ? 10.691 15.878  20.426 1.00 11.80 ? 255  HIS   A NE2  1 
ATOM   3936  H  H    . HIS   A 1 255 ? 6.291  17.937  16.736 1.00 13.52 ? 255  HIS   A H    1 
ATOM   3937  H  HA   . HIS   A 1 255 ? 8.703  18.905  17.660 1.00 13.31 ? 255  HIS   A HA   1 
ATOM   3938  H  HB2  . HIS   A 1 255 ? 7.302  17.951  19.256 1.00 13.77 ? 255  HIS   A HB2  1 
ATOM   3939  H  HB3  . HIS   A 1 255 ? 7.314  16.604  18.470 1.00 13.77 ? 255  HIS   A HB3  1 
ATOM   3940  H  HD1  . HIS   A 1 255 ? 9.640  18.646  20.329 1.00 16.51 ? 255  HIS   A HD1  1 
ATOM   3941  H  HD2  . HIS   A 1 255 ? 9.329  14.952  19.188 1.00 14.63 ? 255  HIS   A HD2  1 
ATOM   3942  H  HE1  . HIS   A 1 255 ? 11.429 17.490  21.365 1.00 14.91 ? 255  HIS   A HE1  1 
ATOM   3943  N  N    . PRO   A 1 256 ? 10.081 17.825  15.844 1.00 11.14 ? 256  PRO   A N    1 
ATOM   3944  C  CA   . PRO   A 1 256 ? 10.800 17.116  14.785 1.00 12.80 ? 256  PRO   A CA   1 
ATOM   3945  C  C    . PRO   A 1 256 ? 11.316 15.733  15.198 1.00 12.95 ? 256  PRO   A C    1 
ATOM   3946  O  O    . PRO   A 1 256 ? 11.899 15.612  16.254 1.00 11.39 ? 256  PRO   A O    1 
ATOM   3947  C  CB   . PRO   A 1 256 ? 11.968 18.048  14.430 1.00 11.59 ? 256  PRO   A CB   1 
ATOM   3948  C  CG   . PRO   A 1 256 ? 11.537 19.403  14.958 1.00 11.44 ? 256  PRO   A CG   1 
ATOM   3949  C  CD   . PRO   A 1 256 ? 10.702 19.105  16.186 1.00 10.96 ? 256  PRO   A CD   1 
ATOM   3950  H  HA   . PRO   A 1 256 ? 10.207 16.931  14.040 1.00 15.36 ? 256  PRO   A HA   1 
ATOM   3951  H  HB2  . PRO   A 1 256 ? 12.795 17.753  14.843 1.00 13.91 ? 256  PRO   A HB2  1 
ATOM   3952  H  HB3  . PRO   A 1 256 ? 12.123 18.074  13.473 1.00 13.91 ? 256  PRO   A HB3  1 
ATOM   3953  H  HG2  . PRO   A 1 256 ? 12.305 19.952  15.181 1.00 13.73 ? 256  PRO   A HG2  1 
ATOM   3954  H  HG3  . PRO   A 1 256 ? 11.023 19.890  14.295 1.00 13.73 ? 256  PRO   A HG3  1 
ATOM   3955  H  HD2  . PRO   A 1 256 ? 11.247 19.040  16.986 1.00 13.16 ? 256  PRO   A HD2  1 
ATOM   3956  H  HD3  . PRO   A 1 256 ? 10.040 19.795  16.349 1.00 13.16 ? 256  PRO   A HD3  1 
ATOM   3957  N  N    . VAL   A 1 257 ? 11.075 14.739  14.338 1.00 11.58 ? 257  VAL   A N    1 
ATOM   3958  C  CA   . VAL   A 1 257 ? 11.512 13.346  14.637 1.00 11.22 ? 257  VAL   A CA   1 
ATOM   3959  C  C    . VAL   A 1 257 ? 12.349 12.828  13.464 1.00 11.79 ? 257  VAL   A C    1 
ATOM   3960  O  O    . VAL   A 1 257 ? 11.941 13.037  12.310 1.00 12.50 ? 257  VAL   A O    1 
ATOM   3961  C  CB   . VAL   A 1 257 ? 10.307 12.430  14.929 1.00 12.55 ? 257  VAL   A CB   1 
ATOM   3962  C  CG1  . VAL   A 1 257 ? 10.720 10.972  15.060 1.00 14.49 ? 257  VAL   A CG1  1 
ATOM   3963  C  CG2  . VAL   A 1 257 ? 9.536  12.885  16.158 1.00 11.03 ? 257  VAL   A CG2  1 
ATOM   3964  H  H    . VAL   A 1 257 ? 10.668 14.836  13.586 1.00 13.89 ? 257  VAL   A H    1 
ATOM   3965  H  HA   . VAL   A 1 257 ? 12.057 13.344  15.439 1.00 13.47 ? 257  VAL   A HA   1 
ATOM   3966  H  HB   . VAL   A 1 257 ? 9.715  12.501  14.164 1.00 15.06 ? 257  VAL   A HB   1 
ATOM   3967  H  HG11 . VAL   A 1 257 ? 9.937  10.429  15.243 1.00 17.40 ? 257  VAL   A HG11 1 
ATOM   3968  H  HG12 . VAL   A 1 257 ? 11.132 10.677  14.233 1.00 17.40 ? 257  VAL   A HG12 1 
ATOM   3969  H  HG13 . VAL   A 1 257 ? 11.355 10.879  15.788 1.00 17.40 ? 257  VAL   A HG13 1 
ATOM   3970  H  HG21 . VAL   A 1 257 ? 8.788  12.287  16.310 1.00 13.23 ? 257  VAL   A HG21 1 
ATOM   3971  H  HG22 . VAL   A 1 257 ? 10.122 12.872  16.931 1.00 13.23 ? 257  VAL   A HG22 1 
ATOM   3972  H  HG23 . VAL   A 1 257 ? 9.206  13.786  16.018 1.00 13.23 ? 257  VAL   A HG23 1 
ATOM   3973  N  N    . LYS   A 1 258 ? 13.486 12.201  13.764 1.00 10.95 ? 258  LYS   A N    1 
ATOM   3974  C  CA   . LYS   A 1 258 ? 14.365 11.609  12.721 1.00 12.46 ? 258  LYS   A CA   1 
ATOM   3975  C  C    . LYS   A 1 258 ? 14.733 12.667  11.678 1.00 11.25 ? 258  LYS   A C    1 
ATOM   3976  O  O    . LYS   A 1 258 ? 14.447 12.451  10.497 1.00 12.10 ? 258  LYS   A O    1 
ATOM   3977  C  CB   . LYS   A 1 258 ? 13.699 10.372  12.110 1.00 14.32 ? 258  LYS   A CB   1 
ATOM   3978  C  CG   . LYS   A 1 258 ? 13.685 9.151   13.021 1.00 15.98 ? 258  LYS   A CG   1 
ATOM   3979  C  CD   . LYS   A 1 258 ? 12.908 7.986   12.447 1.00 17.59 ? 258  LYS   A CD   1 
ATOM   3980  C  CE   . LYS   A 1 258 ? 13.072 6.708   13.241 1.00 23.57 ? 258  LYS   A CE   1 
ATOM   3981  N  NZ   . LYS   A 1 258 ? 12.602 5.530   12.474 1.00 26.76 ? 258  LYS   A NZ   1 
ATOM   3982  H  H    . LYS   A 1 258 ? 13.777 12.101  14.567 1.00 13.15 ? 258  LYS   A H    1 
ATOM   3983  H  HA   . LYS   A 1 258 ? 15.196 11.311  13.122 1.00 14.96 ? 258  LYS   A HA   1 
ATOM   3984  H  HB2  . LYS   A 1 258 ? 12.786 10.594  11.871 1.00 17.18 ? 258  LYS   A HB2  1 
ATOM   3985  H  HB3  . LYS   A 1 258 ? 14.159 10.143  11.287 1.00 17.18 ? 258  LYS   A HB3  1 
ATOM   3986  H  HG2  . LYS   A 1 258 ? 14.598 8.871   13.190 1.00 19.17 ? 258  LYS   A HG2  1 
ATOM   3987  H  HG3  . LYS   A 1 258 ? 13.301 9.398   13.877 1.00 19.17 ? 258  LYS   A HG3  1 
ATOM   3988  H  HD2  . LYS   A 1 258 ? 11.967 8.219   12.412 1.00 21.11 ? 258  LYS   A HD2  1 
ATOM   3989  H  HD3  . LYS   A 1 258 ? 13.196 7.831   11.534 1.00 21.11 ? 258  LYS   A HD3  1 
ATOM   3990  H  HE2  . LYS   A 1 258 ? 14.005 6.590   13.478 1.00 28.28 ? 258  LYS   A HE2  1 
ATOM   3991  H  HE3  . LYS   A 1 258 ? 12.575 6.775   14.071 1.00 28.28 ? 258  LYS   A HE3  1 
ATOM   3992  H  HZ1  . LYS   A 1 258 ? 12.853 4.785   12.891 1.00 32.12 ? 258  LYS   A HZ1  1 
ATOM   3993  H  HZ2  . LYS   A 1 258 ? 11.714 5.550   12.412 1.00 32.12 ? 258  LYS   A HZ2  1 
ATOM   3994  H  HZ3  . LYS   A 1 258 ? 12.956 5.546   11.658 1.00 32.12 ? 258  LYS   A HZ3  1 
ATOM   3995  N  N    . ASN   A 1 259 ? 15.360 13.757  12.122 1.00 10.07 ? 259  ASN   A N    1 
ATOM   3996  C  CA   . ASN   A 1 259 ? 15.826 14.794  11.197 1.00 11.39 ? 259  ASN   A CA   1 
ATOM   3997  C  C    . ASN   A 1 259 ? 14.676 15.411  10.402 1.00 12.69 ? 259  ASN   A C    1 
ATOM   3998  O  O    . ASN   A 1 259 ? 14.797 15.645  9.198  1.00 10.56 ? 259  ASN   A O    1 
ATOM   3999  C  CB   . ASN   A 1 259 ? 16.902 14.249  10.246 1.00 12.66 ? 259  ASN   A CB   1 
ATOM   4000  C  CG   . ASN   A 1 259 ? 17.755 15.354  9.614  1.00 12.09 ? 259  ASN   A CG   1 
ATOM   4001  O  OD1  . ASN   A 1 259 ? 18.117 16.340  10.264 1.00 11.05 ? 259  ASN   A OD1  1 
ATOM   4002  N  ND2  . ASN   A 1 259 ? 18.079 15.187  8.336  1.00 12.48 ? 259  ASN   A ND2  1 
ATOM   4003  H  H    . ASN   A 1 259 ? 15.525 13.916  12.951 1.00 12.09 ? 259  ASN   A H    1 
ATOM   4004  H  HA   . ASN   A 1 259 ? 16.220 15.496  11.739 1.00 13.68 ? 259  ASN   A HA   1 
ATOM   4005  H  HB2  . ASN   A 1 259 ? 17.479 13.640  10.733 1.00 15.20 ? 259  ASN   A HB2  1 
ATOM   4006  H  HB3  . ASN   A 1 259 ? 16.475 13.734  9.543  1.00 15.20 ? 259  ASN   A HB3  1 
ATOM   4007  H  HD21 . ASN   A 1 259 ? 18.557 15.777  7.933  1.00 14.98 ? 259  ASN   A HD21 1 
ATOM   4008  H  HD22 . ASN   A 1 259 ? 17.811 14.489  7.912  1.00 14.98 ? 259  ASN   A HD22 1 
ATOM   4009  N  N    . PHE   A 1 260 ? 13.554 15.674  11.079 1.00 10.59 ? 260  PHE   A N    1 
ATOM   4010  C  CA   . PHE   A 1 260 ? 12.360 16.317  10.522 1.00 10.40 ? 260  PHE   A CA   1 
ATOM   4011  C  C    . PHE   A 1 260 ? 11.605 15.419  9.541  1.00 11.88 ? 260  PHE   A C    1 
ATOM   4012  O  O    . PHE   A 1 260 ? 10.717 15.893  8.819  1.00 13.66 ? 260  PHE   A O    1 
ATOM   4013  C  CB   . PHE   A 1 260 ? 12.696 17.655  9.847  1.00 11.48 ? 260  PHE   A CB   1 
ATOM   4014  C  CG   . PHE   A 1 260 ? 13.065 18.760  10.812 1.00 10.01 ? 260  PHE   A CG   1 
ATOM   4015  C  CD1  . PHE   A 1 260 ? 14.310 18.775  11.434 1.00 11.07 ? 260  PHE   A CD1  1 
ATOM   4016  C  CD2  . PHE   A 1 260 ? 12.181 19.804  11.061 1.00 11.34 ? 260  PHE   A CD2  1 
ATOM   4017  C  CE1  . PHE   A 1 260 ? 14.664 19.809  12.313 1.00 10.54 ? 260  PHE   A CE1  1 
ATOM   4018  C  CE2  . PHE   A 1 260 ? 12.527 20.838  11.935 1.00 9.64  ? 260  PHE   A CE2  1 
ATOM   4019  C  CZ   . PHE   A 1 260 ? 13.769 20.837  12.562 1.00 11.66 ? 260  PHE   A CZ   1 
ATOM   4020  H  H    . PHE   A 1 260 ? 13.465 15.474  11.911 1.00 12.72 ? 260  PHE   A H    1 
ATOM   4021  H  HA   . PHE   A 1 260 ? 11.777 16.484  11.279 1.00 12.48 ? 260  PHE   A HA   1 
ATOM   4022  H  HB2  . PHE   A 1 260 ? 13.432 17.519  9.230  1.00 13.78 ? 260  PHE   A HB2  1 
ATOM   4023  H  HB3  . PHE   A 1 260 ? 11.933 17.941  9.320  1.00 13.78 ? 260  PHE   A HB3  1 
ATOM   4024  H  HD1  . PHE   A 1 260 ? 14.916 18.090  11.264 1.00 13.29 ? 260  PHE   A HD1  1 
ATOM   4025  H  HD2  . PHE   A 1 260 ? 11.351 19.814  10.642 1.00 13.61 ? 260  PHE   A HD2  1 
ATOM   4026  H  HE1  . PHE   A 1 260 ? 15.497 19.805  12.727 1.00 12.65 ? 260  PHE   A HE1  1 
ATOM   4027  H  HE2  . PHE   A 1 260 ? 11.926 21.528  12.098 1.00 11.58 ? 260  PHE   A HE2  1 
ATOM   4028  H  HZ   . PHE   A 1 260 ? 13.998 21.524  13.146 1.00 14.00 ? 260  PHE   A HZ   1 
ATOM   4029  N  N    . GLN   A 1 261 ? 11.950 14.131  9.509  1.00 13.11 ? 261  GLN   A N    1 
ATOM   4030  C  CA   . GLN   A 1 261 ? 11.185 13.193  8.643  1.00 12.70 ? 261  GLN   A CA   1 
ATOM   4031  C  C    . GLN   A 1 261 ? 9.781  13.028  9.232  1.00 14.31 ? 261  GLN   A C    1 
ATOM   4032  O  O    . GLN   A 1 261 ? 8.843  12.812  8.445  1.00 16.20 ? 261  GLN   A O    1 
ATOM   4033  C  CB   . GLN   A 1 261 ? 11.911 11.853  8.508  1.00 15.13 ? 261  GLN   A CB   1 
ATOM   4034  C  CG   . GLN   A 1 261 ? 13.111 11.904  7.575  1.00 14.62 ? 261  GLN   A CG   1 
ATOM   4035  C  CD   . GLN   A 1 261 ? 13.729 10.542  7.388  1.00 14.35 ? 261  GLN   A CD   1 
ATOM   4036  O  OE1  . GLN   A 1 261 ? 13.356 9.788   6.494  1.00 14.23 ? 261  GLN   A OE1  1 
ATOM   4037  N  NE2  . GLN   A 1 261 ? 14.681 10.213  8.245  1.00 15.21 ? 261  GLN   A NE2  1 
ATOM   4038  H  H    . GLN   A 1 261 ? 12.595 13.780  9.957  1.00 15.74 ? 261  GLN   A H    1 
ATOM   4039  H  HA   . GLN   A 1 261 ? 11.112 13.554  7.746  1.00 15.24 ? 261  GLN   A HA   1 
ATOM   4040  H  HB2  . GLN   A 1 261 ? 12.205 11.563  9.386  1.00 18.15 ? 261  GLN   A HB2  1 
ATOM   4041  H  HB3  . GLN   A 1 261 ? 11.286 11.186  8.183  1.00 18.15 ? 261  GLN   A HB3  1 
ATOM   4042  H  HG2  . GLN   A 1 261 ? 12.837 12.256  6.714  1.00 17.55 ? 261  GLN   A HG2  1 
ATOM   4043  H  HG3  . GLN   A 1 261 ? 13.774 12.514  7.933  1.00 17.55 ? 261  GLN   A HG3  1 
ATOM   4044  H  HE21 . GLN   A 1 261 ? 14.917 10.767  8.859  1.00 18.26 ? 261  GLN   A HE21 1 
ATOM   4045  H  HE22 . GLN   A 1 261 ? 15.064 9.445   8.188  1.00 18.26 ? 261  GLN   A HE22 1 
ATOM   4046  N  N    . GLU   A 1 262 ? 9.658  13.137  10.554 1.00 15.73 ? 262  GLU   A N    1 
ATOM   4047  C  CA   . GLU   A 1 262 ? 8.321  13.074  11.199 1.00 12.76 ? 262  GLU   A CA   1 
ATOM   4048  C  C    . GLU   A 1 262 ? 8.166  14.283  12.129 1.00 12.19 ? 262  GLU   A C    1 
ATOM   4049  O  O    . GLU   A 1 262 ? 9.162  15.002  12.316 1.00 11.92 ? 262  GLU   A O    1 
ATOM   4050  C  CB   . GLU   A 1 262 ? 8.140  11.746  11.928 1.00 16.08 ? 262  GLU   A CB   1 
ATOM   4051  C  CG   . GLU   A 1 262 ? 8.150  10.535  11.017 1.00 16.96 ? 262  GLU   A CG   1 
ATOM   4052  C  CD   . GLU   A 1 262 ? 8.034  9.217   11.762 1.00 23.19 ? 262  GLU   A CD   1 
ATOM   4053  O  OE1  . GLU   A 1 262 ? 7.029  9.029   12.472 1.00 23.98 ? 262  GLU   A OE1  1 
ATOM   4054  O  OE2  . GLU   A 1 262 ? 8.953  8.387   11.639 1.00 25.17 ? 262  GLU   A OE2  1 
ATOM   4055  H  H    . GLU   A 1 262 ? 10.316 13.246  11.096 1.00 18.88 ? 262  GLU   A H    1 
ATOM   4056  H  HA   . GLU   A 1 262 ? 7.621  13.115  10.529 1.00 15.32 ? 262  GLU   A HA   1 
ATOM   4057  H  HB2  . GLU   A 1 262 ? 8.846  11.650  12.586 1.00 19.29 ? 262  GLU   A HB2  1 
ATOM   4058  H  HB3  . GLU   A 1 262 ? 7.301  11.766  12.414 1.00 19.29 ? 262  GLU   A HB3  1 
ATOM   4059  H  HG2  . GLU   A 1 262 ? 7.417  10.608  10.386 1.00 20.36 ? 262  GLU   A HG2  1 
ATOM   4060  H  HG3  . GLU   A 1 262 ? 8.970  10.535  10.500 1.00 20.36 ? 262  GLU   A HG3  1 
ATOM   4061  N  N    . SER   A 1 263 ? 6.977  14.484  12.703 1.00 11.38 ? 263  SER   A N    1 
ATOM   4062  C  CA   . SER   A 1 263 ? 6.716  15.712  13.500 1.00 12.55 ? 263  SER   A CA   1 
ATOM   4063  C  C    . SER   A 1 263 ? 5.987  15.347  14.795 1.00 12.78 ? 263  SER   A C    1 
ATOM   4064  O  O    . SER   A 1 263 ? 5.465  16.254  15.457 1.00 10.80 ? 263  SER   A O    1 
ATOM   4065  C  CB   . SER   A 1 263 ? 5.913  16.686  12.678 1.00 11.68 ? 263  SER   A CB   1 
ATOM   4066  O  OG   . SER   A 1 263 ? 6.451  16.802  11.372 1.00 15.92 ? 263  SER   A OG   1 
ATOM   4067  H  H    . SER   A 1 263 ? 6.314  13.939  12.651 1.00 13.66 ? 263  SER   A H    1 
ATOM   4068  H  HA   . SER   A 1 263 ? 7.557  16.133  13.737 1.00 15.06 ? 263  SER   A HA   1 
ATOM   4069  H  HB2  . SER   A 1 263 ? 4.991  16.390  12.628 1.00 14.02 ? 263  SER   A HB2  1 
ATOM   4070  H  HB3  . SER   A 1 263 ? 5.909  17.555  13.110 1.00 14.02 ? 263  SER   A HB3  1 
ATOM   4071  H  HG   . SER   A 1 263 ? 6.758  17.576  11.263 1.00 19.11 ? 263  SER   A HG   1 
ATOM   4072  N  N    . TYR   A 1 264 ? 5.961  14.053  15.115 1.00 13.24 ? 264  TYR   A N    1 
ATOM   4073  C  CA   . TYR   A 1 264 ? 5.232  13.583  16.319 1.00 16.55 ? 264  TYR   A CA   1 
ATOM   4074  C  C    . TYR   A 1 264 ? 5.785  12.222  16.754 1.00 15.33 ? 264  TYR   A C    1 
ATOM   4075  O  O    . TYR   A 1 264 ? 6.074  11.391  15.881 1.00 15.51 ? 264  TYR   A O    1 
ATOM   4076  C  CB   . TYR   A 1 264 ? 3.733  13.462  16.036 1.00 17.87 ? 264  TYR   A CB   1 
ATOM   4077  C  CG   . TYR   A 1 264 ? 2.946  12.888  17.185 1.00 20.74 ? 264  TYR   A CG   1 
ATOM   4078  C  CD1  . TYR   A 1 264 ? 2.756  11.522  17.310 1.00 24.59 ? 264  TYR   A CD1  1 
ATOM   4079  C  CD2  . TYR   A 1 264 ? 2.406  13.709  18.159 1.00 20.94 ? 264  TYR   A CD2  1 
ATOM   4080  C  CE1  . TYR   A 1 264 ? 2.044  10.986  18.370 1.00 26.95 ? 264  TYR   A CE1  1 
ATOM   4081  C  CE2  . TYR   A 1 264 ? 1.690  13.192  19.224 1.00 19.78 ? 264  TYR   A CE2  1 
ATOM   4082  C  CZ   . TYR   A 1 264 ? 1.509  11.825  19.330 1.00 28.64 ? 264  TYR   A CZ   1 
ATOM   4083  O  OH   . TYR   A 1 264 ? 0.797  11.305  20.382 1.00 34.75 ? 264  TYR   A OH   1 
ATOM   4084  H  H    . TYR   A 1 264 ? 6.349  13.433  14.663 1.00 15.90 ? 264  TYR   A H    1 
ATOM   4085  H  HA   . TYR   A 1 264 ? 5.359  14.232  17.029 1.00 19.87 ? 264  TYR   A HA   1 
ATOM   4086  H  HB2  . TYR   A 1 264 ? 3.381  14.339  15.819 1.00 21.45 ? 264  TYR   A HB2  1 
ATOM   4087  H  HB3  . TYR   A 1 264 ? 3.603  12.903  15.254 1.00 21.45 ? 264  TYR   A HB3  1 
ATOM   4088  H  HD1  . TYR   A 1 264 ? 3.114  10.952  16.668 1.00 29.52 ? 264  TYR   A HD1  1 
ATOM   4089  H  HD2  . TYR   A 1 264 ? 2.527  14.629  18.096 1.00 25.13 ? 264  TYR   A HD2  1 
ATOM   4090  H  HE1  . TYR   A 1 264 ? 1.926  10.066  18.436 1.00 32.34 ? 264  TYR   A HE1  1 
ATOM   4091  H  HE2  . TYR   A 1 264 ? 1.332  13.761  19.866 1.00 23.74 ? 264  TYR   A HE2  1 
ATOM   4092  H  HH   . TYR   A 1 264 ? 0.980  11.731  21.082 1.00 41.70 ? 264  TYR   A HH   1 
ATOM   4093  N  N    . THR   A 1 265 ? 5.925  12.020  18.064 1.00 13.71 ? 265  THR   A N    1 
ATOM   4094  C  CA   . THR   A 1 265 ? 6.401  10.712  18.581 1.00 16.01 ? 265  THR   A CA   1 
ATOM   4095  C  C    . THR   A 1 265 ? 5.608  10.334  19.834 1.00 17.25 ? 265  THR   A C    1 
ATOM   4096  O  O    . THR   A 1 265 ? 5.457  11.185  20.722 1.00 16.38 ? 265  THR   A O    1 
ATOM   4097  C  CB   . THR   A 1 265 ? 7.911  10.704  18.854 1.00 15.49 ? 265  THR   A CB   1 
ATOM   4098  O  OG1  . THR   A 1 265 ? 8.248  9.436   19.419 1.00 14.82 ? 265  THR   A OG1  1 
ATOM   4099  C  CG2  . THR   A 1 265 ? 8.353  11.814  19.781 1.00 15.17 ? 265  THR   A CG2  1 
ATOM   4100  H  H    . THR   A 1 265 ? 5.756  12.608  18.668 1.00 16.46 ? 265  THR   A H    1 
ATOM   4101  H  HA   . THR   A 1 265 ? 6.247  10.045  17.893 1.00 19.22 ? 265  THR   A HA   1 
ATOM   4102  H  HB   . THR   A 1 265 ? 8.372  10.854  18.014 1.00 18.60 ? 265  THR   A HB   1 
ATOM   4103  H  HG1  . THR   A 1 265 ? 9.076  9.310   19.351 1.00 17.78 ? 265  THR   A HG1  1 
ATOM   4104  H  HG21 . THR   A 1 265 ? 9.312  11.760  19.917 1.00 18.21 ? 265  THR   A HG21 1 
ATOM   4105  H  HG22 . THR   A 1 265 ? 8.131  12.672  19.387 1.00 18.21 ? 265  THR   A HG22 1 
ATOM   4106  H  HG23 . THR   A 1 265 ? 7.900  11.723  20.634 1.00 18.21 ? 265  THR   A HG23 1 
ATOM   4107  N  N    . ASN   A 1 266 ? 5.082  9.109   19.863 1.00 13.31 ? 266  ASN   A N    1 
ATOM   4108  C  CA   . ASN   A 1 266 ? 4.393  8.638   21.063 1.00 14.75 ? 266  ASN   A CA   1 
ATOM   4109  C  C    . ASN   A 1 266 ? 5.352  8.286   22.198 1.00 17.94 ? 266  ASN   A C    1 
ATOM   4110  O  O    . ASN   A 1 266 ? 4.896  7.837   23.253 1.00 17.55 ? 266  ASN   A O    1 
ATOM   4111  C  CB   . ASN   A 1 266 ? 3.474  7.442   20.729 1.00 20.47 ? 266  ASN   A CB   1 
ATOM   4112  C  CG   . ASN   A 1 266 ? 4.205  6.271   20.061 1.00 19.68 ? 266  ASN   A CG   1 
ATOM   4113  O  OD1  . ASN   A 1 266 ? 5.401  6.053   20.258 1.00 18.50 ? 266  ASN   A OD1  1 
ATOM   4114  N  ND2  . ASN   A 1 266 ? 3.459  5.490   19.282 1.00 22.06 ? 266  ASN   A ND2  1 
ATOM   4115  H  H    . ASN   A 1 266 ? 5.112  8.546   19.213 1.00 15.98 ? 266  ASN   A H    1 
ATOM   4116  H  HA   . ASN   A 1 266 ? 3.848  9.375   21.380 1.00 17.70 ? 266  ASN   A HA   1 
ATOM   4117  H  HB2  . ASN   A 1 266 ? 3.055  7.128   21.546 1.00 24.57 ? 266  ASN   A HB2  1 
ATOM   4118  H  HB3  . ASN   A 1 266 ? 2.762  7.745   20.144 1.00 24.57 ? 266  ASN   A HB3  1 
ATOM   4119  H  HD21 . ASN   A 1 266 ? 3.810  4.806   18.896 1.00 26.47 ? 266  ASN   A HD21 1 
ATOM   4120  H  HD22 . ASN   A 1 266 ? 2.626  5.669   19.165 1.00 26.47 ? 266  ASN   A HD22 1 
ATOM   4121  N  N    . GLN   A 1 267 ? 6.659  8.498   22.023 1.00 14.74 ? 267  GLN   A N    1 
ATOM   4122  C  CA   . GLN   A 1 267 ? 7.650  8.238   23.064 1.00 17.47 ? 267  GLN   A CA   1 
ATOM   4123  C  C    . GLN   A 1 267 ? 8.135  9.499   23.770 1.00 14.91 ? 267  GLN   A C    1 
ATOM   4124  O  O    . GLN   A 1 267 ? 9.015  9.405   24.633 1.00 15.44 ? 267  GLN   A O    1 
ATOM   4125  C  CB   . GLN   A 1 267 ? 8.856  7.501   22.471 1.00 18.69 ? 267  GLN   A CB   1 
ATOM   4126  C  CG   . GLN   A 1 267 ? 8.496  6.172   21.829 1.00 17.01 ? 267  GLN   A CG   1 
ATOM   4127  C  CD   . GLN   A 1 267 ? 7.799  5.250   22.814 1.00 18.66 ? 267  GLN   A CD   1 
ATOM   4128  O  OE1  . GLN   A 1 267 ? 8.362  4.888   23.847 1.00 16.11 ? 267  GLN   A OE1  1 
ATOM   4129  N  NE2  . GLN   A 1 267 ? 6.566  4.873   22.500 1.00 16.88 ? 267  GLN   A NE2  1 
ATOM   4130  H  H    . GLN   A 1 267 ? 6.995  8.799   21.291 1.00 17.69 ? 267  GLN   A H    1 
ATOM   4131  H  HA   . GLN   A 1 267 ? 7.204  7.690   23.729 1.00 20.97 ? 267  GLN   A HA   1 
ATOM   4132  H  HB2  . GLN   A 1 267 ? 9.279  8.069   21.808 1.00 22.43 ? 267  GLN   A HB2  1 
ATOM   4133  H  HB3  . GLN   A 1 267 ? 9.509  7.348   23.172 1.00 22.43 ? 267  GLN   A HB3  1 
ATOM   4134  H  HG2  . GLN   A 1 267 ? 7.919  6.326   21.064 1.00 20.41 ? 267  GLN   A HG2  1 
ATOM   4135  H  HG3  . GLN   A 1 267 ? 9.300  5.744   21.496 1.00 20.41 ? 267  GLN   A HG3  1 
ATOM   4136  H  HE21 . GLN   A 1 267 ? 6.206  5.147   21.769 1.00 20.26 ? 267  GLN   A HE21 1 
ATOM   4137  H  HE22 . GLN   A 1 267 ? 6.127  4.355   23.028 1.00 20.26 ? 267  GLN   A HE22 1 
ATOM   4138  N  N    . ALA   A 1 268 ? 7.579  10.671  23.436 1.00 14.56 ? 268  ALA   A N    1 
ATOM   4139  C  CA   . ALA   A 1 268 ? 8.159  11.934  23.891 1.00 16.82 ? 268  ALA   A CA   1 
ATOM   4140  C  C    . ALA   A 1 268 ? 8.181  12.064  25.411 1.00 14.92 ? 268  ALA   A C    1 
ATOM   4141  O  O    . ALA   A 1 268 ? 9.110  12.667  25.959 1.00 14.37 ? 268  ALA   A O    1 
ATOM   4142  C  CB   . ALA   A 1 268 ? 7.401  13.117  23.280 1.00 14.77 ? 268  ALA   A CB   1 
ATOM   4143  H  H    . ALA   A 1 268 ? 6.873  10.752  22.952 1.00 17.47 ? 268  ALA   A H    1 
ATOM   4144  H  HA   . ALA   A 1 268 ? 9.081  11.941  23.590 1.00 20.19 ? 268  ALA   A HA   1 
ATOM   4145  H  HB1  . ALA   A 1 268 ? 7.795  13.948  23.589 1.00 17.72 ? 268  ALA   A HB1  1 
ATOM   4146  H  HB2  . ALA   A 1 268 ? 7.457  13.073  22.313 1.00 17.72 ? 268  ALA   A HB2  1 
ATOM   4147  H  HB3  . ALA   A 1 268 ? 6.470  13.080  23.551 1.00 17.72 ? 268  ALA   A HB3  1 
ATOM   4148  N  N    . ASP   A 1 269 ? 7.188  11.511  26.116 1.00 17.75 ? 269  ASP   A N    1 
ATOM   4149  C  CA   . ASP   A 1 269 ? 7.146  11.736  27.560 1.00 16.11 ? 269  ASP   A CA   1 
ATOM   4150  C  C    . ASP   A 1 269 ? 8.320  11.087  28.286 1.00 15.31 ? 269  ASP   A C    1 
ATOM   4151  O  O    . ASP   A 1 269 ? 8.617  11.467  29.425 1.00 18.09 ? 269  ASP   A O    1 
ATOM   4152  C  CB   . ASP   A 1 269 ? 5.831  11.239  28.156 1.00 19.00 ? 269  ASP   A CB   1 
ATOM   4153  C  CG   . ASP   A 1 269 ? 5.702  11.574  29.630 1.00 21.05 ? 269  ASP   A CG   1 
ATOM   4154  O  OD1  . ASP   A 1 269 ? 5.783  12.774  29.973 1.00 21.40 ? 269  ASP   A OD1  1 
ATOM   4155  O  OD2  . ASP   A 1 269 ? 5.532  10.641  30.446 1.00 21.58 ? 269  ASP   A OD2  1 
ATOM   4156  H  H    . ASP   A 1 269 ? 6.557  11.024  25.793 1.00 21.30 ? 269  ASP   A H    1 
ATOM   4157  H  HA   . ASP   A 1 269 ? 7.213  12.695  27.689 1.00 19.33 ? 269  ASP   A HA   1 
ATOM   4158  H  HB2  . ASP   A 1 269 ? 5.089  11.633  27.671 1.00 22.80 ? 269  ASP   A HB2  1 
ATOM   4159  H  HB3  . ASP   A 1 269 ? 5.768  10.278  28.038 1.00 22.80 ? 269  ASP   A HB3  1 
ATOM   4160  N  N    . LYS   A 1 270 ? 9.006  10.136  27.652 1.00 13.22 ? 270  LYS   A N    1 
ATOM   4161  C  CA   . LYS   A 1 270 ? 10.202 9.563   28.257 1.00 12.76 ? 270  LYS   A CA   1 
ATOM   4162  C  C    . LYS   A 1 270 ? 11.323 10.592  28.415 1.00 12.96 ? 270  LYS   A C    1 
ATOM   4163  O  O    . LYS   A 1 270 ? 12.205 10.401  29.261 1.00 13.53 ? 270  LYS   A O    1 
ATOM   4164  C  CB   . LYS   A 1 270 ? 10.687 8.373   27.424 1.00 15.30 ? 270  LYS   A CB   1 
ATOM   4165  C  CG   . LYS   A 1 270 ? 9.750  7.164   27.480 1.00 16.75 ? 270  LYS   A CG   1 
ATOM   4166  C  CD   . LYS   A 1 270 ? 10.277 6.000   26.654 1.00 17.00 ? 270  LYS   A CD   1 
ATOM   4167  C  CE   . LYS   A 1 270 ? 11.437 5.290   27.341 1.00 15.00 ? 270  LYS   A CE   1 
ATOM   4168  N  NZ   . LYS   A 1 270 ? 11.618 3.918   26.792 1.00 16.68 ? 270  LYS   A NZ   1 
ATOM   4169  H  H    . LYS   A 1 270 ? 8.798  9.814   26.882 1.00 15.87 ? 270  LYS   A H    1 
ATOM   4170  H  HA   . LYS   A 1 270 ? 9.964  9.262   29.148 1.00 15.31 ? 270  LYS   A HA   1 
ATOM   4171  H  HB2  . LYS   A 1 270 ? 10.786 8.653   26.501 1.00 18.36 ? 270  LYS   A HB2  1 
ATOM   4172  H  HB3  . LYS   A 1 270 ? 11.566 8.106   27.736 1.00 18.36 ? 270  LYS   A HB3  1 
ATOM   4173  H  HG2  . LYS   A 1 270 ? 9.640  6.883   28.402 1.00 20.10 ? 270  LYS   A HG2  1 
ATOM   4174  H  HG3  . LYS   A 1 270 ? 8.873  7.420   27.155 1.00 20.10 ? 270  LYS   A HG3  1 
ATOM   4175  H  HD2  . LYS   A 1 270 ? 9.560  5.367   26.495 1.00 20.40 ? 270  LYS   A HD2  1 
ATOM   4176  H  HD3  . LYS   A 1 270 ? 10.566 6.325   25.787 1.00 20.40 ? 270  LYS   A HD3  1 
ATOM   4177  H  HE2  . LYS   A 1 270 ? 12.252 5.802   27.219 1.00 18.00 ? 270  LYS   A HE2  1 
ATOM   4178  H  HE3  . LYS   A 1 270 ? 11.272 5.242   28.296 1.00 18.00 ? 270  LYS   A HE3  1 
ATOM   4179  H  HZ1  . LYS   A 1 270 ? 12.317 3.531   27.184 1.00 20.02 ? 270  LYS   A HZ1  1 
ATOM   4180  H  HZ2  . LYS   A 1 270 ? 10.886 3.437   26.948 1.00 20.02 ? 270  LYS   A HZ2  1 
ATOM   4181  H  HZ3  . LYS   A 1 270 ? 11.760 3.965   25.915 1.00 20.02 ? 270  LYS   A HZ3  1 
ATOM   4182  N  N    . ILE   A 1 271 ? 11.312 11.676  27.638 1.00 14.65 ? 271  ILE   A N    1 
ATOM   4183  C  CA   . ILE   A 1 271 ? 12.361 12.688  27.752 1.00 12.83 ? 271  ILE   A CA   1 
ATOM   4184  C  C    . ILE   A 1 271 ? 11.757 14.049  28.095 1.00 13.06 ? 271  ILE   A C    1 
ATOM   4185  O  O    . ILE   A 1 271 ? 12.325 15.098  27.768 1.00 12.38 ? 271  ILE   A O    1 
ATOM   4186  C  CB   . ILE   A 1 271 ? 13.210 12.759  26.463 1.00 14.66 ? 271  ILE   A CB   1 
ATOM   4187  C  CG1  . ILE   A 1 271 ? 12.368 13.165  25.246 1.00 15.85 ? 271  ILE   A CG1  1 
ATOM   4188  C  CG2  . ILE   A 1 271 ? 13.904 11.431  26.206 1.00 17.88 ? 271  ILE   A CG2  1 
ATOM   4189  C  CD1  . ILE   A 1 271 ? 13.186 13.294  23.964 1.00 16.81 ? 271  ILE   A CD1  1 
ATOM   4190  H  H    . ILE   A 1 271 ? 10.712 11.843  27.045 1.00 17.58 ? 271  ILE   A H    1 
ATOM   4191  H  HA   . ILE   A 1 271 ? 12.954 12.431  28.476 1.00 15.40 ? 271  ILE   A HA   1 
ATOM   4192  H  HB   . ILE   A 1 271 ? 13.882 13.445  26.597 1.00 17.60 ? 271  ILE   A HB   1 
ATOM   4193  H  HG12 . ILE   A 1 271 ? 11.668 12.508  25.111 1.00 19.02 ? 271  ILE   A HG12 1 
ATOM   4194  H  HG13 . ILE   A 1 271 ? 11.931 14.011  25.430 1.00 19.02 ? 271  ILE   A HG13 1 
ATOM   4195  H  HG21 . ILE   A 1 271 ? 14.432 11.493  25.394 1.00 21.46 ? 271  ILE   A HG21 1 
ATOM   4196  H  HG22 . ILE   A 1 271 ? 14.485 11.219  26.953 1.00 21.46 ? 271  ILE   A HG22 1 
ATOM   4197  H  HG23 . ILE   A 1 271 ? 13.239 10.732  26.106 1.00 21.46 ? 271  ILE   A HG23 1 
ATOM   4198  H  HD11 . ILE   A 1 271 ? 12.603 13.551  23.233 1.00 20.17 ? 271  ILE   A HD11 1 
ATOM   4199  H  HD12 . ILE   A 1 271 ? 13.871 13.970  24.084 1.00 20.17 ? 271  ILE   A HD12 1 
ATOM   4200  H  HD13 . ILE   A 1 271 ? 13.604 12.443  23.760 1.00 20.17 ? 271  ILE   A HD13 1 
ATOM   4201  N  N    . SER   A 1 272 ? 10.621 14.043  28.788 1.00 10.62 ? 272  SER   A N    1 
ATOM   4202  C  CA   . SER   A 1 272 ? 9.959  15.290  29.135 1.00 13.15 ? 272  SER   A CA   1 
ATOM   4203  C  C    . SER   A 1 272 ? 10.540 15.889  30.412 1.00 15.04 ? 272  SER   A C    1 
ATOM   4204  O  O    . SER   A 1 272 ? 11.167 15.204  31.229 1.00 13.74 ? 272  SER   A O    1 
ATOM   4205  C  CB   . SER   A 1 272 ? 8.458  15.072  29.326 1.00 13.65 ? 272  SER   A CB   1 
ATOM   4206  O  OG   . SER   A 1 272 ? 8.202  14.279  30.470 1.00 14.51 ? 272  SER   A OG   1 
ATOM   4207  H  H    . SER   A 1 272 ? 10.222 13.332  29.063 1.00 12.75 ? 272  SER   A H    1 
ATOM   4208  H  HA   . SER   A 1 272 ? 10.107 15.907  28.401 1.00 15.78 ? 272  SER   A HA   1 
ATOM   4209  H  HB2  . SER   A 1 272 ? 8.012  15.929  29.416 1.00 16.39 ? 272  SER   A HB2  1 
ATOM   4210  H  HB3  . SER   A 1 272 ? 8.088  14.641  28.540 1.00 16.39 ? 272  SER   A HB3  1 
ATOM   4211  H  HG   . SER   A 1 272 ? 7.494  13.842  30.355 1.00 17.42 ? 272  SER   A HG   1 
ATOM   4212  N  N    . GLY   A 1 273 ? 10.290 17.187  30.594 1.00 14.01 ? 273  GLY   A N    1 
ATOM   4213  C  CA   . GLY   A 1 273 ? 10.656 17.821  31.850 1.00 12.15 ? 273  GLY   A CA   1 
ATOM   4214  C  C    . GLY   A 1 273 ? 9.934  17.216  33.036 1.00 14.92 ? 273  GLY   A C    1 
ATOM   4215  O  O    . GLY   A 1 273 ? 10.490 17.129  34.136 1.00 14.41 ? 273  GLY   A O    1 
ATOM   4216  H  H    . GLY   A 1 273 ? 9.918  17.703  30.015 1.00 16.82 ? 273  GLY   A H    1 
ATOM   4217  H  HA2  . GLY   A 1 273 ? 11.614 17.741  31.983 1.00 14.58 ? 273  GLY   A HA2  1 
ATOM   4218  H  HA3  . GLY   A 1 273 ? 10.455 18.769  31.801 1.00 14.58 ? 273  GLY   A HA3  1 
ATOM   4219  N  N    . GLU   A 1 274 ? 8.726  16.711  32.793 1.00 14.89 ? 274  GLU   A N    1 
ATOM   4220  C  CA   . GLU   A 1 274 ? 7.989  16.012  33.883 1.00 14.34 ? 274  GLU   A CA   1 
ATOM   4221  C  C    . GLU   A 1 274 ? 8.763  14.752  34.300 1.00 16.15 ? 274  GLU   A C    1 
ATOM   4222  O  O    . GLU   A 1 274 ? 8.894  14.514  35.510 1.00 15.86 ? 274  GLU   A O    1 
ATOM   4223  C  CB   . GLU   A 1 274 ? 6.564  15.696  33.423 1.00 19.46 ? 274  GLU   A CB   1 
ATOM   4224  C  CG   . GLU   A 1 274 ? 5.688  16.927  33.289 1.00 18.84 ? 274  GLU   A CG   1 
ATOM   4225  C  CD   . GLU   A 1 274 ? 5.662  17.553  31.905 1.00 22.42 ? 274  GLU   A CD   1 
ATOM   4226  O  OE1  . GLU   A 1 274 ? 6.527  17.205  31.080 1.00 18.54 ? 274  GLU   A OE1  1 
ATOM   4227  O  OE2  . GLU   A 1 274 ? 4.775  18.389  31.660 1.00 21.98 ? 274  GLU   A OE2  1 
ATOM   4228  H  H    . GLU   A 1 274 ? 8.316  16.752  32.038 1.00 17.87 ? 274  GLU   A H    1 
ATOM   4229  H  HA   . GLU   A 1 274 ? 7.920  16.584  34.663 1.00 17.21 ? 274  GLU   A HA   1 
ATOM   4230  H  HB2  . GLU   A 1 274 ? 6.601  15.239  32.568 1.00 23.35 ? 274  GLU   A HB2  1 
ATOM   4231  H  HB3  . GLU   A 1 274 ? 6.156  15.084  34.055 1.00 23.35 ? 274  GLU   A HB3  1 
ATOM   4232  H  HG2  . GLU   A 1 274 ? 4.781  16.690  33.538 1.00 22.62 ? 274  GLU   A HG2  1 
ATOM   4233  H  HG3  . GLU   A 1 274 ? 5.992  17.594  33.925 1.00 22.62 ? 274  GLU   A HG3  1 
ATOM   4234  N  N    . THR   A 1 275 ? 9.251  13.980  33.330 1.00 13.65 ? 275  THR   A N    1 
ATOM   4235  C  CA   . THR   A 1 275 ? 9.984  12.727  33.649 1.00 15.84 ? 275  THR   A CA   1 
ATOM   4236  C  C    . THR   A 1 275 ? 11.308 13.092  34.324 1.00 13.80 ? 275  THR   A C    1 
ATOM   4237  O  O    . THR   A 1 275 ? 11.698 12.417  35.286 1.00 16.28 ? 275  THR   A O    1 
ATOM   4238  C  CB   . THR   A 1 275 ? 10.187 11.865  32.398 1.00 17.55 ? 275  THR   A CB   1 
ATOM   4239  O  OG1  . THR   A 1 275 ? 8.891  11.528  31.905 1.00 15.62 ? 275  THR   A OG1  1 
ATOM   4240  C  CG2  . THR   A 1 275 ? 10.980 10.605  32.665 1.00 15.03 ? 275  THR   A CG2  1 
ATOM   4241  H  H    . THR   A 1 275 ? 9.176  14.150  32.490 1.00 16.39 ? 275  THR   A H    1 
ATOM   4242  H  HA   . THR   A 1 275 ? 9.460  12.188  34.262 1.00 19.02 ? 275  THR   A HA   1 
ATOM   4243  H  HB   . THR   A 1 275 ? 10.703 12.371  31.751 1.00 21.06 ? 275  THR   A HB   1 
ATOM   4244  H  HG1  . THR   A 1 275 ? 8.764  11.908  31.167 1.00 18.74 ? 275  THR   A HG1  1 
ATOM   4245  H  HG21 . THR   A 1 275 ? 11.076 10.102  31.841 1.00 18.04 ? 275  THR   A HG21 1 
ATOM   4246  H  HG22 . THR   A 1 275 ? 11.858 10.841  33.004 1.00 18.04 ? 275  THR   A HG22 1 
ATOM   4247  H  HG23 . THR   A 1 275 ? 10.515 10.063  33.322 1.00 18.04 ? 275  THR   A HG23 1 
ATOM   4248  N  N    . LEU   A 1 276 ? 11.956 14.147  33.828 1.00 14.29 ? 276  LEU   A N    1 
ATOM   4249  C  CA   . LEU   A 1 276 ? 13.266 14.562  34.396 1.00 14.39 ? 276  LEU   A CA   1 
ATOM   4250  C  C    . LEU   A 1 276 ? 13.061 14.986  35.854 1.00 14.12 ? 276  LEU   A C    1 
ATOM   4251  O  O    . LEU   A 1 276 ? 13.824 14.525  36.710 1.00 14.74 ? 276  LEU   A O    1 
ATOM   4252  C  CB   . LEU   A 1 276 ? 13.841 15.707  33.553 1.00 13.12 ? 276  LEU   A CB   1 
ATOM   4253  C  CG   . LEU   A 1 276 ? 15.227 16.198  33.971 1.00 15.77 ? 276  LEU   A CG   1 
ATOM   4254  C  CD1  . LEU   A 1 276 ? 16.271 15.113  33.760 1.00 14.78 ? 276  LEU   A CD1  1 
ATOM   4255  C  CD2  . LEU   A 1 276 ? 15.607 17.459  33.209 1.00 11.25 ? 276  LEU   A CD2  1 
ATOM   4256  H  H    . LEU   A 1 276 ? 11.672 14.633  33.178 1.00 17.15 ? 276  LEU   A H    1 
ATOM   4257  H  HA   . LEU   A 1 276 ? 13.898 13.827  34.376 1.00 17.27 ? 276  LEU   A HA   1 
ATOM   4258  H  HB2  . LEU   A 1 276 ? 13.883 15.418  32.628 1.00 15.74 ? 276  LEU   A HB2  1 
ATOM   4259  H  HB3  . LEU   A 1 276 ? 13.225 16.456  33.589 1.00 15.74 ? 276  LEU   A HB3  1 
ATOM   4260  H  HG   . LEU   A 1 276 ? 15.196 16.411  34.917 1.00 18.93 ? 276  LEU   A HG   1 
ATOM   4261  H  HD11 . LEU   A 1 276 ? 17.142 15.444  34.031 1.00 17.74 ? 276  LEU   A HD11 1 
ATOM   4262  H  HD12 . LEU   A 1 276 ? 16.042 14.335  34.292 1.00 17.74 ? 276  LEU   A HD12 1 
ATOM   4263  H  HD13 . LEU   A 1 276 ? 16.297 14.866  32.822 1.00 17.74 ? 276  LEU   A HD13 1 
ATOM   4264  H  HD21 . LEU   A 1 276 ? 16.488 17.753  33.489 1.00 13.50 ? 276  LEU   A HD21 1 
ATOM   4265  H  HD22 . LEU   A 1 276 ? 15.616 17.272  32.257 1.00 13.50 ? 276  LEU   A HD22 1 
ATOM   4266  H  HD23 . LEU   A 1 276 ? 14.960 18.157  33.395 1.00 13.50 ? 276  LEU   A HD23 1 
ATOM   4267  N  N    . THR   A 1 277 ? 12.061 15.828  36.108 1.00 15.79 ? 277  THR   A N    1 
ATOM   4268  C  CA   . THR   A 1 277 ? 11.804 16.323  37.485 1.00 16.53 ? 277  THR   A CA   1 
ATOM   4269  C  C    . THR   A 1 277 ? 11.502 15.143  38.416 1.00 15.07 ? 277  THR   A C    1 
ATOM   4270  O  O    . THR   A 1 277 ? 11.897 15.201  39.589 1.00 17.07 ? 277  THR   A O    1 
ATOM   4271  C  CB   . THR   A 1 277 ? 10.677 17.363  37.476 1.00 16.32 ? 277  THR   A CB   1 
ATOM   4272  O  OG1  . THR   A 1 277 ? 11.159 18.527  36.805 1.00 18.05 ? 277  THR   A OG1  1 
ATOM   4273  C  CG2  . THR   A 1 277 ? 10.190 17.728  38.861 1.00 20.37 ? 277  THR   A CG2  1 
ATOM   4274  H  H    . THR   A 1 277 ? 11.519 16.129  35.512 1.00 18.95 ? 277  THR   A H    1 
ATOM   4275  H  HA   . THR   A 1 277 ? 12.597 16.767  37.825 1.00 19.84 ? 277  THR   A HA   1 
ATOM   4276  H  HB   . THR   A 1 277 ? 9.914  16.978  37.017 1.00 19.59 ? 277  THR   A HB   1 
ATOM   4277  H  HG1  . THR   A 1 277 ? 10.888 19.214  37.206 1.00 21.67 ? 277  THR   A HG1  1 
ATOM   4278  H  HG21 . THR   A 1 277 ? 9.481  18.386  38.792 1.00 24.44 ? 277  THR   A HG21 1 
ATOM   4279  H  HG22 . THR   A 1 277 ? 9.852  16.935  39.305 1.00 24.44 ? 277  THR   A HG22 1 
ATOM   4280  H  HG23 . THR   A 1 277 ? 10.925 18.098  39.376 1.00 24.44 ? 277  THR   A HG23 1 
ATOM   4281  N  N    . ALA   A 1 278 ? 10.826 14.113  37.907 1.00 16.71 ? 278  ALA   A N    1 
ATOM   4282  C  CA   . ALA   A 1 278 ? 10.424 12.987  38.783 1.00 18.75 ? 278  ALA   A CA   1 
ATOM   4283  C  C    . ALA   A 1 278 ? 11.580 12.005  38.974 1.00 20.04 ? 278  ALA   A C    1 
ATOM   4284  O  O    . ALA   A 1 278 ? 11.445 11.100  39.812 1.00 20.00 ? 278  ALA   A O    1 
ATOM   4285  C  CB   . ALA   A 1 278 ? 9.227  12.278  38.195 1.00 20.49 ? 278  ALA   A CB   1 
ATOM   4286  H  H    . ALA   A 1 278 ? 10.592 14.038  37.083 1.00 20.06 ? 278  ALA   A H    1 
ATOM   4287  H  HA   . ALA   A 1 278 ? 10.185 13.345  39.652 1.00 22.50 ? 278  ALA   A HA   1 
ATOM   4288  H  HB1  . ALA   A 1 278 ? 8.970  11.543  38.773 1.00 24.59 ? 278  ALA   A HB1  1 
ATOM   4289  H  HB2  . ALA   A 1 278 ? 8.488  12.901  38.117 1.00 24.59 ? 278  ALA   A HB2  1 
ATOM   4290  H  HB3  . ALA   A 1 278 ? 9.454  11.934  37.317 1.00 24.59 ? 278  ALA   A HB3  1 
ATOM   4291  N  N    . ASN   A 1 279 ? 12.681 12.172  38.250 1.00 18.12 ? 279  ASN   A N    1 
ATOM   4292  C  CA   . ASN   A 1 279 ? 13.745 11.140  38.337 1.00 19.40 ? 279  ASN   A CA   1 
ATOM   4293  C  C    . ASN   A 1 279 ? 15.134 11.744  38.576 1.00 22.55 ? 279  ASN   A C    1 
ATOM   4294  O  O    . ASN   A 1 279 ? 15.540 11.815  39.744 1.00 20.48 ? 279  ASN   A O    1 
ATOM   4295  C  CB   . ASN   A 1 279 ? 13.745 10.258  37.086 1.00 18.51 ? 279  ASN   A CB   1 
ATOM   4296  C  CG   . ASN   A 1 279 ? 12.492 9.416   36.964 1.00 23.61 ? 279  ASN   A CG   1 
ATOM   4297  O  OD1  . ASN   A 1 279 ? 12.400 8.346   37.559 1.00 22.08 ? 279  ASN   A OD1  1 
ATOM   4298  N  ND2  . ASN   A 1 279 ? 11.520 9.892   36.203 1.00 21.63 ? 279  ASN   A ND2  1 
ATOM   4299  H  H    . ASN   A 1 279 ? 12.840 12.834  37.725 1.00 21.75 ? 279  ASN   A H    1 
ATOM   4300  H  HA   . ASN   A 1 279 ? 13.542 10.590  39.110 1.00 23.29 ? 279  ASN   A HA   1 
ATOM   4301  H  HB2  . ASN   A 1 279 ? 13.831 10.819  36.299 1.00 22.22 ? 279  ASN   A HB2  1 
ATOM   4302  H  HB3  . ASN   A 1 279 ? 14.521 9.676   37.105 1.00 22.22 ? 279  ASN   A HB3  1 
ATOM   4303  H  HD21 . ASN   A 1 279 ? 10.789 9.448   36.111 1.00 25.96 ? 279  ASN   A HD21 1 
ATOM   4304  H  HD22 . ASN   A 1 279 ? 11.619 10.646  35.801 1.00 25.96 ? 279  ASN   A HD22 1 
ATOM   4305  N  N    . GLN   A 1 280 ? 15.810 12.195  37.519 1.00 15.56 ? 280  GLN   A N    1 
ATOM   4306  C  CA   . GLN   A 1 280 ? 17.231 12.623  37.664 1.00 16.95 ? 280  GLN   A CA   1 
ATOM   4307  C  C    . GLN   A 1 280 ? 17.393 14.059  38.184 1.00 18.89 ? 280  GLN   A C    1 
ATOM   4308  O  O    . GLN   A 1 280 ? 18.542 14.427  38.482 1.00 14.51 ? 280  GLN   A O    1 
ATOM   4309  C  CB   . GLN   A 1 280 ? 17.934 12.451  36.316 1.00 16.24 ? 280  GLN   A CB   1 
ATOM   4310  C  CG   . GLN   A 1 280 ? 17.899 11.025  35.788 1.00 17.82 ? 280  GLN   A CG   1 
ATOM   4311  C  CD   . GLN   A 1 280 ? 16.753 10.796  34.834 1.00 18.61 ? 280  GLN   A CD   1 
ATOM   4312  O  OE1  . GLN   A 1 280 ? 15.748 11.501  34.859 1.00 15.63 ? 280  GLN   A OE1  1 
ATOM   4313  N  NE2  . GLN   A 1 280 ? 16.899 9.796   33.981 1.00 18.33 ? 280  GLN   A NE2  1 
ATOM   4314  H  H    . GLN   A 1 280 ? 15.487 12.265  36.725 1.00 18.68 ? 280  GLN   A H    1 
ATOM   4315  H  HA   . GLN   A 1 280 ? 17.640 12.058  38.338 1.00 20.34 ? 280  GLN   A HA   1 
ATOM   4316  H  HB2  . GLN   A 1 280 ? 17.518 13.039  35.666 1.00 19.49 ? 280  GLN   A HB2  1 
ATOM   4317  H  HB3  . GLN   A 1 280 ? 18.858 12.733  36.403 1.00 19.49 ? 280  GLN   A HB3  1 
ATOM   4318  H  HG2  . GLN   A 1 280 ? 18.736 10.828  35.338 1.00 21.39 ? 280  GLN   A HG2  1 
ATOM   4319  H  HG3  . GLN   A 1 280 ? 17.825 10.408  36.533 1.00 21.39 ? 280  GLN   A HG3  1 
ATOM   4320  H  HE21 . GLN   A 1 280 ? 17.617 9.323   33.992 1.00 22.00 ? 280  GLN   A HE21 1 
ATOM   4321  H  HE22 . GLN   A 1 280 ? 16.276 9.619   33.415 1.00 22.00 ? 280  GLN   A HE22 1 
ATOM   4322  N  N    . LEU   A 1 281 ? 16.315 14.835  38.289 1.00 16.05 ? 281  LEU   A N    1 
ATOM   4323  C  CA   . LEU   A 1 281 ? 16.509 16.246  38.716 1.00 17.08 ? 281  LEU   A CA   1 
ATOM   4324  C  C    . LEU   A 1 281 ? 16.950 16.288  40.182 1.00 15.25 ? 281  LEU   A C    1 
ATOM   4325  O  O    . LEU   A 1 281 ? 16.285 15.650  41.012 1.00 17.49 ? 281  LEU   A O    1 
ATOM   4326  C  CB   . LEU   A 1 281 ? 15.224 17.055  38.531 1.00 16.92 ? 281  LEU   A CB   1 
ATOM   4327  C  CG   . LEU   A 1 281 ? 15.362 18.545  38.840 1.00 14.91 ? 281  LEU   A CG   1 
ATOM   4328  C  CD1  . LEU   A 1 281 ? 16.230 19.237  37.800 1.00 12.54 ? 281  LEU   A CD1  1 
ATOM   4329  C  CD2  . LEU   A 1 281 ? 14.002 19.215  38.935 1.00 12.17 ? 281  LEU   A CD2  1 
ATOM   4330  H  H    . LEU   A 1 281 ? 15.504 14.595  38.131 1.00 19.26 ? 281  LEU   A H    1 
ATOM   4331  H  HA   . LEU   A 1 281 ? 17.199 16.643  38.161 1.00 20.49 ? 281  LEU   A HA   1 
ATOM   4332  H  HB2  . LEU   A 1 281 ? 14.920 16.953  37.615 1.00 20.31 ? 281  LEU   A HB2  1 
ATOM   4333  H  HB3  . LEU   A 1 281 ? 14.535 16.681  39.102 1.00 20.31 ? 281  LEU   A HB3  1 
ATOM   4334  H  HG   . LEU   A 1 281 ? 15.797 18.628  39.703 1.00 17.90 ? 281  LEU   A HG   1 
ATOM   4335  H  HD11 . LEU   A 1 281 ? 16.304 20.180  38.015 1.00 15.06 ? 281  LEU   A HD11 1 
ATOM   4336  H  HD12 . LEU   A 1 281 ? 17.113 18.836  37.797 1.00 15.06 ? 281  LEU   A HD12 1 
ATOM   4337  H  HD13 . LEU   A 1 281 ? 15.827 19.137  36.923 1.00 15.06 ? 281  LEU   A HD13 1 
ATOM   4338  H  HD21 . LEU   A 1 281 ? 14.119 20.158  39.131 1.00 14.61 ? 281  LEU   A HD21 1 
ATOM   4339  H  HD22 . LEU   A 1 281 ? 13.533 19.116  38.092 1.00 14.61 ? 281  LEU   A HD22 1 
ATOM   4340  H  HD23 . LEU   A 1 281 ? 13.485 18.799  39.643 1.00 14.61 ? 281  LEU   A HD23 1 
ATOM   4341  N  N    . VAL   A 1 282 ? 18.022 17.027  40.475 1.00 16.49 ? 282  VAL   A N    1 
ATOM   4342  C  CA   . VAL   A 1 282 ? 18.475 17.203  41.887 1.00 13.62 ? 282  VAL   A CA   1 
ATOM   4343  C  C    . VAL   A 1 282 ? 17.891 18.519  42.409 1.00 12.39 ? 282  VAL   A C    1 
ATOM   4344  O  O    . VAL   A 1 282 ? 17.356 18.528  43.524 1.00 15.49 ? 282  VAL   A O    1 
ATOM   4345  C  CB   . VAL   A 1 282 ? 20.013 17.184  41.982 1.00 16.30 ? 282  VAL   A CB   1 
ATOM   4346  C  CG1  . VAL   A 1 282 ? 20.503 17.525  43.379 1.00 18.08 ? 282  VAL   A CG1  1 
ATOM   4347  C  CG2  . VAL   A 1 282 ? 20.592 15.860  41.511 1.00 18.34 ? 282  VAL   A CG2  1 
ATOM   4348  H  H    . VAL   A 1 282 ? 18.503 17.435  39.890 1.00 19.79 ? 282  VAL   A H    1 
ATOM   4349  H  HA   . VAL   A 1 282 ? 18.159 16.468  42.435 1.00 16.35 ? 282  VAL   A HA   1 
ATOM   4350  H  HB   . VAL   A 1 282 ? 20.335 17.877  41.384 1.00 19.56 ? 282  VAL   A HB   1 
ATOM   4351  H  HG11 . VAL   A 1 282 ? 21.473 17.502  43.397 1.00 21.70 ? 282  VAL   A HG11 1 
ATOM   4352  H  HG12 . VAL   A 1 282 ? 20.196 18.413  43.622 1.00 21.70 ? 282  VAL   A HG12 1 
ATOM   4353  H  HG13 . VAL   A 1 282 ? 20.153 16.878  44.012 1.00 21.70 ? 282  VAL   A HG13 1 
ATOM   4354  H  HG21 . VAL   A 1 282 ? 21.559 15.885  41.585 1.00 22.01 ? 282  VAL   A HG21 1 
ATOM   4355  H  HG22 . VAL   A 1 282 ? 20.244 15.141  42.061 1.00 22.01 ? 282  VAL   A HG22 1 
ATOM   4356  H  HG23 . VAL   A 1 282 ? 20.343 15.708  40.586 1.00 22.01 ? 282  VAL   A HG23 1 
ATOM   4357  N  N    . ARG   A 1 283 ? 17.972 19.579  41.600 1.00 15.17 ? 283  ARG   A N    1 
ATOM   4358  C  CA   . ARG   A 1 283 ? 17.472 20.909  42.024 1.00 13.22 ? 283  ARG   A CA   1 
ATOM   4359  C  C    . ARG   A 1 283 ? 17.520 21.897  40.856 1.00 16.30 ? 283  ARG   A C    1 
ATOM   4360  O  O    . ARG   A 1 283 ? 18.055 21.536  39.793 1.00 14.09 ? 283  ARG   A O    1 
ATOM   4361  C  CB   . ARG   A 1 283 ? 18.353 21.474  43.143 1.00 15.68 ? 283  ARG   A CB   1 
ATOM   4362  C  CG   . ARG   A 1 283 ? 19.839 21.474  42.810 1.00 15.52 ? 283  ARG   A CG   1 
ATOM   4363  C  CD   . ARG   A 1 283 ? 20.640 22.518  43.565 1.00 18.38 ? 283  ARG   A CD   1 
ATOM   4364  N  NE   . ARG   A 1 283 ? 22.071 22.411  43.321 1.00 15.97 ? 283  ARG   A NE   1 
ATOM   4365  C  CZ   . ARG   A 1 283 ? 22.736 23.121  42.416 1.00 18.22 ? 283  ARG   A CZ   1 
ATOM   4366  N  NH1  . ARG   A 1 283 ? 22.090 23.965  41.632 1.00 13.52 ? 283  ARG   A NH1  1 
ATOM   4367  N  NH2  . ARG   A 1 283 ? 24.045 22.985  42.298 1.00 21.25 ? 283  ARG   A NH2  1 
ATOM   4368  H  H    . ARG   A 1 283 ? 18.308 19.558  40.809 1.00 18.21 ? 283  ARG   A H    1 
ATOM   4369  H  HA   . ARG   A 1 283 ? 16.559 20.796  42.332 1.00 15.87 ? 283  ARG   A HA   1 
ATOM   4370  H  HB2  . ARG   A 1 283 ? 18.073 22.382  43.337 1.00 18.81 ? 283  ARG   A HB2  1 
ATOM   4371  H  HB3  . ARG   A 1 283 ? 18.210 20.955  43.950 1.00 18.81 ? 283  ARG   A HB3  1 
ATOM   4372  H  HG2  . ARG   A 1 283 ? 20.205 20.597  43.004 1.00 18.63 ? 283  ARG   A HG2  1 
ATOM   4373  H  HG3  . ARG   A 1 283 ? 19.948 21.623  41.858 1.00 18.63 ? 283  ARG   A HG3  1 
ATOM   4374  H  HD2  . ARG   A 1 283 ? 20.337 23.402  43.307 1.00 22.06 ? 283  ARG   A HD2  1 
ATOM   4375  H  HD3  . ARG   A 1 283 ? 20.470 22.426  44.516 1.00 22.06 ? 283  ARG   A HD3  1 
ATOM   4376  H  HE   . ARG   A 1 283 ? 22.517 21.849  43.796 1.00 19.17 ? 283  ARG   A HE   1 
ATOM   4377  H  HH11 . ARG   A 1 283 ? 21.238 24.055  41.707 1.00 16.23 ? 283  ARG   A HH11 1 
ATOM   4378  H  HH12 . ARG   A 1 283 ? 22.521 24.424  41.047 1.00 16.23 ? 283  ARG   A HH12 1 
ATOM   4379  H  HH21 . ARG   A 1 283 ? 24.468 22.436  42.807 1.00 25.51 ? 283  ARG   A HH21 1 
ATOM   4380  H  HH22 . ARG   A 1 283 ? 24.474 23.445  41.712 1.00 25.51 ? 283  ARG   A HH22 1 
ATOM   4381  N  N    . LYS   A 1 284 ? 16.974 23.092  41.068 1.00 13.40 ? 284  LYS   A N    1 
ATOM   4382  C  CA   . LYS   A 1 284 ? 17.084 24.155  40.040 1.00 16.57 ? 284  LYS   A CA   1 
ATOM   4383  C  C    . LYS   A 1 284 ? 18.509 24.714  40.075 1.00 12.67 ? 284  LYS   A C    1 
ATOM   4384  O  O    . LYS   A 1 284 ? 19.221 24.455  41.057 1.00 16.16 ? 284  LYS   A O    1 
ATOM   4385  C  CB   . LYS   A 1 284 ? 16.083 25.277  40.316 1.00 15.83 ? 284  LYS   A CB   1 
ATOM   4386  C  CG   . LYS   A 1 284 ? 14.627 24.844  40.405 1.00 21.61 ? 284  LYS   A CG   1 
ATOM   4387  C  CD   . LYS   A 1 284 ? 13.685 26.000  40.642 1.00 19.11 ? 284  LYS   A CD   1 
ATOM   4388  C  CE   . LYS   A 1 284 ? 13.981 26.751  41.922 1.00 23.14 ? 284  LYS   A CE   1 
ATOM   4389  N  NZ   . LYS   A 1 284 ? 12.760 27.366  42.491 1.00 28.48 ? 284  LYS   A NZ   1 
ATOM   4390  H  H    . LYS   A 1 284 ? 16.544 23.315  41.779 1.00 16.09 ? 284  LYS   A H    1 
ATOM   4391  H  HA   . LYS   A 1 284 ? 16.887 23.783  39.166 1.00 19.89 ? 284  LYS   A HA   1 
ATOM   4392  H  HB2  . LYS   A 1 284 ? 16.327 25.710  41.149 1.00 19.00 ? 284  LYS   A HB2  1 
ATOM   4393  H  HB3  . LYS   A 1 284 ? 16.165 25.943  39.615 1.00 19.00 ? 284  LYS   A HB3  1 
ATOM   4394  H  HG2  . LYS   A 1 284 ? 14.378 24.392  39.584 1.00 25.93 ? 284  LYS   A HG2  1 
ATOM   4395  H  HG3  . LYS   A 1 284 ? 14.529 24.200  41.124 1.00 25.93 ? 284  LYS   A HG3  1 
ATOM   4396  H  HD2  . LYS   A 1 284 ? 13.739 26.614  39.893 1.00 22.93 ? 284  LYS   A HD2  1 
ATOM   4397  H  HD3  . LYS   A 1 284 ? 12.774 25.668  40.671 1.00 22.93 ? 284  LYS   A HD3  1 
ATOM   4398  H  HE2  . LYS   A 1 284 ? 14.370 26.144  42.571 1.00 27.77 ? 284  LYS   A HE2  1 
ATOM   4399  H  HE3  . LYS   A 1 284 ? 14.640 27.441  41.748 1.00 27.77 ? 284  LYS   A HE3  1 
ATOM   4400  H  HZ1  . LYS   A 1 284 ? 12.869 27.488  43.366 1.00 34.18 ? 284  LYS   A HZ1  1 
ATOM   4401  H  HZ2  . LYS   A 1 284 ? 12.612 28.151  42.098 1.00 34.18 ? 284  LYS   A HZ2  1 
ATOM   4402  H  HZ3  . LYS   A 1 284 ? 12.064 26.829  42.351 1.00 34.18 ? 284  LYS   A HZ3  1 
ATOM   4403  N  N    . ASN   A 1 285 ? 18.888 25.468  39.048 1.00 12.13 ? 285  ASN   A N    1 
ATOM   4404  C  CA   . ASN   A 1 285 ? 20.239 26.075  38.965 1.00 13.28 ? 285  ASN   A CA   1 
ATOM   4405  C  C    . ASN   A 1 285 ? 20.038 27.487  38.417 1.00 14.36 ? 285  ASN   A C    1 
ATOM   4406  O  O    . ASN   A 1 285 ? 20.412 27.732  37.261 1.00 14.47 ? 285  ASN   A O    1 
ATOM   4407  C  CB   . ASN   A 1 285 ? 21.163 25.230  38.091 1.00 15.72 ? 285  ASN   A CB   1 
ATOM   4408  C  CG   . ASN   A 1 285 ? 22.620 25.600  38.258 1.00 14.43 ? 285  ASN   A CG   1 
ATOM   4409  O  OD1  . ASN   A 1 285 ? 23.046 25.964  39.350 1.00 14.28 ? 285  ASN   A OD1  1 
ATOM   4410  N  ND2  . ASN   A 1 285 ? 23.385 25.513  37.183 1.00 14.44 ? 285  ASN   A ND2  1 
ATOM   4411  H  H    . ASN   A 1 285 ? 18.381 25.648  38.377 1.00 14.55 ? 285  ASN   A H    1 
ATOM   4412  H  HA   . ASN   A 1 285 ? 20.672 26.113  39.832 1.00 15.94 ? 285  ASN   A HA   1 
ATOM   4413  H  HB2  . ASN   A 1 285 ? 21.043 24.293  38.311 1.00 18.86 ? 285  ASN   A HB2  1 
ATOM   4414  H  HB3  . ASN   A 1 285 ? 20.910 25.337  37.161 1.00 18.86 ? 285  ASN   A HB3  1 
ATOM   4415  H  HD21 . ASN   A 1 285 ? 24.219 25.716  37.231 1.00 17.33 ? 285  ASN   A HD21 1 
ATOM   4416  H  HD22 . ASN   A 1 285 ? 23.048 25.253  36.435 1.00 17.33 ? 285  ASN   A HD22 1 
ATOM   4417  N  N    . PRO   A 1 286 ? 19.435 28.410  39.191 1.00 12.17 ? 286  PRO   A N    1 
ATOM   4418  C  CA   . PRO   A 1 286 ? 19.087 29.731  38.662 1.00 12.23 ? 286  PRO   A CA   1 
ATOM   4419  C  C    . PRO   A 1 286 ? 20.269 30.652  38.334 1.00 11.14 ? 286  PRO   A C    1 
ATOM   4420  O  O    . PRO   A 1 286 ? 21.241 30.645  39.053 1.00 11.00 ? 286  PRO   A O    1 
ATOM   4421  C  CB   . PRO   A 1 286 ? 18.250 30.358  39.795 1.00 13.39 ? 286  PRO   A CB   1 
ATOM   4422  C  CG   . PRO   A 1 286 ? 17.840 29.186  40.659 1.00 13.32 ? 286  PRO   A CG   1 
ATOM   4423  C  CD   . PRO   A 1 286 ? 19.008 28.228  40.576 1.00 13.62 ? 286  PRO   A CD   1 
ATOM   4424  H  HA   . PRO   A 1 286 ? 18.637 29.629  37.809 1.00 14.68 ? 286  PRO   A HA   1 
ATOM   4425  H  HB2  . PRO   A 1 286 ? 18.768 31.005  40.300 1.00 16.07 ? 286  PRO   A HB2  1 
ATOM   4426  H  HB3  . PRO   A 1 286 ? 17.476 30.826  39.445 1.00 16.07 ? 286  PRO   A HB3  1 
ATOM   4427  H  HG2  . PRO   A 1 286 ? 17.674 29.462  41.574 1.00 15.99 ? 286  PRO   A HG2  1 
ATOM   4428  H  HG3  . PRO   A 1 286 ? 17.023 28.776  40.334 1.00 15.99 ? 286  PRO   A HG3  1 
ATOM   4429  H  HD2  . PRO   A 1 286 ? 19.710 28.452  41.207 1.00 16.35 ? 286  PRO   A HD2  1 
ATOM   4430  H  HD3  . PRO   A 1 286 ? 18.744 27.313  40.759 1.00 16.35 ? 286  PRO   A HD3  1 
ATOM   4431  N  N    . CYS   A 1 287 ? 20.141 31.401  37.240 1.00 11.97 ? 287  CYS   A N    1 
ATOM   4432  C  CA   . CYS   A 1 287 ? 21.181 32.402  36.912 1.00 13.01 ? 287  CYS   A CA   1 
ATOM   4433  C  C    . CYS   A 1 287 ? 21.098 33.548  37.923 1.00 10.94 ? 287  CYS   A C    1 
ATOM   4434  O  O    . CYS   A 1 287 ? 20.207 33.527  38.779 1.00 11.95 ? 287  CYS   A O    1 
ATOM   4435  C  CB   . CYS   A 1 287 ? 20.956 33.010  35.536 1.00 13.29 ? 287  CYS   A CB   1 
ATOM   4436  S  SG   . CYS   A 1 287 ? 20.985 31.812  34.175 1.00 11.79 ? 287  CYS   A SG   1 
ATOM   4437  H  H    . CYS   A 1 287 ? 19.485 31.356  36.685 1.00 14.37 ? 287  CYS   A H    1 
ATOM   4438  H  HA   . CYS   A 1 287 ? 22.041 31.953  36.933 1.00 15.61 ? 287  CYS   A HA   1 
ATOM   4439  H  HB2  . CYS   A 1 287 ? 20.100 33.467  35.532 1.00 15.96 ? 287  CYS   A HB2  1 
ATOM   4440  H  HB3  . CYS   A 1 287 ? 21.637 33.682  35.376 1.00 15.96 ? 287  CYS   A HB3  1 
ATOM   4441  N  N    . TYR   A 1 288 ? 21.980 34.533  37.777 1.00 14.23 ? 288  TYR   A N    1 
ATOM   4442  C  CA   . TYR   A 1 288 ? 22.024 35.688  38.705 1.00 13.01 ? 288  TYR   A CA   1 
ATOM   4443  C  C    . TYR   A 1 288 ? 20.690 36.434  38.779 1.00 12.20 ? 288  TYR   A C    1 
ATOM   4444  O  O    . TYR   A 1 288 ? 20.093 36.670  37.723 1.00 11.19 ? 288  TYR   A O    1 
ATOM   4445  C  CB   . TYR   A 1 288 ? 23.111 36.664  38.247 1.00 13.05 ? 288  TYR   A CB   1 
ATOM   4446  C  CG   . TYR   A 1 288 ? 23.391 37.796  39.203 1.00 13.23 ? 288  TYR   A CG   1 
ATOM   4447  C  CD1  . TYR   A 1 288 ? 24.245 37.626  40.278 1.00 13.96 ? 288  TYR   A CD1  1 
ATOM   4448  C  CD2  . TYR   A 1 288 ? 22.805 39.038  39.030 1.00 12.80 ? 288  TYR   A CD2  1 
ATOM   4449  C  CE1  . TYR   A 1 288 ? 24.509 38.661  41.160 1.00 14.28 ? 288  TYR   A CE1  1 
ATOM   4450  C  CE2  . TYR   A 1 288 ? 23.055 40.083  39.903 1.00 17.70 ? 288  TYR   A CE2  1 
ATOM   4451  C  CZ   . TYR   A 1 288 ? 23.912 39.894  40.972 1.00 16.67 ? 288  TYR   A CZ   1 
ATOM   4452  O  OH   . TYR   A 1 288 ? 24.168 40.925  41.841 1.00 16.33 ? 288  TYR   A OH   1 
ATOM   4453  H  H    . TYR   A 1 288 ? 22.567 34.561  37.149 1.00 17.08 ? 288  TYR   A H    1 
ATOM   4454  H  HA   . TYR   A 1 288 ? 22.217 35.339  39.589 1.00 15.62 ? 288  TYR   A HA   1 
ATOM   4455  H  HB2  . TYR   A 1 288 ? 23.932 36.169  38.103 1.00 15.67 ? 288  TYR   A HB2  1 
ATOM   4456  H  HB3  . TYR   A 1 288 ? 22.852 37.038  37.390 1.00 15.67 ? 288  TYR   A HB3  1 
ATOM   4457  H  HD1  . TYR   A 1 288 ? 24.650 36.800  40.411 1.00 16.75 ? 288  TYR   A HD1  1 
ATOM   4458  H  HD2  . TYR   A 1 288 ? 22.231 39.174  38.311 1.00 15.36 ? 288  TYR   A HD2  1 
ATOM   4459  H  HE1  . TYR   A 1 288 ? 25.086 38.527  41.877 1.00 17.13 ? 288  TYR   A HE1  1 
ATOM   4460  H  HE2  . TYR   A 1 288 ? 22.648 40.909  39.771 1.00 21.24 ? 288  TYR   A HE2  1 
ATOM   4461  H  HH   . TYR   A 1 288 ? 23.448 41.308  42.042 1.00 19.59 ? 288  TYR   A HH   1 
ATOM   4462  N  N    . SER   A 1 289 ? 20.260 36.797  39.990 1.00 14.02 ? 289  SER   A N    1 
ATOM   4463  C  CA   . SER   A 1 289 ? 19.047 37.637  40.184 1.00 15.88 ? 289  SER   A CA   1 
ATOM   4464  C  C    . SER   A 1 289 ? 17.846 37.095  39.401 1.00 12.70 ? 289  SER   A C    1 
ATOM   4465  O  O    . SER   A 1 289 ? 17.086 37.905  38.860 1.00 13.98 ? 289  SER   A O    1 
ATOM   4466  C  CB   . SER   A 1 289 ? 19.336 39.078  39.828 1.00 15.00 ? 289  SER   A CB   1 
ATOM   4467  O  OG   . SER   A 1 289 ? 18.381 39.950  40.407 1.00 15.48 ? 289  SER   A OG   1 
ATOM   4468  H  H    . SER   A 1 289 ? 20.652 36.571  40.722 1.00 16.83 ? 289  SER   A H    1 
ATOM   4469  H  HA   . SER   A 1 289 ? 18.808 37.600  41.123 1.00 19.06 ? 289  SER   A HA   1 
ATOM   4470  H  HB2  . SER   A 1 289 ? 20.224 39.318  40.135 1.00 18.00 ? 289  SER   A HB2  1 
ATOM   4471  H  HB3  . SER   A 1 289 ? 19.331 39.183  38.864 1.00 18.00 ? 289  SER   A HB3  1 
ATOM   4472  H  HG   . SER   A 1 289 ? 18.017 40.407  39.804 1.00 18.58 ? 289  SER   A HG   1 
ATOM   4473  N  N    . CYS   A 1 290 ? 17.680 35.771  39.385 1.00 14.03 ? 290  CYS   A N    1 
ATOM   4474  C  CA   . CYS   A 1 290 ? 16.574 35.179  38.592 1.00 14.92 ? 290  CYS   A CA   1 
ATOM   4475  C  C    . CYS   A 1 290 ? 15.522 34.524  39.494 1.00 14.37 ? 290  CYS   A C    1 
ATOM   4476  O  O    . CYS   A 1 290 ? 15.862 33.566  40.205 1.00 15.57 ? 290  CYS   A O    1 
ATOM   4477  C  CB   . CYS   A 1 290 ? 17.095 34.147  37.606 1.00 12.12 ? 290  CYS   A CB   1 
ATOM   4478  S  SG   . CYS   A 1 290 ? 15.747 33.459  36.611 1.00 14.48 ? 290  CYS   A SG   1 
ATOM   4479  H  H    . CYS   A 1 290 ? 18.173 35.207  39.808 1.00 16.84 ? 290  CYS   A H    1 
ATOM   4480  H  HA   . CYS   A 1 290 ? 16.160 35.908  38.104 1.00 17.91 ? 290  CYS   A HA   1 
ATOM   4481  H  HB2  . CYS   A 1 290 ? 17.755 34.555  37.024 1.00 14.55 ? 290  CYS   A HB2  1 
ATOM   4482  H  HB3  . CYS   A 1 290 ? 17.543 33.433  38.086 1.00 14.55 ? 290  CYS   A HB3  1 
ATOM   4483  N  N    . PRO   A 1 291 ? 14.258 34.998  39.474 1.00 14.06 ? 291  PRO   A N    1 
ATOM   4484  C  CA   . PRO   A 1 291 ? 13.184 34.361  40.242 1.00 15.06 ? 291  PRO   A CA   1 
ATOM   4485  C  C    . PRO   A 1 291 ? 12.537 33.180  39.499 1.00 16.31 ? 291  PRO   A C    1 
ATOM   4486  O  O    . PRO   A 1 291 ? 11.739 32.496  40.093 1.00 14.55 ? 291  PRO   A O    1 
ATOM   4487  C  CB   . PRO   A 1 291 ? 12.168 35.504  40.374 1.00 15.40 ? 291  PRO   A CB   1 
ATOM   4488  C  CG   . PRO   A 1 291 ? 12.331 36.288  39.091 1.00 17.15 ? 291  PRO   A CG   1 
ATOM   4489  C  CD   . PRO   A 1 291 ? 13.803 36.184  38.747 1.00 15.18 ? 291  PRO   A CD   1 
ATOM   4490  H  HA   . PRO   A 1 291 ? 13.502 33.987  41.079 1.00 18.08 ? 291  PRO   A HA   1 
ATOM   4491  H  HB2  . PRO   A 1 291 ? 11.264 35.166  40.471 1.00 18.49 ? 291  PRO   A HB2  1 
ATOM   4492  H  HB3  . PRO   A 1 291 ? 12.351 36.054  41.152 1.00 18.49 ? 291  PRO   A HB3  1 
ATOM   4493  H  HG2  . PRO   A 1 291 ? 11.779 35.921  38.383 1.00 20.58 ? 291  PRO   A HG2  1 
ATOM   4494  H  HG3  . PRO   A 1 291 ? 12.063 37.213  39.209 1.00 20.58 ? 291  PRO   A HG3  1 
ATOM   4495  H  HD2  . PRO   A 1 291 ? 13.938 36.087  37.791 1.00 18.22 ? 291  PRO   A HD2  1 
ATOM   4496  H  HD3  . PRO   A 1 291 ? 14.289 36.977  39.023 1.00 18.22 ? 291  PRO   A HD3  1 
ATOM   4497  N  N    . ILE   A 1 292 ? 12.916 32.965  38.236 1.00 15.28 ? 292  ILE   A N    1 
ATOM   4498  C  CA   . ILE   A 1 292 ? 12.304 31.880  37.410 1.00 14.64 ? 292  ILE   A CA   1 
ATOM   4499  C  C    . ILE   A 1 292 ? 13.038 30.562  37.684 1.00 14.73 ? 292  ILE   A C    1 
ATOM   4500  O  O    . ILE   A 1 292 ? 12.364 29.575  37.984 1.00 17.40 ? 292  ILE   A O    1 
ATOM   4501  C  CB   . ILE   A 1 292 ? 12.306 32.274  35.916 1.00 13.27 ? 292  ILE   A CB   1 
ATOM   4502  C  CG1  . ILE   A 1 292 ? 11.583 33.604  35.685 1.00 13.17 ? 292  ILE   A CG1  1 
ATOM   4503  C  CG2  . ILE   A 1 292 ? 11.725 31.162  35.056 1.00 10.85 ? 292  ILE   A CG2  1 
ATOM   4504  C  CD1  . ILE   A 1 292 ? 11.677 34.120  34.267 1.00 13.88 ? 292  ILE   A CD1  1 
ATOM   4505  H  H    . ILE   A 1 292 ? 13.519 33.424  37.830 1.00 18.34 ? 292  ILE   A H    1 
ATOM   4506  H  HA   . ILE   A 1 292 ? 11.374 31.753  37.656 1.00 17.57 ? 292  ILE   A HA   1 
ATOM   4507  H  HB   . ILE   A 1 292 ? 13.229 32.401  35.646 1.00 15.92 ? 292  ILE   A HB   1 
ATOM   4508  H  HG12 . ILE   A 1 292 ? 10.648 33.497  35.919 1.00 15.81 ? 292  ILE   A HG12 1 
ATOM   4509  H  HG13 . ILE   A 1 292 ? 11.951 34.270  36.286 1.00 15.81 ? 292  ILE   A HG13 1 
ATOM   4510  H  HG21 . ILE   A 1 292 ? 11.737 31.433  34.125 1.00 13.02 ? 292  ILE   A HG21 1 
ATOM   4511  H  HG22 . ILE   A 1 292 ? 12.256 30.357  35.165 1.00 13.02 ? 292  ILE   A HG22 1 
ATOM   4512  H  HG23 . ILE   A 1 292 ? 10.811 30.986  35.329 1.00 13.02 ? 292  ILE   A HG23 1 
ATOM   4513  H  HD11 . ILE   A 1 292 ? 11.199 34.961  34.196 1.00 16.66 ? 292  ILE   A HD11 1 
ATOM   4514  H  HD12 . ILE   A 1 292 ? 12.608 34.258  34.034 1.00 16.66 ? 292  ILE   A HD12 1 
ATOM   4515  H  HD13 . ILE   A 1 292 ? 11.284 33.473  33.660 1.00 16.66 ? 292  ILE   A HD13 1 
ATOM   4516  N  N    . GLY   A 1 293 ? 14.368 30.552  37.582 1.00 14.43 ? 293  GLY   A N    1 
ATOM   4517  C  CA   . GLY   A 1 293 ? 15.146 29.348  37.935 1.00 13.55 ? 293  GLY   A CA   1 
ATOM   4518  C  C    . GLY   A 1 293 ? 14.857 28.165  37.029 1.00 12.48 ? 293  GLY   A C    1 
ATOM   4519  O  O    . GLY   A 1 293 ? 14.694 27.055  37.546 1.00 14.11 ? 293  GLY   A O    1 
ATOM   4520  H  H    . GLY   A 1 293 ? 14.839 31.220  37.315 1.00 17.32 ? 293  GLY   A H    1 
ATOM   4521  H  HA2  . GLY   A 1 293 ? 16.092 29.557  37.893 1.00 16.26 ? 293  GLY   A HA2  1 
ATOM   4522  H  HA3  . GLY   A 1 293 ? 14.951 29.101  38.852 1.00 16.26 ? 293  GLY   A HA3  1 
ATOM   4523  N  N    . CYS   A 1 294 ? 14.837 28.400  35.717 1.00 13.19 ? 294  CYS   A N    1 
ATOM   4524  C  CA   . CYS   A 1 294 ? 14.582 27.300  34.750 1.00 14.13 ? 294  CYS   A CA   1 
ATOM   4525  C  C    . CYS   A 1 294 ? 15.820 26.398  34.674 1.00 12.08 ? 294  CYS   A C    1 
ATOM   4526  O  O    . CYS   A 1 294 ? 15.691 25.249  34.227 1.00 14.25 ? 294  CYS   A O    1 
ATOM   4527  C  CB   . CYS   A 1 294 ? 14.180 27.854  33.383 1.00 13.87 ? 294  CYS   A CB   1 
ATOM   4528  S  SG   . CYS   A 1 294 ? 15.560 28.370  32.322 1.00 12.27 ? 294  CYS   A SG   1 
ATOM   4529  H  H    . CYS   A 1 294 ? 14.965 29.172  35.360 1.00 15.83 ? 294  CYS   A H    1 
ATOM   4530  H  HA   . CYS   A 1 294 ? 13.834 26.763  35.056 1.00 16.96 ? 294  CYS   A HA   1 
ATOM   4531  H  HB2  . CYS   A 1 294 ? 13.666 27.178  32.914 1.00 16.65 ? 294  CYS   A HB2  1 
ATOM   4532  H  HB3  . CYS   A 1 294 ? 13.593 28.614  33.518 1.00 16.65 ? 294  CYS   A HB3  1 
ATOM   4533  N  N    . GLY   A 1 295 ? 16.965 26.894  35.146 1.00 13.01 ? 295  GLY   A N    1 
ATOM   4534  C  CA   . GLY   A 1 295 ? 18.212 26.112  35.094 1.00 14.82 ? 295  GLY   A CA   1 
ATOM   4535  C  C    . GLY   A 1 295 ? 18.056 24.748  35.739 1.00 13.24 ? 295  GLY   A C    1 
ATOM   4536  O  O    . GLY   A 1 295 ? 17.376 24.664  36.764 1.00 14.76 ? 295  GLY   A O    1 
ATOM   4537  H  H    . GLY   A 1 295 ? 17.045 27.674  35.498 1.00 15.62 ? 295  GLY   A H    1 
ATOM   4538  H  HA2  . GLY   A 1 295 ? 18.485 26.002  34.170 1.00 17.79 ? 295  GLY   A HA2  1 
ATOM   4539  H  HA3  . GLY   A 1 295 ? 18.919 26.602  35.543 1.00 17.79 ? 295  GLY   A HA3  1 
ATOM   4540  N  N    . ARG   A 1 296 ? 18.686 23.726  35.156 1.00 14.09 ? 296  ARG   A N    1 
ATOM   4541  C  CA   . ARG   A 1 296 ? 18.543 22.342  35.679 1.00 13.12 ? 296  ARG   A CA   1 
ATOM   4542  C  C    . ARG   A 1 296 ? 19.844 21.821  36.294 1.00 12.57 ? 296  ARG   A C    1 
ATOM   4543  O  O    . ARG   A 1 296 ? 20.915 22.114  35.738 1.00 13.08 ? 296  ARG   A O    1 
ATOM   4544  C  CB   . ARG   A 1 296 ? 18.137 21.372  34.565 1.00 13.97 ? 296  ARG   A CB   1 
ATOM   4545  C  CG   . ARG   A 1 296 ? 16.927 21.815  33.757 1.00 12.10 ? 296  ARG   A CG   1 
ATOM   4546  C  CD   . ARG   A 1 296 ? 15.635 21.634  34.530 1.00 12.10 ? 296  ARG   A CD   1 
ATOM   4547  N  NE   . ARG   A 1 296 ? 15.313 22.811  35.318 1.00 12.52 ? 296  ARG   A NE   1 
ATOM   4548  C  CZ   . ARG   A 1 296 ? 14.355 22.863  36.234 1.00 16.25 ? 296  ARG   A CZ   1 
ATOM   4549  N  NH1  . ARG   A 1 296 ? 13.599 21.804  36.459 1.00 14.49 ? 296  ARG   A NH1  1 
ATOM   4550  N  NH2  . ARG   A 1 296 ? 14.157 23.975  36.921 1.00 14.02 ? 296  ARG   A NH2  1 
ATOM   4551  H  H    . ARG   A 1 296 ? 19.195 23.800  34.467 1.00 16.91 ? 296  ARG   A H    1 
ATOM   4552  H  HA   . ARG   A 1 296 ? 17.856 22.385  36.362 1.00 15.75 ? 296  ARG   A HA   1 
ATOM   4553  H  HB2  . ARG   A 1 296 ? 18.889 21.255  33.963 1.00 16.77 ? 296  ARG   A HB2  1 
ATOM   4554  H  HB3  . ARG   A 1 296 ? 17.950 20.505  34.958 1.00 16.77 ? 296  ARG   A HB3  1 
ATOM   4555  H  HG2  . ARG   A 1 296 ? 17.028 22.747  33.509 1.00 14.53 ? 296  ARG   A HG2  1 
ATOM   4556  H  HG3  . ARG   A 1 296 ? 16.885 21.305  32.933 1.00 14.53 ? 296  ARG   A HG3  1 
ATOM   4557  H  HD2  . ARG   A 1 296 ? 14.911 21.450  33.912 1.00 14.52 ? 296  ARG   A HD2  1 
ATOM   4558  H  HD3  . ARG   A 1 296 ? 15.712 20.864  35.114 1.00 14.52 ? 296  ARG   A HD3  1 
ATOM   4559  H  HE   . ARG   A 1 296 ? 15.775 23.523  35.181 1.00 15.03 ? 296  ARG   A HE   1 
ATOM   4560  H  HH11 . ARG   A 1 296 ? 13.728 21.081  36.012 1.00 17.39 ? 296  ARG   A HH11 1 
ATOM   4561  H  HH12 . ARG   A 1 296 ? 12.978 21.837  37.053 1.00 17.39 ? 296  ARG   A HH12 1 
ATOM   4562  H  HH21 . ARG   A 1 296 ? 14.649 24.665  36.774 1.00 16.83 ? 296  ARG   A HH21 1 
ATOM   4563  H  HH22 . ARG   A 1 296 ? 13.536 24.009  37.515 1.00 16.83 ? 296  ARG   A HH22 1 
ATOM   4564  N  N    . TRP   A 1 297 ? 19.736 21.089  37.404 1.00 13.48 ? 297  TRP   A N    1 
ATOM   4565  C  CA   . TRP   A 1 297 ? 20.900 20.413  38.028 1.00 13.92 ? 297  TRP   A CA   1 
ATOM   4566  C  C    . TRP   A 1 297 ? 20.494 18.942  38.130 1.00 12.14 ? 297  TRP   A C    1 
ATOM   4567  O  O    . TRP   A 1 297 ? 19.494 18.668  38.802 1.00 13.01 ? 297  TRP   A O    1 
ATOM   4568  C  CB   . TRP   A 1 297 ? 21.226 21.025  39.392 1.00 15.03 ? 297  TRP   A CB   1 
ATOM   4569  C  CG   . TRP   A 1 297 ? 22.582 20.647  39.900 1.00 13.76 ? 297  TRP   A CG   1 
ATOM   4570  C  CD1  . TRP   A 1 297 ? 22.872 19.759  40.894 1.00 17.67 ? 297  TRP   A CD1  1 
ATOM   4571  C  CD2  . TRP   A 1 297 ? 23.845 21.147  39.428 1.00 17.78 ? 297  TRP   A CD2  1 
ATOM   4572  N  NE1  . TRP   A 1 297 ? 24.225 19.674  41.076 1.00 18.57 ? 297  TRP   A NE1  1 
ATOM   4573  C  CE2  . TRP   A 1 297 ? 24.849 20.514  40.191 1.00 20.95 ? 297  TRP   A CE2  1 
ATOM   4574  C  CE3  . TRP   A 1 297 ? 24.225 22.064  38.444 1.00 18.43 ? 297  TRP   A CE3  1 
ATOM   4575  C  CZ2  . TRP   A 1 297 ? 26.204 20.771  39.996 1.00 22.65 ? 297  TRP   A CZ2  1 
ATOM   4576  C  CZ3  . TRP   A 1 297 ? 25.565 22.318  38.252 1.00 19.97 ? 297  TRP   A CZ3  1 
ATOM   4577  C  CH2  . TRP   A 1 297 ? 26.538 21.679  39.019 1.00 21.25 ? 297  TRP   A CH2  1 
ATOM   4578  H  H    . TRP   A 1 297 ? 18.994 20.965  37.821 1.00 16.18 ? 297  TRP   A H    1 
ATOM   4579  H  HA   . TRP   A 1 297 ? 21.712 20.516  37.507 1.00 16.71 ? 297  TRP   A HA   1 
ATOM   4580  H  HB2  . TRP   A 1 297 ? 21.169 21.991  39.328 1.00 18.04 ? 297  TRP   A HB2  1 
ATOM   4581  H  HB3  . TRP   A 1 297 ? 20.556 20.743  40.035 1.00 18.04 ? 297  TRP   A HB3  1 
ATOM   4582  H  HD1  . TRP   A 1 297 ? 22.240 19.280  41.379 1.00 21.21 ? 297  TRP   A HD1  1 
ATOM   4583  H  HE1  . TRP   A 1 297 ? 24.621 19.174  41.653 1.00 22.28 ? 297  TRP   A HE1  1 
ATOM   4584  H  HE3  . TRP   A 1 297 ? 23.583 22.496  37.927 1.00 22.12 ? 297  TRP   A HE3  1 
ATOM   4585  H  HZ2  . TRP   A 1 297 ? 26.856 20.346  40.505 1.00 27.18 ? 297  TRP   A HZ2  1 
ATOM   4586  H  HZ3  . TRP   A 1 297 ? 25.825 22.927  37.599 1.00 23.97 ? 297  TRP   A HZ3  1 
ATOM   4587  H  HH2  . TRP   A 1 297 ? 27.435 21.872  38.866 1.00 25.50 ? 297  TRP   A HH2  1 
ATOM   4588  N  N    . VAL   A 1 298 ? 21.229 18.044  37.472 1.00 16.39 ? 298  VAL   A N    1 
ATOM   4589  C  CA   . VAL   A 1 298 ? 20.757 16.630  37.402 1.00 14.84 ? 298  VAL   A CA   1 
ATOM   4590  C  C    . VAL   A 1 298 ? 21.819 15.629  37.862 1.00 14.83 ? 298  VAL   A C    1 
ATOM   4591  O  O    . VAL   A 1 298 ? 22.994 16.010  37.990 1.00 14.60 ? 298  VAL   A O    1 
ATOM   4592  C  CB   . VAL   A 1 298 ? 20.296 16.296  35.968 1.00 14.33 ? 298  VAL   A CB   1 
ATOM   4593  C  CG1  . VAL   A 1 298 ? 19.191 17.228  35.495 1.00 15.04 ? 298  VAL   A CG1  1 
ATOM   4594  C  CG2  . VAL   A 1 298 ? 21.455 16.291  34.983 1.00 13.23 ? 298  VAL   A CG2  1 
ATOM   4595  H  H    . VAL   A 1 298 ? 21.972 18.208  37.072 1.00 19.67 ? 298  VAL   A H    1 
ATOM   4596  H  HA   . VAL   A 1 298 ? 20.009 16.549  38.014 1.00 17.81 ? 298  VAL   A HA   1 
ATOM   4597  H  HB   . VAL   A 1 298 ? 19.932 15.397  36.000 1.00 17.20 ? 298  VAL   A HB   1 
ATOM   4598  H  HG11 . VAL   A 1 298 ? 18.929 16.987  34.593 1.00 18.05 ? 298  VAL   A HG11 1 
ATOM   4599  H  HG12 . VAL   A 1 298 ? 18.426 17.149  36.086 1.00 18.05 ? 298  VAL   A HG12 1 
ATOM   4600  H  HG13 . VAL   A 1 298 ? 19.513 18.143  35.505 1.00 18.05 ? 298  VAL   A HG13 1 
ATOM   4601  H  HG21 . VAL   A 1 298 ? 21.125 16.078  34.096 1.00 15.88 ? 298  VAL   A HG21 1 
ATOM   4602  H  HG22 . VAL   A 1 298 ? 21.873 17.166  34.970 1.00 15.88 ? 298  VAL   A HG22 1 
ATOM   4603  H  HG23 . VAL   A 1 298 ? 22.107 15.626  35.254 1.00 15.88 ? 298  VAL   A HG23 1 
ATOM   4604  N  N    . ARG   A 1 299 ? 21.389 14.381  38.066 1.00 14.13 ? 299  ARG   A N    1 
ATOM   4605  C  CA   . ARG   A 1 299 ? 22.320 13.301  38.478 1.00 12.73 ? 299  ARG   A CA   1 
ATOM   4606  C  C    . ARG   A 1 299 ? 22.531 12.352  37.299 1.00 15.53 ? 299  ARG   A C    1 
ATOM   4607  O  O    . ARG   A 1 299 ? 21.542 11.780  36.822 1.00 17.66 ? 299  ARG   A O    1 
ATOM   4608  C  CB   . ARG   A 1 299 ? 21.722 12.533  39.656 1.00 19.22 ? 299  ARG   A CB   1 
ATOM   4609  C  CG   . ARG   A 1 299 ? 22.587 11.395  40.176 1.00 23.59 ? 299  ARG   A CG   1 
ATOM   4610  C  CD   . ARG   A 1 299 ? 21.955 10.788  41.413 1.00 30.20 ? 299  ARG   A CD   1 
ATOM   4611  N  NE   . ARG   A 1 299 ? 21.576 11.798  42.391 1.00 38.46 ? 299  ARG   A NE   1 
ATOM   4612  C  CZ   . ARG   A 1 299 ? 20.325 12.142  42.680 1.00 36.01 ? 299  ARG   A CZ   1 
ATOM   4613  N  NH1  . ARG   A 1 299 ? 19.325 11.657  41.967 1.00 33.42 ? 299  ARG   A NH1  1 
ATOM   4614  N  NH2  . ARG   A 1 299 ? 20.078 12.969  43.681 1.00 26.63 ? 299  ARG   A NH2  1 
ATOM   4615  H  H    . ARG   A 1 299 ? 20.571 14.132  37.974 1.00 16.96 ? 299  ARG   A H    1 
ATOM   4616  H  HA   . ARG   A 1 299 ? 23.170 13.683  38.747 1.00 15.28 ? 299  ARG   A HA   1 
ATOM   4617  H  HB2  . ARG   A 1 299 ? 21.556 13.155  40.382 1.00 23.06 ? 299  ARG   A HB2  1 
ATOM   4618  H  HB3  . ARG   A 1 299 ? 20.862 12.173  39.389 1.00 23.06 ? 299  ARG   A HB3  1 
ATOM   4619  H  HG2  . ARG   A 1 299 ? 22.690 10.717  39.490 1.00 28.31 ? 299  ARG   A HG2  1 
ATOM   4620  H  HG3  . ARG   A 1 299 ? 23.475 11.723  40.385 1.00 28.31 ? 299  ARG   A HG3  1 
ATOM   4621  H  HD2  . ARG   A 1 299 ? 21.170 10.279  41.156 1.00 36.24 ? 299  ARG   A HD2  1 
ATOM   4622  H  HD3  . ARG   A 1 299 ? 22.577 10.165  41.819 1.00 36.24 ? 299  ARG   A HD3  1 
ATOM   4623  H  HE   . ARG   A 1 299 ? 22.208 12.201  42.812 1.00 46.16 ? 299  ARG   A HE   1 
ATOM   4624  H  HH11 . ARG   A 1 299 ? 19.483 11.118  41.315 1.00 40.11 ? 299  ARG   A HH11 1 
ATOM   4625  H  HH12 . ARG   A 1 299 ? 18.516 11.880  42.154 1.00 40.11 ? 299  ARG   A HH12 1 
ATOM   4626  H  HH21 . ARG   A 1 299 ? 20.727 13.286  44.147 1.00 31.96 ? 299  ARG   A HH21 1 
ATOM   4627  H  HH22 . ARG   A 1 299 ? 19.268 13.190  43.866 1.00 31.96 ? 299  ARG   A HH22 1 
ATOM   4628  N  N    . LEU   A 1 300 ? 23.777 12.201  36.863 1.00 14.68 ? 300  LEU   A N    1 
ATOM   4629  C  CA   . LEU   A 1 300 ? 24.082 11.269  35.750 1.00 18.23 ? 300  LEU   A CA   1 
ATOM   4630  C  C    . LEU   A 1 300 ? 23.896 9.829   36.248 1.00 18.27 ? 300  LEU   A C    1 
ATOM   4631  O  O    . LEU   A 1 300 ? 23.771 9.628   37.465 1.00 18.37 ? 300  LEU   A O    1 
ATOM   4632  C  CB   . LEU   A 1 300 ? 25.514 11.513  35.266 1.00 19.13 ? 300  LEU   A CB   1 
ATOM   4633  C  CG   . LEU   A 1 300 ? 25.788 12.907  34.706 1.00 18.07 ? 300  LEU   A CG   1 
ATOM   4634  C  CD1  . LEU   A 1 300 ? 27.164 12.968  34.061 1.00 18.50 ? 300  LEU   A CD1  1 
ATOM   4635  C  CD2  . LEU   A 1 300 ? 24.714 13.308  33.707 1.00 19.24 ? 300  LEU   A CD2  1 
ATOM   4636  H  H    . LEU   A 1 300 ? 24.458 12.616  37.184 1.00 17.62 ? 300  LEU   A H    1 
ATOM   4637  H  HA   . LEU   A 1 300 ? 23.482 11.417  35.002 1.00 21.88 ? 300  LEU   A HA   1 
ATOM   4638  H  HB2  . LEU   A 1 300 ? 26.121 11.353  36.006 1.00 22.96 ? 300  LEU   A HB2  1 
ATOM   4639  H  HB3  . LEU   A 1 300 ? 25.723 10.859  34.581 1.00 22.96 ? 300  LEU   A HB3  1 
ATOM   4640  H  HG   . LEU   A 1 300 ? 25.768 13.536  35.444 1.00 21.68 ? 300  LEU   A HG   1 
ATOM   4641  H  HD11 . LEU   A 1 300 ? 27.319 13.860  33.712 1.00 22.20 ? 300  LEU   A HD11 1 
ATOM   4642  H  HD12 . LEU   A 1 300 ? 27.841 12.758  34.723 1.00 22.20 ? 300  LEU   A HD12 1 
ATOM   4643  H  HD13 . LEU   A 1 300 ? 27.211 12.325  33.336 1.00 22.20 ? 300  LEU   A HD13 1 
ATOM   4644  H  HD21 . LEU   A 1 300 ? 24.906 14.195  33.364 1.00 23.10 ? 300  LEU   A HD21 1 
ATOM   4645  H  HD22 . LEU   A 1 300 ? 24.701 12.673  32.973 1.00 23.10 ? 300  LEU   A HD22 1 
ATOM   4646  H  HD23 . LEU   A 1 300 ? 23.849 13.312  34.146 1.00 23.10 ? 300  LEU   A HD23 1 
ATOM   4647  N  N    . LYS   A 1 301 ? 23.869 8.880   35.321 1.00 18.81 ? 301  LYS   A N    1 
ATOM   4648  C  CA   . LYS   A 1 301 ? 23.645 7.463   35.706 1.00 22.80 ? 301  LYS   A CA   1 
ATOM   4649  C  C    . LYS   A 1 301 ? 24.722 7.038   36.711 1.00 25.18 ? 301  LYS   A C    1 
ATOM   4650  O  O    . LYS   A 1 301 ? 24.414 6.200   37.575 1.00 23.18 ? 301  LYS   A O    1 
ATOM   4651  C  CB   . LYS   A 1 301 ? 23.647 6.587   34.450 1.00 22.59 ? 301  LYS   A CB   1 
ATOM   4652  C  CG   . LYS   A 1 301 ? 23.357 5.111   34.687 1.00 30.90 ? 301  LYS   A CG   1 
ATOM   4653  C  CD   . LYS   A 1 301 ? 23.323 4.299   33.411 1.00 37.98 ? 301  LYS   A CD   1 
ATOM   4654  C  CE   . LYS   A 1 301 ? 23.058 2.828   33.651 1.00 57.84 ? 301  LYS   A CE   1 
ATOM   4655  N  NZ   . LYS   A 1 301 ? 23.030 2.056   32.386 1.00 65.06 ? 301  LYS   A NZ   1 
ATOM   4656  H  H    . LYS   A 1 301 ? 23.974 9.016   34.478 1.00 22.57 ? 301  LYS   A H    1 
ATOM   4657  H  HA   . LYS   A 1 301 ? 22.781 7.357   36.134 1.00 27.36 ? 301  LYS   A HA   1 
ATOM   4658  H  HB2  . LYS   A 1 301 ? 22.988 6.935   33.829 1.00 27.12 ? 301  LYS   A HB2  1 
ATOM   4659  H  HB3  . LYS   A 1 301 ? 24.512 6.667   34.019 1.00 27.12 ? 301  LYS   A HB3  1 
ATOM   4660  H  HG2  . LYS   A 1 301 ? 24.033 4.745   35.278 1.00 37.08 ? 301  LYS   A HG2  1 
ATOM   4661  H  HG3  . LYS   A 1 301 ? 22.505 5.024   35.142 1.00 37.08 ? 301  LYS   A HG3  1 
ATOM   4662  H  HD2  . LYS   A 1 301 ? 22.636 4.655   32.826 1.00 45.58 ? 301  LYS   A HD2  1 
ATOM   4663  H  HD3  . LYS   A 1 301 ? 24.170 4.398   32.948 1.00 45.58 ? 301  LYS   A HD3  1 
ATOM   4664  H  HE2  . LYS   A 1 301 ? 23.744 2.467   34.234 1.00 69.41 ? 301  LYS   A HE2  1 
ATOM   4665  H  HE3  . LYS   A 1 301 ? 22.211 2.724   34.112 1.00 69.41 ? 301  LYS   A HE3  1 
ATOM   4666  H  HZ1  . LYS   A 1 301 ? 22.872 1.198   32.565 1.00 78.08 ? 301  LYS   A HZ1  1 
ATOM   4667  H  HZ2  . LYS   A 1 301 ? 22.386 2.372   31.859 1.00 78.08 ? 301  LYS   A HZ2  1 
ATOM   4668  H  HZ3  . LYS   A 1 301 ? 23.815 2.133   31.973 1.00 78.08 ? 301  LYS   A HZ3  1 
ATOM   4669  N  N    . ASP   A 1 302 ? 25.925 7.605   36.611 1.00 20.64 ? 302  ASP   A N    1 
ATOM   4670  C  CA   . ASP   A 1 302 ? 27.046 7.188   37.501 1.00 23.48 ? 302  ASP   A CA   1 
ATOM   4671  C  C    . ASP   A 1 302 ? 26.989 7.917   38.855 1.00 24.86 ? 302  ASP   A C    1 
ATOM   4672  O  O    . ASP   A 1 302 ? 27.886 7.679   39.680 1.00 23.34 ? 302  ASP   A O    1 
ATOM   4673  C  CB   . ASP   A 1 302 ? 28.400 7.363   36.807 1.00 22.80 ? 302  ASP   A CB   1 
ATOM   4674  C  CG   . ASP   A 1 302 ? 28.857 8.804   36.658 1.00 28.52 ? 302  ASP   A CG   1 
ATOM   4675  O  OD1  . ASP   A 1 302 ? 28.116 9.705   37.085 1.00 22.73 ? 302  ASP   A OD1  1 
ATOM   4676  O  OD2  . ASP   A 1 302 ? 29.957 9.009   36.112 1.00 27.25 ? 302  ASP   A OD2  1 
ATOM   4677  H  H    . ASP   A 1 302 ? 26.124 8.224   36.048 1.00 24.77 ? 302  ASP   A H    1 
ATOM   4678  H  HA   . ASP   A 1 302 ? 26.942 6.242   37.687 1.00 28.18 ? 302  ASP   A HA   1 
ATOM   4679  H  HB2  . ASP   A 1 302 ? 29.072 6.874   37.308 1.00 27.36 ? 302  ASP   A HB2  1 
ATOM   4680  H  HB3  . ASP   A 1 302 ? 28.353 6.959   35.926 1.00 27.36 ? 302  ASP   A HB3  1 
ATOM   4681  N  N    . GLY   A 1 303 ? 25.981 8.764   39.072 1.00 23.40 ? 303  GLY   A N    1 
ATOM   4682  C  CA   . GLY   A 1 303 ? 25.847 9.495   40.349 1.00 22.77 ? 303  GLY   A CA   1 
ATOM   4683  C  C    . GLY   A 1 303 ? 26.492 10.871  40.321 1.00 23.43 ? 303  GLY   A C    1 
ATOM   4684  O  O    . GLY   A 1 303 ? 26.291 11.627  41.287 1.00 24.58 ? 303  GLY   A O    1 
ATOM   4685  H  H    . GLY   A 1 303 ? 25.363 8.933   38.498 1.00 28.08 ? 303  GLY   A H    1 
ATOM   4686  H  HA2  . GLY   A 1 303 ? 24.906 9.590   40.564 1.00 27.33 ? 303  GLY   A HA2  1 
ATOM   4687  H  HA3  . GLY   A 1 303 ? 26.249 8.970   41.059 1.00 27.33 ? 303  GLY   A HA3  1 
ATOM   4688  N  N    . THR   A 1 304 ? 27.229 11.194  39.256 1.00 21.01 ? 304  THR   A N    1 
ATOM   4689  C  CA   . THR   A 1 304 ? 27.835 12.544  39.111 1.00 22.67 ? 304  THR   A CA   1 
ATOM   4690  C  C    . THR   A 1 304 ? 26.723 13.590  39.004 1.00 21.37 ? 304  THR   A C    1 
ATOM   4691  O  O    . THR   A 1 304 ? 25.733 13.320  38.306 1.00 22.12 ? 304  THR   A O    1 
ATOM   4692  C  CB   . THR   A 1 304 ? 28.734 12.630  37.871 1.00 22.82 ? 304  THR   A CB   1 
ATOM   4693  O  OG1  . THR   A 1 304 ? 29.774 11.658  37.980 1.00 31.11 ? 304  THR   A OG1  1 
ATOM   4694  C  CG2  . THR   A 1 304 ? 29.347 14.001  37.686 1.00 28.57 ? 304  THR   A CG2  1 
ATOM   4695  H  H    . THR   A 1 304 ? 27.395 10.657  38.605 1.00 25.21 ? 304  THR   A H    1 
ATOM   4696  H  HA   . THR   A 1 304 ? 28.384 12.713  39.893 1.00 27.21 ? 304  THR   A HA   1 
ATOM   4697  H  HB   . THR   A 1 304 ? 28.177 12.458  37.096 1.00 27.39 ? 304  THR   A HB   1 
ATOM   4698  H  HG1  . THR   A 1 304 ? 29.436 10.894  38.066 1.00 37.34 ? 304  THR   A HG1  1 
ATOM   4699  H  HG21 . THR   A 1 304 ? 29.904 14.002  36.892 1.00 34.29 ? 304  THR   A HG21 1 
ATOM   4700  H  HG22 . THR   A 1 304 ? 28.642 14.660  37.587 1.00 34.29 ? 304  THR   A HG22 1 
ATOM   4701  H  HG23 . THR   A 1 304 ? 29.888 14.221  38.460 1.00 34.29 ? 304  THR   A HG23 1 
ATOM   4702  N  N    . GLU   A 1 305 ? 26.894 14.741  39.658 1.00 17.90 ? 305  GLU   A N    1 
ATOM   4703  C  CA   . GLU   A 1 305 ? 25.890 15.834  39.577 1.00 18.09 ? 305  GLU   A CA   1 
ATOM   4704  C  C    . GLU   A 1 305 ? 26.441 16.936  38.665 1.00 21.36 ? 305  GLU   A C    1 
ATOM   4705  O  O    . GLU   A 1 305 ? 27.644 17.222  38.753 1.00 22.75 ? 305  GLU   A O    1 
ATOM   4706  C  CB   . GLU   A 1 305 ? 25.567 16.360  40.975 1.00 19.22 ? 305  GLU   A CB   1 
ATOM   4707  C  CG   . GLU   A 1 305 ? 24.738 15.400  41.805 1.00 23.95 ? 305  GLU   A CG   1 
ATOM   4708  C  CD   . GLU   A 1 305 ? 24.317 15.949  43.157 1.00 30.73 ? 305  GLU   A CD   1 
ATOM   4709  O  OE1  . GLU   A 1 305 ? 24.456 17.168  43.367 1.00 28.97 ? 305  GLU   A OE1  1 
ATOM   4710  O  OE2  . GLU   A 1 305 ? 23.855 15.154  43.996 1.00 36.70 ? 305  GLU   A OE2  1 
ATOM   4711  H  H    . GLU   A 1 305 ? 27.575 14.918  40.153 1.00 21.49 ? 305  GLU   A H    1 
ATOM   4712  H  HA   . GLU   A 1 305 ? 25.060 15.504  39.200 1.00 21.72 ? 305  GLU   A HA   1 
ATOM   4713  H  HB2  . GLU   A 1 305 ? 26.396 16.547  41.442 1.00 23.07 ? 305  GLU   A HB2  1 
ATOM   4714  H  HB3  . GLU   A 1 305 ? 25.091 17.201  40.894 1.00 23.07 ? 305  GLU   A HB3  1 
ATOM   4715  H  HG2  . GLU   A 1 305 ? 23.943 15.158  41.304 1.00 28.74 ? 305  GLU   A HG2  1 
ATOM   4716  H  HG3  . GLU   A 1 305 ? 25.246 14.585  41.942 1.00 28.74 ? 305  GLU   A HG3  1 
ATOM   4717  N  N    . CYS   A 1 306 ? 25.588 17.513  37.816 1.00 18.64 ? 306  CYS   A N    1 
ATOM   4718  C  CA   . CYS   A 1 306 ? 26.061 18.544  36.857 1.00 17.63 ? 306  CYS   A CA   1 
ATOM   4719  C  C    . CYS   A 1 306 ? 24.872 19.276  36.232 1.00 14.92 ? 306  CYS   A C    1 
ATOM   4720  O  O    . CYS   A 1 306 ? 23.727 18.861  36.468 1.00 14.89 ? 306  CYS   A O    1 
ATOM   4721  C  CB   . CYS   A 1 306 ? 26.905 17.909  35.760 1.00 15.58 ? 306  CYS   A CB   1 
ATOM   4722  S  SG   . CYS   A 1 306 ? 25.982 16.737  34.729 1.00 18.89 ? 306  CYS   A SG   1 
ATOM   4723  H  H    . CYS   A 1 306 ? 24.748 17.334  37.771 1.00 22.37 ? 306  CYS   A H    1 
ATOM   4724  H  HA   . CYS   A 1 306 ? 26.607 19.181  37.344 1.00 21.16 ? 306  CYS   A HA   1 
ATOM   4725  H  HB2  . CYS   A 1 306 ? 27.269 18.609  35.196 1.00 18.70 ? 306  CYS   A HB2  1 
ATOM   4726  H  HB3  . CYS   A 1 306 ? 27.658 17.450  36.165 1.00 18.70 ? 306  CYS   A HB3  1 
ATOM   4727  H  HG   . CYS   A 1 306 ? 26.710 16.282  33.890 1.00 22.67 ? 306  CYS   A HG   1 
ATOM   4728  N  N    . GLY   A 1 307 ? 25.160 20.341  35.484 1.00 15.38 ? 307  GLY   A N    1 
ATOM   4729  C  CA   . GLY   A 1 307 ? 24.093 21.080  34.793 1.00 14.32 ? 307  GLY   A CA   1 
ATOM   4730  C  C    . GLY   A 1 307 ? 23.275 20.147  33.922 1.00 14.60 ? 307  GLY   A C    1 
ATOM   4731  O  O    . GLY   A 1 307 ? 23.870 19.320  33.216 1.00 13.42 ? 307  GLY   A O    1 
ATOM   4732  H  H    . GLY   A 1 307 ? 25.953 20.651  35.363 1.00 18.46 ? 307  GLY   A H    1 
ATOM   4733  H  HA2  . GLY   A 1 307 ? 23.517 21.511  35.444 1.00 17.19 ? 307  GLY   A HA2  1 
ATOM   4734  H  HA3  . GLY   A 1 307 ? 24.480 21.783  34.248 1.00 17.19 ? 307  GLY   A HA3  1 
ATOM   4735  N  N    . GLY   A 1 308 ? 21.955 20.316  33.947 1.00 12.91 ? 308  GLY   A N    1 
ATOM   4736  C  CA   . GLY   A 1 308 ? 21.071 19.423  33.182 1.00 14.19 ? 308  GLY   A CA   1 
ATOM   4737  C  C    . GLY   A 1 308 ? 20.708 19.972  31.818 1.00 12.97 ? 308  GLY   A C    1 
ATOM   4738  O  O    . GLY   A 1 308 ? 21.068 21.120  31.520 1.00 13.41 ? 308  GLY   A O    1 
ATOM   4739  H  H    . GLY   A 1 308 ? 21.551 20.931  34.392 1.00 15.50 ? 308  GLY   A H    1 
ATOM   4740  H  HA2  . GLY   A 1 308 ? 21.505 18.562  33.073 1.00 17.03 ? 308  GLY   A HA2  1 
ATOM   4741  H  HA3  . GLY   A 1 308 ? 20.259 19.269  33.689 1.00 17.03 ? 308  GLY   A HA3  1 
ATOM   4742  N  N    . PRO   A 1 309 ? 19.970 19.202  30.994 1.00 11.81 ? 309  PRO   A N    1 
ATOM   4743  C  CA   . PRO   A 1 309 ? 19.672 19.613  29.627 1.00 11.82 ? 309  PRO   A CA   1 
ATOM   4744  C  C    . PRO   A 1 309 ? 18.463 20.528  29.431 1.00 12.25 ? 309  PRO   A C    1 
ATOM   4745  O  O    . PRO   A 1 309 ? 17.506 20.435  30.179 1.00 11.19 ? 309  PRO   A O    1 
ATOM   4746  C  CB   . PRO   A 1 309 ? 19.361 18.264  28.960 1.00 10.41 ? 309  PRO   A CB   1 
ATOM   4747  C  CG   . PRO   A 1 309 ? 18.698 17.468  30.058 1.00 10.79 ? 309  PRO   A CG   1 
ATOM   4748  C  CD   . PRO   A 1 309 ? 19.410 17.891  31.327 1.00 10.96 ? 309  PRO   A CD   1 
ATOM   4749  H  HA   . PRO   A 1 309 ? 20.409 20.137  29.276 1.00 14.19 ? 309  PRO   A HA   1 
ATOM   4750  H  HB2  . PRO   A 1 309 ? 18.775 18.371  28.194 1.00 12.49 ? 309  PRO   A HB2  1 
ATOM   4751  H  HB3  . PRO   A 1 309 ? 20.168 17.829  28.642 1.00 12.49 ? 309  PRO   A HB3  1 
ATOM   4752  H  HG2  . PRO   A 1 309 ? 17.748 17.659  30.107 1.00 12.95 ? 309  PRO   A HG2  1 
ATOM   4753  H  HG3  . PRO   A 1 309 ? 18.788 16.514  29.905 1.00 12.95 ? 309  PRO   A HG3  1 
ATOM   4754  H  HD2  . PRO   A 1 309 ? 18.798 17.946  32.077 1.00 13.15 ? 309  PRO   A HD2  1 
ATOM   4755  H  HD3  . PRO   A 1 309 ? 20.104 17.260  31.573 1.00 13.15 ? 309  PRO   A HD3  1 
ATOM   4756  N  N    . GLU   A 1 310 ? 18.559 21.381  28.414 1.00 11.26 ? 310  GLU   A N    1 
ATOM   4757  C  CA   . GLU   A 1 310 ? 17.417 22.253  28.058 1.00 10.31 ? 310  GLU   A CA   1 
ATOM   4758  C  C    . GLU   A 1 310 ? 16.558 21.512  27.033 1.00 8.21  ? 310  GLU   A C    1 
ATOM   4759  O  O    . GLU   A 1 310 ? 16.990 20.465  26.542 1.00 11.27 ? 310  GLU   A O    1 
ATOM   4760  C  CB   . GLU   A 1 310 ? 17.914 23.547  27.418 1.00 9.42  ? 310  GLU   A CB   1 
ATOM   4761  C  CG   . GLU   A 1 310 ? 19.020 24.217  28.208 1.00 11.33 ? 310  GLU   A CG   1 
ATOM   4762  C  CD   . GLU   A 1 310 ? 18.526 24.982  29.422 1.00 13.98 ? 310  GLU   A CD   1 
ATOM   4763  O  OE1  . GLU   A 1 310 ? 17.302 25.014  29.635 1.00 10.17 ? 310  GLU   A OE1  1 
ATOM   4764  O  OE2  . GLU   A 1 310 ? 19.367 25.550  30.139 1.00 10.80 ? 310  GLU   A OE2  1 
ATOM   4765  H  H    . GLU   A 1 310 ? 19.257 21.477  27.921 1.00 13.52 ? 310  GLU   A H    1 
ATOM   4766  H  HA   . GLU   A 1 310 ? 16.912 22.466  28.859 1.00 12.38 ? 310  GLU   A HA   1 
ATOM   4767  H  HB2  . GLU   A 1 310 ? 18.234 23.356  26.523 1.00 11.31 ? 310  GLU   A HB2  1 
ATOM   4768  H  HB3  . GLU   A 1 310 ? 17.170 24.163  27.328 1.00 11.31 ? 310  GLU   A HB3  1 
ATOM   4769  H  HG2  . GLU   A 1 310 ? 19.654 23.542  28.497 1.00 13.60 ? 310  GLU   A HG2  1 
ATOM   4770  H  HG3  . GLU   A 1 310 ? 19.500 24.826  27.625 1.00 13.60 ? 310  GLU   A HG3  1 
ATOM   4771  N  N    . TYR   A 1 311 ? 15.402 22.082  26.713 1.00 9.89  ? 311  TYR   A N    1 
ATOM   4772  C  CA   . TYR   A 1 311 ? 14.495 21.445  25.728 1.00 10.59 ? 311  TYR   A CA   1 
ATOM   4773  C  C    . TYR   A 1 311 ? 15.213 21.138  24.410 1.00 10.65 ? 311  TYR   A C    1 
ATOM   4774  O  O    . TYR   A 1 311 ? 15.115 20.000  23.933 1.00 10.00 ? 311  TYR   A O    1 
ATOM   4775  C  CB   . TYR   A 1 311 ? 13.290 22.343  25.454 1.00 9.73  ? 311  TYR   A CB   1 
ATOM   4776  C  CG   . TYR   A 1 311 ? 12.470 21.903  24.269 1.00 11.43 ? 311  TYR   A CG   1 
ATOM   4777  C  CD1  . TYR   A 1 311 ? 11.920 20.634  24.221 1.00 8.29  ? 311  TYR   A CD1  1 
ATOM   4778  C  CD2  . TYR   A 1 311 ? 12.261 22.742  23.187 1.00 11.61 ? 311  TYR   A CD2  1 
ATOM   4779  C  CE1  . TYR   A 1 311 ? 11.173 20.212  23.135 1.00 10.70 ? 311  TYR   A CE1  1 
ATOM   4780  C  CE2  . TYR   A 1 311 ? 11.515 22.335  22.093 1.00 12.92 ? 311  TYR   A CE2  1 
ATOM   4781  C  CZ   . TYR   A 1 311 ? 10.969 21.065  22.067 1.00 11.13 ? 311  TYR   A CZ   1 
ATOM   4782  O  OH   . TYR   A 1 311 ? 10.231 20.642  20.989 1.00 8.52  ? 311  TYR   A OH   1 
ATOM   4783  H  H    . TYR   A 1 311 ? 15.117 22.824  27.041 1.00 11.88 ? 311  TYR   A H    1 
ATOM   4784  H  HA   . TYR   A 1 311 ? 14.196 20.607  26.113 1.00 12.72 ? 311  TYR   A HA   1 
ATOM   4785  H  HB2  . TYR   A 1 311 ? 12.724 22.361  26.241 1.00 11.68 ? 311  TYR   A HB2  1 
ATOM   4786  H  HB3  . TYR   A 1 311 ? 13.599 23.250  25.306 1.00 11.68 ? 311  TYR   A HB3  1 
ATOM   4787  H  HD1  . TYR   A 1 311 ? 12.055 20.052  24.934 1.00 9.95  ? 311  TYR   A HD1  1 
ATOM   4788  H  HD2  . TYR   A 1 311 ? 12.629 23.596  23.195 1.00 13.94 ? 311  TYR   A HD2  1 
ATOM   4789  H  HE1  . TYR   A 1 311 ? 10.809 19.356  23.124 1.00 12.85 ? 311  TYR   A HE1  1 
ATOM   4790  H  HE2  . TYR   A 1 311 ? 11.382 22.914  21.378 1.00 15.51 ? 311  TYR   A HE2  1 
ATOM   4791  H  HH   . TYR   A 1 311 ? 10.430 21.103  20.315 1.00 10.23 ? 311  TYR   A HH   1 
ATOM   4792  N  N    . GLU   A 1 312 ? 15.897 22.125  23.823 1.00 11.31 ? 312  GLU   A N    1 
ATOM   4793  C  CA   . GLU   A 1 312 ? 16.463 21.868  22.500 1.00 8.69  ? 312  GLU   A CA   1 
ATOM   4794  C  C    . GLU   A 1 312 ? 17.478 20.735  22.543 1.00 9.77  ? 312  GLU   A C    1 
ATOM   4795  O  O    . GLU   A 1 312 ? 17.630 20.001  21.560 1.00 8.42  ? 312  GLU   A O    1 
ATOM   4796  C  CB   . GLU   A 1 312 ? 17.110 23.142  21.935 1.00 8.06  ? 312  GLU   A CB   1 
ATOM   4797  C  CG   . GLU   A 1 312 ? 16.341 24.438  22.232 1.00 7.78  ? 312  GLU   A CG   1 
ATOM   4798  C  CD   . GLU   A 1 312 ? 14.961 24.526  21.579 1.00 11.24 ? 312  GLU   A CD   1 
ATOM   4799  O  OE1  . GLU   A 1 312 ? 14.736 23.912  20.509 1.00 12.36 ? 312  GLU   A OE1  1 
ATOM   4800  O  OE2  . GLU   A 1 312 ? 14.102 25.251  22.134 1.00 12.73 ? 312  GLU   A OE2  1 
ATOM   4801  H  H    . GLU   A 1 312 ? 16.038 22.907  24.152 1.00 13.58 ? 312  GLU   A H    1 
ATOM   4802  H  HA   . GLU   A 1 312 ? 15.738 21.599  21.915 1.00 10.43 ? 312  GLU   A HA   1 
ATOM   4803  H  HB2  . GLU   A 1 312 ? 18.007 23.222  22.296 1.00 9.68  ? 312  GLU   A HB2  1 
ATOM   4804  H  HB3  . GLU   A 1 312 ? 17.199 23.046  20.974 1.00 9.68  ? 312  GLU   A HB3  1 
ATOM   4805  H  HG2  . GLU   A 1 312 ? 16.237 24.525  23.192 1.00 9.34  ? 312  GLU   A HG2  1 
ATOM   4806  H  HG3  . GLU   A 1 312 ? 16.875 25.192  21.935 1.00 9.34  ? 312  GLU   A HG3  1 
ATOM   4807  N  N    . THR   A 1 313 ? 18.126 20.558  23.698 1.00 9.78  ? 313  THR   A N    1 
ATOM   4808  C  CA   . THR   A 1 313 ? 19.123 19.466  23.856 1.00 10.74 ? 313  THR   A CA   1 
ATOM   4809  C  C    . THR   A 1 313 ? 18.388 18.129  24.017 1.00 14.57 ? 313  THR   A C    1 
ATOM   4810  O  O    . THR   A 1 313 ? 18.839 17.135  23.419 1.00 12.47 ? 313  THR   A O    1 
ATOM   4811  C  CB   . THR   A 1 313 ? 20.073 19.762  25.023 1.00 10.87 ? 313  THR   A CB   1 
ATOM   4812  O  OG1  . THR   A 1 313 ? 20.673 21.036  24.788 1.00 11.88 ? 313  THR   A OG1  1 
ATOM   4813  C  CG2  . THR   A 1 313 ? 21.149 18.712  25.183 1.00 11.97 ? 313  THR   A CG2  1 
ATOM   4814  H  H    . THR   A 1 313 ? 18.012 21.046  24.397 1.00 11.74 ? 313  THR   A H    1 
ATOM   4815  H  HA   . THR   A 1 313 ? 19.677 19.408  23.062 1.00 12.90 ? 313  THR   A HA   1 
ATOM   4816  H  HB   . THR   A 1 313 ? 19.559 19.757  25.845 1.00 13.05 ? 313  THR   A HB   1 
ATOM   4817  H  HG1  . THR   A 1 313 ? 20.936 21.361  25.517 1.00 14.26 ? 313  THR   A HG1  1 
ATOM   4818  H  HG21 . THR   A 1 313 ? 21.720 18.945  25.931 1.00 14.37 ? 313  THR   A HG21 1 
ATOM   4819  H  HG22 . THR   A 1 313 ? 20.738 17.849  25.348 1.00 14.37 ? 313  THR   A HG22 1 
ATOM   4820  H  HG23 . THR   A 1 313 ? 21.680 18.667  24.373 1.00 14.37 ? 313  THR   A HG23 1 
ATOM   4821  N  N    . LEU   A 1 314 ? 17.315 18.109  24.811 1.00 10.50 ? 314  LEU   A N    1 
ATOM   4822  C  CA   . LEU   A 1 314 ? 16.515 16.894  24.925 1.00 13.85 ? 314  LEU   A CA   1 
ATOM   4823  C  C    . LEU   A 1 314 ? 16.021 16.450  23.556 1.00 11.53 ? 314  LEU   A C    1 
ATOM   4824  O  O    . LEU   A 1 314 ? 15.989 15.251  23.254 1.00 11.87 ? 314  LEU   A O    1 
ATOM   4825  C  CB   . LEU   A 1 314 ? 15.343 17.140  25.866 1.00 9.87  ? 314  LEU   A CB   1 
ATOM   4826  C  CG   . LEU   A 1 314 ? 15.794 17.274  27.318 1.00 13.85 ? 314  LEU   A CG   1 
ATOM   4827  C  CD1  . LEU   A 1 314 ? 14.749 18.025  28.103 1.00 11.15 ? 314  LEU   A CD1  1 
ATOM   4828  C  CD2  . LEU   A 1 314 ? 16.028 15.894  27.925 1.00 14.07 ? 314  LEU   A CD2  1 
ATOM   4829  H  H    . LEU   A 1 314 ? 17.040 18.774  25.282 1.00 12.60 ? 314  LEU   A H    1 
ATOM   4830  H  HA   . LEU   A 1 314 ? 17.067 16.184  25.289 1.00 16.62 ? 314  LEU   A HA   1 
ATOM   4831  H  HB2  . LEU   A 1 314 ? 14.877 17.947  25.597 1.00 11.85 ? 314  LEU   A HB2  1 
ATOM   4832  H  HB3  . LEU   A 1 314 ? 14.710 16.409  25.791 1.00 11.85 ? 314  LEU   A HB3  1 
ATOM   4833  H  HG   . LEU   A 1 314 ? 16.628 17.768  27.351 1.00 16.62 ? 314  LEU   A HG   1 
ATOM   4834  H  HD11 . LEU   A 1 314 ? 15.036 18.110  29.026 1.00 13.39 ? 314  LEU   A HD11 1 
ATOM   4835  H  HD12 . LEU   A 1 314 ? 14.629 18.908  27.720 1.00 13.39 ? 314  LEU   A HD12 1 
ATOM   4836  H  HD13 . LEU   A 1 314 ? 13.909 17.541  28.069 1.00 13.39 ? 314  LEU   A HD13 1 
ATOM   4837  H  HD21 . LEU   A 1 314 ? 16.314 15.990  28.847 1.00 16.89 ? 314  LEU   A HD21 1 
ATOM   4838  H  HD22 . LEU   A 1 314 ? 15.204 15.383  27.894 1.00 16.89 ? 314  LEU   A HD22 1 
ATOM   4839  H  HD23 . LEU   A 1 314 ? 16.715 15.431  27.421 1.00 16.89 ? 314  LEU   A HD23 1 
ATOM   4840  N  N    . TRP   A 1 315 ? 15.720 17.404  22.684 1.00 9.44  ? 315  TRP   A N    1 
ATOM   4841  C  CA   . TRP   A 1 315 ? 15.232 17.054  21.325 1.00 10.55 ? 315  TRP   A CA   1 
ATOM   4842  C  C    . TRP   A 1 315 ? 16.351 16.520  20.421 1.00 9.23  ? 315  TRP   A C    1 
ATOM   4843  O  O    . TRP   A 1 315 ? 16.148 15.469  19.806 1.00 10.19 ? 315  TRP   A O    1 
ATOM   4844  C  CB   . TRP   A 1 315 ? 14.577 18.281  20.679 1.00 10.28 ? 315  TRP   A CB   1 
ATOM   4845  C  CG   . TRP   A 1 315 ? 14.462 18.154  19.191 1.00 11.14 ? 315  TRP   A CG   1 
ATOM   4846  C  CD1  . TRP   A 1 315 ? 13.570 17.385  18.502 1.00 12.32 ? 315  TRP   A CD1  1 
ATOM   4847  C  CD2  . TRP   A 1 315 ? 15.284 18.794  18.199 1.00 10.94 ? 315  TRP   A CD2  1 
ATOM   4848  N  NE1  . TRP   A 1 315 ? 13.773 17.509  17.156 1.00 9.63  ? 315  TRP   A NE1  1 
ATOM   4849  C  CE2  . TRP   A 1 315 ? 14.817 18.367  16.939 1.00 9.62  ? 315  TRP   A CE2  1 
ATOM   4850  C  CE3  . TRP   A 1 315 ? 16.359 19.688  18.251 1.00 9.66  ? 315  TRP   A CE3  1 
ATOM   4851  C  CZ2  . TRP   A 1 315 ? 15.388 18.805  15.746 1.00 9.81  ? 315  TRP   A CZ2  1 
ATOM   4852  C  CZ3  . TRP   A 1 315 ? 16.924 20.117  17.071 1.00 9.96  ? 315  TRP   A CZ3  1 
ATOM   4853  C  CH2  . TRP   A 1 315 ? 16.444 19.680  15.837 1.00 10.77 ? 315  TRP   A CH2  1 
ATOM   4854  H  H    . TRP   A 1 315 ? 15.785 18.247  22.841 1.00 11.33 ? 315  TRP   A H    1 
ATOM   4855  H  HA   . TRP   A 1 315 ? 14.580 16.343  21.424 1.00 12.66 ? 315  TRP   A HA   1 
ATOM   4856  H  HB2  . TRP   A 1 315 ? 13.694 18.410  21.059 1.00 12.34 ? 315  TRP   A HB2  1 
ATOM   4857  H  HB3  . TRP   A 1 315 ? 15.096 19.072  20.894 1.00 12.34 ? 315  TRP   A HB3  1 
ATOM   4858  H  HD1  . TRP   A 1 315 ? 12.916 16.852  18.893 1.00 14.78 ? 315  TRP   A HD1  1 
ATOM   4859  H  HE1  . TRP   A 1 315 ? 13.318 17.112  16.544 1.00 11.56 ? 315  TRP   A HE1  1 
ATOM   4860  H  HE3  . TRP   A 1 315 ? 16.686 19.987  19.068 1.00 11.59 ? 315  TRP   A HE3  1 
ATOM   4861  H  HZ2  . TRP   A 1 315 ? 15.068 18.517  14.922 1.00 11.78 ? 315  TRP   A HZ2  1 
ATOM   4862  H  HZ3  . TRP   A 1 315 ? 17.640 20.710  17.098 1.00 11.95 ? 315  TRP   A HZ3  1 
ATOM   4863  H  HH2  . TRP   A 1 315 ? 16.848 19.988  15.058 1.00 12.92 ? 315  TRP   A HH2  1 
ATOM   4864  N  N    . CYS   A 1 316 ? 17.498 17.203  20.368 1.00 8.75  ? 316  CYS   A N    1 
ATOM   4865  C  CA   . CYS   A 1 316 ? 18.549 16.844  19.371 1.00 12.13 ? 316  CYS   A CA   1 
ATOM   4866  C  C    . CYS   A 1 316 ? 19.286 15.544  19.719 1.00 12.82 ? 316  CYS   A C    1 
ATOM   4867  O  O    . CYS   A 1 316 ? 19.871 14.954  18.806 1.00 13.03 ? 316  CYS   A O    1 
ATOM   4868  C  CB   . CYS   A 1 316 ? 19.537 17.996  19.199 1.00 12.60 ? 316  CYS   A CB   1 
ATOM   4869  S  SG   . CYS   A 1 316 ? 20.595 18.294  20.644 1.00 13.96 ? 316  CYS   A SG   1 
ATOM   4870  H  H    . CYS   A 1 316 ? 17.696 17.864  20.882 1.00 10.51 ? 316  CYS   A H    1 
ATOM   4871  H  HA   . CYS   A 1 316 ? 18.094 16.685  18.529 1.00 14.56 ? 316  CYS   A HA   1 
ATOM   4872  H  HB2  . CYS   A 1 316 ? 20.100 17.813  18.431 1.00 15.12 ? 316  CYS   A HB2  1 
ATOM   4873  H  HB3  . CYS   A 1 316 ? 19.042 18.806  19.001 1.00 15.12 ? 316  CYS   A HB3  1 
ATOM   4874  H  HG   . CYS   A 1 316 ? 21.648 18.743  20.284 1.00 16.76 ? 316  CYS   A HG   1 
ATOM   4875  N  N    . PHE   A 1 317 ? 19.264 15.142  20.989 1.00 12.88 ? 317  PHE   A N    1 
ATOM   4876  C  CA   . PHE   A 1 317 ? 19.891 13.856  21.389 1.00 12.40 ? 317  PHE   A CA   1 
ATOM   4877  C  C    . PHE   A 1 317 ? 18.778 12.864  21.739 1.00 13.20 ? 317  PHE   A C    1 
ATOM   4878  O  O    . PHE   A 1 317 ? 19.074 11.776  22.265 1.00 12.84 ? 317  PHE   A O    1 
ATOM   4879  C  CB   . PHE   A 1 317 ? 20.874 14.066  22.545 1.00 14.07 ? 317  PHE   A CB   1 
ATOM   4880  C  CG   . PHE   A 1 317 ? 22.163 14.741  22.152 1.00 12.39 ? 317  PHE   A CG   1 
ATOM   4881  C  CD1  . PHE   A 1 317 ? 22.978 14.199  21.172 1.00 12.15 ? 317  PHE   A CD1  1 
ATOM   4882  C  CD2  . PHE   A 1 317 ? 22.559 15.921  22.759 1.00 11.96 ? 317  PHE   A CD2  1 
ATOM   4883  C  CE1  . PHE   A 1 317 ? 24.161 14.820  20.809 1.00 13.57 ? 317  PHE   A CE1  1 
ATOM   4884  C  CE2  . PHE   A 1 317 ? 23.742 16.543  22.394 1.00 12.36 ? 317  PHE   A CE2  1 
ATOM   4885  C  CZ   . PHE   A 1 317 ? 24.539 15.991  21.420 1.00 11.69 ? 317  PHE   A CZ   1 
ATOM   4886  H  H    . PHE   A 1 317 ? 18.901 15.582  21.632 1.00 15.46 ? 317  PHE   A H    1 
ATOM   4887  H  HA   . PHE   A 1 317 ? 20.412 13.492  20.656 1.00 14.89 ? 317  PHE   A HA   1 
ATOM   4888  H  HB2  . PHE   A 1 317 ? 20.440 14.596  23.232 1.00 16.89 ? 317  PHE   A HB2  1 
ATOM   4889  H  HB3  . PHE   A 1 317 ? 21.080 13.204  22.940 1.00 16.89 ? 317  PHE   A HB3  1 
ATOM   4890  H  HD1  . PHE   A 1 317 ? 22.727 13.408  20.752 1.00 14.59 ? 317  PHE   A HD1  1 
ATOM   4891  H  HD2  . PHE   A 1 317 ? 22.025 16.300  23.419 1.00 14.36 ? 317  PHE   A HD2  1 
ATOM   4892  H  HE1  . PHE   A 1 317 ? 24.700 14.444  20.151 1.00 16.29 ? 317  PHE   A HE1  1 
ATOM   4893  H  HE2  . PHE   A 1 317 ? 23.997 17.335  22.809 1.00 14.83 ? 317  PHE   A HE2  1 
ATOM   4894  H  HZ   . PHE   A 1 317 ? 25.333 16.409  21.175 1.00 14.04 ? 317  PHE   A HZ   1 
ATOM   4895  N  N    . GLY   A 1 318 ? 17.533 13.249  21.463 1.00 12.64 ? 318  GLY   A N    1 
ATOM   4896  C  CA   . GLY   A 1 318 ? 16.408 12.324  21.681 1.00 13.06 ? 318  GLY   A CA   1 
ATOM   4897  C  C    . GLY   A 1 318 ? 15.633 12.085  20.397 1.00 11.10 ? 318  GLY   A C    1 
ATOM   4898  O  O    . GLY   A 1 318 ? 16.154 11.375  19.529 1.00 14.21 ? 318  GLY   A O    1 
ATOM   4899  H  H    . GLY   A 1 318 ? 17.316 14.022  21.156 1.00 15.18 ? 318  GLY   A H    1 
ATOM   4900  H  HA2  . GLY   A 1 318 ? 16.742 11.479  22.021 1.00 15.68 ? 318  GLY   A HA2  1 
ATOM   4901  H  HA3  . GLY   A 1 318 ? 15.814 12.687  22.357 1.00 15.68 ? 318  GLY   A HA3  1 
ATOM   4902  N  N    . SER   A 1 319 ? 14.454 12.692  20.277 1.00 12.68 ? 319  SER   A N    1 
ATOM   4903  C  CA   . SER   A 1 319 ? 13.558 12.459  19.109 1.00 12.46 ? 319  SER   A CA   1 
ATOM   4904  C  C    . SER   A 1 319 ? 14.260 12.663  17.759 1.00 11.86 ? 319  SER   A C    1 
ATOM   4905  O  O    . SER   A 1 319 ? 13.952 11.922  16.820 1.00 11.41 ? 319  SER   A O    1 
ATOM   4906  C  CB   . SER   A 1 319 ? 12.340 13.340  19.233 1.00 11.20 ? 319  SER   A CB   1 
ATOM   4907  O  OG   . SER   A 1 319 ? 11.799 13.287  20.543 1.00 12.43 ? 319  SER   A OG   1 
ATOM   4908  H  H    . SER   A 1 319 ? 14.142 13.246  20.856 1.00 15.21 ? 319  SER   A H    1 
ATOM   4909  H  HA   . SER   A 1 319 ? 13.290 11.527  19.123 1.00 14.96 ? 319  SER   A HA   1 
ATOM   4910  H  HB2  . SER   A 1 319 ? 12.576 14.255  19.015 1.00 13.45 ? 319  SER   A HB2  1 
ATOM   4911  H  HB3  . SER   A 1 319 ? 11.668 13.060  18.592 1.00 13.45 ? 319  SER   A HB3  1 
ATOM   4912  H  HG   . SER   A 1 319 ? 11.405 14.009  20.713 1.00 14.92 ? 319  SER   A HG   1 
ATOM   4913  N  N    . ASP   A 1 320 ? 15.151 13.648  17.658 1.00 12.80 ? 320  ASP   A N    1 
ATOM   4914  C  CA   . ASP   A 1 320 ? 15.773 13.947  16.339 1.00 11.65 ? 320  ASP   A CA   1 
ATOM   4915  C  C    . ASP   A 1 320 ? 16.623 12.757  15.882 1.00 10.94 ? 320  ASP   A C    1 
ATOM   4916  O  O    . ASP   A 1 320 ? 16.802 12.596  14.672 1.00 10.70 ? 320  ASP   A O    1 
ATOM   4917  C  CB   . ASP   A 1 320 ? 16.599 15.237  16.395 1.00 9.66  ? 320  ASP   A CB   1 
ATOM   4918  C  CG   . ASP   A 1 320 ? 16.771 15.901  15.040 1.00 10.57 ? 320  ASP   A CG   1 
ATOM   4919  O  OD1  . ASP   A 1 320 ? 15.878 15.735  14.193 1.00 11.35 ? 320  ASP   A OD1  1 
ATOM   4920  O  OD2  . ASP   A 1 320 ? 17.798 16.578  14.847 1.00 12.18 ? 320  ASP   A OD2  1 
ATOM   4921  H  H    . ASP   A 1 320 ? 15.410 14.147  18.309 1.00 15.36 ? 320  ASP   A H    1 
ATOM   4922  H  HA   . ASP   A 1 320 ? 15.068 14.089  15.688 1.00 13.98 ? 320  ASP   A HA   1 
ATOM   4923  H  HB2  . ASP   A 1 320 ? 16.171 15.861  17.002 1.00 11.59 ? 320  ASP   A HB2  1 
ATOM   4924  H  HB3  . ASP   A 1 320 ? 17.474 15.037  16.764 1.00 11.59 ? 320  ASP   A HB3  1 
ATOM   4925  N  N    . CYS   A 1 321 ? 17.158 11.988  16.836 1.00 11.07 ? 321  CYS   A N    1 
ATOM   4926  C  CA   . CYS   A 1 321 ? 18.004 10.811  16.504 1.00 12.13 ? 321  CYS   A CA   1 
ATOM   4927  C  C    . CYS   A 1 321 ? 17.237 9.511   16.793 1.00 13.25 ? 321  CYS   A C    1 
ATOM   4928  O  O    . CYS   A 1 321 ? 17.854 8.437   16.739 1.00 10.83 ? 321  CYS   A O    1 
ATOM   4929  C  CB   . CYS   A 1 321 ? 19.290 10.829  17.320 1.00 12.67 ? 321  CYS   A CB   1 
ATOM   4930  S  SG   . CYS   A 1 321 ? 20.458 12.114  16.790 1.00 13.19 ? 321  CYS   A SG   1 
ATOM   4931  H  H    . CYS   A 1 321 ? 17.050 12.122  17.679 1.00 13.29 ? 321  CYS   A H    1 
ATOM   4932  H  HA   . CYS   A 1 321 ? 18.227 10.853  15.561 1.00 14.55 ? 321  CYS   A HA   1 
ATOM   4933  H  HB2  . CYS   A 1 321 ? 19.071 10.966  18.255 1.00 15.21 ? 321  CYS   A HB2  1 
ATOM   4934  H  HB3  . CYS   A 1 321 ? 19.720 9.962   17.253 1.00 15.21 ? 321  CYS   A HB3  1 
ATOM   4935  H  HG   . CYS   A 1 321 ? 20.292 13.103  17.450 1.00 15.83 ? 321  CYS   A HG   1 
ATOM   4936  N  N    . GLY   A 1 322 ? 15.942 9.623   17.092 1.00 13.27 ? 322  GLY   A N    1 
ATOM   4937  C  CA   . GLY   A 1 322 ? 15.117 8.424   17.324 1.00 15.57 ? 322  GLY   A CA   1 
ATOM   4938  C  C    . GLY   A 1 322 ? 15.467 7.741   18.633 1.00 13.15 ? 322  GLY   A C    1 
ATOM   4939  O  O    . GLY   A 1 322 ? 15.168 6.548   18.761 1.00 12.47 ? 322  GLY   A O    1 
ATOM   4940  H  H    . GLY   A 1 322 ? 15.523 10.370  17.166 1.00 15.93 ? 322  GLY   A H    1 
ATOM   4941  H  HA2  . GLY   A 1 322 ? 14.180 8.673   17.330 1.00 18.69 ? 322  GLY   A HA2  1 
ATOM   4942  H  HA3  . GLY   A 1 322 ? 15.240 7.800   16.591 1.00 18.69 ? 322  GLY   A HA3  1 
ATOM   4943  N  N    . SER   A 1 323 ? 16.101 8.472   19.553 1.00 13.48 ? 323  SER   A N    1 
ATOM   4944  C  CA   . SER   A 1 323 ? 16.489 7.915   20.877 1.00 12.45 ? 323  SER   A CA   1 
ATOM   4945  C  C    . SER   A 1 323 ? 15.587 8.490   21.975 1.00 14.83 ? 323  SER   A C    1 
ATOM   4946  O  O    . SER   A 1 323 ? 15.248 9.676   21.894 1.00 15.97 ? 323  SER   A O    1 
ATOM   4947  C  CB   . SER   A 1 323 ? 17.943 8.186   21.181 1.00 13.13 ? 323  SER   A CB   1 
ATOM   4948  O  OG   . SER   A 1 323 ? 18.336 7.551   22.386 1.00 17.44 ? 323  SER   A OG   1 
ATOM   4949  H  H    . SER   A 1 323 ? 16.321 9.296   19.439 1.00 16.18 ? 323  SER   A H    1 
ATOM   4950  H  HA   . SER   A 1 323 ? 16.371 6.953   20.848 1.00 14.94 ? 323  SER   A HA   1 
ATOM   4951  H  HB2  . SER   A 1 323 ? 18.495 7.868   20.449 1.00 15.76 ? 323  SER   A HB2  1 
ATOM   4952  H  HB3  . SER   A 1 323 ? 18.089 9.142   21.252 1.00 15.76 ? 323  SER   A HB3  1 
ATOM   4953  H  HG   . SER   A 1 323 ? 18.616 8.128   22.928 1.00 20.93 ? 323  SER   A HG   1 
ATOM   4954  N  N    . TYR   A 1 324 ? 15.241 7.678   22.976 1.00 14.28 ? 324  TYR   A N    1 
ATOM   4955  C  CA   . TYR   A 1 324 ? 14.363 8.143   24.083 1.00 13.67 ? 324  TYR   A CA   1 
ATOM   4956  C  C    . TYR   A 1 324 ? 14.995 7.752   25.424 1.00 15.65 ? 324  TYR   A C    1 
ATOM   4957  O  O    . TYR   A 1 324 ? 14.254 7.496   26.386 1.00 16.41 ? 324  TYR   A O    1 
ATOM   4958  C  CB   . TYR   A 1 324 ? 12.931 7.656   23.838 1.00 13.91 ? 324  TYR   A CB   1 
ATOM   4959  C  CG   . TYR   A 1 324 ? 12.419 8.119   22.500 1.00 15.11 ? 324  TYR   A CG   1 
ATOM   4960  C  CD1  . TYR   A 1 324 ? 11.958 9.412   22.330 1.00 14.50 ? 324  TYR   A CD1  1 
ATOM   4961  C  CD2  . TYR   A 1 324 ? 12.462 7.295   21.388 1.00 15.16 ? 324  TYR   A CD2  1 
ATOM   4962  C  CE1  . TYR   A 1 324 ? 11.515 9.866   21.101 1.00 14.09 ? 324  TYR   A CE1  1 
ATOM   4963  C  CE2  . TYR   A 1 324 ? 12.022 7.732   20.150 1.00 20.08 ? 324  TYR   A CE2  1 
ATOM   4964  C  CZ   . TYR   A 1 324 ? 11.546 9.023   20.006 1.00 17.91 ? 324  TYR   A CZ   1 
ATOM   4965  O  OH   . TYR   A 1 324 ? 11.106 9.477   18.787 1.00 19.94 ? 324  TYR   A OH   1 
ATOM   4966  H  H    . TYR   A 1 324 ? 15.496 6.859   23.042 1.00 17.14 ? 324  TYR   A H    1 
ATOM   4967  H  HA   . TYR   A 1 324 ? 14.289 9.110   24.115 1.00 16.41 ? 324  TYR   A HA   1 
ATOM   4968  H  HB2  . TYR   A 1 324 ? 12.905 6.687   23.879 1.00 16.69 ? 324  TYR   A HB2  1 
ATOM   4969  H  HB3  . TYR   A 1 324 ? 12.350 7.986   24.541 1.00 16.69 ? 324  TYR   A HB3  1 
ATOM   4970  H  HD1  . TYR   A 1 324 ? 11.946 9.989   23.059 1.00 17.41 ? 324  TYR   A HD1  1 
ATOM   4971  H  HD2  . TYR   A 1 324 ? 12.793 6.430   21.474 1.00 18.19 ? 324  TYR   A HD2  1 
ATOM   4972  H  HE1  . TYR   A 1 324 ? 11.197 10.735  21.012 1.00 16.91 ? 324  TYR   A HE1  1 
ATOM   4973  H  HE2  . TYR   A 1 324 ? 12.046 7.159   19.418 1.00 24.10 ? 324  TYR   A HE2  1 
ATOM   4974  H  HH   . TYR   A 1 324 ? 11.239 10.305  18.731 1.00 23.94 ? 324  TYR   A HH   1 
ATOM   4975  N  N    . ASP   A 1 325 ? 16.328 7.746   25.471 1.00 14.57 ? 325  ASP   A N    1 
ATOM   4976  C  CA   . ASP   A 1 325 ? 17.072 7.440   26.721 1.00 14.08 ? 325  ASP   A CA   1 
ATOM   4977  C  C    . ASP   A 1 325 ? 17.403 8.767   27.415 1.00 15.00 ? 325  ASP   A C    1 
ATOM   4978  O  O    . ASP   A 1 325 ? 18.244 9.506   26.882 1.00 13.03 ? 325  ASP   A O    1 
ATOM   4979  C  CB   . ASP   A 1 325 ? 18.296 6.595   26.381 1.00 15.48 ? 325  ASP   A CB   1 
ATOM   4980  C  CG   . ASP   A 1 325 ? 19.109 6.148   27.583 1.00 18.15 ? 325  ASP   A CG   1 
ATOM   4981  O  OD1  . ASP   A 1 325 ? 19.023 6.809   28.631 1.00 15.55 ? 325  ASP   A OD1  1 
ATOM   4982  O  OD2  . ASP   A 1 325 ? 19.829 5.145   27.447 1.00 21.24 ? 325  ASP   A OD2  1 
ATOM   4983  H  H    . ASP   A 1 325 ? 16.831 7.916   24.794 1.00 17.49 ? 325  ASP   A H    1 
ATOM   4984  H  HA   . ASP   A 1 325 ? 16.545 6.914   27.343 1.00 16.90 ? 325  ASP   A HA   1 
ATOM   4985  H  HB2  . ASP   A 1 325 ? 18.006 5.810   25.891 1.00 18.57 ? 325  ASP   A HB2  1 
ATOM   4986  H  HB3  . ASP   A 1 325 ? 18.871 7.103   25.788 1.00 18.57 ? 325  ASP   A HB3  1 
ATOM   4987  N  N    . LEU   A 1 326 ? 16.755 9.058   28.544 1.00 13.67 ? 326  LEU   A N    1 
ATOM   4988  C  CA   . LEU   A 1 326 ? 16.931 10.341  29.221 1.00 12.24 ? 326  LEU   A CA   1 
ATOM   4989  C  C    . LEU   A 1 326 ? 18.299 10.441  29.890 1.00 13.69 ? 326  LEU   A C    1 
ATOM   4990  O  O    . LEU   A 1 326 ? 18.966 11.479  29.785 1.00 12.21 ? 326  LEU   A O    1 
ATOM   4991  C  CB   . LEU   A 1 326 ? 15.808 10.557  30.243 1.00 15.69 ? 326  LEU   A CB   1 
ATOM   4992  C  CG   . LEU   A 1 326 ? 15.759 11.909  30.971 1.00 15.99 ? 326  LEU   A CG   1 
ATOM   4993  C  CD1  . LEU   A 1 326 ? 15.953 13.048  29.985 1.00 15.48 ? 326  LEU   A CD1  1 
ATOM   4994  C  CD2  . LEU   A 1 326 ? 14.431 12.064  31.725 1.00 14.10 ? 326  LEU   A CD2  1 
ATOM   4995  H  H    . LEU   A 1 326 ? 16.207 8.523   28.935 1.00 16.41 ? 326  LEU   A H    1 
ATOM   4996  H  HA   . LEU   A 1 326 ? 16.885 11.042  28.552 1.00 14.69 ? 326  LEU   A HA   1 
ATOM   4997  H  HB2  . LEU   A 1 326 ? 14.961 10.432  29.787 1.00 18.83 ? 326  LEU   A HB2  1 
ATOM   4998  H  HB3  . LEU   A 1 326 ? 15.875 9.859   30.913 1.00 18.83 ? 326  LEU   A HB3  1 
ATOM   4999  H  HG   . LEU   A 1 326 ? 16.481 11.939  31.618 1.00 19.19 ? 326  LEU   A HG   1 
ATOM   5000  H  HD11 . LEU   A 1 326 ? 15.920 13.894  30.458 1.00 18.58 ? 326  LEU   A HD11 1 
ATOM   5001  H  HD12 . LEU   A 1 326 ? 16.814 12.955  29.549 1.00 18.58 ? 326  LEU   A HD12 1 
ATOM   5002  H  HD13 . LEU   A 1 326 ? 15.249 13.023  29.318 1.00 18.58 ? 326  LEU   A HD13 1 
ATOM   5003  H  HD21 . LEU   A 1 326 ? 14.415 12.921  32.179 1.00 16.92 ? 326  LEU   A HD21 1 
ATOM   5004  H  HD22 . LEU   A 1 326 ? 13.694 12.018  31.096 1.00 16.92 ? 326  LEU   A HD22 1 
ATOM   5005  H  HD23 . LEU   A 1 326 ? 14.344 11.351  32.377 1.00 16.92 ? 326  LEU   A HD23 1 
ATOM   5006  N  N    . ASP   A 1 327 ? 18.730 9.380   30.592 1.00 13.33 ? 327  ASP   A N    1 
ATOM   5007  C  CA   . ASP   A 1 327 ? 20.085 9.350   31.144 1.00 16.38 ? 327  ASP   A CA   1 
ATOM   5008  C  C    . ASP   A 1 327 ? 21.114 9.693   30.079 1.00 15.85 ? 327  ASP   A C    1 
ATOM   5009  O  O    . ASP   A 1 327 ? 22.068 10.438  30.331 1.00 15.87 ? 327  ASP   A O    1 
ATOM   5010  C  CB   . ASP   A 1 327 ? 20.412 7.968   31.722 1.00 16.17 ? 327  ASP   A CB   1 
ATOM   5011  C  CG   . ASP   A 1 327 ? 19.717 7.694   33.042 1.00 17.34 ? 327  ASP   A CG   1 
ATOM   5012  O  OD1  . ASP   A 1 327 ? 19.540 8.626   33.848 1.00 17.80 ? 327  ASP   A OD1  1 
ATOM   5013  O  OD2  . ASP   A 1 327 ? 19.364 6.526   33.289 1.00 23.47 ? 327  ASP   A OD2  1 
ATOM   5014  H  H    . ASP   A 1 327 ? 18.257 8.680   30.755 1.00 15.99 ? 327  ASP   A H    1 
ATOM   5015  H  HA   . ASP   A 1 327 ? 20.121 10.012  31.852 1.00 19.66 ? 327  ASP   A HA   1 
ATOM   5016  H  HB2  . ASP   A 1 327 ? 20.156 7.287   31.081 1.00 19.40 ? 327  ASP   A HB2  1 
ATOM   5017  H  HB3  . ASP   A 1 327 ? 21.371 7.894   31.847 1.00 19.40 ? 327  ASP   A HB3  1 
ATOM   5018  N  N    . ALA   A 1 328 ? 20.935 9.146   28.879 1.00 13.99 ? 328  ALA   A N    1 
ATOM   5019  C  CA   . ALA   A 1 328 ? 21.876 9.402   27.798 1.00 16.36 ? 328  ALA   A CA   1 
ATOM   5020  C  C    . ALA   A 1 328 ? 21.891 10.869  27.389 1.00 13.05 ? 328  ALA   A C    1 
ATOM   5021  O  O    . ALA   A 1 328 ? 22.944 11.401  27.021 1.00 13.69 ? 328  ALA   A O    1 
ATOM   5022  C  CB   . ALA   A 1 328 ? 21.525 8.529   26.606 1.00 15.73 ? 328  ALA   A CB   1 
ATOM   5023  H  H    . ALA   A 1 328 ? 20.280 8.628   28.673 1.00 16.80 ? 328  ALA   A H    1 
ATOM   5024  H  HA   . ALA   A 1 328 ? 22.766 9.184   28.117 1.00 19.64 ? 328  ALA   A HA   1 
ATOM   5025  H  HB1  . ALA   A 1 328 ? 22.151 8.699   25.885 1.00 18.88 ? 328  ALA   A HB1  1 
ATOM   5026  H  HB2  . ALA   A 1 328 ? 21.574 7.595   26.863 1.00 18.88 ? 328  ALA   A HB2  1 
ATOM   5027  H  HB3  . ALA   A 1 328 ? 20.625 8.735   26.307 1.00 18.88 ? 328  ALA   A HB3  1 
ATOM   5028  N  N    . ILE   A 1 329 ? 20.723 11.501  27.406 1.00 14.16 ? 329  ILE   A N    1 
ATOM   5029  C  CA   . ILE   A 1 329 ? 20.680 12.948  27.057 1.00 13.24 ? 329  ILE   A CA   1 
ATOM   5030  C  C    . ILE   A 1 329 ? 21.459 13.718  28.130 1.00 16.38 ? 329  ILE   A C    1 
ATOM   5031  O  O    . ILE   A 1 329 ? 22.221 14.632  27.769 1.00 15.58 ? 329  ILE   A O    1 
ATOM   5032  C  CB   . ILE   A 1 329 ? 19.230 13.438  26.898 1.00 11.58 ? 329  ILE   A CB   1 
ATOM   5033  C  CG1  . ILE   A 1 329 ? 18.508 12.686  25.778 1.00 14.69 ? 329  ILE   A CG1  1 
ATOM   5034  C  CG2  . ILE   A 1 329 ? 19.202 14.937  26.675 1.00 13.03 ? 329  ILE   A CG2  1 
ATOM   5035  C  CD1  . ILE   A 1 329 ? 17.035 12.996  25.677 1.00 16.05 ? 329  ILE   A CD1  1 
ATOM   5036  H  H    . ILE   A 1 329 ? 19.967 11.143  27.605 1.00 17.00 ? 329  ILE   A H    1 
ATOM   5037  H  HA   . ILE   A 1 329 ? 21.100 13.104  26.197 1.00 15.90 ? 329  ILE   A HA   1 
ATOM   5038  H  HB   . ILE   A 1 329 ? 18.751 13.248  27.720 1.00 13.90 ? 329  ILE   A HB   1 
ATOM   5039  H  HG12 . ILE   A 1 329 ? 18.932 12.900  24.932 1.00 17.63 ? 329  ILE   A HG12 1 
ATOM   5040  H  HG13 . ILE   A 1 329 ? 18.619 11.733  25.918 1.00 17.63 ? 329  ILE   A HG13 1 
ATOM   5041  H  HG21 . ILE   A 1 329 ? 18.283 15.233  26.576 1.00 15.64 ? 329  ILE   A HG21 1 
ATOM   5042  H  HG22 . ILE   A 1 329 ? 19.606 15.385  27.435 1.00 15.64 ? 329  ILE   A HG22 1 
ATOM   5043  H  HG23 . ILE   A 1 329 ? 19.699 15.154  25.871 1.00 15.64 ? 329  ILE   A HG23 1 
ATOM   5044  H  HD11 . ILE   A 1 329 ? 16.646 12.486  24.949 1.00 19.26 ? 329  ILE   A HD11 1 
ATOM   5045  H  HD12 . ILE   A 1 329 ? 16.596 12.758  26.509 1.00 19.26 ? 329  ILE   A HD12 1 
ATOM   5046  H  HD13 . ILE   A 1 329 ? 16.914 13.943  25.508 1.00 19.26 ? 329  ILE   A HD13 1 
ATOM   5047  N  N    . ASN   A 1 330 ? 21.288 13.332  29.397 1.00 13.33 ? 330  ASN   A N    1 
ATOM   5048  C  CA   . ASN   A 1 330 ? 22.025 14.005  30.497 1.00 16.77 ? 330  ASN   A CA   1 
ATOM   5049  C  C    . ASN   A 1 330 ? 23.533 13.860  30.247 1.00 13.63 ? 330  ASN   A C    1 
ATOM   5050  O  O    . ASN   A 1 330 ? 24.260 14.844  30.456 1.00 13.62 ? 330  ASN   A O    1 
ATOM   5051  C  CB   . ASN   A 1 330 ? 21.575 13.475  31.859 1.00 15.49 ? 330  ASN   A CB   1 
ATOM   5052  C  CG   . ASN   A 1 330 ? 20.126 13.795  32.157 1.00 16.00 ? 330  ASN   A CG   1 
ATOM   5053  O  OD1  . ASN   A 1 330 ? 19.553 14.700  31.558 1.00 14.61 ? 330  ASN   A OD1  1 
ATOM   5054  N  ND2  . ASN   A 1 330 ? 19.527 13.060  33.080 1.00 16.80 ? 330  ASN   A ND2  1 
ATOM   5055  H  H    . ASN   A 1 330 ? 20.764 12.698  29.647 1.00 16.00 ? 330  ASN   A H    1 
ATOM   5056  H  HA   . ASN   A 1 330 ? 21.822 14.953  30.511 1.00 20.12 ? 330  ASN   A HA   1 
ATOM   5057  H  HB2  . ASN   A 1 330 ? 21.703 12.514  31.887 1.00 18.59 ? 330  ASN   A HB2  1 
ATOM   5058  H  HB3  . ASN   A 1 330 ? 22.136 13.856  32.552 1.00 18.59 ? 330  ASN   A HB3  1 
ATOM   5059  H  HD21 . ASN   A 1 330 ? 18.704 13.209  33.281 1.00 20.16 ? 330  ASN   A HD21 1 
ATOM   5060  H  HD22 . ASN   A 1 330 ? 19.961 12.434  33.479 1.00 20.16 ? 330  ASN   A HD22 1 
ATOM   5061  N  N    . GLU   A 1 331 ? 23.972 12.681  29.801 1.00 13.75 ? 331  GLU   A N    1 
ATOM   5062  C  CA   . GLU   A 1 331 ? 25.416 12.447  29.524 1.00 14.09 ? 331  GLU   A CA   1 
ATOM   5063  C  C    . GLU   A 1 331 ? 25.859 13.273  28.310 1.00 13.70 ? 331  GLU   A C    1 
ATOM   5064  O  O    . GLU   A 1 331 ? 26.918 13.906  28.381 1.00 13.29 ? 331  GLU   A O    1 
ATOM   5065  C  CB   . GLU   A 1 331 ? 25.675 10.963  29.261 1.00 15.74 ? 331  GLU   A CB   1 
ATOM   5066  C  CG   . GLU   A 1 331 ? 27.145 10.597  29.243 1.00 21.72 ? 331  GLU   A CG   1 
ATOM   5067  C  CD   . GLU   A 1 331 ? 27.729 10.281  30.609 1.00 34.66 ? 331  GLU   A CD   1 
ATOM   5068  O  OE1  . GLU   A 1 331 ? 26.951 10.175  31.577 1.00 36.76 ? 331  GLU   A OE1  1 
ATOM   5069  O  OE2  . GLU   A 1 331 ? 28.962 10.142  30.700 1.00 37.39 ? 331  GLU   A OE2  1 
ATOM   5070  H  H    . GLU   A 1 331 ? 23.465 12.003  29.650 1.00 16.50 ? 331  GLU   A H    1 
ATOM   5071  H  HA   . GLU   A 1 331 ? 25.927 12.722  30.301 1.00 16.91 ? 331  GLU   A HA   1 
ATOM   5072  H  HB2  . GLU   A 1 331 ? 25.227 10.439  29.943 1.00 18.89 ? 331  GLU   A HB2  1 
ATOM   5073  H  HB3  . GLU   A 1 331 ? 25.278 10.719  28.410 1.00 18.89 ? 331  GLU   A HB3  1 
ATOM   5074  H  HG2  . GLU   A 1 331 ? 27.269 9.828   28.665 1.00 26.07 ? 331  GLU   A HG2  1 
ATOM   5075  H  HG3  . GLU   A 1 331 ? 27.645 11.330  28.851 1.00 26.07 ? 331  GLU   A HG3  1 
ATOM   5076  N  N    . ALA   A 1 332 ? 25.076 13.226  27.230 1.00 13.71 ? 332  ALA   A N    1 
ATOM   5077  C  CA   . ALA   A 1 332 ? 25.419 13.974  25.999 1.00 12.96 ? 332  ALA   A CA   1 
ATOM   5078  C  C    . ALA   A 1 332 ? 25.542 15.468  26.314 1.00 14.49 ? 332  ALA   A C    1 
ATOM   5079  O  O    . ALA   A 1 332 ? 26.448 16.111  25.776 1.00 12.70 ? 332  ALA   A O    1 
ATOM   5080  C  CB   . ALA   A 1 332 ? 24.359 13.741  24.950 1.00 12.32 ? 332  ALA   A CB   1 
ATOM   5081  H  H    . ALA   A 1 332 ? 24.346 12.773  27.182 1.00 16.46 ? 332  ALA   A H    1 
ATOM   5082  H  HA   . ALA   A 1 332 ? 26.271 13.659  25.658 1.00 15.56 ? 332  ALA   A HA   1 
ATOM   5083  H  HB1  . ALA   A 1 332 ? 24.587 14.232  24.145 1.00 14.78 ? 332  ALA   A HB1  1 
ATOM   5084  H  HB2  . ALA   A 1 332 ? 24.307 12.794  24.747 1.00 14.78 ? 332  ALA   A HB2  1 
ATOM   5085  H  HB3  . ALA   A 1 332 ? 23.501 14.047  25.283 1.00 14.78 ? 332  ALA   A HB3  1 
ATOM   5086  N  N    . ASN   A 1 333 ? 24.632 15.982  27.139 1.00 12.28 ? 333  ASN   A N    1 
ATOM   5087  C  CA   . ASN   A 1 333 ? 24.649 17.426  27.489 1.00 12.12 ? 333  ASN   A CA   1 
ATOM   5088  C  C    . ASN   A 1 333 ? 25.959 17.733  28.221 1.00 13.32 ? 333  ASN   A C    1 
ATOM   5089  O  O    . ASN   A 1 333 ? 26.633 18.703  27.859 1.00 10.78 ? 333  ASN   A O    1 
ATOM   5090  C  CB   . ASN   A 1 333 ? 23.432 17.806  28.331 1.00 13.53 ? 333  ASN   A CB   1 
ATOM   5091  C  CG   . ASN   A 1 333 ? 23.369 19.283  28.653 1.00 12.19 ? 333  ASN   A CG   1 
ATOM   5092  O  OD1  . ASN   A 1 333 ? 23.292 20.114  27.753 1.00 13.16 ? 333  ASN   A OD1  1 
ATOM   5093  N  ND2  . ASN   A 1 333 ? 23.394 19.617  29.933 1.00 11.65 ? 333  ASN   A ND2  1 
ATOM   5094  H  H    . ASN   A 1 333 ? 24.001 15.529  27.508 1.00 14.74 ? 333  ASN   A H    1 
ATOM   5095  H  HA   . ASN   A 1 333 ? 24.601 17.959  26.680 1.00 14.55 ? 333  ASN   A HA   1 
ATOM   5096  H  HB2  . ASN   A 1 333 ? 22.625 17.549  27.857 1.00 16.24 ? 333  ASN   A HB2  1 
ATOM   5097  H  HB3  . ASN   A 1 333 ? 23.448 17.301  29.159 1.00 16.24 ? 333  ASN   A HB3  1 
ATOM   5098  H  HD21 . ASN   A 1 333 ? 23.356 20.445  30.162 1.00 13.99 ? 333  ASN   A HD21 1 
ATOM   5099  H  HD22 . ASN   A 1 333 ? 23.449 19.006  30.536 1.00 13.99 ? 333  ASN   A HD22 1 
ATOM   5100  N  N    . MET   A 1 334 ? 26.291 16.897  29.200 1.00 12.55 ? 334  MET   A N    1 
ATOM   5101  C  CA   . MET   A 1 334 ? 27.565 17.081  29.939 1.00 11.83 ? 334  MET   A CA   1 
ATOM   5102  C  C    . MET   A 1 334 ? 28.739 17.036  28.955 1.00 14.45 ? 334  MET   A C    1 
ATOM   5103  O  O    . MET   A 1 334 ? 29.632 17.891  29.074 1.00 10.96 ? 334  MET   A O    1 
ATOM   5104  C  CB   . MET   A 1 334 ? 27.727 15.984  30.997 1.00 14.65 ? 334  MET   A CB   1 
ATOM   5105  C  CG   . MET   A 1 334 ? 29.024 16.067  31.773 1.00 15.23 ? 334  MET   A CG   1 
ATOM   5106  S  SD   . MET   A 1 334 ? 30.316 15.058  31.010 1.00 17.26 ? 334  MET   A SD   1 
ATOM   5107  C  CE   . MET   A 1 334 ? 29.550 13.439  31.068 1.00 22.36 ? 334  MET   A CE   1 
ATOM   5108  H  H    . MET   A 1 334 ? 25.814 16.229  29.456 1.00 15.06 ? 334  MET   A H    1 
ATOM   5109  H  HA   . MET   A 1 334 ? 27.552 17.942  30.385 1.00 14.20 ? 334  MET   A HA   1 
ATOM   5110  H  HB2  . MET   A 1 334 ? 26.984 16.035  31.619 1.00 17.58 ? 334  MET   A HB2  1 
ATOM   5111  H  HB3  . MET   A 1 334 ? 27.675 15.118  30.563 1.00 17.58 ? 334  MET   A HB3  1 
ATOM   5112  H  HG2  . MET   A 1 334 ? 29.317 16.991  31.818 1.00 18.27 ? 334  MET   A HG2  1 
ATOM   5113  H  HG3  . MET   A 1 334 ? 28.877 15.771  32.685 1.00 18.27 ? 334  MET   A HG3  1 
ATOM   5114  H  HE1  . MET   A 1 334 ? 30.150 12.783  30.680 1.00 26.83 ? 334  MET   A HE1  1 
ATOM   5115  H  HE2  . MET   A 1 334 ? 29.364 13.202  31.990 1.00 26.83 ? 334  MET   A HE2  1 
ATOM   5116  H  HE3  . MET   A 1 334 ? 28.721 13.455  30.565 1.00 26.83 ? 334  MET   A HE3  1 
ATOM   5117  N  N    . LEU   A 1 335 ? 28.728 16.092  28.009 1.00 11.11 ? 335  LEU   A N    1 
ATOM   5118  C  CA   . LEU   A 1 335 ? 29.888 15.942  27.090 1.00 11.89 ? 335  LEU   A CA   1 
ATOM   5119  C  C    . LEU   A 1 335 ? 30.002 17.185  26.203 1.00 14.54 ? 335  LEU   A C    1 
ATOM   5120  O  O    . LEU   A 1 335 ? 31.130 17.633  25.959 1.00 11.92 ? 335  LEU   A O    1 
ATOM   5121  C  CB   . LEU   A 1 335 ? 29.727 14.675  26.245 1.00 13.87 ? 335  LEU   A CB   1 
ATOM   5122  C  CG   . LEU   A 1 335 ? 29.965 13.360  26.985 1.00 14.42 ? 335  LEU   A CG   1 
ATOM   5123  C  CD1  . LEU   A 1 335 ? 29.743 12.173  26.059 1.00 17.62 ? 335  LEU   A CD1  1 
ATOM   5124  C  CD2  . LEU   A 1 335 ? 31.366 13.320  27.575 1.00 16.78 ? 335  LEU   A CD2  1 
ATOM   5125  H  H    . LEU   A 1 335 ? 28.083 15.538  27.877 1.00 13.34 ? 335  LEU   A H    1 
ATOM   5126  H  HA   . LEU   A 1 335 ? 30.704 15.856  27.607 1.00 14.28 ? 335  LEU   A HA   1 
ATOM   5127  H  HB2  . LEU   A 1 335 ? 28.830 14.663  25.875 1.00 16.65 ? 335  LEU   A HB2  1 
ATOM   5128  H  HB3  . LEU   A 1 335 ? 30.342 14.723  25.496 1.00 16.65 ? 335  LEU   A HB3  1 
ATOM   5129  H  HG   . LEU   A 1 335 ? 29.326 13.304  27.712 1.00 17.31 ? 335  LEU   A HG   1 
ATOM   5130  H  HD11 . LEU   A 1 335 ? 29.899 11.349  26.546 1.00 21.15 ? 335  LEU   A HD11 1 
ATOM   5131  H  HD12 . LEU   A 1 335 ? 28.831 12.186  25.729 1.00 21.15 ? 335  LEU   A HD12 1 
ATOM   5132  H  HD13 . LEU   A 1 335 ? 30.358 12.227  25.311 1.00 21.15 ? 335  LEU   A HD13 1 
ATOM   5133  H  HD21 . LEU   A 1 335 ? 31.498 12.479  28.040 1.00 20.13 ? 335  LEU   A HD21 1 
ATOM   5134  H  HD22 . LEU   A 1 335 ? 32.020 13.401  26.863 1.00 20.13 ? 335  LEU   A HD22 1 
ATOM   5135  H  HD23 . LEU   A 1 335 ? 31.476 14.054  28.199 1.00 20.13 ? 335  LEU   A HD23 1 
ATOM   5136  N  N    . CYS   A 1 336 ? 28.861 17.715  25.761 1.00 11.77 ? 336  CYS   A N    1 
ATOM   5137  C  CA   . CYS   A 1 336 ? 28.912 18.912  24.935 1.00 10.55 ? 336  CYS   A CA   1 
ATOM   5138  C  C    . CYS   A 1 336 ? 29.409 20.106  25.737 1.00 11.11 ? 336  CYS   A C    1 
ATOM   5139  O  O    . CYS   A 1 336 ? 30.185 20.924  25.230 1.00 10.37 ? 336  CYS   A O    1 
ATOM   5140  C  CB   . CYS   A 1 336 ? 27.542 19.192  24.333 1.00 11.66 ? 336  CYS   A CB   1 
ATOM   5141  S  SG   . CYS   A 1 336 ? 27.110 18.052  23.009 1.00 12.20 ? 336  CYS   A SG   1 
ATOM   5142  H  H    . CYS   A 1 336 ? 28.074 17.407  25.923 1.00 14.12 ? 336  CYS   A H    1 
ATOM   5143  H  HA   . CYS   A 1 336 ? 29.541 18.761  24.212 1.00 12.67 ? 336  CYS   A HA   1 
ATOM   5144  H  HB2  . CYS   A 1 336 ? 26.870 19.139  25.031 1.00 14.00 ? 336  CYS   A HB2  1 
ATOM   5145  H  HB3  . CYS   A 1 336 ? 27.524 20.099  23.991 1.00 14.00 ? 336  CYS   A HB3  1 
ATOM   5146  H  HG   . CYS   A 1 336 ? 25.978 17.681  23.153 1.00 14.64 ? 336  CYS   A HG   1 
ATOM   5147  N  N    . ASN   A 1 337 ? 28.990 20.211  27.003 1.00 11.23 ? 337  ASN   A N    1 
ATOM   5148  C  CA   . ASN   A 1 337 ? 29.489 21.283  27.858 1.00 11.10 ? 337  ASN   A CA   1 
ATOM   5149  C  C    . ASN   A 1 337 ? 30.976 21.121  28.151 1.00 13.51 ? 337  ASN   A C    1 
ATOM   5150  O  O    . ASN   A 1 337 ? 31.690 22.121  28.305 1.00 13.10 ? 337  ASN   A O    1 
ATOM   5151  C  CB   . ASN   A 1 337 ? 28.694 21.322  29.167 1.00 10.18 ? 337  ASN   A CB   1 
ATOM   5152  C  CG   . ASN   A 1 337 ? 27.286 21.865  28.971 1.00 10.35 ? 337  ASN   A CG   1 
ATOM   5153  O  OD1  . ASN   A 1 337 ? 27.025 22.575  28.006 1.00 10.94 ? 337  ASN   A OD1  1 
ATOM   5154  N  ND2  . ASN   A 1 337 ? 26.375 21.531  29.887 1.00 10.31 ? 337  ASN   A ND2  1 
ATOM   5155  H  H    . ASN   A 1 337 ? 28.427 19.679  27.377 1.00 13.48 ? 337  ASN   A H    1 
ATOM   5156  H  HA   . ASN   A 1 337 ? 29.371 22.121  27.384 1.00 13.32 ? 337  ASN   A HA   1 
ATOM   5157  H  HB2  . ASN   A 1 337 ? 28.645 20.428  29.540 1.00 12.22 ? 337  ASN   A HB2  1 
ATOM   5158  H  HB3  . ASN   A 1 337 ? 29.164 21.873  29.812 1.00 12.22 ? 337  ASN   A HB3  1 
ATOM   5159  H  HD21 . ASN   A 1 337 ? 25.567 21.816  29.814 1.00 12.38 ? 337  ASN   A HD21 1 
ATOM   5160  H  HD22 . ASN   A 1 337 ? 26.596 21.031  30.551 1.00 12.38 ? 337  ASN   A HD22 1 
ATOM   5161  N  N    . GLU   A 1 338 ? 31.455 19.877  28.234 1.00 10.20 ? 338  GLU   A N    1 
ATOM   5162  C  CA   . GLU   A 1 338 ? 32.855 19.638  28.571 1.00 11.64 ? 338  GLU   A CA   1 
ATOM   5163  C  C    . GLU   A 1 338 ? 33.770 19.829  27.369 1.00 12.78 ? 338  GLU   A C    1 
ATOM   5164  O  O    . GLU   A 1 338 ? 34.839 20.441  27.497 1.00 12.12 ? 338  GLU   A O    1 
ATOM   5165  C  CB   . GLU   A 1 338 ? 33.016 18.237  29.155 1.00 12.77 ? 338  GLU   A CB   1 
ATOM   5166  C  CG   . GLU   A 1 338 ? 32.453 18.111  30.565 1.00 12.36 ? 338  GLU   A CG   1 
ATOM   5167  C  CD   . GLU   A 1 338 ? 33.360 18.735  31.611 1.00 15.52 ? 338  GLU   A CD   1 
ATOM   5168  O  OE1  . GLU   A 1 338 ? 33.496 19.979  31.639 1.00 13.77 ? 338  GLU   A OE1  1 
ATOM   5169  O  OE2  . GLU   A 1 338 ? 33.950 17.977  32.405 1.00 15.65 ? 338  GLU   A OE2  1 
ATOM   5170  H  H    . GLU   A 1 338 ? 30.989 19.167  28.100 1.00 12.25 ? 338  GLU   A H    1 
ATOM   5171  H  HA   . GLU   A 1 338 ? 33.118 20.293  29.236 1.00 13.97 ? 338  GLU   A HA   1 
ATOM   5172  H  HB2  . GLU   A 1 338 ? 32.571 17.598  28.576 1.00 15.33 ? 338  GLU   A HB2  1 
ATOM   5173  H  HB3  . GLU   A 1 338 ? 33.957 18.003  29.166 1.00 15.33 ? 338  GLU   A HB3  1 
ATOM   5174  H  HG2  . GLU   A 1 338 ? 31.582 18.536  30.601 1.00 14.83 ? 338  GLU   A HG2  1 
ATOM   5175  H  HG3  . GLU   A 1 338 ? 32.320 17.173  30.774 1.00 14.83 ? 338  GLU   A HG3  1 
ATOM   5176  N  N    . TYR   A 1 339 ? 33.376 19.316  26.200 1.00 12.19 ? 339  TYR   A N    1 
ATOM   5177  C  CA   . TYR   A 1 339 ? 34.163 19.555  25.000 1.00 12.66 ? 339  TYR   A CA   1 
ATOM   5178  C  C    . TYR   A 1 339 ? 33.978 20.968  24.471 1.00 10.81 ? 339  TYR   A C    1 
ATOM   5179  O  O    . TYR   A 1 339 ? 34.805 21.435  23.678 1.00 14.23 ? 339  TYR   A O    1 
ATOM   5180  C  CB   . TYR   A 1 339 ? 33.804 18.549  23.909 1.00 12.51 ? 339  TYR   A CB   1 
ATOM   5181  C  CG   . TYR   A 1 339 ? 34.116 17.107  24.253 1.00 13.07 ? 339  TYR   A CG   1 
ATOM   5182  C  CD1  . TYR   A 1 339 ? 35.354 16.743  24.777 1.00 13.69 ? 339  TYR   A CD1  1 
ATOM   5183  C  CD2  . TYR   A 1 339 ? 33.172 16.106  24.032 1.00 14.30 ? 339  TYR   A CD2  1 
ATOM   5184  C  CE1  . TYR   A 1 339 ? 35.636 15.414  25.088 1.00 15.09 ? 339  TYR   A CE1  1 
ATOM   5185  C  CE2  . TYR   A 1 339 ? 33.443 14.791  24.335 1.00 15.51 ? 339  TYR   A CE2  1 
ATOM   5186  C  CZ   . TYR   A 1 339 ? 34.676 14.445  24.862 1.00 16.45 ? 339  TYR   A CZ   1 
ATOM   5187  O  OH   . TYR   A 1 339 ? 34.938 13.125  25.162 1.00 17.65 ? 339  TYR   A OH   1 
ATOM   5188  H  H    . TYR   A 1 339 ? 32.671 18.837  26.086 1.00 14.63 ? 339  TYR   A H    1 
ATOM   5189  H  HA   . TYR   A 1 339 ? 35.095 19.445  25.247 1.00 15.20 ? 339  TYR   A HA   1 
ATOM   5190  H  HB2  . TYR   A 1 339 ? 32.857 18.625  23.714 1.00 15.02 ? 339  TYR   A HB2  1 
ATOM   5191  H  HB3  . TYR   A 1 339 ? 34.280 18.786  23.098 1.00 15.02 ? 339  TYR   A HB3  1 
ATOM   5192  H  HD1  . TYR   A 1 339 ? 36.001 17.395  24.921 1.00 16.43 ? 339  TYR   A HD1  1 
ATOM   5193  H  HD2  . TYR   A 1 339 ? 32.344 16.331  23.673 1.00 17.17 ? 339  TYR   A HD2  1 
ATOM   5194  H  HE1  . TYR   A 1 339 ? 36.463 15.181  25.444 1.00 18.12 ? 339  TYR   A HE1  1 
ATOM   5195  H  HE2  . TYR   A 1 339 ? 32.799 14.136  24.186 1.00 18.61 ? 339  TYR   A HE2  1 
ATOM   5196  H  HH   . TYR   A 1 339 ? 35.762 13.024  25.288 1.00 21.19 ? 339  TYR   A HH   1 
ATOM   5197  N  N    . GLY   A 1 340 ? 32.923 21.658  24.901 1.00 10.49 ? 340  GLY   A N    1 
ATOM   5198  C  CA   . GLY   A 1 340 ? 32.648 22.996  24.425 1.00 13.23 ? 340  GLY   A CA   1 
ATOM   5199  C  C    . GLY   A 1 340 ? 32.071 23.055  23.023 1.00 10.14 ? 340  GLY   A C    1 
ATOM   5200  O  O    . GLY   A 1 340 ? 32.637 23.721  22.146 1.00 10.58 ? 340  GLY   A O    1 
ATOM   5201  H  H    . GLY   A 1 340 ? 32.354 21.360  25.473 1.00 12.60 ? 340  GLY   A H    1 
ATOM   5202  H  HA2  . GLY   A 1 340 ? 32.029 23.424  25.036 1.00 15.88 ? 340  GLY   A HA2  1 
ATOM   5203  H  HA3  . GLY   A 1 340 ? 33.470 23.511  24.447 1.00 15.88 ? 340  GLY   A HA3  1 
ATOM   5204  N  N    . ILE   A 1 341 ? 30.937 22.384  22.800 1.00 12.47 ? 341  ILE   A N    1 
ATOM   5205  C  CA   . ILE   A 1 341 ? 30.216 22.479  21.537 1.00 10.00 ? 341  ILE   A CA   1 
ATOM   5206  C  C    . ILE   A 1 341 ? 28.746 22.768  21.792 1.00 9.56  ? 341  ILE   A C    1 
ATOM   5207  O  O    . ILE   A 1 341 ? 28.182 22.416  22.830 1.00 9.34  ? 341  ILE   A O    1 
ATOM   5208  C  CB   . ILE   A 1 341 ? 30.339 21.211  20.667 1.00 11.01 ? 341  ILE   A CB   1 
ATOM   5209  C  CG1  . ILE   A 1 341 ? 29.880 19.968  21.424 1.00 9.39  ? 341  ILE   A CG1  1 
ATOM   5210  C  CG2  . ILE   A 1 341 ? 31.757 21.034  20.174 1.00 10.13 ? 341  ILE   A CG2  1 
ATOM   5211  C  CD1  . ILE   A 1 341 ? 30.004 18.692  20.584 1.00 11.88 ? 341  ILE   A CD1  1 
ATOM   5212  H  H    . ILE   A 1 341 ? 30.569 21.864  23.378 1.00 14.97 ? 341  ILE   A H    1 
ATOM   5213  H  HA   . ILE   A 1 341 ? 30.627 23.207  21.045 1.00 12.00 ? 341  ILE   A HA   1 
ATOM   5214  H  HB   . ILE   A 1 341 ? 29.756 21.326  19.900 1.00 13.22 ? 341  ILE   A HB   1 
ATOM   5215  H  HG12 . ILE   A 1 341 ? 30.407 19.872  22.233 1.00 11.27 ? 341  ILE   A HG12 1 
ATOM   5216  H  HG13 . ILE   A 1 341 ? 28.957 20.083  21.699 1.00 11.27 ? 341  ILE   A HG13 1 
ATOM   5217  H  HG21 . ILE   A 1 341 ? 31.813 20.233  19.630 1.00 12.15 ? 341  ILE   A HG21 1 
ATOM   5218  H  HG22 . ILE   A 1 341 ? 32.013 21.804  19.642 1.00 12.15 ? 341  ILE   A HG22 1 
ATOM   5219  H  HG23 . ILE   A 1 341 ? 32.356 20.952  20.933 1.00 12.15 ? 341  ILE   A HG23 1 
ATOM   5220  H  HD11 . ILE   A 1 341 ? 29.702 17.931  21.104 1.00 14.26 ? 341  ILE   A HD11 1 
ATOM   5221  H  HD12 . ILE   A 1 341 ? 29.458 18.775  19.787 1.00 14.26 ? 341  ILE   A HD12 1 
ATOM   5222  H  HD13 . ILE   A 1 341 ? 30.931 18.561  20.329 1.00 14.26 ? 341  ILE   A HD13 1 
ATOM   5223  N  N    . ASP   A 1 342 ? 28.128 23.389  20.792 1.00 10.21 ? 342  ASP   A N    1 
ATOM   5224  C  CA   . ASP   A 1 342 ? 26.690 23.631  20.774 1.00 10.64 ? 342  ASP   A CA   1 
ATOM   5225  C  C    . ASP   A 1 342 ? 25.945 22.304  20.673 1.00 10.34 ? 342  ASP   A C    1 
ATOM   5226  O  O    . ASP   A 1 342 ? 26.131 21.556  19.705 1.00 8.99  ? 342  ASP   A O    1 
ATOM   5227  C  CB   . ASP   A 1 342 ? 26.361 24.526  19.580 1.00 9.14  ? 342  ASP   A CB   1 
ATOM   5228  C  CG   . ASP   A 1 342 ? 24.881 24.613  19.292 1.00 9.10  ? 342  ASP   A CG   1 
ATOM   5229  O  OD1  . ASP   A 1 342 ? 24.074 24.555  20.242 1.00 10.98 ? 342  ASP   A OD1  1 
ATOM   5230  O  OD2  . ASP   A 1 342 ? 24.533 24.757  18.098 1.00 10.11 ? 342  ASP   A OD2  1 
ATOM   5231  H  H    . ASP   A 1 342 ? 28.538 23.685  20.096 1.00 12.26 ? 342  ASP   A H    1 
ATOM   5232  H  HA   . ASP   A 1 342 ? 26.413 24.072  21.592 1.00 12.77 ? 342  ASP   A HA   1 
ATOM   5233  H  HB2  . ASP   A 1 342 ? 26.705 25.417  19.747 1.00 10.98 ? 342  ASP   A HB2  1 
ATOM   5234  H  HB3  . ASP   A 1 342 ? 26.818 24.188  18.794 1.00 10.98 ? 342  ASP   A HB3  1 
ATOM   5235  N  N    . THR   A 1 343 ? 25.085 22.019  21.657 1.00 8.51  ? 343  THR   A N    1 
ATOM   5236  C  CA   . THR   A 1 343 ? 24.332 20.766  21.643 1.00 11.06 ? 343  THR   A CA   1 
ATOM   5237  C  C    . THR   A 1 343 ? 23.495 20.635  20.380 1.00 11.68 ? 343  THR   A C    1 
ATOM   5238  O  O    . THR   A 1 343 ? 23.437 19.560  19.774 1.00 10.71 ? 343  THR   A O    1 
ATOM   5239  C  CB   . THR   A 1 343 ? 23.410 20.673  22.859 1.00 10.07 ? 343  THR   A CB   1 
ATOM   5240  O  OG1  . THR   A 1 343 ? 22.669 21.892  22.985 1.00 9.62  ? 343  THR   A OG1  1 
ATOM   5241  C  CG2  . THR   A 1 343 ? 24.219 20.416  24.139 1.00 9.53  ? 343  THR   A CG2  1 
ATOM   5242  H  H    . THR   A 1 343 ? 24.927 22.530  22.330 1.00 10.22 ? 343  THR   A H    1 
ATOM   5243  H  HA   . THR   A 1 343 ? 24.980 20.045  21.669 1.00 13.27 ? 343  THR   A HA   1 
ATOM   5244  H  HB   . THR   A 1 343 ? 22.799 19.930  22.733 1.00 12.08 ? 343  THR   A HB   1 
ATOM   5245  H  HG1  . THR   A 1 343 ? 22.032 21.779  23.520 1.00 11.55 ? 343  THR   A HG1  1 
ATOM   5246  H  HG21 . THR   A 1 343 ? 23.617 20.361  24.897 1.00 11.44 ? 343  THR   A HG21 1 
ATOM   5247  H  HG22 . THR   A 1 343 ? 24.706 19.582  24.052 1.00 11.44 ? 343  THR   A HG22 1 
ATOM   5248  H  HG23 . THR   A 1 343 ? 24.846 21.143  24.277 1.00 11.44 ? 343  THR   A HG23 1 
ATOM   5249  N  N    . ILE   A 1 344 ? 22.854 21.728  19.963 1.00 9.27  ? 344  ILE   A N    1 
ATOM   5250  C  CA   . ILE   A 1 344 ? 21.862 21.661  18.891 1.00 9.60  ? 344  ILE   A CA   1 
ATOM   5251  C  C    . ILE   A 1 344 ? 22.511 21.261  17.574 1.00 9.85  ? 344  ILE   A C    1 
ATOM   5252  O  O    . ILE   A 1 344 ? 22.057 20.332  16.902 1.00 8.89  ? 344  ILE   A O    1 
ATOM   5253  C  CB   . ILE   A 1 344 ? 21.113 22.999  18.768 1.00 8.58  ? 344  ILE   A CB   1 
ATOM   5254  C  CG1  . ILE   A 1 344 ? 20.453 23.366  20.099 1.00 10.93 ? 344  ILE   A CG1  1 
ATOM   5255  C  CG2  . ILE   A 1 344 ? 20.061 22.922  17.661 1.00 9.70  ? 344  ILE   A CG2  1 
ATOM   5256  C  CD1  . ILE   A 1 344 ? 19.714 24.687  20.056 1.00 10.78 ? 344  ILE   A CD1  1 
ATOM   5257  H  H    . ILE   A 1 344 ? 22.979 22.515  20.287 1.00 11.13 ? 344  ILE   A H    1 
ATOM   5258  H  HA   . ILE   A 1 344 ? 21.213 20.975  19.114 1.00 11.53 ? 344  ILE   A HA   1 
ATOM   5259  H  HB   . ILE   A 1 344 ? 21.755 23.689  18.539 1.00 10.30 ? 344  ILE   A HB   1 
ATOM   5260  H  HG12 . ILE   A 1 344 ? 19.833 22.664  20.350 1.00 13.12 ? 344  ILE   A HG12 1 
ATOM   5261  H  HG13 . ILE   A 1 344 ? 21.133 23.405  20.790 1.00 13.12 ? 344  ILE   A HG13 1 
ATOM   5262  H  HG21 . ILE   A 1 344 ? 19.597 23.772  17.595 1.00 11.64 ? 344  ILE   A HG21 1 
ATOM   5263  H  HG22 . ILE   A 1 344 ? 20.494 22.724  16.816 1.00 11.64 ? 344  ILE   A HG22 1 
ATOM   5264  H  HG23 . ILE   A 1 344 ? 19.423 22.221  17.869 1.00 11.64 ? 344  ILE   A HG23 1 
ATOM   5265  H  HD11 . ILE   A 1 344 ? 19.319 24.865  20.924 1.00 12.94 ? 344  ILE   A HD11 1 
ATOM   5266  H  HD12 . ILE   A 1 344 ? 20.335 25.398  19.832 1.00 12.94 ? 344  ILE   A HD12 1 
ATOM   5267  H  HD13 . ILE   A 1 344 ? 19.015 24.645  19.385 1.00 12.94 ? 344  ILE   A HD13 1 
ATOM   5268  N  N    . THR   A 1 345 ? 23.579 21.952  17.186 1.00 9.79  ? 345  THR   A N    1 
ATOM   5269  C  CA   . THR   A 1 345 ? 24.282 21.611  15.921 1.00 10.81 ? 345  THR   A CA   1 
ATOM   5270  C  C    . THR   A 1 345 ? 24.870 20.194  16.019 1.00 11.70 ? 345  THR   A C    1 
ATOM   5271  O  O    . THR   A 1 345 ? 24.894 19.491  15.002 1.00 11.81 ? 345  THR   A O    1 
ATOM   5272  C  CB   . THR   A 1 345 ? 25.338 22.670  15.573 1.00 10.80 ? 345  THR   A CB   1 
ATOM   5273  O  OG1  . THR   A 1 345 ? 24.659 23.831  15.095 1.00 11.89 ? 345  THR   A OG1  1 
ATOM   5274  C  CG2  . THR   A 1 345 ? 26.326 22.194  14.532 1.00 8.74  ? 345  THR   A CG2  1 
ATOM   5275  H  H    . THR   A 1 345 ? 23.917 22.612  17.622 1.00 11.75 ? 345  THR   A H    1 
ATOM   5276  H  HA   . THR   A 1 345 ? 23.646 21.614  15.189 1.00 12.98 ? 345  THR   A HA   1 
ATOM   5277  H  HB   . THR   A 1 345 ? 25.851 22.862  16.374 1.00 12.96 ? 345  THR   A HB   1 
ATOM   5278  H  HG1  . THR   A 1 345 ? 24.406 23.702  14.305 1.00 14.27 ? 345  THR   A HG1  1 
ATOM   5279  H  HG21 . THR   A 1 345 ? 26.968 22.898  14.349 1.00 10.50 ? 345  THR   A HG21 1 
ATOM   5280  H  HG22 . THR   A 1 345 ? 26.792 21.410  14.862 1.00 10.50 ? 345  THR   A HG22 1 
ATOM   5281  H  HG23 . THR   A 1 345 ? 25.853 21.969  13.716 1.00 10.50 ? 345  THR   A HG23 1 
ATOM   5282  N  N    . CYS   A 1 346 ? 25.323 19.806  17.211 1.00 10.88 ? 346  CYS   A N    1 
ATOM   5283  C  CA   . CYS   A 1 346 ? 25.938 18.467  17.390 1.00 12.96 ? 346  CYS   A CA   1 
ATOM   5284  C  C    . CYS   A 1 346 ? 24.892 17.373  17.140 1.00 12.32 ? 346  CYS   A C    1 
ATOM   5285  O  O    . CYS   A 1 346 ? 25.106 16.554  16.243 1.00 10.95 ? 346  CYS   A O    1 
ATOM   5286  C  CB   . CYS   A 1 346 ? 26.501 18.320  18.796 1.00 13.11 ? 346  CYS   A CB   1 
ATOM   5287  S  SG   . CYS   A 1 346 ? 27.252 16.694  19.071 1.00 12.24 ? 346  CYS   A SG   1 
ATOM   5288  H  H    . CYS   A 1 346 ? 25.290 20.286  17.924 1.00 13.06 ? 346  CYS   A H    1 
ATOM   5289  H  HA   . CYS   A 1 346 ? 26.662 18.375  16.751 1.00 15.56 ? 346  CYS   A HA   1 
ATOM   5290  H  HB2  . CYS   A 1 346 ? 27.165 19.010  18.950 1.00 15.73 ? 346  CYS   A HB2  1 
ATOM   5291  H  HB3  . CYS   A 1 346 ? 25.791 18.459  19.442 1.00 15.73 ? 346  CYS   A HB3  1 
ATOM   5292  H  HG   . CYS   A 1 346 ? 27.679 16.634  20.191 1.00 14.70 ? 346  CYS   A HG   1 
ATOM   5293  N  N    . GLY   A 1 347 ? 23.813 17.379  17.923 1.00 13.21 ? 347  GLY   A N    1 
ATOM   5294  C  CA   . GLY   A 1 347 ? 22.775 16.342  17.775 1.00 11.87 ? 347  GLY   A CA   1 
ATOM   5295  C  C    . GLY   A 1 347 ? 22.148 16.340  16.390 1.00 11.71 ? 347  GLY   A C    1 
ATOM   5296  O  O    . GLY   A 1 347 ? 21.890 15.254  15.859 1.00 11.88 ? 347  GLY   A O    1 
ATOM   5297  H  H    . GLY   A 1 347 ? 23.659 17.961  18.537 1.00 15.86 ? 347  GLY   A H    1 
ATOM   5298  H  HA2  . GLY   A 1 347 ? 23.164 15.471  17.952 1.00 14.25 ? 347  GLY   A HA2  1 
ATOM   5299  H  HA3  . GLY   A 1 347 ? 22.083 16.484  18.440 1.00 14.25 ? 347  GLY   A HA3  1 
ATOM   5300  N  N    . ALA   A 1 348 ? 21.883 17.525  15.844 1.00 11.71 ? 348  ALA   A N    1 
ATOM   5301  C  CA   . ALA   A 1 348 ? 21.205 17.600  14.531 1.00 10.70 ? 348  ALA   A CA   1 
ATOM   5302  C  C    . ALA   A 1 348 ? 22.178 17.210  13.414 1.00 11.60 ? 348  ALA   A C    1 
ATOM   5303  O  O    . ALA   A 1 348 ? 21.700 16.823  12.338 1.00 11.91 ? 348  ALA   A O    1 
ATOM   5304  C  CB   . ALA   A 1 348 ? 20.609 18.969  14.331 1.00 13.03 ? 348  ALA   A CB   1 
ATOM   5305  H  H    . ALA   A 1 348 ? 22.078 18.284  16.199 1.00 14.05 ? 348  ALA   A H    1 
ATOM   5306  H  HA   . ALA   A 1 348 ? 20.472 16.966  14.504 1.00 12.84 ? 348  ALA   A HA   1 
ATOM   5307  H  HB1  . ALA   A 1 348 ? 20.168 19.007  13.468 1.00 15.63 ? 348  ALA   A HB1  1 
ATOM   5308  H  HB2  . ALA   A 1 348 ? 19.963 19.146  15.032 1.00 15.63 ? 348  ALA   A HB2  1 
ATOM   5309  H  HB3  . ALA   A 1 348 ? 21.312 19.636  14.364 1.00 15.63 ? 348  ALA   A HB3  1 
ATOM   5310  N  N    . THR   A 1 349 ? 23.487 17.325  13.653 1.00 11.29 ? 349  THR   A N    1 
ATOM   5311  C  CA   . THR   A 1 349 ? 24.461 16.831  12.644 1.00 12.46 ? 349  THR   A CA   1 
ATOM   5312  C  C    . THR   A 1 349 ? 24.475 15.301  12.715 1.00 11.80 ? 349  THR   A C    1 
ATOM   5313  O  O    . THR   A 1 349 ? 24.537 14.667  11.652 1.00 12.38 ? 349  THR   A O    1 
ATOM   5314  C  CB   . THR   A 1 349 ? 25.855 17.450  12.829 1.00 9.74  ? 349  THR   A CB   1 
ATOM   5315  O  OG1  . THR   A 1 349 ? 25.764 18.854  12.593 1.00 10.05 ? 349  THR   A OG1  1 
ATOM   5316  C  CG2  . THR   A 1 349 ? 26.892 16.844  11.909 1.00 14.41 ? 349  THR   A CG2  1 
ATOM   5317  H  H    . THR   A 1 349 ? 23.832 17.670  14.361 1.00 13.55 ? 349  THR   A H    1 
ATOM   5318  H  HA   . THR   A 1 349 ? 24.186 17.108  11.756 1.00 14.96 ? 349  THR   A HA   1 
ATOM   5319  H  HB   . THR   A 1 349 ? 26.145 17.267  13.736 1.00 11.70 ? 349  THR   A HB   1 
ATOM   5320  H  HG1  . THR   A 1 349 ? 25.449 19.233  13.273 1.00 12.07 ? 349  THR   A HG1  1 
ATOM   5321  H  HG21 . THR   A 1 349 ? 27.750 17.268  12.065 1.00 17.29 ? 349  THR   A HG21 1 
ATOM   5322  H  HG22 . THR   A 1 349 ? 26.965 15.893  12.085 1.00 17.29 ? 349  THR   A HG22 1 
ATOM   5323  H  HG23 . THR   A 1 349 ? 26.627 16.982  10.986 1.00 17.29 ? 349  THR   A HG23 1 
ATOM   5324  N  N    . ILE   A 1 350 ? 24.434 14.741  13.929 1.00 10.93 ? 350  ILE   A N    1 
ATOM   5325  C  CA   . ILE   A 1 350 ? 24.321 13.286  14.024 1.00 10.91 ? 350  ILE   A CA   1 
ATOM   5326  C  C    . ILE   A 1 350 ? 23.033 12.816  13.355 1.00 11.04 ? 350  ILE   A C    1 
ATOM   5327  O  O    . ILE   A 1 350 ? 23.004 11.774  12.684 1.00 12.50 ? 350  ILE   A O    1 
ATOM   5328  C  CB   . ILE   A 1 350 ? 24.402 12.825  15.496 1.00 11.01 ? 350  ILE   A CB   1 
ATOM   5329  C  CG1  . ILE   A 1 350 ? 25.781 13.140  16.093 1.00 14.30 ? 350  ILE   A CG1  1 
ATOM   5330  C  CG2  . ILE   A 1 350 ? 24.082 11.330  15.616 1.00 15.10 ? 350  ILE   A CG2  1 
ATOM   5331  C  CD1  . ILE   A 1 350 ? 25.868 12.882  17.605 1.00 14.61 ? 350  ILE   A CD1  1 
ATOM   5332  H  H    . ILE   A 1 350 ? 24.469 15.165  14.677 1.00 13.12 ? 350  ILE   A H    1 
ATOM   5333  H  HA   . ILE   A 1 350 ? 25.067 12.881  13.555 1.00 13.10 ? 350  ILE   A HA   1 
ATOM   5334  H  HB   . ILE   A 1 350 ? 23.737 13.317  16.003 1.00 13.21 ? 350  ILE   A HB   1 
ATOM   5335  H  HG12 . ILE   A 1 350 ? 26.451 12.603  15.642 1.00 17.16 ? 350  ILE   A HG12 1 
ATOM   5336  H  HG13 . ILE   A 1 350 ? 25.997 14.069  15.918 1.00 17.16 ? 350  ILE   A HG13 1 
ATOM   5337  H  HG21 . ILE   A 1 350 ? 24.138 11.061  16.546 1.00 18.12 ? 350  ILE   A HG21 1 
ATOM   5338  H  HG22 . ILE   A 1 350 ? 23.186 11.163  15.285 1.00 18.12 ? 350  ILE   A HG22 1 
ATOM   5339  H  HG23 . ILE   A 1 350 ? 24.720 10.819  15.093 1.00 18.12 ? 350  ILE   A HG23 1 
ATOM   5340  H  HD11 . ILE   A 1 350 ? 26.759 13.099  17.920 1.00 17.54 ? 350  ILE   A HD11 1 
ATOM   5341  H  HD12 . ILE   A 1 350 ? 25.219 13.436  18.066 1.00 17.54 ? 350  ILE   A HD12 1 
ATOM   5342  H  HD13 . ILE   A 1 350 ? 25.681 11.948  17.785 1.00 17.54 ? 350  ILE   A HD13 1 
ATOM   5343  N  N    . ALA   A 1 351 ? 21.946 13.574  13.520 1.00 11.70 ? 351  ALA   A N    1 
ATOM   5344  C  CA   . ALA   A 1 351 ? 20.679 13.185  12.903 1.00 10.78 ? 351  ALA   A CA   1 
ATOM   5345  C  C    . ALA   A 1 351 ? 20.773 13.211  11.380 1.00 10.92 ? 351  ALA   A C    1 
ATOM   5346  O  O    . ALA   A 1 351 ? 20.236 12.327  10.702 1.00 12.33 ? 351  ALA   A O    1 
ATOM   5347  C  CB   . ALA   A 1 351 ? 19.555 14.103  13.386 1.00 10.81 ? 351  ALA   A CB   1 
ATOM   5348  H  H    . ALA   A 1 351 ? 21.921 14.303  13.976 1.00 14.04 ? 351  ALA   A H    1 
ATOM   5349  H  HA   . ALA   A 1 351 ? 20.480 12.274  13.171 1.00 12.94 ? 351  ALA   A HA   1 
ATOM   5350  H  HB1  . ALA   A 1 351 ? 18.719 13.837  12.972 1.00 12.98 ? 351  ALA   A HB1  1 
ATOM   5351  H  HB2  . ALA   A 1 351 ? 19.473 14.035  14.350 1.00 12.98 ? 351  ALA   A HB2  1 
ATOM   5352  H  HB3  . ALA   A 1 351 ? 19.759 15.020  13.143 1.00 12.98 ? 351  ALA   A HB3  1 
ATOM   5353  N  N    . ALA   A 1 352 ? 21.442 14.226  10.825 1.00 11.69 ? 352  ALA   A N    1 
ATOM   5354  C  CA   . ALA   A 1 352 ? 21.644 14.276  9.378  1.00 11.32 ? 352  ALA   A CA   1 
ATOM   5355  C  C    . ALA   A 1 352 ? 22.462 13.082  8.903  1.00 10.94 ? 352  ALA   A C    1 
ATOM   5356  O  O    . ALA   A 1 352 ? 22.135 12.461  7.881  1.00 10.67 ? 352  ALA   A O    1 
ATOM   5357  C  CB   . ALA   A 1 352 ? 22.329 15.579  8.972  1.00 12.06 ? 352  ALA   A CB   1 
ATOM   5358  H  H    . ALA   A 1 352 ? 21.781 14.884  11.262 1.00 14.04 ? 352  ALA   A H    1 
ATOM   5359  H  HA   . ALA   A 1 352 ? 20.772 14.240  8.954  1.00 13.59 ? 352  ALA   A HA   1 
ATOM   5360  H  HB1  . ALA   A 1 352 ? 22.454 15.593  8.010  1.00 14.48 ? 352  ALA   A HB1  1 
ATOM   5361  H  HB2  . ALA   A 1 352 ? 21.777 16.331  9.237  1.00 14.48 ? 352  ALA   A HB2  1 
ATOM   5362  H  HB3  . ALA   A 1 352 ? 23.192 15.641  9.411  1.00 14.48 ? 352  ALA   A HB3  1 
ATOM   5363  N  N    . ALA   A 1 353 ? 23.521 12.736  9.645  1.00 10.02 ? 353  ALA   A N    1 
ATOM   5364  C  CA   . ALA   A 1 353 ? 24.328 11.569  9.294  1.00 12.94 ? 353  ALA   A CA   1 
ATOM   5365  C  C    . ALA   A 1 353 ? 23.504 10.288  9.346  1.00 13.20 ? 353  ALA   A C    1 
ATOM   5366  O  O    . ALA   A 1 353 ? 23.668 9.402   8.500  1.00 12.05 ? 353  ALA   A O    1 
ATOM   5367  C  CB   . ALA   A 1 353 ? 25.540 11.459  10.228 1.00 14.32 ? 353  ALA   A CB   1 
ATOM   5368  H  H    . ALA   A 1 353 ? 23.783 13.160  10.346 1.00 12.03 ? 353  ALA   A H    1 
ATOM   5369  H  HA   . ALA   A 1 353 ? 24.640 11.686  8.383  1.00 15.53 ? 353  ALA   A HA   1 
ATOM   5370  H  HB1  . ALA   A 1 353 ? 26.067 10.682  9.985  1.00 17.19 ? 353  ALA   A HB1  1 
ATOM   5371  H  HB2  . ALA   A 1 353 ? 26.085 12.257  10.146 1.00 17.19 ? 353  ALA   A HB2  1 
ATOM   5372  H  HB3  . ALA   A 1 353 ? 25.235 11.369  11.144 1.00 17.19 ? 353  ALA   A HB3  1 
ATOM   5373  N  N    . MET   A 1 354 ? 22.609 10.184  10.323 1.00 11.53 ? 354  MET   A N    1 
ATOM   5374  C  CA   . MET   A 1 354 ? 21.761 8.972   10.428 1.00 12.24 ? 354  MET   A CA   1 
ATOM   5375  C  C    . MET   A 1 354 ? 20.834 8.882   9.207  1.00 13.36 ? 354  MET   A C    1 
ATOM   5376  O  O    . MET   A 1 354 ? 20.571 7.760   8.755  1.00 14.94 ? 354  MET   A O    1 
ATOM   5377  C  CB   . MET   A 1 354 ? 20.943 8.988   11.721 1.00 11.30 ? 354  MET   A CB   1 
ATOM   5378  C  CG   . MET   A 1 354 ? 21.784 8.683   12.941 1.00 13.43 ? 354  MET   A CG   1 
ATOM   5379  S  SD   . MET   A 1 354 ? 20.827 8.679   14.471 1.00 14.22 ? 354  MET   A SD   1 
ATOM   5380  C  CE   . MET   A 1 354 ? 21.981 7.860   15.571 1.00 18.44 ? 354  MET   A CE   1 
ATOM   5381  H  H    . MET   A 1 354 ? 22.470 10.781  10.926 1.00 13.83 ? 354  MET   A H    1 
ATOM   5382  H  HA   . MET   A 1 354 ? 22.336 8.191   10.449 1.00 14.69 ? 354  MET   A HA   1 
ATOM   5383  H  HB2  . MET   A 1 354 ? 20.528 9.858   11.827 1.00 13.56 ? 354  MET   A HB2  1 
ATOM   5384  H  HB3  . MET   A 1 354 ? 20.226 8.338   11.655 1.00 13.56 ? 354  MET   A HB3  1 
ATOM   5385  H  HG2  . MET   A 1 354 ? 22.208 7.818   12.828 1.00 16.12 ? 354  MET   A HG2  1 
ATOM   5386  H  HG3  . MET   A 1 354 ? 22.494 9.340   13.011 1.00 16.12 ? 354  MET   A HG3  1 
ATOM   5387  H  HE1  . MET   A 1 354 ? 21.589 7.786   16.455 1.00 22.13 ? 354  MET   A HE1  1 
ATOM   5388  H  HE2  . MET   A 1 354 ? 22.179 6.973   15.231 1.00 22.13 ? 354  MET   A HE2  1 
ATOM   5389  H  HE3  . MET   A 1 354 ? 22.801 8.376   15.623 1.00 22.13 ? 354  MET   A HE3  1 
ATOM   5390  N  N    . GLU   A 1 355 ? 20.374 10.027  8.691  1.00 12.86 ? 355  GLU   A N    1 
ATOM   5391  C  CA   . GLU   A 1 355 ? 19.502 10.013  7.480  1.00 13.43 ? 355  GLU   A CA   1 
ATOM   5392  C  C    . GLU   A 1 355 ? 20.338 9.668   6.238  1.00 13.61 ? 355  GLU   A C    1 
ATOM   5393  O  O    . GLU   A 1 355 ? 19.849 8.906   5.389  1.00 11.53 ? 355  GLU   A O    1 
ATOM   5394  C  CB   . GLU   A 1 355 ? 18.746 11.334  7.303  1.00 12.01 ? 355  GLU   A CB   1 
ATOM   5395  C  CG   . GLU   A 1 355 ? 17.941 11.381  6.015  1.00 13.81 ? 355  GLU   A CG   1 
ATOM   5396  C  CD   . GLU   A 1 355 ? 16.690 12.242  6.044  1.00 13.96 ? 355  GLU   A CD   1 
ATOM   5397  O  OE1  . GLU   A 1 355 ? 16.670 13.228  6.799  1.00 12.02 ? 355  GLU   A OE1  1 
ATOM   5398  O  OE2  . GLU   A 1 355 ? 15.743 11.928  5.299  1.00 13.53 ? 355  GLU   A OE2  1 
ATOM   5399  H  H    . GLU   A 1 355 ? 20.543 10.808  9.008  1.00 15.43 ? 355  GLU   A H    1 
ATOM   5400  H  HA   . GLU   A 1 355 ? 18.828 9.326   7.599  1.00 16.12 ? 355  GLU   A HA   1 
ATOM   5401  H  HB2  . GLU   A 1 355 ? 18.150 11.465  8.057  1.00 14.42 ? 355  GLU   A HB2  1 
ATOM   5402  H  HB3  . GLU   A 1 355 ? 19.380 12.068  7.311  1.00 14.42 ? 355  GLU   A HB3  1 
ATOM   5403  H  HG2  . GLU   A 1 355 ? 18.518 11.704  5.305  1.00 16.57 ? 355  GLU   A HG2  1 
ATOM   5404  H  HG3  . GLU   A 1 355 ? 17.684 10.475  5.782  1.00 16.57 ? 355  GLU   A HG3  1 
ATOM   5405  N  N    . LEU   A 1 356 ? 21.548 10.223  6.135  1.00 12.69 ? 356  LEU   A N    1 
ATOM   5406  C  CA   . LEU   A 1 356 ? 22.438 9.894   4.994  1.00 15.54 ? 356  LEU   A CA   1 
ATOM   5407  C  C    . LEU   A 1 356 ? 22.693 8.381   4.996  1.00 15.45 ? 356  LEU   A C    1 
ATOM   5408  O  O    . LEU   A 1 356 ? 22.718 7.779   3.913  1.00 15.22 ? 356  LEU   A O    1 
ATOM   5409  C  CB   . LEU   A 1 356 ? 23.755 10.663  5.139  1.00 14.91 ? 356  LEU   A CB   1 
ATOM   5410  C  CG   . LEU   A 1 356 ? 23.695 12.159  4.835  1.00 11.59 ? 356  LEU   A CG   1 
ATOM   5411  C  CD1  . LEU   A 1 356 ? 25.074 12.787  4.964  1.00 15.70 ? 356  LEU   A CD1  1 
ATOM   5412  C  CD2  . LEU   A 1 356 ? 23.125 12.409  3.447  1.00 14.43 ? 356  LEU   A CD2  1 
ATOM   5413  H  H    . LEU   A 1 356 ? 21.876 10.783  6.699  1.00 15.24 ? 356  LEU   A H    1 
ATOM   5414  H  HA   . LEU   A 1 356 ? 22.024 10.149  4.154  1.00 18.65 ? 356  LEU   A HA   1 
ATOM   5415  H  HB2  . LEU   A 1 356 ? 24.077 10.548  6.047  1.00 17.90 ? 356  LEU   A HB2  1 
ATOM   5416  H  HB3  . LEU   A 1 356 ? 24.412 10.258  4.551  1.00 17.90 ? 356  LEU   A HB3  1 
ATOM   5417  H  HG   . LEU   A 1 356 ? 23.105 12.574  5.484  1.00 13.91 ? 356  LEU   A HG   1 
ATOM   5418  H  HD11 . LEU   A 1 356 ? 25.018 13.735  4.768  1.00 18.84 ? 356  LEU   A HD11 1 
ATOM   5419  H  HD12 . LEU   A 1 356 ? 25.403 12.663  5.868  1.00 18.84 ? 356  LEU   A HD12 1 
ATOM   5420  H  HD13 . LEU   A 1 356 ? 25.682 12.364  4.338  1.00 18.84 ? 356  LEU   A HD13 1 
ATOM   5421  H  HD21 . LEU   A 1 356 ? 23.096 13.363  3.276  1.00 17.32 ? 356  LEU   A HD21 1 
ATOM   5422  H  HD22 . LEU   A 1 356 ? 23.687 11.979  2.784  1.00 17.32 ? 356  LEU   A HD22 1 
ATOM   5423  H  HD23 . LEU   A 1 356 ? 22.228 12.044  3.395  1.00 17.32 ? 356  LEU   A HD23 1 
ATOM   5424  N  N    . TYR   A 1 357 ? 22.889 7.802   6.181  1.00 14.66 ? 357  TYR   A N    1 
ATOM   5425  C  CA   . TYR   A 1 357 ? 23.076 6.331   6.269  1.00 15.40 ? 357  TYR   A CA   1 
ATOM   5426  C  C    . TYR   A 1 357 ? 21.776 5.627   5.862  1.00 13.39 ? 357  TYR   A C    1 
ATOM   5427  O  O    . TYR   A 1 357 ? 21.839 4.686   5.054  1.00 13.81 ? 357  TYR   A O    1 
ATOM   5428  C  CB   . TYR   A 1 357 ? 23.487 5.886   7.674  1.00 14.34 ? 357  TYR   A CB   1 
ATOM   5429  C  CG   . TYR   A 1 357 ? 23.666 4.393   7.775  1.00 15.31 ? 357  TYR   A CG   1 
ATOM   5430  C  CD1  . TYR   A 1 357 ? 24.800 3.781   7.271  1.00 16.27 ? 357  TYR   A CD1  1 
ATOM   5431  C  CD2  . TYR   A 1 357 ? 22.682 3.588   8.323  1.00 15.55 ? 357  TYR   A CD2  1 
ATOM   5432  C  CE1  . TYR   A 1 357 ? 24.969 2.409   7.334  1.00 17.71 ? 357  TYR   A CE1  1 
ATOM   5433  C  CE2  . TYR   A 1 357 ? 22.834 2.214   8.393  1.00 16.55 ? 357  TYR   A CE2  1 
ATOM   5434  C  CZ   . TYR   A 1 357 ? 23.982 1.623   7.897  1.00 16.82 ? 357  TYR   A CZ   1 
ATOM   5435  O  OH   . TYR   A 1 357 ? 24.145 0.263   7.960  1.00 19.03 ? 357  TYR   A OH   1 
ATOM   5436  H  H    . TYR   A 1 357 ? 22.918 8.220   6.932  1.00 17.60 ? 357  TYR   A H    1 
ATOM   5437  H  HA   . TYR   A 1 357 ? 23.794 6.086   5.664  1.00 18.48 ? 357  TYR   A HA   1 
ATOM   5438  H  HB2  . TYR   A 1 357 ? 24.316 6.326   7.920  1.00 17.21 ? 357  TYR   A HB2  1 
ATOM   5439  H  HB3  . TYR   A 1 357 ? 22.814 6.172   8.311  1.00 17.21 ? 357  TYR   A HB3  1 
ATOM   5440  H  HD1  . TYR   A 1 357 ? 25.463 4.303   6.881  1.00 19.52 ? 357  TYR   A HD1  1 
ATOM   5441  H  HD2  . TYR   A 1 357 ? 21.904 3.978   8.650  1.00 18.66 ? 357  TYR   A HD2  1 
ATOM   5442  H  HE1  . TYR   A 1 357 ? 25.743 2.018   6.999  1.00 21.26 ? 357  TYR   A HE1  1 
ATOM   5443  H  HE2  . TYR   A 1 357 ? 22.166 1.690   8.772  1.00 19.87 ? 357  TYR   A HE2  1 
ATOM   5444  H  HH   . TYR   A 1 357 ? 24.896 0.056   7.646  1.00 22.84 ? 357  TYR   A HH   1 
ATOM   5445  N  N    . GLN   A 1 358 ? 20.650 6.065   6.433  1.00 14.55 ? 358  GLN   A N    1 
ATOM   5446  C  CA   . GLN   A 1 358 ? 19.367 5.477   6.063  1.00 13.69 ? 358  GLN   A CA   1 
ATOM   5447  C  C    . GLN   A 1 358 ? 19.193 5.409   4.552  1.00 14.79 ? 358  GLN   A C    1 
ATOM   5448  O  O    . GLN   A 1 358 ? 18.653 4.430   4.021  1.00 13.50 ? 358  GLN   A O    1 
ATOM   5449  C  CB   . GLN   A 1 358 ? 18.233 6.287   6.696  1.00 16.17 ? 358  GLN   A CB   1 
ATOM   5450  C  CG   . GLN   A 1 358 ? 16.854 6.044   6.091  1.00 18.88 ? 358  GLN   A CG   1 
ATOM   5451  C  CD   . GLN   A 1 358 ? 15.841 7.098   6.508  1.00 16.28 ? 358  GLN   A CD   1 
ATOM   5452  O  OE1  . GLN   A 1 358 ? 15.842 7.560   7.651  1.00 14.80 ? 358  GLN   A OE1  1 
ATOM   5453  N  NE2  . GLN   A 1 358 ? 14.968 7.484   5.579  1.00 16.65 ? 358  GLN   A NE2  1 
ATOM   5454  H  H    . GLN   A 1 358 ? 20.610 6.688   7.024  1.00 17.46 ? 358  GLN   A H    1 
ATOM   5455  H  HA   . GLN   A 1 358 ? 19.342 4.567   6.397  1.00 16.43 ? 358  GLN   A HA   1 
ATOM   5456  H  HB2  . GLN   A 1 358 ? 18.197 6.082   7.643  1.00 19.41 ? 358  GLN   A HB2  1 
ATOM   5457  H  HB3  . GLN   A 1 358 ? 18.444 7.230   6.618  1.00 19.41 ? 358  GLN   A HB3  1 
ATOM   5458  H  HG2  . GLN   A 1 358 ? 16.926 6.034   5.124  1.00 22.66 ? 358  GLN   A HG2  1 
ATOM   5459  H  HG3  . GLN   A 1 358 ? 16.535 5.169   6.361  1.00 22.66 ? 358  GLN   A HG3  1 
ATOM   5460  H  HE21 . GLN   A 1 358 ? 14.997 7.139   4.792  1.00 19.99 ? 358  GLN   A HE21 1 
ATOM   5461  H  HE22 . GLN   A 1 358 ? 14.375 8.078   5.767  1.00 19.99 ? 358  GLN   A HE22 1 
ATOM   5462  N  N    . ARG   A 1 359 ? 19.656 6.436   3.842  1.00 15.14 ? 359  ARG   A N    1 
ATOM   5463  C  CA   . ARG   A 1 359 ? 19.417 6.561   2.414  1.00 16.57 ? 359  ARG   A CA   1 
ATOM   5464  C  C    . ARG   A 1 359 ? 20.613 6.120   1.579  1.00 17.30 ? 359  ARG   A C    1 
ATOM   5465  O  O    . ARG   A 1 359 ? 20.660 6.407   0.377  1.00 17.39 ? 359  ARG   A O    1 
ATOM   5466  C  CB   . ARG   A 1 359 ? 19.020 8.000   2.082  1.00 13.19 ? 359  ARG   A CB   1 
ATOM   5467  C  CG   . ARG   A 1 359 ? 17.757 8.444   2.825  1.00 17.12 ? 359  ARG   A CG   1 
ATOM   5468  C  CD   . ARG   A 1 359 ? 17.262 9.811   2.378  1.00 17.35 ? 359  ARG   A CD   1 
ATOM   5469  N  NE   . ARG   A 1 359 ? 16.037 10.192  3.079  1.00 14.44 ? 359  ARG   A NE   1 
ATOM   5470  C  CZ   . ARG   A 1 359 ? 14.812 9.864   2.693  1.00 18.72 ? 359  ARG   A CZ   1 
ATOM   5471  N  NH1  . ARG   A 1 359 ? 14.595 9.179   1.582  1.00 20.41 ? 359  ARG   A NH1  1 
ATOM   5472  N  NH2  . ARG   A 1 359 ? 13.775 10.229  3.447  1.00 16.84 ? 359  ARG   A NH2  1 
ATOM   5473  H  H    . ARG   A 1 359 ? 20.118 7.079   4.179  1.00 18.17 ? 359  ARG   A H    1 
ATOM   5474  H  HA   . ARG   A 1 359 ? 18.688 5.963   2.184  1.00 19.89 ? 359  ARG   A HA   1 
ATOM   5475  H  HB2  . ARG   A 1 359 ? 19.752 8.595   2.309  1.00 15.84 ? 359  ARG   A HB2  1 
ATOM   5476  H  HB3  . ARG   A 1 359 ? 18.875 8.080   1.126  1.00 15.84 ? 359  ARG   A HB3  1 
ATOM   5477  H  HG2  . ARG   A 1 359 ? 17.056 7.788   2.684  1.00 20.55 ? 359  ARG   A HG2  1 
ATOM   5478  H  HG3  . ARG   A 1 359 ? 17.938 8.465   3.778  1.00 20.55 ? 359  ARG   A HG3  1 
ATOM   5479  H  HD2  . ARG   A 1 359 ? 17.950 10.475  2.542  1.00 20.82 ? 359  ARG   A HD2  1 
ATOM   5480  H  HD3  . ARG   A 1 359 ? 17.099 9.801   1.422  1.00 20.82 ? 359  ARG   A HD3  1 
ATOM   5481  H  HE   . ARG   A 1 359 ? 16.117 10.663  3.794  1.00 17.33 ? 359  ARG   A HE   1 
ATOM   5482  H  HH11 . ARG   A 1 359 ? 15.257 8.935   1.091  1.00 24.49 ? 359  ARG   A HH11 1 
ATOM   5483  H  HH12 . ARG   A 1 359 ? 13.791 8.977   1.351  1.00 24.49 ? 359  ARG   A HH12 1 
ATOM   5484  H  HH21 . ARG   A 1 359 ? 13.906 10.671  4.173  1.00 20.21 ? 359  ARG   A HH21 1 
ATOM   5485  H  HH22 . ARG   A 1 359 ? 12.975 10.022  3.207  1.00 20.21 ? 359  ARG   A HH22 1 
ATOM   5486  N  N    . GLY   A 1 360 ? 21.576 5.427   2.188  1.00 17.58 ? 360  GLY   A N    1 
ATOM   5487  C  CA   . GLY   A 1 360 ? 22.639 4.780   1.446  1.00 18.50 ? 360  GLY   A CA   1 
ATOM   5488  C  C    . GLY   A 1 360 ? 23.800 5.659   1.034  1.00 21.31 ? 360  GLY   A C    1 
ATOM   5489  O  O    . GLY   A 1 360 ? 24.647 5.202   0.259  1.00 16.44 ? 360  GLY   A O    1 
ATOM   5490  H  H    . GLY   A 1 360 ? 21.625 5.323   3.040  1.00 21.10 ? 360  GLY   A H    1 
ATOM   5491  H  HA2  . GLY   A 1 360 ? 22.985 4.050   1.983  1.00 22.20 ? 360  GLY   A HA2  1 
ATOM   5492  H  HA3  . GLY   A 1 360 ? 22.256 4.386   0.646  1.00 22.20 ? 360  GLY   A HA3  1 
ATOM   5493  N  N    . TYR   A 1 361 ? 23.879 6.899   1.523  1.00 16.33 ? 361  TYR   A N    1 
ATOM   5494  C  CA   . TYR   A 1 361 ? 24.994 7.761   1.141  1.00 20.66 ? 361  TYR   A CA   1 
ATOM   5495  C  C    . TYR   A 1 361 ? 26.266 7.384   1.889  1.00 18.38 ? 361  TYR   A C    1 
ATOM   5496  O  O    . TYR   A 1 361 ? 27.361 7.418   1.317  1.00 19.70 ? 361  TYR   A O    1 
ATOM   5497  C  CB   . TYR   A 1 361 ? 24.641 9.230   1.394  1.00 16.82 ? 361  TYR   A CB   1 
ATOM   5498  C  CG   . TYR   A 1 361 ? 23.614 9.783   0.439  1.00 16.66 ? 361  TYR   A CG   1 
ATOM   5499  C  CD1  . TYR   A 1 361 ? 23.997 10.370  -0.764 1.00 18.01 ? 361  TYR   A CD1  1 
ATOM   5500  C  CD2  . TYR   A 1 361 ? 22.259 9.746   0.747  1.00 16.24 ? 361  TYR   A CD2  1 
ATOM   5501  C  CE1  . TYR   A 1 361 ? 23.057 10.887  -1.640 1.00 19.40 ? 361  TYR   A CE1  1 
ATOM   5502  C  CE2  . TYR   A 1 361 ? 21.315 10.261  -0.119 1.00 17.86 ? 361  TYR   A CE2  1 
ATOM   5503  C  CZ   . TYR   A 1 361 ? 21.720 10.831  -1.312 1.00 19.73 ? 361  TYR   A CZ   1 
ATOM   5504  O  OH   . TYR   A 1 361 ? 20.778 11.344  -2.176 1.00 22.81 ? 361  TYR   A OH   1 
ATOM   5505  H  H    . TYR   A 1 361 ? 23.311 7.251   2.064  1.00 19.60 ? 361  TYR   A H    1 
ATOM   5506  H  HA   . TYR   A 1 361 ? 25.158 7.636   0.193  1.00 24.80 ? 361  TYR   A HA   1 
ATOM   5507  H  HB2  . TYR   A 1 361 ? 24.310 9.323   2.301  1.00 20.19 ? 361  TYR   A HB2  1 
ATOM   5508  H  HB3  . TYR   A 1 361 ? 25.449 9.763   1.331  1.00 20.19 ? 361  TYR   A HB3  1 
ATOM   5509  H  HD1  . TYR   A 1 361 ? 24.900 10.416  -0.983 1.00 21.62 ? 361  TYR   A HD1  1 
ATOM   5510  H  HD2  . TYR   A 1 361 ? 21.983 9.368   1.551  1.00 19.49 ? 361  TYR   A HD2  1 
ATOM   5511  H  HE1  . TYR   A 1 361 ? 23.326 11.269  -2.444 1.00 23.28 ? 361  TYR   A HE1  1 
ATOM   5512  H  HE2  . TYR   A 1 361 ? 20.412 10.225  0.099  1.00 21.44 ? 361  TYR   A HE2  1 
ATOM   5513  H  HH   . TYR   A 1 361 ? 20.013 11.089  -1.940 1.00 27.38 ? 361  TYR   A HH   1 
ATOM   5514  N  N    . ILE   A 1 362 ? 26.140 7.022   3.162  1.00 18.03 ? 362  ILE   A N    1 
ATOM   5515  C  CA   . ILE   A 1 362 ? 27.262 6.553   3.967  1.00 18.87 ? 362  ILE   A CA   1 
ATOM   5516  C  C    . ILE   A 1 362 ? 27.194 5.033   4.032  1.00 18.11 ? 362  ILE   A C    1 
ATOM   5517  O  O    . ILE   A 1 362 ? 26.161 4.467   4.414  1.00 19.54 ? 362  ILE   A O    1 
ATOM   5518  C  CB   . ILE   A 1 362 ? 27.230 7.168   5.377  1.00 16.62 ? 362  ILE   A CB   1 
ATOM   5519  C  CG1  . ILE   A 1 362 ? 27.290 8.694   5.297  1.00 16.36 ? 362  ILE   A CG1  1 
ATOM   5520  C  CG2  . ILE   A 1 362 ? 28.377 6.623   6.232  1.00 17.30 ? 362  ILE   A CG2  1 
ATOM   5521  C  CD1  . ILE   A 1 362 ? 26.897 9.379   6.586  1.00 17.31 ? 362  ILE   A CD1  1 
ATOM   5522  H  H    . ILE   A 1 362 ? 25.392 7.042   3.587  1.00 21.64 ? 362  ILE   A H    1 
ATOM   5523  H  HA   . ILE   A 1 362 ? 28.098 6.830   3.560  1.00 22.65 ? 362  ILE   A HA   1 
ATOM   5524  H  HB   . ILE   A 1 362 ? 26.394 6.918   5.801  1.00 19.94 ? 362  ILE   A HB   1 
ATOM   5525  H  HG12 . ILE   A 1 362 ? 28.190 8.963   5.057  1.00 19.64 ? 362  ILE   A HG12 1 
ATOM   5526  H  HG13 . ILE   A 1 362 ? 26.704 8.997   4.586  1.00 19.64 ? 362  ILE   A HG13 1 
ATOM   5527  H  HG21 . ILE   A 1 362 ? 28.340 7.022   7.115  1.00 20.76 ? 362  ILE   A HG21 1 
ATOM   5528  H  HG22 . ILE   A 1 362 ? 28.294 5.660   6.309  1.00 20.76 ? 362  ILE   A HG22 1 
ATOM   5529  H  HG23 . ILE   A 1 362 ? 29.225 6.842   5.814  1.00 20.76 ? 362  ILE   A HG23 1 
ATOM   5530  H  HD11 . ILE   A 1 362 ? 26.955 10.341  6.472  1.00 20.77 ? 362  ILE   A HD11 1 
ATOM   5531  H  HD12 . ILE   A 1 362 ? 25.987 9.135   6.818  1.00 20.77 ? 362  ILE   A HD12 1 
ATOM   5532  H  HD13 . ILE   A 1 362 ? 27.496 9.101   7.296  1.00 20.77 ? 362  ILE   A HD13 1 
ATOM   5533  N  N    . LYS   A 1 363 ? 28.283 4.371   3.656  1.00 17.92 ? 363  LYS   A N    1 
ATOM   5534  C  CA   . LYS   A 1 363 ? 28.332 2.915   3.642  1.00 15.70 ? 363  LYS   A CA   1 
ATOM   5535  C  C    . LYS   A 1 363 ? 28.897 2.386   4.961  1.00 17.17 ? 363  LYS   A C    1 
ATOM   5536  O  O    . LYS   A 1 363 ? 29.607 3.088   5.685  1.00 19.12 ? 363  LYS   A O    1 
ATOM   5537  C  CB   . LYS   A 1 363 ? 29.174 2.417   2.465  1.00 19.76 ? 363  LYS   A CB   1 
ATOM   5538  C  CG   . LYS   A 1 363 ? 28.800 3.021   1.111  1.00 24.34 ? 363  LYS   A CG   1 
ATOM   5539  C  CD   . LYS   A 1 363 ? 27.349 2.755   0.761  1.00 24.40 ? 363  LYS   A CD   1 
ATOM   5540  C  CE   . LYS   A 1 363 ? 27.048 3.129   -0.682 1.00 30.56 ? 363  LYS   A CE   1 
ATOM   5541  N  NZ   . LYS   A 1 363 ? 25.678 2.707   -1.094 1.00 33.62 ? 363  LYS   A NZ   1 
ATOM   5542  H  H    . LYS   A 1 363 ? 29.011 4.752   3.403  1.00 21.51 ? 363  LYS   A H    1 
ATOM   5543  H  HA   . LYS   A 1 363 ? 27.428 2.580   3.537  1.00 18.85 ? 363  LYS   A HA   1 
ATOM   5544  H  HB2  . LYS   A 1 363 ? 30.107 2.611   2.645  1.00 23.71 ? 363  LYS   A HB2  1 
ATOM   5545  H  HB3  . LYS   A 1 363 ? 29.091 1.452   2.409  1.00 23.71 ? 363  LYS   A HB3  1 
ATOM   5546  H  HG2  . LYS   A 1 363 ? 28.959 3.978   1.128  1.00 29.21 ? 363  LYS   A HG2  1 
ATOM   5547  H  HG3  . LYS   A 1 363 ? 29.373 2.650   0.422  1.00 29.21 ? 363  LYS   A HG3  1 
ATOM   5548  H  HD2  . LYS   A 1 363 ? 27.147 1.817   0.902  1.00 29.28 ? 363  LYS   A HD2  1 
ATOM   5549  H  HD3  . LYS   A 1 363 ? 26.773 3.262   1.355  1.00 29.28 ? 363  LYS   A HD3  1 
ATOM   5550  H  HE2  . LYS   A 1 363 ? 27.137 4.089   -0.792 1.00 36.68 ? 363  LYS   A HE2  1 
ATOM   5551  H  HE3  . LYS   A 1 363 ? 27.703 2.715   -1.266 1.00 36.68 ? 363  LYS   A HE3  1 
ATOM   5552  H  HZ1  . LYS   A 1 363 ? 25.732 2.176   -1.807 1.00 40.35 ? 363  LYS   A HZ1  1 
ATOM   5553  H  HZ2  . LYS   A 1 363 ? 25.289 2.267   -0.425 1.00 40.35 ? 363  LYS   A HZ2  1 
ATOM   5554  H  HZ3  . LYS   A 1 363 ? 25.194 3.426   -1.296 1.00 40.35 ? 363  LYS   A HZ3  1 
ATOM   5555  N  N    . ASP   A 1 364 ? 28.606 1.120   5.253  1.00 19.59 ? 364  ASP   A N    1 
ATOM   5556  C  CA   . ASP   A 1 364 ? 29.107 0.494   6.504  1.00 20.62 ? 364  ASP   A CA   1 
ATOM   5557  C  C    . ASP   A 1 364 ? 30.635 0.580   6.569  1.00 20.77 ? 364  ASP   A C    1 
ATOM   5558  O  O    . ASP   A 1 364 ? 31.164 0.783   7.672  1.00 19.52 ? 364  ASP   A O    1 
ATOM   5559  C  CB   . ASP   A 1 364 ? 28.680 -0.973  6.575  1.00 21.16 ? 364  ASP   A CB   1 
ATOM   5560  C  CG   . ASP   A 1 364 ? 27.191 -1.152  6.806  1.00 24.14 ? 364  ASP   A CG   1 
ATOM   5561  O  OD1  . ASP   A 1 364 ? 26.604 -0.300  7.493  1.00 21.78 ? 364  ASP   A OD1  1 
ATOM   5562  O  OD2  . ASP   A 1 364 ? 26.637 -2.143  6.298  1.00 26.50 ? 364  ASP   A OD2  1 
ATOM   5563  H  H    . ASP   A 1 364 ? 28.129 0.604   4.757  1.00 23.51 ? 364  ASP   A H    1 
ATOM   5564  H  HA   . ASP   A 1 364 ? 28.727 0.975   7.256  1.00 24.75 ? 364  ASP   A HA   1 
ATOM   5565  H  HB2  . ASP   A 1 364 ? 28.929 -1.416  5.749  1.00 25.39 ? 364  ASP   A HB2  1 
ATOM   5566  H  HB3  . ASP   A 1 364 ? 29.167 -1.411  7.290  1.00 25.39 ? 364  ASP   A HB3  1 
ATOM   5567  N  N    . GLU   A 1 365 ? 31.312 0.420   5.429  1.00 21.82 ? 365  GLU   A N    1 
ATOM   5568  C  CA   . GLU   A 1 365 ? 32.801 0.387   5.409  1.00 24.63 ? 365  GLU   A CA   1 
ATOM   5569  C  C    . GLU   A 1 365 ? 33.380 1.708   5.925  1.00 19.32 ? 365  GLU   A C    1 
ATOM   5570  O  O    . GLU   A 1 365 ? 34.457 1.671   6.545  1.00 21.04 ? 365  GLU   A O    1 
ATOM   5571  C  CB   . GLU   A 1 365 ? 33.287 0.109   3.986  1.00 32.38 ? 365  GLU   A CB   1 
ATOM   5572  C  CG   . GLU   A 1 365 ? 34.697 -0.444  3.913  1.00 44.10 ? 365  GLU   A CG   1 
ATOM   5573  C  CD   . GLU   A 1 365 ? 35.037 -1.097  2.585  1.00 55.49 ? 365  GLU   A CD   1 
ATOM   5574  O  OE1  . GLU   A 1 365 ? 34.388 -2.106  2.242  1.00 63.29 ? 365  GLU   A OE1  1 
ATOM   5575  O  OE2  . GLU   A 1 365 ? 35.946 -0.594  1.894  1.00 53.31 ? 365  GLU   A OE2  1 
ATOM   5576  H  H    . GLU   A 1 365 ? 30.942 0.329   4.658  1.00 26.19 ? 365  GLU   A H    1 
ATOM   5577  H  HA   . GLU   A 1 365 ? 33.108 -0.323  5.995  1.00 29.57 ? 365  GLU   A HA   1 
ATOM   5578  H  HB2  . GLU   A 1 365 ? 32.681 -0.520  3.564  1.00 38.86 ? 365  GLU   A HB2  1 
ATOM   5579  H  HB3  . GLU   A 1 365 ? 33.245 0.931   3.473  1.00 38.86 ? 365  GLU   A HB3  1 
ATOM   5580  H  HG2  . GLU   A 1 365 ? 35.326 0.276   4.079  1.00 52.92 ? 365  GLU   A HG2  1 
ATOM   5581  H  HG3  . GLU   A 1 365 ? 34.816 -1.094  4.623  1.00 52.92 ? 365  GLU   A HG3  1 
ATOM   5582  N  N    . GLU   A 1 366 ? 32.693 2.824   5.677  1.00 19.32 ? 366  GLU   A N    1 
ATOM   5583  C  CA   . GLU   A 1 366 ? 33.231 4.158   6.064  1.00 19.88 ? 366  GLU   A CA   1 
ATOM   5584  C  C    . GLU   A 1 366 ? 33.225 4.317   7.590  1.00 21.48 ? 366  GLU   A C    1 
ATOM   5585  O  O    . GLU   A 1 366 ? 34.071 5.066   8.095  1.00 18.14 ? 366  GLU   A O    1 
ATOM   5586  C  CB   . GLU   A 1 366 ? 32.436 5.270   5.368  1.00 18.74 ? 366  GLU   A CB   1 
ATOM   5587  C  CG   . GLU   A 1 366 ? 32.861 6.664   5.787  1.00 21.97 ? 366  GLU   A CG   1 
ATOM   5588  C  CD   . GLU   A 1 366 ? 32.827 7.706   4.683  1.00 28.54 ? 366  GLU   A CD   1 
ATOM   5589  O  OE1  . GLU   A 1 366 ? 31.996 7.568   3.766  1.00 20.06 ? 366  GLU   A OE1  1 
ATOM   5590  O  OE2  . GLU   A 1 366 ? 33.630 8.654   4.747  1.00 28.94 ? 366  GLU   A OE2  1 
ATOM   5591  H  H    . GLU   A 1 366 ? 31.924 2.844   5.292  1.00 23.18 ? 366  GLU   A H    1 
ATOM   5592  H  HA   . GLU   A 1 366 ? 34.153 4.228   5.771  1.00 23.86 ? 366  GLU   A HA   1 
ATOM   5593  H  HB2  . GLU   A 1 366 ? 32.541 5.182   4.408  1.00 22.49 ? 366  GLU   A HB2  1 
ATOM   5594  H  HB3  . GLU   A 1 366 ? 31.493 5.154   5.562  1.00 22.49 ? 366  GLU   A HB3  1 
ATOM   5595  H  HG2  . GLU   A 1 366 ? 32.285 6.959   6.509  1.00 26.37 ? 366  GLU   A HG2  1 
ATOM   5596  H  HG3  . GLU   A 1 366 ? 33.762 6.619   6.143  1.00 26.37 ? 366  GLU   A HG3  1 
ATOM   5597  N  N    . ILE   A 1 367 ? 32.320 3.630   8.298  1.00 16.99 ? 367  ILE   A N    1 
ATOM   5598  C  CA   . ILE   A 1 367 ? 32.216 3.826   9.777  1.00 17.21 ? 367  ILE   A CA   1 
ATOM   5599  C  C    . ILE   A 1 367 ? 32.675 2.574   10.541 1.00 19.73 ? 367  ILE   A C    1 
ATOM   5600  O  O    . ILE   A 1 367 ? 32.633 2.603   11.779 1.00 22.72 ? 367  ILE   A O    1 
ATOM   5601  C  CB   . ILE   A 1 367 ? 30.785 4.238   10.178 1.00 18.72 ? 367  ILE   A CB   1 
ATOM   5602  C  CG1  . ILE   A 1 367 ? 29.737 3.271   9.620  1.00 18.38 ? 367  ILE   A CG1  1 
ATOM   5603  C  CG2  . ILE   A 1 367 ? 30.504 5.674   9.765  1.00 17.17 ? 367  ILE   A CG2  1 
ATOM   5604  C  CD1  . ILE   A 1 367 ? 28.356 3.464   10.203 1.00 17.26 ? 367  ILE   A CD1  1 
ATOM   5605  H  H    . ILE   A 1 367 ? 31.768 3.061   7.966  1.00 20.40 ? 367  ILE   A H    1 
ATOM   5606  H  HA   . ILE   A 1 367 ? 32.813 4.550   10.024 1.00 20.65 ? 367  ILE   A HA   1 
ATOM   5607  H  HB   . ILE   A 1 367 ? 30.722 4.189   11.145 1.00 22.47 ? 367  ILE   A HB   1 
ATOM   5608  H  HG12 . ILE   A 1 367 ? 29.690 3.379   8.657  1.00 22.06 ? 367  ILE   A HG12 1 
ATOM   5609  H  HG13 . ILE   A 1 367 ? 30.026 2.361   9.790  1.00 22.06 ? 367  ILE   A HG13 1 
ATOM   5610  H  HG21 . ILE   A 1 367 ? 29.601 5.915   10.025 1.00 20.61 ? 367  ILE   A HG21 1 
ATOM   5611  H  HG22 . ILE   A 1 367 ? 31.135 6.266   10.203 1.00 20.61 ? 367  ILE   A HG22 1 
ATOM   5612  H  HG23 . ILE   A 1 367 ? 30.596 5.758   8.803  1.00 20.61 ? 367  ILE   A HG23 1 
ATOM   5613  H  HD11 . ILE   A 1 367 ? 27.745 2.822   9.808  1.00 20.71 ? 367  ILE   A HD11 1 
ATOM   5614  H  HD12 . ILE   A 1 367 ? 28.388 3.330   11.163 1.00 20.71 ? 367  ILE   A HD12 1 
ATOM   5615  H  HD13 . ILE   A 1 367 ? 28.047 4.364   10.013 1.00 20.71 ? 367  ILE   A HD13 1 
ATOM   5616  N  N    . ALA   A 1 368 ? 33.106 1.528   9.834  1.00 18.92 ? 368  ALA   A N    1 
ATOM   5617  C  CA   . ALA   A 1 368 ? 33.495 0.271   10.517 1.00 19.38 ? 368  ALA   A CA   1 
ATOM   5618  C  C    . ALA   A 1 368 ? 34.686 0.521   11.448 1.00 23.38 ? 368  ALA   A C    1 
ATOM   5619  O  O    . ALA   A 1 368 ? 34.683 -0.004  12.569 1.00 21.86 ? 368  ALA   A O    1 
ATOM   5620  C  CB   . ALA   A 1 368 ? 33.795 -0.797  9.496  1.00 22.74 ? 368  ALA   A CB   1 
ATOM   5621  H  H    . ALA   A 1 368 ? 33.183 1.515   8.978  1.00 22.71 ? 368  ALA   A H    1 
ATOM   5622  H  HA   . ALA   A 1 368 ? 32.758 -0.042  11.065 1.00 23.26 ? 368  ALA   A HA   1 
ATOM   5623  H  HB1  . ALA   A 1 368 ? 34.049 -1.616  9.949  1.00 27.29 ? 368  ALA   A HB1  1 
ATOM   5624  H  HB2  . ALA   A 1 368 ? 33.006 -0.958  8.955  1.00 27.29 ? 368  ALA   A HB2  1 
ATOM   5625  H  HB3  . ALA   A 1 368 ? 34.523 -0.505  8.926  1.00 27.29 ? 368  ALA   A HB3  1 
ATOM   5626  N  N    . GLY   A 1 369 ? 35.652 1.317   10.995 1.00 26.48 ? 369  GLY   A N    1 
ATOM   5627  C  CA   . GLY   A 1 369 ? 36.831 1.635   11.822 1.00 25.71 ? 369  GLY   A CA   1 
ATOM   5628  C  C    . GLY   A 1 369 ? 36.467 2.377   13.094 1.00 25.62 ? 369  GLY   A C    1 
ATOM   5629  O  O    . GLY   A 1 369 ? 37.247 2.302   14.055 1.00 25.29 ? 369  GLY   A O    1 
ATOM   5630  H  H    . GLY   A 1 369 ? 35.650 1.684   10.217 1.00 31.78 ? 369  GLY   A H    1 
ATOM   5631  H  HA2  . GLY   A 1 369 ? 37.292 0.813   12.052 1.00 30.85 ? 369  GLY   A HA2  1 
ATOM   5632  H  HA3  . GLY   A 1 369 ? 37.450 2.173   11.304 1.00 30.85 ? 369  GLY   A HA3  1 
ATOM   5633  N  N    . ASP   A 1 370 ? 35.313 3.050   13.103 1.00 20.44 ? 370  ASP   A N    1 
ATOM   5634  C  CA   . ASP   A 1 370 ? 34.865 3.816   14.296 1.00 22.49 ? 370  ASP   A CA   1 
ATOM   5635  C  C    . ASP   A 1 370 ? 34.196 2.878   15.308 1.00 22.08 ? 370  ASP   A C    1 
ATOM   5636  O  O    . ASP   A 1 370 ? 34.083 3.275   16.480 1.00 25.20 ? 370  ASP   A O    1 
ATOM   5637  C  CB   . ASP   A 1 370 ? 33.928 4.960   13.900 1.00 19.46 ? 370  ASP   A CB   1 
ATOM   5638  C  CG   . ASP   A 1 370 ? 34.580 5.989   12.991 1.00 20.32 ? 370  ASP   A CG   1 
ATOM   5639  O  OD1  . ASP   A 1 370 ? 35.323 6.841   13.511 1.00 25.35 ? 370  ASP   A OD1  1 
ATOM   5640  O  OD2  . ASP   A 1 370 ? 34.336 5.930   11.773 1.00 21.65 ? 370  ASP   A OD2  1 
ATOM   5641  H  H    . ASP   A 1 370 ? 34.771 3.082   12.436 1.00 24.53 ? 370  ASP   A H    1 
ATOM   5642  H  HA   . ASP   A 1 370 ? 35.645 4.212   14.715 1.00 27.00 ? 370  ASP   A HA   1 
ATOM   5643  H  HB2  . ASP   A 1 370 ? 33.150 4.591   13.454 1.00 23.35 ? 370  ASP   A HB2  1 
ATOM   5644  H  HB3  . ASP   A 1 370 ? 33.612 5.402   14.703 1.00 23.35 ? 370  ASP   A HB3  1 
ATOM   5645  N  N    . ASN   A 1 371 ? 33.753 1.697   14.865 1.00 22.90 ? 371  ASN   A N    1 
ATOM   5646  C  CA   . ASN   A 1 371 ? 33.056 0.741   15.766 1.00 23.51 ? 371  ASN   A CA   1 
ATOM   5647  C  C    . ASN   A 1 371 ? 31.773 1.386   16.295 1.00 21.48 ? 371  ASN   A C    1 
ATOM   5648  O  O    . ASN   A 1 371 ? 31.385 1.073   17.429 1.00 22.52 ? 371  ASN   A O    1 
ATOM   5649  C  CB   . ASN   A 1 371 ? 33.967 0.263   16.899 1.00 26.82 ? 371  ASN   A CB   1 
ATOM   5650  C  CG   . ASN   A 1 371 ? 35.268 -0.331  16.403 1.00 37.10 ? 371  ASN   A CG   1 
ATOM   5651  O  OD1  . ASN   A 1 371 ? 35.369 -0.742  15.250 1.00 44.56 ? 371  ASN   A OD1  1 
ATOM   5652  N  ND2  . ASN   A 1 371 ? 36.267 -0.383  17.268 1.00 41.74 ? 371  ASN   A ND2  1 
ATOM   5653  H  H    . ASN   A 1 371 ? 33.841 1.423   14.054 1.00 27.48 ? 371  ASN   A H    1 
ATOM   5654  H  HA   . ASN   A 1 371 ? 32.818 -0.052  15.260 1.00 28.22 ? 371  ASN   A HA   1 
ATOM   5655  H  HB2  . ASN   A 1 371 ? 34.162 1.009   17.487 1.00 32.19 ? 371  ASN   A HB2  1 
ATOM   5656  H  HB3  . ASN   A 1 371 ? 33.496 -0.400  17.428 1.00 32.19 ? 371  ASN   A HB3  1 
ATOM   5657  H  HD21 . ASN   A 1 371 ? 37.024 -0.714  17.031 1.00 50.09 ? 371  ASN   A HD21 1 
ATOM   5658  H  HD22 . ASN   A 1 371 ? 36.159 -0.085  18.068 1.00 50.09 ? 371  ASN   A HD22 1 
ATOM   5659  N  N    . LEU   A 1 372 ? 31.157 2.271   15.503 1.00 18.95 ? 372  LEU   A N    1 
ATOM   5660  C  CA   . LEU   A 1 372 ? 29.860 2.886   15.893 1.00 19.56 ? 372  LEU   A CA   1 
ATOM   5661  C  C    . LEU   A 1 372 ? 28.899 2.771   14.706 1.00 19.08 ? 372  LEU   A C    1 
ATOM   5662  O  O    . LEU   A 1 372 ? 29.387 2.713   13.568 1.00 21.07 ? 372  LEU   A O    1 
ATOM   5663  C  CB   . LEU   A 1 372 ? 30.048 4.362   16.264 1.00 20.52 ? 372  LEU   A CB   1 
ATOM   5664  C  CG   . LEU   A 1 372 ? 31.018 4.661   17.404 1.00 18.48 ? 372  LEU   A CG   1 
ATOM   5665  C  CD1  . LEU   A 1 372 ? 31.294 6.155   17.485 1.00 17.17 ? 372  LEU   A CD1  1 
ATOM   5666  C  CD2  . LEU   A 1 372 ? 30.467 4.155   18.727 1.00 19.61 ? 372  LEU   A CD2  1 
ATOM   5667  H  H    . LEU   A 1 372 ? 31.462 2.532   14.743 1.00 22.74 ? 372  LEU   A H    1 
ATOM   5668  H  HA   . LEU   A 1 372 ? 29.502 2.424   16.668 1.00 23.48 ? 372  LEU   A HA   1 
ATOM   5669  H  HB2  . LEU   A 1 372 ? 30.352 4.837   15.475 1.00 24.63 ? 372  LEU   A HB2  1 
ATOM   5670  H  HB3  . LEU   A 1 372 ? 29.181 4.728   16.499 1.00 24.63 ? 372  LEU   A HB3  1 
ATOM   5671  H  HG   . LEU   A 1 372 ? 31.851 4.199   17.224 1.00 22.18 ? 372  LEU   A HG   1 
ATOM   5672  H  HD11 . LEU   A 1 372 ? 31.911 6.331   18.212 1.00 20.60 ? 372  LEU   A HD11 1 
ATOM   5673  H  HD12 . LEU   A 1 372 ? 31.684 6.458   16.650 1.00 20.60 ? 372  LEU   A HD12 1 
ATOM   5674  H  HD13 . LEU   A 1 372 ? 30.463 6.630   17.644 1.00 20.60 ? 372  LEU   A HD13 1 
ATOM   5675  H  HD21 . LEU   A 1 372 ? 31.097 4.354   19.437 1.00 23.53 ? 372  LEU   A HD21 1 
ATOM   5676  H  HD22 . LEU   A 1 372 ? 29.621 4.591   18.914 1.00 23.53 ? 372  LEU   A HD22 1 
ATOM   5677  H  HD23 . LEU   A 1 372 ? 30.331 3.196   18.676 1.00 23.53 ? 372  LEU   A HD23 1 
ATOM   5678  N  N    . SER   A 1 373 ? 27.595 2.752   14.976 1.00 17.92 ? 373  SER   A N    1 
ATOM   5679  C  CA   . SER   A 1 373 ? 26.599 2.731   13.875 1.00 16.99 ? 373  SER   A CA   1 
ATOM   5680  C  C    . SER   A 1 373 ? 26.014 4.121   13.653 1.00 17.37 ? 373  SER   A C    1 
ATOM   5681  O  O    . SER   A 1 373 ? 26.297 5.026   14.452 1.00 14.18 ? 373  SER   A O    1 
ATOM   5682  C  CB   . SER   A 1 373 ? 25.445 1.793   14.142 1.00 18.32 ? 373  SER   A CB   1 
ATOM   5683  O  OG   . SER   A 1 373 ? 24.367 2.474   14.765 1.00 15.74 ? 373  SER   A OG   1 
ATOM   5684  H  H    . SER   A 1 373 ? 27.261 2.751   15.768 1.00 21.51 ? 373  SER   A H    1 
ATOM   5685  H  HA   . SER   A 1 373 ? 27.082 2.422   13.093 1.00 20.39 ? 373  SER   A HA   1 
ATOM   5686  H  HB2  . SER   A 1 373 ? 25.144 1.400   13.308 1.00 21.99 ? 373  SER   A HB2  1 
ATOM   5687  H  HB3  . SER   A 1 373 ? 25.742 1.064   14.709 1.00 21.99 ? 373  SER   A HB3  1 
ATOM   5688  H  HG   . SER   A 1 373 ? 24.414 2.372   15.597 1.00 18.89 ? 373  SER   A HG   1 
ATOM   5689  N  N    . LEU   A 1 374 ? 25.213 4.244   12.602 1.00 16.23 ? 374  LEU   A N    1 
ATOM   5690  C  CA   . LEU   A 1 374 ? 24.470 5.502   12.362 1.00 12.89 ? 374  LEU   A CA   1 
ATOM   5691  C  C    . LEU   A 1 374 ? 22.999 5.085   12.243 1.00 15.73 ? 374  LEU   A C    1 
ATOM   5692  O  O    . LEU   A 1 374 ? 22.291 5.657   11.401 1.00 14.43 ? 374  LEU   A O    1 
ATOM   5693  C  CB   . LEU   A 1 374 ? 25.002 6.172   11.091 1.00 15.87 ? 374  LEU   A CB   1 
ATOM   5694  C  CG   . LEU   A 1 374 ? 26.233 7.056   11.287 1.00 16.03 ? 374  LEU   A CG   1 
ATOM   5695  C  CD1  . LEU   A 1 374 ? 26.778 7.533   9.950  1.00 17.30 ? 374  LEU   A CD1  1 
ATOM   5696  C  CD2  . LEU   A 1 374 ? 25.910 8.238   12.186 1.00 14.59 ? 374  LEU   A CD2  1 
ATOM   5697  H  H    . LEU   A 1 374 ? 25.079 3.628   12.017 1.00 19.48 ? 374  LEU   A H    1 
ATOM   5698  H  HA   . LEU   A 1 374 ? 24.575 6.154   13.072 1.00 15.47 ? 374  LEU   A HA   1 
ATOM   5699  H  HB2  . LEU   A 1 374 ? 25.217 5.482   10.445 1.00 19.04 ? 374  LEU   A HB2  1 
ATOM   5700  H  HB3  . LEU   A 1 374 ? 24.293 6.710   10.706 1.00 19.04 ? 374  LEU   A HB3  1 
ATOM   5701  H  HG   . LEU   A 1 374 ? 26.918 6.523   11.719 1.00 19.23 ? 374  LEU   A HG   1 
ATOM   5702  H  HD11 . LEU   A 1 374 ? 27.557 8.091   10.099 1.00 20.77 ? 374  LEU   A HD11 1 
ATOM   5703  H  HD12 . LEU   A 1 374 ? 27.028 6.767   9.410  1.00 20.77 ? 374  LEU   A HD12 1 
ATOM   5704  H  HD13 . LEU   A 1 374 ? 26.097 8.046   9.487  1.00 20.77 ? 374  LEU   A HD13 1 
ATOM   5705  H  HD21 . LEU   A 1 374 ? 26.703 8.786   12.298 1.00 17.52 ? 374  LEU   A HD21 1 
ATOM   5706  H  HD22 . LEU   A 1 374 ? 25.205 8.768   11.783 1.00 17.52 ? 374  LEU   A HD22 1 
ATOM   5707  H  HD23 . LEU   A 1 374 ? 25.616 7.915   13.052 1.00 17.52 ? 374  LEU   A HD23 1 
ATOM   5708  N  N    . LYS   A 1 375 ? 22.582 4.098   13.052 1.00 13.64 ? 375  LYS   A N    1 
ATOM   5709  C  CA   . LYS   A 1 375 ? 21.181 3.615   13.014 1.00 15.70 ? 375  LYS   A CA   1 
ATOM   5710  C  C    . LYS   A 1 375 ? 20.332 4.430   13.987 1.00 15.53 ? 375  LYS   A C    1 
ATOM   5711  O  O    . LYS   A 1 375 ? 20.763 4.624   15.131 1.00 16.49 ? 375  LYS   A O    1 
ATOM   5712  C  CB   . LYS   A 1 375 ? 21.119 2.122   13.354 1.00 16.69 ? 375  LYS   A CB   1 
ATOM   5713  C  CG   . LYS   A 1 375 ? 21.831 1.209   12.366 1.00 19.61 ? 375  LYS   A CG   1 
ATOM   5714  C  CD   . LYS   A 1 375 ? 22.239 -0.118  12.963 1.00 28.40 ? 375  LYS   A CD   1 
ATOM   5715  C  CE   . LYS   A 1 375 ? 23.027 -0.978  11.999 1.00 36.80 ? 375  LYS   A CE   1 
ATOM   5716  N  NZ   . LYS   A 1 375 ? 22.516 -0.858  10.614 1.00 38.53 ? 375  LYS   A NZ   1 
ATOM   5717  H  H    . LYS   A 1 375 ? 23.084 3.697   13.624 1.00 16.38 ? 375  LYS   A H    1 
ATOM   5718  H  HA   . LYS   A 1 375 ? 20.828 3.731   12.118 1.00 18.84 ? 375  LYS   A HA   1 
ATOM   5719  H  HB2  . LYS   A 1 375 ? 21.505 1.988   14.234 1.00 20.03 ? 375  LYS   A HB2  1 
ATOM   5720  H  HB3  . LYS   A 1 375 ? 20.188 1.855   13.408 1.00 20.03 ? 375  LYS   A HB3  1 
ATOM   5721  H  HG2  . LYS   A 1 375 ? 21.249 1.049   11.606 1.00 23.54 ? 375  LYS   A HG2  1 
ATOM   5722  H  HG3  . LYS   A 1 375 ? 22.620 1.661   12.029 1.00 23.54 ? 375  LYS   A HG3  1 
ATOM   5723  H  HD2  . LYS   A 1 375 ? 22.771 0.040   13.758 1.00 34.08 ? 375  LYS   A HD2  1 
ATOM   5724  H  HD3  . LYS   A 1 375 ? 21.445 -0.599  13.244 1.00 34.08 ? 375  LYS   A HD3  1 
ATOM   5725  H  HE2  . LYS   A 1 375 ? 23.961 -0.719  12.023 1.00 44.16 ? 375  LYS   A HE2  1 
ATOM   5726  H  HE3  . LYS   A 1 375 ? 22.983 -1.905  12.281 1.00 44.16 ? 375  LYS   A HE3  1 
ATOM   5727  H  HZ1  . LYS   A 1 375 ? 22.796 -1.553  10.133 1.00 46.24 ? 375  LYS   A HZ1  1 
ATOM   5728  H  HZ2  . LYS   A 1 375 ? 21.626 -0.845  10.626 1.00 46.24 ? 375  LYS   A HZ2  1 
ATOM   5729  H  HZ3  . LYS   A 1 375 ? 22.819 -0.104  10.250 1.00 46.24 ? 375  LYS   A HZ3  1 
ATOM   5730  N  N    . TRP   A 1 376 ? 19.168 4.885   13.525 1.00 17.18 ? 376  TRP   A N    1 
ATOM   5731  C  CA   . TRP   A 1 376 ? 18.239 5.603   14.428 1.00 17.24 ? 376  TRP   A CA   1 
ATOM   5732  C  C    . TRP   A 1 376 ? 18.076 4.811   15.726 1.00 15.35 ? 376  TRP   A C    1 
ATOM   5733  O  O    . TRP   A 1 376 ? 17.955 3.580   15.646 1.00 15.98 ? 376  TRP   A O    1 
ATOM   5734  C  CB   . TRP   A 1 376 ? 16.876 5.811   13.758 1.00 16.78 ? 376  TRP   A CB   1 
ATOM   5735  C  CG   . TRP   A 1 376 ? 16.911 6.499   12.429 1.00 16.03 ? 376  TRP   A CG   1 
ATOM   5736  C  CD1  . TRP   A 1 376 ? 16.672 5.939   11.207 1.00 17.08 ? 376  TRP   A CD1  1 
ATOM   5737  C  CD2  . TRP   A 1 376 ? 17.169 7.893   12.186 1.00 13.83 ? 376  TRP   A CD2  1 
ATOM   5738  N  NE1  . TRP   A 1 376 ? 16.778 6.882   10.222 1.00 14.55 ? 376  TRP   A NE1  1 
ATOM   5739  C  CE2  . TRP   A 1 376 ? 17.081 8.091   10.792 1.00 15.62 ? 376  TRP   A CE2  1 
ATOM   5740  C  CE3  . TRP   A 1 376 ? 17.470 8.987   13.003 1.00 13.43 ? 376  TRP   A CE3  1 
ATOM   5741  C  CZ2  . TRP   A 1 376 ? 17.286 9.338   10.204 1.00 11.59 ? 376  TRP   A CZ2  1 
ATOM   5742  C  CZ3  . TRP   A 1 376 ? 17.675 10.217  12.421 1.00 12.85 ? 376  TRP   A CZ3  1 
ATOM   5743  C  CH2  . TRP   A 1 376 ? 17.581 10.388  11.041 1.00 14.02 ? 376  TRP   A CH2  1 
ATOM   5744  H  H    . TRP   A 1 376 ? 18.894 4.796   12.715 1.00 20.62 ? 376  TRP   A H    1 
ATOM   5745  H  HA   . TRP   A 1 376 ? 18.610 6.477   14.627 1.00 20.70 ? 376  TRP   A HA   1 
ATOM   5746  H  HB2  . TRP   A 1 376 ? 16.453 4.946   13.646 1.00 20.13 ? 376  TRP   A HB2  1 
ATOM   5747  H  HB3  . TRP   A 1 376 ? 16.314 6.326   14.357 1.00 20.13 ? 376  TRP   A HB3  1 
ATOM   5748  H  HD1  . TRP   A 1 376 ? 16.466 5.043   11.065 1.00 20.49 ? 376  TRP   A HD1  1 
ATOM   5749  H  HE1  . TRP   A 1 376 ? 16.672 6.739   9.381  1.00 17.46 ? 376  TRP   A HE1  1 
ATOM   5750  H  HE3  . TRP   A 1 376 ? 17.531 8.885   13.925 1.00 16.12 ? 376  TRP   A HE3  1 
ATOM   5751  H  HZ2  . TRP   A 1 376 ? 17.226 9.455   9.283  1.00 13.91 ? 376  TRP   A HZ2  1 
ATOM   5752  H  HZ3  . TRP   A 1 376 ? 17.880 10.948  12.958 1.00 15.42 ? 376  TRP   A HZ3  1 
ATOM   5753  H  HH2  . TRP   A 1 376 ? 17.721 11.233  10.678 1.00 16.83 ? 376  TRP   A HH2  1 
ATOM   5754  N  N    . GLY   A 1 377 ? 18.076 5.495   16.869 1.00 12.72 ? 377  GLY   A N    1 
ATOM   5755  C  CA   . GLY   A 1 377 ? 17.813 4.814   18.150 1.00 17.97 ? 377  GLY   A CA   1 
ATOM   5756  C  C    . GLY   A 1 377 ? 19.031 4.141   18.758 1.00 18.26 ? 377  GLY   A C    1 
ATOM   5757  O  O    . GLY   A 1 377 ? 18.916 3.680   19.897 1.00 17.46 ? 377  GLY   A O    1 
ATOM   5758  H  H    . GLY   A 1 377 ? 18.223 6.340   16.931 1.00 15.27 ? 377  GLY   A H    1 
ATOM   5759  H  HA2  . GLY   A 1 377 ? 17.464 5.461   18.783 1.00 21.57 ? 377  GLY   A HA2  1 
ATOM   5760  H  HA3  . GLY   A 1 377 ? 17.121 4.147   18.015 1.00 21.57 ? 377  GLY   A HA3  1 
ATOM   5761  N  N    . ASP   A 1 378 ? 20.146 4.073   18.028 1.00 15.62 ? 378  ASP   A N    1 
ATOM   5762  C  CA   . ASP   A 1 378 ? 21.396 3.511   18.609 1.00 17.44 ? 378  ASP   A CA   1 
ATOM   5763  C  C    . ASP   A 1 378 ? 21.999 4.564   19.544 1.00 16.49 ? 378  ASP   A C    1 
ATOM   5764  O  O    . ASP   A 1 378 ? 22.946 5.248   19.138 1.00 14.93 ? 378  ASP   A O    1 
ATOM   5765  C  CB   . ASP   A 1 378 ? 22.367 3.009   17.538 1.00 18.77 ? 378  ASP   A CB   1 
ATOM   5766  C  CG   . ASP   A 1 378 ? 23.550 2.244   18.111 1.00 19.30 ? 378  ASP   A CG   1 
ATOM   5767  O  OD1  . ASP   A 1 378 ? 23.654 2.163   19.348 1.00 16.99 ? 378  ASP   A OD1  1 
ATOM   5768  O  OD2  . ASP   A 1 378 ? 24.356 1.737   17.313 1.00 17.68 ? 378  ASP   A OD2  1 
ATOM   5769  H  H    . ASP   A 1 378 ? 20.212 4.337   17.212 1.00 18.75 ? 378  ASP   A H    1 
ATOM   5770  H  HA   . ASP   A 1 378 ? 21.193 2.716   19.127 1.00 20.93 ? 378  ASP   A HA   1 
ATOM   5771  H  HB2  . ASP   A 1 378 ? 21.888 2.436   16.919 1.00 22.52 ? 378  ASP   A HB2  1 
ATOM   5772  H  HB3  . ASP   A 1 378 ? 22.695 3.766   17.028 1.00 22.52 ? 378  ASP   A HB3  1 
ATOM   5773  N  N    . THR   A 1 379 ? 21.464 4.648   20.756 1.00 17.69 ? 379  THR   A N    1 
ATOM   5774  C  CA   . THR   A 1 379 ? 21.913 5.674   21.731 1.00 18.80 ? 379  THR   A CA   1 
ATOM   5775  C  C    . THR   A 1 379 ? 23.424 5.589   21.973 1.00 15.85 ? 379  THR   A C    1 
ATOM   5776  O  O    . THR   A 1 379 ? 24.074 6.650   22.001 1.00 17.93 ? 379  THR   A O    1 
ATOM   5777  C  CB   . THR   A 1 379 ? 21.122 5.513   23.035 1.00 20.01 ? 379  THR   A CB   1 
ATOM   5778  O  OG1  . THR   A 1 379 ? 19.757 5.272   22.693 1.00 16.07 ? 379  THR   A OG1  1 
ATOM   5779  C  CG2  . THR   A 1 379 ? 21.223 6.726   23.930 1.00 20.02 ? 379  THR   A CG2  1 
ATOM   5780  H  H    . THR   A 1 379 ? 20.842 4.129   21.045 1.00 21.24 ? 379  THR   A H    1 
ATOM   5781  H  HA   . THR   A 1 379 ? 21.739 6.556   21.367 1.00 22.56 ? 379  THR   A HA   1 
ATOM   5782  H  HB   . THR   A 1 379 ? 21.497 4.771   23.535 1.00 24.01 ? 379  THR   A HB   1 
ATOM   5783  H  HG1  . THR   A 1 379 ? 19.355 6.005   22.609 1.00 19.29 ? 379  THR   A HG1  1 
ATOM   5784  H  HG21 . THR   A 1 379 ? 20.708 6.576   24.738 1.00 24.02 ? 379  THR   A HG21 1 
ATOM   5785  H  HG22 . THR   A 1 379 ? 22.152 6.880   24.163 1.00 24.02 ? 379  THR   A HG22 1 
ATOM   5786  H  HG23 . THR   A 1 379 ? 20.874 7.502   23.464 1.00 24.02 ? 379  THR   A HG23 1 
ATOM   5787  N  N    . GLU   A 1 380 ? 23.956 4.382   22.165 1.00 17.11 ? 380  GLU   A N    1 
ATOM   5788  C  CA   . GLU   A 1 380 ? 25.397 4.248   22.506 1.00 20.43 ? 380  GLU   A CA   1 
ATOM   5789  C  C    . GLU   A 1 380 ? 26.261 4.817   21.378 1.00 17.68 ? 380  GLU   A C    1 
ATOM   5790  O  O    . GLU   A 1 380 ? 27.263 5.476   21.681 1.00 17.78 ? 380  GLU   A O    1 
ATOM   5791  C  CB   . GLU   A 1 380 ? 25.764 2.784   22.742 1.00 24.25 ? 380  GLU   A CB   1 
ATOM   5792  C  CG   . GLU   A 1 380 ? 27.072 2.594   23.477 1.00 30.63 ? 380  GLU   A CG   1 
ATOM   5793  C  CD   . GLU   A 1 380 ? 27.312 1.155   23.894 1.00 39.46 ? 380  GLU   A CD   1 
ATOM   5794  O  OE1  . GLU   A 1 380 ? 26.374 0.538   24.438 1.00 41.97 ? 380  GLU   A OE1  1 
ATOM   5795  O  OE2  . GLU   A 1 380 ? 28.427 0.655   23.663 1.00 41.32 ? 380  GLU   A OE2  1 
ATOM   5796  H  H    . GLU   A 1 380 ? 23.524 3.641   22.107 1.00 20.53 ? 380  GLU   A H    1 
ATOM   5797  H  HA   . GLU   A 1 380 ? 25.562 4.747   23.321 1.00 24.52 ? 380  GLU   A HA   1 
ATOM   5798  H  HB2  . GLU   A 1 380 ? 25.054 2.359   23.248 1.00 29.10 ? 380  GLU   A HB2  1 
ATOM   5799  H  HB3  . GLU   A 1 380 ? 25.814 2.330   21.886 1.00 29.10 ? 380  GLU   A HB3  1 
ATOM   5800  H  HG2  . GLU   A 1 380 ? 27.802 2.887   22.910 1.00 36.76 ? 380  GLU   A HG2  1 
ATOM   5801  H  HG3  . GLU   A 1 380 ? 27.080 3.160   24.265 1.00 36.76 ? 380  GLU   A HG3  1 
ATOM   5802  N  N    . SER   A 1 381 ? 25.885 4.545   20.129 1.00 19.06 ? 381  SER   A N    1 
ATOM   5803  C  CA   . SER   A 1 381 ? 26.656 5.068   18.973 1.00 18.63 ? 381  SER   A CA   1 
ATOM   5804  C  C    . SER   A 1 381 ? 26.503 6.593   18.899 1.00 16.23 ? 381  SER   A C    1 
ATOM   5805  O  O    . SER   A 1 381 ? 27.510 7.272   18.648 1.00 16.29 ? 381  SER   A O    1 
ATOM   5806  C  CB   . SER   A 1 381 ? 26.235 4.398   17.689 1.00 18.47 ? 381  SER   A CB   1 
ATOM   5807  O  OG   . SER   A 1 381 ? 26.683 3.054   17.645 1.00 19.76 ? 381  SER   A OG   1 
ATOM   5808  H  H    . SER   A 1 381 ? 25.200 4.069   19.921 1.00 22.88 ? 381  SER   A H    1 
ATOM   5809  H  HA   . SER   A 1 381 ? 27.595 4.862   19.099 1.00 22.36 ? 381  SER   A HA   1 
ATOM   5810  H  HB2  . SER   A 1 381 ? 25.269 4.423   17.609 1.00 22.16 ? 381  SER   A HB2  1 
ATOM   5811  H  HB3  . SER   A 1 381 ? 26.595 4.887   16.932 1.00 22.16 ? 381  SER   A HB3  1 
ATOM   5812  H  HG   . SER   A 1 381 ? 26.026 2.543   17.529 1.00 23.72 ? 381  SER   A HG   1 
ATOM   5813  N  N    . MET   A 1 382 ? 25.285 7.092   19.106 1.00 16.13 ? 382  MET   A N    1 
ATOM   5814  C  CA   . MET   A 1 382 ? 25.031 8.556   19.073 1.00 16.58 ? 382  MET   A CA   1 
ATOM   5815  C  C    . MET   A 1 382 ? 25.978 9.238   20.067 1.00 16.21 ? 382  MET   A C    1 
ATOM   5816  O  O    . MET   A 1 382 ? 26.658 10.196  19.679 1.00 16.47 ? 382  MET   A O    1 
ATOM   5817  C  CB   . MET   A 1 382 ? 23.575 8.847   19.451 1.00 18.05 ? 382  MET   A CB   1 
ATOM   5818  C  CG   . MET   A 1 382 ? 23.229 10.316  19.568 1.00 16.68 ? 382  MET   A CG   1 
ATOM   5819  S  SD   . MET   A 1 382 ? 21.609 10.521  20.355 1.00 14.40 ? 382  MET   A SD   1 
ATOM   5820  C  CE   . MET   A 1 382 ? 22.042 10.227  22.069 1.00 17.77 ? 382  MET   A CE   1 
ATOM   5821  H  H    . MET   A 1 382 ? 24.589 6.613   19.267 1.00 19.36 ? 382  MET   A H    1 
ATOM   5822  H  HA   . MET   A 1 382 ? 25.189 8.897   18.179 1.00 19.90 ? 382  MET   A HA   1 
ATOM   5823  H  HB2  . MET   A 1 382 ? 22.995 8.443   18.786 1.00 21.67 ? 382  MET   A HB2  1 
ATOM   5824  H  HB3  . MET   A 1 382 ? 23.381 8.414   20.297 1.00 21.67 ? 382  MET   A HB3  1 
ATOM   5825  H  HG2  . MET   A 1 382 ? 23.908 10.774  20.088 1.00 20.01 ? 382  MET   A HG2  1 
ATOM   5826  H  HG3  . MET   A 1 382 ? 23.222 10.724  18.688 1.00 20.01 ? 382  MET   A HG3  1 
ATOM   5827  H  HE1  . MET   A 1 382 ? 21.249 10.307  22.622 1.00 21.33 ? 382  MET   A HE1  1 
ATOM   5828  H  HE2  . MET   A 1 382 ? 22.412 9.335   22.161 1.00 21.33 ? 382  MET   A HE2  1 
ATOM   5829  H  HE3  . MET   A 1 382 ? 22.700 10.880  22.353 1.00 21.33 ? 382  MET   A HE3  1 
ATOM   5830  N  N    A ILE   A 1 383 ? 25.988 8.762   21.315 0.40 17.19 ? 383  ILE   A N    1 
ATOM   5831  N  N    B ILE   A 1 383 ? 25.995 8.755   21.311 0.60 17.19 ? 383  ILE   A N    1 
ATOM   5832  C  CA   A ILE   A 1 383 ? 26.872 9.354   22.362 0.40 17.06 ? 383  ILE   A CA   1 
ATOM   5833  C  CA   B ILE   A 1 383 ? 26.872 9.353   22.360 0.60 17.06 ? 383  ILE   A CA   1 
ATOM   5834  C  C    A ILE   A 1 383 ? 28.326 9.242   21.897 0.40 15.30 ? 383  ILE   A C    1 
ATOM   5835  C  C    B ILE   A 1 383 ? 28.327 9.240   21.901 0.60 15.30 ? 383  ILE   A C    1 
ATOM   5836  O  O    A ILE   A 1 383 ? 29.042 10.259  21.953 0.40 17.99 ? 383  ILE   A O    1 
ATOM   5837  O  O    B ILE   A 1 383 ? 29.066 10.233  22.027 0.60 17.99 ? 383  ILE   A O    1 
ATOM   5838  C  CB   A ILE   A 1 383 ? 26.665 8.646   23.715 0.40 18.91 ? 383  ILE   A CB   1 
ATOM   5839  C  CB   B ILE   A 1 383 ? 26.651 8.655   23.716 0.60 18.91 ? 383  ILE   A CB   1 
ATOM   5840  C  CG1  A ILE   A 1 383 ? 25.291 8.950   24.316 0.40 21.85 ? 383  ILE   A CG1  1 
ATOM   5841  C  CG1  B ILE   A 1 383 ? 25.246 8.910   24.265 0.60 21.85 ? 383  ILE   A CG1  1 
ATOM   5842  C  CG2  A ILE   A 1 383 ? 27.790 8.987   24.680 0.40 24.40 ? 383  ILE   A CG2  1 
ATOM   5843  C  CG2  B ILE   A 1 383 ? 27.730 9.057   24.711 0.60 24.40 ? 383  ILE   A CG2  1 
ATOM   5844  C  CD1  A ILE   A 1 383 ? 25.010 8.197   25.595 0.40 26.60 ? 383  ILE   A CD1  1 
ATOM   5845  C  CD1  B ILE   A 1 383 ? 25.010 10.335  24.704 0.60 26.60 ? 383  ILE   A CD1  1 
ATOM   5846  H  H    A ILE   A 1 383 ? 25.502 8.106   21.586 0.40 20.63 ? 383  ILE   A H    1 
ATOM   5847  H  H    B ILE   A 1 383 ? 25.518 8.091   21.578 0.60 20.63 ? 383  ILE   A H    1 
ATOM   5848  H  HA   A ILE   A 1 383 ? 26.647 10.289  22.490 0.40 20.47 ? 383  ILE   A HA   1 
ATOM   5849  H  HA   B ILE   A 1 383 ? 26.650 10.289  22.484 0.60 20.47 ? 383  ILE   A HA   1 
ATOM   5850  H  HB   A ILE   A 1 383 ? 26.691 7.690   23.553 0.40 22.70 ? 383  ILE   A HB   1 
ATOM   5851  H  HB   B ILE   A 1 383 ? 26.722 7.698   23.572 0.60 22.70 ? 383  ILE   A HB   1 
ATOM   5852  H  HG12 A ILE   A 1 383 ? 25.226 9.902   24.489 0.40 26.22 ? 383  ILE   A HG12 1 
ATOM   5853  H  HG12 B ILE   A 1 383 ? 24.595 8.679   23.584 0.60 26.22 ? 383  ILE   A HG12 1 
ATOM   5854  H  HG13 A ILE   A 1 383 ? 24.606 8.733   23.664 0.40 26.22 ? 383  ILE   A HG13 1 
ATOM   5855  H  HG13 B ILE   A 1 383 ? 25.090 8.319   25.018 0.60 26.22 ? 383  ILE   A HG13 1 
ATOM   5856  H  HG21 A ILE   A 1 383 ? 27.642 8.533   25.524 0.40 29.28 ? 383  ILE   A HG21 1 
ATOM   5857  H  HG21 B ILE   A 1 383 ? 27.574 8.608   25.557 0.60 29.29 ? 383  ILE   A HG21 1 
ATOM   5858  H  HG22 A ILE   A 1 383 ? 28.637 8.701   24.304 0.40 29.28 ? 383  ILE   A HG22 1 
ATOM   5859  H  HG22 B ILE   A 1 383 ? 28.600 8.802   24.366 0.60 29.29 ? 383  ILE   A HG22 1 
ATOM   5860  H  HG23 A ILE   A 1 383 ? 27.810 9.945   24.828 0.40 29.28 ? 383  ILE   A HG23 1 
ATOM   5861  H  HG23 B ILE   A 1 383 ? 27.705 10.017  24.846 0.60 29.29 ? 383  ILE   A HG23 1 
ATOM   5862  H  HD11 A ILE   A 1 383 ? 24.128 8.433   25.923 0.40 31.93 ? 383  ILE   A HD11 1 
ATOM   5863  H  HD11 B ILE   A 1 383 ? 24.104 10.425  25.039 0.60 31.93 ? 383  ILE   A HD11 1 
ATOM   5864  H  HD12 A ILE   A 1 383 ? 25.046 7.243   25.424 0.40 31.93 ? 383  ILE   A HD12 1 
ATOM   5865  H  HD12 B ILE   A 1 383 ? 25.638 10.566  25.406 0.60 31.93 ? 383  ILE   A HD12 1 
ATOM   5866  H  HD13 A ILE   A 1 383 ? 25.675 8.431   26.261 0.40 31.93 ? 383  ILE   A HD13 1 
ATOM   5867  H  HD13 B ILE   A 1 383 ? 25.136 10.931  23.949 0.60 31.93 ? 383  ILE   A HD13 1 
ATOM   5868  N  N    . GLY   A 1 384 ? 28.719 8.070   21.392 1.00 15.65 ? 384  GLY   A N    1 
ATOM   5869  C  CA   . GLY   A 1 384 ? 30.100 7.870   20.985 1.00 17.26 ? 384  GLY   A CA   1 
ATOM   5870  C  C    . GLY   A 1 384 ? 30.563 8.805   19.882 1.00 17.04 ? 384  GLY   A C    1 
ATOM   5871  O  O    . GLY   A 1 384 ? 31.758 9.104   19.796 1.00 15.39 ? 384  GLY   A O    1 
ATOM   5872  H  H    A GLY   A 1 384 ? 28.205 7.390   21.280 0.40 18.79 ? 384  GLY   A H    1 
ATOM   5873  H  H    B GLY   A 1 384 ? 28.204 7.391   21.277 0.60 18.79 ? 384  GLY   A H    1 
ATOM   5874  H  HA2  . GLY   A 1 384 ? 30.675 7.987   21.757 1.00 20.72 ? 384  GLY   A HA2  1 
ATOM   5875  H  HA3  . GLY   A 1 384 ? 30.210 6.954   20.686 1.00 20.72 ? 384  GLY   A HA3  1 
ATOM   5876  N  N    . TRP   A 1 385 ? 29.645 9.284   19.041 1.00 12.65 ? 385  TRP   A N    1 
ATOM   5877  C  CA   . TRP   A 1 385 ? 30.063 10.153  17.948 1.00 17.29 ? 385  TRP   A CA   1 
ATOM   5878  C  C    . TRP   A 1 385 ? 30.559 11.503  18.446 1.00 14.04 ? 385  TRP   A C    1 
ATOM   5879  O  O    . TRP   A 1 385 ? 31.370 12.135  17.762 1.00 15.48 ? 385  TRP   A O    1 
ATOM   5880  C  CB   . TRP   A 1 385 ? 28.922 10.334  16.942 1.00 12.74 ? 385  TRP   A CB   1 
ATOM   5881  C  CG   . TRP   A 1 385 ? 28.788 9.143   16.022 1.00 14.95 ? 385  TRP   A CG   1 
ATOM   5882  C  CD1  . TRP   A 1 385 ? 27.699 8.328   15.895 1.00 15.09 ? 385  TRP   A CD1  1 
ATOM   5883  C  CD2  . TRP   A 1 385 ? 29.785 8.621   15.130 1.00 13.52 ? 385  TRP   A CD2  1 
ATOM   5884  N  NE1  . TRP   A 1 385 ? 27.950 7.341   14.969 1.00 14.79 ? 385  TRP   A NE1  1 
ATOM   5885  C  CE2  . TRP   A 1 385 ? 29.224 7.498   14.488 1.00 15.13 ? 385  TRP   A CE2  1 
ATOM   5886  C  CE3  . TRP   A 1 385 ? 31.097 8.996   14.810 1.00 14.97 ? 385  TRP   A CE3  1 
ATOM   5887  C  CZ2  . TRP   A 1 385 ? 29.928 6.743   13.545 1.00 16.71 ? 385  TRP   A CZ2  1 
ATOM   5888  C  CZ3  . TRP   A 1 385 ? 31.797 8.246   13.870 1.00 16.13 ? 385  TRP   A CZ3  1 
ATOM   5889  C  CH2  . TRP   A 1 385 ? 31.211 7.135   13.250 1.00 17.37 ? 385  TRP   A CH2  1 
ATOM   5890  H  H    . TRP   A 1 385 ? 28.801 9.123   19.085 1.00 15.19 ? 385  TRP   A H    1 
ATOM   5891  H  HA   . TRP   A 1 385 ? 30.809 9.721   17.504 1.00 20.75 ? 385  TRP   A HA   1 
ATOM   5892  H  HB2  . TRP   A 1 385 ? 28.089 10.469  17.420 1.00 15.29 ? 385  TRP   A HB2  1 
ATOM   5893  H  HB3  . TRP   A 1 385 ? 29.079 11.133  16.415 1.00 15.29 ? 385  TRP   A HB3  1 
ATOM   5894  H  HD1  . TRP   A 1 385 ? 26.903 8.426   16.366 1.00 18.11 ? 385  TRP   A HD1  1 
ATOM   5895  H  HE1  . TRP   A 1 385 ? 27.398 6.726   14.731 1.00 17.75 ? 385  TRP   A HE1  1 
ATOM   5896  H  HE3  . TRP   A 1 385 ? 31.492 9.732   15.218 1.00 17.97 ? 385  TRP   A HE3  1 
ATOM   5897  H  HZ2  . TRP   A 1 385 ? 29.542 6.004   13.133 1.00 20.06 ? 385  TRP   A HZ2  1 
ATOM   5898  H  HZ3  . TRP   A 1 385 ? 32.668 8.486   13.650 1.00 19.36 ? 385  TRP   A HZ3  1 
ATOM   5899  H  HH2  . TRP   A 1 385 ? 31.702 6.652   12.625 1.00 20.85 ? 385  TRP   A HH2  1 
ATOM   5900  N  N    . ILE   A 1 386 ? 30.104 11.954  19.618 1.00 15.09 ? 386  ILE   A N    1 
ATOM   5901  C  CA   . ILE   A 1 386 ? 30.449 13.296  20.096 1.00 15.18 ? 386  ILE   A CA   1 
ATOM   5902  C  C    . ILE   A 1 386 ? 31.962 13.483  20.194 1.00 14.47 ? 386  ILE   A C    1 
ATOM   5903  O  O    . ILE   A 1 386 ? 32.525 14.430  19.630 1.00 15.47 ? 386  ILE   A O    1 
ATOM   5904  C  CB   . ILE   A 1 386 ? 29.755 13.581  21.441 1.00 15.25 ? 386  ILE   A CB   1 
ATOM   5905  C  CG1  . ILE   A 1 386 ? 28.238 13.453  21.291 1.00 16.26 ? 386  ILE   A CG1  1 
ATOM   5906  C  CG2  . ILE   A 1 386 ? 30.145 14.958  21.970 1.00 18.55 ? 386  ILE   A CG2  1 
ATOM   5907  C  CD1  . ILE   A 1 386 ? 27.474 13.534  22.605 1.00 17.68 ? 386  ILE   A CD1  1 
ATOM   5908  H  H    . ILE   A 1 386 ? 29.598 11.503  20.147 1.00 18.11 ? 386  ILE   A H    1 
ATOM   5909  H  HA   . ILE   A 1 386 ? 30.126 13.941  19.447 1.00 18.22 ? 386  ILE   A HA   1 
ATOM   5910  H  HB   . ILE   A 1 386 ? 30.051 12.923  22.089 1.00 18.31 ? 386  ILE   A HB   1 
ATOM   5911  H  HG12 . ILE   A 1 386 ? 27.921 14.154  20.700 1.00 19.52 ? 386  ILE   A HG12 1 
ATOM   5912  H  HG13 . ILE   A 1 386 ? 28.035 12.607  20.862 1.00 19.52 ? 386  ILE   A HG13 1 
ATOM   5913  H  HG21 . ILE   A 1 386 ? 29.698 15.118  22.816 1.00 22.26 ? 386  ILE   A HG21 1 
ATOM   5914  H  HG22 . ILE   A 1 386 ? 31.106 14.995  22.100 1.00 22.26 ? 386  ILE   A HG22 1 
ATOM   5915  H  HG23 . ILE   A 1 386 ? 29.879 15.638  21.331 1.00 22.26 ? 386  ILE   A HG23 1 
ATOM   5916  H  HD11 . ILE   A 1 386 ? 26.523 13.446  22.433 1.00 21.22 ? 386  ILE   A HD11 1 
ATOM   5917  H  HD12 . ILE   A 1 386 ? 27.764 12.819  23.193 1.00 21.22 ? 386  ILE   A HD12 1 
ATOM   5918  H  HD13 . ILE   A 1 386 ? 27.647 14.389  23.028 1.00 21.22 ? 386  ILE   A HD13 1 
ATOM   5919  N  N    . LYS   A 1 387 ? 32.642 12.588  20.914 1.00 16.95 ? 387  LYS   A N    1 
ATOM   5920  C  CA   . LYS   A 1 387 ? 34.090 12.721  21.060 1.00 14.93 ? 387  LYS   A CA   1 
ATOM   5921  C  C    . LYS   A 1 387 ? 34.795 12.633  19.713 1.00 15.27 ? 387  LYS   A C    1 
ATOM   5922  O  O    . LYS   A 1 387 ? 35.763 13.362  19.461 1.00 16.19 ? 387  LYS   A O    1 
ATOM   5923  C  CB   . LYS   A 1 387 ? 34.628 11.653  22.014 1.00 17.82 ? 387  LYS   A CB   1 
ATOM   5924  C  CG   . LYS   A 1 387 ? 36.156 11.588  22.090 1.00 18.75 ? 387  LYS   A CG   1 
ATOM   5925  C  CD   . LYS   A 1 387 ? 36.620 10.475  23.028 1.00 23.06 ? 387  LYS   A CD   1 
ATOM   5926  C  CE   . LYS   A 1 387 ? 38.121 10.218  22.898 1.00 33.35 ? 387  LYS   A CE   1 
ATOM   5927  N  NZ   . LYS   A 1 387 ? 38.484 9.597   21.588 1.00 32.08 ? 387  LYS   A NZ   1 
ATOM   5928  H  H    . LYS   A 1 387 ? 32.293 11.913  21.316 1.00 20.35 ? 387  LYS   A H    1 
ATOM   5929  H  HA   . LYS   A 1 387 ? 34.272 13.597  21.433 1.00 17.92 ? 387  LYS   A HA   1 
ATOM   5930  H  HB2  . LYS   A 1 387 ? 34.277 11.822  22.903 1.00 21.39 ? 387  LYS   A HB2  1 
ATOM   5931  H  HB3  . LYS   A 1 387 ? 34.291 10.787  21.736 1.00 21.39 ? 387  LYS   A HB3  1 
ATOM   5932  H  HG2  . LYS   A 1 387 ? 36.520 11.439  21.203 1.00 22.51 ? 387  LYS   A HG2  1 
ATOM   5933  H  HG3  . LYS   A 1 387 ? 36.503 12.440  22.399 1.00 22.51 ? 387  LYS   A HG3  1 
ATOM   5934  H  HD2  . LYS   A 1 387 ? 36.410 10.715  23.944 1.00 27.67 ? 387  LYS   A HD2  1 
ATOM   5935  H  HD3  . LYS   A 1 387 ? 36.133 9.660   22.830 1.00 27.67 ? 387  LYS   A HD3  1 
ATOM   5936  H  HE2  . LYS   A 1 387 ? 38.599 11.056  22.999 1.00 40.02 ? 387  LYS   A HE2  1 
ATOM   5937  H  HE3  . LYS   A 1 387 ? 38.410 9.637   23.619 1.00 40.02 ? 387  LYS   A HE3  1 
ATOM   5938  H  HZ1  . LYS   A 1 387 ? 38.985 8.875   21.730 1.00 38.50 ? 387  LYS   A HZ1  1 
ATOM   5939  H  HZ2  . LYS   A 1 387 ? 37.743 9.362   21.155 1.00 38.50 ? 387  LYS   A HZ2  1 
ATOM   5940  H  HZ3  . LYS   A 1 387 ? 38.941 10.183  21.098 1.00 38.50 ? 387  LYS   A HZ3  1 
ATOM   5941  N  N    . ARG   A 1 388 ? 34.315 11.750  18.835 1.00 18.54 ? 388  ARG   A N    1 
ATOM   5942  C  CA   . ARG   A 1 388 ? 35.002 11.542  17.532 1.00 15.70 ? 388  ARG   A CA   1 
ATOM   5943  C  C    . ARG   A 1 388 ? 34.832 12.777  16.640 1.00 13.78 ? 388  ARG   A C    1 
ATOM   5944  O  O    . ARG   A 1 388 ? 35.740 13.052  15.847 1.00 16.33 ? 388  ARG   A O    1 
ATOM   5945  C  CB   . ARG   A 1 388 ? 34.477 10.276  16.848 1.00 20.60 ? 388  ARG   A CB   1 
ATOM   5946  C  CG   . ARG   A 1 388 ? 34.509 9.045   17.743 1.00 23.26 ? 388  ARG   A CG   1 
ATOM   5947  C  CD   . ARG   A 1 388 ? 34.403 7.740   16.978 1.00 25.15 ? 388  ARG   A CD   1 
ATOM   5948  N  NE   . ARG   A 1 388 ? 35.519 7.536   16.069 1.00 25.41 ? 388  ARG   A NE   1 
ATOM   5949  C  CZ   . ARG   A 1 388 ? 36.655 6.931   16.393 1.00 27.28 ? 388  ARG   A CZ   1 
ATOM   5950  N  NH1  . ARG   A 1 388 ? 36.959 6.734   17.663 1.00 29.89 ? 388  ARG   A NH1  1 
ATOM   5951  N  NH2  . ARG   A 1 388 ? 37.485 6.532   15.446 1.00 23.73 ? 388  ARG   A NH2  1 
ATOM   5952  H  H    . ARG   A 1 388 ? 33.613 11.268  18.959 1.00 22.25 ? 388  ARG   A H    1 
ATOM   5953  H  HA   . ARG   A 1 388 ? 35.951 11.419  17.690 1.00 18.85 ? 388  ARG   A HA   1 
ATOM   5954  H  HB2  . ARG   A 1 388 ? 33.565 10.430  16.554 1.00 24.72 ? 388  ARG   A HB2  1 
ATOM   5955  H  HB3  . ARG   A 1 388 ? 35.006 10.103  16.053 1.00 24.72 ? 388  ARG   A HB3  1 
ATOM   5956  H  HG2  . ARG   A 1 388 ? 35.334 9.046   18.254 1.00 27.91 ? 388  ARG   A HG2  1 
ATOM   5957  H  HG3  . ARG   A 1 388 ? 33.780 9.098   18.381 1.00 27.91 ? 388  ARG   A HG3  1 
ATOM   5958  H  HD2  . ARG   A 1 388 ? 34.363 7.002   17.607 1.00 30.18 ? 388  ARG   A HD2  1 
ATOM   5959  H  HD3  . ARG   A 1 388 ? 33.574 7.730   16.475 1.00 30.18 ? 388  ARG   A HD3  1 
ATOM   5960  H  HE   . ARG   A 1 388 ? 35.437 7.828   15.264 1.00 30.50 ? 388  ARG   A HE   1 
ATOM   5961  H  HH11 . ARG   A 1 388 ? 36.421 6.998   18.280 1.00 35.87 ? 388  ARG   A HH11 1 
ATOM   5962  H  HH12 . ARG   A 1 388 ? 37.695 6.342   17.873 1.00 35.87 ? 388  ARG   A HH12 1 
ATOM   5963  H  HH21 . ARG   A 1 388 ? 37.289 6.664   14.619 1.00 28.48 ? 388  ARG   A HH21 1 
ATOM   5964  H  HH22 . ARG   A 1 388 ? 38.221 6.140   15.656 1.00 28.48 ? 388  ARG   A HH22 1 
ATOM   5965  N  N    . MET   A 1 389 ? 33.697 13.465  16.755 1.00 13.05 ? 389  MET   A N    1 
ATOM   5966  C  CA   . MET   A 1 389 ? 33.496 14.718  15.982 1.00 14.82 ? 389  MET   A CA   1 
ATOM   5967  C  C    . MET   A 1 389 ? 34.432 15.797  16.545 1.00 15.59 ? 389  MET   A C    1 
ATOM   5968  O  O    . MET   A 1 389 ? 35.083 16.488  15.750 1.00 16.75 ? 389  MET   A O    1 
ATOM   5969  C  CB   . MET   A 1 389 ? 32.039 15.190  16.078 1.00 14.37 ? 389  MET   A CB   1 
ATOM   5970  C  CG   . MET   A 1 389 ? 31.031 14.171  15.576 1.00 15.46 ? 389  MET   A CG   1 
ATOM   5971  S  SD   . MET   A 1 389 ? 29.346 14.504  16.165 1.00 21.39 ? 389  MET   A SD   1 
ATOM   5972  C  CE   . MET   A 1 389 ? 29.352 16.296  16.145 1.00 11.79 ? 389  MET   A CE   1 
ATOM   5973  H  H    . MET   A 1 389 ? 33.038 13.240  17.260 1.00 15.66 ? 389  MET   A H    1 
ATOM   5974  H  HA   . MET   A 1 389 ? 33.697 14.554  15.047 1.00 17.79 ? 389  MET   A HA   1 
ATOM   5975  H  HB2  . MET   A 1 389 ? 31.837 15.404  17.002 1.00 17.25 ? 389  MET   A HB2  1 
ATOM   5976  H  HB3  . MET   A 1 389 ? 31.939 16.010  15.569 1.00 17.25 ? 389  MET   A HB3  1 
ATOM   5977  H  HG2  . MET   A 1 389 ? 31.036 14.168  14.606 1.00 18.56 ? 389  MET   A HG2  1 
ATOM   5978  H  HG3  . MET   A 1 389 ? 31.301 13.285  15.864 1.00 18.56 ? 389  MET   A HG3  1 
ATOM   5979  H  HE1  . MET   A 1 389 ? 28.490 16.626  16.445 1.00 14.15 ? 389  MET   A HE1  1 
ATOM   5980  H  HE2  . MET   A 1 389 ? 30.047 16.624  16.737 1.00 14.15 ? 389  MET   A HE2  1 
ATOM   5981  H  HE3  . MET   A 1 389 ? 29.522 16.609  15.243 1.00 14.15 ? 389  MET   A HE3  1 
ATOM   5982  N  N    . VAL   A 1 390 ? 34.501 15.911  17.872 1.00 15.02 ? 390  VAL   A N    1 
ATOM   5983  C  CA   . VAL   A 1 390 ? 35.343 16.957  18.523 1.00 16.64 ? 390  VAL   A CA   1 
ATOM   5984  C  C    . VAL   A 1 390 ? 36.807 16.786  18.102 1.00 15.55 ? 390  VAL   A C    1 
ATOM   5985  O  O    . VAL   A 1 390 ? 37.462 17.805  17.818 1.00 15.63 ? 390  VAL   A O    1 
ATOM   5986  C  CB   . VAL   A 1 390 ? 35.196 16.887  20.054 1.00 15.44 ? 390  VAL   A CB   1 
ATOM   5987  C  CG1  . VAL   A 1 390 ? 36.284 17.672  20.769 1.00 15.78 ? 390  VAL   A CG1  1 
ATOM   5988  C  CG2  . VAL   A 1 390 ? 33.817 17.334  20.510 1.00 15.11 ? 390  VAL   A CG2  1 
ATOM   5989  H  H    . VAL   A 1 390 ? 34.076 15.403  18.421 1.00 18.02 ? 390  VAL   A H    1 
ATOM   5990  H  HA   . VAL   A 1 390 ? 35.042 17.832  18.234 1.00 19.97 ? 390  VAL   A HA   1 
ATOM   5991  H  HB   . VAL   A 1 390 ? 35.301 15.954  20.298 1.00 18.53 ? 390  VAL   A HB   1 
ATOM   5992  H  HG11 . VAL   A 1 390 ? 36.156 17.603  21.728 1.00 18.94 ? 390  VAL   A HG11 1 
ATOM   5993  H  HG12 . VAL   A 1 390 ? 37.153 17.311  20.532 1.00 18.94 ? 390  VAL   A HG12 1 
ATOM   5994  H  HG13 . VAL   A 1 390 ? 36.238 18.604  20.504 1.00 18.94 ? 390  VAL   A HG13 1 
ATOM   5995  H  HG21 . VAL   A 1 390 ? 33.761 17.277  21.477 1.00 18.13 ? 390  VAL   A HG21 1 
ATOM   5996  H  HG22 . VAL   A 1 390 ? 33.665 18.251  20.231 1.00 18.13 ? 390  VAL   A HG22 1 
ATOM   5997  H  HG23 . VAL   A 1 390 ? 33.143 16.760  20.113 1.00 18.13 ? 390  VAL   A HG23 1 
ATOM   5998  N  N    . TYR   A 1 391 ? 37.294 15.546  18.049 1.00 15.54 ? 391  TYR   A N    1 
ATOM   5999  C  CA   . TYR   A 1 391 ? 38.736 15.315  17.767 1.00 16.11 ? 391  TYR   A CA   1 
ATOM   6000  C  C    . TYR   A 1 391 ? 38.970 14.851  16.324 1.00 14.34 ? 391  TYR   A C    1 
ATOM   6001  O  O    . TYR   A 1 391 ? 40.085 14.417  16.016 1.00 13.02 ? 391  TYR   A O    1 
ATOM   6002  C  CB   . TYR   A 1 391 ? 39.299 14.301  18.768 1.00 17.26 ? 391  TYR   A CB   1 
ATOM   6003  C  CG   . TYR   A 1 391 ? 39.400 14.812  20.182 1.00 15.76 ? 391  TYR   A CG   1 
ATOM   6004  C  CD1  . TYR   A 1 391 ? 40.477 15.585  20.580 1.00 18.81 ? 391  TYR   A CD1  1 
ATOM   6005  C  CD2  . TYR   A 1 391 ? 38.422 14.533  21.121 1.00 18.15 ? 391  TYR   A CD2  1 
ATOM   6006  C  CE1  . TYR   A 1 391 ? 40.582 16.064  21.874 1.00 18.86 ? 391  TYR   A CE1  1 
ATOM   6007  C  CE2  . TYR   A 1 391 ? 38.512 15.005  22.420 1.00 19.28 ? 391  TYR   A CE2  1 
ATOM   6008  C  CZ   . TYR   A 1 391 ? 39.597 15.775  22.798 1.00 17.36 ? 391  TYR   A CZ   1 
ATOM   6009  O  OH   . TYR   A 1 391 ? 39.705 16.252  24.081 1.00 17.09 ? 391  TYR   A OH   1 
ATOM   6010  H  H    . TYR   A 1 391 ? 36.828 14.833  18.169 1.00 18.66 ? 391  TYR   A H    1 
ATOM   6011  H  HA   . TYR   A 1 391 ? 39.204 16.158  17.869 1.00 19.33 ? 391  TYR   A HA   1 
ATOM   6012  H  HB2  . TYR   A 1 391 ? 38.737 13.510  18.761 1.00 20.71 ? 391  TYR   A HB2  1 
ATOM   6013  H  HB3  . TYR   A 1 391 ? 40.181 14.026  18.472 1.00 20.71 ? 391  TYR   A HB3  1 
ATOM   6014  H  HD1  . TYR   A 1 391 ? 41.144 15.787  19.965 1.00 22.58 ? 391  TYR   A HD1  1 
ATOM   6015  H  HD2  . TYR   A 1 391 ? 37.688 14.017  20.874 1.00 21.79 ? 391  TYR   A HD2  1 
ATOM   6016  H  HE1  . TYR   A 1 391 ? 41.315 16.580  22.121 1.00 22.63 ? 391  TYR   A HE1  1 
ATOM   6017  H  HE2  . TYR   A 1 391 ? 37.845 14.805  23.036 1.00 23.14 ? 391  TYR   A HE2  1 
ATOM   6018  H  HH   . TYR   A 1 391 ? 40.445 16.638  24.175 1.00 20.51 ? 391  TYR   A HH   1 
ATOM   6019  N  N    . SER   A 1 392 ? 37.949 14.941  15.471 1.00 15.04 ? 392  SER   A N    1 
ATOM   6020  C  CA   . SER   A 1 392 ? 38.113 14.568  14.043 1.00 16.20 ? 392  SER   A CA   1 
ATOM   6021  C  C    . SER   A 1 392 ? 38.683 13.148  13.920 1.00 19.05 ? 392  SER   A C    1 
ATOM   6022  O  O    . SER   A 1 392 ? 39.642 12.966  13.157 1.00 19.94 ? 392  SER   A O    1 
ATOM   6023  C  CB   . SER   A 1 392 ? 38.967 15.577  13.312 1.00 13.09 ? 392  SER   A CB   1 
ATOM   6024  O  OG   . SER   A 1 392 ? 38.321 16.839  13.254 1.00 16.24 ? 392  SER   A OG   1 
ATOM   6025  H  H    . SER   A 1 392 ? 37.161 15.210  15.685 1.00 18.05 ? 392  SER   A H    1 
ATOM   6026  H  HA   . SER   A 1 392 ? 37.239 14.574  13.622 1.00 19.45 ? 392  SER   A HA   1 
ATOM   6027  H  HB2  . SER   A 1 392 ? 39.822 15.668  13.760 1.00 15.72 ? 392  SER   A HB2  1 
ATOM   6028  H  HB3  . SER   A 1 392 ? 39.150 15.261  12.413 1.00 15.72 ? 392  SER   A HB3  1 
ATOM   6029  H  HG   . SER   A 1 392 ? 38.505 17.280  13.944 1.00 19.49 ? 392  SER   A HG   1 
ATOM   6030  N  N    . GLU   A 1 393 ? 38.078 12.187  14.619 1.00 16.67 ? 393  GLU   A N    1 
ATOM   6031  C  CA   . GLU   A 1 393 ? 38.546 10.778  14.567 1.00 19.83 ? 393  GLU   A CA   1 
ATOM   6032  C  C    . GLU   A 1 393 ? 37.697 9.987   13.566 1.00 20.83 ? 393  GLU   A C    1 
ATOM   6033  O  O    . GLU   A 1 393 ? 36.464 10.020  13.693 1.00 19.14 ? 393  GLU   A O    1 
ATOM   6034  C  CB   . GLU   A 1 393 ? 38.464 10.148  15.957 1.00 22.23 ? 393  GLU   A CB   1 
ATOM   6035  C  CG   . GLU   A 1 393 ? 39.294 10.886  16.991 1.00 24.99 ? 393  GLU   A CG   1 
ATOM   6036  C  CD   . GLU   A 1 393 ? 39.023 10.492  18.432 1.00 27.34 ? 393  GLU   A CD   1 
ATOM   6037  O  OE1  . GLU   A 1 393 ? 37.882 10.093  18.732 1.00 32.06 ? 393  GLU   A OE1  1 
ATOM   6038  O  OE2  . GLU   A 1 393 ? 39.955 10.587  19.251 1.00 33.64 ? 393  GLU   A OE2  1 
ATOM   6039  H  H    . GLU   A 1 393 ? 37.398 12.318  15.129 1.00 20.01 ? 393  GLU   A H    1 
ATOM   6040  H  HA   . GLU   A 1 393 ? 39.471 10.758  14.275 1.00 23.80 ? 393  GLU   A HA   1 
ATOM   6041  H  HB2  . GLU   A 1 393 ? 37.538 10.131  16.245 1.00 26.68 ? 393  GLU   A HB2  1 
ATOM   6042  H  HB3  . GLU   A 1 393 ? 38.763 9.226   15.907 1.00 26.68 ? 393  GLU   A HB3  1 
ATOM   6043  H  HG2  . GLU   A 1 393 ? 40.233 10.735  16.800 1.00 29.99 ? 393  GLU   A HG2  1 
ATOM   6044  H  HG3  . GLU   A 1 393 ? 39.134 11.838  16.895 1.00 29.99 ? 393  GLU   A HG3  1 
ATOM   6045  N  N    . GLY   A 1 394 ? 38.350 9.313   12.617 1.00 18.99 ? 394  GLY   A N    1 
ATOM   6046  C  CA   . GLY   A 1 394 ? 37.630 8.519   11.605 1.00 20.91 ? 394  GLY   A CA   1 
ATOM   6047  C  C    . GLY   A 1 394 ? 36.536 9.321   10.922 1.00 19.70 ? 394  GLY   A C    1 
ATOM   6048  O  O    . GLY   A 1 394 ? 36.817 10.446  10.484 1.00 17.62 ? 394  GLY   A O    1 
ATOM   6049  H  H    . GLY   A 1 394 ? 39.206 9.300   12.538 1.00 22.80 ? 394  GLY   A H    1 
ATOM   6050  H  HA2  . GLY   A 1 394 ? 38.259 8.199   10.939 1.00 25.09 ? 394  GLY   A HA2  1 
ATOM   6051  H  HA3  . GLY   A 1 394 ? 37.241 7.737   12.026 1.00 25.09 ? 394  GLY   A HA3  1 
ATOM   6052  N  N    . PHE   A 1 395 ? 35.329 8.754   10.839 1.00 21.83 ? 395  PHE   A N    1 
ATOM   6053  C  CA   . PHE   A 1 395 ? 34.204 9.436   10.146 1.00 18.05 ? 395  PHE   A CA   1 
ATOM   6054  C  C    . PHE   A 1 395 ? 33.775 10.686  10.924 1.00 17.98 ? 395  PHE   A C    1 
ATOM   6055  O  O    . PHE   A 1 395 ? 33.168 11.584  10.323 1.00 15.54 ? 395  PHE   A O    1 
ATOM   6056  C  CB   . PHE   A 1 395 ? 33.021 8.481   9.961  1.00 17.59 ? 395  PHE   A CB   1 
ATOM   6057  C  CG   . PHE   A 1 395 ? 31.772 9.152   9.451  1.00 15.33 ? 395  PHE   A CG   1 
ATOM   6058  C  CD1  . PHE   A 1 395 ? 31.654 9.507   8.117  1.00 20.88 ? 395  PHE   A CD1  1 
ATOM   6059  C  CD2  . PHE   A 1 395 ? 30.727 9.454   10.308 1.00 17.62 ? 395  PHE   A CD2  1 
ATOM   6060  C  CE1  . PHE   A 1 395 ? 30.512 10.135  7.649  1.00 16.28 ? 395  PHE   A CE1  1 
ATOM   6061  C  CE2  . PHE   A 1 395 ? 29.584 10.082  9.839  1.00 18.64 ? 395  PHE   A CE2  1 
ATOM   6062  C  CZ   . PHE   A 1 395 ? 29.480 10.422  8.511  1.00 20.27 ? 395  PHE   A CZ   1 
ATOM   6063  H  H    . PHE   A 1 395 ? 35.133 7.985   11.170 1.00 26.21 ? 395  PHE   A H    1 
ATOM   6064  H  HA   . PHE   A 1 395 ? 34.509 9.711   9.267  1.00 21.67 ? 395  PHE   A HA   1 
ATOM   6065  H  HB2  . PHE   A 1 395 ? 33.277 7.779   9.342  1.00 21.11 ? 395  PHE   A HB2  1 
ATOM   6066  H  HB3  . PHE   A 1 395 ? 32.825 8.054   10.810 1.00 21.11 ? 395  PHE   A HB3  1 
ATOM   6067  H  HD1  . PHE   A 1 395 ? 32.350 9.321   7.529  1.00 25.06 ? 395  PHE   A HD1  1 
ATOM   6068  H  HD2  . PHE   A 1 395 ? 30.793 9.233   11.209 1.00 21.14 ? 395  PHE   A HD2  1 
ATOM   6069  H  HE1  . PHE   A 1 395 ? 30.443 10.363  6.750  1.00 19.54 ? 395  PHE   A HE1  1 
ATOM   6070  H  HE2  . PHE   A 1 395 ? 28.886 10.274  10.423 1.00 22.37 ? 395  PHE   A HE2  1 
ATOM   6071  H  HZ   . PHE   A 1 395 ? 28.714 10.845  8.197  1.00 24.32 ? 395  PHE   A HZ   1 
ATOM   6072  N  N    . GLY   A 1 396 ? 34.069 10.723  12.224 1.00 15.75 ? 396  GLY   A N    1 
ATOM   6073  C  CA   . GLY   A 1 396 ? 33.730 11.912  13.027 1.00 15.97 ? 396  GLY   A CA   1 
ATOM   6074  C  C    . GLY   A 1 396 ? 34.243 13.181  12.368 1.00 14.89 ? 396  GLY   A C    1 
ATOM   6075  O  O    . GLY   A 1 396 ? 33.602 14.227  12.524 1.00 13.15 ? 396  GLY   A O    1 
ATOM   6076  H  H    . GLY   A 1 396 ? 34.456 10.088  12.657 1.00 18.91 ? 396  GLY   A H    1 
ATOM   6077  H  HA2  . GLY   A 1 396 ? 32.768 11.968  13.138 1.00 19.17 ? 396  GLY   A HA2  1 
ATOM   6078  H  HA3  . GLY   A 1 396 ? 34.113 11.827  13.914 1.00 19.17 ? 396  GLY   A HA3  1 
ATOM   6079  N  N    . ALA   A 1 397 ? 35.356 13.080  11.641 1.00 14.18 ? 397  ALA   A N    1 
ATOM   6080  C  CA   . ALA   A 1 397 ? 35.974 14.277  11.025 1.00 17.88 ? 397  ALA   A CA   1 
ATOM   6081  C  C    . ALA   A 1 397 ? 35.027 14.917  10.003 1.00 14.52 ? 397  ALA   A C    1 
ATOM   6082  O  O    . ALA   A 1 397 ? 35.178 16.114  9.735  1.00 16.47 ? 397  ALA   A O    1 
ATOM   6083  C  CB   . ALA   A 1 397 ? 37.295 13.910  10.395 1.00 16.10 ? 397  ALA   A CB   1 
ATOM   6084  H  H    . ALA   A 1 397 ? 35.771 12.342  11.489 1.00 17.02 ? 397  ALA   A H    1 
ATOM   6085  H  HA   . ALA   A 1 397 ? 36.139 14.935  11.718 1.00 21.46 ? 397  ALA   A HA   1 
ATOM   6086  H  HB1  . ALA   A 1 397 ? 37.693 14.699  9.994  1.00 19.33 ? 397  ALA   A HB1  1 
ATOM   6087  H  HB2  . ALA   A 1 397 ? 37.891 13.558  11.074 1.00 19.33 ? 397  ALA   A HB2  1 
ATOM   6088  H  HB3  . ALA   A 1 397 ? 37.152 13.237  9.711  1.00 19.33 ? 397  ALA   A HB3  1 
ATOM   6089  N  N    . LYS   A 1 398 ? 34.111 14.132  9.436  1.00 15.94 ? 398  LYS   A N    1 
ATOM   6090  C  CA   . LYS   A 1 398 ? 33.193 14.667  8.395  1.00 14.42 ? 398  LYS   A CA   1 
ATOM   6091  C  C    . LYS   A 1 398 ? 32.029 15.405  9.066  1.00 13.41 ? 398  LYS   A C    1 
ATOM   6092  O  O    . LYS   A 1 398 ? 31.362 16.186  8.381  1.00 14.07 ? 398  LYS   A O    1 
ATOM   6093  C  CB   . LYS   A 1 398 ? 32.680 13.532  7.503  1.00 17.06 ? 398  LYS   A CB   1 
ATOM   6094  C  CG   . LYS   A 1 398 ? 33.741 12.862  6.641  1.00 20.51 ? 398  LYS   A CG   1 
ATOM   6095  C  CD   . LYS   A 1 398 ? 33.198 12.312  5.343  1.00 23.34 ? 398  LYS   A CD   1 
ATOM   6096  C  CE   . LYS   A 1 398 ? 34.285 11.964  4.349  1.00 22.99 ? 398  LYS   A CE   1 
ATOM   6097  N  NZ   . LYS   A 1 398 ? 33.788 11.051  3.293  1.00 23.20 ? 398  LYS   A NZ   1 
ATOM   6098  H  H    . LYS   A 1 398 ? 33.996 13.301  9.627  1.00 19.13 ? 398  LYS   A H    1 
ATOM   6099  H  HA   . LYS   A 1 398 ? 33.676 15.293  7.833  1.00 17.31 ? 398  LYS   A HA   1 
ATOM   6100  H  HB2  . LYS   A 1 398 ? 32.267 12.858  8.065  1.00 20.48 ? 398  LYS   A HB2  1 
ATOM   6101  H  HB3  . LYS   A 1 398 ? 31.986 13.883  6.923  1.00 20.48 ? 398  LYS   A HB3  1 
ATOM   6102  H  HG2  . LYS   A 1 398 ? 34.442 13.504  6.445  1.00 24.61 ? 398  LYS   A HG2  1 
ATOM   6103  H  HG3  . LYS   A 1 398 ? 34.150 12.141  7.145  1.00 24.61 ? 398  LYS   A HG3  1 
ATOM   6104  H  HD2  . LYS   A 1 398 ? 32.670 11.520  5.529  1.00 28.01 ? 398  LYS   A HD2  1 
ATOM   6105  H  HD3  . LYS   A 1 398 ? 32.600 12.964  4.946  1.00 28.01 ? 398  LYS   A HD3  1 
ATOM   6106  H  HE2  . LYS   A 1 398 ? 34.624 12.776  3.942  1.00 27.59 ? 398  LYS   A HE2  1 
ATOM   6107  H  HE3  . LYS   A 1 398 ? 35.028 11.548  4.814  1.00 27.59 ? 398  LYS   A HE3  1 
ATOM   6108  H  HZ1  . LYS   A 1 398 ? 34.431 10.912  2.694  1.00 27.84 ? 398  LYS   A HZ1  1 
ATOM   6109  H  HZ2  . LYS   A 1 398 ? 33.551 10.275  3.659  1.00 27.84 ? 398  LYS   A HZ2  1 
ATOM   6110  H  HZ3  . LYS   A 1 398 ? 33.083 11.417  2.891  1.00 27.84 ? 398  LYS   A HZ3  1 
ATOM   6111  N  N    . MET   A 1 399 ? 31.829 15.171  10.363 1.00 13.87 ? 399  MET   A N    1 
ATOM   6112  C  CA   . MET   A 1 399 ? 30.697 15.801  11.095 1.00 13.03 ? 399  MET   A CA   1 
ATOM   6113  C  C    . MET   A 1 399 ? 31.202 16.965  11.956 1.00 14.56 ? 399  MET   A C    1 
ATOM   6114  O  O    . MET   A 1 399 ? 30.359 17.727  12.439 1.00 11.43 ? 399  MET   A O    1 
ATOM   6115  C  CB   . MET   A 1 399 ? 30.017 14.774  12.009 1.00 14.18 ? 399  MET   A CB   1 
ATOM   6116  C  CG   . MET   A 1 399 ? 29.191 13.744  11.269 1.00 17.05 ? 399  MET   A CG   1 
ATOM   6117  S  SD   . MET   A 1 399 ? 28.249 12.707  12.418 1.00 18.01 ? 399  MET   A SD   1 
ATOM   6118  C  CE   . MET   A 1 399 ? 29.564 11.689  13.086 1.00 16.55 ? 399  MET   A CE   1 
ATOM   6119  H  H    . MET   A 1 399 ? 32.325 14.658  10.843 1.00 16.65 ? 399  MET   A H    1 
ATOM   6120  H  HA   . MET   A 1 399 ? 30.061 16.129  10.440 1.00 15.64 ? 399  MET   A HA   1 
ATOM   6121  H  HB2  . MET   A 1 399 ? 30.697 14.317  12.529 1.00 17.01 ? 399  MET   A HB2  1 
ATOM   6122  H  HB3  . MET   A 1 399 ? 29.446 15.242  12.638 1.00 17.01 ? 399  MET   A HB3  1 
ATOM   6123  H  HG2  . MET   A 1 399 ? 28.582 14.191  10.660 1.00 20.47 ? 399  MET   A HG2  1 
ATOM   6124  H  HG3  . MET   A 1 399 ? 29.773 13.186  10.730 1.00 20.47 ? 399  MET   A HG3  1 
ATOM   6125  H  HE1  . MET   A 1 399 ? 29.196 11.068  13.734 1.00 19.86 ? 399  MET   A HE1  1 
ATOM   6126  H  HE2  . MET   A 1 399 ? 29.986 11.193  12.367 1.00 19.86 ? 399  MET   A HE2  1 
ATOM   6127  H  HE3  . MET   A 1 399 ? 30.223 12.254  13.519 1.00 19.86 ? 399  MET   A HE3  1 
ATOM   6128  N  N    . THR   A 1 400 ? 32.519 17.105  12.100 1.00 13.96 ? 400  THR   A N    1 
ATOM   6129  C  CA   . THR   A 1 400 ? 33.094 18.139  13.001 1.00 14.44 ? 400  THR   A CA   1 
ATOM   6130  C  C    . THR   A 1 400 ? 32.553 19.538  12.687 1.00 15.01 ? 400  THR   A C    1 
ATOM   6131  O  O    . THR   A 1 400 ? 32.366 20.315  13.642 1.00 13.90 ? 400  THR   A O    1 
ATOM   6132  C  CB   . THR   A 1 400 ? 34.624 18.134  12.901 1.00 12.76 ? 400  THR   A CB   1 
ATOM   6133  O  OG1  . THR   A 1 400 ? 35.091 16.810  13.161 1.00 15.27 ? 400  THR   A OG1  1 
ATOM   6134  C  CG2  . THR   A 1 400 ? 35.281 19.112  13.850 1.00 14.24 ? 400  THR   A CG2  1 
ATOM   6135  H  H    . THR   A 1 400 ? 33.102 16.621  11.694 1.00 16.75 ? 400  THR   A H    1 
ATOM   6136  H  HA   . THR   A 1 400 ? 32.827 17.917  13.907 1.00 17.33 ? 400  THR   A HA   1 
ATOM   6137  H  HB   . THR   A 1 400 ? 34.866 18.418  12.006 1.00 15.32 ? 400  THR   A HB   1 
ATOM   6138  H  HG1  . THR   A 1 400 ? 34.852 16.574  13.931 1.00 18.33 ? 400  THR   A HG1  1 
ATOM   6139  H  HG21 . THR   A 1 400 ? 36.244 19.067  13.745 1.00 17.09 ? 400  THR   A HG21 1 
ATOM   6140  H  HG22 . THR   A 1 400 ? 34.976 20.011  13.651 1.00 17.09 ? 400  THR   A HG22 1 
ATOM   6141  H  HG23 . THR   A 1 400 ? 35.045 18.885  14.763 1.00 17.09 ? 400  THR   A HG23 1 
ATOM   6142  N  N    . ASN   A 1 401 ? 32.308 19.848  11.414 1.00 12.75 ? 401  ASN   A N    1 
ATOM   6143  C  CA   . ASN   A 1 401 ? 31.926 21.244  11.063 1.00 13.50 ? 401  ASN   A CA   1 
ATOM   6144  C  C    . ASN   A 1 401 ? 30.437 21.371  10.722 1.00 11.38 ? 401  ASN   A C    1 
ATOM   6145  O  O    . ASN   A 1 401 ? 30.078 22.371  10.098 1.00 13.91 ? 401  ASN   A O    1 
ATOM   6146  C  CB   . ASN   A 1 401 ? 32.820 21.807  9.959  1.00 13.26 ? 401  ASN   A CB   1 
ATOM   6147  C  CG   . ASN   A 1 401 ? 34.250 21.986  10.421 1.00 16.24 ? 401  ASN   A CG   1 
ATOM   6148  O  OD1  . ASN   A 1 401 ? 34.498 22.213  11.602 1.00 12.63 ? 401  ASN   A OD1  1 
ATOM   6149  N  ND2  . ASN   A 1 401 ? 35.193 21.880  9.502  1.00 25.10 ? 401  ASN   A ND2  1 
ATOM   6150  H  H    . ASN   A 1 401 ? 32.351 19.299  10.754 1.00 15.30 ? 401  ASN   A H    1 
ATOM   6151  H  HA   . ASN   A 1 401 ? 32.071 21.786  11.854 1.00 16.20 ? 401  ASN   A HA   1 
ATOM   6152  H  HB2  . ASN   A 1 401 ? 32.801 21.211  9.194  1.00 15.92 ? 401  ASN   A HB2  1 
ATOM   6153  H  HB3  . ASN   A 1 401 ? 32.468 22.661  9.663  1.00 15.92 ? 401  ASN   A HB3  1 
ATOM   6154  H  HD21 . ASN   A 1 401 ? 36.020 21.971  9.722  1.00 30.12 ? 401  ASN   A HD21 1 
ATOM   6155  H  HD22 . ASN   A 1 401 ? 34.980 21.720  8.684  1.00 30.12 ? 401  ASN   A HD22 1 
ATOM   6156  N  N    . GLY   A 1 402 ? 29.618 20.390  11.100 1.00 10.95 ? 402  GLY   A N    1 
ATOM   6157  C  CA   . GLY   A 1 402 ? 28.165 20.572  10.923 1.00 11.07 ? 402  GLY   A CA   1 
ATOM   6158  C  C    . GLY   A 1 402 ? 27.519 19.811  9.777  1.00 12.44 ? 402  GLY   A C    1 
ATOM   6159  O  O    . GLY   A 1 402 ? 28.245 19.343  8.889  1.00 11.19 ? 402  GLY   A O    1 
ATOM   6160  H  H    . GLY   A 1 402 ? 29.862 19.642  11.446 1.00 13.15 ? 402  GLY   A H    1 
ATOM   6161  H  HA2  . GLY   A 1 402 ? 27.724 20.311  11.747 1.00 13.29 ? 402  GLY   A HA2  1 
ATOM   6162  H  HA3  . GLY   A 1 402 ? 27.991 21.518  10.795 1.00 13.29 ? 402  GLY   A HA3  1 
ATOM   6163  N  N    . SER   A 1 403 ? 26.184 19.763  9.784  1.00 11.27 ? 403  SER   A N    1 
ATOM   6164  C  CA   . SER   A 1 403 ? 25.416 18.984  8.777  1.00 11.13 ? 403  SER   A CA   1 
ATOM   6165  C  C    . SER   A 1 403 ? 25.513 19.583  7.372  1.00 11.42 ? 403  SER   A C    1 
ATOM   6166  O  O    . SER   A 1 403 ? 25.521 18.811  6.410  1.00 11.02 ? 403  SER   A O    1 
ATOM   6167  C  CB   . SER   A 1 403 ? 23.977 18.891  9.215  1.00 9.68  ? 403  SER   A CB   1 
ATOM   6168  O  OG   . SER   A 1 403 ? 23.307 20.123  9.004  1.00 11.24 ? 403  SER   A OG   1 
ATOM   6169  H  H    . SER   A 1 403 ? 25.695 20.172  10.361 1.00 13.53 ? 403  SER   A H    1 
ATOM   6170  H  HA   . SER   A 1 403 ? 25.806 18.097  8.725  1.00 13.35 ? 403  SER   A HA   1 
ATOM   6171  H  HB2  . SER   A 1 403 ? 23.529 18.186  8.722  1.00 11.62 ? 403  SER   A HB2  1 
ATOM   6172  H  HB3  . SER   A 1 403 ? 23.935 18.652  10.154 1.00 11.62 ? 403  SER   A HB3  1 
ATOM   6173  H  HG   . SER   A 1 403 ? 23.525 20.667  9.605  1.00 13.49 ? 403  SER   A HG   1 
ATOM   6174  N  N    . TYR   A 1 404 ? 25.551 20.910  7.261  1.00 11.21 ? 404  TYR   A N    1 
ATOM   6175  C  CA   . TYR   A 1 404 ? 25.528 21.520  5.906  1.00 10.43 ? 404  TYR   A CA   1 
ATOM   6176  C  C    . TYR   A 1 404 ? 26.761 21.055  5.130  1.00 12.25 ? 404  TYR   A C    1 
ATOM   6177  O  O    . TYR   A 1 404 ? 26.628 20.600  3.985  1.00 12.02 ? 404  TYR   A O    1 
ATOM   6178  C  CB   . TYR   A 1 404 ? 25.471 23.047  5.997  1.00 11.00 ? 404  TYR   A CB   1 
ATOM   6179  C  CG   . TYR   A 1 404 ? 25.470 23.750  4.663  1.00 13.86 ? 404  TYR   A CG   1 
ATOM   6180  C  CD1  . TYR   A 1 404 ? 26.652 24.005  3.989  1.00 12.33 ? 404  TYR   A CD1  1 
ATOM   6181  C  CD2  . TYR   A 1 404 ? 24.286 24.152  4.069  1.00 16.11 ? 404  TYR   A CD2  1 
ATOM   6182  C  CE1  . TYR   A 1 404 ? 26.660 24.644  2.760  1.00 18.62 ? 404  TYR   A CE1  1 
ATOM   6183  C  CE2  . TYR   A 1 404 ? 24.276 24.792  2.841  1.00 17.33 ? 404  TYR   A CE2  1 
ATOM   6184  C  CZ   . TYR   A 1 404 ? 25.467 25.040  2.184  1.00 21.46 ? 404  TYR   A CZ   1 
ATOM   6185  O  OH   . TYR   A 1 404 ? 25.463 25.676  0.967  1.00 21.73 ? 404  TYR   A OH   1 
ATOM   6186  H  H    . TYR   A 1 404 ? 25.589 21.463  7.918  1.00 13.46 ? 404  TYR   A H    1 
ATOM   6187  H  HA   . TYR   A 1 404 ? 24.731 21.232  5.435  1.00 12.51 ? 404  TYR   A HA   1 
ATOM   6188  H  HB2  . TYR   A 1 404 ? 24.672 23.302  6.485  1.00 13.20 ? 404  TYR   A HB2  1 
ATOM   6189  H  HB3  . TYR   A 1 404 ? 26.231 23.358  6.514  1.00 13.20 ? 404  TYR   A HB3  1 
ATOM   6190  H  HD1  . TYR   A 1 404 ? 27.459 23.741  4.370  1.00 14.80 ? 404  TYR   A HD1  1 
ATOM   6191  H  HD2  . TYR   A 1 404 ? 23.480 23.989  4.504  1.00 19.33 ? 404  TYR   A HD2  1 
ATOM   6192  H  HE1  . TYR   A 1 404 ? 27.465 24.806  2.324  1.00 22.34 ? 404  TYR   A HE1  1 
ATOM   6193  H  HE2  . TYR   A 1 404 ? 23.470 25.054  2.459  1.00 20.80 ? 404  TYR   A HE2  1 
ATOM   6194  H  HH   . TYR   A 1 404 ? 26.119 25.414  0.512  1.00 26.08 ? 404  TYR   A HH   1 
ATOM   6195  N  N    . ARG   A 1 405 ? 27.930 21.163  5.758  1.00 11.36 ? 405  ARG   A N    1 
ATOM   6196  C  CA   . ARG   A 1 405 ? 29.188 20.794  5.063  1.00 12.32 ? 405  ARG   A CA   1 
ATOM   6197  C  C    . ARG   A 1 405 ? 29.242 19.271  4.884  1.00 15.37 ? 405  ARG   A C    1 
ATOM   6198  O  O    . ARG   A 1 405 ? 29.766 18.816  3.859  1.00 12.89 ? 405  ARG   A O    1 
ATOM   6199  C  CB   . ARG   A 1 405 ? 30.383 21.339  5.851  1.00 14.64 ? 405  ARG   A CB   1 
ATOM   6200  C  CG   . ARG   A 1 405 ? 30.652 22.818  5.609  1.00 14.05 ? 405  ARG   A CG   1 
ATOM   6201  C  CD   . ARG   A 1 405 ? 31.240 23.522  6.817  1.00 14.07 ? 405  ARG   A CD   1 
ATOM   6202  N  NE   . ARG   A 1 405 ? 31.417 24.951  6.596  1.00 14.98 ? 405  ARG   A NE   1 
ATOM   6203  C  CZ   . ARG   A 1 405 ? 30.608 25.891  7.071  1.00 11.97 ? 405  ARG   A CZ   1 
ATOM   6204  N  NH1  . ARG   A 1 405 ? 29.508 25.552  7.717  1.00 10.80 ? 405  ARG   A NH1  1 
ATOM   6205  N  NH2  . ARG   A 1 405 ? 30.905 27.167  6.899  1.00 12.64 ? 405  ARG   A NH2  1 
ATOM   6206  H  H    . ARG   A 1 405 ? 28.028 21.440  6.566  1.00 13.64 ? 405  ARG   A H    1 
ATOM   6207  H  HA   . ARG   A 1 405 ? 29.221 21.190  4.178  1.00 14.78 ? 405  ARG   A HA   1 
ATOM   6208  H  HB2  . ARG   A 1 405 ? 30.228 21.197  6.798  1.00 17.57 ? 405  ARG   A HB2  1 
ATOM   6209  H  HB3  . ARG   A 1 405 ? 31.175 20.831  5.614  1.00 17.57 ? 405  ARG   A HB3  1 
ATOM   6210  H  HG2  . ARG   A 1 405 ? 31.260 22.912  4.859  1.00 16.87 ? 405  ARG   A HG2  1 
ATOM   6211  H  HG3  . ARG   A 1 405 ? 29.823 23.255  5.359  1.00 16.87 ? 405  ARG   A HG3  1 
ATOM   6212  H  HD2  . ARG   A 1 405 ? 30.660 23.385  7.582  1.00 16.89 ? 405  ARG   A HD2  1 
ATOM   6213  H  HD3  . ARG   A 1 405 ? 32.097 23.123  7.036  1.00 16.89 ? 405  ARG   A HD3  1 
ATOM   6214  H  HE   . ARG   A 1 405 ? 32.091 25.203  6.126  1.00 17.98 ? 405  ARG   A HE   1 
ATOM   6215  H  HH11 . ARG   A 1 405 ? 29.315 24.722  7.831  1.00 12.97 ? 405  ARG   A HH11 1 
ATOM   6216  H  HH12 . ARG   A 1 405 ? 28.985 26.161  8.024  1.00 12.97 ? 405  ARG   A HH12 1 
ATOM   6217  H  HH21 . ARG   A 1 405 ? 31.622 27.389  6.479  1.00 15.17 ? 405  ARG   A HH21 1 
ATOM   6218  H  HH22 . ARG   A 1 405 ? 30.381 27.776  7.207  1.00 15.17 ? 405  ARG   A HH22 1 
ATOM   6219  N  N    . LEU   A 1 406 ? 28.714 18.526  5.857  1.00 13.44 ? 406  LEU   A N    1 
ATOM   6220  C  CA   . LEU   A 1 406 ? 28.709 17.043  5.770  1.00 12.88 ? 406  LEU   A CA   1 
ATOM   6221  C  C    . LEU   A 1 406 ? 27.870 16.610  4.565  1.00 13.61 ? 406  LEU   A C    1 
ATOM   6222  O  O    . LEU   A 1 406 ? 28.342 15.769  3.792  1.00 13.46 ? 406  LEU   A O    1 
ATOM   6223  C  CB   . LEU   A 1 406 ? 28.116 16.482  7.067  1.00 12.01 ? 406  LEU   A CB   1 
ATOM   6224  C  CG   . LEU   A 1 406 ? 27.568 15.058  6.980  1.00 14.16 ? 406  LEU   A CG   1 
ATOM   6225  C  CD1  . LEU   A 1 406 ? 28.699 14.042  7.019  1.00 15.90 ? 406  LEU   A CD1  1 
ATOM   6226  C  CD2  . LEU   A 1 406 ? 26.577 14.790  8.102  1.00 13.88 ? 406  LEU   A CD2  1 
ATOM   6227  H  H    . LEU   A 1 406 ? 28.356 18.845  6.571  1.00 16.14 ? 406  LEU   A H    1 
ATOM   6228  H  HA   . LEU   A 1 406 ? 29.611 16.705  5.656  1.00 15.46 ? 406  LEU   A HA   1 
ATOM   6229  H  HB2  . LEU   A 1 406 ? 28.800 16.507  7.754  1.00 14.42 ? 406  LEU   A HB2  1 
ATOM   6230  H  HB3  . LEU   A 1 406 ? 27.401 17.070  7.358  1.00 14.42 ? 406  LEU   A HB3  1 
ATOM   6231  H  HG   . LEU   A 1 406 ? 27.103 14.968  6.134  1.00 17.00 ? 406  LEU   A HG   1 
ATOM   6232  H  HD11 . LEU   A 1 406 ? 28.332 13.146  6.963  1.00 19.08 ? 406  LEU   A HD11 1 
ATOM   6233  H  HD12 . LEU   A 1 406 ? 29.296 14.194  6.270  1.00 19.08 ? 406  LEU   A HD12 1 
ATOM   6234  H  HD13 . LEU   A 1 406 ? 29.191 14.137  7.849  1.00 19.08 ? 406  LEU   A HD13 1 
ATOM   6235  H  HD21 . LEU   A 1 406 ? 26.242 13.883  8.028  1.00 16.66 ? 406  LEU   A HD21 1 
ATOM   6236  H  HD22 . LEU   A 1 406 ? 27.019 14.903  8.958  1.00 16.66 ? 406  LEU   A HD22 1 
ATOM   6237  H  HD23 . LEU   A 1 406 ? 25.837 15.414  8.036  1.00 16.66 ? 406  LEU   A HD23 1 
ATOM   6238  N  N    . CYS   A 1 407 ? 26.683 17.195  4.412  1.00 14.27 ? 407  CYS   A N    1 
ATOM   6239  C  CA   . CYS   A 1 407 ? 25.763 16.775  3.319  1.00 12.86 ? 407  CYS   A CA   1 
ATOM   6240  C  C    . CYS   A 1 407 ? 26.287 17.273  1.968  1.00 12.94 ? 407  CYS   A C    1 
ATOM   6241  O  O    . CYS   A 1 407 ? 26.102 16.568  0.968  1.00 13.67 ? 407  CYS   A O    1 
ATOM   6242  C  CB   . CYS   A 1 407 ? 24.358 17.302  3.582  1.00 10.63 ? 407  CYS   A CB   1 
ATOM   6243  S  SG   . CYS   A 1 407 ? 23.536 16.483  4.977  1.00 12.73 ? 407  CYS   A SG   1 
ATOM   6244  H  H    . CYS   A 1 407 ? 26.384 17.826  4.913  1.00 17.13 ? 407  CYS   A H    1 
ATOM   6245  H  HA   . CYS   A 1 407 ? 25.725 15.806  3.294  1.00 15.43 ? 407  CYS   A HA   1 
ATOM   6246  H  HB2  . CYS   A 1 407 ? 24.404 18.255  3.756  1.00 12.76 ? 407  CYS   A HB2  1 
ATOM   6247  H  HB3  . CYS   A 1 407 ? 23.820 17.185  2.783  1.00 12.76 ? 407  CYS   A HB3  1 
ATOM   6248  H  HG   . CYS   A 1 407 ? 23.910 16.974  6.006  1.00 15.27 ? 407  CYS   A HG   1 
ATOM   6249  N  N    . GLU   A 1 408 ? 26.934 18.438  1.960  1.00 11.85 ? 408  GLU   A N    1 
ATOM   6250  C  CA   . GLU   A 1 408 ? 27.532 18.949  0.700  1.00 16.25 ? 408  GLU   A CA   1 
ATOM   6251  C  C    . GLU   A 1 408 ? 28.572 17.934  0.230  1.00 15.10 ? 408  GLU   A C    1 
ATOM   6252  O  O    . GLU   A 1 408 ? 28.624 17.656  -0.976 1.00 14.95 ? 408  GLU   A O    1 
ATOM   6253  C  CB   . GLU   A 1 408 ? 28.185 20.316  0.906  1.00 17.80 ? 408  GLU   A CB   1 
ATOM   6254  C  CG   . GLU   A 1 408 ? 28.717 20.931  -0.374 1.00 21.04 ? 408  GLU   A CG   1 
ATOM   6255  C  CD   . GLU   A 1 408 ? 28.959 22.428  -0.298 1.00 27.48 ? 408  GLU   A CD   1 
ATOM   6256  O  OE1  . GLU   A 1 408 ? 27.976 23.179  -0.163 1.00 33.55 ? 408  GLU   A OE1  1 
ATOM   6257  O  OE2  . GLU   A 1 408 ? 30.130 22.839  -0.373 1.00 39.45 ? 408  GLU   A OE2  1 
ATOM   6258  H  H    . GLU   A 1 408 ? 27.042 18.944  2.647  1.00 14.23 ? 408  GLU   A H    1 
ATOM   6259  H  HA   . GLU   A 1 408 ? 26.836 19.062  0.034  1.00 19.50 ? 408  GLU   A HA   1 
ATOM   6260  H  HB2  . GLU   A 1 408 ? 27.537 20.920  1.302  1.00 21.37 ? 408  GLU   A HB2  1 
ATOM   6261  H  HB3  . GLU   A 1 408 ? 28.913 20.226  1.540  1.00 21.37 ? 408  GLU   A HB3  1 
ATOM   6262  H  HG2  . GLU   A 1 408 ? 29.549 20.492  -0.609 1.00 25.25 ? 408  GLU   A HG2  1 
ATOM   6263  H  HG3  . GLU   A 1 408 ? 28.089 20.752  -1.091 1.00 25.25 ? 408  GLU   A HG3  1 
ATOM   6264  N  N    . GLY   A 1 409 ? 29.353 17.385  1.152  1.00 12.01 ? 409  GLY   A N    1 
ATOM   6265  C  CA   . GLY   A 1 409 ? 30.388 16.408  0.769  1.00 15.84 ? 409  GLY   A CA   1 
ATOM   6266  C  C    . GLY   A 1 409 ? 29.801 15.195  0.065  1.00 16.58 ? 409  GLY   A C    1 
ATOM   6267  O  O    . GLY   A 1 409 ? 30.462 14.669  -0.847 1.00 17.04 ? 409  GLY   A O    1 
ATOM   6268  H  H    . GLY   A 1 409 ? 29.308 17.555  1.994  1.00 14.42 ? 409  GLY   A H    1 
ATOM   6269  H  HA2  . GLY   A 1 409 ? 31.035 16.836  0.187  1.00 19.01 ? 409  GLY   A HA2  1 
ATOM   6270  H  HA3  . GLY   A 1 409 ? 30.867 16.119  1.562  1.00 19.01 ? 409  GLY   A HA3  1 
ATOM   6271  N  N    . TYR   A 1 410 ? 28.607 14.767  0.477  1.00 12.46 ? 410  TYR   A N    1 
ATOM   6272  C  CA   . TYR   A 1 410 ? 27.988 13.547  -0.108 1.00 13.85 ? 410  TYR   A CA   1 
ATOM   6273  C  C    . TYR   A 1 410 ? 27.072 13.921  -1.280 1.00 15.40 ? 410  TYR   A C    1 
ATOM   6274  O  O    . TYR   A 1 410 ? 26.428 13.023  -1.839 1.00 16.74 ? 410  TYR   A O    1 
ATOM   6275  C  CB   . TYR   A 1 410 ? 27.248 12.755  0.975  1.00 12.43 ? 410  TYR   A CB   1 
ATOM   6276  C  CG   . TYR   A 1 410 ? 28.178 11.987  1.877  1.00 16.75 ? 410  TYR   A CG   1 
ATOM   6277  C  CD1  . TYR   A 1 410 ? 28.693 10.761  1.490  1.00 17.07 ? 410  TYR   A CD1  1 
ATOM   6278  C  CD2  . TYR   A 1 410 ? 28.576 12.500  3.099  1.00 14.35 ? 410  TYR   A CD2  1 
ATOM   6279  C  CE1  . TYR   A 1 410 ? 29.562 10.054  2.304  1.00 16.99 ? 410  TYR   A CE1  1 
ATOM   6280  C  CE2  . TYR   A 1 410 ? 29.444 11.806  3.925  1.00 15.05 ? 410  TYR   A CE2  1 
ATOM   6281  C  CZ   . TYR   A 1 410 ? 29.940 10.579  3.525  1.00 15.55 ? 410  TYR   A CZ   1 
ATOM   6282  O  OH   . TYR   A 1 410 ? 30.802 9.889   4.339  1.00 20.53 ? 410  TYR   A OH   1 
ATOM   6283  H  H    . TYR   A 1 410 ? 28.136 15.154  1.084  1.00 14.95 ? 410  TYR   A H    1 
ATOM   6284  H  HA   . TYR   A 1 410 ? 28.686 12.973  -0.461 1.00 16.62 ? 410  TYR   A HA   1 
ATOM   6285  H  HB2  . TYR   A 1 410 ? 26.717 13.366  1.510  1.00 14.92 ? 410  TYR   A HB2  1 
ATOM   6286  H  HB3  . TYR   A 1 410 ? 26.631 12.137  0.553  1.00 14.92 ? 410  TYR   A HB3  1 
ATOM   6287  H  HD1  . TYR   A 1 410 ? 28.450 10.405  0.666  1.00 20.48 ? 410  TYR   A HD1  1 
ATOM   6288  H  HD2  . TYR   A 1 410 ? 28.254 13.329  3.371  1.00 17.23 ? 410  TYR   A HD2  1 
ATOM   6289  H  HE1  . TYR   A 1 410 ? 29.890 9.228   2.030  1.00 20.40 ? 410  TYR   A HE1  1 
ATOM   6290  H  HE2  . TYR   A 1 410 ? 29.693 12.164  4.746  1.00 18.06 ? 410  TYR   A HE2  1 
ATOM   6291  H  HH   . TYR   A 1 410 ? 30.977 9.143   3.994  1.00 24.64 ? 410  TYR   A HH   1 
ATOM   6292  N  N    . GLY   A 1 411 ? 27.028 15.207  -1.634 1.00 16.33 ? 411  GLY   A N    1 
ATOM   6293  C  CA   . GLY   A 1 411 ? 26.145 15.657  -2.726 1.00 16.35 ? 411  GLY   A CA   1 
ATOM   6294  C  C    . GLY   A 1 411 ? 24.678 15.476  -2.377 1.00 16.93 ? 411  GLY   A C    1 
ATOM   6295  O  O    . GLY   A 1 411 ? 23.884 15.228  -3.297 1.00 17.11 ? 411  GLY   A O    1 
ATOM   6296  H  H    . GLY   A 1 411 ? 27.492 15.830  -1.264 1.00 19.60 ? 411  GLY   A H    1 
ATOM   6297  H  HA2  . GLY   A 1 411 ? 26.319 16.592  -2.918 1.00 19.62 ? 411  GLY   A HA2  1 
ATOM   6298  H  HA3  . GLY   A 1 411 ? 26.349 15.159  -3.533 1.00 19.62 ? 411  GLY   A HA3  1 
ATOM   6299  N  N    . ALA   A 1 412 ? 24.331 15.612  -1.096 1.00 14.47 ? 412  ALA   A N    1 
ATOM   6300  C  CA   . ALA   A 1 412 ? 22.926 15.469  -0.648 1.00 16.23 ? 412  ALA   A CA   1 
ATOM   6301  C  C    . ALA   A 1 412 ? 22.553 16.630  0.282  1.00 13.54 ? 412  ALA   A C    1 
ATOM   6302  O  O    . ALA   A 1 412 ? 22.167 16.367  1.427  1.00 13.46 ? 412  ALA   A O    1 
ATOM   6303  C  CB   . ALA   A 1 412 ? 22.734 14.141  0.032  1.00 16.36 ? 412  ALA   A CB   1 
ATOM   6304  H  H    . ALA   A 1 412 ? 24.888 15.787  -0.465 1.00 17.37 ? 412  ALA   A H    1 
ATOM   6305  H  HA   . ALA   A 1 412 ? 22.338 15.499  -1.419 1.00 19.48 ? 412  ALA   A HA   1 
ATOM   6306  H  HB1  . ALA   A 1 412 ? 21.812 14.056  0.322  1.00 19.64 ? 412  ALA   A HB1  1 
ATOM   6307  H  HB2  . ALA   A 1 412 ? 22.945 13.426  -0.589 1.00 19.64 ? 412  ALA   A HB2  1 
ATOM   6308  H  HB3  . ALA   A 1 412 ? 23.321 14.084  0.802  1.00 19.64 ? 412  ALA   A HB3  1 
ATOM   6309  N  N    . PRO   A 1 413 ? 22.622 17.898  -0.178 1.00 15.25 ? 413  PRO   A N    1 
ATOM   6310  C  CA   . PRO   A 1 413 ? 22.352 19.051  0.688  1.00 15.19 ? 413  PRO   A CA   1 
ATOM   6311  C  C    . PRO   A 1 413 ? 20.914 19.057  1.216  1.00 13.58 ? 413  PRO   A C    1 
ATOM   6312  O  O    . PRO   A 1 413 ? 20.656 19.725  2.188  1.00 14.80 ? 413  PRO   A O    1 
ATOM   6313  C  CB   . PRO   A 1 413 ? 22.558 20.259  -0.242 1.00 14.86 ? 413  PRO   A CB   1 
ATOM   6314  C  CG   . PRO   A 1 413 ? 22.361 19.705  -1.631 1.00 15.87 ? 413  PRO   A CG   1 
ATOM   6315  C  CD   . PRO   A 1 413 ? 22.938 18.310  -1.553 1.00 15.56 ? 413  PRO   A CD   1 
ATOM   6316  H  HA   . PRO   A 1 413 ? 22.924 19.048  1.471  1.00 18.23 ? 413  PRO   A HA   1 
ATOM   6317  H  HB2  . PRO   A 1 413 ? 21.921 20.965  -0.050 1.00 17.84 ? 413  PRO   A HB2  1 
ATOM   6318  H  HB3  . PRO   A 1 413 ? 23.444 20.639  -0.136 1.00 17.84 ? 413  PRO   A HB3  1 
ATOM   6319  H  HG2  . PRO   A 1 413 ? 21.423 19.688  -1.877 1.00 19.05 ? 413  PRO   A HG2  1 
ATOM   6320  H  HG3  . PRO   A 1 413 ? 22.819 20.242  -2.296 1.00 19.05 ? 413  PRO   A HG3  1 
ATOM   6321  H  HD2  . PRO   A 1 413 ? 22.535 17.718  -2.207 1.00 18.68 ? 413  PRO   A HD2  1 
ATOM   6322  H  HD3  . PRO   A 1 413 ? 23.894 18.307  -1.718 1.00 18.68 ? 413  PRO   A HD3  1 
ATOM   6323  N  N    . GLU   A 1 414 ? 20.033 18.285  0.581  1.00 15.50 ? 414  GLU   A N    1 
ATOM   6324  C  CA   . GLU   A 1 414 ? 18.596 18.292  0.966  1.00 14.68 ? 414  GLU   A CA   1 
ATOM   6325  C  C    . GLU   A 1 414 ? 18.385 17.675  2.355  1.00 15.38 ? 414  GLU   A C    1 
ATOM   6326  O  O    . GLU   A 1 414 ? 17.280 17.828  2.886  1.00 14.92 ? 414  GLU   A O    1 
ATOM   6327  C  CB   . GLU   A 1 414 ? 17.761 17.540  -0.077 1.00 18.77 ? 414  GLU   A CB   1 
ATOM   6328  C  CG   . GLU   A 1 414 ? 18.184 16.097  -0.262 1.00 18.25 ? 414  GLU   A CG   1 
ATOM   6329  C  CD   . GLU   A 1 414 ? 19.116 15.857  -1.437 1.00 19.12 ? 414  GLU   A CD   1 
ATOM   6330  O  OE1  . GLU   A 1 414 ? 20.057 16.650  -1.613 1.00 17.64 ? 414  GLU   A OE1  1 
ATOM   6331  O  OE2  . GLU   A 1 414 ? 18.893 14.878  -2.172 1.00 21.50 ? 414  GLU   A OE2  1 
ATOM   6332  H  H    . GLU   A 1 414 ? 20.230 17.754  -0.066 1.00 18.60 ? 414  GLU   A H    1 
ATOM   6333  H  HA   . GLU   A 1 414 ? 18.304 19.216  1.001  1.00 17.62 ? 414  GLU   A HA   1 
ATOM   6334  H  HB2  . GLU   A 1 414 ? 16.828 17.565  0.187  1.00 22.53 ? 414  GLU   A HB2  1 
ATOM   6335  H  HB3  . GLU   A 1 414 ? 17.828 18.001  -0.928 1.00 22.53 ? 414  GLU   A HB3  1 
ATOM   6336  H  HG2  . GLU   A 1 414 ? 18.621 15.794  0.549  1.00 21.91 ? 414  GLU   A HG2  1 
ATOM   6337  H  HG3  . GLU   A 1 414 ? 17.390 15.552  -0.377 1.00 21.91 ? 414  GLU   A HG3  1 
ATOM   6338  N  N    . TYR   A 1 415 ? 19.397 17.009  2.912  1.00 14.04 ? 415  TYR   A N    1 
ATOM   6339  C  CA   . TYR   A 1 415 ? 19.201 16.309  4.213  1.00 14.07 ? 415  TYR   A CA   1 
ATOM   6340  C  C    . TYR   A 1 415 ? 19.794 17.146  5.354  1.00 14.08 ? 415  TYR   A C    1 
ATOM   6341  O  O    . TYR   A 1 415 ? 19.756 16.690  6.504  1.00 13.23 ? 415  TYR   A O    1 
ATOM   6342  C  CB   . TYR   A 1 415 ? 19.715 14.870  4.110  1.00 14.34 ? 415  TYR   A CB   1 
ATOM   6343  C  CG   . TYR   A 1 415 ? 18.986 14.110  3.033  1.00 13.12 ? 415  TYR   A CG   1 
ATOM   6344  C  CD1  . TYR   A 1 415 ? 17.608 13.991  3.067  1.00 14.48 ? 415  TYR   A CD1  1 
ATOM   6345  C  CD2  . TYR   A 1 415 ? 19.658 13.575  1.949  1.00 12.49 ? 415  TYR   A CD2  1 
ATOM   6346  C  CE1  . TYR   A 1 415 ? 16.916 13.323  2.072  1.00 16.13 ? 415  TYR   A CE1  1 
ATOM   6347  C  CE2  . TYR   A 1 415 ? 18.982 12.903  0.945  1.00 18.28 ? 415  TYR   A CE2  1 
ATOM   6348  C  CZ   . TYR   A 1 415 ? 17.607 12.778  1.006  1.00 16.86 ? 415  TYR   A CZ   1 
ATOM   6349  O  OH   . TYR   A 1 415 ? 16.928 12.115  0.015  1.00 19.71 ? 415  TYR   A OH   1 
ATOM   6350  H  H    . TYR   A 1 415 ? 20.186 16.943  2.576  1.00 16.85 ? 415  TYR   A H    1 
ATOM   6351  H  HA   . TYR   A 1 415 ? 18.259 16.226  4.430  1.00 16.89 ? 415  TYR   A HA   1 
ATOM   6352  H  HB2  . TYR   A 1 415 ? 20.666 14.876  3.919  1.00 17.21 ? 415  TYR   A HB2  1 
ATOM   6353  H  HB3  . TYR   A 1 415 ? 19.600 14.420  4.962  1.00 17.21 ? 415  TYR   A HB3  1 
ATOM   6354  H  HD1  . TYR   A 1 415 ? 17.136 14.368  3.774  1.00 17.37 ? 415  TYR   A HD1  1 
ATOM   6355  H  HD2  . TYR   A 1 415 ? 20.582 13.668  1.893  1.00 14.99 ? 415  TYR   A HD2  1 
ATOM   6356  H  HE1  . TYR   A 1 415 ? 15.991 13.241  2.120  1.00 19.36 ? 415  TYR   A HE1  1 
ATOM   6357  H  HE2  . TYR   A 1 415 ? 19.452 12.537  0.231  1.00 21.94 ? 415  TYR   A HE2  1 
ATOM   6358  H  HH   . TYR   A 1 415 ? 16.116 12.330  0.039  1.00 23.65 ? 415  TYR   A HH   1 
ATOM   6359  N  N    . SER   A 1 416 ? 20.294 18.340  5.031  1.00 12.89 ? 416  SER   A N    1 
ATOM   6360  C  CA   . SER   A 1 416 ? 20.782 19.251  6.100  1.00 11.19 ? 416  SER   A CA   1 
ATOM   6361  C  C    . SER   A 1 416 ? 19.638 20.196  6.479  1.00 10.89 ? 416  SER   A C    1 
ATOM   6362  O  O    . SER   A 1 416 ? 19.283 21.050  5.659  1.00 11.36 ? 416  SER   A O    1 
ATOM   6363  C  CB   . SER   A 1 416 ? 22.009 20.024  5.678  1.00 14.49 ? 416  SER   A CB   1 
ATOM   6364  O  OG   . SER   A 1 416 ? 22.316 21.039  6.619  1.00 10.37 ? 416  SER   A OG   1 
ATOM   6365  H  H    . SER   A 1 416 ? 20.363 18.644  4.229  1.00 15.47 ? 416  SER   A H    1 
ATOM   6366  H  HA   . SER   A 1 416 ? 21.051 18.723  6.868  1.00 13.43 ? 416  SER   A HA   1 
ATOM   6367  H  HB2  . SER   A 1 416 ? 22.763 19.420  5.591  1.00 17.40 ? 416  SER   A HB2  1 
ATOM   6368  H  HB3  . SER   A 1 416 ? 21.862 20.421  4.805  1.00 17.40 ? 416  SER   A HB3  1 
ATOM   6369  H  HG   . SER   A 1 416 ? 22.612 20.689  7.323  1.00 12.44 ? 416  SER   A HG   1 
ATOM   6370  N  N    . MET   A 1 417 ? 19.072 20.010  7.670  1.00 10.63 ? 417  MET   A N    1 
ATOM   6371  C  CA   . MET   A 1 417 ? 17.962 20.880  8.134  1.00 10.51 ? 417  MET   A CA   1 
ATOM   6372  C  C    . MET   A 1 417 ? 18.579 22.157  8.708  1.00 9.68  ? 417  MET   A C    1 
ATOM   6373  O  O    . MET   A 1 417 ? 18.580 22.324  9.933  1.00 10.64 ? 417  MET   A O    1 
ATOM   6374  C  CB   . MET   A 1 417 ? 17.096 20.147  9.158  1.00 10.25 ? 417  MET   A CB   1 
ATOM   6375  C  CG   . MET   A 1 417 ? 16.380 18.941  8.558  1.00 13.06 ? 417  MET   A CG   1 
ATOM   6376  S  SD   . MET   A 1 417 ? 15.301 19.340  7.142  1.00 11.14 ? 417  MET   A SD   1 
ATOM   6377  C  CE   . MET   A 1 417 ? 16.201 18.581  5.790  1.00 14.20 ? 417  MET   A CE   1 
ATOM   6378  H  H    . MET   A 1 417 ? 19.305 19.397  8.226  1.00 12.76 ? 417  MET   A H    1 
ATOM   6379  H  HA   . MET   A 1 417 ? 17.375 21.112  7.398  1.00 12.62 ? 417  MET   A HA   1 
ATOM   6380  H  HB2  . MET   A 1 417 ? 17.652 19.855  9.898  1.00 12.31 ? 417  MET   A HB2  1 
ATOM   6381  H  HB3  . MET   A 1 417 ? 16.440 20.762  9.522  1.00 12.31 ? 417  MET   A HB3  1 
ATOM   6382  H  HG2  . MET   A 1 417 ? 17.043 18.292  8.274  1.00 15.67 ? 417  MET   A HG2  1 
ATOM   6383  H  HG3  . MET   A 1 417 ? 15.847 18.518  9.249  1.00 15.67 ? 417  MET   A HG3  1 
ATOM   6384  H  HE1  . MET   A 1 417 ? 15.720 18.725  4.960  1.00 17.05 ? 417  MET   A HE1  1 
ATOM   6385  H  HE2  . MET   A 1 417 ? 17.084 18.978  5.725  1.00 17.05 ? 417  MET   A HE2  1 
ATOM   6386  H  HE3  . MET   A 1 417 ? 16.287 17.629  5.952  1.00 17.05 ? 417  MET   A HE3  1 
ATOM   6387  N  N    . THR   A 1 418 ? 19.068 23.018  7.816  1.00 10.68 ? 418  THR   A N    1 
ATOM   6388  C  CA   . THR   A 1 418 ? 19.773 24.243  8.249  1.00 10.05 ? 418  THR   A CA   1 
ATOM   6389  C  C    . THR   A 1 418 ? 19.321 25.478  7.474  1.00 10.63 ? 418  THR   A C    1 
ATOM   6390  O  O    . THR   A 1 418 ? 18.725 25.314  6.399  1.00 10.56 ? 418  THR   A O    1 
ATOM   6391  C  CB   . THR   A 1 418 ? 21.262 24.138  7.907  1.00 10.27 ? 418  THR   A CB   1 
ATOM   6392  O  OG1  . THR   A 1 418 ? 21.387 23.618  6.584  1.00 10.33 ? 418  THR   A OG1  1 
ATOM   6393  C  CG2  . THR   A 1 418 ? 22.024 23.249  8.866  1.00 11.79 ? 418  THR   A CG2  1 
ATOM   6394  H  H    . THR   A 1 418 ? 19.007 22.920  6.964  1.00 12.82 ? 418  THR   A H    1 
ATOM   6395  H  HA   . THR   A 1 418 ? 19.588 24.325  9.198  1.00 12.06 ? 418  THR   A HA   1 
ATOM   6396  H  HB   . THR   A 1 418 ? 21.645 25.026  7.978  1.00 12.33 ? 418  THR   A HB   1 
ATOM   6397  H  HG1  . THR   A 1 418 ? 21.673 22.829  6.619  1.00 12.40 ? 418  THR   A HG1  1 
ATOM   6398  H  HG21 . THR   A 1 418 ? 22.958 23.217  8.605  1.00 14.16 ? 418  THR   A HG21 1 
ATOM   6399  H  HG22 . THR   A 1 418 ? 21.952 23.606  9.765  1.00 14.16 ? 418  THR   A HG22 1 
ATOM   6400  H  HG23 . THR   A 1 418 ? 21.652 22.354  8.843  1.00 14.16 ? 418  THR   A HG23 1 
ATOM   6401  N  N    . VAL   A 1 419 ? 19.560 26.659  8.037  1.00 10.60 ? 419  VAL   A N    1 
ATOM   6402  C  CA   . VAL   A 1 419 ? 19.332 27.932  7.301  1.00 10.31 ? 419  VAL   A CA   1 
ATOM   6403  C  C    . VAL   A 1 419 ? 20.647 28.702  7.466  1.00 11.47 ? 419  VAL   A C    1 
ATOM   6404  O  O    . VAL   A 1 419 ? 21.111 28.816  8.606  1.00 10.53 ? 419  VAL   A O    1 
ATOM   6405  C  CB   . VAL   A 1 419 ? 18.124 28.730  7.824  1.00 8.53  ? 419  VAL   A CB   1 
ATOM   6406  C  CG1  . VAL   A 1 419 ? 17.917 30.013  7.036  1.00 11.74 ? 419  VAL   A CG1  1 
ATOM   6407  C  CG2  . VAL   A 1 419 ? 16.854 27.894  7.837  1.00 8.62  ? 419  VAL   A CG2  1 
ATOM   6408  H  H    . VAL   A 1 419 ? 19.853 26.759  8.839  1.00 12.72 ? 419  VAL   A H    1 
ATOM   6409  H  HA   . VAL   A 1 419 ? 19.109 27.769  6.371  1.00 12.38 ? 419  VAL   A HA   1 
ATOM   6410  H  HB   . VAL   A 1 419 ? 18.326 28.972  8.741  1.00 10.24 ? 419  VAL   A HB   1 
ATOM   6411  H  HG11 . VAL   A 1 419 ? 17.150 30.490  7.390  1.00 14.09 ? 419  VAL   A HG11 1 
ATOM   6412  H  HG12 . VAL   A 1 419 ? 18.707 30.570  7.111  1.00 14.09 ? 419  VAL   A HG12 1 
ATOM   6413  H  HG13 . VAL   A 1 419 ? 17.761 29.798  6.103  1.00 14.09 ? 419  VAL   A HG13 1 
ATOM   6414  H  HG21 . VAL   A 1 419 ? 16.117 28.429  8.172  1.00 10.35 ? 419  VAL   A HG21 1 
ATOM   6415  H  HG22 . VAL   A 1 419 ? 16.653 27.596  6.936  1.00 10.35 ? 419  VAL   A HG22 1 
ATOM   6416  H  HG23 . VAL   A 1 419 ? 16.980 27.123  8.412  1.00 10.35 ? 419  VAL   A HG23 1 
ATOM   6417  N  N    . LYS   A 1 420 ? 21.245 29.155  6.367  1.00 9.99  ? 420  LYS   A N    1 
ATOM   6418  C  CA   . LYS   A 1 420 ? 22.577 29.813  6.455  1.00 10.42 ? 420  LYS   A CA   1 
ATOM   6419  C  C    . LYS   A 1 420 ? 23.562 28.857  7.141  1.00 10.40 ? 420  LYS   A C    1 
ATOM   6420  O  O    . LYS   A 1 420 ? 24.431 29.353  7.874  1.00 8.89  ? 420  LYS   A O    1 
ATOM   6421  C  CB   . LYS   A 1 420 ? 22.462 31.185  7.128  1.00 10.79 ? 420  LYS   A CB   1 
ATOM   6422  C  CG   . LYS   A 1 420 ? 21.529 32.156  6.415  1.00 12.60 ? 420  LYS   A CG   1 
ATOM   6423  C  CD   . LYS   A 1 420 ? 21.259 33.432  7.178  1.00 11.88 ? 420  LYS   A CD   1 
ATOM   6424  C  CE   . LYS   A 1 420 ? 20.311 34.358  6.446  1.00 13.18 ? 420  LYS   A CE   1 
ATOM   6425  N  NZ   . LYS   A 1 420 ? 18.960 33.766  6.308  1.00 11.44 ? 420  LYS   A NZ   1 
ATOM   6426  H  H    . LYS   A 1 420 ? 20.917 29.100  5.574  1.00 11.99 ? 420  LYS   A H    1 
ATOM   6427  H  HA   . LYS   A 1 420 ? 22.928 29.995  5.569  1.00 12.51 ? 420  LYS   A HA   1 
ATOM   6428  H  HB2  . LYS   A 1 420 ? 22.150 31.062  8.038  1.00 12.95 ? 420  LYS   A HB2  1 
ATOM   6429  H  HB3  . LYS   A 1 420 ? 23.345 31.582  7.182  1.00 12.95 ? 420  LYS   A HB3  1 
ATOM   6430  H  HG2  . LYS   A 1 420 ? 21.912 32.382  5.553  1.00 15.13 ? 420  LYS   A HG2  1 
ATOM   6431  H  HG3  . LYS   A 1 420 ? 20.685 31.710  6.243  1.00 15.13 ? 420  LYS   A HG3  1 
ATOM   6432  H  HD2  . LYS   A 1 420 ? 20.886 33.213  8.046  1.00 14.25 ? 420  LYS   A HD2  1 
ATOM   6433  H  HD3  . LYS   A 1 420 ? 22.097 33.893  7.338  1.00 14.25 ? 420  LYS   A HD3  1 
ATOM   6434  H  HE2  . LYS   A 1 420 ? 20.248 35.200  6.924  1.00 15.82 ? 420  LYS   A HE2  1 
ATOM   6435  H  HE3  . LYS   A 1 420 ? 20.668 34.557  5.566  1.00 15.82 ? 420  LYS   A HE3  1 
ATOM   6436  H  HZ1  . LYS   A 1 420 ? 18.385 34.394  6.049  1.00 13.73 ? 420  LYS   A HZ1  1 
ATOM   6437  H  HZ2  . LYS   A 1 420 ? 18.981 33.116  5.701  1.00 13.73 ? 420  LYS   A HZ2  1 
ATOM   6438  H  HZ3  . LYS   A 1 420 ? 18.701 33.432  7.091  1.00 13.73 ? 420  LYS   A HZ3  1 
ATOM   6439  N  N    . LYS   A 1 421 ? 23.407 27.551  6.918  1.00 9.85  ? 421  LYS   A N    1 
ATOM   6440  C  CA   . LYS   A 1 421 ? 24.353 26.518  7.434  1.00 9.72  ? 421  LYS   A CA   1 
ATOM   6441  C  C    . LYS   A 1 421 ? 24.236 26.322  8.948  1.00 11.10 ? 421  LYS   A C    1 
ATOM   6442  O  O    . LYS   A 1 421 ? 25.101 25.624  9.499  1.00 11.04 ? 421  LYS   A O    1 
ATOM   6443  C  CB   . LYS   A 1 421 ? 25.797 26.834  7.025  1.00 11.57 ? 421  LYS   A CB   1 
ATOM   6444  C  CG   . LYS   A 1 421 ? 25.986 27.262  5.576  1.00 14.40 ? 421  LYS   A CG   1 
ATOM   6445  C  CD   . LYS   A 1 421 ? 27.425 27.565  5.227  1.00 15.03 ? 421  LYS   A CD   1 
ATOM   6446  C  CE   . LYS   A 1 421 ? 27.589 28.112  3.825  1.00 20.11 ? 421  LYS   A CE   1 
ATOM   6447  N  NZ   . LYS   A 1 421 ? 29.004 28.432  3.524  1.00 25.52 ? 421  LYS   A NZ   1 
ATOM   6448  H  H    . LYS   A 1 421 ? 22.753 27.225  6.464  1.00 11.83 ? 421  LYS   A H    1 
ATOM   6449  H  HA   . LYS   A 1 421 ? 24.100 25.677  7.023  1.00 11.67 ? 421  LYS   A HA   1 
ATOM   6450  H  HB2  . LYS   A 1 421 ? 26.134 27.538  7.601  1.00 13.89 ? 421  LYS   A HB2  1 
ATOM   6451  H  HB3  . LYS   A 1 421 ? 26.343 26.049  7.188  1.00 13.89 ? 421  LYS   A HB3  1 
ATOM   6452  H  HG2  . LYS   A 1 421 ? 25.659 26.560  4.992  1.00 17.29 ? 421  LYS   A HG2  1 
ATOM   6453  H  HG3  . LYS   A 1 421 ? 25.445 28.049  5.404  1.00 17.29 ? 421  LYS   A HG3  1 
ATOM   6454  H  HD2  . LYS   A 1 421 ? 27.779 28.206  5.863  1.00 18.04 ? 421  LYS   A HD2  1 
ATOM   6455  H  HD3  . LYS   A 1 421 ? 27.952 26.756  5.317  1.00 18.04 ? 421  LYS   A HD3  1 
ATOM   6456  H  HE2  . LYS   A 1 421 ? 27.260 27.463  3.184  1.00 24.14 ? 421  LYS   A HE2  1 
ATOM   6457  H  HE3  . LYS   A 1 421 ? 27.048 28.910  3.723  1.00 24.14 ? 421  LYS   A HE3  1 
ATOM   6458  H  HZ1  . LYS   A 1 421 ? 29.061 28.791  2.712  1.00 30.63 ? 421  LYS   A HZ1  1 
ATOM   6459  H  HZ2  . LYS   A 1 421 ? 29.312 29.011  4.126  1.00 30.63 ? 421  LYS   A HZ2  1 
ATOM   6460  H  HZ3  . LYS   A 1 421 ? 29.490 27.687  3.554  1.00 30.63 ? 421  LYS   A HZ3  1 
ATOM   6461  N  N    . GLN   A 1 422 ? 23.192 26.862  9.575  1.00 11.58 ? 422  GLN   A N    1 
ATOM   6462  C  CA   . GLN   A 1 422 ? 23.010 26.595  11.027 1.00 10.54 ? 422  GLN   A CA   1 
ATOM   6463  C  C    . GLN   A 1 422 ? 21.765 25.721  11.229 1.00 9.00  ? 422  GLN   A C    1 
ATOM   6464  O  O    . GLN   A 1 422 ? 20.740 26.003  10.597 1.00 9.27  ? 422  GLN   A O    1 
ATOM   6465  C  CB   . GLN   A 1 422 ? 23.002 27.876  11.860 1.00 9.41  ? 422  GLN   A CB   1 
ATOM   6466  C  CG   . GLN   A 1 422 ? 22.952 27.604  13.357 1.00 11.15 ? 422  GLN   A CG   1 
ATOM   6467  C  CD   . GLN   A 1 422 ? 23.302 28.823  14.172 1.00 10.38 ? 422  GLN   A CD   1 
ATOM   6468  O  OE1  . GLN   A 1 422 ? 24.470 29.141  14.376 1.00 9.95  ? 422  GLN   A OE1  1 
ATOM   6469  N  NE2  . GLN   A 1 422 ? 22.281 29.522  14.641 1.00 11.36 ? 422  GLN   A NE2  1 
ATOM   6470  H  H    . GLN   A 1 422 ? 22.597 27.364  9.210  1.00 13.90 ? 422  GLN   A H    1 
ATOM   6471  H  HA   . GLN   A 1 422 ? 23.776 26.100  11.357 1.00 12.65 ? 422  GLN   A HA   1 
ATOM   6472  H  HB2  . GLN   A 1 422 ? 23.796 28.395  11.656 1.00 11.29 ? 422  GLN   A HB2  1 
ATOM   6473  H  HB3  . GLN   A 1 422 ? 22.237 28.416  11.608 1.00 11.29 ? 422  GLN   A HB3  1 
ATOM   6474  H  HG2  . GLN   A 1 422 ? 22.063 27.300  13.599 1.00 13.39 ? 422  GLN   A HG2  1 
ATOM   6475  H  HG3  . GLN   A 1 422 ? 23.566 26.885  13.574 1.00 13.39 ? 422  GLN   A HG3  1 
ATOM   6476  H  HE21 . GLN   A 1 422 ? 21.475 29.269  14.478 1.00 13.63 ? 422  GLN   A HE21 1 
ATOM   6477  H  HE22 . GLN   A 1 422 ? 22.423 30.229  15.109 1.00 13.63 ? 422  GLN   A HE22 1 
ATOM   6478  N  N    . GLU   A 1 423 ? 21.867 24.722  12.107 1.00 9.03  ? 423  GLU   A N    1 
ATOM   6479  C  CA   . GLU   A 1 423 ? 20.779 23.725  12.280 1.00 8.33  ? 423  GLU   A CA   1 
ATOM   6480  C  C    . GLU   A 1 423 ? 19.516 24.321  12.908 1.00 10.11 ? 423  GLU   A C    1 
ATOM   6481  O  O    . GLU   A 1 423 ? 19.626 25.004  13.935 1.00 9.98  ? 423  GLU   A O    1 
ATOM   6482  C  CB   . GLU   A 1 423 ? 21.320 22.552  13.102 1.00 8.52  ? 423  GLU   A CB   1 
ATOM   6483  C  CG   . GLU   A 1 423 ? 22.204 21.613  12.303 1.00 12.04 ? 423  GLU   A CG   1 
ATOM   6484  C  CD   . GLU   A 1 423 ? 23.565 22.170  11.921 1.00 9.38  ? 423  GLU   A CD   1 
ATOM   6485  O  OE1  . GLU   A 1 423 ? 23.964 23.198  12.496 1.00 10.50 ? 423  GLU   A OE1  1 
ATOM   6486  O  OE2  . GLU   A 1 423 ? 24.219 21.574  11.046 1.00 11.20 ? 423  GLU   A OE2  1 
ATOM   6487  H  H    . GLU   A 1 423 ? 22.550 24.595  12.614 1.00 10.84 ? 423  GLU   A H    1 
ATOM   6488  H  HA   . GLU   A 1 423 ? 20.504 23.415  11.403 1.00 10.00 ? 423  GLU   A HA   1 
ATOM   6489  H  HB2  . GLU   A 1 423 ? 21.825 22.899  13.854 1.00 10.23 ? 423  GLU   A HB2  1 
ATOM   6490  H  HB3  . GLU   A 1 423 ? 20.574 22.051  13.467 1.00 10.23 ? 423  GLU   A HB3  1 
ATOM   6491  H  HG2  . GLU   A 1 423 ? 22.336 20.801  12.817 1.00 14.45 ? 423  GLU   A HG2  1 
ATOM   6492  H  HG3  . GLU   A 1 423 ? 21.734 21.362  11.492 1.00 14.45 ? 423  GLU   A HG3  1 
ATOM   6493  N  N    . ILE   A 1 424 ? 18.364 24.044  12.292 1.00 8.99  ? 424  ILE   A N    1 
ATOM   6494  C  CA   . ILE   A 1 424 ? 17.052 24.501  12.825 1.00 7.99  ? 424  ILE   A CA   1 
ATOM   6495  C  C    . ILE   A 1 424 ? 16.757 23.720  14.109 1.00 10.57 ? 424  ILE   A C    1 
ATOM   6496  O  O    . ILE   A 1 424 ? 17.042 22.516  14.137 1.00 11.76 ? 424  ILE   A O    1 
ATOM   6497  C  CB   . ILE   A 1 424 ? 15.963 24.269  11.758 1.00 12.11 ? 424  ILE   A CB   1 
ATOM   6498  C  CG1  . ILE   A 1 424 ? 16.165 25.168  10.536 1.00 14.61 ? 424  ILE   A CG1  1 
ATOM   6499  C  CG2  . ILE   A 1 424 ? 14.573 24.424  12.352 1.00 14.50 ? 424  ILE   A CG2  1 
ATOM   6500  C  CD1  . ILE   A 1 424 ? 15.485 24.657  9.288  1.00 15.43 ? 424  ILE   A CD1  1 
ATOM   6501  H  H    . ILE   A 1 424 ? 18.310 23.592  11.562 1.00 10.79 ? 424  ILE   A H    1 
ATOM   6502  H  HA   . ILE   A 1 424 ? 17.069 25.448  13.032 1.00 9.59  ? 424  ILE   A HA   1 
ATOM   6503  H  HB   . ILE   A 1 424 ? 16.047 23.354  11.448 1.00 14.54 ? 424  ILE   A HB   1 
ATOM   6504  H  HG12 . ILE   A 1 424 ? 15.829 26.055  10.738 1.00 17.53 ? 424  ILE   A HG12 1 
ATOM   6505  H  HG13 . ILE   A 1 424 ? 17.115 25.257  10.364 1.00 17.53 ? 424  ILE   A HG13 1 
ATOM   6506  H  HG21 . ILE   A 1 424 ? 13.908 24.274  11.662 1.00 17.40 ? 424  ILE   A HG21 1 
ATOM   6507  H  HG22 . ILE   A 1 424 ? 14.451 23.777  13.065 1.00 17.40 ? 424  ILE   A HG22 1 
ATOM   6508  H  HG23 . ILE   A 1 424 ? 14.471 25.320  12.709 1.00 17.40 ? 424  ILE   A HG23 1 
ATOM   6509  H  HD11 . ILE   A 1 424 ? 15.652 25.270  8.555  1.00 18.52 ? 424  ILE   A HD11 1 
ATOM   6510  H  HD12 . ILE   A 1 424 ? 15.836 23.781  9.063  1.00 18.52 ? 424  ILE   A HD12 1 
ATOM   6511  H  HD13 . ILE   A 1 424 ? 14.530 24.592  9.443  1.00 18.52 ? 424  ILE   A HD13 1 
ATOM   6512  N  N    . PRO   A 1 425 ? 16.208 24.359  15.162 1.00 11.10 ? 425  PRO   A N    1 
ATOM   6513  C  CA   . PRO   A 1 425 ? 15.964 23.682  16.436 1.00 10.50 ? 425  PRO   A CA   1 
ATOM   6514  C  C    . PRO   A 1 425 ? 14.668 22.863  16.554 1.00 10.89 ? 425  PRO   A C    1 
ATOM   6515  O  O    . PRO   A 1 425 ? 14.128 22.510  15.531 1.00 11.11 ? 425  PRO   A O    1 
ATOM   6516  C  CB   . PRO   A 1 425 ? 16.028 24.834  17.457 1.00 10.53 ? 425  PRO   A CB   1 
ATOM   6517  C  CG   . PRO   A 1 425 ? 15.545 26.042  16.684 1.00 12.26 ? 425  PRO   A CG   1 
ATOM   6518  C  CD   . PRO   A 1 425 ? 15.903 25.790  15.232 1.00 13.23 ? 425  PRO   A CD   1 
ATOM   6519  H  HA   . PRO   A 1 425 ? 16.620 22.981  16.572 1.00 12.60 ? 425  PRO   A HA   1 
ATOM   6520  H  HB2  . PRO   A 1 425 ? 15.465 24.657  18.227 1.00 12.64 ? 425  PRO   A HB2  1 
ATOM   6521  H  HB3  . PRO   A 1 425 ? 16.930 24.963  17.789 1.00 12.64 ? 425  PRO   A HB3  1 
ATOM   6522  H  HG2  . PRO   A 1 425 ? 14.588 26.160  16.789 1.00 14.72 ? 425  PRO   A HG2  1 
ATOM   6523  H  HG3  . PRO   A 1 425 ? 15.968 26.852  17.009 1.00 14.72 ? 425  PRO   A HG3  1 
ATOM   6524  H  HD2  . PRO   A 1 425 ? 15.168 26.022  14.643 1.00 15.88 ? 425  PRO   A HD2  1 
ATOM   6525  H  HD3  . PRO   A 1 425 ? 16.664 26.326  14.960 1.00 15.88 ? 425  PRO   A HD3  1 
ATOM   6526  N  N    . ALA   A 1 426 ? 14.184 22.640  17.773 1.00 11.21 ? 426  ALA   A N    1 
ATOM   6527  C  CA   . ALA   A 1 426 ? 13.086 21.668  18.019 1.00 12.29 ? 426  ALA   A CA   1 
ATOM   6528  C  C    . ALA   A 1 426 ? 11.659 22.169  17.752 1.00 9.73  ? 426  ALA   A C    1 
ATOM   6529  O  O    . ALA   A 1 426 ? 10.795 21.908  18.595 1.00 10.85 ? 426  ALA   A O    1 
ATOM   6530  C  CB   . ALA   A 1 426 ? 13.225 21.199  19.441 1.00 10.45 ? 426  ALA   A CB   1 
ATOM   6531  H  H    . ALA   A 1 426 ? 14.470 23.036  18.481 1.00 13.46 ? 426  ALA   A H    1 
ATOM   6532  H  HA   . ALA   A 1 426 ? 13.191 20.954  17.371 1.00 14.76 ? 426  ALA   A HA   1 
ATOM   6533  H  HB1  . ALA   A 1 426 ? 12.523 20.560  19.641 1.00 12.54 ? 426  ALA   A HB1  1 
ATOM   6534  H  HB2  . ALA   A 1 426 ? 14.090 20.776  19.559 1.00 12.54 ? 426  ALA   A HB2  1 
ATOM   6535  H  HB3  . ALA   A 1 426 ? 13.152 21.958  20.041 1.00 12.54 ? 426  ALA   A HB3  1 
ATOM   6536  N  N    . TYR   A 1 427 ? 11.411 22.792  16.605 1.00 10.74 ? 427  TYR   A N    1 
ATOM   6537  C  CA   . TYR   A 1 427 ? 10.021 23.182  16.251 1.00 12.85 ? 427  TYR   A CA   1 
ATOM   6538  C  C    . TYR   A 1 427 ? 9.865  23.053  14.735 1.00 12.39 ? 427  TYR   A C    1 
ATOM   6539  O  O    . TYR   A 1 427 ? 10.662 23.655  14.007 1.00 10.92 ? 427  TYR   A O    1 
ATOM   6540  C  CB   . TYR   A 1 427 ? 9.666  24.595  16.724 1.00 10.30 ? 427  TYR   A CB   1 
ATOM   6541  C  CG   . TYR   A 1 427 ? 10.187 24.960  18.090 1.00 11.01 ? 427  TYR   A CG   1 
ATOM   6542  C  CD1  . TYR   A 1 427 ? 11.470 25.452  18.255 1.00 9.51  ? 427  TYR   A CD1  1 
ATOM   6543  C  CD2  . TYR   A 1 427 ? 9.398  24.810  19.218 1.00 11.38 ? 427  TYR   A CD2  1 
ATOM   6544  C  CE1  . TYR   A 1 427 ? 11.958 25.783  19.507 1.00 11.45 ? 427  TYR   A CE1  1 
ATOM   6545  C  CE2  . TYR   A 1 427 ? 9.869  25.142  20.476 1.00 10.02 ? 427  TYR   A CE2  1 
ATOM   6546  C  CZ   . TYR   A 1 427 ? 11.155 25.630  20.621 1.00 10.13 ? 427  TYR   A CZ   1 
ATOM   6547  O  OH   . TYR   A 1 427 ? 11.632 25.959  21.865 1.00 12.75 ? 427  TYR   A OH   1 
ATOM   6548  H  H    . TYR   A 1 427 ? 12.008 23.000  16.022 1.00 12.90 ? 427  TYR   A H    1 
ATOM   6549  H  HA   . TYR   A 1 427 ? 9.403  22.590  16.708 1.00 15.43 ? 427  TYR   A HA   1 
ATOM   6550  H  HB2  . TYR   A 1 427 ? 10.011 25.233  16.080 1.00 12.37 ? 427  TYR   A HB2  1 
ATOM   6551  H  HB3  . TYR   A 1 427 ? 8.700  24.688  16.726 1.00 12.37 ? 427  TYR   A HB3  1 
ATOM   6552  H  HD1  . TYR   A 1 427 ? 12.015 25.562  17.510 1.00 11.42 ? 427  TYR   A HD1  1 
ATOM   6553  H  HD2  . TYR   A 1 427 ? 8.533  24.479  19.128 1.00 13.66 ? 427  TYR   A HD2  1 
ATOM   6554  H  HE1  . TYR   A 1 427 ? 12.825 26.108  19.598 1.00 13.75 ? 427  TYR   A HE1  1 
ATOM   6555  H  HE2  . TYR   A 1 427 ? 9.323  25.037  21.221 1.00 12.03 ? 427  TYR   A HE2  1 
ATOM   6556  H  HH   . TYR   A 1 427 ? 12.383 25.602  21.981 1.00 15.30 ? 427  TYR   A HH   1 
ATOM   6557  N  N    . ASP   A 1 428 ? 8.879  22.269  14.292 1.00 10.14 ? 428  ASP   A N    1 
ATOM   6558  C  CA   . ASP   A 1 428 ? 8.628  22.071  12.841 1.00 10.58 ? 428  ASP   A CA   1 
ATOM   6559  C  C    . ASP   A 1 428 ? 7.800  23.246  12.312 1.00 10.91 ? 428  ASP   A C    1 
ATOM   6560  O  O    . ASP   A 1 428 ? 6.633  23.362  12.692 1.00 10.88 ? 428  ASP   A O    1 
ATOM   6561  C  CB   . ASP   A 1 428 ? 7.932  20.730  12.594 1.00 9.70  ? 428  ASP   A CB   1 
ATOM   6562  C  CG   . ASP   A 1 428 ? 7.872  20.324  11.131 1.00 11.53 ? 428  ASP   A CG   1 
ATOM   6563  O  OD1  . ASP   A 1 428 ? 8.012  21.207  10.269 1.00 11.30 ? 428  ASP   A OD1  1 
ATOM   6564  O  OD2  . ASP   A 1 428 ? 7.680  19.124  10.872 1.00 15.88 ? 428  ASP   A OD2  1 
ATOM   6565  H  H    . ASP   A 1 428 ? 8.340  21.840  14.807 1.00 12.18 ? 428  ASP   A H    1 
ATOM   6566  H  HA   . ASP   A 1 428 ? 9.471  22.046  12.362 1.00 12.69 ? 428  ASP   A HA   1 
ATOM   6567  H  HB2  . ASP   A 1 428 ? 8.395  20.039  13.093 1.00 11.64 ? 428  ASP   A HB2  1 
ATOM   6568  H  HB3  . ASP   A 1 428 ? 7.029  20.776  12.945 1.00 11.64 ? 428  ASP   A HB3  1 
ATOM   6569  N  N    . PRO   A 1 429 ? 8.370  24.119  11.456 1.00 9.74  ? 429  PRO   A N    1 
ATOM   6570  C  CA   . PRO   A 1 429 ? 7.648  25.311  11.000 1.00 11.56 ? 429  PRO   A CA   1 
ATOM   6571  C  C    . PRO   A 1 429 ? 6.491  25.008  10.033 1.00 11.67 ? 429  PRO   A C    1 
ATOM   6572  O  O    . PRO   A 1 429 ? 5.696  25.883  9.787  1.00 11.60 ? 429  PRO   A O    1 
ATOM   6573  C  CB   . PRO   A 1 429 ? 8.758  26.101  10.292 1.00 10.06 ? 429  PRO   A CB   1 
ATOM   6574  C  CG   . PRO   A 1 429 ? 9.716  25.047  9.792  1.00 12.25 ? 429  PRO   A CG   1 
ATOM   6575  C  CD   . PRO   A 1 429 ? 9.710  23.994  10.878 1.00 11.58 ? 429  PRO   A CD   1 
ATOM   6576  H  HA   . PRO   A 1 429 ? 7.213  25.776  11.732 1.00 13.87 ? 429  PRO   A HA   1 
ATOM   6577  H  HB2  . PRO   A 1 429 ? 8.403  26.630  9.561  1.00 12.08 ? 429  PRO   A HB2  1 
ATOM   6578  H  HB3  . PRO   A 1 429 ? 9.196  26.716  10.901 1.00 12.08 ? 429  PRO   A HB3  1 
ATOM   6579  H  HG2  . PRO   A 1 429 ? 9.427  24.681  8.942  1.00 14.70 ? 429  PRO   A HG2  1 
ATOM   6580  H  HG3  . PRO   A 1 429 ? 10.605 25.411  9.657  1.00 14.70 ? 429  PRO   A HG3  1 
ATOM   6581  H  HD2  . PRO   A 1 429 ? 9.864  23.107  10.518 1.00 13.90 ? 429  PRO   A HD2  1 
ATOM   6582  H  HD3  . PRO   A 1 429 ? 10.402 24.156  11.538 1.00 13.90 ? 429  PRO   A HD3  1 
ATOM   6583  N  N    . ARG   A 1 430 ? 6.425  23.772  9.538  1.00 10.40 ? 430  ARG   A N    1 
ATOM   6584  C  CA   . ARG   A 1 430 ? 5.313  23.388  8.627  1.00 12.87 ? 430  ARG   A CA   1 
ATOM   6585  C  C    . ARG   A 1 430 ? 3.981  23.600  9.354  1.00 10.43 ? 430  ARG   A C    1 
ATOM   6586  O  O    . ARG   A 1 430 ? 2.983  23.863  8.675  1.00 12.05 ? 430  ARG   A O    1 
ATOM   6587  C  CB   . ARG   A 1 430 ? 5.480  21.945  8.143  1.00 11.23 ? 430  ARG   A CB   1 
ATOM   6588  C  CG   . ARG   A 1 430 ? 6.649  21.737  7.190  1.00 13.27 ? 430  ARG   A CG   1 
ATOM   6589  C  CD   . ARG   A 1 430 ? 6.803  20.292  6.756  1.00 13.40 ? 430  ARG   A CD   1 
ATOM   6590  N  NE   . ARG   A 1 430 ? 7.307  19.440  7.823  1.00 14.04 ? 430  ARG   A NE   1 
ATOM   6591  C  CZ   . ARG   A 1 430 ? 7.881  18.257  7.636  1.00 13.95 ? 430  ARG   A CZ   1 
ATOM   6592  N  NH1  . ARG   A 1 430 ? 7.843  17.682  6.448  1.00 14.81 ? 430  ARG   A NH1  1 
ATOM   6593  N  NH2  . ARG   A 1 430 ? 8.488  17.650  8.641  1.00 13.88 ? 430  ARG   A NH2  1 
ATOM   6594  H  H    . ARG   A 1 430 ? 6.992  23.147  9.704  1.00 12.49 ? 430  ARG   A H    1 
ATOM   6595  H  HA   . ARG   A 1 430 ? 5.326  23.949  7.836  1.00 15.44 ? 430  ARG   A HA   1 
ATOM   6596  H  HB2  . ARG   A 1 430 ? 5.598  21.368  8.914  1.00 13.48 ? 430  ARG   A HB2  1 
ATOM   6597  H  HB3  . ARG   A 1 430 ? 4.663  21.666  7.702  1.00 13.48 ? 430  ARG   A HB3  1 
ATOM   6598  H  HG2  . ARG   A 1 430 ? 6.525  22.294  6.406  1.00 15.93 ? 430  ARG   A HG2  1 
ATOM   6599  H  HG3  . ARG   A 1 430 ? 7.468  22.030  7.620  1.00 15.93 ? 430  ARG   A HG3  1 
ATOM   6600  H  HD2  . ARG   A 1 430 ? 5.945  19.955  6.455  1.00 16.09 ? 430  ARG   A HD2  1 
ATOM   6601  H  HD3  . ARG   A 1 430 ? 7.407  20.248  5.998  1.00 16.09 ? 430  ARG   A HD3  1 
ATOM   6602  H  HE   . ARG   A 1 430 ? 7.228  19.722  8.631  1.00 16.85 ? 430  ARG   A HE   1 
ATOM   6603  H  HH11 . ARG   A 1 430 ? 7.446  18.074  5.793  1.00 17.78 ? 430  ARG   A HH11 1 
ATOM   6604  H  HH12 . ARG   A 1 430 ? 8.215  16.916  6.329  1.00 17.78 ? 430  ARG   A HH12 1 
ATOM   6605  H  HH21 . ARG   A 1 430 ? 8.511  18.021  9.416  1.00 16.66 ? 430  ARG   A HH21 1 
ATOM   6606  H  HH22 . ARG   A 1 430 ? 8.860  16.884  8.519  1.00 16.66 ? 430  ARG   A HH22 1 
ATOM   6607  N  N    . GLY   A 1 431 ? 3.987  23.532  10.688 1.00 9.50  ? 431  GLY   A N    1 
ATOM   6608  C  CA   . GLY   A 1 431 ? 2.755  23.767  11.473 1.00 10.73 ? 431  GLY   A CA   1 
ATOM   6609  C  C    . GLY   A 1 431 ? 2.807  25.021  12.333 1.00 13.56 ? 431  GLY   A C    1 
ATOM   6610  O  O    . GLY   A 1 431 ? 1.981  25.129  13.247 1.00 12.68 ? 431  GLY   A O    1 
ATOM   6611  H  H    . GLY   A 1 431 ? 4.684  23.353  11.160 1.00 11.40 ? 431  GLY   A H    1 
ATOM   6612  H  HA2  . GLY   A 1 431 ? 2.002  23.832  10.866 1.00 12.88 ? 431  GLY   A HA2  1 
ATOM   6613  H  HA3  . GLY   A 1 431 ? 2.594  23.000  12.044 1.00 12.88 ? 431  GLY   A HA3  1 
ATOM   6614  N  N    . ILE   A 1 432 ? 3.745  25.930  12.059 1.00 11.28 ? 432  ILE   A N    1 
ATOM   6615  C  CA   . ILE   A 1 432 ? 3.897  27.174  12.820 1.00 9.65  ? 432  ILE   A CA   1 
ATOM   6616  C  C    . ILE   A 1 432 ? 4.362  28.276  11.868 1.00 9.71  ? 432  ILE   A C    1 
ATOM   6617  O  O    . ILE   A 1 432 ? 5.564  28.520  11.721 1.00 9.93  ? 432  ILE   A O    1 
ATOM   6618  C  CB   . ILE   A 1 432 ? 4.895  27.027  13.989 1.00 11.60 ? 432  ILE   A CB   1 
ATOM   6619  C  CG1  . ILE   A 1 432 ? 4.925  25.607  14.560 1.00 12.88 ? 432  ILE   A CG1  1 
ATOM   6620  C  CG2  . ILE   A 1 432 ? 4.564  28.030  15.103 1.00 10.46 ? 432  ILE   A CG2  1 
ATOM   6621  C  CD1  . ILE   A 1 432 ? 6.076  25.374  15.528 1.00 11.68 ? 432  ILE   A CD1  1 
ATOM   6622  H  H    . ILE   A 1 432 ? 4.315  25.842  11.422 1.00 13.54 ? 432  ILE   A H    1 
ATOM   6623  H  HA   . ILE   A 1 432 ? 3.038  27.400  13.210 1.00 11.59 ? 432  ILE   A HA   1 
ATOM   6624  H  HB   . ILE   A 1 432 ? 5.777  27.214  13.631 1.00 13.93 ? 432  ILE   A HB   1 
ATOM   6625  H  HG12 . ILE   A 1 432 ? 4.087  25.430  15.015 1.00 15.46 ? 432  ILE   A HG12 1 
ATOM   6626  H  HG13 . ILE   A 1 432 ? 4.991  24.972  13.829 1.00 15.46 ? 432  ILE   A HG13 1 
ATOM   6627  H  HG21 . ILE   A 1 432 ? 5.198  27.927  15.830 1.00 12.56 ? 432  ILE   A HG21 1 
ATOM   6628  H  HG22 . ILE   A 1 432 ? 4.619  28.933  14.753 1.00 12.56 ? 432  ILE   A HG22 1 
ATOM   6629  H  HG23 . ILE   A 1 432 ? 3.666  27.865  15.431 1.00 12.56 ? 432  ILE   A HG23 1 
ATOM   6630  H  HD11 . ILE   A 1 432 ? 6.044  24.462  15.856 1.00 14.02 ? 432  ILE   A HD11 1 
ATOM   6631  H  HD12 . ILE   A 1 432 ? 6.919  25.524  15.071 1.00 14.02 ? 432  ILE   A HD12 1 
ATOM   6632  H  HD13 . ILE   A 1 432 ? 6.000  25.988  16.275 1.00 14.02 ? 432  ILE   A HD13 1 
ATOM   6633  N  N    . GLN   A 1 433 ? 3.423  28.889  11.149 1.00 11.65 ? 433  GLN   A N    1 
ATOM   6634  C  CA   . GLN   A 1 433 ? 3.805  29.806  10.038 1.00 11.19 ? 433  GLN   A CA   1 
ATOM   6635  C  C    . GLN   A 1 433 ? 4.689  30.986  10.468 1.00 11.40 ? 433  GLN   A C    1 
ATOM   6636  O  O    . GLN   A 1 433 ? 5.676  31.254  9.768  1.00 9.44  ? 433  GLN   A O    1 
ATOM   6637  C  CB   . GLN   A 1 433 ? 2.538  30.265  9.309  1.00 12.27 ? 433  GLN   A CB   1 
ATOM   6638  C  CG   . GLN   A 1 433 ? 1.728  29.114  8.729  1.00 12.58 ? 433  GLN   A CG   1 
ATOM   6639  C  CD   . GLN   A 1 433 ? 2.414  28.454  7.558  1.00 13.69 ? 433  GLN   A CD   1 
ATOM   6640  O  OE1  . GLN   A 1 433 ? 3.255  29.048  6.889  1.00 12.53 ? 433  GLN   A OE1  1 
ATOM   6641  N  NE2  . GLN   A 1 433 ? 2.050  27.210  7.295  1.00 15.74 ? 433  GLN   A NE2  1 
ATOM   6642  H  H    . GLN   A 1 433 ? 2.577  28.800  11.273 1.00 13.99 ? 433  GLN   A H    1 
ATOM   6643  H  HA   . GLN   A 1 433 ? 4.368  29.304  9.428  1.00 13.43 ? 433  GLN   A HA   1 
ATOM   6644  H  HB2  . GLN   A 1 433 ? 1.981  30.766  9.925  1.00 14.73 ? 433  GLN   A HB2  1 
ATOM   6645  H  HB3  . GLN   A 1 433 ? 2.786  30.871  8.593  1.00 14.73 ? 433  GLN   A HB3  1 
ATOM   6646  H  HG2  . GLN   A 1 433 ? 1.570  28.453  9.421  1.00 15.10 ? 433  GLN   A HG2  1 
ATOM   6647  H  HG3  . GLN   A 1 433 ? 0.860  29.443  8.447  1.00 15.10 ? 433  GLN   A HG3  1 
ATOM   6648  H  HE21 . GLN   A 1 433 ? 1.458  26.823  7.784  1.00 18.89 ? 433  GLN   A HE21 1 
ATOM   6649  H  HE22 . GLN   A 1 433 ? 2.406  26.788  6.635  1.00 18.89 ? 433  GLN   A HE22 1 
ATOM   6650  N  N    . GLY   A 1 434 ? 4.315  31.703  11.523 1.00 10.29 ? 434  GLY   A N    1 
ATOM   6651  C  CA   . GLY   A 1 434 ? 5.108  32.885  11.905 1.00 9.67  ? 434  GLY   A CA   1 
ATOM   6652  C  C    . GLY   A 1 434 ? 6.513  32.465  12.300 1.00 9.55  ? 434  GLY   A C    1 
ATOM   6653  O  O    . GLY   A 1 434 ? 7.469  33.144  11.904 1.00 9.27  ? 434  GLY   A O    1 
ATOM   6654  H  H    . GLY   A 1 434 ? 3.633  31.537  12.019 1.00 12.35 ? 434  GLY   A H    1 
ATOM   6655  H  HA2  . GLY   A 1 434 ? 5.146  33.511  11.165 1.00 11.61 ? 434  GLY   A HA2  1 
ATOM   6656  H  HA3  . GLY   A 1 434 ? 4.680  33.345  12.644 1.00 11.61 ? 434  GLY   A HA3  1 
ATOM   6657  N  N    . HIS   A 1 435 ? 6.626  31.355  13.030 1.00 10.54 ? 435  HIS   A N    1 
ATOM   6658  C  CA   . HIS   A 1 435 ? 7.959  30.907  13.523 1.00 9.14  ? 435  HIS   A CA   1 
ATOM   6659  C  C    . HIS   A 1 435 ? 8.887  30.534  12.358 1.00 10.05 ? 435  HIS   A C    1 
ATOM   6660  O  O    . HIS   A 1 435 ? 10.105 30.733  12.455 1.00 10.14 ? 435  HIS   A O    1 
ATOM   6661  C  CB   . HIS   A 1 435 ? 7.799  29.740  14.507 1.00 10.61 ? 435  HIS   A CB   1 
ATOM   6662  C  CG   . HIS   A 1 435 ? 9.024  29.488  15.320 1.00 10.75 ? 435  HIS   A CG   1 
ATOM   6663  N  ND1  . HIS   A 1 435 ? 9.559  30.438  16.162 1.00 10.04 ? 435  HIS   A ND1  1 
ATOM   6664  C  CD2  . HIS   A 1 435 ? 9.819  28.416  15.416 1.00 12.94 ? 435  HIS   A CD2  1 
ATOM   6665  C  CE1  . HIS   A 1 435 ? 10.638 29.942  16.748 1.00 13.13 ? 435  HIS   A CE1  1 
ATOM   6666  N  NE2  . HIS   A 1 435 ? 10.815 28.716  16.309 1.00 12.59 ? 435  HIS   A NE2  1 
ATOM   6667  H  H    . HIS   A 1 435 ? 5.967  30.849  13.253 1.00 12.65 ? 435  HIS   A H    1 
ATOM   6668  H  HA   . HIS   A 1 435 ? 8.374  31.646  13.995 1.00 10.97 ? 435  HIS   A HA   1 
ATOM   6669  H  HB2  . HIS   A 1 435 ? 7.055  29.925  15.102 1.00 12.74 ? 435  HIS   A HB2  1 
ATOM   6670  H  HB3  . HIS   A 1 435 ? 7.574  28.936  14.013 1.00 12.74 ? 435  HIS   A HB3  1 
ATOM   6671  H  HD2  . HIS   A 1 435 ? 9.715  27.613  14.959 1.00 15.54 ? 435  HIS   A HD2  1 
ATOM   6672  H  HE1  . HIS   A 1 435 ? 11.177 30.384  17.363 1.00 15.76 ? 435  HIS   A HE1  1 
ATOM   6673  H  HE2  . HIS   A 1 435 ? 11.452 28.188  16.544 1.00 15.11 ? 435  HIS   A HE2  1 
ATOM   6674  N  N    . GLY   A 1 436 ? 8.318  29.970  11.295 1.00 9.74  ? 436  GLY   A N    1 
ATOM   6675  C  CA   . GLY   A 1 436 ? 9.134  29.615  10.121 1.00 10.30 ? 436  GLY   A CA   1 
ATOM   6676  C  C    . GLY   A 1 436 ? 9.761  30.850  9.499  1.00 9.38  ? 436  GLY   A C    1 
ATOM   6677  O  O    . GLY   A 1 436 ? 10.832 30.732  8.890  1.00 10.19 ? 436  GLY   A O    1 
ATOM   6678  H  H    . GLY   A 1 436 ? 7.481  29.786  11.227 1.00 11.69 ? 436  GLY   A H    1 
ATOM   6679  H  HA2  . GLY   A 1 436 ? 9.830  28.992  10.383 1.00 12.37 ? 436  GLY   A HA2  1 
ATOM   6680  H  HA3  . GLY   A 1 436 ? 8.582  29.163  9.464  1.00 12.37 ? 436  GLY   A HA3  1 
ATOM   6681  N  N    . ILE   A 1 437 ? 9.083  31.987  9.619  1.00 9.12  ? 437  ILE   A N    1 
ATOM   6682  C  CA   . ILE   A 1 437 ? 9.678  33.255  9.108  1.00 10.35 ? 437  ILE   A CA   1 
ATOM   6683  C  C    . ILE   A 1 437 ? 10.967 33.502  9.894  1.00 8.02  ? 437  ILE   A C    1 
ATOM   6684  O  O    . ILE   A 1 437 ? 11.996 33.804  9.276  1.00 10.58 ? 437  ILE   A O    1 
ATOM   6685  C  CB   . ILE   A 1 437 ? 8.693  34.432  9.249  1.00 9.98  ? 437  ILE   A CB   1 
ATOM   6686  C  CG1  . ILE   A 1 437 ? 7.358  34.143  8.560  1.00 10.13 ? 437  ILE   A CG1  1 
ATOM   6687  C  CG2  . ILE   A 1 437 ? 9.320  35.722  8.742  1.00 11.01 ? 437  ILE   A CG2  1 
ATOM   6688  C  CD1  . ILE   A 1 437 ? 6.363  35.274  8.663  1.00 12.35 ? 437  ILE   A CD1  1 
ATOM   6689  H  H    . ILE   A 1 437 ? 8.305  32.062  9.977  1.00 10.95 ? 437  ILE   A H    1 
ATOM   6690  H  HA   . ILE   A 1 437 ? 9.873  33.180  8.161  1.00 12.43 ? 437  ILE   A HA   1 
ATOM   6691  H  HB   . ILE   A 1 437 ? 8.500  34.545  10.193 1.00 11.97 ? 437  ILE   A HB   1 
ATOM   6692  H  HG12 . ILE   A 1 437 ? 7.522  33.951  7.623  1.00 12.16 ? 437  ILE   A HG12 1 
ATOM   6693  H  HG13 . ILE   A 1 437 ? 6.969  33.344  8.949  1.00 12.16 ? 437  ILE   A HG13 1 
ATOM   6694  H  HG21 . ILE   A 1 437 ? 8.686  36.450  8.839  1.00 13.22 ? 437  ILE   A HG21 1 
ATOM   6695  H  HG22 . ILE   A 1 437 ? 10.118 35.918  9.257  1.00 13.22 ? 437  ILE   A HG22 1 
ATOM   6696  H  HG23 . ILE   A 1 437 ? 9.556  35.621  7.807  1.00 13.22 ? 437  ILE   A HG23 1 
ATOM   6697  H  HD11 . ILE   A 1 437 ? 5.543  35.026  8.208  1.00 14.83 ? 437  ILE   A HD11 1 
ATOM   6698  H  HD12 . ILE   A 1 437 ? 6.172  35.453  9.597  1.00 14.83 ? 437  ILE   A HD12 1 
ATOM   6699  H  HD13 . ILE   A 1 437 ? 6.734  36.070  8.251  1.00 14.83 ? 437  ILE   A HD13 1 
ATOM   6700  N  N    . THR   A 1 438 ? 10.886 33.377  11.219 1.00 8.92  ? 438  THR   A N    1 
ATOM   6701  C  CA   . THR   A 1 438 ? 12.078 33.598  12.076 1.00 7.83  ? 438  THR   A CA   1 
ATOM   6702  C  C    . THR   A 1 438 ? 13.251 32.760  11.554 1.00 8.15  ? 438  THR   A C    1 
ATOM   6703  O  O    . THR   A 1 438 ? 14.346 33.306  11.406 1.00 8.60  ? 438  THR   A O    1 
ATOM   6704  C  CB   . THR   A 1 438 ? 11.752 33.313  13.550 1.00 8.47  ? 438  THR   A CB   1 
ATOM   6705  O  OG1  . THR   A 1 438 ? 10.846 34.302  14.037 1.00 10.32 ? 438  THR   A OG1  1 
ATOM   6706  C  CG2  . THR   A 1 438 ? 12.987 33.275  14.423 1.00 9.52  ? 438  THR   A CG2  1 
ATOM   6707  H  H    . THR   A 1 438 ? 10.168 33.169  11.645 1.00 10.71 ? 438  THR   A H    1 
ATOM   6708  H  HA   . THR   A 1 438 ? 12.343 34.530  12.032 1.00 9.40  ? 438  THR   A HA   1 
ATOM   6709  H  HB   . THR   A 1 438 ? 11.346 32.433  13.592 1.00 10.17 ? 438  THR   A HB   1 
ATOM   6710  H  HG1  . THR   A 1 438 ? 10.728 34.192  14.861 1.00 12.39 ? 438  THR   A HG1  1 
ATOM   6711  H  HG21 . THR   A 1 438 ? 12.730 33.093  15.340 1.00 11.42 ? 438  THR   A HG21 1 
ATOM   6712  H  HG22 . THR   A 1 438 ? 13.583 32.577  14.110 1.00 11.42 ? 438  THR   A HG22 1 
ATOM   6713  H  HG23 . THR   A 1 438 ? 13.441 34.131  14.379 1.00 11.42 ? 438  THR   A HG23 1 
ATOM   6714  N  N    . TYR   A 1 439 ? 13.023 31.469  11.318 1.00 9.97  ? 439  TYR   A N    1 
ATOM   6715  C  CA   . TYR   A 1 439 ? 14.120 30.580  10.853 1.00 10.67 ? 439  TYR   A CA   1 
ATOM   6716  C  C    . TYR   A 1 439 ? 14.728 31.119  9.552  1.00 8.73  ? 439  TYR   A C    1 
ATOM   6717  O  O    . TYR   A 1 439 ? 15.956 31.140  9.422  1.00 10.61 ? 439  TYR   A O    1 
ATOM   6718  C  CB   . TYR   A 1 439 ? 13.606 29.166  10.571 1.00 8.95  ? 439  TYR   A CB   1 
ATOM   6719  C  CG   . TYR   A 1 439 ? 13.202 28.345  11.769 1.00 9.65  ? 439  TYR   A CG   1 
ATOM   6720  C  CD1  . TYR   A 1 439 ? 13.700 28.609  13.033 1.00 8.54  ? 439  TYR   A CD1  1 
ATOM   6721  C  CD2  . TYR   A 1 439 ? 12.334 27.276  11.627 1.00 9.93  ? 439  TYR   A CD2  1 
ATOM   6722  C  CE1  . TYR   A 1 439 ? 13.332 27.844  14.128 1.00 9.16  ? 439  TYR   A CE1  1 
ATOM   6723  C  CE2  . TYR   A 1 439 ? 11.956 26.501  12.709 1.00 11.21 ? 439  TYR   A CE2  1 
ATOM   6724  C  CZ   . TYR   A 1 439 ? 12.459 26.783  13.965 1.00 10.24 ? 439  TYR   A CZ   1 
ATOM   6725  O  OH   . TYR   A 1 439 ? 12.083 26.006  15.034 1.00 13.11 ? 439  TYR   A OH   1 
ATOM   6726  H  H    . TYR   A 1 439 ? 12.260 31.083  11.415 1.00 11.96 ? 439  TYR   A H    1 
ATOM   6727  H  HA   . TYR   A 1 439 ? 14.785 30.555  11.559 1.00 12.80 ? 439  TYR   A HA   1 
ATOM   6728  H  HB2  . TYR   A 1 439 ? 12.842 29.234  9.978  1.00 10.75 ? 439  TYR   A HB2  1 
ATOM   6729  H  HB3  . TYR   A 1 439 ? 14.296 28.682  10.090 1.00 10.75 ? 439  TYR   A HB3  1 
ATOM   6730  H  HD1  . TYR   A 1 439 ? 14.294 29.315  13.150 1.00 10.25 ? 439  TYR   A HD1  1 
ATOM   6731  H  HD2  . TYR   A 1 439 ? 11.997 27.074  10.784 1.00 11.92 ? 439  TYR   A HD2  1 
ATOM   6732  H  HE1  . TYR   A 1 439 ? 13.671 28.043  14.971 1.00 11.00 ? 439  TYR   A HE1  1 
ATOM   6733  H  HE2  . TYR   A 1 439 ? 11.365 25.792  12.591 1.00 13.45 ? 439  TYR   A HE2  1 
ATOM   6734  H  HH   . TYR   A 1 439 ? 11.777 25.275  14.755 1.00 15.74 ? 439  TYR   A HH   1 
ATOM   6735  N  N    . ALA   A 1 440 ? 13.879 31.540  8.614  1.00 9.38  ? 440  ALA   A N    1 
ATOM   6736  C  CA   . ALA   A 1 440 ? 14.387 31.955  7.286  1.00 9.92  ? 440  ALA   A CA   1 
ATOM   6737  C  C    . ALA   A 1 440 ? 15.127 33.296  7.336  1.00 9.99  ? 440  ALA   A C    1 
ATOM   6738  O  O    . ALA   A 1 440 ? 16.113 33.429  6.606  1.00 11.39 ? 440  ALA   A O    1 
ATOM   6739  C  CB   . ALA   A 1 440 ? 13.235 32.021  6.312  1.00 14.08 ? 440  ALA   A CB   1 
ATOM   6740  H  H    . ALA   A 1 440 ? 13.027 31.595  8.713  1.00 11.26 ? 440  ALA   A H    1 
ATOM   6741  H  HA   . ALA   A 1 440 ? 15.032 31.293  6.992  1.00 11.91 ? 440  ALA   A HA   1 
ATOM   6742  H  HB1  . ALA   A 1 440 ? 13.563 32.293  5.440  1.00 16.90 ? 440  ALA   A HB1  1 
ATOM   6743  H  HB2  . ALA   A 1 440 ? 12.819 31.147  6.243  1.00 16.90 ? 440  ALA   A HB2  1 
ATOM   6744  H  HB3  . ALA   A 1 440 ? 12.582 32.666  6.626  1.00 16.90 ? 440  ALA   A HB3  1 
ATOM   6745  N  N    . VAL   A 1 441 ? 14.667 34.239  8.160  1.00 9.71  ? 441  VAL   A N    1 
ATOM   6746  C  CA   . VAL   A 1 441 ? 15.266 35.610  8.132  1.00 9.30  ? 441  VAL   A CA   1 
ATOM   6747  C  C    . VAL   A 1 441 ? 16.231 35.862  9.301  1.00 9.44  ? 441  VAL   A C    1 
ATOM   6748  O  O    . VAL   A 1 441 ? 16.890 36.905  9.271  1.00 10.98 ? 441  VAL   A O    1 
ATOM   6749  C  CB   . VAL   A 1 441 ? 14.164 36.686  8.106  1.00 10.74 ? 441  VAL   A CB   1 
ATOM   6750  C  CG1  . VAL   A 1 441 ? 13.204 36.462  6.948  1.00 11.63 ? 441  VAL   A CG1  1 
ATOM   6751  C  CG2  . VAL   A 1 441 ? 13.407 36.751  9.422  1.00 12.46 ? 441  VAL   A CG2  1 
ATOM   6752  H  H    . VAL   A 1 441 ? 14.032 34.127  8.729  1.00 11.66 ? 441  VAL   A H    1 
ATOM   6753  H  HA   . VAL   A 1 441 ? 15.788 35.667  7.316  1.00 11.16 ? 441  VAL   A HA   1 
ATOM   6754  H  HB   . VAL   A 1 441 ? 14.605 37.540  7.977  1.00 12.89 ? 441  VAL   A HB   1 
ATOM   6755  H  HG11 . VAL   A 1 441 ? 12.522 37.152  6.955  1.00 13.96 ? 441  VAL   A HG11 1 
ATOM   6756  H  HG12 . VAL   A 1 441 ? 13.692 36.499  6.111  1.00 13.96 ? 441  VAL   A HG12 1 
ATOM   6757  H  HG13 . VAL   A 1 441 ? 12.785 35.592  7.039  1.00 13.96 ? 441  VAL   A HG13 1 
ATOM   6758  H  HG21 . VAL   A 1 441 ? 12.723 37.437  9.369  1.00 14.96 ? 441  VAL   A HG21 1 
ATOM   6759  H  HG22 . VAL   A 1 441 ? 12.990 35.893  9.599  1.00 14.96 ? 441  VAL   A HG22 1 
ATOM   6760  H  HG23 . VAL   A 1 441 ? 14.023 36.964  10.140 1.00 14.96 ? 441  VAL   A HG23 1 
ATOM   6761  N  N    . ASN   A 1 442 ? 16.292 34.959  10.276 1.00 9.96  ? 442  ASN   A N    1 
ATOM   6762  C  CA   . ASN   A 1 442 ? 17.174 35.176  11.452 1.00 10.19 ? 442  ASN   A CA   1 
ATOM   6763  C  C    . ASN   A 1 442 ? 18.560 35.636  10.975 1.00 9.64  ? 442  ASN   A C    1 
ATOM   6764  O  O    . ASN   A 1 442 ? 19.173 34.921  10.174 1.00 11.22 ? 442  ASN   A O    1 
ATOM   6765  C  CB   . ASN   A 1 442 ? 17.240 33.918  12.320 1.00 11.36 ? 442  ASN   A CB   1 
ATOM   6766  C  CG   . ASN   A 1 442 ? 17.807 34.176  13.698 1.00 10.87 ? 442  ASN   A CG   1 
ATOM   6767  O  OD1  . ASN   A 1 442 ? 18.674 35.029  13.869 1.00 10.20 ? 442  ASN   A OD1  1 
ATOM   6768  N  ND2  . ASN   A 1 442 ? 17.320 33.444  14.685 1.00 9.11  ? 442  ASN   A ND2  1 
ATOM   6769  H  H    . ASN   A 1 442 ? 15.845 34.224  10.288 1.00 11.96 ? 442  ASN   A H    1 
ATOM   6770  H  HA   . ASN   A 1 442 ? 16.805 35.877  12.012 1.00 12.23 ? 442  ASN   A HA   1 
ATOM   6771  H  HB2  . ASN   A 1 442 ? 16.349 33.545  12.408 1.00 13.64 ? 442  ASN   A HB2  1 
ATOM   6772  H  HB3  . ASN   A 1 442 ? 17.784 33.251  11.872 1.00 13.64 ? 442  ASN   A HB3  1 
ATOM   6773  H  HD21 . ASN   A 1 442 ? 17.610 33.556  15.487 1.00 10.93 ? 442  ASN   A HD21 1 
ATOM   6774  H  HD22 . ASN   A 1 442 ? 16.713 32.856  14.525 1.00 10.93 ? 442  ASN   A HD22 1 
ATOM   6775  N  N    . ASN   A 1 443 ? 19.034 36.779  11.479 1.00 10.58 ? 443  ASN   A N    1 
ATOM   6776  C  CA   . ASN   A 1 443 ? 20.341 37.335  11.024 1.00 11.15 ? 443  ASN   A CA   1 
ATOM   6777  C  C    . ASN   A 1 443 ? 21.505 36.403  11.399 1.00 10.21 ? 443  ASN   A C    1 
ATOM   6778  O  O    . ASN   A 1 443 ? 22.565 36.521  10.775 1.00 13.43 ? 443  ASN   A O    1 
ATOM   6779  C  CB   . ASN   A 1 443 ? 20.579 38.748  11.569 1.00 12.24 ? 443  ASN   A CB   1 
ATOM   6780  C  CG   . ASN   A 1 443 ? 19.602 39.769  11.024 1.00 14.74 ? 443  ASN   A CG   1 
ATOM   6781  O  OD1  . ASN   A 1 443 ? 19.360 39.821  9.821  1.00 12.88 ? 443  ASN   A OD1  1 
ATOM   6782  N  ND2  . ASN   A 1 443 ? 19.041 40.585  11.899 1.00 10.70 ? 443  ASN   A ND2  1 
ATOM   6783  H  H    . ASN   A 1 443 ? 18.631 37.249  12.076 1.00 12.70 ? 443  ASN   A H    1 
ATOM   6784  H  HA   . ASN   A 1 443 ? 20.303 37.396  10.057 1.00 13.38 ? 443  ASN   A HA   1 
ATOM   6785  H  HB2  . ASN   A 1 443 ? 20.514 38.731  12.537 1.00 14.69 ? 443  ASN   A HB2  1 
ATOM   6786  H  HB3  . ASN   A 1 443 ? 21.483 39.025  11.351 1.00 14.69 ? 443  ASN   A HB3  1 
ATOM   6787  H  HD21 . ASN   A 1 443 ? 18.482 41.182  11.633 1.00 12.85 ? 443  ASN   A HD21 1 
ATOM   6788  H  HD22 . ASN   A 1 443 ? 19.235 40.519  12.734 1.00 12.85 ? 443  ASN   A HD22 1 
ATOM   6789  N  N    . ARG   A 1 444 ? 21.312 35.517  12.380 1.00 9.74  ? 444  ARG   A N    1 
ATOM   6790  C  CA   . ARG   A 1 444 ? 22.450 34.668  12.828 1.00 10.38 ? 444  ARG   A CA   1 
ATOM   6791  C  C    . ARG   A 1 444 ? 22.313 33.245  12.272 1.00 11.74 ? 444  ARG   A C    1 
ATOM   6792  O  O    . ARG   A 1 444 ? 23.137 32.389  12.578 1.00 10.20 ? 444  ARG   A O    1 
ATOM   6793  C  CB   . ARG   A 1 444 ? 22.582 34.655  14.357 1.00 9.59  ? 444  ARG   A CB   1 
ATOM   6794  C  CG   . ARG   A 1 444 ? 21.715 33.643  15.095 1.00 9.88  ? 444  ARG   A CG   1 
ATOM   6795  C  CD   . ARG   A 1 444 ? 21.994 33.697  16.588 1.00 8.83  ? 444  ARG   A CD   1 
ATOM   6796  N  NE   . ARG   A 1 444 ? 21.380 32.631  17.361 1.00 10.24 ? 444  ARG   A NE   1 
ATOM   6797  C  CZ   . ARG   A 1 444 ? 21.936 32.037  18.412 1.00 9.93  ? 444  ARG   A CZ   1 
ATOM   6798  N  NH1  . ARG   A 1 444 ? 23.143 32.388  18.813 1.00 8.00  ? 444  ARG   A NH1  1 
ATOM   6799  N  NH2  . ARG   A 1 444 ? 21.281 31.094  19.063 1.00 7.51  ? 444  ARG   A NH2  1 
ATOM   6800  H  H    . ARG   A 1 444 ? 20.568 35.387  12.791 1.00 11.69 ? 444  ARG   A H    1 
ATOM   6801  H  HA   . ARG   A 1 444 ? 23.265 35.057  12.474 1.00 12.45 ? 444  ARG   A HA   1 
ATOM   6802  H  HB2  . ARG   A 1 444 ? 23.510 34.484  14.582 1.00 11.52 ? 444  ARG   A HB2  1 
ATOM   6803  H  HB3  . ARG   A 1 444 ? 22.368 35.541  14.690 1.00 11.52 ? 444  ARG   A HB3  1 
ATOM   6804  H  HG2  . ARG   A 1 444 ? 20.778 33.828  14.928 1.00 11.86 ? 444  ARG   A HG2  1 
ATOM   6805  H  HG3  . ARG   A 1 444 ? 21.892 32.750  14.759 1.00 11.86 ? 444  ARG   A HG3  1 
ATOM   6806  H  HD2  . ARG   A 1 444 ? 22.954 33.668  16.726 1.00 10.60 ? 444  ARG   A HD2  1 
ATOM   6807  H  HD3  . ARG   A 1 444 ? 21.683 34.549  16.932 1.00 10.60 ? 444  ARG   A HD3  1 
ATOM   6808  H  HE   . ARG   A 1 444 ? 20.598 32.364  17.121 1.00 12.29 ? 444  ARG   A HE   1 
ATOM   6809  H  HH11 . ARG   A 1 444 ? 23.573 33.003  18.394 1.00 9.60  ? 444  ARG   A HH11 1 
ATOM   6810  H  HH12 . ARG   A 1 444 ? 23.499 32.001  19.493 1.00 9.60  ? 444  ARG   A HH12 1 
ATOM   6811  H  HH21 . ARG   A 1 444 ? 20.493 30.863  18.807 1.00 9.02  ? 444  ARG   A HH21 1 
ATOM   6812  H  HH22 . ARG   A 1 444 ? 21.642 30.711  19.743 1.00 9.02  ? 444  ARG   A HH22 1 
ATOM   6813  N  N    . GLY   A 1 445 ? 21.327 33.054  11.411 1.00 10.30 ? 445  GLY   A N    1 
ATOM   6814  C  CA   . GLY   A 1 445 ? 21.110 31.729  10.827 1.00 10.65 ? 445  GLY   A CA   1 
ATOM   6815  C  C    . GLY   A 1 445 ? 19.979 30.960  11.502 1.00 11.08 ? 445  GLY   A C    1 
ATOM   6816  O  O    . GLY   A 1 445 ? 19.333 31.503  12.367 1.00 10.04 ? 445  GLY   A O    1 
ATOM   6817  H  H    . GLY   A 1 445 ? 20.778 33.663  11.151 1.00 12.37 ? 445  GLY   A H    1 
ATOM   6818  H  HA2  . GLY   A 1 445 ? 20.910 31.826  9.883  1.00 12.78 ? 445  GLY   A HA2  1 
ATOM   6819  H  HA3  . GLY   A 1 445 ? 21.929 31.214  10.892 1.00 12.78 ? 445  GLY   A HA3  1 
ATOM   6820  N  N    . GLY   A 1 446 ? 19.793 29.709  11.071 1.00 9.16  ? 446  GLY   A N    1 
ATOM   6821  C  CA   . GLY   A 1 446 ? 18.731 28.856  11.632 1.00 9.32  ? 446  GLY   A CA   1 
ATOM   6822  C  C    . GLY   A 1 446 ? 18.714 28.905  13.145 1.00 11.06 ? 446  GLY   A C    1 
ATOM   6823  O  O    . GLY   A 1 446 ? 19.633 28.359  13.760 1.00 9.87  ? 446  GLY   A O    1 
ATOM   6824  H  H    . GLY   A 1 446 ? 20.266 29.334  10.458 1.00 11.00 ? 446  GLY   A H    1 
ATOM   6825  H  HA2  . GLY   A 1 446 ? 17.870 29.143  11.289 1.00 11.19 ? 446  GLY   A HA2  1 
ATOM   6826  H  HA3  . GLY   A 1 446 ? 18.862 27.941  11.339 1.00 11.19 ? 446  GLY   A HA3  1 
ATOM   6827  N  N    . CYS   A 1 447 ? 17.682 29.527  13.708 1.00 9.44  ? 447  CYS   A N    1 
ATOM   6828  C  CA   . CYS   A 1 447 ? 17.616 29.711  15.177 1.00 9.57  ? 447  CYS   A CA   1 
ATOM   6829  C  C    . CYS   A 1 447 ? 16.208 30.191  15.539 1.00 8.18  ? 447  CYS   A C    1 
ATOM   6830  O  O    . CYS   A 1 447 ? 15.632 30.968  14.763 1.00 8.34  ? 447  CYS   A O    1 
ATOM   6831  C  CB   . CYS   A 1 447 ? 18.660 30.723  15.632 1.00 10.38 ? 447  CYS   A CB   1 
ATOM   6832  S  SG   . CYS   A 1 447 ? 18.310 31.473  17.243 1.00 10.65 ? 447  CYS   A SG   1 
ATOM   6833  H  H    . CYS   A 1 447 ? 17.014 29.849  13.274 1.00 11.33 ? 447  CYS   A H    1 
ATOM   6834  H  HA   . CYS   A 1 447 ? 17.803 28.871  15.626 1.00 11.48 ? 447  CYS   A HA   1 
ATOM   6835  H  HB2  . CYS   A 1 447 ? 19.525 30.286  15.671 1.00 12.45 ? 447  CYS   A HB2  1 
ATOM   6836  H  HB3  . CYS   A 1 447 ? 18.727 31.426  14.967 1.00 12.45 ? 447  CYS   A HB3  1 
ATOM   6837  H  HG   . CYS   A 1 447 ? 17.189 31.900  17.251 1.00 12.79 ? 447  CYS   A HG   1 
ATOM   6838  N  N    . HIS   A 1 448 ? 15.694 29.758  16.687 1.00 9.60  ? 448  HIS   A N    1 
ATOM   6839  C  CA   . HIS   A 1 448 ? 14.311 30.100  17.093 1.00 9.66  ? 448  HIS   A CA   1 
ATOM   6840  C  C    . HIS   A 1 448 ? 14.245 31.234  18.113 1.00 10.92 ? 448  HIS   A C    1 
ATOM   6841  O  O    . HIS   A 1 448 ? 13.241 31.956  18.120 1.00 9.20  ? 448  HIS   A O    1 
ATOM   6842  C  CB   . HIS   A 1 448 ? 13.734 28.910  17.868 1.00 8.18  ? 448  HIS   A CB   1 
ATOM   6843  C  CG   . HIS   A 1 448 ? 14.550 28.565  19.071 1.00 12.35 ? 448  HIS   A CG   1 
ATOM   6844  N  ND1  . HIS   A 1 448 ? 15.901 28.305  18.998 1.00 10.01 ? 448  HIS   A ND1  1 
ATOM   6845  C  CD2  . HIS   A 1 448 ? 14.226 28.463  20.363 1.00 8.78  ? 448  HIS   A CD2  1 
ATOM   6846  C  CE1  . HIS   A 1 448 ? 16.363 28.043  20.209 1.00 11.64 ? 448  HIS   A CE1  1 
ATOM   6847  N  NE2  . HIS   A 1 448 ? 15.364 28.136  21.054 1.00 11.24 ? 448  HIS   A NE2  1 
ATOM   6848  H  H    . HIS   A 1 448 ? 16.120 29.266  17.250 1.00 11.53 ? 448  HIS   A H    1 
ATOM   6849  H  HA   . HIS   A 1 448 ? 13.845 30.340  16.277 1.00 11.59 ? 448  HIS   A HA   1 
ATOM   6850  H  HB2  . HIS   A 1 448 ? 12.827 29.116  18.144 1.00 9.82  ? 448  HIS   A HB2  1 
ATOM   6851  H  HB3  . HIS   A 1 448 ? 13.684 28.139  17.282 1.00 9.82  ? 448  HIS   A HB3  1 
ATOM   6852  H  HD2  . HIS   A 1 448 ? 13.380 28.591  20.728 1.00 10.54 ? 448  HIS   A HD2  1 
ATOM   6853  H  HE1  . HIS   A 1 448 ? 17.242 27.830  20.424 1.00 13.97 ? 448  HIS   A HE1  1 
ATOM   6854  H  HE2  . HIS   A 1 448 ? 15.415 28.012  21.904 1.00 13.49 ? 448  HIS   A HE2  1 
ATOM   6855  N  N    . ILE   A 1 449 ? 15.296 31.407  18.917 1.00 9.55  ? 449  ILE   A N    1 
ATOM   6856  C  CA   . ILE   A 1 449 ? 15.199 32.333  20.088 1.00 11.83 ? 449  ILE   A CA   1 
ATOM   6857  C  C    . ILE   A 1 449 ? 15.405 33.824  19.753 1.00 11.36 ? 449  ILE   A C    1 
ATOM   6858  O  O    . ILE   A 1 449 ? 15.092 34.643  20.622 1.00 9.46  ? 449  ILE   A O    1 
ATOM   6859  C  CB   . ILE   A 1 449 ? 16.098 31.796  21.232 1.00 8.56  ? 449  ILE   A CB   1 
ATOM   6860  C  CG1  . ILE   A 1 449 ? 15.639 32.313  22.598 1.00 8.61  ? 449  ILE   A CG1  1 
ATOM   6861  C  CG2  . ILE   A 1 449 ? 17.585 32.032  20.984 1.00 12.80 ? 449  ILE   A CG2  1 
ATOM   6862  C  CD1  . ILE   A 1 449 ? 14.246 31.861  22.977 1.00 9.99  ? 449  ILE   A CD1  1 
ATOM   6863  H  H    . ILE   A 1 449 ? 16.057 31.018  18.820 1.00 11.46 ? 449  ILE   A H    1 
ATOM   6864  H  HA   . ILE   A 1 449 ? 14.280 32.331  20.398 1.00 14.20 ? 449  ILE   A HA   1 
ATOM   6865  H  HB   . ILE   A 1 449 ? 15.989 30.832  21.241 1.00 10.27 ? 449  ILE   A HB   1 
ATOM   6866  H  HG12 . ILE   A 1 449 ? 16.264 32.013  23.276 1.00 10.33 ? 449  ILE   A HG12 1 
ATOM   6867  H  HG13 . ILE   A 1 449 ? 15.667 33.283  22.595 1.00 10.33 ? 449  ILE   A HG13 1 
ATOM   6868  H  HG21 . ILE   A 1 449 ? 18.097 31.678  21.728 1.00 15.36 ? 449  ILE   A HG21 1 
ATOM   6869  H  HG22 . ILE   A 1 449 ? 17.852 31.585  20.166 1.00 15.36 ? 449  ILE   A HG22 1 
ATOM   6870  H  HG23 . ILE   A 1 449 ? 17.752 32.984  20.901 1.00 15.36 ? 449  ILE   A HG23 1 
ATOM   6871  H  HD11 . ILE   A 1 449 ? 14.015 32.220  23.848 1.00 12.00 ? 449  ILE   A HD11 1 
ATOM   6872  H  HD12 . ILE   A 1 449 ? 13.611 32.181  22.317 1.00 12.00 ? 449  ILE   A HD12 1 
ATOM   6873  H  HD13 . ILE   A 1 449 ? 14.218 30.892  23.009 1.00 12.00 ? 449  ILE   A HD13 1 
ATOM   6874  N  N    . LYS   A 1 450 ? 15.880 34.173  18.553 1.00 9.85  ? 450  LYS   A N    1 
ATOM   6875  C  CA   . LYS   A 1 450 ? 15.948 35.618  18.184 1.00 9.71  ? 450  LYS   A CA   1 
ATOM   6876  C  C    . LYS   A 1 450 ? 14.567 36.064  17.681 1.00 12.06 ? 450  LYS   A C    1 
ATOM   6877  O  O    . LYS   A 1 450 ? 14.401 37.255  17.391 1.00 11.58 ? 450  LYS   A O    1 
ATOM   6878  C  CB   . LYS   A 1 450 ? 17.044 35.906  17.151 1.00 10.41 ? 450  LYS   A CB   1 
ATOM   6879  C  CG   . LYS   A 1 450 ? 18.440 35.427  17.528 1.00 8.94  ? 450  LYS   A CG   1 
ATOM   6880  C  CD   . LYS   A 1 450 ? 18.991 36.084  18.778 1.00 9.87  ? 450  LYS   A CD   1 
ATOM   6881  C  CE   . LYS   A 1 450 ? 18.755 35.272  20.034 1.00 10.23 ? 450  LYS   A CE   1 
ATOM   6882  N  NZ   . LYS   A 1 450 ? 19.452 35.851  21.206 1.00 10.84 ? 450  LYS   A NZ   1 
ATOM   6883  H  H    . LYS   A 1 450 ? 16.160 33.624  17.953 1.00 11.82 ? 450  LYS   A H    1 
ATOM   6884  H  HA   . LYS   A 1 450 ? 16.188 36.130  18.972 1.00 11.66 ? 450  LYS   A HA   1 
ATOM   6885  H  HB2  . LYS   A 1 450 ? 16.792 35.491  16.311 1.00 12.50 ? 450  LYS   A HB2  1 
ATOM   6886  H  HB3  . LYS   A 1 450 ? 17.078 36.863  16.996 1.00 12.50 ? 450  LYS   A HB3  1 
ATOM   6887  H  HG2  . LYS   A 1 450 ? 18.419 34.466  17.659 1.00 10.73 ? 450  LYS   A HG2  1 
ATOM   6888  H  HG3  . LYS   A 1 450 ? 19.043 35.599  16.788 1.00 10.73 ? 450  LYS   A HG3  1 
ATOM   6889  H  HD2  . LYS   A 1 450 ? 19.944 36.228  18.667 1.00 11.85 ? 450  LYS   A HD2  1 
ATOM   6890  H  HD3  . LYS   A 1 450 ? 18.583 36.958  18.884 1.00 11.85 ? 450  LYS   A HD3  1 
ATOM   6891  H  HE2  . LYS   A 1 450 ? 17.803 35.226  20.215 1.00 12.27 ? 450  LYS   A HE2  1 
ATOM   6892  H  HE3  . LYS   A 1 450 ? 19.061 34.363  19.893 1.00 12.27 ? 450  LYS   A HE3  1 
ATOM   6893  H  HZ1  . LYS   A 1 450 ? 19.107 35.513  21.954 1.00 13.02 ? 450  LYS   A HZ1  1 
ATOM   6894  H  HZ2  . LYS   A 1 450 ? 20.319 35.653  21.164 1.00 13.02 ? 450  LYS   A HZ2  1 
ATOM   6895  H  HZ3  . LYS   A 1 450 ? 19.349 36.735  21.206 1.00 13.02 ? 450  LYS   A HZ3  1 
ATOM   6896  N  N    . GLY   A 1 451 ? 13.617 35.132  17.601 1.00 10.31 ? 451  GLY   A N    1 
ATOM   6897  C  CA   . GLY   A 1 451 ? 12.234 35.453  17.183 1.00 10.80 ? 451  GLY   A CA   1 
ATOM   6898  C  C    . GLY   A 1 451 ? 11.286 34.361  17.643 1.00 11.47 ? 451  GLY   A C    1 
ATOM   6899  O  O    . GLY   A 1 451 ? 10.725 33.680  16.772 1.00 11.71 ? 451  GLY   A O    1 
ATOM   6900  H  H    . GLY   A 1 451 ? 13.746 34.302  17.784 1.00 12.38 ? 451  GLY   A H    1 
ATOM   6901  H  HA2  . GLY   A 1 451 ? 11.964 36.305  17.559 1.00 12.96 ? 451  GLY   A HA2  1 
ATOM   6902  H  HA3  . GLY   A 1 451 ? 12.192 35.543  16.218 1.00 12.96 ? 451  GLY   A HA3  1 
ATOM   6903  N  N    . TYR   A 1 452 ? 11.085 34.231  18.953 1.00 10.58 ? 452  TYR   A N    1 
ATOM   6904  C  CA   . TYR   A 1 452 ? 10.308 33.088  19.506 1.00 14.14 ? 452  TYR   A CA   1 
ATOM   6905  C  C    . TYR   A 1 452 ? 8.803  33.234  19.272 1.00 12.32 ? 452  TYR   A C    1 
ATOM   6906  O  O    . TYR   A 1 452 ? 8.053  33.465  20.232 1.00 12.01 ? 452  TYR   A O    1 
ATOM   6907  C  CB   . TYR   A 1 452 ? 10.637 32.918  20.991 1.00 12.01 ? 452  TYR   A CB   1 
ATOM   6908  C  CG   . TYR   A 1 452 ? 10.433 31.527  21.532 1.00 11.80 ? 452  TYR   A CG   1 
ATOM   6909  C  CD1  . TYR   A 1 452 ? 11.022 30.430  20.930 1.00 9.72  ? 452  TYR   A CD1  1 
ATOM   6910  C  CD2  . TYR   A 1 452 ? 9.656  31.310  22.657 1.00 10.59 ? 452  TYR   A CD2  1 
ATOM   6911  C  CE1  . TYR   A 1 452 ? 10.844 29.151  21.430 1.00 12.00 ? 452  TYR   A CE1  1 
ATOM   6912  C  CE2  . TYR   A 1 452 ? 9.466  30.039  23.169 1.00 12.30 ? 452  TYR   A CE2  1 
ATOM   6913  C  CZ   . TYR   A 1 452 ? 10.062 28.954  22.553 1.00 11.98 ? 452  TYR   A CZ   1 
ATOM   6914  O  OH   . TYR   A 1 452 ? 9.877  27.692  23.057 1.00 12.17 ? 452  TYR   A OH   1 
ATOM   6915  H  H    . TYR   A 1 452 ? 11.382 34.781  19.544 1.00 12.70 ? 452  TYR   A H    1 
ATOM   6916  H  HA   . TYR   A 1 452 ? 10.571 32.285  19.030 1.00 16.97 ? 452  TYR   A HA   1 
ATOM   6917  H  HB2  . TYR   A 1 452 ? 11.561 33.174  21.135 1.00 14.41 ? 452  TYR   A HB2  1 
ATOM   6918  H  HB3  . TYR   A 1 452 ? 10.089 33.533  21.503 1.00 14.41 ? 452  TYR   A HB3  1 
ATOM   6919  H  HD1  . TYR   A 1 452 ? 11.549 30.554  20.174 1.00 11.66 ? 452  TYR   A HD1  1 
ATOM   6920  H  HD2  . TYR   A 1 452 ? 9.253  32.035  23.078 1.00 12.71 ? 452  TYR   A HD2  1 
ATOM   6921  H  HE1  . TYR   A 1 452 ? 11.250 28.426  21.011 1.00 14.41 ? 452  TYR   A HE1  1 
ATOM   6922  H  HE2  . TYR   A 1 452 ? 8.939  29.915  23.925 1.00 14.76 ? 452  TYR   A HE2  1 
ATOM   6923  H  HH   . TYR   A 1 452 ? 10.418 27.163  22.693 1.00 14.60 ? 452  TYR   A HH   1 
ATOM   6924  N  N    . MET   A 1 453 ? 8.393  33.067  18.020 1.00 12.49 ? 453  MET   A N    1 
ATOM   6925  C  CA   . MET   A 1 453 ? 6.976  33.116  17.693 1.00 10.37 ? 453  MET   A CA   1 
ATOM   6926  C  C    . MET   A 1 453 ? 6.220  31.954  18.320 1.00 11.51 ? 453  MET   A C    1 
ATOM   6927  O  O    . MET   A 1 453 ? 4.983  31.923  18.265 1.00 12.18 ? 453  MET   A O    1 
ATOM   6928  C  CB   . MET   A 1 453 ? 6.783  33.081  16.176 1.00 11.01 ? 453  MET   A CB   1 
ATOM   6929  C  CG   . MET   A 1 453 ? 6.915  34.428  15.465 1.00 12.66 ? 453  MET   A CG   1 
ATOM   6930  S  SD   . MET   A 1 453 ? 5.826  35.728  16.053 1.00 13.15 ? 453  MET   A SD   1 
ATOM   6931  C  CE   . MET   A 1 453 ? 4.419  35.442  14.979 1.00 16.27 ? 453  MET   A CE   1 
ATOM   6932  H  H    . MET   A 1 453 ? 8.915  32.925  17.351 1.00 14.99 ? 453  MET   A H    1 
ATOM   6933  H  HA   . MET   A 1 453 ? 6.622  33.945  18.052 1.00 12.45 ? 453  MET   A HA   1 
ATOM   6934  H  HB2  . MET   A 1 453 ? 7.432  32.468  15.797 1.00 13.22 ? 453  MET   A HB2  1 
ATOM   6935  H  HB3  . MET   A 1 453 ? 5.904  32.717  15.986 1.00 13.22 ? 453  MET   A HB3  1 
ATOM   6936  H  HG2  . MET   A 1 453 ? 7.832  34.733  15.552 1.00 15.19 ? 453  MET   A HG2  1 
ATOM   6937  H  HG3  . MET   A 1 453 ? 6.749  34.293  14.519 1.00 15.19 ? 453  MET   A HG3  1 
ATOM   6938  H  HE1  . MET   A 1 453 ? 3.722  36.086  15.180 1.00 19.53 ? 453  MET   A HE1  1 
ATOM   6939  H  HE2  . MET   A 1 453 ? 4.693  35.541  14.054 1.00 19.53 ? 453  MET   A HE2  1 
ATOM   6940  H  HE3  . MET   A 1 453 ? 4.080  34.544  15.122 1.00 19.53 ? 453  MET   A HE3  1 
ATOM   6941  N  N    . ILE   A 1 454 ? 6.951  30.985  18.875 1.00 11.25 ? 454  ILE   A N    1 
ATOM   6942  C  CA   . ILE   A 1 454 ? 6.359  29.920  19.679 1.00 11.72 ? 454  ILE   A CA   1 
ATOM   6943  C  C    . ILE   A 1 454 ? 5.488  30.510  20.783 1.00 12.18 ? 454  ILE   A C    1 
ATOM   6944  O  O    . ILE   A 1 454 ? 4.433  29.962  21.122 1.00 14.66 ? 454  ILE   A O    1 
ATOM   6945  C  CB   . ILE   A 1 454 ? 7.476  29.022  20.251 1.00 10.14 ? 454  ILE   A CB   1 
ATOM   6946  C  CG1  . ILE   A 1 454 ? 8.298  28.383  19.118 1.00 9.94  ? 454  ILE   A CG1  1 
ATOM   6947  C  CG2  . ILE   A 1 454 ? 6.908  27.979  21.208 1.00 14.00 ? 454  ILE   A CG2  1 
ATOM   6948  C  CD1  . ILE   A 1 454 ? 7.483  27.525  18.165 1.00 11.50 ? 454  ILE   A CD1  1 
ATOM   6949  H  H    . ILE   A 1 454 ? 7.805  30.929  18.794 1.00 13.51 ? 454  ILE   A H    1 
ATOM   6950  H  HA   . ILE   A 1 454 ? 5.786  29.371  19.121 1.00 14.06 ? 454  ILE   A HA   1 
ATOM   6951  H  HB   . ILE   A 1 454 ? 8.081  29.578  20.767 1.00 12.17 ? 454  ILE   A HB   1 
ATOM   6952  H  HG12 . ILE   A 1 454 ? 8.734  29.086  18.612 1.00 11.94 ? 454  ILE   A HG12 1 
ATOM   6953  H  HG13 . ILE   A 1 454 ? 8.999  27.838  19.508 1.00 11.94 ? 454  ILE   A HG13 1 
ATOM   6954  H  HG21 . ILE   A 1 454 ? 7.629  27.429  21.553 1.00 16.80 ? 454  ILE   A HG21 1 
ATOM   6955  H  HG22 . ILE   A 1 454 ? 6.461  28.425  21.945 1.00 16.80 ? 454  ILE   A HG22 1 
ATOM   6956  H  HG23 . ILE   A 1 454 ? 6.272  27.419  20.736 1.00 16.80 ? 454  ILE   A HG23 1 
ATOM   6957  H  HD11 . ILE   A 1 454 ? 8.065  27.158  17.481 1.00 13.81 ? 454  ILE   A HD11 1 
ATOM   6958  H  HD12 . ILE   A 1 454 ? 7.066  26.801  18.657 1.00 13.81 ? 454  ILE   A HD12 1 
ATOM   6959  H  HD13 . ILE   A 1 454 ? 6.797  28.068  17.747 1.00 13.81 ? 454  ILE   A HD13 1 
ATOM   6960  N  N    . ASN   A 1 455 ? 5.908  31.644  21.336 1.00 12.68 ? 455  ASN   A N    1 
ATOM   6961  C  CA   . ASN   A 1 455 ? 5.135  32.270  22.442 1.00 13.91 ? 455  ASN   A CA   1 
ATOM   6962  C  C    . ASN   A 1 455 ? 3.681  32.504  22.000 1.00 14.49 ? 455  ASN   A C    1 
ATOM   6963  O  O    . ASN   A 1 455 ? 2.780  31.960  22.648 1.00 13.48 ? 455  ASN   A O    1 
ATOM   6964  C  CB   . ASN   A 1 455 ? 5.806  33.544  22.963 1.00 14.27 ? 455  ASN   A CB   1 
ATOM   6965  C  CG   . ASN   A 1 455 ? 6.771  33.273  24.098 1.00 15.93 ? 455  ASN   A CG   1 
ATOM   6966  O  OD1  . ASN   A 1 455 ? 7.159  32.131  24.327 1.00 15.80 ? 455  ASN   A OD1  1 
ATOM   6967  N  ND2  . ASN   A 1 455 ? 7.159  34.315  24.814 1.00 17.84 ? 455  ASN   A ND2  1 
ATOM   6968  H  H    . ASN   A 1 455 ? 6.618  32.068  21.102 1.00 15.22 ? 455  ASN   A H    1 
ATOM   6969  H  HA   . ASN   A 1 455 ? 5.122  31.657  23.194 1.00 16.70 ? 455  ASN   A HA   1 
ATOM   6970  H  HB2  . ASN   A 1 455 ? 6.281  33.976  22.236 1.00 17.13 ? 455  ASN   A HB2  1 
ATOM   6971  H  HB3  . ASN   A 1 455 ? 5.124  34.164  23.264 1.00 17.13 ? 455  ASN   A HB3  1 
ATOM   6972  H  HD21 . ASN   A 1 455 ? 7.705  34.207  25.470 1.00 21.42 ? 455  ASN   A HD21 1 
ATOM   6973  H  HD22 . ASN   A 1 455 ? 6.866  35.101  24.624 1.00 21.42 ? 455  ASN   A HD22 1 
ATOM   6974  N  N    . PRO   A 1 456 ? 3.392  33.326  20.966 1.00 16.97 ? 456  PRO   A N    1 
ATOM   6975  C  CA   . PRO   A 1 456 ? 2.000  33.585  20.594 1.00 14.89 ? 456  PRO   A CA   1 
ATOM   6976  C  C    . PRO   A 1 456 ? 1.338  32.444  19.805 1.00 15.51 ? 456  PRO   A C    1 
ATOM   6977  O  O    . PRO   A 1 456 ? 0.155  32.243  19.960 1.00 14.32 ? 456  PRO   A O    1 
ATOM   6978  C  CB   . PRO   A 1 456 ? 2.096  34.817  19.682 1.00 14.84 ? 456  PRO   A CB   1 
ATOM   6979  C  CG   . PRO   A 1 456 ? 3.479  34.731  19.080 1.00 15.97 ? 456  PRO   A CG   1 
ATOM   6980  C  CD   . PRO   A 1 456 ? 4.339  34.108  20.159 1.00 12.90 ? 456  PRO   A CD   1 
ATOM   6981  H  HA   . PRO   A 1 456 ? 1.456  33.694  21.390 1.00 17.88 ? 456  PRO   A HA   1 
ATOM   6982  H  HB2  . PRO   A 1 456 ? 1.410  34.804  18.996 1.00 17.81 ? 456  PRO   A HB2  1 
ATOM   6983  H  HB3  . PRO   A 1 456 ? 1.979  35.639  20.184 1.00 17.81 ? 456  PRO   A HB3  1 
ATOM   6984  H  HG2  . PRO   A 1 456 ? 3.479  34.190  18.275 1.00 19.17 ? 456  PRO   A HG2  1 
ATOM   6985  H  HG3  . PRO   A 1 456 ? 3.809  35.609  18.831 1.00 19.17 ? 456  PRO   A HG3  1 
ATOM   6986  H  HD2  . PRO   A 1 456 ? 5.031  33.544  19.779 1.00 15.48 ? 456  PRO   A HD2  1 
ATOM   6987  H  HD3  . PRO   A 1 456 ? 4.785  34.785  20.692 1.00 15.48 ? 456  PRO   A HD3  1 
ATOM   6988  N  N    . GLU   A 1 457 ? 2.107  31.734  18.983 1.00 13.70 ? 457  GLU   A N    1 
ATOM   6989  C  CA   . GLU   A 1 457 ? 1.485  30.709  18.097 1.00 12.13 ? 457  GLU   A CA   1 
ATOM   6990  C  C    . GLU   A 1 457 ? 1.177  29.420  18.871 1.00 14.95 ? 457  GLU   A C    1 
ATOM   6991  O  O    . GLU   A 1 457 ? 0.281  28.686  18.437 1.00 13.19 ? 457  GLU   A O    1 
ATOM   6992  C  CB   . GLU   A 1 457 ? 2.376  30.459  16.877 1.00 11.09 ? 457  GLU   A CB   1 
ATOM   6993  C  CG   . GLU   A 1 457 ? 2.392  31.616  15.897 1.00 14.29 ? 457  GLU   A CG   1 
ATOM   6994  C  CD   . GLU   A 1 457 ? 3.149  31.333  14.612 1.00 12.10 ? 457  GLU   A CD   1 
ATOM   6995  O  OE1  . GLU   A 1 457 ? 4.391  31.296  14.658 1.00 11.62 ? 457  GLU   A OE1  1 
ATOM   6996  O  OE2  . GLU   A 1 457 ? 2.494  31.147  13.573 1.00 10.77 ? 457  GLU   A OE2  1 
ATOM   6997  H  H    . GLU   A 1 457 ? 2.960  31.814  18.913 1.00 16.45 ? 457  GLU   A H    1 
ATOM   6998  H  HA   . GLU   A 1 457 ? 0.634  31.045  17.775 1.00 14.56 ? 457  GLU   A HA   1 
ATOM   6999  H  HB2  . GLU   A 1 457 ? 3.282  30.285  17.177 1.00 13.31 ? 457  GLU   A HB2  1 
ATOM   7000  H  HB3  . GLU   A 1 457 ? 2.070  29.660  16.419 1.00 13.31 ? 457  GLU   A HB3  1 
ATOM   7001  H  HG2  . GLU   A 1 457 ? 1.477  31.852  15.676 1.00 17.15 ? 457  GLU   A HG2  1 
ATOM   7002  H  HG3  . GLU   A 1 457 ? 2.788  32.388  16.330 1.00 17.15 ? 457  GLU   A HG3  1 
ATOM   7003  N  N    . ILE   A 1 458 ? 1.892  29.157  19.963 1.00 15.14 ? 458  ILE   A N    1 
ATOM   7004  C  CA   . ILE   A 1 458 ? 1.694  27.866  20.687 1.00 16.01 ? 458  ILE   A CA   1 
ATOM   7005  C  C    . ILE   A 1 458 ? 1.352  28.113  22.159 1.00 14.41 ? 458  ILE   A C    1 
ATOM   7006  O  O    . ILE   A 1 458 ? 0.404  27.481  22.646 1.00 12.68 ? 458  ILE   A O    1 
ATOM   7007  C  CB   . ILE   A 1 458 ? 2.961  26.994  20.563 1.00 14.92 ? 458  ILE   A CB   1 
ATOM   7008  C  CG1  . ILE   A 1 458 ? 3.276  26.646  19.106 1.00 18.33 ? 458  ILE   A CG1  1 
ATOM   7009  C  CG2  . ILE   A 1 458 ? 2.855  25.751  21.434 1.00 16.31 ? 458  ILE   A CG2  1 
ATOM   7010  C  CD1  . ILE   A 1 458 ? 2.538  25.434  18.596 1.00 20.64 ? 458  ILE   A CD1  1 
ATOM   7011  H  H    . ILE   A 1 458 ? 2.481  29.683  20.304 1.00 18.17 ? 458  ILE   A H    1 
ATOM   7012  H  HA   . ILE   A 1 458 ? 0.948  27.396  20.283 1.00 19.22 ? 458  ILE   A HA   1 
ATOM   7013  H  HB   . ILE   A 1 458 ? 3.709  27.518  20.890 1.00 17.91 ? 458  ILE   A HB   1 
ATOM   7014  H  HG12 . ILE   A 1 458 ? 3.057  27.407  18.546 1.00 22.00 ? 458  ILE   A HG12 1 
ATOM   7015  H  HG13 . ILE   A 1 458 ? 4.230  26.494  19.018 1.00 22.00 ? 458  ILE   A HG13 1 
ATOM   7016  H  HG21 . ILE   A 1 458 ? 3.661  25.220  21.340 1.00 19.58 ? 458  ILE   A HG21 1 
ATOM   7017  H  HG22 . ILE   A 1 458 ? 2.748  26.014  22.362 1.00 19.58 ? 458  ILE   A HG22 1 
ATOM   7018  H  HG23 . ILE   A 1 458 ? 2.088  25.226  21.157 1.00 19.58 ? 458  ILE   A HG23 1 
ATOM   7019  H  HD11 . ILE   A 1 458 ? 2.783  25.271  17.672 1.00 24.77 ? 458  ILE   A HD11 1 
ATOM   7020  H  HD12 . ILE   A 1 458 ? 2.774  24.662  19.133 1.00 24.77 ? 458  ILE   A HD12 1 
ATOM   7021  H  HD13 . ILE   A 1 458 ? 1.582  25.589  18.654 1.00 24.77 ? 458  ILE   A HD13 1 
ATOM   7022  N  N    . LEU   A 1 459 ? 2.075  29.008  22.837 1.00 15.05 ? 459  LEU   A N    1 
ATOM   7023  C  CA   . LEU   A 1 459 ? 1.893  29.159  24.311 1.00 15.23 ? 459  LEU   A CA   1 
ATOM   7024  C  C    . LEU   A 1 459 ? 0.865  30.234  24.705 1.00 18.50 ? 459  LEU   A C    1 
ATOM   7025  O  O    . LEU   A 1 459 ? 0.447  30.218  25.869 1.00 18.93 ? 459  LEU   A O    1 
ATOM   7026  C  CB   . LEU   A 1 459 ? 3.263  29.463  24.929 1.00 17.69 ? 459  LEU   A CB   1 
ATOM   7027  C  CG   . LEU   A 1 459 ? 4.357  28.440  24.630 1.00 16.22 ? 459  LEU   A CG   1 
ATOM   7028  C  CD1  . LEU   A 1 459 ? 5.706  28.931  25.131 1.00 16.17 ? 459  LEU   A CD1  1 
ATOM   7029  C  CD2  . LEU   A 1 459 ? 4.019  27.091  25.245 1.00 18.95 ? 459  LEU   A CD2  1 
ATOM   7030  H  H    . LEU   A 1 459 ? 2.663  29.529  22.487 1.00 18.06 ? 459  LEU   A H    1 
ATOM   7031  H  HA   . LEU   A 1 459 ? 1.530  28.327  24.654 1.00 18.28 ? 459  LEU   A HA   1 
ATOM   7032  H  HB2  . LEU   A 1 459 ? 3.558  30.331  24.613 1.00 21.23 ? 459  LEU   A HB2  1 
ATOM   7033  H  HB3  . LEU   A 1 459 ? 3.159  29.531  25.891 1.00 21.23 ? 459  LEU   A HB3  1 
ATOM   7034  H  HG   . LEU   A 1 459 ? 4.410  28.331  23.668 1.00 19.46 ? 459  LEU   A HG   1 
ATOM   7035  H  HD11 . LEU   A 1 459 ? 6.386  28.269  24.932 1.00 19.41 ? 459  LEU   A HD11 1 
ATOM   7036  H  HD12 . LEU   A 1 459 ? 5.930  29.766  24.691 1.00 19.41 ? 459  LEU   A HD12 1 
ATOM   7037  H  HD13 . LEU   A 1 459 ? 5.664  29.072  26.090 1.00 19.41 ? 459  LEU   A HD13 1 
ATOM   7038  H  HD21 . LEU   A 1 459 ? 4.725  26.457  25.044 1.00 22.74 ? 459  LEU   A HD21 1 
ATOM   7039  H  HD22 . LEU   A 1 459 ? 3.935  27.186  26.207 1.00 22.74 ? 459  LEU   A HD22 1 
ATOM   7040  H  HD23 . LEU   A 1 459 ? 3.181  26.768  24.878 1.00 22.74 ? 459  LEU   A HD23 1 
ATOM   7041  N  N    . GLY   A 1 460 ? 0.497  31.137  23.796 1.00 17.38 ? 460  GLY   A N    1 
ATOM   7042  C  CA   . GLY   A 1 460 ? -0.541 32.147  24.097 1.00 20.51 ? 460  GLY   A CA   1 
ATOM   7043  C  C    . GLY   A 1 460 ? 0.015  33.421  24.716 1.00 18.44 ? 460  GLY   A C    1 
ATOM   7044  O  O    . GLY   A 1 460 ? -0.762 34.137  25.362 1.00 16.14 ? 460  GLY   A O    1 
ATOM   7045  H  H    . GLY   A 1 460 ? 0.828  31.188  23.004 1.00 20.86 ? 460  GLY   A H    1 
ATOM   7046  H  HA2  . GLY   A 1 460 ? -1.011 32.372  23.279 1.00 24.61 ? 460  GLY   A HA2  1 
ATOM   7047  H  HA3  . GLY   A 1 460 ? -1.193 31.760  24.702 1.00 24.61 ? 460  GLY   A HA3  1 
ATOM   7048  N  N    . TYR   A 1 461 ? 1.302  33.695  24.507 1.00 17.32 ? 461  TYR   A N    1 
ATOM   7049  C  CA   . TYR   A 1 461 ? 1.916  34.940  25.032 1.00 19.45 ? 461  TYR   A CA   1 
ATOM   7050  C  C    . TYR   A 1 461 ? 2.313  35.843  23.864 1.00 15.29 ? 461  TYR   A C    1 
ATOM   7051  O  O    . TYR   A 1 461 ? 2.999  35.368  22.951 1.00 16.84 ? 461  TYR   A O    1 
ATOM   7052  C  CB   . TYR   A 1 461 ? 3.142  34.618  25.887 1.00 16.02 ? 461  TYR   A CB   1 
ATOM   7053  C  CG   . TYR   A 1 461 ? 2.833  34.013  27.232 1.00 18.04 ? 461  TYR   A CG   1 
ATOM   7054  C  CD1  . TYR   A 1 461 ? 2.500  32.674  27.354 1.00 18.17 ? 461  TYR   A CD1  1 
ATOM   7055  C  CD2  . TYR   A 1 461 ? 2.874  34.777  28.385 1.00 17.73 ? 461  TYR   A CD2  1 
ATOM   7056  C  CE1  . TYR   A 1 461 ? 2.216  32.110  28.586 1.00 21.72 ? 461  TYR   A CE1  1 
ATOM   7057  C  CE2  . TYR   A 1 461 ? 2.594  34.229  29.625 1.00 17.76 ? 461  TYR   A CE2  1 
ATOM   7058  C  CZ   . TYR   A 1 461 ? 2.261  32.891  29.727 1.00 18.76 ? 461  TYR   A CZ   1 
ATOM   7059  O  OH   . TYR   A 1 461 ? 1.980  32.340  30.953 1.00 19.02 ? 461  TYR   A OH   1 
ATOM   7060  H  H    . TYR   A 1 461 ? 1.840  33.186  24.070 1.00 20.79 ? 461  TYR   A H    1 
ATOM   7061  H  HA   . TYR   A 1 461 ? 1.269  35.399  25.590 1.00 23.34 ? 461  TYR   A HA   1 
ATOM   7062  H  HB2  . TYR   A 1 461 ? 3.712  34.007  25.395 1.00 19.23 ? 461  TYR   A HB2  1 
ATOM   7063  H  HB3  . TYR   A 1 461 ? 3.650  35.433  26.022 1.00 19.23 ? 461  TYR   A HB3  1 
ATOM   7064  H  HD1  . TYR   A 1 461 ? 2.466  32.142  26.592 1.00 21.81 ? 461  TYR   A HD1  1 
ATOM   7065  H  HD2  . TYR   A 1 461 ? 3.095  35.679  28.326 1.00 21.28 ? 461  TYR   A HD2  1 
ATOM   7066  H  HE1  . TYR   A 1 461 ? 1.996  31.209  28.646 1.00 26.07 ? 461  TYR   A HE1  1 
ATOM   7067  H  HE2  . TYR   A 1 461 ? 2.630  34.760  30.388 1.00 21.32 ? 461  TYR   A HE2  1 
ATOM   7068  H  HH   . TYR   A 1 461 ? 1.872  32.953  31.518 1.00 22.82 ? 461  TYR   A HH   1 
ATOM   7069  N  N    . PRO   A 1 462 ? 1.929  37.136  23.864 1.00 18.91 ? 462  PRO   A N    1 
ATOM   7070  C  CA   . PRO   A 1 462 ? 1.044  37.703  24.888 1.00 19.46 ? 462  PRO   A CA   1 
ATOM   7071  C  C    . PRO   A 1 462 ? -0.423 37.363  24.610 1.00 19.74 ? 462  PRO   A C    1 
ATOM   7072  O  O    . PRO   A 1 462 ? -1.249 37.608  25.459 1.00 21.18 ? 462  PRO   A O    1 
ATOM   7073  C  CB   . PRO   A 1 462 ? 1.259  39.204  24.700 1.00 19.99 ? 462  PRO   A CB   1 
ATOM   7074  C  CG   . PRO   A 1 462 ? 1.536  39.354  23.227 1.00 23.19 ? 462  PRO   A CG   1 
ATOM   7075  C  CD   . PRO   A 1 462 ? 2.353  38.130  22.877 1.00 19.29 ? 462  PRO   A CD   1 
ATOM   7076  H  HA   . PRO   A 1 462 ? 1.234  37.371  25.779 1.00 23.35 ? 462  PRO   A HA   1 
ATOM   7077  H  HB2  . PRO   A 1 462 ? 0.476  39.711  24.967 1.00 23.99 ? 462  PRO   A HB2  1 
ATOM   7078  H  HB3  . PRO   A 1 462 ? 2.001  39.526  25.235 1.00 23.99 ? 462  PRO   A HB3  1 
ATOM   7079  H  HG2  . PRO   A 1 462 ? 0.714  39.390  22.714 1.00 27.83 ? 462  PRO   A HG2  1 
ATOM   7080  H  HG3  . PRO   A 1 462 ? 2.024  40.171  23.039 1.00 27.83 ? 462  PRO   A HG3  1 
ATOM   7081  H  HD2  . PRO   A 1 462 ? 2.176  37.831  21.971 1.00 23.15 ? 462  PRO   A HD2  1 
ATOM   7082  H  HD3  . PRO   A 1 462 ? 3.305  38.308  22.937 1.00 23.15 ? 462  PRO   A HD3  1 
ATOM   7083  N  N    . GLU   A 1 463 ? -0.711 36.853  23.413 1.00 19.49 ? 463  GLU   A N    1 
ATOM   7084  C  CA   . GLU   A 1 463 ? -2.075 36.397  23.050 1.00 18.50 ? 463  GLU   A CA   1 
ATOM   7085  C  C    . GLU   A 1 463 ? -1.903 35.098  22.263 1.00 18.10 ? 463  GLU   A C    1 
ATOM   7086  O  O    . GLU   A 1 463 ? -0.776 34.818  21.842 1.00 18.92 ? 463  GLU   A O    1 
ATOM   7087  C  CB   . GLU   A 1 463 ? -2.787 37.434  22.184 1.00 22.12 ? 463  GLU   A CB   1 
ATOM   7088  C  CG   . GLU   A 1 463 ? -2.165 37.584  20.809 1.00 25.25 ? 463  GLU   A CG   1 
ATOM   7089  C  CD   . GLU   A 1 463 ? -2.602 38.818  20.038 1.00 28.38 ? 463  GLU   A CD   1 
ATOM   7090  O  OE1  . GLU   A 1 463 ? -3.730 38.811  19.514 1.00 30.46 ? 463  GLU   A OE1  1 
ATOM   7091  O  OE2  . GLU   A 1 463 ? -1.812 39.778  19.963 1.00 33.70 ? 463  GLU   A OE2  1 
ATOM   7092  H  H    . GLU   A 1 463 ? -0.131 36.758  22.785 1.00 23.39 ? 463  GLU   A H    1 
ATOM   7093  H  HA   . GLU   A 1 463 ? -2.613 36.267  23.846 1.00 22.20 ? 463  GLU   A HA   1 
ATOM   7094  H  HB2  . GLU   A 1 463 ? -3.719 37.182  22.086 1.00 26.55 ? 463  GLU   A HB2  1 
ATOM   7095  H  HB3  . GLU   A 1 463 ? -2.771 38.292  22.636 1.00 26.55 ? 463  GLU   A HB3  1 
ATOM   7096  H  HG2  . GLU   A 1 463 ? -1.200 37.605  20.906 1.00 30.31 ? 463  GLU   A HG2  1 
ATOM   7097  H  HG3  . GLU   A 1 463 ? -2.381 36.798  20.284 1.00 30.31 ? 463  GLU   A HG3  1 
ATOM   7098  N  N    . LYS   A 1 464 ? -2.984 34.343  22.068 1.00 18.21 ? 464  LYS   A N    1 
ATOM   7099  C  CA   . LYS   A 1 464 ? -2.911 33.098  21.262 1.00 19.11 ? 464  LYS   A CA   1 
ATOM   7100  C  C    . LYS   A 1 464 ? -3.250 33.404  19.803 1.00 19.56 ? 464  LYS   A C    1 
ATOM   7101  O  O    . LYS   A 1 464 ? -4.308 33.995  19.557 1.00 20.58 ? 464  LYS   A O    1 
ATOM   7102  C  CB   . LYS   A 1 464 ? -3.874 32.036  21.798 1.00 20.22 ? 464  LYS   A CB   1 
ATOM   7103  C  CG   . LYS   A 1 464 ? -3.761 30.671  21.132 1.00 19.13 ? 464  LYS   A CG   1 
ATOM   7104  C  CD   . LYS   A 1 464 ? -2.388 30.050  21.275 1.00 18.84 ? 464  LYS   A CD   1 
ATOM   7105  C  CE   . LYS   A 1 464 ? -2.304 28.651  20.702 1.00 22.22 ? 464  LYS   A CE   1 
ATOM   7106  N  NZ   . LYS   A 1 464 ? -2.577 28.638  19.246 1.00 21.01 ? 464  LYS   A NZ   1 
ATOM   7107  H  H    . LYS   A 1 464 ? -3.763 34.522  22.384 1.00 21.85 ? 464  LYS   A H    1 
ATOM   7108  H  HA   . LYS   A 1 464 ? -2.007 32.752  21.324 1.00 22.94 ? 464  LYS   A HA   1 
ATOM   7109  H  HB2  . LYS   A 1 464 ? -3.720 31.930  22.750 1.00 24.26 ? 464  LYS   A HB2  1 
ATOM   7110  H  HB3  . LYS   A 1 464 ? -4.782 32.359  21.691 1.00 24.26 ? 464  LYS   A HB3  1 
ATOM   7111  H  HG2  . LYS   A 1 464 ? -4.421 30.074  21.517 1.00 22.96 ? 464  LYS   A HG2  1 
ATOM   7112  H  HG3  . LYS   A 1 464 ? -3.973 30.759  20.190 1.00 22.96 ? 464  LYS   A HG3  1 
ATOM   7113  H  HD2  . LYS   A 1 464 ? -1.736 30.615  20.831 1.00 22.61 ? 464  LYS   A HD2  1 
ATOM   7114  H  HD3  . LYS   A 1 464 ? -2.148 30.024  22.214 1.00 22.61 ? 464  LYS   A HD3  1 
ATOM   7115  H  HE2  . LYS   A 1 464 ? -1.421 28.285  20.869 1.00 26.67 ? 464  LYS   A HE2  1 
ATOM   7116  H  HE3  . LYS   A 1 464 ? -2.940 28.076  21.156 1.00 26.67 ? 464  LYS   A HE3  1 
ATOM   7117  H  HZ1  . LYS   A 1 464 ? -2.161 27.946  18.872 1.00 25.21 ? 464  LYS   A HZ1  1 
ATOM   7118  H  HZ2  . LYS   A 1 464 ? -3.453 28.567  19.109 1.00 25.21 ? 464  LYS   A HZ2  1 
ATOM   7119  H  HZ3  . LYS   A 1 464 ? -2.280 29.394  18.881 1.00 25.21 ? 464  LYS   A HZ3  1 
ATOM   7120  N  N    . LEU   A 1 465 ? -2.370 33.016  18.880 1.00 18.69 ? 465  LEU   A N    1 
ATOM   7121  C  CA   . LEU   A 1 465 ? -2.657 33.189  17.436 1.00 16.96 ? 465  LEU   A CA   1 
ATOM   7122  C  C    . LEU   A 1 465 ? -2.901 31.811  16.817 1.00 18.81 ? 465  LEU   A C    1 
ATOM   7123  O  O    . LEU   A 1 465 ? -2.438 30.818  17.400 1.00 18.48 ? 465  LEU   A O    1 
ATOM   7124  C  CB   . LEU   A 1 465 ? -1.458 33.861  16.761 1.00 15.89 ? 465  LEU   A CB   1 
ATOM   7125  C  CG   . LEU   A 1 465 ? -1.061 35.233  17.299 1.00 16.89 ? 465  LEU   A CG   1 
ATOM   7126  C  CD1  . LEU   A 1 465 ? 0.168  35.752  16.570 1.00 20.18 ? 465  LEU   A CD1  1 
ATOM   7127  C  CD2  . LEU   A 1 465 ? -2.210 36.219  17.172 1.00 21.17 ? 465  LEU   A CD2  1 
ATOM   7128  H  H    . LEU   A 1 465 ? -1.610 32.655  19.056 1.00 22.43 ? 465  LEU   A H    1 
ATOM   7129  H  HA   . LEU   A 1 465 ? -3.442 33.745  17.312 1.00 20.36 ? 465  LEU   A HA   1 
ATOM   7130  H  HB2  . LEU   A 1 465 ? -0.693 33.270  16.840 1.00 19.07 ? 465  LEU   A HB2  1 
ATOM   7131  H  HB3  . LEU   A 1 465 ? -1.651 33.949  15.815 1.00 19.07 ? 465  LEU   A HB3  1 
ATOM   7132  H  HG   . LEU   A 1 465 ? -0.847 35.139  18.240 1.00 20.27 ? 465  LEU   A HG   1 
ATOM   7133  H  HD11 . LEU   A 1 465 ? 0.409  36.623  16.921 1.00 24.22 ? 465  LEU   A HD11 1 
ATOM   7134  H  HD12 . LEU   A 1 465 ? 0.906  35.136  16.700 1.00 24.22 ? 465  LEU   A HD12 1 
ATOM   7135  H  HD13 . LEU   A 1 465 ? -0.026 35.828  15.623 1.00 24.22 ? 465  LEU   A HD13 1 
ATOM   7136  H  HD21 . LEU   A 1 465 ? -1.936 37.082  17.519 1.00 25.40 ? 465  LEU   A HD21 1 
ATOM   7137  H  HD22 . LEU   A 1 465 ? -2.457 36.310  16.238 1.00 25.40 ? 465  LEU   A HD22 1 
ATOM   7138  H  HD23 . LEU   A 1 465 ? -2.972 35.895  17.677 1.00 25.40 ? 465  LEU   A HD23 1 
ATOM   7139  N  N    . ASP   A 1 466 ? -3.606 31.760  15.687 1.00 16.16 ? 466  ASP   A N    1 
ATOM   7140  C  CA   . ASP   A 1 466 ? -3.775 30.479  14.957 1.00 16.32 ? 466  ASP   A CA   1 
ATOM   7141  C  C    . ASP   A 1 466 ? -2.446 30.176  14.258 1.00 16.23 ? 466  ASP   A C    1 
ATOM   7142  O  O    . ASP   A 1 466 ? -2.092 30.915  13.334 1.00 16.29 ? 466  ASP   A O    1 
ATOM   7143  C  CB   . ASP   A 1 466 ? -4.954 30.564  13.987 1.00 19.08 ? 466  ASP   A CB   1 
ATOM   7144  C  CG   . ASP   A 1 466 ? -5.095 29.374  13.055 1.00 23.29 ? 466  ASP   A CG   1 
ATOM   7145  O  OD1  . ASP   A 1 466 ? -4.338 28.401  13.219 1.00 21.36 ? 466  ASP   A OD1  1 
ATOM   7146  O  OD2  . ASP   A 1 466 ? -5.969 29.436  12.173 1.00 23.23 ? 466  ASP   A OD2  1 
ATOM   7147  H  H    . ASP   A 1 466 ? -3.992 32.437  15.323 1.00 19.40 ? 466  ASP   A H    1 
ATOM   7148  H  HA   . ASP   A 1 466 ? -3.987 29.751  15.562 1.00 19.59 ? 466  ASP   A HA   1 
ATOM   7149  H  HB2  . ASP   A 1 466 ? -5.772 30.657  14.499 1.00 22.90 ? 466  ASP   A HB2  1 
ATOM   7150  H  HB3  . ASP   A 1 466 ? -4.861 31.368  13.453 1.00 22.90 ? 466  ASP   A HB3  1 
ATOM   7151  N  N    . ARG   A 1 467 ? -1.747 29.128  14.696 1.00 17.40 ? 467  ARG   A N    1 
ATOM   7152  C  CA   . ARG   A 1 467 ? -0.393 28.832  14.155 1.00 14.65 ? 467  ARG   A CA   1 
ATOM   7153  C  C    . ARG   A 1 467 ? -0.449 28.470  12.667 1.00 13.39 ? 467  ARG   A C    1 
ATOM   7154  O  O    . ARG   A 1 467 ? 0.577  28.592  11.996 1.00 14.45 ? 467  ARG   A O    1 
ATOM   7155  C  CB   . ARG   A 1 467 ? 0.255  27.712  14.976 1.00 13.84 ? 467  ARG   A CB   1 
ATOM   7156  C  CG   . ARG   A 1 467 ? -0.580 26.446  15.097 1.00 17.75 ? 467  ARG   A CG   1 
ATOM   7157  C  CD   . ARG   A 1 467 ? -0.030 25.537  16.180 1.00 17.41 ? 467  ARG   A CD   1 
ATOM   7158  N  NE   . ARG   A 1 467 ? -0.750 24.279  16.310 1.00 18.10 ? 467  ARG   A NE   1 
ATOM   7159  C  CZ   . ARG   A 1 467 ? -0.380 23.137  15.743 1.00 19.65 ? 467  ARG   A CZ   1 
ATOM   7160  N  NH1  . ARG   A 1 467 ? 0.589  23.126  14.846 1.00 16.85 ? 467  ARG   A NH1  1 
ATOM   7161  N  NH2  . ARG   A 1 467 ? -0.985 22.010  16.072 1.00 22.05 ? 467  ARG   A NH2  1 
ATOM   7162  H  H    . ARG   A 1 467 ? -2.023 28.577  15.296 1.00 20.89 ? 467  ARG   A H    1 
ATOM   7163  H  HA   . ARG   A 1 467 ? 0.152  29.631  14.230 1.00 17.58 ? 467  ARG   A HA   1 
ATOM   7164  H  HB2  . ARG   A 1 467 ? 1.108  27.485  14.574 1.00 16.61 ? 467  ARG   A HB2  1 
ATOM   7165  H  HB3  . ARG   A 1 467 ? 0.442  28.048  15.867 1.00 16.61 ? 467  ARG   A HB3  1 
ATOM   7166  H  HG2  . ARG   A 1 467 ? -1.499 26.679  15.301 1.00 21.30 ? 467  ARG   A HG2  1 
ATOM   7167  H  HG3  . ARG   A 1 467 ? -0.588 25.976  14.248 1.00 21.30 ? 467  ARG   A HG3  1 
ATOM   7168  H  HD2  . ARG   A 1 467 ? 0.902  25.349  15.990 1.00 20.90 ? 467  ARG   A HD2  1 
ATOM   7169  H  HD3  . ARG   A 1 467 ? -0.058 26.005  17.029 1.00 20.90 ? 467  ARG   A HD3  1 
ATOM   7170  H  HE   . ARG   A 1 467 ? -1.465 24.275  16.788 1.00 21.73 ? 467  ARG   A HE   1 
ATOM   7171  H  HH11 . ARG   A 1 467 ? 0.982  23.859  14.628 1.00 20.23 ? 467  ARG   A HH11 1 
ATOM   7172  H  HH12 . ARG   A 1 467 ? 0.827  22.385  14.480 1.00 20.23 ? 467  ARG   A HH12 1 
ATOM   7173  H  HH21 . ARG   A 1 467 ? -1.619 22.016  16.653 1.00 26.47 ? 467  ARG   A HH21 1 
ATOM   7174  H  HH22 . ARG   A 1 467 ? -0.745 21.270  15.705 1.00 26.47 ? 467  ARG   A HH22 1 
ATOM   7175  N  N    . PHE   A 1 468 ? -1.613 28.038  12.178 1.00 14.31 ? 468  PHE   A N    1 
ATOM   7176  C  CA   . PHE   A 1 468 ? -1.728 27.620  10.759 1.00 15.35 ? 468  PHE   A CA   1 
ATOM   7177  C  C    . PHE   A 1 468 ? -2.045 28.829  9.874  1.00 16.04 ? 468  PHE   A C    1 
ATOM   7178  O  O    . PHE   A 1 468 ? -1.887 28.728  8.648  1.00 17.38 ? 468  PHE   A O    1 
ATOM   7179  C  CB   . PHE   A 1 468 ? -2.827 26.566  10.605 1.00 18.74 ? 468  PHE   A CB   1 
ATOM   7180  C  CG   . PHE   A 1 468 ? -2.647 25.343  11.467 1.00 16.69 ? 468  PHE   A CG   1 
ATOM   7181  C  CD1  . PHE   A 1 468 ? -1.577 24.489  11.268 1.00 16.12 ? 468  PHE   A CD1  1 
ATOM   7182  C  CD2  . PHE   A 1 468 ? -3.546 25.049  12.479 1.00 20.63 ? 468  PHE   A CD2  1 
ATOM   7183  C  CE1  . PHE   A 1 468 ? -1.411 23.363  12.058 1.00 19.87 ? 468  PHE   A CE1  1 
ATOM   7184  C  CE2  . PHE   A 1 468 ? -3.378 23.924  13.270 1.00 22.71 ? 468  PHE   A CE2  1 
ATOM   7185  C  CZ   . PHE   A 1 468 ? -2.313 23.082  13.056 1.00 20.28 ? 468  PHE   A CZ   1 
ATOM   7186  H  H    . PHE   A 1 468 ? -2.340 27.977  12.634 1.00 17.17 ? 468  PHE   A H    1 
ATOM   7187  H  HA   . PHE   A 1 468 ? -0.881 27.238  10.481 1.00 18.43 ? 468  PHE   A HA   1 
ATOM   7188  H  HB2  . PHE   A 1 468 ? -3.682 26.973  10.816 1.00 22.49 ? 468  PHE   A HB2  1 
ATOM   7189  H  HB3  . PHE   A 1 468 ? -2.866 26.290  9.676  1.00 22.49 ? 468  PHE   A HB3  1 
ATOM   7190  H  HD1  . PHE   A 1 468 ? -0.961 24.673  10.596 1.00 19.35 ? 468  PHE   A HD1  1 
ATOM   7191  H  HD2  . PHE   A 1 468 ? -4.270 25.613  12.629 1.00 24.76 ? 468  PHE   A HD2  1 
ATOM   7192  H  HE1  . PHE   A 1 468 ? -0.688 22.796  11.913 1.00 23.85 ? 468  PHE   A HE1  1 
ATOM   7193  H  HE2  . PHE   A 1 468 ? -3.987 23.738  13.947 1.00 27.25 ? 468  PHE   A HE2  1 
ATOM   7194  H  HZ   . PHE   A 1 468 ? -2.203 22.325  13.585 1.00 24.34 ? 468  PHE   A HZ   1 
ATOM   7195  N  N    . ALA   A 1 469 ? -2.452 29.940  10.486 1.00 14.53 ? 469  ALA   A N    1 
ATOM   7196  C  CA   . ALA   A 1 469 ? -2.887 31.117  9.703  1.00 17.92 ? 469  ALA   A CA   1 
ATOM   7197  C  C    . ALA   A 1 469 ? -1.704 31.894  9.126  1.00 16.20 ? 469  ALA   A C    1 
ATOM   7198  O  O    . ALA   A 1 469 ? -0.597 31.784  9.675  1.00 12.70 ? 469  ALA   A O    1 
ATOM   7199  C  CB   . ALA   A 1 469 ? -3.730 32.008  10.576 1.00 19.71 ? 469  ALA   A CB   1 
ATOM   7200  H  H    . ALA   A 1 469 ? -2.487 30.040  11.339 1.00 17.43 ? 469  ALA   A H    1 
ATOM   7201  H  HA   . ALA   A 1 469 ? -3.411 30.803  8.949  1.00 21.51 ? 469  ALA   A HA   1 
ATOM   7202  H  HB1  . ALA   A 1 469 ? -4.018 32.782  10.067 1.00 23.65 ? 469  ALA   A HB1  1 
ATOM   7203  H  HB2  . ALA   A 1 469 ? -4.508 31.517  10.885 1.00 23.65 ? 469  ALA   A HB2  1 
ATOM   7204  H  HB3  . ALA   A 1 469 ? -3.208 32.300  11.340 1.00 23.65 ? 469  ALA   A HB3  1 
ATOM   7205  N  N    . LEU   A 1 470 ? -1.961 32.665  8.070  1.00 17.03 ? 470  LEU   A N    1 
ATOM   7206  C  CA   . LEU   A 1 470 ? -0.937 33.494  7.440  1.00 17.33 ? 470  LEU   A CA   1 
ATOM   7207  C  C    . LEU   A 1 470 ? -1.098 34.983  7.730  1.00 17.28 ? 470  LEU   A C    1 
ATOM   7208  O  O    . LEU   A 1 470 ? -0.097 35.676  7.927  1.00 14.13 ? 470  LEU   A O    1 
ATOM   7209  C  CB   . LEU   A 1 470 ? -0.938 33.281  5.921  1.00 19.28 ? 470  LEU   A CB   1 
ATOM   7210  C  CG   . LEU   A 1 470 ? -0.739 31.860  5.383  1.00 15.46 ? 470  LEU   A CG   1 
ATOM   7211  C  CD1  . LEU   A 1 470 ? -0.752 31.865  3.854  1.00 22.30 ? 470  LEU   A CD1  1 
ATOM   7212  C  CD2  . LEU   A 1 470 ? 0.546  31.223  5.917  1.00 17.02 ? 470  LEU   A CD2  1 
ATOM   7213  H  H    . LEU   A 1 470 ? -2.735 32.721  7.699  1.00 20.44 ? 470  LEU   A H    1 
ATOM   7214  H  HA   . LEU   A 1 470 ? -0.093 33.212  7.826  1.00 20.80 ? 470  LEU   A HA   1 
ATOM   7215  H  HB2  . LEU   A 1 470 ? -1.783 33.611  5.577  1.00 23.14 ? 470  LEU   A HB2  1 
ATOM   7216  H  HB3  . LEU   A 1 470 ? -0.240 33.840  5.544  1.00 23.14 ? 470  LEU   A HB3  1 
ATOM   7217  H  HG   . LEU   A 1 470 ? -1.478 31.318  5.699  1.00 18.55 ? 470  LEU   A HG   1 
ATOM   7218  H  HD11 . LEU   A 1 470 ? -0.625 30.961  3.526  1.00 26.76 ? 470  LEU   A HD11 1 
ATOM   7219  H  HD12 . LEU   A 1 470 ? -1.603 32.207  3.539  1.00 26.76 ? 470  LEU   A HD12 1 
ATOM   7220  H  HD13 . LEU   A 1 470 ? -0.036 32.431  3.526  1.00 26.76 ? 470  LEU   A HD13 1 
ATOM   7221  H  HD21 . LEU   A 1 470 ? 0.638  30.327  5.556  1.00 20.43 ? 470  LEU   A HD21 1 
ATOM   7222  H  HD22 . LEU   A 1 470 ? 1.309  31.759  5.649  1.00 20.43 ? 470  LEU   A HD22 1 
ATOM   7223  H  HD23 . LEU   A 1 470 ? 0.507  31.178  6.885  1.00 20.43 ? 470  LEU   A HD23 1 
ATOM   7224  N  N    . ASP   A 1 471 ? -2.330 35.493  7.745  1.00 17.25 ? 471  ASP   A N    1 
ATOM   7225  C  CA   . ASP   A 1 471 ? -2.559 36.925  7.923  1.00 18.76 ? 471  ASP   A CA   1 
ATOM   7226  C  C    . ASP   A 1 471 ? -1.945 37.441  9.220  1.00 16.30 ? 471  ASP   A C    1 
ATOM   7227  O  O    . ASP   A 1 471 ? -2.138 36.862  10.294 1.00 16.22 ? 471  ASP   A O    1 
ATOM   7228  C  CB   . ASP   A 1 471 ? -4.063 37.220  7.906  1.00 20.10 ? 471  ASP   A CB   1 
ATOM   7229  C  CG   . ASP   A 1 471 ? -4.685 37.017  6.536  1.00 26.51 ? 471  ASP   A CG   1 
ATOM   7230  O  OD1  . ASP   A 1 471 ? -3.939 36.944  5.533  1.00 26.03 ? 471  ASP   A OD1  1 
ATOM   7231  O  OD2  . ASP   A 1 471 ? -5.931 36.951  6.465  1.00 28.97 ? 471  ASP   A OD2  1 
ATOM   7232  H  H    . ASP   A 1 471 ? -3.046 35.026  7.654  1.00 20.70 ? 471  ASP   A H    1 
ATOM   7233  H  HA   . ASP   A 1 471 ? -2.126 37.386  7.187  1.00 22.51 ? 471  ASP   A HA   1 
ATOM   7234  H  HB2  . ASP   A 1 471 ? -4.509 36.645  8.548  1.00 24.12 ? 471  ASP   A HB2  1 
ATOM   7235  H  HB3  . ASP   A 1 471 ? -4.213 38.135  8.193  1.00 24.12 ? 471  ASP   A HB3  1 
ATOM   7236  N  N    . GLY   A 1 472 ? -1.149 38.506  9.105  1.00 16.27 ? 472  GLY   A N    1 
ATOM   7237  C  CA   . GLY   A 1 472 ? -0.591 39.171  10.295 1.00 17.53 ? 472  GLY   A CA   1 
ATOM   7238  C  C    . GLY   A 1 472 ? 0.713  38.593  10.815 1.00 15.38 ? 472  GLY   A C    1 
ATOM   7239  O  O    . GLY   A 1 472 ? 1.283  39.200  11.705 1.00 13.24 ? 472  GLY   A O    1 
ATOM   7240  H  H    . GLY   A 1 472 ? -0.919 38.859  8.355  1.00 19.53 ? 472  GLY   A H    1 
ATOM   7241  H  HA2  . GLY   A 1 472 ? -0.451 40.108  10.087 1.00 21.04 ? 472  GLY   A HA2  1 
ATOM   7242  H  HA3  . GLY   A 1 472 ? -1.250 39.133  11.006 1.00 21.04 ? 472  GLY   A HA3  1 
ATOM   7243  N  N    . LYS   A 1 473 ? 1.140  37.449  10.274 1.00 14.01 ? 473  LYS   A N    1 
ATOM   7244  C  CA   . LYS   A 1 473 ? 2.336  36.749  10.818 1.00 13.40 ? 473  LYS   A CA   1 
ATOM   7245  C  C    . LYS   A 1 473 ? 3.628  37.518  10.509 1.00 10.99 ? 473  LYS   A C    1 
ATOM   7246  O  O    . LYS   A 1 473 ? 4.504  37.558  11.381 1.00 12.32 ? 473  LYS   A O    1 
ATOM   7247  C  CB   . LYS   A 1 473 ? 2.397  35.320  10.270 1.00 10.62 ? 473  LYS   A CB   1 
ATOM   7248  C  CG   . LYS   A 1 473 ? 1.296  34.394  10.773 1.00 13.54 ? 473  LYS   A CG   1 
ATOM   7249  C  CD   . LYS   A 1 473 ? 1.210  34.335  12.283 1.00 13.40 ? 473  LYS   A CD   1 
ATOM   7250  C  CE   . LYS   A 1 473 ? 0.040  33.516  12.789 1.00 15.22 ? 473  LYS   A CE   1 
ATOM   7251  N  NZ   . LYS   A 1 473 ? 0.132  32.100  12.364 1.00 15.10 ? 473  LYS   A NZ   1 
ATOM   7252  H  H    . LYS   A 1 473 ? 0.767  37.059  9.604  1.00 16.82 ? 473  LYS   A H    1 
ATOM   7253  H  HA   . LYS   A 1 473 ? 2.254  36.709  11.784 1.00 16.08 ? 473  LYS   A HA   1 
ATOM   7254  H  HB2  . LYS   A 1 473 ? 2.354  35.357  9.302  1.00 12.75 ? 473  LYS   A HB2  1 
ATOM   7255  H  HB3  . LYS   A 1 473 ? 3.257  34.935  10.501 1.00 12.75 ? 473  LYS   A HB3  1 
ATOM   7256  H  HG2  . LYS   A 1 473 ? 0.444  34.692  10.418 1.00 16.25 ? 473  LYS   A HG2  1 
ATOM   7257  H  HG3  . LYS   A 1 473 ? 1.450  33.500  10.429 1.00 16.25 ? 473  LYS   A HG3  1 
ATOM   7258  H  HD2  . LYS   A 1 473 ? 2.033  33.960  12.632 1.00 16.08 ? 473  LYS   A HD2  1 
ATOM   7259  H  HD3  . LYS   A 1 473 ? 1.139  35.237  12.631 1.00 16.08 ? 473  LYS   A HD3  1 
ATOM   7260  H  HE2  . LYS   A 1 473 ? 0.009  33.561  13.757 1.00 18.26 ? 473  LYS   A HE2  1 
ATOM   7261  H  HE3  . LYS   A 1 473 ? -0.788 33.899  12.460 1.00 18.26 ? 473  LYS   A HE3  1 
ATOM   7262  H  HZ1  . LYS   A 1 473 ? -0.493 31.623  12.782 1.00 18.12 ? 473  LYS   A HZ1  1 
ATOM   7263  H  HZ2  . LYS   A 1 473 ? 0.008  32.045  11.484 1.00 18.12 ? 473  LYS   A HZ2  1 
ATOM   7264  H  HZ3  . LYS   A 1 473 ? 0.936  31.780  12.570 1.00 18.12 ? 473  LYS   A HZ3  1 
ATOM   7265  N  N    . ALA   A 1 474 ? 3.740  38.073  9.306  1.00 12.50 ? 474  ALA   A N    1 
ATOM   7266  C  CA   . ALA   A 1 474 ? 4.955  38.831  8.938  1.00 12.70 ? 474  ALA   A CA   1 
ATOM   7267  C  C    . ALA   A 1 474 ? 5.140  39.990  9.919  1.00 11.80 ? 474  ALA   A C    1 
ATOM   7268  O  O    . ALA   A 1 474 ? 6.258  40.177  10.420 1.00 13.07 ? 474  ALA   A O    1 
ATOM   7269  C  CB   . ALA   A 1 474 ? 4.855  39.325  7.520  1.00 15.59 ? 474  ALA   A CB   1 
ATOM   7270  H  H    . ALA   A 1 474 ? 3.140  38.029  8.691  1.00 15.01 ? 474  ALA   A H    1 
ATOM   7271  H  HA   . ALA   A 1 474 ? 5.731  38.251  8.991  1.00 15.25 ? 474  ALA   A HA   1 
ATOM   7272  H  HB1  . ALA   A 1 474 ? 5.658  39.820  7.292  1.00 18.72 ? 474  ALA   A HB1  1 
ATOM   7273  H  HB2  . ALA   A 1 474 ? 4.760  38.569  6.920  1.00 18.72 ? 474  ALA   A HB2  1 
ATOM   7274  H  HB3  . ALA   A 1 474 ? 4.082  39.905  7.433  1.00 18.72 ? 474  ALA   A HB3  1 
ATOM   7275  N  N    . ALA   A 1 475 ? 4.071  40.749  10.153 1.00 14.16 ? 475  ALA   A N    1 
ATOM   7276  C  CA   . ALA   A 1 475 ? 4.165  41.916  11.055 1.00 15.07 ? 475  ALA   A CA   1 
ATOM   7277  C  C    . ALA   A 1 475 ? 4.467  41.445  12.481 1.00 13.60 ? 475  ALA   A C    1 
ATOM   7278  O  O    . ALA   A 1 475 ? 5.241  42.120  13.177 1.00 14.51 ? 475  ALA   A O    1 
ATOM   7279  C  CB   . ALA   A 1 475 ? 2.883  42.709  10.993 1.00 19.72 ? 475  ALA   A CB   1 
ATOM   7280  H  H    . ALA   A 1 475 ? 3.293  40.616  9.811  1.00 17.00 ? 475  ALA   A H    1 
ATOM   7281  H  HA   . ALA   A 1 475 ? 4.890  42.495  10.772 1.00 18.09 ? 475  ALA   A HA   1 
ATOM   7282  H  HB1  . ALA   A 1 475 ? 2.947  43.474  11.586 1.00 23.67 ? 475  ALA   A HB1  1 
ATOM   7283  H  HB2  . ALA   A 1 475 ? 2.735  43.015  10.085 1.00 23.67 ? 475  ALA   A HB2  1 
ATOM   7284  H  HB3  . ALA   A 1 475 ? 2.141  42.148  11.269 1.00 23.67 ? 475  ALA   A HB3  1 
ATOM   7285  N  N    . TYR   A 1 476 ? 3.859  40.335  12.897 1.00 12.91 ? 476  TYR   A N    1 
ATOM   7286  C  CA   . TYR   A 1 476 ? 4.054  39.844  14.286 1.00 12.82 ? 476  TYR   A CA   1 
ATOM   7287  C  C    . TYR   A 1 476 ? 5.503  39.380  14.448 1.00 13.97 ? 476  TYR   A C    1 
ATOM   7288  O  O    . TYR   A 1 476 ? 6.090  39.607  15.514 1.00 13.68 ? 476  TYR   A O    1 
ATOM   7289  C  CB   . TYR   A 1 476 ? 3.065  38.722  14.614 1.00 15.92 ? 476  TYR   A CB   1 
ATOM   7290  C  CG   . TYR   A 1 476 ? 2.486  38.793  16.002 1.00 15.48 ? 476  TYR   A CG   1 
ATOM   7291  C  CD1  . TYR   A 1 476 ? 3.244  38.449  17.108 1.00 20.75 ? 476  TYR   A CD1  1 
ATOM   7292  C  CD2  . TYR   A 1 476 ? 1.185  39.214  16.211 1.00 20.78 ? 476  TYR   A CD2  1 
ATOM   7293  C  CE1  . TYR   A 1 476 ? 2.723  38.515  18.388 1.00 27.11 ? 476  TYR   A CE1  1 
ATOM   7294  C  CE2  . TYR   A 1 476 ? 0.647  39.284  17.484 1.00 26.11 ? 476  TYR   A CE2  1 
ATOM   7295  C  CZ   . TYR   A 1 476 ? 1.418  38.933  18.577 1.00 24.24 ? 476  TYR   A CZ   1 
ATOM   7296  O  OH   . TYR   A 1 476 ? 0.892  39.000  19.842 1.00 29.66 ? 476  TYR   A OH   1 
ATOM   7297  H  H    . TYR   A 1 476 ? 3.338  39.853  12.411 1.00 15.50 ? 476  TYR   A H    1 
ATOM   7298  H  HA   . TYR   A 1 476 ? 3.881  40.564  14.913 1.00 15.38 ? 476  TYR   A HA   1 
ATOM   7299  H  HB2  . TYR   A 1 476 ? 2.340  38.746  13.971 1.00 19.11 ? 476  TYR   A HB2  1 
ATOM   7300  H  HB3  . TYR   A 1 476 ? 3.513  37.868  14.505 1.00 19.11 ? 476  TYR   A HB3  1 
ATOM   7301  H  HD1  . TYR   A 1 476 ? 4.122  38.168  16.988 1.00 24.91 ? 476  TYR   A HD1  1 
ATOM   7302  H  HD2  . TYR   A 1 476 ? 0.661  39.455  15.481 1.00 24.94 ? 476  TYR   A HD2  1 
ATOM   7303  H  HE1  . TYR   A 1 476 ? 3.248  38.279  19.118 1.00 32.53 ? 476  TYR   A HE1  1 
ATOM   7304  H  HE2  . TYR   A 1 476 ? -0.231 39.566  17.604 1.00 31.33 ? 476  TYR   A HE2  1 
ATOM   7305  H  HH   . TYR   A 1 476 ? 0.089  39.243  19.799 1.00 35.60 ? 476  TYR   A HH   1 
ATOM   7306  N  N    . ALA   A 1 477 ? 6.040  38.741  13.408 1.00 12.95 ? 477  ALA   A N    1 
ATOM   7307  C  CA   . ALA   A 1 477 ? 7.437  38.263  13.463 1.00 11.38 ? 477  ALA   A CA   1 
ATOM   7308  C  C    . ALA   A 1 477 ? 8.372  39.471  13.585 1.00 11.70 ? 477  ALA   A C    1 
ATOM   7309  O  O    . ALA   A 1 477 ? 9.288  39.431  14.411 1.00 11.75 ? 477  ALA   A O    1 
ATOM   7310  C  CB   . ALA   A 1 477 ? 7.739  37.423  12.249 1.00 11.76 ? 477  ALA   A CB   1 
ATOM   7311  H  H    . ALA   A 1 477 ? 5.627  38.573  12.672 1.00 15.55 ? 477  ALA   A H    1 
ATOM   7312  H  HA   . ALA   A 1 477 ? 7.574  37.699  14.240 1.00 13.66 ? 477  ALA   A HA   1 
ATOM   7313  H  HB1  . ALA   A 1 477 ? 8.657  37.112  12.291 1.00 14.12 ? 477  ALA   A HB1  1 
ATOM   7314  H  HB2  . ALA   A 1 477 ? 7.140  36.660  12.226 1.00 14.12 ? 477  ALA   A HB2  1 
ATOM   7315  H  HB3  . ALA   A 1 477 ? 7.614  37.955  11.448 1.00 14.12 ? 477  ALA   A HB3  1 
ATOM   7316  N  N    . LYS   A 1 478 ? 8.113  40.518  12.800 1.00 11.75 ? 478  LYS   A N    1 
ATOM   7317  C  CA   . LYS   A 1 478 ? 8.949  41.743  12.886 1.00 11.64 ? 478  LYS   A CA   1 
ATOM   7318  C  C    . LYS   A 1 478 ? 8.934  42.272  14.324 1.00 14.16 ? 478  LYS   A C    1 
ATOM   7319  O  O    . LYS   A 1 478 ? 10.007 42.618  14.837 1.00 12.57 ? 478  LYS   A O    1 
ATOM   7320  C  CB   . LYS   A 1 478 ? 8.459  42.834  11.929 1.00 15.05 ? 478  LYS   A CB   1 
ATOM   7321  C  CG   . LYS   A 1 478 ? 9.235  44.142  12.023 1.00 14.43 ? 478  LYS   A CG   1 
ATOM   7322  C  CD   . LYS   A 1 478 ? 8.723  45.232  11.110 1.00 16.70 ? 478  LYS   A CD   1 
ATOM   7323  C  CE   . LYS   A 1 478 ? 9.566  46.488  11.172 1.00 18.10 ? 478  LYS   A CE   1 
ATOM   7324  N  NZ   . LYS   A 1 478 ? 9.648  47.025  12.550 1.00 17.62 ? 478  LYS   A NZ   1 
ATOM   7325  H  H    . LYS   A 1 478 ? 7.477  40.551  12.222 1.00 14.11 ? 478  LYS   A H    1 
ATOM   7326  H  HA   . LYS   A 1 478 ? 9.853  41.507  12.627 1.00 13.98 ? 478  LYS   A HA   1 
ATOM   7327  H  HB2  . LYS   A 1 478 ? 8.515  42.501  11.020 1.00 18.06 ? 478  LYS   A HB2  1 
ATOM   7328  H  HB3  . LYS   A 1 478 ? 7.523  43.012  12.109 1.00 18.06 ? 478  LYS   A HB3  1 
ATOM   7329  H  HG2  . LYS   A 1 478 ? 9.204  44.460  12.939 1.00 17.32 ? 478  LYS   A HG2  1 
ATOM   7330  H  HG3  . LYS   A 1 478 ? 10.166 43.970  11.814 1.00 17.32 ? 478  LYS   A HG3  1 
ATOM   7331  H  HD2  . LYS   A 1 478 ? 8.706  44.903  10.198 1.00 20.04 ? 478  LYS   A HD2  1 
ATOM   7332  H  HD3  . LYS   A 1 478 ? 7.809  45.448  11.351 1.00 20.04 ? 478  LYS   A HD3  1 
ATOM   7333  H  HE2  . LYS   A 1 478 ? 10.459 46.295  10.846 1.00 21.73 ? 478  LYS   A HE2  1 
ATOM   7334  H  HE3  . LYS   A 1 478 ? 9.188  47.161  10.584 1.00 21.73 ? 478  LYS   A HE3  1 
ATOM   7335  H  HZ1  . LYS   A 1 478 ? 10.023 47.832  12.533 1.00 21.15 ? 478  LYS   A HZ1  1 
ATOM   7336  H  HZ2  . LYS   A 1 478 ? 8.830  47.086  12.894 1.00 21.15 ? 478  LYS   A HZ2  1 
ATOM   7337  H  HZ3  . LYS   A 1 478 ? 10.141 46.480  13.052 1.00 21.15 ? 478  LYS   A HZ3  1 
ATOM   7338  N  N    . LEU   A 1 479 ? 7.745  42.352  14.930 1.00 12.08 ? 479  LEU   A N    1 
ATOM   7339  C  CA   . LEU   A 1 479 ? 7.629  42.885  16.311 1.00 16.68 ? 479  LEU   A CA   1 
ATOM   7340  C  C    . LEU   A 1 479 ? 8.456  42.023  17.273 1.00 14.23 ? 479  LEU   A C    1 
ATOM   7341  O  O    . LEU   A 1 479 ? 9.168  42.589  18.109 1.00 15.07 ? 479  LEU   A O    1 
ATOM   7342  C  CB   . LEU   A 1 479 ? 6.153  42.901  16.719 1.00 15.27 ? 479  LEU   A CB   1 
ATOM   7343  C  CG   . LEU   A 1 479 ? 5.887  43.085  18.211 1.00 21.72 ? 479  LEU   A CG   1 
ATOM   7344  C  CD1  . LEU   A 1 479 ? 6.286  44.482  18.662 1.00 23.97 ? 479  LEU   A CD1  1 
ATOM   7345  C  CD2  . LEU   A 1 479 ? 4.429  42.811  18.542 1.00 30.25 ? 479  LEU   A CD2  1 
ATOM   7346  H  H    . LEU   A 1 479 ? 7.001  42.110  14.573 1.00 14.50 ? 479  LEU   A H    1 
ATOM   7347  H  HA   . LEU   A 1 479 ? 7.974  43.791  16.347 1.00 20.01 ? 479  LEU   A HA   1 
ATOM   7348  H  HB2  . LEU   A 1 479 ? 5.708  43.615  16.236 1.00 18.32 ? 479  LEU   A HB2  1 
ATOM   7349  H  HB3  . LEU   A 1 479 ? 5.745  42.068  16.434 1.00 18.32 ? 479  LEU   A HB3  1 
ATOM   7350  H  HG   . LEU   A 1 479 ? 6.431  42.442  18.693 1.00 26.07 ? 479  LEU   A HG   1 
ATOM   7351  H  HD11 . LEU   A 1 479 ? 6.110  44.579  19.611 1.00 28.77 ? 479  LEU   A HD11 1 
ATOM   7352  H  HD12 . LEU   A 1 479 ? 7.231  44.619  18.494 1.00 28.77 ? 479  LEU   A HD12 1 
ATOM   7353  H  HD13 . LEU   A 1 479 ? 5.772  45.141  18.169 1.00 28.77 ? 479  LEU   A HD13 1 
ATOM   7354  H  HD21 . LEU   A 1 479 ? 4.284  42.934  19.493 1.00 36.31 ? 479  LEU   A HD21 1 
ATOM   7355  H  HD22 . LEU   A 1 479 ? 3.864  43.425  18.047 1.00 36.31 ? 479  LEU   A HD22 1 
ATOM   7356  H  HD23 . LEU   A 1 479 ? 4.207  41.899  18.297 1.00 36.31 ? 479  LEU   A HD23 1 
ATOM   7357  N  N    . PHE   A 1 480 ? 8.334  40.697  17.156 1.00 13.71 ? 480  PHE   A N    1 
ATOM   7358  C  CA   . PHE   A 1 480 ? 9.081  39.782  18.058 1.00 14.94 ? 480  PHE   A CA   1 
ATOM   7359  C  C    . PHE   A 1 480 ? 10.583 39.937  17.799 1.00 11.83 ? 480  PHE   A C    1 
ATOM   7360  O  O    . PHE   A 1 480 ? 11.368 39.843  18.750 1.00 12.25 ? 480  PHE   A O    1 
ATOM   7361  C  CB   . PHE   A 1 480 ? 8.620  38.331  17.884 1.00 16.67 ? 480  PHE   A CB   1 
ATOM   7362  C  CG   . PHE   A 1 480 ? 8.090  37.721  19.154 1.00 17.98 ? 480  PHE   A CG   1 
ATOM   7363  C  CD1  . PHE   A 1 480 ? 8.945  37.104  20.052 1.00 22.75 ? 480  PHE   A CD1  1 
ATOM   7364  C  CD2  . PHE   A 1 480 ? 6.744  37.794  19.466 1.00 21.39 ? 480  PHE   A CD2  1 
ATOM   7365  C  CE1  . PHE   A 1 480 ? 8.459  36.553  21.227 1.00 27.74 ? 480  PHE   A CE1  1 
ATOM   7366  C  CE2  . PHE   A 1 480 ? 6.260  37.243  20.641 1.00 22.62 ? 480  PHE   A CE2  1 
ATOM   7367  C  CZ   . PHE   A 1 480 ? 7.118  36.626  21.518 1.00 25.68 ? 480  PHE   A CZ   1 
ATOM   7368  H  H    . PHE   A 1 480 ? 7.836  40.304  16.575 1.00 16.46 ? 480  PHE   A H    1 
ATOM   7369  H  HA   . PHE   A 1 480 ? 8.898  40.021  18.980 1.00 17.93 ? 480  PHE   A HA   1 
ATOM   7370  H  HB2  . PHE   A 1 480 ? 7.930  38.296  17.203 1.00 20.01 ? 480  PHE   A HB2  1 
ATOM   7371  H  HB3  . PHE   A 1 480 ? 9.364  37.798  17.562 1.00 20.01 ? 480  PHE   A HB3  1 
ATOM   7372  H  HD1  . PHE   A 1 480 ? 9.855  37.059  19.865 1.00 27.31 ? 480  PHE   A HD1  1 
ATOM   7373  H  HD2  . PHE   A 1 480 ? 6.158  38.217  18.881 1.00 25.67 ? 480  PHE   A HD2  1 
ATOM   7374  H  HE1  . PHE   A 1 480 ? 9.041  36.134  21.819 1.00 33.29 ? 480  PHE   A HE1  1 
ATOM   7375  H  HE2  . PHE   A 1 480 ? 5.352  37.291  20.836 1.00 27.15 ? 480  PHE   A HE2  1 
ATOM   7376  H  HZ   . PHE   A 1 480 ? 6.792  36.258  22.308 1.00 30.82 ? 480  PHE   A HZ   1 
ATOM   7377  N  N    . HIS   A 1 481 ? 10.949 40.153  16.537 1.00 11.47 ? 481  HIS   A N    1 
ATOM   7378  C  CA   . HIS   A 1 481 ? 12.382 40.313  16.185 1.00 12.23 ? 481  HIS   A CA   1 
ATOM   7379  C  C    . HIS   A 1 481 ? 12.912 41.580  16.861 1.00 10.54 ? 481  HIS   A C    1 
ATOM   7380  O  O    . HIS   A 1 481 ? 14.019 41.547  17.425 1.00 12.12 ? 481  HIS   A O    1 
ATOM   7381  C  CB   . HIS   A 1 481 ? 12.545 40.329  14.661 1.00 13.06 ? 481  HIS   A CB   1 
ATOM   7382  C  CG   . HIS   A 1 481 ? 12.198 39.028  14.022 1.00 12.38 ? 481  HIS   A CG   1 
ATOM   7383  N  ND1  . HIS   A 1 481 ? 11.936 38.894  12.677 1.00 13.44 ? 481  HIS   A ND1  1 
ATOM   7384  C  CD2  . HIS   A 1 481 ? 12.071 37.805  14.547 1.00 10.27 ? 481  HIS   A CD2  1 
ATOM   7385  C  CE1  . HIS   A 1 481 ? 11.663 37.628  12.409 1.00 10.68 ? 481  HIS   A CE1  1 
ATOM   7386  N  NE2  . HIS   A 1 481 ? 11.737 36.949  13.531 1.00 11.35 ? 481  HIS   A NE2  1 
ATOM   7387  H  H    . HIS   A 1 481 ? 10.404 40.211  15.874 1.00 13.77 ? 481  HIS   A H    1 
ATOM   7388  H  HA   . HIS   A 1 481 ? 12.908 39.565  16.508 1.00 14.68 ? 481  HIS   A HA   1 
ATOM   7389  H  HB2  . HIS   A 1 481 ? 11.983 41.026  14.288 1.00 15.67 ? 481  HIS   A HB2  1 
ATOM   7390  H  HB3  . HIS   A 1 481 ? 13.462 40.556  14.442 1.00 15.67 ? 481  HIS   A HB3  1 
ATOM   7391  H  HD2  . HIS   A 1 481 ? 12.188 37.577  15.441 1.00 12.33 ? 481  HIS   A HD2  1 
ATOM   7392  H  HE1  . HIS   A 1 481 ? 11.455 37.279  11.572 1.00 12.81 ? 481  HIS   A HE1  1 
ATOM   7393  H  HE2  . HIS   A 1 481 ? 11.598 36.104  13.614 1.00 13.62 ? 481  HIS   A HE2  1 
ATOM   7394  N  N    . ASP   A 1 482 ? 12.129 42.663  16.814 1.00 13.00 ? 482  ASP   A N    1 
ATOM   7395  C  CA   . ASP   A 1 482 ? 12.590 43.921  17.385 1.00 14.53 ? 482  ASP   A CA   1 
ATOM   7396  C  C    . ASP   A 1 482 ? 12.550 43.880  18.912 1.00 14.09 ? 482  ASP   A C    1 
ATOM   7397  O  O    . ASP   A 1 482 ? 13.487 44.337  19.569 1.00 14.57 ? 482  ASP   A O    1 
ATOM   7398  C  CB   . ASP   A 1 482 ? 11.761 45.085  16.840 1.00 14.58 ? 482  ASP   A CB   1 
ATOM   7399  C  CG   . ASP   A 1 482 ? 11.816 45.189  15.318 1.00 14.84 ? 482  ASP   A CG   1 
ATOM   7400  O  OD1  . ASP   A 1 482 ? 12.704 44.560  14.698 1.00 13.59 ? 482  ASP   A OD1  1 
ATOM   7401  O  OD2  . ASP   A 1 482 ? 10.968 45.914  14.750 1.00 16.07 ? 482  ASP   A OD2  1 
ATOM   7402  H  H    . ASP   A 1 482 ? 11.344 42.686  16.463 1.00 15.60 ? 482  ASP   A H    1 
ATOM   7403  H  HA   . ASP   A 1 482 ? 13.514 44.056  17.123 1.00 17.44 ? 482  ASP   A HA   1 
ATOM   7404  H  HB2  . ASP   A 1 482 ? 10.838 44.978  17.120 1.00 17.49 ? 482  ASP   A HB2  1 
ATOM   7405  H  HB3  . ASP   A 1 482 ? 12.081 45.914  17.228 1.00 17.49 ? 482  ASP   A HB3  1 
ATOM   7406  N  N    . LEU   A 1 483 ? 11.487 43.311  19.497 1.00 14.27 ? 483  LEU   A N    1 
ATOM   7407  C  CA   . LEU   A 1 483 ? 11.416 43.206  20.955 1.00 14.04 ? 483  LEU   A CA   1 
ATOM   7408  C  C    . LEU   A 1 483 ? 12.547 42.343  21.505 1.00 12.33 ? 483  LEU   A C    1 
ATOM   7409  O  O    . LEU   A 1 483 ? 13.146 42.667  22.539 1.00 12.00 ? 483  LEU   A O    1 
ATOM   7410  C  CB   . LEU   A 1 483 ? 10.061 42.642  21.385 1.00 13.65 ? 483  LEU   A CB   1 
ATOM   7411  C  CG   . LEU   A 1 483 ? 9.855  42.445  22.891 1.00 12.59 ? 483  LEU   A CG   1 
ATOM   7412  C  CD1  . LEU   A 1 483 ? 9.972  43.765  23.642 1.00 17.12 ? 483  LEU   A CD1  1 
ATOM   7413  C  CD2  . LEU   A 1 483 ? 8.516  41.774  23.177 1.00 13.88 ? 483  LEU   A CD2  1 
ATOM   7414  H  H    . LEU   A 1 483 ? 10.811 42.987  19.075 1.00 17.12 ? 483  LEU   A H    1 
ATOM   7415  H  HA   . LEU   A 1 483 ? 11.515 44.099  21.322 1.00 16.86 ? 483  LEU   A HA   1 
ATOM   7416  H  HB2  . LEU   A 1 483 ? 9.367  43.235  21.058 1.00 16.38 ? 483  LEU   A HB2  1 
ATOM   7417  H  HB3  . LEU   A 1 483 ? 9.934  41.787  20.946 1.00 16.38 ? 483  LEU   A HB3  1 
ATOM   7418  H  HG   . LEU   A 1 483 ? 10.559 41.859  23.210 1.00 15.12 ? 483  LEU   A HG   1 
ATOM   7419  H  HD11 . LEU   A 1 483 ? 9.838  43.611  24.590 1.00 20.54 ? 483  LEU   A HD11 1 
ATOM   7420  H  HD12 . LEU   A 1 483 ? 10.854 44.142  23.498 1.00 20.54 ? 483  LEU   A HD12 1 
ATOM   7421  H  HD13 . LEU   A 1 483 ? 9.299  44.383  23.317 1.00 20.54 ? 483  LEU   A HD13 1 
ATOM   7422  H  HD21 . LEU   A 1 483 ? 8.409  41.660  24.134 1.00 16.66 ? 483  LEU   A HD21 1 
ATOM   7423  H  HD22 . LEU   A 1 483 ? 7.797  42.328  22.835 1.00 16.66 ? 483  LEU   A HD22 1 
ATOM   7424  H  HD23 . LEU   A 1 483 ? 8.490  40.906  22.744 1.00 16.66 ? 483  LEU   A HD23 1 
ATOM   7425  N  N    . THR   A 1 484 ? 12.854 41.254  20.805 1.00 11.40 ? 484  THR   A N    1 
ATOM   7426  C  CA   . THR   A 1 484 ? 13.935 40.349  21.274 1.00 14.37 ? 484  THR   A CA   1 
ATOM   7427  C  C    . THR   A 1 484 ? 15.272 41.100  21.202 1.00 10.62 ? 484  THR   A C    1 
ATOM   7428  O  O    . THR   A 1 484 ? 16.117 40.896  22.083 1.00 10.49 ? 484  THR   A O    1 
ATOM   7429  C  CB   . THR   A 1 484 ? 13.926 39.032  20.488 1.00 10.46 ? 484  THR   A CB   1 
ATOM   7430  O  OG1  . THR   A 1 484 ? 12.661 38.410  20.706 1.00 9.92  ? 484  THR   A OG1  1 
ATOM   7431  C  CG2  . THR   A 1 484 ? 15.042 38.098  20.902 1.00 10.51 ? 484  THR   A CG2  1 
ATOM   7432  H  H    . THR   A 1 484 ? 12.468 41.015  20.075 1.00 13.69 ? 484  THR   A H    1 
ATOM   7433  H  HA   . THR   A 1 484 ? 13.790 40.096  22.199 1.00 17.25 ? 484  THR   A HA   1 
ATOM   7434  H  HB   . THR   A 1 484 ? 14.069 39.227  19.549 1.00 12.56 ? 484  THR   A HB   1 
ATOM   7435  H  HG1  . THR   A 1 484 ? 12.095 38.731  20.174 1.00 11.90 ? 484  THR   A HG1  1 
ATOM   7436  H  HG21 . THR   A 1 484 ? 14.993 37.283  20.378 1.00 12.62 ? 484  THR   A HG21 1 
ATOM   7437  H  HG22 . THR   A 1 484 ? 15.898 38.529  20.750 1.00 12.62 ? 484  THR   A HG22 1 
ATOM   7438  H  HG23 . THR   A 1 484 ? 14.951 37.883  21.843 1.00 12.62 ? 484  THR   A HG23 1 
ATOM   7439  N  N    . ALA   A 1 485 ? 15.428 41.956  20.193 1.00 9.52  ? 485  ALA   A N    1 
ATOM   7440  C  CA   . ALA   A 1 485 ? 16.683 42.740  20.074 1.00 12.52 ? 485  ALA   A CA   1 
ATOM   7441  C  C    . ALA   A 1 485 ? 16.792 43.712  21.257 1.00 12.83 ? 485  ALA   A C    1 
ATOM   7442  O  O    . ALA   A 1 485 ? 17.912 43.944  21.728 1.00 12.88 ? 485  ALA   A O    1 
ATOM   7443  C  CB   . ALA   A 1 485 ? 16.737 43.445  18.741 1.00 14.84 ? 485  ALA   A CB   1 
ATOM   7444  H  H    . ALA   A 1 485 ? 14.845 42.103  19.578 1.00 11.43 ? 485  ALA   A H    1 
ATOM   7445  H  HA   . ALA   A 1 485 ? 17.449 42.146  20.108 1.00 15.03 ? 485  ALA   A HA   1 
ATOM   7446  H  HB1  . ALA   A 1 485 ? 17.561 43.953  18.676 1.00 17.82 ? 485  ALA   A HB1  1 
ATOM   7447  H  HB2  . ALA   A 1 485 ? 16.705 42.790  18.027 1.00 17.82 ? 485  ALA   A HB2  1 
ATOM   7448  H  HB3  . ALA   A 1 485 ? 15.980 44.046  18.662 1.00 17.82 ? 485  ALA   A HB3  1 
ATOM   7449  N  N    . VAL   A 1 486 ? 15.660 44.246  21.716 1.00 12.92 ? 486  VAL   A N    1 
ATOM   7450  C  CA   . VAL   A 1 486 ? 15.678 45.124  22.923 1.00 14.06 ? 486  VAL   A CA   1 
ATOM   7451  C  C    . VAL   A 1 486 ? 16.114 44.293  24.137 1.00 12.84 ? 486  VAL   A C    1 
ATOM   7452  O  O    . VAL   A 1 486 ? 17.073 44.694  24.806 1.00 13.84 ? 486  VAL   A O    1 
ATOM   7453  C  CB   . VAL   A 1 486 ? 14.296 45.763  23.168 1.00 12.89 ? 486  VAL   A CB   1 
ATOM   7454  C  CG1  . VAL   A 1 486 ? 14.216 46.454  24.520 1.00 14.50 ? 486  VAL   A CG1  1 
ATOM   7455  C  CG2  . VAL   A 1 486 ? 13.897 46.709  22.046 1.00 14.56 ? 486  VAL   A CG2  1 
ATOM   7456  H  H    . VAL   A 1 486 ? 14.884 44.126  21.364 1.00 15.51 ? 486  VAL   A H    1 
ATOM   7457  H  HA   . VAL   A 1 486 ? 16.309 45.847  22.780 1.00 16.88 ? 486  VAL   A HA   1 
ATOM   7458  H  HB   . VAL   A 1 486 ? 13.656 45.034  23.176 1.00 15.47 ? 486  VAL   A HB   1 
ATOM   7459  H  HG11 . VAL   A 1 486 ? 13.334 46.841  24.634 1.00 17.40 ? 486  VAL   A HG11 1 
ATOM   7460  H  HG12 . VAL   A 1 486 ? 14.378 45.807  25.224 1.00 17.40 ? 486  VAL   A HG12 1 
ATOM   7461  H  HG13 . VAL   A 1 486 ? 14.885 47.155  24.565 1.00 17.40 ? 486  VAL   A HG13 1 
ATOM   7462  H  HG21 . VAL   A 1 486 ? 13.025 47.089  22.237 1.00 17.47 ? 486  VAL   A HG21 1 
ATOM   7463  H  HG22 . VAL   A 1 486 ? 14.551 47.422  21.975 1.00 17.47 ? 486  VAL   A HG22 1 
ATOM   7464  H  HG23 . VAL   A 1 486 ? 13.860 46.221  21.209 1.00 17.47 ? 486  VAL   A HG23 1 
ATOM   7465  N  N    . ILE   A 1 487 ? 15.427 43.177  24.397 1.00 11.98 ? 487  ILE   A N    1 
ATOM   7466  C  CA   . ILE   A 1 487 ? 15.706 42.366  25.622 1.00 11.30 ? 487  ILE   A CA   1 
ATOM   7467  C  C    . ILE   A 1 487 ? 17.154 41.865  25.607 1.00 10.30 ? 487  ILE   A C    1 
ATOM   7468  O  O    . ILE   A 1 487 ? 17.815 41.954  26.648 1.00 11.86 ? 487  ILE   A O    1 
ATOM   7469  C  CB   . ILE   A 1 487 ? 14.691 41.212  25.735 1.00 11.43 ? 487  ILE   A CB   1 
ATOM   7470  C  CG1  . ILE   A 1 487 ? 13.256 41.742  25.757 1.00 12.60 ? 487  ILE   A CG1  1 
ATOM   7471  C  CG2  . ILE   A 1 487 ? 14.990 40.342  26.946 1.00 11.74 ? 487  ILE   A CG2  1 
ATOM   7472  C  CD1  . ILE   A 1 487 ? 12.200 40.675  25.616 1.00 13.78 ? 487  ILE   A CD1  1 
ATOM   7473  H  H    . ILE   A 1 487 ? 14.803 42.865  23.894 1.00 14.38 ? 487  ILE   A H    1 
ATOM   7474  H  HA   . ILE   A 1 487 ? 15.602 42.922  26.410 1.00 13.57 ? 487  ILE   A HA   1 
ATOM   7475  H  HB   . ILE   A 1 487 ? 14.779 40.653  24.947 1.00 13.72 ? 487  ILE   A HB   1 
ATOM   7476  H  HG12 . ILE   A 1 487 ? 13.111 42.218  26.589 1.00 15.12 ? 487  ILE   A HG12 1 
ATOM   7477  H  HG13 . ILE   A 1 487 ? 13.149 42.386  25.039 1.00 15.12 ? 487  ILE   A HG13 1 
ATOM   7478  H  HG21 . ILE   A 1 487 ? 14.340 39.624  26.997 1.00 14.10 ? 487  ILE   A HG21 1 
ATOM   7479  H  HG22 . ILE   A 1 487 ? 15.880 39.966  26.863 1.00 14.10 ? 487  ILE   A HG22 1 
ATOM   7480  H  HG23 . ILE   A 1 487 ? 14.940 40.880  27.751 1.00 14.10 ? 487  ILE   A HG23 1 
ATOM   7481  H  HD11 . ILE   A 1 487 ? 11.321 41.084  25.639 1.00 16.54 ? 487  ILE   A HD11 1 
ATOM   7482  H  HD12 . ILE   A 1 487 ? 12.319 40.211  24.772 1.00 16.54 ? 487  ILE   A HD12 1 
ATOM   7483  H  HD13 . ILE   A 1 487 ? 12.280 40.042  26.346 1.00 16.54 ? 487  ILE   A HD13 1 
ATOM   7484  N  N    . ASP   A 1 488 ? 17.619 41.363  24.463 1.00 12.20 ? 488  ASP   A N    1 
ATOM   7485  C  CA   . ASP   A 1 488 ? 19.038 40.939  24.358 1.00 9.06  ? 488  ASP   A CA   1 
ATOM   7486  C  C    . ASP   A 1 488 ? 19.941 42.128  24.686 1.00 13.51 ? 488  ASP   A C    1 
ATOM   7487  O  O    . ASP   A 1 488 ? 20.925 41.929  25.419 1.00 12.06 ? 488  ASP   A O    1 
ATOM   7488  C  CB   . ASP   A 1 488 ? 19.376 40.433  22.956 1.00 11.40 ? 488  ASP   A CB   1 
ATOM   7489  C  CG   . ASP   A 1 488 ? 19.033 38.974  22.718 1.00 9.90  ? 488  ASP   A CG   1 
ATOM   7490  O  OD1  . ASP   A 1 488 ? 18.777 38.265  23.706 1.00 13.00 ? 488  ASP   A OD1  1 
ATOM   7491  O  OD2  . ASP   A 1 488 ? 19.034 38.560  21.544 1.00 10.90 ? 488  ASP   A OD2  1 
ATOM   7492  H  H    . ASP   A 1 488 ? 17.152 41.257  23.748 1.00 14.65 ? 488  ASP   A H    1 
ATOM   7493  H  HA   . ASP   A 1 488 ? 19.181 40.213  24.985 1.00 10.87 ? 488  ASP   A HA   1 
ATOM   7494  H  HB2  . ASP   A 1 488 ? 18.904 40.976  22.305 1.00 13.69 ? 488  ASP   A HB2  1 
ATOM   7495  H  HB3  . ASP   A 1 488 ? 20.324 40.561  22.797 1.00 13.69 ? 488  ASP   A HB3  1 
ATOM   7496  N  N    . SER   A 1 489 ? 19.603 43.315  24.172 1.00 11.92 ? 489  SER   A N    1 
ATOM   7497  C  CA   . SER   A 1 489 ? 20.493 44.497  24.338 1.00 11.13 ? 489  SER   A CA   1 
ATOM   7498  C  C    . SER   A 1 489 ? 20.498 45.017  25.783 1.00 14.17 ? 489  SER   A C    1 
ATOM   7499  O  O    . SER   A 1 489 ? 21.492 45.659  26.161 1.00 13.27 ? 489  SER   A O    1 
ATOM   7500  C  CB   . SER   A 1 489 ? 20.142 45.573  23.341 1.00 10.34 ? 489  SER   A CB   1 
ATOM   7501  O  OG   . SER   A 1 489 ? 20.286 45.089  22.015 1.00 12.91 ? 489  SER   A OG   1 
ATOM   7502  H  H    . SER   A 1 489 ? 18.880 43.466  23.731 1.00 14.31 ? 489  SER   A H    1 
ATOM   7503  H  HA   . SER   A 1 489 ? 21.402 44.213  24.153 1.00 13.35 ? 489  SER   A HA   1 
ATOM   7504  H  HB2  . SER   A 1 489 ? 19.230 45.870  23.485 1.00 12.41 ? 489  SER   A HB2  1 
ATOM   7505  H  HB3  . SER   A 1 489 ? 20.716 46.344  23.474 1.00 12.41 ? 489  SER   A HB3  1 
ATOM   7506  H  HG   . SER   A 1 489 ? 19.574 44.713  21.775 1.00 15.49 ? 489  SER   A HG   1 
ATOM   7507  N  N    . LEU   A 1 490 ? 19.445 44.747  26.556 1.00 12.14 ? 490  LEU   A N    1 
ATOM   7508  C  CA   . LEU   A 1 490 ? 19.348 45.283  27.941 1.00 12.98 ? 490  LEU   A CA   1 
ATOM   7509  C  C    . LEU   A 1 490 ? 20.187 44.446  28.914 1.00 13.14 ? 490  LEU   A C    1 
ATOM   7510  O  O    . LEU   A 1 490 ? 20.556 44.982  29.973 1.00 13.15 ? 490  LEU   A O    1 
ATOM   7511  C  CB   . LEU   A 1 490 ? 17.879 45.253  28.374 1.00 13.27 ? 490  LEU   A CB   1 
ATOM   7512  C  CG   . LEU   A 1 490 ? 16.972 46.302  27.738 1.00 14.67 ? 490  LEU   A CG   1 
ATOM   7513  C  CD1  . LEU   A 1 490 ? 15.515 46.015  28.066 1.00 15.12 ? 490  LEU   A CD1  1 
ATOM   7514  C  CD2  . LEU   A 1 490 ? 17.356 47.697  28.205 1.00 16.83 ? 490  LEU   A CD2  1 
ATOM   7515  H  H    . LEU   A 1 490 ? 18.778 44.263  26.312 1.00 14.57 ? 490  LEU   A H    1 
ATOM   7516  H  HA   . LEU   A 1 490 ? 19.688 46.191  27.954 1.00 15.57 ? 490  LEU   A HA   1 
ATOM   7517  H  HB2  . LEU   A 1 490 ? 17.519 44.375  28.173 1.00 15.92 ? 490  LEU   A HB2  1 
ATOM   7518  H  HB3  . LEU   A 1 490 ? 17.842 45.361  29.337 1.00 15.92 ? 490  LEU   A HB3  1 
ATOM   7519  H  HG   . LEU   A 1 490 ? 17.086 46.260  26.776 1.00 17.61 ? 490  LEU   A HG   1 
ATOM   7520  H  HD11 . LEU   A 1 490 ? 14.952 46.689  27.655 1.00 18.14 ? 490  LEU   A HD11 1 
ATOM   7521  H  HD12 . LEU   A 1 490 ? 15.272 45.140  27.724 1.00 18.14 ? 490  LEU   A HD12 1 
ATOM   7522  H  HD13 . LEU   A 1 490 ? 15.390 46.032  29.028 1.00 18.14 ? 490  LEU   A HD13 1 
ATOM   7523  H  HD21 . LEU   A 1 490 ? 16.770 48.350  27.791 1.00 20.20 ? 490  LEU   A HD21 1 
ATOM   7524  H  HD22 . LEU   A 1 490 ? 17.269 47.751  29.170 1.00 20.20 ? 490  LEU   A HD22 1 
ATOM   7525  H  HD23 . LEU   A 1 490 ? 18.274 47.882  27.952 1.00 20.20 ? 490  LEU   A HD23 1 
ATOM   7526  N  N    . GLY   A 1 491 ? 20.466 43.185  28.579 1.00 13.32 ? 491  GLY   A N    1 
ATOM   7527  C  CA   . GLY   A 1 491 ? 21.161 42.290  29.527 1.00 13.40 ? 491  GLY   A CA   1 
ATOM   7528  C  C    . GLY   A 1 491 ? 20.184 41.485  30.367 1.00 12.71 ? 491  GLY   A C    1 
ATOM   7529  O  O    . GLY   A 1 491 ? 20.577 41.019  31.443 1.00 13.43 ? 491  GLY   A O    1 
ATOM   7530  H  H    . GLY   A 1 491 ? 20.268 42.827  27.822 1.00 15.98 ? 491  GLY   A H    1 
ATOM   7531  H  HA2  . GLY   A 1 491 ? 21.739 41.685  29.036 1.00 16.08 ? 491  GLY   A HA2  1 
ATOM   7532  H  HA3  . GLY   A 1 491 ? 21.731 42.816  30.110 1.00 16.08 ? 491  GLY   A HA3  1 
ATOM   7533  N  N    . LEU   A 1 492 ? 18.950 41.328  29.882 1.00 13.42 ? 492  LEU   A N    1 
ATOM   7534  C  CA   . LEU   A 1 492 ? 17.924 40.542  30.614 1.00 11.55 ? 492  LEU   A CA   1 
ATOM   7535  C  C    . LEU   A 1 492 ? 17.618 39.237  29.874 1.00 12.88 ? 492  LEU   A C    1 
ATOM   7536  O  O    . LEU   A 1 492 ? 18.101 39.063  28.745 1.00 12.45 ? 492  LEU   A O    1 
ATOM   7537  C  CB   . LEU   A 1 492 ? 16.649 41.378  30.768 1.00 11.00 ? 492  LEU   A CB   1 
ATOM   7538  C  CG   . LEU   A 1 492 ? 16.781 42.641  31.616 1.00 14.62 ? 492  LEU   A CG   1 
ATOM   7539  C  CD1  . LEU   A 1 492 ? 15.410 43.217  31.926 1.00 14.16 ? 492  LEU   A CD1  1 
ATOM   7540  C  CD2  . LEU   A 1 492 ? 17.540 42.355  32.902 1.00 16.40 ? 492  LEU   A CD2  1 
ATOM   7541  H  H    . LEU   A 1 492 ? 18.679 41.662  29.137 1.00 16.10 ? 492  LEU   A H    1 
ATOM   7542  H  HA   . LEU   A 1 492 ? 18.267 40.319  31.494 1.00 13.86 ? 492  LEU   A HA   1 
ATOM   7543  H  HB2  . LEU   A 1 492 ? 16.341 41.633  29.884 1.00 13.20 ? 492  LEU   A HB2  1 
ATOM   7544  H  HB3  . LEU   A 1 492 ? 15.960 40.817  31.158 1.00 13.20 ? 492  LEU   A HB3  1 
ATOM   7545  H  HG   . LEU   A 1 492 ? 17.285 43.295  31.107 1.00 17.54 ? 492  LEU   A HG   1 
ATOM   7546  H  HD11 . LEU   A 1 492 ? 15.509 44.018  32.464 1.00 16.99 ? 492  LEU   A HD11 1 
ATOM   7547  H  HD12 . LEU   A 1 492 ? 14.957 43.439  31.097 1.00 16.99 ? 492  LEU   A HD12 1 
ATOM   7548  H  HD13 . LEU   A 1 492 ? 14.887 42.562  32.414 1.00 16.99 ? 492  LEU   A HD13 1 
ATOM   7549  H  HD21 . LEU   A 1 492 ? 17.612 43.170  33.424 1.00 19.68 ? 492  LEU   A HD21 1 
ATOM   7550  H  HD22 . LEU   A 1 492 ? 17.065 41.683  33.416 1.00 19.68 ? 492  LEU   A HD22 1 
ATOM   7551  H  HD23 . LEU   A 1 492 ? 18.428 42.029  32.688 1.00 19.68 ? 492  LEU   A HD23 1 
ATOM   7552  N  N    . CYS   A 1 493 ? 16.820 38.373  30.506 1.00 12.39 ? 493  CYS   A N    1 
ATOM   7553  C  CA   . CYS   A 1 493 ? 16.505 37.050  29.913 1.00 12.25 ? 493  CYS   A CA   1 
ATOM   7554  C  C    . CYS   A 1 493 ? 15.211 37.112  29.094 1.00 10.55 ? 493  CYS   A C    1 
ATOM   7555  O  O    . CYS   A 1 493 ? 14.242 37.723  29.563 1.00 12.35 ? 493  CYS   A O    1 
ATOM   7556  C  CB   . CYS   A 1 493 ? 16.362 36.007  31.011 1.00 14.79 ? 493  CYS   A CB   1 
ATOM   7557  S  SG   . CYS   A 1 493 ? 16.024 34.340  30.386 1.00 12.58 ? 493  CYS   A SG   1 
ATOM   7558  H  H    . CYS   A 1 493 ? 16.451 38.522  31.269 1.00 14.87 ? 493  CYS   A H    1 
ATOM   7559  H  HA   . CYS   A 1 493 ? 17.234 36.802  29.323 1.00 14.71 ? 493  CYS   A HA   1 
ATOM   7560  H  HB2  . CYS   A 1 493 ? 17.177 35.988  31.537 1.00 17.75 ? 493  CYS   A HB2  1 
ATOM   7561  H  HB3  . CYS   A 1 493 ? 15.645 36.272  31.608 1.00 17.75 ? 493  CYS   A HB3  1 
ATOM   7562  N  N    . ILE   A 1 494 ? 15.202 36.468  27.928 1.00 11.38 ? 494  ILE   A N    1 
ATOM   7563  C  CA   . ILE   A 1 494 ? 14.004 36.462  27.040 1.00 10.65 ? 494  ILE   A CA   1 
ATOM   7564  C  C    . ILE   A 1 494 ? 12.811 35.829  27.768 1.00 12.15 ? 494  ILE   A C    1 
ATOM   7565  O  O    . ILE   A 1 494 ? 11.674 36.143  27.403 1.00 14.38 ? 494  ILE   A O    1 
ATOM   7566  C  CB   . ILE   A 1 494 ? 14.333 35.722  25.728 1.00 10.61 ? 494  ILE   A CB   1 
ATOM   7567  C  CG1  . ILE   A 1 494 ? 13.270 35.967  24.656 1.00 9.65  ? 494  ILE   A CG1  1 
ATOM   7568  C  CG2  . ILE   A 1 494 ? 14.553 34.239  25.985 1.00 10.94 ? 494  ILE   A CG2  1 
ATOM   7569  C  CD1  . ILE   A 1 494 ? 13.111 37.419  24.281 1.00 14.65 ? 494  ILE   A CD1  1 
ATOM   7570  H  H    . ILE   A 1 494 ? 15.872 36.025  27.621 1.00 13.66 ? 494  ILE   A H    1 
ATOM   7571  H  HA   . ILE   A 1 494 ? 13.759 37.373  26.815 1.00 12.79 ? 494  ILE   A HA   1 
ATOM   7572  H  HB   . ILE   A 1 494 ? 15.163 36.086  25.381 1.00 12.74 ? 494  ILE   A HB   1 
ATOM   7573  H  HG12 . ILE   A 1 494 ? 13.500 35.459  23.862 1.00 11.59 ? 494  ILE   A HG12 1 
ATOM   7574  H  HG13 . ILE   A 1 494 ? 12.418 35.628  24.973 1.00 11.59 ? 494  ILE   A HG13 1 
ATOM   7575  H  HG21 . ILE   A 1 494 ? 14.758 33.792  25.149 1.00 13.13 ? 494  ILE   A HG21 1 
ATOM   7576  H  HG22 . ILE   A 1 494 ? 15.292 34.124  26.603 1.00 13.13 ? 494  ILE   A HG22 1 
ATOM   7577  H  HG23 . ILE   A 1 494 ? 13.749 33.854  26.368 1.00 13.13 ? 494  ILE   A HG23 1 
ATOM   7578  H  HD11 . ILE   A 1 494 ? 12.425 37.504  23.600 1.00 17.58 ? 494  ILE   A HD11 1 
ATOM   7579  H  HD12 . ILE   A 1 494 ? 12.854 37.929  25.065 1.00 17.58 ? 494  ILE   A HD12 1 
ATOM   7580  H  HD13 . ILE   A 1 494 ? 13.952 37.758  23.936 1.00 17.58 ? 494  ILE   A HD13 1 
ATOM   7581  N  N    . PHE   A 1 495 ? 13.063 34.986  28.769 1.00 12.15 ? 495  PHE   A N    1 
ATOM   7582  C  CA   . PHE   A 1 495 ? 11.953 34.266  29.452 1.00 12.57 ? 495  PHE   A CA   1 
ATOM   7583  C  C    . PHE   A 1 495 ? 11.147 35.233  30.329 1.00 15.49 ? 495  PHE   A C    1 
ATOM   7584  O  O    . PHE   A 1 495 ? 10.130 34.808  30.894 1.00 13.30 ? 495  PHE   A O    1 
ATOM   7585  C  CB   . PHE   A 1 495 ? 12.472 33.047  30.222 1.00 14.06 ? 495  PHE   A CB   1 
ATOM   7586  C  CG   . PHE   A 1 495 ? 12.997 31.944  29.339 1.00 11.04 ? 495  PHE   A CG   1 
ATOM   7587  C  CD1  . PHE   A 1 495 ? 12.457 31.728  28.082 1.00 14.02 ? 495  PHE   A CD1  1 
ATOM   7588  C  CD2  . PHE   A 1 495 ? 14.034 31.129  29.758 1.00 14.00 ? 495  PHE   A CD2  1 
ATOM   7589  C  CE1  . PHE   A 1 495 ? 12.940 30.717  27.267 1.00 14.62 ? 495  PHE   A CE1  1 
ATOM   7590  C  CE2  . PHE   A 1 495 ? 14.518 30.121  28.942 1.00 15.17 ? 495  PHE   A CE2  1 
ATOM   7591  C  CZ   . PHE   A 1 495 ? 13.967 29.915  27.701 1.00 14.25 ? 495  PHE   A CZ   1 
ATOM   7592  H  H    . PHE   A 1 495 ? 13.849 34.811  29.072 1.00 14.59 ? 495  PHE   A H    1 
ATOM   7593  H  HA   . PHE   A 1 495 ? 11.344 33.919  28.781 1.00 15.09 ? 495  PHE   A HA   1 
ATOM   7594  H  HB2  . PHE   A 1 495 ? 13.178 33.332  30.823 1.00 16.88 ? 495  PHE   A HB2  1 
ATOM   7595  H  HB3  . PHE   A 1 495 ? 11.756 32.695  30.773 1.00 16.88 ? 495  PHE   A HB3  1 
ATOM   7596  H  HD1  . PHE   A 1 495 ? 11.762 32.268  27.781 1.00 16.83 ? 495  PHE   A HD1  1 
ATOM   7597  H  HD2  . PHE   A 1 495 ? 14.410 31.260  30.598 1.00 16.80 ? 495  PHE   A HD2  1 
ATOM   7598  H  HE1  . PHE   A 1 495 ? 12.568 30.581  26.425 1.00 17.54 ? 495  PHE   A HE1  1 
ATOM   7599  H  HE2  . PHE   A 1 495 ? 15.217 29.582  29.235 1.00 18.21 ? 495  PHE   A HE2  1 
ATOM   7600  H  HZ   . PHE   A 1 495 ? 14.289 29.234  27.156 1.00 17.11 ? 495  PHE   A HZ   1 
ATOM   7601  N  N    . THR   A 1 496 ? 11.581 36.490  30.426 1.00 13.62 ? 496  THR   A N    1 
ATOM   7602  C  CA   . THR   A 1 496 ? 10.768 37.501  31.154 1.00 14.43 ? 496  THR   A CA   1 
ATOM   7603  C  C    . THR   A 1 496 ? 9.496  37.800  30.350 1.00 12.96 ? 496  THR   A C    1 
ATOM   7604  O  O    . THR   A 1 496 ? 8.581  38.398  30.924 1.00 15.86 ? 496  THR   A O    1 
ATOM   7605  C  CB   . THR   A 1 496 ? 11.559 38.788  31.432 1.00 11.35 ? 496  THR   A CB   1 
ATOM   7606  O  OG1  . THR   A 1 496 ? 12.210 39.216  30.237 1.00 14.24 ? 496  THR   A OG1  1 
ATOM   7607  C  CG2  . THR   A 1 496 ? 12.575 38.611  32.539 1.00 15.31 ? 496  THR   A CG2  1 
ATOM   7608  H  H    . THR   A 1 496 ? 12.318 36.783  30.093 1.00 16.35 ? 496  THR   A H    1 
ATOM   7609  H  HA   . THR   A 1 496 ? 10.527 37.134  32.019 1.00 17.31 ? 496  THR   A HA   1 
ATOM   7610  H  HB   . THR   A 1 496 ? 10.928 39.463  31.728 1.00 13.62 ? 496  THR   A HB   1 
ATOM   7611  H  HG1  . THR   A 1 496 ? 12.954 38.832  30.170 1.00 17.10 ? 496  THR   A HG1  1 
ATOM   7612  H  HG21 . THR   A 1 496 ? 13.049 39.445  32.680 1.00 18.37 ? 496  THR   A HG21 1 
ATOM   7613  H  HG22 . THR   A 1 496 ? 12.121 38.355  33.357 1.00 18.37 ? 496  THR   A HG22 1 
ATOM   7614  H  HG23 . THR   A 1 496 ? 13.207 37.918  32.291 1.00 18.37 ? 496  THR   A HG23 1 
ATOM   7615  N  N    . THR   A 1 497 ? 9.461  37.401  29.075 1.00 15.38 ? 497  THR   A N    1 
ATOM   7616  C  CA   . THR   A 1 497 ? 8.256  37.615  28.227 1.00 14.83 ? 497  THR   A CA   1 
ATOM   7617  C  C    . THR   A 1 497 ? 7.087  36.783  28.769 1.00 17.30 ? 497  THR   A C    1 
ATOM   7618  O  O    . THR   A 1 497 ? 5.971  36.955  28.269 1.00 14.12 ? 497  THR   A O    1 
ATOM   7619  C  CB   . THR   A 1 497 ? 8.540  37.288  26.756 1.00 16.28 ? 497  THR   A CB   1 
ATOM   7620  O  OG1  . THR   A 1 497 ? 9.143  35.997  26.682 1.00 17.15 ? 497  THR   A OG1  1 
ATOM   7621  C  CG2  . THR   A 1 497 ? 9.438  38.312  26.097 1.00 16.72 ? 497  THR   A CG2  1 
ATOM   7622  H  H    . THR   A 1 497 ? 10.113 37.007  28.676 1.00 18.45 ? 497  THR   A H    1 
ATOM   7623  H  HA   . THR   A 1 497 ? 8.014  38.553  28.265 1.00 17.80 ? 497  THR   A HA   1 
ATOM   7624  H  HB   . THR   A 1 497 ? 7.697  37.303  26.277 1.00 19.54 ? 497  THR   A HB   1 
ATOM   7625  H  HG1  . THR   A 1 497 ? 9.971  36.067  26.805 1.00 20.59 ? 497  THR   A HG1  1 
ATOM   7626  H  HG21 . THR   A 1 497 ? 9.588  38.063  25.172 1.00 20.07 ? 497  THR   A HG21 1 
ATOM   7627  H  HG22 . THR   A 1 497 ? 9.015  39.184  26.132 1.00 20.07 ? 497  THR   A HG22 1 
ATOM   7628  H  HG23 . THR   A 1 497 ? 10.287 38.346  26.564 1.00 20.07 ? 497  THR   A HG23 1 
ATOM   7629  N  N    . PHE   A 1 498 ? 7.353  35.903  29.732 1.00 14.38 ? 498  PHE   A N    1 
ATOM   7630  C  CA   . PHE   A 1 498 ? 6.266  35.125  30.376 1.00 15.38 ? 498  PHE   A CA   1 
ATOM   7631  C  C    . PHE   A 1 498 ? 5.698  35.984  31.507 1.00 18.14 ? 498  PHE   A C    1 
ATOM   7632  O  O    . PHE   A 1 498 ? 5.791  35.589  32.680 1.00 18.03 ? 498  PHE   A O    1 
ATOM   7633  C  CB   . PHE   A 1 498 ? 6.778  33.762  30.842 1.00 15.65 ? 498  PHE   A CB   1 
ATOM   7634  C  CG   . PHE   A 1 498 ? 7.095  32.819  29.710 1.00 15.10 ? 498  PHE   A CG   1 
ATOM   7635  C  CD1  . PHE   A 1 498 ? 6.135  32.510  28.762 1.00 18.50 ? 498  PHE   A CD1  1 
ATOM   7636  C  CD2  . PHE   A 1 498 ? 8.353  32.256  29.584 1.00 17.90 ? 498  PHE   A CD2  1 
ATOM   7637  C  CE1  . PHE   A 1 498 ? 6.423  31.649  27.716 1.00 16.29 ? 498  PHE   A CE1  1 
ATOM   7638  C  CE2  . PHE   A 1 498 ? 8.640  31.394  28.538 1.00 19.57 ? 498  PHE   A CE2  1 
ATOM   7639  C  CZ   . PHE   A 1 498 ? 7.676  31.094  27.605 1.00 18.74 ? 498  PHE   A CZ   1 
ATOM   7640  H  H    . PHE   A 1 498 ? 8.142  35.735  30.031 1.00 17.25 ? 498  PHE   A H    1 
ATOM   7641  H  HA   . PHE   A 1 498 ? 5.552  34.926  29.750 1.00 18.46 ? 498  PHE   A HA   1 
ATOM   7642  H  HB2  . PHE   A 1 498 ? 7.575  33.891  31.379 1.00 18.79 ? 498  PHE   A HB2  1 
ATOM   7643  H  HB3  . PHE   A 1 498 ? 6.112  33.354  31.417 1.00 18.79 ? 498  PHE   A HB3  1 
ATOM   7644  H  HD1  . PHE   A 1 498 ? 5.287  32.885  28.828 1.00 22.21 ? 498  PHE   A HD1  1 
ATOM   7645  H  HD2  . PHE   A 1 498 ? 9.012  32.458  30.208 1.00 21.48 ? 498  PHE   A HD2  1 
ATOM   7646  H  HE1  . PHE   A 1 498 ? 5.768  31.446  27.088 1.00 19.55 ? 498  PHE   A HE1  1 
ATOM   7647  H  HE2  . PHE   A 1 498 ? 9.487  31.017  28.467 1.00 23.49 ? 498  PHE   A HE2  1 
ATOM   7648  H  HZ   . PHE   A 1 498 ? 7.871  30.518  26.901 1.00 22.49 ? 498  PHE   A HZ   1 
ATOM   7649  N  N    . GLY   A 1 499 ? 5.164  37.148  31.142 1.00 17.46 ? 499  GLY   A N    1 
ATOM   7650  C  CA   . GLY   A 1 499 ? 4.569  38.050  32.143 1.00 20.07 ? 499  GLY   A CA   1 
ATOM   7651  C  C    . GLY   A 1 499 ? 4.870  39.507  31.845 1.00 18.29 ? 499  GLY   A C    1 
ATOM   7652  O  O    . GLY   A 1 499 ? 4.039  40.355  32.201 1.00 19.77 ? 499  GLY   A O    1 
ATOM   7653  H  H    . GLY   A 1 499 ? 5.133  37.436  30.332 1.00 20.95 ? 499  GLY   A H    1 
ATOM   7654  H  HA2  . GLY   A 1 499 ? 3.608  37.917  32.166 1.00 24.09 ? 499  GLY   A HA2  1 
ATOM   7655  H  HA3  . GLY   A 1 499 ? 4.908  37.824  33.023 1.00 24.09 ? 499  GLY   A HA3  1 
ATOM   7656  N  N    . LEU   A 1 500 ? 6.006  39.788  31.201 1.00 18.34 ? 500  LEU   A N    1 
ATOM   7657  C  CA   . LEU   A 1 500 ? 6.419  41.198  30.982 1.00 18.17 ? 500  LEU   A CA   1 
ATOM   7658  C  C    . LEU   A 1 500 ? 6.338  41.606  29.511 1.00 18.48 ? 500  LEU   A C    1 
ATOM   7659  O  O    . LEU   A 1 500 ? 6.468  40.724  28.644 1.00 17.77 ? 500  LEU   A O    1 
ATOM   7660  C  CB   . LEU   A 1 500 ? 7.854  41.382  31.492 1.00 17.79 ? 500  LEU   A CB   1 
ATOM   7661  C  CG   . LEU   A 1 500 ? 8.091  41.067  32.968 1.00 18.40 ? 500  LEU   A CG   1 
ATOM   7662  C  CD1  . LEU   A 1 500 ? 9.477  41.522  33.396 1.00 19.17 ? 500  LEU   A CD1  1 
ATOM   7663  C  CD2  . LEU   A 1 500 ? 7.029  41.713  33.845 1.00 16.86 ? 500  LEU   A CD2  1 
ATOM   7664  H  H    . LEU   A 1 500 ? 6.547  39.198  30.886 1.00 22.02 ? 500  LEU   A H    1 
ATOM   7665  H  HA   . LEU   A 1 500 ? 5.806  41.768  31.471 1.00 21.81 ? 500  LEU   A HA   1 
ATOM   7666  H  HB2  . LEU   A 1 500 ? 8.440  40.819  30.962 1.00 21.35 ? 500  LEU   A HB2  1 
ATOM   7667  H  HB3  . LEU   A 1 500 ? 8.120  42.301  31.330 1.00 21.35 ? 500  LEU   A HB3  1 
ATOM   7668  H  HG   . LEU   A 1 500 ? 8.031  40.105  33.080 1.00 22.08 ? 500  LEU   A HG   1 
ATOM   7669  H  HD11 . LEU   A 1 500 ? 9.611  41.315  34.334 1.00 23.01 ? 500  LEU   A HD11 1 
ATOM   7670  H  HD12 . LEU   A 1 500 ? 10.147 41.063  32.865 1.00 23.01 ? 500  LEU   A HD12 1 
ATOM   7671  H  HD13 . LEU   A 1 500 ? 9.559  42.479  33.262 1.00 23.01 ? 500  LEU   A HD13 1 
ATOM   7672  H  HD21 . LEU   A 1 500 ? 7.202  41.498  34.775 1.00 20.23 ? 500  LEU   A HD21 1 
ATOM   7673  H  HD22 . LEU   A 1 500 ? 7.053  42.675  33.726 1.00 20.23 ? 500  LEU   A HD22 1 
ATOM   7674  H  HD23 . LEU   A 1 500 ? 6.154  41.378  33.594 1.00 20.23 ? 500  LEU   A HD23 1 
ATOM   7675  N  N    . GLY   A 1 501 ? 6.123  42.904  29.272 1.00 19.08 ? 501  GLY   A N    1 
ATOM   7676  C  CA   . GLY   A 1 501 ? 6.070  43.459  27.910 1.00 19.11 ? 501  GLY   A CA   1 
ATOM   7677  C  C    . GLY   A 1 501 ? 6.945  44.697  27.795 1.00 18.65 ? 501  GLY   A C    1 
ATOM   7678  O  O    . GLY   A 1 501 ? 7.654  44.995  28.766 1.00 15.45 ? 501  GLY   A O    1 
ATOM   7679  H  H    . GLY   A 1 501 ? 6.004  43.488  29.892 1.00 22.90 ? 501  GLY   A H    1 
ATOM   7680  H  HA2  . GLY   A 1 501 ? 6.364  42.790  27.272 1.00 22.93 ? 501  GLY   A HA2  1 
ATOM   7681  H  HA3  . GLY   A 1 501 ? 5.154  43.683  27.683 1.00 22.93 ? 501  GLY   A HA3  1 
ATOM   7682  N  N    . ILE   A 1 502 ? 6.866  45.417  26.675 1.00 18.48 ? 502  ILE   A N    1 
ATOM   7683  C  CA   . ILE   A 1 502 ? 7.796  46.560  26.420 1.00 19.27 ? 502  ILE   A CA   1 
ATOM   7684  C  C    . ILE   A 1 502 ? 7.774  47.583  27.563 1.00 18.55 ? 502  ILE   A C    1 
ATOM   7685  O  O    . ILE   A 1 502 ? 8.855  48.066  27.926 1.00 17.93 ? 502  ILE   A O    1 
ATOM   7686  C  CB   . ILE   A 1 502 ? 7.489  47.217  25.060 1.00 20.06 ? 502  ILE   A CB   1 
ATOM   7687  C  CG1  . ILE   A 1 502 ? 8.526  48.282  24.697 1.00 22.67 ? 502  ILE   A CG1  1 
ATOM   7688  C  CG2  . ILE   A 1 502 ? 6.073  47.773  25.033 1.00 23.29 ? 502  ILE   A CG2  1 
ATOM   7689  C  CD1  . ILE   A 1 502 ? 9.910  47.730  24.457 1.00 20.66 ? 502  ILE   A CD1  1 
ATOM   7690  H  H    . ILE   A 1 502 ? 6.294  45.274  26.049 1.00 22.18 ? 502  ILE   A H    1 
ATOM   7691  H  HA   . ILE   A 1 502 ? 8.698  46.205  26.384 1.00 23.13 ? 502  ILE   A HA   1 
ATOM   7692  H  HB   . ILE   A 1 502 ? 7.547  46.528  24.380 1.00 24.08 ? 502  ILE   A HB   1 
ATOM   7693  H  HG12 . ILE   A 1 502 ? 8.231  48.750  23.900 1.00 27.21 ? 502  ILE   A HG12 1 
ATOM   7694  H  HG13 . ILE   A 1 502 ? 8.568  48.937  25.411 1.00 27.21 ? 502  ILE   A HG13 1 
ATOM   7695  H  HG21 . ILE   A 1 502 ? 5.902  48.181  24.170 1.00 27.95 ? 502  ILE   A HG21 1 
ATOM   7696  H  HG22 . ILE   A 1 502 ? 5.440  47.053  25.181 1.00 27.95 ? 502  ILE   A HG22 1 
ATOM   7697  H  HG23 . ILE   A 1 502 ? 5.974  48.440  25.731 1.00 27.95 ? 502  ILE   A HG23 1 
ATOM   7698  H  HD11 . ILE   A 1 502 ? 10.514 48.455  24.233 1.00 24.79 ? 502  ILE   A HD11 1 
ATOM   7699  H  HD12 . ILE   A 1 502 ? 10.225 47.285  25.259 1.00 24.79 ? 502  ILE   A HD12 1 
ATOM   7700  H  HD13 . ILE   A 1 502 ? 9.883  47.095  23.725 1.00 24.79 ? 502  ILE   A HD13 1 
ATOM   7701  N  N    . GLN   A 1 503 ? 6.593  47.928  28.080 1.00 16.62 ? 503  GLN   A N    1 
ATOM   7702  C  CA   . GLN   A 1 503 ? 6.541  48.999  29.113 1.00 19.99 ? 503  GLN   A CA   1 
ATOM   7703  C  C    . GLN   A 1 503 ? 7.342  48.557  30.344 1.00 20.48 ? 503  GLN   A C    1 
ATOM   7704  O  O    . GLN   A 1 503 ? 7.989  49.411  30.961 1.00 19.89 ? 503  GLN   A O    1 
ATOM   7705  C  CB   . GLN   A 1 503 ? 5.095  49.347  29.473 1.00 21.96 ? 503  GLN   A CB   1 
ATOM   7706  C  CG   . GLN   A 1 503 ? 4.968  50.540  30.410 1.00 26.26 ? 503  GLN   A CG   1 
ATOM   7707  C  CD   . GLN   A 1 503 ? 5.654  51.771  29.872 1.00 28.57 ? 503  GLN   A CD   1 
ATOM   7708  O  OE1  . GLN   A 1 503 ? 5.480  52.148  28.716 1.00 24.15 ? 503  GLN   A OE1  1 
ATOM   7709  N  NE2  . GLN   A 1 503 ? 6.447  52.412  30.715 1.00 24.22 ? 503  GLN   A NE2  1 
ATOM   7710  H  H    . GLN   A 1 503 ? 5.836  47.580  27.866 1.00 19.95 ? 503  GLN   A H    1 
ATOM   7711  H  HA   . GLN   A 1 503 ? 6.943  49.807  28.757 1.00 23.99 ? 503  GLN   A HA   1 
ATOM   7712  H  HB2  . GLN   A 1 503 ? 4.603  49.532  28.658 1.00 26.36 ? 503  GLN   A HB2  1 
ATOM   7713  H  HB3  . GLN   A 1 503 ? 4.678  48.575  29.887 1.00 26.36 ? 503  GLN   A HB3  1 
ATOM   7714  H  HG2  . GLN   A 1 503 ? 4.029  50.734  30.556 1.00 31.51 ? 503  GLN   A HG2  1 
ATOM   7715  H  HG3  . GLN   A 1 503 ? 5.348  50.312  31.273 1.00 31.51 ? 503  GLN   A HG3  1 
ATOM   7716  H  HE21 . GLN   A 1 503 ? 6.546  52.121  31.518 1.00 29.07 ? 503  GLN   A HE21 1 
ATOM   7717  H  HE22 . GLN   A 1 503 ? 6.863  53.120  30.460 1.00 29.07 ? 503  GLN   A HE22 1 
ATOM   7718  N  N    . ASP   A 1 504 ? 7.281  47.271  30.688 1.00 20.15 ? 504  ASP   A N    1 
ATOM   7719  C  CA   . ASP   A 1 504 ? 8.014  46.750  31.870 1.00 18.59 ? 504  ASP   A CA   1 
ATOM   7720  C  C    . ASP   A 1 504 ? 9.519  46.932  31.652 1.00 18.61 ? 504  ASP   A C    1 
ATOM   7721  O  O    . ASP   A 1 504 ? 10.223 47.226  32.626 1.00 17.27 ? 504  ASP   A O    1 
ATOM   7722  C  CB   . ASP   A 1 504 ? 7.647  45.289  32.139 1.00 18.14 ? 504  ASP   A CB   1 
ATOM   7723  C  CG   . ASP   A 1 504 ? 6.157  45.085  32.350 1.00 20.13 ? 504  ASP   A CG   1 
ATOM   7724  O  OD1  . ASP   A 1 504 ? 5.623  45.654  33.321 1.00 22.96 ? 504  ASP   A OD1  1 
ATOM   7725  O  OD2  . ASP   A 1 504 ? 5.547  44.364  31.543 1.00 21.95 ? 504  ASP   A OD2  1 
ATOM   7726  H  H    . ASP   A 1 504 ? 6.827  46.679  30.260 1.00 24.19 ? 504  ASP   A H    1 
ATOM   7727  H  HA   . ASP   A 1 504 ? 7.756  47.252  32.659 1.00 22.32 ? 504  ASP   A HA   1 
ATOM   7728  H  HB2  . ASP   A 1 504 ? 7.941  44.743  31.393 1.00 21.77 ? 504  ASP   A HB2  1 
ATOM   7729  H  HB3  . ASP   A 1 504 ? 8.126  44.979  32.923 1.00 21.77 ? 504  ASP   A HB3  1 
ATOM   7730  N  N    . TYR   A 1 505 ? 9.974  46.769  30.408 1.00 17.19 ? 505  TYR   A N    1 
ATOM   7731  C  CA   . TYR   A 1 505 ? 11.413 46.933  30.083 1.00 14.58 ? 505  TYR   A CA   1 
ATOM   7732  C  C    . TYR   A 1 505 ? 11.769 48.423  30.160 1.00 17.72 ? 505  TYR   A C    1 
ATOM   7733  O  O    . TYR   A 1 505 ? 12.838 48.760  30.686 1.00 15.06 ? 505  TYR   A O    1 
ATOM   7734  C  CB   . TYR   A 1 505 ? 11.721 46.294  28.725 1.00 13.91 ? 505  TYR   A CB   1 
ATOM   7735  C  CG   . TYR   A 1 505 ? 11.428 44.816  28.690 1.00 14.77 ? 505  TYR   A CG   1 
ATOM   7736  C  CD1  . TYR   A 1 505 ? 12.067 43.946  29.557 1.00 15.83 ? 505  TYR   A CD1  1 
ATOM   7737  C  CD2  . TYR   A 1 505 ? 10.494 44.287  27.816 1.00 15.71 ? 505  TYR   A CD2  1 
ATOM   7738  C  CE1  . TYR   A 1 505 ? 11.795 42.588  29.551 1.00 15.54 ? 505  TYR   A CE1  1 
ATOM   7739  C  CE2  . TYR   A 1 505 ? 10.210 42.932  27.796 1.00 14.35 ? 505  TYR   A CE2  1 
ATOM   7740  C  CZ   . TYR   A 1 505 ? 10.864 42.078  28.665 1.00 16.75 ? 505  TYR   A CZ   1 
ATOM   7741  O  OH   . TYR   A 1 505 ? 10.592 40.732  28.654 1.00 16.57 ? 505  TYR   A OH   1 
ATOM   7742  H  H    . TYR   A 1 505 ? 9.477  46.565  29.736 1.00 20.63 ? 505  TYR   A H    1 
ATOM   7743  H  HA   . TYR   A 1 505 ? 11.972 46.470  30.726 1.00 17.50 ? 505  TYR   A HA   1 
ATOM   7744  H  HB2  . TYR   A 1 505 ? 11.200 46.738  28.038 1.00 16.69 ? 505  TYR   A HB2  1 
ATOM   7745  H  HB3  . TYR   A 1 505 ? 12.656 46.439  28.510 1.00 16.69 ? 505  TYR   A HB3  1 
ATOM   7746  H  HD1  . TYR   A 1 505 ? 12.693 44.281  30.157 1.00 19.00 ? 505  TYR   A HD1  1 
ATOM   7747  H  HD2  . TYR   A 1 505 ? 10.048 44.854  27.229 1.00 18.86 ? 505  TYR   A HD2  1 
ATOM   7748  H  HE1  . TYR   A 1 505 ? 12.237 42.021  30.141 1.00 18.65 ? 505  TYR   A HE1  1 
ATOM   7749  H  HE2  . TYR   A 1 505 ? 9.580  42.597  27.199 1.00 17.23 ? 505  TYR   A HE2  1 
ATOM   7750  H  HH   . TYR   A 1 505 ? 11.120 40.335  29.172 1.00 19.89 ? 505  TYR   A HH   1 
ATOM   7751  N  N    . VAL   A 1 506 ? 10.891 49.278  29.638 1.00 17.55 ? 506  VAL   A N    1 
ATOM   7752  C  CA   . VAL   A 1 506 ? 11.116 50.747  29.754 1.00 17.95 ? 506  VAL   A CA   1 
ATOM   7753  C  C    . VAL   A 1 506 ? 11.195 51.108  31.242 1.00 21.55 ? 506  VAL   A C    1 
ATOM   7754  O  O    . VAL   A 1 506 ? 12.093 51.880  31.616 1.00 20.23 ? 506  VAL   A O    1 
ATOM   7755  C  CB   . VAL   A 1 506 ? 9.996  51.529  29.044 1.00 18.51 ? 506  VAL   A CB   1 
ATOM   7756  C  CG1  . VAL   A 1 506 ? 10.004 53.001  29.428 1.00 21.07 ? 506  VAL   A CG1  1 
ATOM   7757  C  CG2  . VAL   A 1 506 ? 10.059 51.365  27.534 1.00 17.33 ? 506  VAL   A CG2  1 
ATOM   7758  H  H    . VAL   A 1 506 ? 10.174 49.050  29.221 1.00 21.06 ? 506  VAL   A H    1 
ATOM   7759  H  HA   . VAL   A 1 506 ? 11.948 50.991  29.320 1.00 21.54 ? 506  VAL   A HA   1 
ATOM   7760  H  HB   . VAL   A 1 506 ? 9.157  51.148  29.347 1.00 22.21 ? 506  VAL   A HB   1 
ATOM   7761  H  HG11 . VAL   A 1 506 ? 9.287  53.461  28.963 1.00 25.28 ? 506  VAL   A HG11 1 
ATOM   7762  H  HG12 . VAL   A 1 506 ? 9.875  53.087  30.386 1.00 25.28 ? 506  VAL   A HG12 1 
ATOM   7763  H  HG13 . VAL   A 1 506 ? 10.855 53.396  29.180 1.00 25.28 ? 506  VAL   A HG13 1 
ATOM   7764  H  HG21 . VAL   A 1 506 ? 9.340  51.870  27.123 1.00 20.80 ? 506  VAL   A HG21 1 
ATOM   7765  H  HG22 . VAL   A 1 506 ? 10.912 51.693  27.208 1.00 20.80 ? 506  VAL   A HG22 1 
ATOM   7766  H  HG23 . VAL   A 1 506 ? 9.965  50.427  27.306 1.00 20.80 ? 506  VAL   A HG23 1 
ATOM   7767  N  N    . ASP   A 1 507 ? 10.277 50.579  32.054 1.00 19.69 ? 507  ASP   A N    1 
ATOM   7768  C  CA   . ASP   A 1 507 ? 10.250 50.915  33.500 1.00 18.75 ? 507  ASP   A CA   1 
ATOM   7769  C  C    . ASP   A 1 507 ? 11.601 50.569  34.136 1.00 22.12 ? 507  ASP   A C    1 
ATOM   7770  O  O    . ASP   A 1 507 ? 12.140 51.414  34.870 1.00 22.69 ? 507  ASP   A O    1 
ATOM   7771  C  CB   . ASP   A 1 507 ? 9.129  50.176  34.231 1.00 23.57 ? 507  ASP   A CB   1 
ATOM   7772  C  CG   . ASP   A 1 507 ? 7.734  50.579  33.790 1.00 26.26 ? 507  ASP   A CG   1 
ATOM   7773  O  OD1  . ASP   A 1 507 ? 7.593  51.681  33.232 1.00 22.01 ? 507  ASP   A OD1  1 
ATOM   7774  O  OD2  . ASP   A 1 507 ? 6.804  49.782  34.009 1.00 27.91 ? 507  ASP   A OD2  1 
ATOM   7775  H  H    . ASP   A 1 507 ? 9.665  50.030  31.801 1.00 23.64 ? 507  ASP   A H    1 
ATOM   7776  H  HA   . ASP   A 1 507 ? 10.081 51.867  33.582 1.00 22.50 ? 507  ASP   A HA   1 
ATOM   7777  H  HB2  . ASP   A 1 507 ? 9.239  49.222  34.093 1.00 28.29 ? 507  ASP   A HB2  1 
ATOM   7778  H  HB3  . ASP   A 1 507 ? 9.216  50.336  35.184 1.00 28.29 ? 507  ASP   A HB3  1 
ATOM   7779  N  N    . MET   A 1 508 ? 12.116 49.370  33.864 1.00 22.31 ? 508  MET   A N    1 
ATOM   7780  C  CA   . MET   A 1 508 ? 13.380 48.921  34.506 1.00 21.12 ? 508  MET   A CA   1 
ATOM   7781  C  C    . MET   A 1 508 ? 14.560 49.732  33.954 1.00 20.87 ? 508  MET   A C    1 
ATOM   7782  O  O    . MET   A 1 508 ? 15.411 50.145  34.755 1.00 22.38 ? 508  MET   A O    1 
ATOM   7783  C  CB   . MET   A 1 508 ? 13.606 47.419  34.278 1.00 19.95 ? 508  MET   A CB   1 
ATOM   7784  C  CG   . MET   A 1 508 ? 12.614 46.548  35.024 1.00 20.61 ? 508  MET   A CG   1 
ATOM   7785  S  SD   . MET   A 1 508 ? 12.981 44.778  34.895 1.00 21.26 ? 508  MET   A SD   1 
ATOM   7786  C  CE   . MET   A 1 508 ? 12.256 44.406  33.299 1.00 19.77 ? 508  MET   A CE   1 
ATOM   7787  H  H    . MET   A 1 508 ? 11.765 48.802  33.322 1.00 26.77 ? 508  MET   A H    1 
ATOM   7788  H  HA   . MET   A 1 508 ? 13.313 49.071  35.462 1.00 25.35 ? 508  MET   A HA   1 
ATOM   7789  H  HB2  . MET   A 1 508 ? 13.545 47.229  33.329 1.00 23.95 ? 508  MET   A HB2  1 
ATOM   7790  H  HB3  . MET   A 1 508 ? 14.506 47.187  34.557 1.00 23.95 ? 508  MET   A HB3  1 
ATOM   7791  H  HG2  . MET   A 1 508 ? 12.607 46.804  35.960 1.00 24.74 ? 508  MET   A HG2  1 
ATOM   7792  H  HG3  . MET   A 1 508 ? 11.723 46.714  34.678 1.00 24.74 ? 508  MET   A HG3  1 
ATOM   7793  H  HE1  . MET   A 1 508 ? 12.383 43.466  33.097 1.00 23.73 ? 508  MET   A HE1  1 
ATOM   7794  H  HE2  . MET   A 1 508 ? 11.307 44.607  33.320 1.00 23.73 ? 508  MET   A HE2  1 
ATOM   7795  H  HE3  . MET   A 1 508 ? 12.685 44.944  32.615 1.00 23.73 ? 508  MET   A HE3  1 
ATOM   7796  N  N    . TYR   A 1 509 ? 14.593 49.958  32.641 1.00 19.98 ? 509  TYR   A N    1 
ATOM   7797  C  CA   . TYR   A 1 509 ? 15.720 50.702  32.023 1.00 22.19 ? 509  TYR   A CA   1 
ATOM   7798  C  C    . TYR   A 1 509 ? 15.799 52.118  32.600 1.00 23.13 ? 509  TYR   A C    1 
ATOM   7799  O  O    . TYR   A 1 509 ? 16.896 52.536  33.007 1.00 22.97 ? 509  TYR   A O    1 
ATOM   7800  C  CB   . TYR   A 1 509 ? 15.561 50.801  30.505 1.00 18.73 ? 509  TYR   A CB   1 
ATOM   7801  C  CG   . TYR   A 1 509 ? 16.671 51.546  29.808 1.00 18.52 ? 509  TYR   A CG   1 
ATOM   7802  C  CD1  . TYR   A 1 509 ? 16.620 52.921  29.648 1.00 24.25 ? 509  TYR   A CD1  1 
ATOM   7803  C  CD2  . TYR   A 1 509 ? 17.778 50.880  29.312 1.00 20.89 ? 509  TYR   A CD2  1 
ATOM   7804  C  CE1  . TYR   A 1 509 ? 17.639 53.614  29.016 1.00 23.77 ? 509  TYR   A CE1  1 
ATOM   7805  C  CE2  . TYR   A 1 509 ? 18.804 51.556  28.674 1.00 21.18 ? 509  TYR   A CE2  1 
ATOM   7806  C  CZ   . TYR   A 1 509 ? 18.736 52.930  28.525 1.00 20.92 ? 509  TYR   A CZ   1 
ATOM   7807  O  OH   . TYR   A 1 509 ? 19.749 53.606  27.893 1.00 19.76 ? 509  TYR   A OH   1 
ATOM   7808  H  H    . TYR   A 1 509 ? 13.987 49.698  32.089 1.00 23.98 ? 509  TYR   A H    1 
ATOM   7809  H  HA   . TYR   A 1 509 ? 16.533 50.212  32.223 1.00 26.63 ? 509  TYR   A HA   1 
ATOM   7810  H  HB2  . TYR   A 1 509 ? 15.508 49.905  30.138 1.00 22.48 ? 509  TYR   A HB2  1 
ATOM   7811  H  HB3  . TYR   A 1 509 ? 14.719 51.239  30.307 1.00 22.48 ? 509  TYR   A HB3  1 
ATOM   7812  H  HD1  . TYR   A 1 509 ? 15.885 53.389  29.972 1.00 29.11 ? 509  TYR   A HD1  1 
ATOM   7813  H  HD2  . TYR   A 1 509 ? 17.834 49.957  29.410 1.00 25.07 ? 509  TYR   A HD2  1 
ATOM   7814  H  HE1  . TYR   A 1 509 ? 17.586 54.538  28.922 1.00 28.53 ? 509  TYR   A HE1  1 
ATOM   7815  H  HE2  . TYR   A 1 509 ? 19.537 51.088  28.346 1.00 25.43 ? 509  TYR   A HE2  1 
ATOM   7816  H  HH   . TYR   A 1 509 ? 20.389 53.082  27.750 1.00 23.71 ? 509  TYR   A HH   1 
ATOM   7817  N  N    . ASN   A 1 510 ? 14.667 52.827  32.626 1.00 22.12 ? 510  ASN   A N    1 
ATOM   7818  C  CA   . ASN   A 1 510 ? 14.668 54.242  33.087 1.00 23.65 ? 510  ASN   A CA   1 
ATOM   7819  C  C    . ASN   A 1 510 ? 15.027 54.306  34.576 1.00 24.64 ? 510  ASN   A C    1 
ATOM   7820  O  O    . ASN   A 1 510 ? 15.823 55.179  34.948 1.00 24.24 ? 510  ASN   A O    1 
ATOM   7821  C  CB   . ASN   A 1 510 ? 13.334 54.924  32.768 1.00 20.13 ? 510  ASN   A CB   1 
ATOM   7822  C  CG   . ASN   A 1 510 ? 13.171 55.243  31.298 1.00 23.42 ? 510  ASN   A CG   1 
ATOM   7823  O  OD1  . ASN   A 1 510 ? 14.144 55.257  30.548 1.00 22.42 ? 510  ASN   A OD1  1 
ATOM   7824  N  ND2  . ASN   A 1 510 ? 11.945 55.502  30.877 1.00 26.80 ? 510  ASN   A ND2  1 
ATOM   7825  H  H    . ASN   A 1 510 ? 13.898 52.524  32.388 1.00 26.54 ? 510  ASN   A H    1 
ATOM   7826  H  HA   . ASN   A 1 510 ? 15.348 54.737  32.603 1.00 28.38 ? 510  ASN   A HA   1 
ATOM   7827  H  HB2  . ASN   A 1 510 ? 12.606 54.349  33.052 1.00 24.16 ? 510  ASN   A HB2  1 
ATOM   7828  H  HB3  . ASN   A 1 510 ? 13.264 55.744  33.282 1.00 24.16 ? 510  ASN   A HB3  1 
ATOM   7829  H  HD21 . ASN   A 1 510 ? 11.805 55.689  30.049 1.00 32.16 ? 510  ASN   A HD21 1 
ATOM   7830  H  HD22 . ASN   A 1 510 ? 11.287 55.483  31.431 1.00 32.16 ? 510  ASN   A HD22 1 
ATOM   7831  N  N    . ALA   A 1 511 ? 14.454 53.417  35.385 1.00 24.64 ? 511  ALA   A N    1 
ATOM   7832  C  CA   . ALA   A 1 511 ? 14.757 53.384  36.834 1.00 26.32 ? 511  ALA   A CA   1 
ATOM   7833  C  C    . ALA   A 1 511 ? 16.263 53.213  37.063 1.00 23.96 ? 511  ALA   A C    1 
ATOM   7834  O  O    . ALA   A 1 511 ? 16.775 53.799  38.030 1.00 27.47 ? 511  ALA   A O    1 
ATOM   7835  C  CB   . ALA   A 1 511 ? 13.969 52.280  37.496 1.00 26.12 ? 511  ALA   A CB   1 
ATOM   7836  H  H    . ALA   A 1 511 ? 13.889 52.823  35.125 1.00 29.57 ? 511  ALA   A H    1 
ATOM   7837  H  HA   . ALA   A 1 511 ? 14.494 54.227  37.235 1.00 31.59 ? 511  ALA   A HA   1 
ATOM   7838  H  HB1  . ALA   A 1 511 ? 14.171 52.262  38.445 1.00 31.35 ? 511  ALA   A HB1  1 
ATOM   7839  H  HB2  . ALA   A 1 511 ? 13.020 52.439  37.370 1.00 31.35 ? 511  ALA   A HB2  1 
ATOM   7840  H  HB3  . ALA   A 1 511 ? 14.209 51.428  37.099 1.00 31.35 ? 511  ALA   A HB3  1 
ATOM   7841  N  N    . VAL   A 1 512 ? 16.949 52.464  36.196 1.00 22.22 ? 512  VAL   A N    1 
ATOM   7842  C  CA   . VAL   A 1 512 ? 18.368 52.195  36.402 1.00 23.88 ? 512  VAL   A CA   1 
ATOM   7843  C  C    . VAL   A 1 512 ? 19.230 53.280  35.764 1.00 23.41 ? 512  VAL   A C    1 
ATOM   7844  O  O    . VAL   A 1 512 ? 20.155 53.807  36.393 1.00 24.34 ? 512  VAL   A O    1 
ATOM   7845  C  CB   . VAL   A 1 512 ? 18.728 50.802  35.854 1.00 23.11 ? 512  VAL   A CB   1 
ATOM   7846  C  CG1  . VAL   A 1 512 ? 20.237 50.639  35.774 1.00 19.83 ? 512  VAL   A CG1  1 
ATOM   7847  C  CG2  . VAL   A 1 512 ? 18.104 49.710  36.712 1.00 22.72 ? 512  VAL   A CG2  1 
ATOM   7848  H  H    . VAL   A 1 512 ? 16.612 52.107  35.490 1.00 26.67 ? 512  VAL   A H    1 
ATOM   7849  H  HA   . VAL   A 1 512 ? 18.549 52.205  37.355 1.00 28.66 ? 512  VAL   A HA   1 
ATOM   7850  H  HB   . VAL   A 1 512 ? 18.367 50.719  34.958 1.00 27.73 ? 512  VAL   A HB   1 
ATOM   7851  H  HG11 . VAL   A 1 512 ? 20.450 49.758  35.428 1.00 23.80 ? 512  VAL   A HG11 1 
ATOM   7852  H  HG12 . VAL   A 1 512 ? 20.605 51.315  35.184 1.00 23.80 ? 512  VAL   A HG12 1 
ATOM   7853  H  HG13 . VAL   A 1 512 ? 20.621 50.739  36.659 1.00 23.80 ? 512  VAL   A HG13 1 
ATOM   7854  H  HG21 . VAL   A 1 512 ? 18.341 48.841  36.353 1.00 27.27 ? 512  VAL   A HG21 1 
ATOM   7855  H  HG22 . VAL   A 1 512 ? 18.434 49.784  37.621 1.00 27.27 ? 512  VAL   A HG22 1 
ATOM   7856  H  HG23 . VAL   A 1 512 ? 17.139 49.808  36.710 1.00 27.27 ? 512  VAL   A HG23 1 
ATOM   7857  N  N    . VAL   A 1 513 ? 18.939 53.631  34.514 1.00 22.05 ? 513  VAL   A N    1 
ATOM   7858  C  CA   . VAL   A 1 513 ? 19.822 54.485  33.722 1.00 24.53 ? 513  VAL   A CA   1 
ATOM   7859  C  C    . VAL   A 1 513 ? 19.507 55.963  33.911 1.00 27.78 ? 513  VAL   A C    1 
ATOM   7860  O  O    . VAL   A 1 513 ? 20.415 56.795  34.011 1.00 26.32 ? 513  VAL   A O    1 
ATOM   7861  C  CB   . VAL   A 1 513 ? 19.729 54.077  32.238 1.00 23.82 ? 513  VAL   A CB   1 
ATOM   7862  C  CG1  . VAL   A 1 513 ? 20.416 55.105  31.355 1.00 27.98 ? 513  VAL   A CG1  1 
ATOM   7863  C  CG2  . VAL   A 1 513 ? 20.339 52.689  32.027 1.00 20.78 ? 513  VAL   A CG2  1 
ATOM   7864  H  H    . VAL   A 1 513 ? 18.227 53.382  34.102 1.00 26.46 ? 513  VAL   A H    1 
ATOM   7865  H  HA   . VAL   A 1 513 ? 20.732 54.358  34.032 1.00 29.44 ? 513  VAL   A HA   1 
ATOM   7866  H  HB   . VAL   A 1 513 ? 18.793 54.042  31.988 1.00 28.59 ? 513  VAL   A HB   1 
ATOM   7867  H  HG11 . VAL   A 1 513 ? 20.347 54.832  30.427 1.00 33.58 ? 513  VAL   A HG11 1 
ATOM   7868  H  HG12 . VAL   A 1 513 ? 19.989 55.968  31.470 1.00 33.58 ? 513  VAL   A HG12 1 
ATOM   7869  H  HG13 . VAL   A 1 513 ? 21.351 55.172  31.604 1.00 33.58 ? 513  VAL   A HG13 1 
ATOM   7870  H  HG21 . VAL   A 1 513 ? 20.274 52.446  31.090 1.00 24.94 ? 513  VAL   A HG21 1 
ATOM   7871  H  HG22 . VAL   A 1 513 ? 21.272 52.701  32.293 1.00 24.94 ? 513  VAL   A HG22 1 
ATOM   7872  H  HG23 . VAL   A 1 513 ? 19.859 52.039  32.564 1.00 24.94 ? 513  VAL   A HG23 1 
ATOM   7873  N  N    . GLY   A 1 514 ? 18.214 56.288  33.914 1.00 26.55 ? 514  GLY   A N    1 
ATOM   7874  C  CA   . GLY   A 1 514 ? 17.818 57.706  33.996 1.00 30.04 ? 514  GLY   A CA   1 
ATOM   7875  C  C    . GLY   A 1 514 ? 16.367 57.906  33.605 1.00 29.38 ? 514  GLY   A C    1 
ATOM   7876  O  O    . GLY   A 1 514 ? 15.944 57.334  32.590 1.00 27.26 ? 514  GLY   A O    1 
ATOM   7877  H  H    . GLY   A 1 514 ? 17.564 55.726  33.871 1.00 31.86 ? 514  GLY   A H    1 
ATOM   7878  H  HA2  . GLY   A 1 514 ? 17.957 58.030  34.900 1.00 36.06 ? 514  GLY   A HA2  1 
ATOM   7879  H  HA3  . GLY   A 1 514 ? 18.386 58.235  33.414 1.00 36.06 ? 514  GLY   A HA3  1 
ATOM   7880  N  N    . GLU   A 1 515 ? 15.643 58.716  34.378 1.00 29.90 ? 515  GLU   A N    1 
ATOM   7881  C  CA   . GLU   A 1 515 ? 14.199 58.949  34.110 1.00 35.07 ? 515  GLU   A CA   1 
ATOM   7882  C  C    . GLU   A 1 515 ? 13.962 59.439  32.677 1.00 28.74 ? 515  GLU   A C    1 
ATOM   7883  O  O    . GLU   A 1 515 ? 14.717 60.314  32.227 1.00 30.17 ? 515  GLU   A O    1 
ATOM   7884  C  CB   . GLU   A 1 515 ? 13.648 59.941  35.138 1.00 35.49 ? 515  GLU   A CB   1 
ATOM   7885  C  CG   . GLU   A 1 515 ? 12.169 60.228  34.980 1.00 43.46 ? 515  GLU   A CG   1 
ATOM   7886  C  CD   . GLU   A 1 515 ? 11.486 60.605  36.282 1.00 53.79 ? 515  GLU   A CD   1 
ATOM   7887  O  OE1  . GLU   A 1 515 ? 12.034 61.460  37.005 1.00 45.35 ? 515  GLU   A OE1  1 
ATOM   7888  O  OE2  . GLU   A 1 515 ? 10.416 60.038  36.573 1.00 63.02 ? 515  GLU   A OE2  1 
ATOM   7889  H  H    . GLU   A 1 515 ? 15.954 59.141  35.058 1.00 35.89 ? 515  GLU   A H    1 
ATOM   7890  H  HA   . GLU   A 1 515 ? 13.725 58.107  34.196 1.00 42.08 ? 515  GLU   A HA   1 
ATOM   7891  H  HB2  . GLU   A 1 515 ? 13.808 59.592  36.029 1.00 42.59 ? 515  GLU   A HB2  1 
ATOM   7892  H  HB3  . GLU   A 1 515 ? 14.140 60.774  35.067 1.00 42.59 ? 515  GLU   A HB3  1 
ATOM   7893  H  HG2  . GLU   A 1 515 ? 12.053 60.948  34.341 1.00 52.15 ? 515  GLU   A HG2  1 
ATOM   7894  H  HG3  . GLU   A 1 515 ? 11.732 59.446  34.608 1.00 52.15 ? 515  GLU   A HG3  1 
ATOM   7895  N  N    . SER   A 1 516 ? 12.987 58.852  31.979 1.00 30.39 ? 516  SER   A N    1 
ATOM   7896  C  CA   . SER   A 1 516 ? 12.573 59.314  30.624 1.00 28.19 ? 516  SER   A CA   1 
ATOM   7897  C  C    . SER   A 1 516 ? 13.655 59.211  29.539 1.00 26.95 ? 516  SER   A C    1 
ATOM   7898  O  O    . SER   A 1 516 ? 13.537 59.949  28.551 1.00 29.37 ? 516  SER   A O    1 
ATOM   7899  C  CB   . SER   A 1 516 ? 12.018 60.715  30.714 1.00 33.00 ? 516  SER   A CB   1 
ATOM   7900  O  OG   . SER   A 1 516 ? 11.046 60.803  31.746 1.00 36.63 ? 516  SER   A OG   1 
ATOM   7901  H  H    . SER   A 1 516 ? 12.541 58.175  32.267 1.00 36.47 ? 516  SER   A H    1 
ATOM   7902  H  HA   . SER   A 1 516 ? 11.885 58.697  30.330 1.00 33.83 ? 516  SER   A HA   1 
ATOM   7903  H  HB2  . SER   A 1 516 ? 12.737 61.343  30.886 1.00 39.60 ? 516  SER   A HB2  1 
ATOM   7904  H  HB3  . SER   A 1 516 ? 11.620 60.966  29.866 1.00 39.60 ? 516  SER   A HB3  1 
ATOM   7905  H  HG   . SER   A 1 516 ? 10.748 61.587  31.785 1.00 43.96 ? 516  SER   A HG   1 
ATOM   7906  N  N    . THR   A 1 517 ? 14.635 58.309  29.663 1.00 28.18 ? 517  THR   A N    1 
ATOM   7907  C  CA   . THR   A 1 517 ? 15.616 58.158  28.552 1.00 27.44 ? 517  THR   A CA   1 
ATOM   7908  C  C    . THR   A 1 517 ? 14.908 57.519  27.351 1.00 29.38 ? 517  THR   A C    1 
ATOM   7909  O  O    . THR   A 1 517 ? 15.158 57.951  26.216 1.00 29.61 ? 517  THR   A O    1 
ATOM   7910  C  CB   . THR   A 1 517 ? 16.862 57.375  28.997 1.00 26.87 ? 517  THR   A CB   1 
ATOM   7911  O  OG1  . THR   A 1 517 ? 17.278 57.862  30.273 1.00 27.90 ? 517  THR   A OG1  1 
ATOM   7912  C  CG2  . THR   A 1 517 ? 18.000 57.472  28.005 1.00 29.23 ? 517  THR   A CG2  1 
ATOM   7913  H  H    . THR   A 1 517 ? 14.756 57.794  30.341 1.00 33.82 ? 517  THR   A H    1 
ATOM   7914  H  HA   . THR   A 1 517 ? 15.944 59.031  28.285 1.00 32.94 ? 517  THR   A HA   1 
ATOM   7915  H  HB   . THR   A 1 517 ? 16.623 56.436  29.050 1.00 32.25 ? 517  THR   A HB   1 
ATOM   7916  H  HG1  . THR   A 1 517 ? 16.774 57.552  30.869 1.00 33.48 ? 517  THR   A HG1  1 
ATOM   7917  H  HG21 . THR   A 1 517 ? 18.758 56.963  28.332 1.00 35.08 ? 517  THR   A HG21 1 
ATOM   7918  H  HG22 . THR   A 1 517 ? 17.715 57.114  27.150 1.00 35.08 ? 517  THR   A HG22 1 
ATOM   7919  H  HG23 . THR   A 1 517 ? 18.257 58.401  27.897 1.00 35.08 ? 517  THR   A HG23 1 
ATOM   7920  N  N    . TYR   A 1 518 ? 14.014 56.563  27.614 1.00 26.88 ? 518  TYR   A N    1 
ATOM   7921  C  CA   . TYR   A 1 518 ? 13.327 55.870  26.496 1.00 22.58 ? 518  TYR   A CA   1 
ATOM   7922  C  C    . TYR   A 1 518 ? 11.812 55.821  26.704 1.00 26.43 ? 518  TYR   A C    1 
ATOM   7923  O  O    . TYR   A 1 518 ? 11.365 55.972  27.854 1.00 23.61 ? 518  TYR   A O    1 
ATOM   7924  C  CB   . TYR   A 1 518 ? 13.867 54.446  26.335 1.00 25.56 ? 518  TYR   A CB   1 
ATOM   7925  C  CG   . TYR   A 1 518 ? 14.901 54.274  25.253 1.00 21.96 ? 518  TYR   A CG   1 
ATOM   7926  C  CD1  . TYR   A 1 518 ? 14.568 54.407  23.916 1.00 22.38 ? 518  TYR   A CD1  1 
ATOM   7927  C  CD2  . TYR   A 1 518 ? 16.216 53.973  25.566 1.00 20.84 ? 518  TYR   A CD2  1 
ATOM   7928  C  CE1  . TYR   A 1 518 ? 15.512 54.247  22.917 1.00 21.88 ? 518  TYR   A CE1  1 
ATOM   7929  C  CE2  . TYR   A 1 518 ? 17.173 53.809  24.580 1.00 19.49 ? 518  TYR   A CE2  1 
ATOM   7930  C  CZ   . TYR   A 1 518 ? 16.821 53.949  23.250 1.00 22.17 ? 518  TYR   A CZ   1 
ATOM   7931  O  OH   . TYR   A 1 518 ? 17.769 53.787  22.271 1.00 24.42 ? 518  TYR   A OH   1 
ATOM   7932  H  H    . TYR   A 1 518 ? 13.790 56.301  28.402 1.00 32.26 ? 518  TYR   A H    1 
ATOM   7933  H  HA   . TYR   A 1 518 ? 13.507 56.379  25.690 1.00 27.11 ? 518  TYR   A HA   1 
ATOM   7934  H  HB2  . TYR   A 1 518 ? 14.252 54.164  27.179 1.00 30.67 ? 518  TYR   A HB2  1 
ATOM   7935  H  HB3  . TYR   A 1 518 ? 13.123 53.852  26.150 1.00 30.67 ? 518  TYR   A HB3  1 
ATOM   7936  H  HD1  . TYR   A 1 518 ? 13.690 54.608  23.684 1.00 26.86 ? 518  TYR   A HD1  1 
ATOM   7937  H  HD2  . TYR   A 1 518 ? 16.461 53.879  26.458 1.00 25.01 ? 518  TYR   A HD2  1 
ATOM   7938  H  HE1  . TYR   A 1 518 ? 15.267 54.340  22.025 1.00 26.26 ? 518  TYR   A HE1  1 
ATOM   7939  H  HE2  . TYR   A 1 518 ? 18.050 53.605  24.811 1.00 23.39 ? 518  TYR   A HE2  1 
ATOM   7940  H  HH   . TYR   A 1 518 ? 18.528 53.719  22.624 1.00 29.31 ? 518  TYR   A HH   1 
ATOM   7941  N  N    . ASP   A 1 519 ? 11.062 55.642  25.622 1.00 24.68 ? 519  ASP   A N    1 
ATOM   7942  C  CA   . ASP   A 1 519 ? 9.604  55.409  25.760 1.00 27.94 ? 519  ASP   A CA   1 
ATOM   7943  C  C    . ASP   A 1 519 ? 9.336  54.082  25.035 1.00 21.29 ? 519  ASP   A C    1 
ATOM   7944  O  O    . ASP   A 1 519 ? 10.234 53.609  24.323 1.00 22.52 ? 519  ASP   A O    1 
ATOM   7945  C  CB   . ASP   A 1 519 ? 8.769  56.608  25.293 1.00 26.41 ? 519  ASP   A CB   1 
ATOM   7946  C  CG   . ASP   A 1 519 ? 8.928  56.965  23.827 1.00 26.34 ? 519  ASP   A CG   1 
ATOM   7947  O  OD1  . ASP   A 1 519 ? 8.799  56.057  22.990 1.00 35.68 ? 519  ASP   A OD1  1 
ATOM   7948  O  OD2  . ASP   A 1 519 ? 9.197  58.145  23.540 1.00 47.07 ? 519  ASP   A OD2  1 
ATOM   7949  H  H    . ASP   A 1 519 ? 11.357 55.649  24.814 1.00 29.63 ? 519  ASP   A H    1 
ATOM   7950  H  HA   . ASP   A 1 519 ? 9.323  55.330  26.685 1.00 33.53 ? 519  ASP   A HA   1 
ATOM   7951  H  HB2  . ASP   A 1 519 ? 7.833  56.421  25.467 1.00 31.69 ? 519  ASP   A HB2  1 
ATOM   7952  H  HB3  . ASP   A 1 519 ? 9.009  57.381  25.828 1.00 31.69 ? 519  ASP   A HB3  1 
ATOM   7953  N  N    . ALA   A 1 520 ? 8.160  53.500  25.238 1.00 21.13 ? 520  ALA   A N    1 
ATOM   7954  C  CA   . ALA   A 1 520 ? 7.845  52.202  24.595 1.00 22.86 ? 520  ALA   A CA   1 
ATOM   7955  C  C    . ALA   A 1 520 ? 8.108  52.263  23.086 1.00 22.62 ? 520  ALA   A C    1 
ATOM   7956  O  O    . ALA   A 1 520 ? 8.668  51.294  22.548 1.00 24.08 ? 520  ALA   A O    1 
ATOM   7957  C  CB   . ALA   A 1 520 ? 6.420  51.813  24.891 1.00 26.18 ? 520  ALA   A CB   1 
ATOM   7958  H  H    . ALA   A 1 520 ? 7.534  53.822  25.732 1.00 25.36 ? 520  ALA   A H    1 
ATOM   7959  H  HA   . ALA   A 1 520 ? 8.428  51.520  24.963 1.00 27.43 ? 520  ALA   A HA   1 
ATOM   7960  H  HB1  . ALA   A 1 520 ? 6.222  50.963  24.467 1.00 31.42 ? 520  ALA   A HB1  1 
ATOM   7961  H  HB2  . ALA   A 1 520 ? 6.299  51.732  25.850 1.00 31.42 ? 520  ALA   A HB2  1 
ATOM   7962  H  HB3  . ALA   A 1 520 ? 5.820  52.493  24.547 1.00 31.42 ? 520  ALA   A HB3  1 
ATOM   7963  N  N    . ASP   A 1 521 ? 7.713  53.355  22.427 1.00 26.40 ? 521  ASP   A N    1 
ATOM   7964  C  CA   . ASP   A 1 521 ? 7.852  53.445  20.947 1.00 22.87 ? 521  ASP   A CA   1 
ATOM   7965  C  C    . ASP   A 1 521 ? 9.327  53.592  20.555 1.00 22.16 ? 521  ASP   A C    1 
ATOM   7966  O  O    . ASP   A 1 521 ? 9.747  52.908  19.617 1.00 22.13 ? 521  ASP   A O    1 
ATOM   7967  C  CB   . ASP   A 1 521 ? 7.006  54.589  20.378 1.00 27.86 ? 521  ASP   A CB   1 
ATOM   7968  C  CG   . ASP   A 1 521 ? 5.524  54.447  20.675 1.00 37.29 ? 521  ASP   A CG   1 
ATOM   7969  O  OD1  . ASP   A 1 521 ? 5.089  54.950  21.728 1.00 42.98 ? 521  ASP   A OD1  1 
ATOM   7970  O  OD2  . ASP   A 1 521 ? 4.820  53.835  19.853 1.00 40.67 ? 521  ASP   A OD2  1 
ATOM   7971  H  H    . ASP   A 1 521 ? 7.367  54.048  22.800 1.00 31.68 ? 521  ASP   A H    1 
ATOM   7972  H  HA   . ASP   A 1 521 ? 7.518  52.620  20.560 1.00 27.45 ? 521  ASP   A HA   1 
ATOM   7973  H  HB2  . ASP   A 1 521 ? 7.323  55.430  20.743 1.00 33.43 ? 521  ASP   A HB2  1 
ATOM   7974  H  HB3  . ASP   A 1 521 ? 7.134  54.631  19.417 1.00 33.43 ? 521  ASP   A HB3  1 
ATOM   7975  N  N    . SER   A 1 522 ? 10.067 54.469  21.236 1.00 20.82 ? 522  SER   A N    1 
ATOM   7976  C  CA   . SER   A 1 522 ? 11.482 54.735  20.879 1.00 22.89 ? 522  SER   A CA   1 
ATOM   7977  C  C    . SER   A 1 522 ? 12.312 53.474  21.136 1.00 17.78 ? 522  SER   A C    1 
ATOM   7978  O  O    . SER   A 1 522 ? 13.233 53.197  20.353 1.00 21.10 ? 522  SER   A O    1 
ATOM   7979  C  CB   . SER   A 1 522 ? 12.015 55.917  21.656 1.00 22.24 ? 522  SER   A CB   1 
ATOM   7980  O  OG   . SER   A 1 522 ? 11.729 55.787  23.037 1.00 25.69 ? 522  SER   A OG   1 
ATOM   7981  H  H    . SER   A 1 522 ? 9.778  54.923  21.907 1.00 24.98 ? 522  SER   A H    1 
ATOM   7982  H  HA   . SER   A 1 522 ? 11.543 54.960  19.937 1.00 27.48 ? 522  SER   A HA   1 
ATOM   7983  H  HB2  . SER   A 1 522 ? 12.974 55.988  21.526 1.00 26.69 ? 522  SER   A HB2  1 
ATOM   7984  H  HB3  . SER   A 1 522 ? 11.621 56.736  21.316 1.00 26.69 ? 522  SER   A HB3  1 
ATOM   7985  H  HG   . SER   A 1 522 ? 11.336 55.057  23.174 1.00 30.83 ? 522  SER   A HG   1 
ATOM   7986  N  N    . LEU   A 1 523 ? 11.975 52.746  22.196 1.00 17.89 ? 523  LEU   A N    1 
ATOM   7987  C  CA   . LEU   A 1 523 ? 12.782 51.546  22.554 1.00 19.43 ? 523  LEU   A CA   1 
ATOM   7988  C  C    . LEU   A 1 523 ? 12.564 50.443  21.512 1.00 16.80 ? 523  LEU   A C    1 
ATOM   7989  O  O    . LEU   A 1 523 ? 13.545 49.831  21.085 1.00 16.14 ? 523  LEU   A O    1 
ATOM   7990  C  CB   . LEU   A 1 523 ? 12.386 51.062  23.951 1.00 18.58 ? 523  LEU   A CB   1 
ATOM   7991  C  CG   . LEU   A 1 523 ? 13.316 50.022  24.573 1.00 17.54 ? 523  LEU   A CG   1 
ATOM   7992  C  CD1  . LEU   A 1 523 ? 14.756 50.512  24.571 1.00 14.88 ? 523  LEU   A CD1  1 
ATOM   7993  C  CD2  . LEU   A 1 523 ? 12.870 49.677  25.985 1.00 15.80 ? 523  LEU   A CD2  1 
ATOM   7994  H  H    . LEU   A 1 523 ? 11.309 52.910  22.714 1.00 21.47 ? 523  LEU   A H    1 
ATOM   7995  H  HA   . LEU   A 1 523 ? 13.724 51.776  22.561 1.00 23.32 ? 523  LEU   A HA   1 
ATOM   7996  H  HB2  . LEU   A 1 523 ? 12.343 51.830  24.542 1.00 22.30 ? 523  LEU   A HB2  1 
ATOM   7997  H  HB3  . LEU   A 1 523 ? 11.492 50.688  23.906 1.00 22.30 ? 523  LEU   A HB3  1 
ATOM   7998  H  HG   . LEU   A 1 523 ? 13.270 49.217  24.034 1.00 21.05 ? 523  LEU   A HG   1 
ATOM   7999  H  HD11 . LEU   A 1 523 ? 15.328 49.838  24.970 1.00 17.86 ? 523  LEU   A HD11 1 
ATOM   8000  H  HD12 . LEU   A 1 523 ? 15.040 50.678  23.659 1.00 17.86 ? 523  LEU   A HD12 1 
ATOM   8001  H  HD13 . LEU   A 1 523 ? 14.819 51.333  25.084 1.00 17.86 ? 523  LEU   A HD13 1 
ATOM   8002  H  HD21 . LEU   A 1 523 ? 13.472 49.016  26.362 1.00 18.96 ? 523  LEU   A HD21 1 
ATOM   8003  H  HD22 . LEU   A 1 523 ? 12.884 50.477  26.533 1.00 18.96 ? 523  LEU   A HD22 1 
ATOM   8004  H  HD23 . LEU   A 1 523 ? 11.970 49.317  25.961 1.00 18.96 ? 523  LEU   A HD23 1 
ATOM   8005  N  N    . LEU   A 1 524 ? 11.309 50.203  21.135 1.00 17.86 ? 524  LEU   A N    1 
ATOM   8006  C  CA   . LEU   A 1 524 ? 11.029 49.191  20.084 1.00 20.24 ? 524  LEU   A CA   1 
ATOM   8007  C  C    . LEU   A 1 524 ? 11.678 49.638  18.768 1.00 15.99 ? 524  LEU   A C    1 
ATOM   8008  O  O    . LEU   A 1 524 ? 12.169 48.776  18.031 1.00 14.08 ? 524  LEU   A O    1 
ATOM   8009  C  CB   . LEU   A 1 524 ? 9.513  49.013  19.941 1.00 21.68 ? 524  LEU   A CB   1 
ATOM   8010  C  CG   . LEU   A 1 524 ? 8.908  47.877  20.762 1.00 22.30 ? 524  LEU   A CG   1 
ATOM   8011  C  CD1  . LEU   A 1 524 ? 7.397  47.836  20.598 1.00 27.59 ? 524  LEU   A CD1  1 
ATOM   8012  C  CD2  . LEU   A 1 524 ? 9.521  46.541  20.370 1.00 21.11 ? 524  LEU   A CD2  1 
ATOM   8013  H  H    . LEU   A 1 524 ? 10.616 50.597  21.458 1.00 21.43 ? 524  LEU   A H    1 
ATOM   8014  H  HA   . LEU   A 1 524 ? 11.407 48.332  20.329 1.00 24.29 ? 524  LEU   A HA   1 
ATOM   8015  H  HB2  . LEU   A 1 524 ? 9.080  49.843  20.196 1.00 26.02 ? 524  LEU   A HB2  1 
ATOM   8016  H  HB3  . LEU   A 1 524 ? 9.307  48.861  19.005 1.00 26.02 ? 524  LEU   A HB3  1 
ATOM   8017  H  HG   . LEU   A 1 524 ? 9.109  48.044  21.696 1.00 26.76 ? 524  LEU   A HG   1 
ATOM   8018  H  HD11 . LEU   A 1 524 ? 7.034  47.109  21.127 1.00 33.11 ? 524  LEU   A HD11 1 
ATOM   8019  H  HD12 . LEU   A 1 524 ? 7.016  48.676  20.899 1.00 33.11 ? 524  LEU   A HD12 1 
ATOM   8020  H  HD13 . LEU   A 1 524 ? 7.176  47.698  19.664 1.00 33.11 ? 524  LEU   A HD13 1 
ATOM   8021  H  HD21 . LEU   A 1 524 ? 9.124  45.834  20.902 1.00 25.34 ? 524  LEU   A HD21 1 
ATOM   8022  H  HD22 . LEU   A 1 524 ? 9.353  46.371  19.430 1.00 25.34 ? 524  LEU   A HD22 1 
ATOM   8023  H  HD23 . LEU   A 1 524 ? 10.478 46.565  20.528 1.00 25.34 ? 524  LEU   A HD23 1 
ATOM   8024  N  N    . GLU   A 1 525 ? 11.665 50.945  18.491 1.00 18.59 ? 525  GLU   A N    1 
ATOM   8025  C  CA   . GLU   A 1 525 ? 12.299 51.467  17.251 1.00 17.19 ? 525  GLU   A CA   1 
ATOM   8026  C  C    . GLU   A 1 525 ? 13.802 51.167  17.304 1.00 16.61 ? 525  GLU   A C    1 
ATOM   8027  O  O    . GLU   A 1 525 ? 14.396 50.906  16.251 1.00 14.55 ? 525  GLU   A O    1 
ATOM   8028  C  CB   . GLU   A 1 525 ? 12.040 52.968  17.093 1.00 19.54 ? 525  GLU   A CB   1 
ATOM   8029  C  CG   . GLU   A 1 525 ? 12.621 53.545  15.819 1.00 23.53 ? 525  GLU   A CG   1 
ATOM   8030  C  CD   . GLU   A 1 525 ? 12.278 55.006  15.591 1.00 30.03 ? 525  GLU   A CD   1 
ATOM   8031  O  OE1  . GLU   A 1 525 ? 12.736 55.848  16.385 1.00 31.27 ? 525  GLU   A OE1  1 
ATOM   8032  O  OE2  . GLU   A 1 525 ? 11.554 55.293  14.624 1.00 27.51 ? 525  GLU   A OE2  1 
ATOM   8033  H  H    . GLU   A 1 525 ? 11.304 51.544  18.991 1.00 22.31 ? 525  GLU   A H    1 
ATOM   8034  H  HA   . GLU   A 1 525 ? 11.910 51.029  16.478 1.00 20.64 ? 525  GLU   A HA   1 
ATOM   8035  H  HB2  . GLU   A 1 525 ? 11.083 53.128  17.106 1.00 23.46 ? 525  GLU   A HB2  1 
ATOM   8036  H  HB3  . GLU   A 1 525 ? 12.417 53.437  17.854 1.00 23.46 ? 525  GLU   A HB3  1 
ATOM   8037  H  HG2  . GLU   A 1 525 ? 13.586 53.449  15.842 1.00 28.24 ? 525  GLU   A HG2  1 
ATOM   8038  H  HG3  . GLU   A 1 525 ? 12.302 53.026  15.065 1.00 28.24 ? 525  GLU   A HG3  1 
ATOM   8039  N  N    . ALA   A 1 526 ? 14.379 51.215  18.503 1.00 16.49 ? 526  ALA   A N    1 
ATOM   8040  C  CA   . ALA   A 1 526 ? 15.816 50.892  18.650 1.00 15.96 ? 526  ALA   A CA   1 
ATOM   8041  C  C    . ALA   A 1 526 ? 16.037 49.412  18.305 1.00 15.32 ? 526  ALA   A C    1 
ATOM   8042  O  O    . ALA   A 1 526 ? 17.058 49.097  17.677 1.00 14.11 ? 526  ALA   A O    1 
ATOM   8043  C  CB   . ALA   A 1 526 ? 16.263 51.225  20.050 1.00 20.11 ? 526  ALA   A CB   1 
ATOM   8044  H  H    . ALA   A 1 526 ? 13.976 51.426  19.233 1.00 19.80 ? 526  ALA   A H    1 
ATOM   8045  H  HA   . ALA   A 1 526 ? 16.352 51.422  18.039 1.00 19.15 ? 526  ALA   A HA   1 
ATOM   8046  H  HB1  . ALA   A 1 526 ? 17.205 51.014  20.148 1.00 24.13 ? 526  ALA   A HB1  1 
ATOM   8047  H  HB2  . ALA   A 1 526 ? 16.125 52.170  20.218 1.00 24.13 ? 526  ALA   A HB2  1 
ATOM   8048  H  HB3  . ALA   A 1 526 ? 15.748 50.705  20.687 1.00 24.13 ? 526  ALA   A HB3  1 
ATOM   8049  N  N    . GLY   A 1 527 ? 15.103 48.542  18.700 1.00 16.47 ? 527  GLY   A N    1 
ATOM   8050  C  CA   . GLY   A 1 527 ? 15.210 47.116  18.333 1.00 13.76 ? 527  GLY   A CA   1 
ATOM   8051  C  C    . GLY   A 1 527 ? 15.185 46.947  16.824 1.00 12.19 ? 527  GLY   A C    1 
ATOM   8052  O  O    . GLY   A 1 527 ? 15.945 46.116  16.308 1.00 12.98 ? 527  GLY   A O    1 
ATOM   8053  H  H    . GLY   A 1 527 ? 14.413 48.746  19.171 1.00 19.77 ? 527  GLY   A H    1 
ATOM   8054  H  HA2  . GLY   A 1 527 ? 16.032 46.746  18.691 1.00 16.51 ? 527  GLY   A HA2  1 
ATOM   8055  H  HA3  . GLY   A 1 527 ? 14.478 46.619  18.731 1.00 16.51 ? 527  GLY   A HA3  1 
ATOM   8056  N  N    . ASP   A 1 528 ? 14.338 47.724  16.142 1.00 13.72 ? 528  ASP   A N    1 
ATOM   8057  C  CA   . ASP   A 1 528 ? 14.275 47.691  14.657 1.00 12.89 ? 528  ASP   A CA   1 
ATOM   8058  C  C    . ASP   A 1 528 ? 15.622 48.156  14.093 1.00 12.22 ? 528  ASP   A C    1 
ATOM   8059  O  O    . ASP   A 1 528 ? 16.125 47.530  13.155 1.00 11.47 ? 528  ASP   A O    1 
ATOM   8060  C  CB   . ASP   A 1 528 ? 13.090 48.534  14.174 1.00 16.18 ? 528  ASP   A CB   1 
ATOM   8061  C  CG   . ASP   A 1 528 ? 12.837 48.508  12.677 1.00 18.20 ? 528  ASP   A CG   1 
ATOM   8062  O  OD1  . ASP   A 1 528 ? 13.676 47.958  11.944 1.00 16.19 ? 528  ASP   A OD1  1 
ATOM   8063  O  OD2  . ASP   A 1 528 ? 11.794 49.046  12.262 1.00 16.40 ? 528  ASP   A OD2  1 
ATOM   8064  H  H    . ASP   A 1 528 ? 13.791 48.277  16.509 1.00 16.47 ? 528  ASP   A H    1 
ATOM   8065  H  HA   . ASP   A 1 528 ? 14.123 46.790  14.332 1.00 15.47 ? 528  ASP   A HA   1 
ATOM   8066  H  HB2  . ASP   A 1 528 ? 12.289 48.227  14.627 1.00 19.42 ? 528  ASP   A HB2  1 
ATOM   8067  H  HB3  . ASP   A 1 528 ? 13.235 49.454  14.446 1.00 19.42 ? 528  ASP   A HB3  1 
ATOM   8068  N  N    A ARG   A 1 529 ? 16.189 49.211  14.684 0.33 13.83 ? 529  ARG   A N    1 
ATOM   8069  N  N    B ARG   A 1 529 ? 16.181 49.221  14.671 0.67 13.83 ? 529  ARG   A N    1 
ATOM   8070  C  CA   A ARG   A 1 529 ? 17.505 49.731  14.230 0.33 13.66 ? 529  ARG   A CA   1 
ATOM   8071  C  CA   B ARG   A 1 529 ? 17.505 49.730  14.225 0.67 13.66 ? 529  ARG   A CA   1 
ATOM   8072  C  C    A ARG   A 1 529 ? 18.572 48.645  14.411 0.33 11.75 ? 529  ARG   A C    1 
ATOM   8073  C  C    B ARG   A 1 529 ? 18.562 48.633  14.403 0.67 11.75 ? 529  ARG   A C    1 
ATOM   8074  O  O    A ARG   A 1 529 ? 19.407 48.486  13.503 0.33 14.50 ? 529  ARG   A O    1 
ATOM   8075  O  O    B ARG   A 1 529 ? 19.434 48.514  13.528 0.67 14.50 ? 529  ARG   A O    1 
ATOM   8076  C  CB   A ARG   A 1 529 ? 17.863 50.999  15.012 0.33 15.97 ? 529  ARG   A CB   1 
ATOM   8077  C  CB   B ARG   A 1 529 ? 17.869 50.988  15.020 0.67 15.98 ? 529  ARG   A CB   1 
ATOM   8078  C  CG   A ARG   A 1 529 ? 19.336 51.377  14.945 0.33 15.40 ? 529  ARG   A CG   1 
ATOM   8079  C  CG   B ARG   A 1 529 ? 19.335 51.385  14.925 0.67 15.40 ? 529  ARG   A CG   1 
ATOM   8080  C  CD   A ARG   A 1 529 ? 19.721 52.355  16.038 0.33 18.27 ? 529  ARG   A CD   1 
ATOM   8081  C  CD   B ARG   A 1 529 ? 19.596 52.762  15.506 0.67 18.26 ? 529  ARG   A CD   1 
ATOM   8082  N  NE   A ARG   A 1 529 ? 19.005 53.616  15.927 0.33 21.45 ? 529  ARG   A NE   1 
ATOM   8083  N  NE   B ARG   A 1 529 ? 19.045 52.914  16.844 0.67 21.45 ? 529  ARG   A NE   1 
ATOM   8084  C  CZ   A ARG   A 1 529 ? 18.018 53.995  16.731 0.33 18.38 ? 529  ARG   A CZ   1 
ATOM   8085  C  CZ   B ARG   A 1 529 ? 18.055 53.739  17.164 0.67 18.38 ? 529  ARG   A CZ   1 
ATOM   8086  N  NH1  A ARG   A 1 529 ? 18.048 53.675  18.013 0.33 20.66 ? 529  ARG   A NH1  1 
ATOM   8087  N  NH1  B ARG   A 1 529 ? 17.365 54.346  16.213 0.67 20.66 ? 529  ARG   A NH1  1 
ATOM   8088  N  NH2  A ARG   A 1 529 ? 17.005 54.693  16.250 0.33 20.49 ? 529  ARG   A NH2  1 
ATOM   8089  N  NH2  B ARG   A 1 529 ? 17.756 53.952  18.432 0.67 20.49 ? 529  ARG   A NH2  1 
ATOM   8090  H  H    A ARG   A 1 529 ? 15.841 49.642  15.342 0.33 16.60 ? 529  ARG   A H    1 
ATOM   8091  H  H    B ARG   A 1 529 ? 15.824 49.665  15.315 0.67 16.60 ? 529  ARG   A H    1 
ATOM   8092  H  HA   A ARG   A 1 529 ? 17.461 49.963  13.289 0.33 16.40 ? 529  ARG   A HA   1 
ATOM   8093  H  HA   B ARG   A 1 529 ? 17.468 49.968  13.285 0.67 16.40 ? 529  ARG   A HA   1 
ATOM   8094  H  HB2  A ARG   A 1 529 ? 17.334 51.737  14.671 0.33 19.17 ? 529  ARG   A HB2  1 
ATOM   8095  H  HB2  B ARG   A 1 529 ? 17.324 51.726  14.705 0.67 19.17 ? 529  ARG   A HB2  1 
ATOM   8096  H  HB3  A ARG   A 1 529 ? 17.613 50.876  15.941 0.33 19.17 ? 529  ARG   A HB3  1 
ATOM   8097  H  HB3  B ARG   A 1 529 ? 17.643 50.846  15.952 0.67 19.17 ? 529  ARG   A HB3  1 
ATOM   8098  H  HG2  A ARG   A 1 529 ? 19.878 50.577  15.022 0.33 18.49 ? 529  ARG   A HG2  1 
ATOM   8099  H  HG2  B ARG   A 1 529 ? 19.876 50.730  15.393 0.67 18.49 ? 529  ARG   A HG2  1 
ATOM   8100  H  HG3  A ARG   A 1 529 ? 19.530 51.768  14.079 0.33 18.49 ? 529  ARG   A HG3  1 
ATOM   8101  H  HG3  B ARG   A 1 529 ? 19.613 51.370  13.996 0.67 18.49 ? 529  ARG   A HG3  1 
ATOM   8102  H  HD2  A ARG   A 1 529 ? 19.539 51.957  16.904 0.33 21.92 ? 529  ARG   A HD2  1 
ATOM   8103  H  HD2  B ARG   A 1 529 ? 20.552 52.923  15.533 0.67 21.92 ? 529  ARG   A HD2  1 
ATOM   8104  H  HD3  A ARG   A 1 529 ? 20.676 52.523  15.998 0.33 21.92 ? 529  ARG   A HD3  1 
ATOM   8105  H  HD3  B ARG   A 1 529 ? 19.211 53.435  14.922 0.67 21.92 ? 529  ARG   A HD3  1 
ATOM   8106  H  HE   A ARG   A 1 529 ? 19.237 54.154  15.297 0.33 25.74 ? 529  ARG   A HE   1 
ATOM   8107  H  HE   B ARG   A 1 529 ? 19.385 52.435  17.472 0.67 25.74 ? 529  ARG   A HE   1 
ATOM   8108  H  HH11 A ARG   A 1 529 ? 18.707 53.221  18.328 0.33 24.80 ? 529  ARG   A HH11 1 
ATOM   8109  H  HH11 B ARG   A 1 529 ? 17.557 54.207  15.386 0.67 24.80 ? 529  ARG   A HH11 1 
ATOM   8110  H  HH12 A ARG   A 1 529 ? 17.408 53.921  18.533 0.33 24.80 ? 529  ARG   A HH12 1 
ATOM   8111  H  HH12 B ARG   A 1 529 ? 16.724 54.880  16.421 0.67 24.80 ? 529  ARG   A HH12 1 
ATOM   8112  H  HH21 A ARG   A 1 529 ? 16.984 54.902  15.416 0.33 24.60 ? 529  ARG   A HH21 1 
ATOM   8113  H  HH21 B ARG   A 1 529 ? 18.203 53.556  19.051 0.67 24.60 ? 529  ARG   A HH21 1 
ATOM   8114  H  HH22 A ARG   A 1 529 ? 16.366 54.938  16.771 0.33 24.60 ? 529  ARG   A HH22 1 
ATOM   8115  H  HH22 B ARG   A 1 529 ? 17.115 54.486  18.639 0.67 24.60 ? 529  ARG   A HH22 1 
ATOM   8116  N  N    . ILE   A 1 530 ? 18.510 47.899  15.520 1.00 12.54 ? 530  ILE   A N    1 
ATOM   8117  C  CA   . ILE   A 1 530 ? 19.546 46.856  15.797 1.00 16.20 ? 530  ILE   A CA   1 
ATOM   8118  C  C    . ILE   A 1 530 ? 19.410 45.695  14.800 1.00 10.03 ? 530  ILE   A C    1 
ATOM   8119  O  O    . ILE   A 1 530 ? 20.428 45.250  14.266 1.00 10.64 ? 530  ILE   A O    1 
ATOM   8120  C  CB   . ILE   A 1 530 ? 19.451 46.378  17.259 1.00 14.40 ? 530  ILE   A CB   1 
ATOM   8121  C  CG1  . ILE   A 1 530 ? 19.925 47.461  18.231 1.00 12.39 ? 530  ILE   A CG1  1 
ATOM   8122  C  CG2  . ILE   A 1 530 ? 20.212 45.076  17.450 1.00 15.07 ? 530  ILE   A CG2  1 
ATOM   8123  C  CD1  . ILE   A 1 530 ? 19.423 47.285  19.641 1.00 15.04 ? 530  ILE   A CD1  1 
ATOM   8124  H  H    A ILE   A 1 530 ? 17.897 47.968  16.119 0.33 15.06 ? 530  ILE   A H    1 
ATOM   8125  H  H    B ILE   A 1 530 ? 17.904 47.976  16.125 0.67 15.06 ? 530  ILE   A H    1 
ATOM   8126  H  HA   . ILE   A 1 530 ? 20.428 47.242  15.677 1.00 19.45 ? 530  ILE   A HA   1 
ATOM   8127  H  HB   . ILE   A 1 530 ? 18.518 46.205  17.460 1.00 17.29 ? 530  ILE   A HB   1 
ATOM   8128  H  HG12 . ILE   A 1 530 ? 20.895 47.470  18.242 1.00 14.87 ? 530  ILE   A HG12 1 
ATOM   8129  H  HG13 . ILE   A 1 530 ? 19.637 48.327  17.901 1.00 14.87 ? 530  ILE   A HG13 1 
ATOM   8130  H  HG21 . ILE   A 1 530 ? 20.141 44.792  18.375 1.00 18.09 ? 530  ILE   A HG21 1 
ATOM   8131  H  HG22 . ILE   A 1 530 ? 19.836 44.393  16.872 1.00 18.09 ? 530  ILE   A HG22 1 
ATOM   8132  H  HG23 . ILE   A 1 530 ? 21.146 45.211  17.225 1.00 18.09 ? 530  ILE   A HG23 1 
ATOM   8133  H  HD11 . ILE   A 1 530 ? 19.762 48.004  20.197 1.00 18.05 ? 530  ILE   A HD11 1 
ATOM   8134  H  HD12 . ILE   A 1 530 ? 18.453 47.304  19.644 1.00 18.05 ? 530  ILE   A HD12 1 
ATOM   8135  H  HD13 . ILE   A 1 530 ? 19.731 46.434  19.990 1.00 18.05 ? 530  ILE   A HD13 1 
ATOM   8136  N  N    . TRP   A 1 531 ? 18.184 45.226  14.572 1.00 11.48 ? 531  TRP   A N    1 
ATOM   8137  C  CA   . TRP   A 1 531 ? 17.961 44.131  13.594 1.00 12.11 ? 531  TRP   A CA   1 
ATOM   8138  C  C    . TRP   A 1 531 ? 18.420 44.569  12.199 1.00 12.25 ? 531  TRP   A C    1 
ATOM   8139  O  O    . TRP   A 1 531 ? 19.007 43.745  11.482 1.00 12.42 ? 531  TRP   A O    1 
ATOM   8140  C  CB   . TRP   A 1 531 ? 16.481 43.722  13.584 1.00 11.61 ? 531  TRP   A CB   1 
ATOM   8141  C  CG   . TRP   A 1 531 ? 16.187 42.565  12.683 1.00 11.63 ? 531  TRP   A CG   1 
ATOM   8142  C  CD1  . TRP   A 1 531 ? 16.001 42.598  11.332 1.00 11.80 ? 531  TRP   A CD1  1 
ATOM   8143  C  CD2  . TRP   A 1 531 ? 16.064 41.186  13.071 1.00 11.45 ? 531  TRP   A CD2  1 
ATOM   8144  N  NE1  . TRP   A 1 531 ? 15.764 41.338  10.853 1.00 14.31 ? 531  TRP   A NE1  1 
ATOM   8145  C  CE2  . TRP   A 1 531 ? 15.797 40.451  11.897 1.00 12.21 ? 531  TRP   A CE2  1 
ATOM   8146  C  CE3  . TRP   A 1 531 ? 16.151 40.505  14.289 1.00 11.48 ? 531  TRP   A CE3  1 
ATOM   8147  C  CZ2  . TRP   A 1 531 ? 15.618 39.070  11.911 1.00 10.91 ? 531  TRP   A CZ2  1 
ATOM   8148  C  CZ3  . TRP   A 1 531 ? 15.971 39.140  14.301 1.00 12.52 ? 531  TRP   A CZ3  1 
ATOM   8149  C  CH2  . TRP   A 1 531 ? 15.709 38.436  13.127 1.00 11.46 ? 531  TRP   A CH2  1 
ATOM   8150  H  H    . TRP   A 1 531 ? 17.473 45.515  14.960 1.00 13.78 ? 531  TRP   A H    1 
ATOM   8151  H  HA   . TRP   A 1 531 ? 18.486 43.359  13.857 1.00 14.54 ? 531  TRP   A HA   1 
ATOM   8152  H  HB2  . TRP   A 1 531 ? 16.209 43.496  14.487 1.00 13.94 ? 531  TRP   A HB2  1 
ATOM   8153  H  HB3  . TRP   A 1 531 ? 15.945 44.482  13.308 1.00 13.94 ? 531  TRP   A HB3  1 
ATOM   8154  H  HD1  . TRP   A 1 531 ? 16.031 43.367  10.810 1.00 14.16 ? 531  TRP   A HD1  1 
ATOM   8155  H  HE1  . TRP   A 1 531 ? 15.618 41.136  10.030 1.00 17.18 ? 531  TRP   A HE1  1 
ATOM   8156  H  HE3  . TRP   A 1 531 ? 16.327 40.966  15.077 1.00 13.77 ? 531  TRP   A HE3  1 
ATOM   8157  H  HZ2  . TRP   A 1 531 ? 15.444 38.596  11.130 1.00 13.10 ? 531  TRP   A HZ2  1 
ATOM   8158  H  HZ3  . TRP   A 1 531 ? 16.025 38.679  15.107 1.00 15.03 ? 531  TRP   A HZ3  1 
ATOM   8159  H  HH2  . TRP   A 1 531 ? 15.593 37.514  13.167 1.00 13.76 ? 531  TRP   A HH2  1 
ATOM   8160  N  N    . THR   A 1 532 ? 18.115 45.815  11.829 1.00 11.99 ? 532  THR   A N    1 
ATOM   8161  C  CA   . THR   A 1 532 ? 18.468 46.311  10.472 1.00 11.48 ? 532  THR   A CA   1 
ATOM   8162  C  C    . THR   A 1 532 ? 19.989 46.452  10.373 1.00 10.19 ? 532  THR   A C    1 
ATOM   8163  O  O    . THR   A 1 532 ? 20.542 46.147  9.314  1.00 14.28 ? 532  THR   A O    1 
ATOM   8164  C  CB   . THR   A 1 532 ? 17.709 47.607  10.156 1.00 13.58 ? 532  THR   A CB   1 
ATOM   8165  O  OG1  . THR   A 1 532 ? 16.316 47.353  10.344 1.00 14.05 ? 532  THR   A OG1  1 
ATOM   8166  C  CG2  . THR   A 1 532 ? 17.968 48.115  8.755  1.00 11.74 ? 532  THR   A CG2  1 
ATOM   8167  H  H    . THR   A 1 532 ? 17.712 46.387  12.330 1.00 14.39 ? 532  THR   A H    1 
ATOM   8168  H  HA   . THR   A 1 532 ? 18.192 45.674  9.794  1.00 13.78 ? 532  THR   A HA   1 
ATOM   8169  H  HB   . THR   A 1 532 ? 18.023 48.304  10.753 1.00 16.30 ? 532  THR   A HB   1 
ATOM   8170  H  HG1  . THR   A 1 532 ? 16.137 47.365  11.165 1.00 16.86 ? 532  THR   A HG1  1 
ATOM   8171  H  HG21 . THR   A 1 532 ? 17.466 48.932  8.609  1.00 14.10 ? 532  THR   A HG21 1 
ATOM   8172  H  HG22 . THR   A 1 532 ? 18.915 48.294  8.645  1.00 14.10 ? 532  THR   A HG22 1 
ATOM   8173  H  HG23 . THR   A 1 532 ? 17.689 47.445  8.111  1.00 14.10 ? 532  THR   A HG23 1 
ATOM   8174  N  N    . LEU   A 1 533 ? 20.622 46.873  11.469 1.00 12.74 ? 533  LEU   A N    1 
ATOM   8175  C  CA   . LEU   A 1 533 ? 22.105 46.981  11.483 1.00 12.76 ? 533  LEU   A CA   1 
ATOM   8176  C  C    . LEU   A 1 533 ? 22.710 45.593  11.244 1.00 12.08 ? 533  LEU   A C    1 
ATOM   8177  O  O    . LEU   A 1 533 ? 23.660 45.502  10.460 1.00 11.20 ? 533  LEU   A O    1 
ATOM   8178  C  CB   . LEU   A 1 533 ? 22.558 47.570  12.823 1.00 13.20 ? 533  LEU   A CB   1 
ATOM   8179  C  CG   . LEU   A 1 533 ? 24.069 47.720  12.996 1.00 13.37 ? 533  LEU   A CG   1 
ATOM   8180  C  CD1  . LEU   A 1 533 ? 24.597 48.877  12.164 1.00 16.93 ? 533  LEU   A CD1  1 
ATOM   8181  C  CD2  . LEU   A 1 533 ? 24.428 47.913  14.462 1.00 15.26 ? 533  LEU   A CD2  1 
ATOM   8182  H  H    . LEU   A 1 533 ? 20.233 47.098  12.202 1.00 15.30 ? 533  LEU   A H    1 
ATOM   8183  H  HA   . LEU   A 1 533 ? 22.411 47.572  10.777 1.00 15.31 ? 533  LEU   A HA   1 
ATOM   8184  H  HB2  . LEU   A 1 533 ? 22.147 48.442  12.931 1.00 15.84 ? 533  LEU   A HB2  1 
ATOM   8185  H  HB3  . LEU   A 1 533 ? 22.220 47.007  13.537 1.00 15.84 ? 533  LEU   A HB3  1 
ATOM   8186  H  HG   . LEU   A 1 533 ? 24.488 46.903  12.683 1.00 16.05 ? 533  LEU   A HG   1 
ATOM   8187  H  HD11 . LEU   A 1 533 ? 25.556 48.954  12.288 1.00 20.31 ? 533  LEU   A HD11 1 
ATOM   8188  H  HD12 . LEU   A 1 533 ? 24.405 48.716  11.227 1.00 20.31 ? 533  LEU   A HD12 1 
ATOM   8189  H  HD13 . LEU   A 1 533 ? 24.168 49.700  12.445 1.00 20.31 ? 533  LEU   A HD13 1 
ATOM   8190  H  HD21 . LEU   A 1 533 ? 25.389 48.006  14.550 1.00 18.32 ? 533  LEU   A HD21 1 
ATOM   8191  H  HD22 . LEU   A 1 533 ? 23.994 48.712  14.799 1.00 18.32 ? 533  LEU   A HD22 1 
ATOM   8192  H  HD23 . LEU   A 1 533 ? 24.130 47.144  14.972 1.00 18.32 ? 533  LEU   A HD23 1 
ATOM   8193  N  N    . GLU   A 1 534 ? 22.175 44.557  11.890 1.00 11.93 ? 534  GLU   A N    1 
ATOM   8194  C  CA   . GLU   A 1 534 ? 22.692 43.180  11.665 1.00 11.31 ? 534  GLU   A CA   1 
ATOM   8195  C  C    . GLU   A 1 534 ? 22.516 42.799  10.188 1.00 13.22 ? 534  GLU   A C    1 
ATOM   8196  O  O    . GLU   A 1 534 ? 23.428 42.186  9.624  1.00 11.56 ? 534  GLU   A O    1 
ATOM   8197  C  CB   . GLU   A 1 534 ? 22.000 42.192  12.607 1.00 11.62 ? 534  GLU   A CB   1 
ATOM   8198  C  CG   . GLU   A 1 534 ? 22.265 42.468  14.075 1.00 13.49 ? 534  GLU   A CG   1 
ATOM   8199  C  CD   . GLU   A 1 534 ? 21.419 41.656  15.040 1.00 14.23 ? 534  GLU   A CD   1 
ATOM   8200  O  OE1  . GLU   A 1 534 ? 20.439 41.037  14.588 1.00 11.74 ? 534  GLU   A OE1  1 
ATOM   8201  O  OE2  . GLU   A 1 534 ? 21.745 41.647  16.240 1.00 13.63 ? 534  GLU   A OE2  1 
ATOM   8202  H  H    . GLU   A 1 534 ? 21.527 44.614  12.452 1.00 14.32 ? 534  GLU   A H    1 
ATOM   8203  H  HA   . GLU   A 1 534 ? 23.640 43.147  11.867 1.00 13.58 ? 534  GLU   A HA   1 
ATOM   8204  H  HB2  . GLU   A 1 534 ? 21.044 42.220  12.448 1.00 13.94 ? 534  GLU   A HB2  1 
ATOM   8205  H  HB3  . GLU   A 1 534 ? 22.297 41.293  12.396 1.00 13.94 ? 534  GLU   A HB3  1 
ATOM   8206  H  HG2  . GLU   A 1 534 ? 23.201 42.293  14.260 1.00 16.19 ? 534  GLU   A HG2  1 
ATOM   8207  H  HG3  . GLU   A 1 534 ? 22.113 43.411  14.246 1.00 16.19 ? 534  GLU   A HG3  1 
ATOM   8208  N  N    . LYS   A 1 535 ? 21.374 43.160  9.597  1.00 13.07 ? 535  LYS   A N    1 
ATOM   8209  C  CA   . LYS   A 1 535 ? 21.106 42.849  8.168  1.00 13.34 ? 535  LYS   A CA   1 
ATOM   8210  C  C    . LYS   A 1 535 ? 22.168 43.506  7.276  1.00 12.91 ? 535  LYS   A C    1 
ATOM   8211  O  O    . LYS   A 1 535 ? 22.686 42.830  6.380  1.00 12.88 ? 535  LYS   A O    1 
ATOM   8212  C  CB   . LYS   A 1 535 ? 19.707 43.353  7.799  1.00 13.10 ? 535  LYS   A CB   1 
ATOM   8213  C  CG   . LYS   A 1 535 ? 19.351 43.270  6.321  1.00 13.49 ? 535  LYS   A CG   1 
ATOM   8214  C  CD   . LYS   A 1 535 ? 19.249 41.851  5.809  1.00 12.43 ? 535  LYS   A CD   1 
ATOM   8215  C  CE   . LYS   A 1 535 ? 18.696 41.776  4.402  1.00 16.77 ? 535  LYS   A CE   1 
ATOM   8216  N  NZ   . LYS   A 1 535 ? 18.733 40.396  3.865  1.00 14.40 ? 535  LYS   A NZ   1 
ATOM   8217  H  H    . LYS   A 1 535 ? 20.740 43.583  9.994  1.00 15.69 ? 535  LYS   A H    1 
ATOM   8218  H  HA   . LYS   A 1 535 ? 21.147 41.890  8.030  1.00 16.01 ? 535  LYS   A HA   1 
ATOM   8219  H  HB2  . LYS   A 1 535 ? 19.053 42.843  8.303  1.00 15.73 ? 535  LYS   A HB2  1 
ATOM   8220  H  HB3  . LYS   A 1 535 ? 19.627 44.277  8.084  1.00 15.73 ? 535  LYS   A HB3  1 
ATOM   8221  H  HG2  . LYS   A 1 535 ? 18.506 43.722  6.172  1.00 16.19 ? 535  LYS   A HG2  1 
ATOM   8222  H  HG3  . LYS   A 1 535 ? 20.022 43.746  5.806  1.00 16.19 ? 535  LYS   A HG3  1 
ATOM   8223  H  HD2  . LYS   A 1 535 ? 20.127 41.440  5.830  1.00 14.92 ? 535  LYS   A HD2  1 
ATOM   8224  H  HD3  . LYS   A 1 535 ? 18.681 41.337  6.404  1.00 14.92 ? 535  LYS   A HD3  1 
ATOM   8225  H  HE2  . LYS   A 1 535 ? 17.782 42.100  4.397  1.00 20.12 ? 535  LYS   A HE2  1 
ATOM   8226  H  HE3  . LYS   A 1 535 ? 19.208 42.362  3.822  1.00 20.12 ? 535  LYS   A HE3  1 
ATOM   8227  H  HZ1  . LYS   A 1 535 ? 18.540 40.410  2.996  1.00 17.28 ? 535  LYS   A HZ1  1 
ATOM   8228  H  HZ2  . LYS   A 1 535 ? 19.546 40.053  3.982  1.00 17.28 ? 535  LYS   A HZ2  1 
ATOM   8229  H  HZ3  . LYS   A 1 535 ? 18.135 39.894  4.293  1.00 17.28 ? 535  LYS   A HZ3  1 
ATOM   8230  N  N    . LEU   A 1 536 ? 22.470 44.780  7.531  1.00 13.95 ? 536  LEU   A N    1 
ATOM   8231  C  CA   . LEU   A 1 536 ? 23.480 45.506  6.716  1.00 12.88 ? 536  LEU   A CA   1 
ATOM   8232  C  C    . LEU   A 1 536 ? 24.847 44.835  6.891  1.00 10.98 ? 536  LEU   A C    1 
ATOM   8233  O  O    . LEU   A 1 536 ? 25.577 44.722  5.910  1.00 14.33 ? 536  LEU   A O    1 
ATOM   8234  C  CB   . LEU   A 1 536 ? 23.514 46.969  7.162  1.00 11.89 ? 536  LEU   A CB   1 
ATOM   8235  C  CG   . LEU   A 1 536 ? 22.220 47.749  6.939  1.00 13.78 ? 536  LEU   A CG   1 
ATOM   8236  C  CD1  . LEU   A 1 536 ? 22.276 49.106  7.622  1.00 17.72 ? 536  LEU   A CD1  1 
ATOM   8237  C  CD2  . LEU   A 1 536 ? 21.939 47.906  5.452  1.00 17.22 ? 536  LEU   A CD2  1 
ATOM   8238  H  H    . LEU   A 1 536 ? 22.113 45.246  8.160  1.00 16.75 ? 536  LEU   A H    1 
ATOM   8239  H  HA   . LEU   A 1 536 ? 23.248 45.476  5.775  1.00 15.46 ? 536  LEU   A HA   1 
ATOM   8240  H  HB2  . LEU   A 1 536 ? 23.734 46.999  8.106  1.00 14.28 ? 536  LEU   A HB2  1 
ATOM   8241  H  HB3  . LEU   A 1 536 ? 24.231 47.419  6.689  1.00 14.28 ? 536  LEU   A HB3  1 
ATOM   8242  H  HG   . LEU   A 1 536 ? 21.493 47.245  7.336  1.00 16.54 ? 536  LEU   A HG   1 
ATOM   8243  H  HD11 . LEU   A 1 536 ? 21.445 49.581  7.466  1.00 21.26 ? 536  LEU   A HD11 1 
ATOM   8244  H  HD12 . LEU   A 1 536 ? 22.404 48.983  8.576  1.00 21.26 ? 536  LEU   A HD12 1 
ATOM   8245  H  HD13 . LEU   A 1 536 ? 23.015 49.620  7.260  1.00 21.26 ? 536  LEU   A HD13 1 
ATOM   8246  H  HD21 . LEU   A 1 536 ? 21.115 48.403  5.329  1.00 20.67 ? 536  LEU   A HD21 1 
ATOM   8247  H  HD22 . LEU   A 1 536 ? 22.671 48.385  5.033  1.00 20.67 ? 536  LEU   A HD22 1 
ATOM   8248  H  HD23 . LEU   A 1 536 ? 21.852 47.030  5.045  1.00 20.67 ? 536  LEU   A HD23 1 
ATOM   8249  N  N    . PHE   A 1 537 ? 25.158 44.403  8.115  1.00 12.52 ? 537  PHE   A N    1 
ATOM   8250  C  CA   . PHE   A 1 537 ? 26.438 43.686  8.337  1.00 11.38 ? 537  PHE   A CA   1 
ATOM   8251  C  C    . PHE   A 1 537 ? 26.473 42.446  7.441  1.00 11.41 ? 537  PHE   A C    1 
ATOM   8252  O  O    . PHE   A 1 537 ? 27.484 42.210  6.778  1.00 14.85 ? 537  PHE   A O    1 
ATOM   8253  C  CB   . PHE   A 1 537 ? 26.600 43.307  9.812  1.00 10.66 ? 537  PHE   A CB   1 
ATOM   8254  C  CG   . PHE   A 1 537 ? 27.823 42.474  10.098 1.00 11.95 ? 537  PHE   A CG   1 
ATOM   8255  C  CD1  . PHE   A 1 537 ? 27.823 41.108  9.863  1.00 10.87 ? 537  PHE   A CD1  1 
ATOM   8256  C  CD2  . PHE   A 1 537 ? 28.980 43.058  10.585 1.00 11.79 ? 537  PHE   A CD2  1 
ATOM   8257  C  CE1  . PHE   A 1 537 ? 28.950 40.345  10.117 1.00 10.73 ? 537  PHE   A CE1  1 
ATOM   8258  C  CE2  . PHE   A 1 537 ? 30.106 42.292  10.841 1.00 13.99 ? 537  PHE   A CE2  1 
ATOM   8259  C  CZ   . PHE   A 1 537 ? 30.090 40.938  10.603 1.00 12.22 ? 537  PHE   A CZ   1 
ATOM   8260  H  H    . PHE   A 1 537 ? 24.667 44.505  8.814  1.00 15.02 ? 537  PHE   A H    1 
ATOM   8261  H  HA   . PHE   A 1 537 ? 27.180 44.267  8.107  1.00 13.65 ? 537  PHE   A HA   1 
ATOM   8262  H  HB2  . PHE   A 1 537 ? 26.641 44.118  10.343 1.00 12.79 ? 537  PHE   A HB2  1 
ATOM   8263  H  HB3  . PHE   A 1 537 ? 25.813 42.819  10.100 1.00 12.79 ? 537  PHE   A HB3  1 
ATOM   8264  H  HD1  . PHE   A 1 537 ? 27.057 40.699  9.531  1.00 13.04 ? 537  PHE   A HD1  1 
ATOM   8265  H  HD2  . PHE   A 1 537 ? 29.002 43.974  10.742 1.00 14.15 ? 537  PHE   A HD2  1 
ATOM   8266  H  HE1  . PHE   A 1 537 ? 28.935 39.429  9.958  1.00 12.88 ? 537  PHE   A HE1  1 
ATOM   8267  H  HE2  . PHE   A 1 537 ? 30.875 42.695  11.175 1.00 16.79 ? 537  PHE   A HE2  1 
ATOM   8268  H  HZ   . PHE   A 1 537 ? 30.848 40.426  10.770 1.00 14.66 ? 537  PHE   A HZ   1 
ATOM   8269  N  N    . ASN   A 1 538 ? 25.385 41.676  7.444  1.00 11.83 ? 538  ASN   A N    1 
ATOM   8270  C  CA   . ASN   A 1 538 ? 25.333 40.429  6.637  1.00 13.66 ? 538  ASN   A CA   1 
ATOM   8271  C  C    . ASN   A 1 538 ? 25.479 40.766  5.146  1.00 12.25 ? 538  ASN   A C    1 
ATOM   8272  O  O    . ASN   A 1 538 ? 26.194 40.048  4.445  1.00 15.93 ? 538  ASN   A O    1 
ATOM   8273  C  CB   . ASN   A 1 538 ? 24.049 39.643  6.921  1.00 13.86 ? 538  ASN   A CB   1 
ATOM   8274  C  CG   . ASN   A 1 538 ? 24.108 38.843  8.204  1.00 12.43 ? 538  ASN   A CG   1 
ATOM   8275  O  OD1  . ASN   A 1 538 ? 25.114 38.861  8.907  1.00 10.41 ? 538  ASN   A OD1  1 
ATOM   8276  N  ND2  . ASN   A 1 538 ? 23.032 38.142  8.517  1.00 14.64 ? 538  ASN   A ND2  1 
ATOM   8277  H  H    . ASN   A 1 538 ? 24.672 41.844  7.895  1.00 14.19 ? 538  ASN   A H    1 
ATOM   8278  H  HA   . ASN   A 1 538 ? 26.075 39.858  6.891  1.00 16.40 ? 538  ASN   A HA   1 
ATOM   8279  H  HB2  . ASN   A 1 538 ? 23.303 40.261  6.967  1.00 16.64 ? 538  ASN   A HB2  1 
ATOM   8280  H  HB3  . ASN   A 1 538 ? 23.875 39.042  6.180  1.00 16.64 ? 538  ASN   A HB3  1 
ATOM   8281  H  HD21 . ASN   A 1 538 ? 23.019 37.674  9.238  1.00 17.57 ? 538  ASN   A HD21 1 
ATOM   8282  H  HD22 . ASN   A 1 538 ? 22.345 38.154  7.999  1.00 17.57 ? 538  ASN   A HD22 1 
ATOM   8283  N  N    . LEU   A 1 539 ? 24.807 41.823  4.696  1.00 10.96 ? 539  LEU   A N    1 
ATOM   8284  C  CA   . LEU   A 1 539 ? 24.927 42.240  3.273  1.00 14.33 ? 539  LEU   A CA   1 
ATOM   8285  C  C    . LEU   A 1 539 ? 26.390 42.583  2.970  1.00 16.08 ? 539  LEU   A C    1 
ATOM   8286  O  O    . LEU   A 1 539 ? 26.896 42.132  1.933  1.00 17.40 ? 539  LEU   A O    1 
ATOM   8287  C  CB   . LEU   A 1 539 ? 24.007 43.439  3.029  1.00 13.06 ? 539  LEU   A CB   1 
ATOM   8288  C  CG   . LEU   A 1 539 ? 22.512 43.119  3.036  1.00 15.15 ? 539  LEU   A CG   1 
ATOM   8289  C  CD1  . LEU   A 1 539 ? 21.679 44.390  3.026  1.00 14.30 ? 539  LEU   A CD1  1 
ATOM   8290  C  CD2  . LEU   A 1 539 ? 22.144 42.228  1.861  1.00 14.38 ? 539  LEU   A CD2  1 
ATOM   8291  H  H    . LEU   A 1 539 ? 24.285 42.310  5.175  1.00 13.15 ? 539  LEU   A H    1 
ATOM   8292  H  HA   . LEU   A 1 539 ? 24.657 41.521  2.680  1.00 17.20 ? 539  LEU   A HA   1 
ATOM   8293  H  HB2  . LEU   A 1 539 ? 24.184 44.109  3.708  1.00 15.67 ? 539  LEU   A HB2  1 
ATOM   8294  H  HB3  . LEU   A 1 539 ? 24.235 43.836  2.174  1.00 15.67 ? 539  LEU   A HB3  1 
ATOM   8295  H  HG   . LEU   A 1 539 ? 22.316 42.639  3.856  1.00 18.19 ? 539  LEU   A HG   1 
ATOM   8296  H  HD11 . LEU   A 1 539 ? 20.737 44.160  3.031  1.00 17.17 ? 539  LEU   A HD11 1 
ATOM   8297  H  HD12 . LEU   A 1 539 ? 21.886 44.919  3.812  1.00 17.17 ? 539  LEU   A HD12 1 
ATOM   8298  H  HD13 . LEU   A 1 539 ? 21.882 44.904  2.229  1.00 17.17 ? 539  LEU   A HD13 1 
ATOM   8299  H  HD21 . LEU   A 1 539 ? 21.193 42.038  1.884  1.00 17.26 ? 539  LEU   A HD21 1 
ATOM   8300  H  HD22 . LEU   A 1 539 ? 22.362 42.680  1.031  1.00 17.26 ? 539  LEU   A HD22 1 
ATOM   8301  H  HD23 . LEU   A 1 539 ? 22.641 41.397  1.917  1.00 17.26 ? 539  LEU   A HD23 1 
ATOM   8302  N  N    . ALA   A 1 540 ? 27.037 43.325  3.869  1.00 14.49 ? 540  ALA   A N    1 
ATOM   8303  C  CA   . ALA   A 1 540 ? 28.461 43.681  3.670  1.00 15.07 ? 540  ALA   A CA   1 
ATOM   8304  C  C    . ALA   A 1 540 ? 29.319 42.414  3.685  1.00 16.47 ? 540  ALA   A C    1 
ATOM   8305  O  O    . ALA   A 1 540 ? 30.373 42.411  3.039  1.00 18.43 ? 540  ALA   A O    1 
ATOM   8306  C  CB   . ALA   A 1 540 ? 28.896 44.652  4.737  1.00 17.57 ? 540  ALA   A CB   1 
ATOM   8307  H  H    . ALA   A 1 540 ? 26.685 43.632  4.591  1.00 17.40 ? 540  ALA   A H    1 
ATOM   8308  H  HA   . ALA   A 1 540 ? 28.574 44.110  2.807  1.00 18.09 ? 540  ALA   A HA   1 
ATOM   8309  H  HB1  . ALA   A 1 540 ? 29.829 44.883  4.604  1.00 21.08 ? 540  ALA   A HB1  1 
ATOM   8310  H  HB2  . ALA   A 1 540 ? 28.354 45.455  4.685  1.00 21.08 ? 540  ALA   A HB2  1 
ATOM   8311  H  HB3  . ALA   A 1 540 ? 28.786 44.244  5.610  1.00 21.08 ? 540  ALA   A HB3  1 
ATOM   8312  N  N    . ALA   A 1 541 ? 28.869 41.378  4.397  1.00 14.98 ? 541  ALA   A N    1 
ATOM   8313  C  CA   . ALA   A 1 541 ? 29.649 40.125  4.517  1.00 16.47 ? 541  ALA   A CA   1 
ATOM   8314  C  C    . ALA   A 1 541 ? 29.405 39.215  3.313  1.00 19.27 ? 541  ALA   A C    1 
ATOM   8315  O  O    . ALA   A 1 541 ? 30.004 38.130  3.266  1.00 18.10 ? 541  ALA   A O    1 
ATOM   8316  C  CB   . ALA   A 1 541 ? 29.259 39.419  5.790  1.00 13.93 ? 541  ALA   A CB   1 
ATOM   8317  H  H    . ALA   A 1 541 ? 28.119 41.373  4.819  1.00 17.98 ? 541  ALA   A H    1 
ATOM   8318  H  HA   . ALA   A 1 541 ? 30.594 40.343  4.541  1.00 19.77 ? 541  ALA   A HA   1 
ATOM   8319  H  HB1  . ALA   A 1 541 ? 29.767 38.597  5.873  1.00 16.71 ? 541  ALA   A HB1  1 
ATOM   8320  H  HB2  . ALA   A 1 541 ? 29.446 39.993  6.549  1.00 16.71 ? 541  ALA   A HB2  1 
ATOM   8321  H  HB3  . ALA   A 1 541 ? 28.312 39.212  5.768  1.00 16.71 ? 541  ALA   A HB3  1 
ATOM   8322  N  N    . GLY   A 1 542 ? 28.539 39.636  2.393  1.00 16.02 ? 542  GLY   A N    1 
ATOM   8323  C  CA   . GLY   A 1 542 ? 28.214 38.789  1.264  1.00 19.63 ? 542  GLY   A CA   1 
ATOM   8324  C  C    . GLY   A 1 542 ? 27.099 37.798  1.505  1.00 19.16 ? 542  GLY   A C    1 
ATOM   8325  O  O    . GLY   A 1 542 ? 26.944 36.857  0.720  1.00 22.21 ? 542  GLY   A O    1 
ATOM   8326  H  H    . GLY   A 1 542 ? 28.138 40.397  2.408  1.00 19.23 ? 542  GLY   A H    1 
ATOM   8327  H  HA2  . GLY   A 1 542 ? 27.970 39.353  0.514  1.00 23.56 ? 542  GLY   A HA2  1 
ATOM   8328  H  HA3  . GLY   A 1 542 ? 29.011 38.301  1.004  1.00 23.56 ? 542  GLY   A HA3  1 
ATOM   8329  N  N    . ILE   A 1 543 ? 26.314 38.015  2.562  1.00 15.75 ? 543  ILE   A N    1 
ATOM   8330  C  CA   . ILE   A 1 543 ? 25.127 37.142  2.811  1.00 16.22 ? 543  ILE   A CA   1 
ATOM   8331  C  C    . ILE   A 1 543 ? 23.919 37.769  2.107  1.00 19.26 ? 543  ILE   A C    1 
ATOM   8332  O  O    . ILE   A 1 543 ? 23.334 38.707  2.666  1.00 21.21 ? 543  ILE   A O    1 
ATOM   8333  C  CB   . ILE   A 1 543 ? 24.883 36.927  4.316  1.00 13.82 ? 543  ILE   A CB   1 
ATOM   8334  C  CG1  . ILE   A 1 543 ? 26.134 36.391  5.015  1.00 14.11 ? 543  ILE   A CG1  1 
ATOM   8335  C  CG2  . ILE   A 1 543 ? 23.682 36.020  4.538  1.00 17.34 ? 543  ILE   A CG2  1 
ATOM   8336  C  CD1  . ILE   A 1 543 ? 26.577 35.038  4.518  1.00 19.23 ? 543  ILE   A CD1  1 
ATOM   8337  H  H    . ILE   A 1 543 ? 26.434 38.640  3.140  1.00 18.91 ? 543  ILE   A H    1 
ATOM   8338  H  HA   . ILE   A 1 543 ? 25.285 36.257  2.447  1.00 19.47 ? 543  ILE   A HA   1 
ATOM   8339  H  HB   . ILE   A 1 543 ? 24.684 37.788  4.716  1.00 16.59 ? 543  ILE   A HB   1 
ATOM   8340  H  HG12 . ILE   A 1 543 ? 26.859 37.024  4.893  1.00 16.94 ? 543  ILE   A HG12 1 
ATOM   8341  H  HG13 . ILE   A 1 543 ? 25.963 36.336  5.968  1.00 16.94 ? 543  ILE   A HG13 1 
ATOM   8342  H  HG21 . ILE   A 1 543 ? 23.542 35.895  5.490  1.00 20.82 ? 543  ILE   A HG21 1 
ATOM   8343  H  HG22 . ILE   A 1 543 ? 22.893 36.426  4.146  1.00 20.82 ? 543  ILE   A HG22 1 
ATOM   8344  H  HG23 . ILE   A 1 543 ? 23.844 35.160  4.120  1.00 20.82 ? 543  ILE   A HG23 1 
ATOM   8345  H  HD11 . ILE   A 1 543 ? 27.371 34.760  5.001  1.00 23.08 ? 543  ILE   A HD11 1 
ATOM   8346  H  HD12 . ILE   A 1 543 ? 25.868 34.392  4.662  1.00 23.08 ? 543  ILE   A HD12 1 
ATOM   8347  H  HD13 . ILE   A 1 543 ? 26.778 35.091  3.570  1.00 23.08 ? 543  ILE   A HD13 1 
ATOM   8348  N  N    . ASP   A 1 544 ? 23.573 37.241  0.936  1.00 17.10 ? 544  ASP   A N    1 
ATOM   8349  C  CA   . ASP   A 1 544 ? 22.450 37.775  0.129  1.00 23.38 ? 544  ASP   A CA   1 
ATOM   8350  C  C    . ASP   A 1 544 ? 21.098 37.406  0.740  1.00 20.95 ? 544  ASP   A C    1 
ATOM   8351  O  O    . ASP   A 1 544 ? 21.037 36.425  1.496  1.00 15.74 ? 544  ASP   A O    1 
ATOM   8352  C  CB   . ASP   A 1 544 ? 22.518 37.201  -1.287 1.00 25.05 ? 544  ASP   A CB   1 
ATOM   8353  C  CG   . ASP   A 1 544 ? 21.624 37.900  -2.291 1.00 30.65 ? 544  ASP   A CG   1 
ATOM   8354  O  OD1  . ASP   A 1 544 ? 22.058 38.928  -2.839 1.00 35.19 ? 544  ASP   A OD1  1 
ATOM   8355  O  OD2  . ASP   A 1 544 ? 20.509 37.399  -2.524 1.00 33.46 ? 544  ASP   A OD2  1 
ATOM   8356  H  H    . ASP   A 1 544 ? 23.973 36.568  0.580  1.00 20.52 ? 544  ASP   A H    1 
ATOM   8357  H  HA   . ASP   A 1 544 ? 22.531 38.741  0.111  1.00 28.07 ? 544  ASP   A HA   1 
ATOM   8358  H  HB2  . ASP   A 1 544 ? 23.435 37.248  -1.599 1.00 30.06 ? 544  ASP   A HB2  1 
ATOM   8359  H  HB3  . ASP   A 1 544 ? 22.277 36.262  -1.255 1.00 30.06 ? 544  ASP   A HB3  1 
ATOM   8360  N  N    . SER   A 1 545 ? 20.060 38.172  0.399  1.00 18.18 ? 545  SER   A N    1 
ATOM   8361  C  CA   . SER   A 1 545 ? 18.689 37.840  0.855  1.00 18.86 ? 545  SER   A CA   1 
ATOM   8362  C  C    . SER   A 1 545 ? 18.275 36.485  0.265  1.00 13.36 ? 545  SER   A C    1 
ATOM   8363  O  O    . SER   A 1 545 ? 17.343 35.880  0.808  1.00 15.22 ? 545  SER   A O    1 
ATOM   8364  C  CB   . SER   A 1 545 ? 17.727 38.940  0.482  1.00 18.21 ? 545  SER   A CB   1 
ATOM   8365  O  OG   . SER   A 1 545 ? 18.124 40.181  1.044  1.00 20.75 ? 545  SER   A OG   1 
ATOM   8366  H  H    . SER   A 1 545 ? 20.117 38.879  -0.087 1.00 21.82 ? 545  SER   A H    1 
ATOM   8367  H  HA   . SER   A 1 545 ? 18.671 37.767  1.822  1.00 22.63 ? 545  SER   A HA   1 
ATOM   8368  H  HB2  . SER   A 1 545 ? 17.681 39.019  -0.484 1.00 21.85 ? 545  SER   A HB2  1 
ATOM   8369  H  HB3  . SER   A 1 545 ? 16.836 38.712  0.791  1.00 21.85 ? 545  SER   A HB3  1 
ATOM   8370  H  HG   . SER   A 1 545 ? 17.814 40.810  0.582  1.00 24.90 ? 545  SER   A HG   1 
ATOM   8371  N  N    . SER   A 1 546 ? 18.942 36.032  -0.805 1.00 15.23 ? 546  SER   A N    1 
ATOM   8372  C  CA   . SER   A 1 546 ? 18.627 34.704  -1.316 1.00 18.65 ? 546  SER   A CA   1 
ATOM   8373  C  C    . SER   A 1 546 ? 18.912 33.610  -0.299 1.00 16.08 ? 546  SER   A C    1 
ATOM   8374  O  O    . SER   A 1 546 ? 18.452 32.477  -0.485 1.00 14.35 ? 546  SER   A O    1 
ATOM   8375  C  CB   . SER   A 1 546 ? 19.408 34.414  -2.605 1.00 19.76 ? 546  SER   A CB   1 
ATOM   8376  O  OG   . SER   A 1 546 ? 20.806 34.486  -2.383 1.00 23.91 ? 546  SER   A OG   1 
ATOM   8377  H  H    . SER   A 1 546 ? 19.554 36.461  -1.230 1.00 18.28 ? 546  SER   A H    1 
ATOM   8378  H  HA   . SER   A 1 546 ? 17.675 34.701  -1.503 1.00 22.38 ? 546  SER   A HA   1 
ATOM   8379  H  HB2  . SER   A 1 546 ? 19.175 33.532  -2.936 1.00 23.71 ? 546  SER   A HB2  1 
ATOM   8380  H  HB3  . SER   A 1 546 ? 19.153 35.051  -3.291 1.00 23.71 ? 546  SER   A HB3  1 
ATOM   8381  H  HG   . SER   A 1 546 ? 21.120 33.710  -2.316 1.00 28.70 ? 546  SER   A HG   1 
ATOM   8382  N  N    . GLN   A 1 547 ? 19.652 33.914  0.763  1.00 14.30 ? 547  GLN   A N    1 
ATOM   8383  C  CA   . GLN   A 1 547 ? 19.893 32.949  1.826  1.00 15.47 ? 547  GLN   A CA   1 
ATOM   8384  C  C    . GLN   A 1 547 ? 18.764 32.912  2.852  1.00 13.72 ? 547  GLN   A C    1 
ATOM   8385  O  O    . GLN   A 1 547 ? 18.852 32.150  3.822  1.00 13.29 ? 547  GLN   A O    1 
ATOM   8386  C  CB   . GLN   A 1 547 ? 21.240 33.251  2.494  1.00 15.25 ? 547  GLN   A CB   1 
ATOM   8387  C  CG   . GLN   A 1 547 ? 22.440 33.030  1.556  1.00 15.84 ? 547  GLN   A CG   1 
ATOM   8388  C  CD   . GLN   A 1 547 ? 23.745 32.711  2.288  1.00 16.77 ? 547  GLN   A CD   1 
ATOM   8389  O  OE1  . GLN   A 1 547 ? 23.754 32.001  3.293  1.00 18.17 ? 547  GLN   A OE1  1 
ATOM   8390  N  NE2  . GLN   A 1 547 ? 24.853 33.231  1.771  1.00 19.72 ? 547  GLN   A NE2  1 
ATOM   8391  H  H    . GLN   A 1 547 ? 20.025 34.679  0.886  1.00 17.16 ? 547  GLN   A H    1 
ATOM   8392  H  HA   . GLN   A 1 547 ? 19.922 32.066  1.427  1.00 18.56 ? 547  GLN   A HA   1 
ATOM   8393  H  HB2  . GLN   A 1 547 ? 21.243 34.170  2.803  1.00 18.30 ? 547  GLN   A HB2  1 
ATOM   8394  H  HB3  . GLN   A 1 547 ? 21.340 32.688  3.277  1.00 18.30 ? 547  GLN   A HB3  1 
ATOM   8395  H  HG2  . GLN   A 1 547 ? 22.234 32.303  0.947  1.00 19.01 ? 547  GLN   A HG2  1 
ATOM   8396  H  HG3  . GLN   A 1 547 ? 22.568 33.825  1.016  1.00 19.01 ? 547  GLN   A HG3  1 
ATOM   8397  H  HE21 . GLN   A 1 547 ? 24.809 33.723  1.067  1.00 23.67 ? 547  GLN   A HE21 1 
ATOM   8398  H  HE22 . GLN   A 1 547 ? 25.614 33.075  2.140  1.00 23.67 ? 547  GLN   A HE22 1 
ATOM   8399  N  N    . ASP   A 1 548 ? 17.715 33.703  2.618  1.00 12.50 ? 548  ASP   A N    1 
ATOM   8400  C  CA   . ASP   A 1 548 ? 16.502 33.641  3.452  1.00 12.19 ? 548  ASP   A CA   1 
ATOM   8401  C  C    . ASP   A 1 548 ? 15.603 32.529  2.894  1.00 14.33 ? 548  ASP   A C    1 
ATOM   8402  O  O    . ASP   A 1 548 ? 14.817 32.783  2.008  1.00 13.79 ? 548  ASP   A O    1 
ATOM   8403  C  CB   . ASP   A 1 548 ? 15.756 34.966  3.495  1.00 11.47 ? 548  ASP   A CB   1 
ATOM   8404  C  CG   . ASP   A 1 548 ? 16.502 36.069  4.224  1.00 12.66 ? 548  ASP   A CG   1 
ATOM   8405  O  OD1  . ASP   A 1 548 ? 17.492 35.756  4.891  1.00 11.29 ? 548  ASP   A OD1  1 
ATOM   8406  O  OD2  . ASP   A 1 548 ? 16.083 37.222  4.113  1.00 13.20 ? 548  ASP   A OD2  1 
ATOM   8407  H  H    . ASP   A 1 548 ? 17.682 34.283  1.983  1.00 15.00 ? 548  ASP   A H    1 
ATOM   8408  H  HA   . ASP   A 1 548 ? 16.759 33.449  4.368  1.00 14.63 ? 548  ASP   A HA   1 
ATOM   8409  H  HB2  . ASP   A 1 548 ? 15.576 35.255  2.587  1.00 13.76 ? 548  ASP   A HB2  1 
ATOM   8410  H  HB3  . ASP   A 1 548 ? 14.897 34.830  3.925  1.00 13.76 ? 548  ASP   A HB3  1 
ATOM   8411  N  N    . THR   A 1 549 ? 15.751 31.342  3.456  1.00 13.05 ? 549  THR   A N    1 
ATOM   8412  C  CA   . THR   A 1 549 ? 14.998 30.213  2.906  1.00 13.65 ? 549  THR   A CA   1 
ATOM   8413  C  C    . THR   A 1 549 ? 14.796 29.135  3.954  1.00 11.64 ? 549  THR   A C    1 
ATOM   8414  O  O    . THR   A 1 549 ? 15.218 29.333  5.076  1.00 10.11 ? 549  THR   A O    1 
ATOM   8415  C  CB   . THR   A 1 549 ? 15.786 29.585  1.762  1.00 20.75 ? 549  THR   A CB   1 
ATOM   8416  O  OG1  . THR   A 1 549 ? 14.907 28.686  1.076  1.00 28.84 ? 549  THR   A OG1  1 
ATOM   8417  C  CG2  . THR   A 1 549 ? 17.030 28.874  2.244  1.00 19.89 ? 549  THR   A CG2  1 
ATOM   8418  H  H    . THR   A 1 549 ? 16.258 31.165  4.128  1.00 15.66 ? 549  THR   A H    1 
ATOM   8419  H  HA   . THR   A 1 549 ? 14.140 30.549  2.604  1.00 16.38 ? 549  THR   A HA   1 
ATOM   8420  H  HB   . THR   A 1 549 ? 16.098 30.281  1.163  1.00 24.90 ? 549  THR   A HB   1 
ATOM   8421  H  HG1  . THR   A 1 549 ? 15.156 27.895  1.208  1.00 34.61 ? 549  THR   A HG1  1 
ATOM   8422  H  HG21 . THR   A 1 549 ? 17.498 28.491  1.486  1.00 23.87 ? 549  THR   A HG21 1 
ATOM   8423  H  HG22 . THR   A 1 549 ? 17.610 29.507  2.696  1.00 23.87 ? 549  THR   A HG22 1 
ATOM   8424  H  HG23 . THR   A 1 549 ? 16.781 28.167  2.860  1.00 23.87 ? 549  THR   A HG23 1 
ATOM   8425  N  N    . LEU   A 1 550 ? 14.101 28.077  3.549  1.00 11.22 ? 550  LEU   A N    1 
ATOM   8426  C  CA   . LEU   A 1 550 ? 13.922 26.891  4.413  1.00 11.43 ? 550  LEU   A CA   1 
ATOM   8427  C  C    . LEU   A 1 550 ? 14.289 25.678  3.566  1.00 11.34 ? 550  LEU   A C    1 
ATOM   8428  O  O    . LEU   A 1 550 ? 14.252 25.748  2.350  1.00 12.88 ? 550  LEU   A O    1 
ATOM   8429  C  CB   . LEU   A 1 550 ? 12.482 26.747  4.916  1.00 14.35 ? 550  LEU   A CB   1 
ATOM   8430  C  CG   . LEU   A 1 550 ? 12.065 27.698  6.035  1.00 11.04 ? 550  LEU   A CG   1 
ATOM   8431  C  CD1  . LEU   A 1 550 ? 10.603 27.506  6.392  1.00 13.31 ? 550  LEU   A CD1  1 
ATOM   8432  C  CD2  . LEU   A 1 550 ? 12.939 27.509  7.261  1.00 12.62 ? 550  LEU   A CD2  1 
ATOM   8433  H  H    . LEU   A 1 550 ? 13.722 28.017  2.779  1.00 13.46 ? 550  LEU   A H    1 
ATOM   8434  H  HA   . LEU   A 1 550 ? 14.482 26.976  5.200  1.00 13.71 ? 550  LEU   A HA   1 
ATOM   8435  H  HB2  . LEU   A 1 550 ? 11.882 26.877  4.165  1.00 17.22 ? 550  LEU   A HB2  1 
ATOM   8436  H  HB3  . LEU   A 1 550 ? 12.356 25.837  5.226  1.00 17.22 ? 550  LEU   A HB3  1 
ATOM   8437  H  HG   . LEU   A 1 550 ? 12.184 28.605  5.713  1.00 13.25 ? 550  LEU   A HG   1 
ATOM   8438  H  HD11 . LEU   A 1 550 ? 10.360 28.119  7.103  1.00 15.98 ? 550  LEU   A HD11 1 
ATOM   8439  H  HD12 . LEU   A 1 550 ? 10.053 27.682  5.612  1.00 15.98 ? 550  LEU   A HD12 1 
ATOM   8440  H  HD13 . LEU   A 1 550 ? 10.459 26.594  6.689  1.00 15.98 ? 550  LEU   A HD13 1 
ATOM   8441  H  HD21 . LEU   A 1 550 ? 12.657 28.122  7.958  1.00 15.15 ? 550  LEU   A HD21 1 
ATOM   8442  H  HD22 . LEU   A 1 550 ? 12.856 26.597  7.580  1.00 15.15 ? 550  LEU   A HD22 1 
ATOM   8443  H  HD23 . LEU   A 1 550 ? 13.864 27.687  7.030  1.00 15.15 ? 550  LEU   A HD23 1 
ATOM   8444  N  N    . PRO   A 1 551 ? 14.745 24.602  4.205  1.00 9.96  ? 551  PRO   A N    1 
ATOM   8445  C  CA   . PRO   A 1 551 ? 14.980 23.367  3.448  1.00 13.45 ? 551  PRO   A CA   1 
ATOM   8446  C  C    . PRO   A 1 551 ? 13.763 22.983  2.622  1.00 13.70 ? 551  PRO   A C    1 
ATOM   8447  O  O    . PRO   A 1 551 ? 12.617 23.207  3.025  1.00 10.87 ? 551  PRO   A O    1 
ATOM   8448  C  CB   . PRO   A 1 551 ? 15.271 22.334  4.542  1.00 14.05 ? 551  PRO   A CB   1 
ATOM   8449  C  CG   . PRO   A 1 551 ? 15.846 23.142  5.666  1.00 12.08 ? 551  PRO   A CG   1 
ATOM   8450  C  CD   . PRO   A 1 551 ? 15.124 24.463  5.625  1.00 10.70 ? 551  PRO   A CD   1 
ATOM   8451  H  HA   . PRO   A 1 551 ? 15.702 23.447  2.805  1.00 16.14 ? 551  PRO   A HA   1 
ATOM   8452  H  HB2  . PRO   A 1 551 ? 14.464 21.870  4.815  1.00 16.87 ? 551  PRO   A HB2  1 
ATOM   8453  H  HB3  . PRO   A 1 551 ? 15.896 21.659  4.235  1.00 16.87 ? 551  PRO   A HB3  1 
ATOM   8454  H  HG2  . PRO   A 1 551 ? 15.713 22.698  6.518  1.00 14.49 ? 551  PRO   A HG2  1 
ATOM   8455  H  HG3  . PRO   A 1 551 ? 16.802 23.263  5.555  1.00 14.49 ? 551  PRO   A HG3  1 
ATOM   8456  H  HD2  . PRO   A 1 551 ? 14.346 24.463  6.204  1.00 12.85 ? 551  PRO   A HD2  1 
ATOM   8457  H  HD3  . PRO   A 1 551 ? 15.695 25.192  5.916  1.00 12.85 ? 551  PRO   A HD3  1 
ATOM   8458  N  N    . LYS   A 1 552 ? 14.020 22.397  1.450  1.00 14.32 ? 552  LYS   A N    1 
ATOM   8459  C  CA   . LYS   A 1 552 ? 12.907 21.994  0.548  1.00 15.55 ? 552  LYS   A CA   1 
ATOM   8460  C  C    . LYS   A 1 552 ? 11.902 21.132  1.320  1.00 13.47 ? 552  LYS   A C    1 
ATOM   8461  O  O    . LYS   A 1 552 ? 10.694 21.290  1.087  1.00 12.39 ? 552  LYS   A O    1 
ATOM   8462  C  CB   . LYS   A 1 552 ? 13.454 21.246  -0.671 1.00 18.37 ? 552  LYS   A CB   1 
ATOM   8463  C  CG   . LYS   A 1 552 ? 12.401 20.732  -1.644 1.00 27.02 ? 552  LYS   A CG   1 
ATOM   8464  C  CD   . LYS   A 1 552 ? 12.971 19.829  -2.715 1.00 36.47 ? 552  LYS   A CD   1 
ATOM   8465  C  CE   . LYS   A 1 552 ? 12.831 20.402  -4.109 1.00 43.39 ? 552  LYS   A CE   1 
ATOM   8466  N  NZ   . LYS   A 1 552 ? 12.980 19.357  -5.149 1.00 47.39 ? 552  LYS   A NZ   1 
ATOM   8467  H  H    . LYS   A 1 552 ? 14.808 22.223  1.154  1.00 17.19 ? 552  LYS   A H    1 
ATOM   8468  H  HA   . LYS   A 1 552 ? 12.450 22.788  0.229  1.00 18.67 ? 552  LYS   A HA   1 
ATOM   8469  H  HB2  . LYS   A 1 552 ? 14.056 21.836  -1.151 1.00 22.05 ? 552  LYS   A HB2  1 
ATOM   8470  H  HB3  . LYS   A 1 552 ? 13.981 20.493  -0.361 1.00 22.05 ? 552  LYS   A HB3  1 
ATOM   8471  H  HG2  . LYS   A 1 552 ? 11.721 20.249  -1.150 1.00 32.43 ? 552  LYS   A HG2  1 
ATOM   8472  H  HG3  . LYS   A 1 552 ? 11.962 21.487  -2.066 1.00 32.43 ? 552  LYS   A HG3  1 
ATOM   8473  H  HD2  . LYS   A 1 552 ? 13.909 19.668  -2.530 1.00 43.77 ? 552  LYS   A HD2  1 
ATOM   8474  H  HD3  . LYS   A 1 552 ? 12.523 18.969  -2.678 1.00 43.77 ? 552  LYS   A HD3  1 
ATOM   8475  H  HE2  . LYS   A 1 552 ? 11.964 20.827  -4.199 1.00 52.07 ? 552  LYS   A HE2  1 
ATOM   8476  H  HE3  . LYS   A 1 552 ? 13.500 21.091  -4.244 1.00 52.07 ? 552  LYS   A HE3  1 
ATOM   8477  H  HZ1  . LYS   A 1 552 ? 12.893 19.725  -5.955 1.00 56.87 ? 552  LYS   A HZ1  1 
ATOM   8478  H  HZ2  . LYS   A 1 552 ? 13.784 18.982  -5.080 1.00 56.87 ? 552  LYS   A HZ2  1 
ATOM   8479  H  HZ3  . LYS   A 1 552 ? 12.353 18.736  -5.038 1.00 56.87 ? 552  LYS   A HZ3  1 
ATOM   8480  N  N    . ARG   A 1 553 ? 12.389 20.255  2.204  1.00 13.40 ? 553  ARG   A N    1 
ATOM   8481  C  CA   . ARG   A 1 553 ? 11.480 19.377  2.939  1.00 16.33 ? 553  ARG   A CA   1 
ATOM   8482  C  C    . ARG   A 1 553 ? 10.387 20.171  3.648  1.00 14.53 ? 553  ARG   A C    1 
ATOM   8483  O  O    . ARG   A 1 553 ? 9.217  19.770  3.658  1.00 11.00 ? 553  ARG   A O    1 
ATOM   8484  C  CB   . ARG   A 1 553 ? 12.272 18.552  3.954  1.00 14.85 ? 553  ARG   A CB   1 
ATOM   8485  C  CG   . ARG   A 1 553 ? 11.421 17.866  5.009  1.00 14.70 ? 553  ARG   A CG   1 
ATOM   8486  C  CD   . ARG   A 1 553 ? 12.247 16.845  5.783  1.00 15.74 ? 553  ARG   A CD   1 
ATOM   8487  N  NE   . ARG   A 1 553 ? 12.685 15.731  4.948  1.00 14.99 ? 553  ARG   A NE   1 
ATOM   8488  C  CZ   . ARG   A 1 553 ? 13.716 14.947  5.233  1.00 14.60 ? 553  ARG   A CZ   1 
ATOM   8489  N  NH1  . ARG   A 1 553 ? 14.412 15.101  6.351  1.00 10.30 ? 553  ARG   A NH1  1 
ATOM   8490  N  NH2  . ARG   A 1 553 ? 14.059 13.989  4.375  1.00 15.30 ? 553  ARG   A NH2  1 
ATOM   8491  H  H    . ARG   A 1 553 ? 13.223 20.155  2.388  1.00 16.08 ? 553  ARG   A H    1 
ATOM   8492  H  HA   . ARG   A 1 553 ? 11.049 18.785  2.302  1.00 19.60 ? 553  ARG   A HA   1 
ATOM   8493  H  HB2  . ARG   A 1 553 ? 12.783 17.878  3.478  1.00 17.82 ? 553  ARG   A HB2  1 
ATOM   8494  H  HB3  . ARG   A 1 553 ? 12.911 19.132  4.397  1.00 17.82 ? 553  ARG   A HB3  1 
ATOM   8495  H  HG2  . ARG   A 1 553 ? 11.059 18.527  5.620  1.00 17.64 ? 553  ARG   A HG2  1 
ATOM   8496  H  HG3  . ARG   A 1 553 ? 10.666 17.426  4.587  1.00 17.64 ? 553  ARG   A HG3  1 
ATOM   8497  H  HD2  . ARG   A 1 553 ? 13.023 17.284  6.165  1.00 18.89 ? 553  ARG   A HD2  1 
ATOM   8498  H  HD3  . ARG   A 1 553 ? 11.722 16.503  6.524  1.00 18.89 ? 553  ARG   A HD3  1 
ATOM   8499  H  HE   . ARG   A 1 553 ? 12.247 15.573  4.225  1.00 18.00 ? 553  ARG   A HE   1 
ATOM   8500  H  HH11 . ARG   A 1 553 ? 14.198 15.719  6.909  1.00 12.37 ? 553  ARG   A HH11 1 
ATOM   8501  H  HH12 . ARG   A 1 553 ? 15.077 14.583  6.518  1.00 12.37 ? 553  ARG   A HH12 1 
ATOM   8502  H  HH21 . ARG   A 1 553 ? 13.614 13.885  3.647  1.00 18.37 ? 553  ARG   A HH21 1 
ATOM   8503  H  HH22 . ARG   A 1 553 ? 14.726 13.474  4.549  1.00 18.37 ? 553  ARG   A HH22 1 
ATOM   8504  N  N    . LEU   A 1 554 ? 10.755 21.302  4.251  1.00 13.94 ? 554  LEU   A N    1 
ATOM   8505  C  CA   . LEU   A 1 554 ? 9.804  22.078  5.033  1.00 11.59 ? 554  LEU   A CA   1 
ATOM   8506  C  C    . LEU   A 1 554 ? 8.897  22.935  4.167  1.00 12.78 ? 554  LEU   A C    1 
ATOM   8507  O  O    . LEU   A 1 554 ? 7.872  23.425  4.658  1.00 12.70 ? 554  LEU   A O    1 
ATOM   8508  C  CB   . LEU   A 1 554 ? 10.557 22.956  6.035  1.00 9.72  ? 554  LEU   A CB   1 
ATOM   8509  C  CG   . LEU   A 1 554 ? 11.502 22.156  6.938  1.00 12.36 ? 554  LEU   A CG   1 
ATOM   8510  C  CD1  . LEU   A 1 554 ? 12.188 23.040  7.976  1.00 12.03 ? 554  LEU   A CD1  1 
ATOM   8511  C  CD2  . LEU   A 1 554 ? 10.753 21.003  7.622  1.00 12.51 ? 554  LEU   A CD2  1 
ATOM   8512  H  H    . LEU   A 1 554 ? 11.548 21.633  4.218  1.00 16.73 ? 554  LEU   A H    1 
ATOM   8513  H  HA   . LEU   A 1 554 ? 9.234  21.450  5.503  1.00 13.92 ? 554  LEU   A HA   1 
ATOM   8514  H  HB2  . LEU   A 1 554 ? 11.068 23.625  5.552  1.00 11.67 ? 554  LEU   A HB2  1 
ATOM   8515  H  HB3  . LEU   A 1 554 ? 9.916  23.432  6.586  1.00 11.67 ? 554  LEU   A HB3  1 
ATOM   8516  H  HG   . LEU   A 1 554 ? 12.195 21.785  6.370  1.00 14.83 ? 554  LEU   A HG   1 
ATOM   8517  H  HD11 . LEU   A 1 554 ? 12.775 22.498  8.526  1.00 14.43 ? 554  LEU   A HD11 1 
ATOM   8518  H  HD12 . LEU   A 1 554 ? 12.708 23.724  7.526  1.00 14.43 ? 554  LEU   A HD12 1 
ATOM   8519  H  HD13 . LEU   A 1 554 ? 11.518 23.460  8.537  1.00 14.43 ? 554  LEU   A HD13 1 
ATOM   8520  H  HD21 . LEU   A 1 554 ? 11.366 20.509  8.188  1.00 15.02 ? 554  LEU   A HD21 1 
ATOM   8521  H  HD22 . LEU   A 1 554 ? 10.032 21.361  8.163  1.00 15.02 ? 554  LEU   A HD22 1 
ATOM   8522  H  HD23 . LEU   A 1 554 ? 10.387 20.409  6.948  1.00 15.02 ? 554  LEU   A HD23 1 
ATOM   8523  N  N    . LEU   A 1 555 ? 9.247  23.127  2.896  1.00 11.33 ? 555  LEU   A N    1 
ATOM   8524  C  CA   . LEU   A 1 555 ? 8.402  23.867  1.970  1.00 13.66 ? 555  LEU   A CA   1 
ATOM   8525  C  C    . LEU   A 1 555 ? 7.539  22.969  1.088  1.00 15.22 ? 555  LEU   A C    1 
ATOM   8526  O  O    . LEU   A 1 555 ? 6.524  23.443  0.564  1.00 15.45 ? 555  LEU   A O    1 
ATOM   8527  C  CB   . LEU   A 1 555 ? 9.266  24.761  1.070  1.00 13.85 ? 555  LEU   A CB   1 
ATOM   8528  C  CG   . LEU   A 1 555 ? 10.214 25.768  1.729  1.00 12.29 ? 555  LEU   A CG   1 
ATOM   8529  C  CD1  . LEU   A 1 555 ? 11.108 26.416  0.682  1.00 17.73 ? 555  LEU   A CD1  1 
ATOM   8530  C  CD2  . LEU   A 1 555 ? 9.447  26.838  2.500  1.00 13.00 ? 555  LEU   A CD2  1 
ATOM   8531  H  H    . LEU   A 1 555 ? 9.977  22.833  2.551  1.00 13.60 ? 555  LEU   A H    1 
ATOM   8532  H  HA   . LEU   A 1 555 ? 7.804  24.400  2.517  1.00 16.40 ? 555  LEU   A HA   1 
ATOM   8533  H  HB2  . LEU   A 1 555 ? 9.799  24.181  0.504  1.00 16.62 ? 555  LEU   A HB2  1 
ATOM   8534  H  HB3  . LEU   A 1 555 ? 8.669  25.256  0.487  1.00 16.62 ? 555  LEU   A HB3  1 
ATOM   8535  H  HG   . LEU   A 1 555 ? 10.766 25.283  2.362  1.00 14.75 ? 555  LEU   A HG   1 
ATOM   8536  H  HD11 . LEU   A 1 555 ? 11.703 27.051  1.112  1.00 21.28 ? 555  LEU   A HD11 1 
ATOM   8537  H  HD12 . LEU   A 1 555 ? 11.633 25.733  0.236  1.00 21.28 ? 555  LEU   A HD12 1 
ATOM   8538  H  HD13 . LEU   A 1 555 ? 10.559 26.879  0.029  1.00 21.28 ? 555  LEU   A HD13 1 
ATOM   8539  H  HD21 . LEU   A 1 555 ? 10.074 27.458  2.904  1.00 15.61 ? 555  LEU   A HD21 1 
ATOM   8540  H  HD22 . LEU   A 1 555 ? 8.863  27.319  1.893  1.00 15.61 ? 555  LEU   A HD22 1 
ATOM   8541  H  HD23 . LEU   A 1 555 ? 8.915  26.418  3.194  1.00 15.61 ? 555  LEU   A HD23 1 
ATOM   8542  N  N    . GLU   A 1 556 ? 7.954  21.713  0.878  1.00 14.30 ? 556  GLU   A N    1 
ATOM   8543  C  CA   . GLU   A 1 556 ? 7.225  20.860  -0.105 1.00 13.96 ? 556  GLU   A CA   1 
ATOM   8544  C  C    . GLU   A 1 556 ? 6.682  19.557  0.495  1.00 14.31 ? 556  GLU   A C    1 
ATOM   8545  O  O    . GLU   A 1 556 ? 5.722  19.021  -0.084 1.00 14.92 ? 556  GLU   A O    1 
ATOM   8546  C  CB   . GLU   A 1 556 ? 8.148  20.529  -1.280 1.00 16.61 ? 556  GLU   A CB   1 
ATOM   8547  C  CG   . GLU   A 1 556 ? 8.801  21.753  -1.892 1.00 22.86 ? 556  GLU   A CG   1 
ATOM   8548  C  CD   . GLU   A 1 556 ? 9.531  21.486  -3.197 1.00 31.01 ? 556  GLU   A CD   1 
ATOM   8549  O  OE1  . GLU   A 1 556 ? 9.614  20.308  -3.594 1.00 34.33 ? 556  GLU   A OE1  1 
ATOM   8550  O  OE2  . GLU   A 1 556 ? 10.015 22.456  -3.809 1.00 31.88 ? 556  GLU   A OE2  1 
ATOM   8551  H  H    . GLU   A 1 556 ? 8.623  21.340  1.269  1.00 17.17 ? 556  GLU   A H    1 
ATOM   8552  H  HA   . GLU   A 1 556 ? 6.457  21.374  -0.399 1.00 16.76 ? 556  GLU   A HA   1 
ATOM   8553  H  HB2  . GLU   A 1 556 ? 8.839  19.918  -0.979 1.00 19.94 ? 556  GLU   A HB2  1 
ATOM   8554  H  HB3  . GLU   A 1 556 ? 7.638  20.066  -1.963 1.00 19.94 ? 556  GLU   A HB3  1 
ATOM   8555  H  HG2  . GLU   A 1 556 ? 8.120  22.427  -2.046 1.00 27.44 ? 556  GLU   A HG2  1 
ATOM   8556  H  HG3  . GLU   A 1 556 ? 9.429  22.125  -1.253 1.00 27.44 ? 556  GLU   A HG3  1 
ATOM   8557  N  N    . GLU   A 1 557 ? 7.276  19.042  1.573  1.00 15.70 ? 557  GLU   A N    1 
ATOM   8558  C  CA   . GLU   A 1 557 ? 6.831  17.727  2.112  1.00 15.21 ? 557  GLU   A CA   1 
ATOM   8559  C  C    . GLU   A 1 557 ? 5.821  17.947  3.241  1.00 15.16 ? 557  GLU   A C    1 
ATOM   8560  O  O    . GLU   A 1 557 ? 6.212  18.415  4.313  1.00 13.39 ? 557  GLU   A O    1 
ATOM   8561  C  CB   . GLU   A 1 557 ? 8.022  16.891  2.587  1.00 19.18 ? 557  GLU   A CB   1 
ATOM   8562  C  CG   . GLU   A 1 557 ? 8.954  16.463  1.472  1.00 22.63 ? 557  GLU   A CG   1 
ATOM   8563  C  CD   . GLU   A 1 557 ? 10.192 15.721  1.946  1.00 29.70 ? 557  GLU   A CD   1 
ATOM   8564  O  OE1  . GLU   A 1 557 ? 10.207 15.280  3.110  1.00 28.44 ? 557  GLU   A OE1  1 
ATOM   8565  O  OE2  . GLU   A 1 557 ? 11.135 15.588  1.149  1.00 33.05 ? 557  GLU   A OE2  1 
ATOM   8566  H  H    . GLU   A 1 557 ? 7.920  19.415  2.004  1.00 18.85 ? 557  GLU   A H    1 
ATOM   8567  H  HA   . GLU   A 1 557 ? 6.399  17.229  1.401  1.00 18.25 ? 557  GLU   A HA   1 
ATOM   8568  H  HB2  . GLU   A 1 557 ? 8.526  17.403  3.239  1.00 23.02 ? 557  GLU   A HB2  1 
ATOM   8569  H  HB3  . GLU   A 1 557 ? 7.691  16.101  3.041  1.00 23.02 ? 557  GLU   A HB3  1 
ATOM   8570  H  HG2  . GLU   A 1 557 ? 8.465  15.896  0.855  1.00 27.17 ? 557  GLU   A HG2  1 
ATOM   8571  H  HG3  . GLU   A 1 557 ? 9.231  17.249  0.976  1.00 27.17 ? 557  GLU   A HG3  1 
ATOM   8572  N  N    . PRO   A 1 558 ? 4.527  17.631  3.029  1.00 15.18 ? 558  PRO   A N    1 
ATOM   8573  C  CA   . PRO   A 1 558 ? 3.514  17.842  4.047  1.00 15.59 ? 558  PRO   A CA   1 
ATOM   8574  C  C    . PRO   A 1 558 ? 3.832  16.982  5.278  1.00 15.68 ? 558  PRO   A C    1 
ATOM   8575  O  O    . PRO   A 1 558 ? 4.323  15.888  5.111  1.00 14.12 ? 558  PRO   A O    1 
ATOM   8576  C  CB   . PRO   A 1 558 ? 2.209  17.363  3.395  1.00 19.41 ? 558  PRO   A CB   1 
ATOM   8577  C  CG   . PRO   A 1 558 ? 2.501  17.383  1.912  1.00 22.61 ? 558  PRO   A CG   1 
ATOM   8578  C  CD   . PRO   A 1 558 ? 3.977  17.064  1.799  1.00 21.52 ? 558  PRO   A CD   1 
ATOM   8579  H  HA   . PRO   A 1 558 ? 3.464  18.765  4.341  1.00 18.71 ? 558  PRO   A HA   1 
ATOM   8580  H  HB2  . PRO   A 1 558 ? 1.969  16.473  3.696  1.00 23.30 ? 558  PRO   A HB2  1 
ATOM   8581  H  HB3  . PRO   A 1 558 ? 1.467  17.947  3.617  1.00 23.30 ? 558  PRO   A HB3  1 
ATOM   8582  H  HG2  . PRO   A 1 558 ? 1.963  16.729  1.439  1.00 27.14 ? 558  PRO   A HG2  1 
ATOM   8583  H  HG3  . PRO   A 1 558 ? 2.298  18.249  1.526  1.00 27.14 ? 558  PRO   A HG3  1 
ATOM   8584  H  HD2  . PRO   A 1 558 ? 4.135  16.109  1.741  1.00 25.82 ? 558  PRO   A HD2  1 
ATOM   8585  H  HD3  . PRO   A 1 558 ? 4.372  17.465  1.009  1.00 25.82 ? 558  PRO   A HD3  1 
ATOM   8586  N  N    . ILE   A 1 559 ? 3.558  17.517  6.467  1.00 12.64 ? 559  ILE   A N    1 
ATOM   8587  C  CA   . ILE   A 1 559 ? 3.768  16.717  7.679  1.00 12.82 ? 559  ILE   A CA   1 
ATOM   8588  C  C    . ILE   A 1 559 ? 3.017  15.403  7.521  1.00 13.69 ? 559  ILE   A C    1 
ATOM   8589  O  O    . ILE   A 1 559 ? 1.819  15.412  7.166  1.00 14.29 ? 559  ILE   A O    1 
ATOM   8590  C  CB   . ILE   A 1 559 ? 3.300  17.479  8.928  1.00 12.43 ? 559  ILE   A CB   1 
ATOM   8591  C  CG1  . ILE   A 1 559 ? 4.319  18.560  9.304  1.00 12.68 ? 559  ILE   A CG1  1 
ATOM   8592  C  CG2  . ILE   A 1 559 ? 3.086  16.511  10.103 1.00 13.31 ? 559  ILE   A CG2  1 
ATOM   8593  C  CD1  . ILE   A 1 559 ? 3.875  19.429  10.453 1.00 11.79 ? 559  ILE   A CD1  1 
ATOM   8594  H  H    . ILE   A 1 559 ? 3.260  18.313  6.595  1.00 15.17 ? 559  ILE   A H    1 
ATOM   8595  H  HA   . ILE   A 1 559 ? 4.714  16.538  7.796  1.00 15.39 ? 559  ILE   A HA   1 
ATOM   8596  H  HB   . ILE   A 1 559 ? 2.453  17.908  8.728  1.00 14.92 ? 559  ILE   A HB   1 
ATOM   8597  H  HG12 . ILE   A 1 559 ? 5.160  18.136  9.535  1.00 15.22 ? 559  ILE   A HG12 1 
ATOM   8598  H  HG13 . ILE   A 1 559 ? 4.487  19.120  8.530  1.00 15.22 ? 559  ILE   A HG13 1 
ATOM   8599  H  HG21 . ILE   A 1 559 ? 2.791  17.008  10.882 1.00 15.97 ? 559  ILE   A HG21 1 
ATOM   8600  H  HG22 . ILE   A 1 559 ? 2.412  15.856  9.864  1.00 15.97 ? 559  ILE   A HG22 1 
ATOM   8601  H  HG23 . ILE   A 1 559 ? 3.920  16.058  10.305 1.00 15.97 ? 559  ILE   A HG23 1 
ATOM   8602  H  HD11 . ILE   A 1 559 ? 4.559  20.090  10.642 1.00 14.15 ? 559  ILE   A HD11 1 
ATOM   8603  H  HD12 . ILE   A 1 559 ? 3.048  19.878  10.218 1.00 14.15 ? 559  ILE   A HD12 1 
ATOM   8604  H  HD13 . ILE   A 1 559 ? 3.732  18.879  11.239 1.00 14.15 ? 559  ILE   A HD13 1 
ATOM   8605  N  N    . PRO   A 1 560 ? 3.696  14.233  7.630  1.00 14.04 ? 560  PRO   A N    1 
ATOM   8606  C  CA   . PRO   A 1 560 ? 3.060  12.944  7.296  1.00 16.34 ? 560  PRO   A CA   1 
ATOM   8607  C  C    . PRO   A 1 560 ? 1.949  12.457  8.228  1.00 17.24 ? 560  PRO   A C    1 
ATOM   8608  O  O    . PRO   A 1 560 ? 1.081  11.763  7.755  1.00 18.44 ? 560  PRO   A O    1 
ATOM   8609  C  CB   . PRO   A 1 560 ? 4.229  11.946  7.360  1.00 17.95 ? 560  PRO   A CB   1 
ATOM   8610  C  CG   . PRO   A 1 560 ? 5.185  12.559  8.352  1.00 19.03 ? 560  PRO   A CG   1 
ATOM   8611  C  CD   . PRO   A 1 560 ? 5.084  14.045  8.091  1.00 16.64 ? 560  PRO   A CD   1 
ATOM   8612  H  HA   . PRO   A 1 560 ? 2.608  13.035  6.443  1.00 19.61 ? 560  PRO   A HA   1 
ATOM   8613  H  HB2  . PRO   A 1 560 ? 3.931  11.070  7.650  1.00 21.54 ? 560  PRO   A HB2  1 
ATOM   8614  H  HB3  . PRO   A 1 560 ? 4.645  11.831  6.491  1.00 21.54 ? 560  PRO   A HB3  1 
ATOM   8615  H  HG2  . PRO   A 1 560 ? 4.938  12.341  9.264  1.00 22.84 ? 560  PRO   A HG2  1 
ATOM   8616  H  HG3  . PRO   A 1 560 ? 6.090  12.236  8.219  1.00 22.84 ? 560  PRO   A HG3  1 
ATOM   8617  H  HD2  . PRO   A 1 560 ? 5.265  14.560  8.893  1.00 19.97 ? 560  PRO   A HD2  1 
ATOM   8618  H  HD3  . PRO   A 1 560 ? 5.723  14.332  7.420  1.00 19.97 ? 560  PRO   A HD3  1 
ATOM   8619  N  N    . ASP   A 1 561 ? 2.016  12.813  9.507  1.00 20.32 ? 561  ASP   A N    1 
ATOM   8620  C  CA   . ASP   A 1 561 ? 1.021  12.273  10.460 1.00 22.63 ? 561  ASP   A CA   1 
ATOM   8621  C  C    . ASP   A 1 561 ? 0.932  13.154  11.702 1.00 20.20 ? 561  ASP   A C    1 
ATOM   8622  O  O    . ASP   A 1 561 ? 1.865  13.930  11.947 1.00 17.85 ? 561  ASP   A O    1 
ATOM   8623  C  CB   . ASP   A 1 561 ? 1.403  10.859  10.893 1.00 23.24 ? 561  ASP   A CB   1 
ATOM   8624  C  CG   . ASP   A 1 561 ? 0.232  10.069  11.443 1.00 36.26 ? 561  ASP   A CG   1 
ATOM   8625  O  OD1  . ASP   A 1 561 ? -0.797 9.994   10.749 1.00 36.68 ? 561  ASP   A OD1  1 
ATOM   8626  O  OD2  . ASP   A 1 561 ? 0.358  9.544   12.566 1.00 52.61 ? 561  ASP   A OD2  1 
ATOM   8627  H  H    . ASP   A 1 561 ? 2.602  13.345  9.844  1.00 24.39 ? 561  ASP   A H    1 
ATOM   8628  H  HA   . ASP   A 1 561 ? 0.162  12.256  10.009 1.00 27.17 ? 561  ASP   A HA   1 
ATOM   8629  H  HB2  . ASP   A 1 561 ? 1.779  10.385  10.135 1.00 27.89 ? 561  ASP   A HB2  1 
ATOM   8630  H  HB3  . ASP   A 1 561 ? 2.098  10.910  11.568 1.00 27.89 ? 561  ASP   A HB3  1 
ATOM   8631  N  N    . GLY   A 1 562 ? -0.152 13.010  12.458 1.00 20.10 ? 562  GLY   A N    1 
ATOM   8632  C  CA   . GLY   A 1 562 ? -0.252 13.744  13.728 1.00 19.51 ? 562  GLY   A CA   1 
ATOM   8633  C  C    . GLY   A 1 562 ? -1.179 14.938  13.657 1.00 19.21 ? 562  GLY   A C    1 
ATOM   8634  O  O    . GLY   A 1 562 ? -1.822 15.136  12.616 1.00 20.14 ? 562  GLY   A O    1 
ATOM   8635  H  H    . GLY   A 1 562 ? -0.825 12.509  12.267 1.00 24.13 ? 562  GLY   A H    1 
ATOM   8636  H  HA2  . GLY   A 1 562 ? -0.565 13.140  14.420 1.00 23.42 ? 562  GLY   A HA2  1 
ATOM   8637  H  HA3  . GLY   A 1 562 ? 0.632  14.044  13.992 1.00 23.42 ? 562  GLY   A HA3  1 
ATOM   8638  N  N    . PRO   A 1 563 ? -1.274 15.736  14.737 1.00 18.11 ? 563  PRO   A N    1 
ATOM   8639  C  CA   . PRO   A 1 563 ? -2.206 16.870  14.785 1.00 20.35 ? 563  PRO   A CA   1 
ATOM   8640  C  C    . PRO   A 1 563 ? -1.963 17.962  13.728 1.00 21.79 ? 563  PRO   A C    1 
ATOM   8641  O  O    . PRO   A 1 563 ? -2.847 18.756  13.506 1.00 24.19 ? 563  PRO   A O    1 
ATOM   8642  C  CB   . PRO   A 1 563 ? -1.960 17.449  16.189 1.00 20.90 ? 563  PRO   A CB   1 
ATOM   8643  C  CG   . PRO   A 1 563 ? -1.378 16.301  16.979 1.00 23.30 ? 563  PRO   A CG   1 
ATOM   8644  C  CD   . PRO   A 1 563 ? -0.522 15.560  15.978 1.00 21.70 ? 563  PRO   A CD   1 
ATOM   8645  H  HA   . PRO   A 1 563 ? -3.111 16.572  14.602 1.00 24.42 ? 563  PRO   A HA   1 
ATOM   8646  H  HB2  . PRO   A 1 563 ? -1.349 18.201  16.158 1.00 25.08 ? 563  PRO   A HB2  1 
ATOM   8647  H  HB3  . PRO   A 1 563 ? -2.784 17.769  16.588 1.00 25.08 ? 563  PRO   A HB3  1 
ATOM   8648  H  HG2  . PRO   A 1 563 ? -0.852 16.618  17.730 1.00 27.96 ? 563  PRO   A HG2  1 
ATOM   8649  H  HG3  . PRO   A 1 563 ? -2.074 15.731  17.341 1.00 27.96 ? 563  PRO   A HG3  1 
ATOM   8650  H  HD2  . PRO   A 1 563 ? 0.371  15.935  15.917 1.00 26.04 ? 563  PRO   A HD2  1 
ATOM   8651  H  HD3  . PRO   A 1 563 ? -0.421 14.624  16.211 1.00 26.04 ? 563  PRO   A HD3  1 
ATOM   8652  N  N    . SER   A 1 564 ? -0.769 17.991  13.129 1.00 19.93 ? 564  SER   A N    1 
ATOM   8653  C  CA   . SER   A 1 564 ? -0.449 19.014  12.099 1.00 15.47 ? 564  SER   A CA   1 
ATOM   8654  C  C    . SER   A 1 564 ? -0.313 18.346  10.726 1.00 16.33 ? 564  SER   A C    1 
ATOM   8655  O  O    . SER   A 1 564 ? 0.340  18.920  9.841  1.00 13.80 ? 564  SER   A O    1 
ATOM   8656  C  CB   . SER   A 1 564 ? 0.791  19.792  12.479 1.00 15.09 ? 564  SER   A CB   1 
ATOM   8657  O  OG   . SER   A 1 564 ? 0.580  20.508  13.684 1.00 14.76 ? 564  SER   A OG   1 
ATOM   8658  H  H    . SER   A 1 564 ? -0.131 17.438  13.296 1.00 23.92 ? 564  SER   A H    1 
ATOM   8659  H  HA   . SER   A 1 564 ? -1.177 19.654  12.048 1.00 18.56 ? 564  SER   A HA   1 
ATOM   8660  H  HB2  . SER   A 1 564 ? 1.540  19.185  12.584 1.00 18.12 ? 564  SER   A HB2  1 
ATOM   8661  H  HB3  . SER   A 1 564 ? 1.023  20.408  11.767 1.00 18.12 ? 564  SER   A HB3  1 
ATOM   8662  H  HG   . SER   A 1 564 ? 0.806  20.031  14.337 1.00 17.72 ? 564  SER   A HG   1 
ATOM   8663  N  N    . LYS   A 1 565 ? -0.935 17.179  10.569 1.00 17.68 ? 565  LYS   A N    1 
ATOM   8664  C  CA   . LYS   A 1 565 ? -0.818 16.417  9.302  1.00 15.82 ? 565  LYS   A CA   1 
ATOM   8665  C  C    . LYS   A 1 565 ? -1.272 17.248  8.104  1.00 15.19 ? 565  LYS   A C    1 
ATOM   8666  O  O    . LYS   A 1 565 ? -2.317 17.905  8.202  1.00 16.96 ? 565  LYS   A O    1 
ATOM   8667  C  CB   . LYS   A 1 565 ? -1.655 15.135  9.361  1.00 17.15 ? 565  LYS   A CB   1 
ATOM   8668  C  CG   . LYS   A 1 565 ? -1.507 14.216  8.157  1.00 20.05 ? 565  LYS   A CG   1 
ATOM   8669  C  CD   . LYS   A 1 565 ? -2.484 13.063  8.159  1.00 21.65 ? 565  LYS   A CD   1 
ATOM   8670  C  CE   . LYS   A 1 565 ? -2.392 12.213  6.910  1.00 22.47 ? 565  LYS   A CE   1 
ATOM   8671  N  NZ   . LYS   A 1 565 ? -2.896 10.840  7.146  1.00 33.54 ? 565  LYS   A NZ   1 
ATOM   8672  H  H    . LYS   A 1 565 ? -1.426 16.807  11.169 1.00 21.22 ? 565  LYS   A H    1 
ATOM   8673  H  HA   . LYS   A 1 565 ? 0.119  16.192  9.192  1.00 18.99 ? 565  LYS   A HA   1 
ATOM   8674  H  HB2  . LYS   A 1 565 ? -1.411 14.642  10.160 1.00 20.58 ? 565  LYS   A HB2  1 
ATOM   8675  H  HB3  . LYS   A 1 565 ? -2.589 15.379  9.452  1.00 20.58 ? 565  LYS   A HB3  1 
ATOM   8676  H  HG2  . LYS   A 1 565 ? -1.630 14.734  7.346  1.00 24.06 ? 565  LYS   A HG2  1 
ATOM   8677  H  HG3  . LYS   A 1 565 ? -0.603 13.865  8.135  1.00 24.06 ? 565  LYS   A HG3  1 
ATOM   8678  H  HD2  . LYS   A 1 565 ? -2.320 12.507  8.936  1.00 25.99 ? 565  LYS   A HD2  1 
ATOM   8679  H  HD3  . LYS   A 1 565 ? -3.386 13.409  8.244  1.00 25.99 ? 565  LYS   A HD3  1 
ATOM   8680  H  HE2  . LYS   A 1 565 ? -2.903 12.628  6.197  1.00 26.97 ? 565  LYS   A HE2  1 
ATOM   8681  H  HE3  . LYS   A 1 565 ? -1.470 12.173  6.612  1.00 26.97 ? 565  LYS   A HE3  1 
ATOM   8682  H  HZ1  . LYS   A 1 565 ? -2.829 10.366  6.396  1.00 40.25 ? 565  LYS   A HZ1  1 
ATOM   8683  H  HZ2  . LYS   A 1 565 ? -2.414 10.452  7.785  1.00 40.25 ? 565  LYS   A HZ2  1 
ATOM   8684  H  HZ3  . LYS   A 1 565 ? -3.749 10.876  7.399  1.00 40.25 ? 565  LYS   A HZ3  1 
ATOM   8685  N  N    . GLY   A 1 566 ? -0.489 17.228  7.034  1.00 16.50 ? 566  GLY   A N    1 
ATOM   8686  C  CA   . GLY   A 1 566 ? -0.851 17.867  5.784  1.00 18.30 ? 566  GLY   A CA   1 
ATOM   8687  C  C    . GLY   A 1 566 ? -0.235 19.230  5.544  1.00 16.69 ? 566  GLY   A C    1 
ATOM   8688  O  O    . GLY   A 1 566 ? -0.311 19.730  4.416  1.00 18.32 ? 566  GLY   A O    1 
ATOM   8689  H  H    . GLY   A 1 566 ? 0.277  16.837  7.016  1.00 19.81 ? 566  GLY   A H    1 
ATOM   8690  H  HA2  . GLY   A 1 566 ? -0.596 17.281  5.054  1.00 21.97 ? 566  GLY   A HA2  1 
ATOM   8691  H  HA3  . GLY   A 1 566 ? -1.816 17.956  5.752  1.00 21.97 ? 566  GLY   A HA3  1 
ATOM   8692  N  N    . GLU   A 1 567 ? 0.380  19.800  6.578  1.00 13.59 ? 567  GLU   A N    1 
ATOM   8693  C  CA   . GLU   A 1 567 ? 0.838  21.210  6.475  1.00 12.67 ? 567  GLU   A CA   1 
ATOM   8694  C  C    . GLU   A 1 567 ? 2.265  21.374  5.951  1.00 15.18 ? 567  GLU   A C    1 
ATOM   8695  O  O    . GLU   A 1 567 ? 3.089  20.477  6.176  1.00 12.09 ? 567  GLU   A O    1 
ATOM   8696  C  CB   . GLU   A 1 567 ? 0.736  21.862  7.854  1.00 13.00 ? 567  GLU   A CB   1 
ATOM   8697  C  CG   . GLU   A 1 567 ? -0.681 21.922  8.388  1.00 18.47 ? 567  GLU   A CG   1 
ATOM   8698  C  CD   . GLU   A 1 567 ? -1.578 22.894  7.643  1.00 21.67 ? 567  GLU   A CD   1 
ATOM   8699  O  OE1  . GLU   A 1 567 ? -1.192 24.067  7.515  1.00 20.84 ? 567  GLU   A OE1  1 
ATOM   8700  O  OE2  . GLU   A 1 567 ? -2.656 22.472  7.189  1.00 24.27 ? 567  GLU   A OE2  1 
ATOM   8701  H  H    . GLU   A 1 567 ? 0.543  19.414  7.329  1.00 16.32 ? 567  GLU   A H    1 
ATOM   8702  H  HA   . GLU   A 1 567 ? 0.260  21.639  5.825  1.00 15.21 ? 567  GLU   A HA   1 
ATOM   8703  H  HB2  . GLU   A 1 567 ? 1.290  21.369  8.479  1.00 15.60 ? 567  GLU   A HB2  1 
ATOM   8704  H  HB3  . GLU   A 1 567 ? 1.095  22.762  7.806  1.00 15.60 ? 567  GLU   A HB3  1 
ATOM   8705  H  HG2  . GLU   A 1 567 ? -1.072 21.035  8.343  1.00 22.17 ? 567  GLU   A HG2  1 
ATOM   8706  H  HG3  . GLU   A 1 567 ? -0.654 22.173  9.325  1.00 22.17 ? 567  GLU   A HG3  1 
ATOM   8707  N  N    . VAL   A 1 568 ? 2.509  22.486  5.255  1.00 14.08 ? 568  VAL   A N    1 
ATOM   8708  C  CA   . VAL   A 1 568 ? 3.880  22.850  4.803  1.00 12.51 ? 568  VAL   A CA   1 
ATOM   8709  C  C    . VAL   A 1 568 ? 4.029  24.329  5.174  1.00 14.30 ? 568  VAL   A C    1 
ATOM   8710  O  O    . VAL   A 1 568 ? 2.998  24.999  5.340  1.00 10.18 ? 568  VAL   A O    1 
ATOM   8711  C  CB   . VAL   A 1 568 ? 4.101  22.637  3.295  1.00 13.90 ? 568  VAL   A CB   1 
ATOM   8712  C  CG1  . VAL   A 1 568 ? 4.070  21.167  2.909  1.00 17.04 ? 568  VAL   A CG1  1 
ATOM   8713  C  CG2  . VAL   A 1 568 ? 3.121  23.443  2.457  1.00 16.77 ? 568  VAL   A CG2  1 
ATOM   8714  H  H    . VAL   A 1 568 ? 1.901  23.051  5.029  1.00 16.90 ? 568  VAL   A H    1 
ATOM   8715  H  HA   . VAL   A 1 568 ? 4.543  22.282  5.226  1.00 15.01 ? 568  VAL   A HA   1 
ATOM   8716  H  HB   . VAL   A 1 568 ? 4.993  22.966  3.102  1.00 16.68 ? 568  VAL   A HB   1 
ATOM   8717  H  HG11 . VAL   A 1 568 ? 4.213  21.080  1.954  1.00 20.46 ? 568  VAL   A HG11 1 
ATOM   8718  H  HG12 . VAL   A 1 568 ? 4.770  20.692  3.385  1.00 20.46 ? 568  VAL   A HG12 1 
ATOM   8719  H  HG13 . VAL   A 1 568 ? 3.208  20.789  3.142  1.00 20.46 ? 568  VAL   A HG13 1 
ATOM   8720  H  HG21 . VAL   A 1 568 ? 3.292  23.283  1.516  1.00 20.12 ? 568  VAL   A HG21 1 
ATOM   8721  H  HG22 . VAL   A 1 568 ? 2.214  23.174  2.671  1.00 20.12 ? 568  VAL   A HG22 1 
ATOM   8722  H  HG23 . VAL   A 1 568 ? 3.231  24.387  2.649  1.00 20.12 ? 568  VAL   A HG23 1 
ATOM   8723  N  N    . HIS   A 1 569 ? 5.260  24.818  5.304  1.00 13.39 ? 569  HIS   A N    1 
ATOM   8724  C  CA   . HIS   A 1 569 ? 5.443  26.264  5.587  1.00 14.12 ? 569  HIS   A CA   1 
ATOM   8725  C  C    . HIS   A 1 569 ? 5.222  27.070  4.302  1.00 12.76 ? 569  HIS   A C    1 
ATOM   8726  O  O    . HIS   A 1 569 ? 5.853  26.738  3.285  1.00 13.23 ? 569  HIS   A O    1 
ATOM   8727  C  CB   . HIS   A 1 569 ? 6.819  26.538  6.200  1.00 11.36 ? 569  HIS   A CB   1 
ATOM   8728  C  CG   . HIS   A 1 569 ? 6.923  27.934  6.701  1.00 10.56 ? 569  HIS   A CG   1 
ATOM   8729  N  ND1  . HIS   A 1 569 ? 7.477  28.952  5.957  1.00 9.56  ? 569  HIS   A ND1  1 
ATOM   8730  C  CD2  . HIS   A 1 569 ? 6.513  28.489  7.844  1.00 12.06 ? 569  HIS   A CD2  1 
ATOM   8731  C  CE1  . HIS   A 1 569 ? 7.411  30.077  6.648  1.00 12.11 ? 569  HIS   A CE1  1 
ATOM   8732  N  NE2  . HIS   A 1 569 ? 6.830  29.818  7.796  1.00 10.61 ? 569  HIS   A NE2  1 
ATOM   8733  H  H    . HIS   A 1 569 ? 5.984  24.359  5.237  1.00 16.07 ? 569  HIS   A H    1 
ATOM   8734  H  HA   . HIS   A 1 569 ? 4.785  26.545  6.242  1.00 16.95 ? 569  HIS   A HA   1 
ATOM   8735  H  HB2  . HIS   A 1 569 ? 6.979  25.918  6.929  1.00 13.63 ? 569  HIS   A HB2  1 
ATOM   8736  H  HB3  . HIS   A 1 569 ? 7.508  26.379  5.536  1.00 13.63 ? 569  HIS   A HB3  1 
ATOM   8737  H  HD2  . HIS   A 1 569 ? 6.089  28.051  8.546  1.00 14.48 ? 569  HIS   A HD2  1 
ATOM   8738  H  HE1  . HIS   A 1 569 ? 7.722  30.908  6.369  1.00 14.54 ? 569  HIS   A HE1  1 
ATOM   8739  H  HE2  . HIS   A 1 569 ? 6.674  30.392  8.418  1.00 12.74 ? 569  HIS   A HE2  1 
ATOM   8740  N  N    A ARG   A 1 570 ? 4.532  28.199  4.413  0.57 10.73 ? 570  ARG   A N    1 
ATOM   8741  N  N    B ARG   A 1 570 ? 4.533  28.210  4.416  0.43 10.73 ? 570  ARG   A N    1 
ATOM   8742  C  CA   A ARG   A 1 570 ? 4.227  29.031  3.218  0.57 13.38 ? 570  ARG   A CA   1 
ATOM   8743  C  CA   B ARG   A 1 570 ? 4.211  29.041  3.225  0.43 13.38 ? 570  ARG   A CA   1 
ATOM   8744  C  C    A ARG   A 1 570 ? 5.154  30.250  3.177  0.57 13.58 ? 570  ARG   A C    1 
ATOM   8745  C  C    B ARG   A 1 570 ? 5.134  30.263  3.178  0.43 13.58 ? 570  ARG   A C    1 
ATOM   8746  O  O    A ARG   A 1 570 ? 4.643  31.357  2.967  0.57 14.40 ? 570  ARG   A O    1 
ATOM   8747  O  O    B ARG   A 1 570 ? 4.620  31.363  2.921  0.43 14.40 ? 570  ARG   A O    1 
ATOM   8748  C  CB   A ARG   A 1 570 ? 2.757  29.454  3.256  0.57 15.22 ? 570  ARG   A CB   1 
ATOM   8749  C  CB   B ARG   A 1 570 ? 2.738  29.457  3.281  0.43 15.22 ? 570  ARG   A CB   1 
ATOM   8750  C  CG   A ARG   A 1 570 ? 1.792  28.311  3.538  0.57 17.00 ? 570  ARG   A CG   1 
ATOM   8751  C  CG   B ARG   A 1 570 ? 1.771  28.284  3.349  0.43 17.00 ? 570  ARG   A CG   1 
ATOM   8752  C  CD   A ARG   A 1 570 ? 1.374  27.575  2.279  0.57 19.24 ? 570  ARG   A CD   1 
ATOM   8753  C  CD   B ARG   A 1 570 ? 1.400  27.789  1.965  0.43 19.24 ? 570  ARG   A CD   1 
ATOM   8754  N  NE   A ARG   A 1 570 ? 0.952  28.479  1.218  0.57 29.71 ? 570  ARG   A NE   1 
ATOM   8755  N  NE   B ARG   A 1 570 ? 1.229  26.346  1.891  0.43 29.71 ? 570  ARG   A NE   1 
ATOM   8756  C  CZ   A ARG   A 1 570 ? -0.227 29.090  1.167  0.57 30.33 ? 570  ARG   A CZ   1 
ATOM   8757  C  CZ   B ARG   A 1 570 ? 0.964  25.677  0.774  0.43 30.33 ? 570  ARG   A CZ   1 
ATOM   8758  N  NH1  A ARG   A 1 570 ? -1.184 28.757  2.013  0.57 28.39 ? 570  ARG   A NH1  1 
ATOM   8759  N  NH1  B ARG   A 1 570 ? 1.897  25.539  -0.152 0.43 28.39 ? 570  ARG   A NH1  1 
ATOM   8760  N  NH2  A ARG   A 1 570 ? -0.443 30.032  0.266  0.57 35.33 ? 570  ARG   A NH2  1 
ATOM   8761  N  NH2  B ARG   A 1 570 ? -0.231 25.148  0.585  0.43 35.32 ? 570  ARG   A NH2  1 
ATOM   8762  H  H    A ARG   A 1 570 ? 4.228  28.510  5.155  0.57 12.88 ? 570  ARG   A H    1 
ATOM   8763  H  H    B ARG   A 1 570 ? 4.242  28.525  5.161  0.43 12.88 ? 570  ARG   A H    1 
ATOM   8764  H  HA   A ARG   A 1 570 ? 4.379  28.515  2.411  0.57 16.06 ? 570  ARG   A HA   1 
ATOM   8765  H  HA   B ARG   A 1 570 ? 4.355  28.528  2.414  0.43 16.06 ? 570  ARG   A HA   1 
ATOM   8766  H  HB2  A ARG   A 1 570 ? 2.644  30.136  3.936  0.57 18.26 ? 570  ARG   A HB2  1 
ATOM   8767  H  HB2  B ARG   A 1 570 ? 2.600  30.024  4.056  0.43 18.26 ? 570  ARG   A HB2  1 
ATOM   8768  H  HB3  A ARG   A 1 570 ? 2.524  29.859  2.406  0.57 18.26 ? 570  ARG   A HB3  1 
ATOM   8769  H  HB3  B ARG   A 1 570 ? 2.531  29.991  2.498  0.43 18.26 ? 570  ARG   A HB3  1 
ATOM   8770  H  HG2  A ARG   A 1 570 ? 2.208  27.685  4.151  0.57 20.41 ? 570  ARG   A HG2  1 
ATOM   8771  H  HG2  B ARG   A 1 570 ? 2.173  27.561  3.856  0.43 20.41 ? 570  ARG   A HG2  1 
ATOM   8772  H  HG3  A ARG   A 1 570 ? 1.003  28.660  3.981  0.57 20.41 ? 570  ARG   A HG3  1 
ATOM   8773  H  HG3  B ARG   A 1 570 ? 0.969  28.552  3.824  0.43 20.41 ? 570  ARG   A HG3  1 
ATOM   8774  H  HD2  A ARG   A 1 570 ? 2.115  27.034  1.963  0.57 23.09 ? 570  ARG   A HD2  1 
ATOM   8775  H  HD2  B ARG   A 1 570 ? 0.577  28.220  1.685  0.43 23.09 ? 570  ARG   A HD2  1 
ATOM   8776  H  HD3  A ARG   A 1 570 ? 0.648  26.967  2.489  0.57 23.09 ? 570  ARG   A HD3  1 
ATOM   8777  H  HD3  B ARG   A 1 570 ? 2.089  28.058  1.338  0.43 23.09 ? 570  ARG   A HD3  1 
ATOM   8778  H  HE   A ARG   A 1 570 ? 1.506  28.628  0.578  0.57 35.65 ? 570  ARG   A HE   1 
ATOM   8779  H  HE   B ARG   A 1 570 ? 1.305  25.896  2.620  0.43 35.65 ? 570  ARG   A HE   1 
ATOM   8780  H  HH11 A ARG   A 1 570 ? -1.045 28.143  2.599  0.57 34.08 ? 570  ARG   A HH11 1 
ATOM   8781  H  HH11 B ARG   A 1 570 ? 2.676  25.882  -0.032 0.43 34.08 ? 570  ARG   A HH11 1 
ATOM   8782  H  HH12 A ARG   A 1 570 ? -1.946 29.154  1.978  0.57 34.08 ? 570  ARG   A HH12 1 
ATOM   8783  H  HH12 B ARG   A 1 570 ? 1.725  25.106  -0.875 0.43 34.08 ? 570  ARG   A HH12 1 
ATOM   8784  H  HH21 A ARG   A 1 570 ? 0.179  30.249  -0.287 0.57 42.39 ? 570  ARG   A HH21 1 
ATOM   8785  H  HH21 B ARG   A 1 570 ? -0.840 25.236  1.186  0.43 42.39 ? 570  ARG   A HH21 1 
ATOM   8786  H  HH22 A ARG   A 1 570 ? -1.206 30.428  0.232  0.57 42.39 ? 570  ARG   A HH22 1 
ATOM   8787  H  HH22 B ARG   A 1 570 ? -0.400 24.715  -0.139 0.43 42.39 ? 570  ARG   A HH22 1 
ATOM   8788  N  N    . LEU   A 1 571 ? 6.439  30.015  3.062  1.00 12.54 ? 571  LEU   A N    1 
ATOM   8789  C  CA   . LEU   A 1 571 ? 7.429  31.123  3.015  1.00 12.70 ? 571  LEU   A CA   1 
ATOM   8790  C  C    . LEU   A 1 571 ? 7.257  31.918  1.717  1.00 14.62 ? 571  LEU   A C    1 
ATOM   8791  O  O    . LEU   A 1 571 ? 7.562  33.113  1.722  1.00 14.00 ? 571  LEU   A O    1 
ATOM   8792  C  CB   . LEU   A 1 571 ? 8.835  30.523  3.092  1.00 11.31 ? 571  LEU   A CB   1 
ATOM   8793  C  CG   . LEU   A 1 571 ? 9.967  31.531  3.276  1.00 15.50 ? 571  LEU   A CG   1 
ATOM   8794  C  CD1  . LEU   A 1 571 ? 9.836  32.246  4.611  1.00 13.40 ? 571  LEU   A CD1  1 
ATOM   8795  C  CD2  . LEU   A 1 571 ? 11.323 30.852  3.161  1.00 14.75 ? 571  LEU   A CD2  1 
ATOM   8796  H  H    A LEU   A 1 571 ? 6.782  29.228  3.008  0.57 15.05 ? 571  LEU   A H    1 
ATOM   8797  H  H    B LEU   A 1 571 ? 6.779  29.227  3.009  0.43 15.05 ? 571  LEU   A H    1 
ATOM   8798  H  HA   . LEU   A 1 571 ? 7.292  31.726  3.762  1.00 15.25 ? 571  LEU   A HA   1 
ATOM   8799  H  HB2  . LEU   A 1 571 ? 8.861  29.892  3.828  1.00 13.57 ? 571  LEU   A HB2  1 
ATOM   8800  H  HB3  . LEU   A 1 571 ? 9.000  30.019  2.280  1.00 13.57 ? 571  LEU   A HB3  1 
ATOM   8801  H  HG   . LEU   A 1 571 ? 9.901  32.191  2.568  1.00 18.61 ? 571  LEU   A HG   1 
ATOM   8802  H  HD11 . LEU   A 1 571 ? 10.562 32.881  4.711  1.00 16.09 ? 571  LEU   A HD11 1 
ATOM   8803  H  HD12 . LEU   A 1 571 ? 8.988  32.716  4.645  1.00 16.09 ? 571  LEU   A HD12 1 
ATOM   8804  H  HD13 . LEU   A 1 571 ? 9.874  31.597  5.331  1.00 16.09 ? 571  LEU   A HD13 1 
ATOM   8805  H  HD21 . LEU   A 1 571 ? 12.026 31.510  3.281  1.00 17.71 ? 571  LEU   A HD21 1 
ATOM   8806  H  HD22 . LEU   A 1 571 ? 11.401 30.168  3.844  1.00 17.71 ? 571  LEU   A HD22 1 
ATOM   8807  H  HD23 . LEU   A 1 571 ? 11.408 30.445  2.285  1.00 17.71 ? 571  LEU   A HD23 1 
ATOM   8808  N  N    . ASP   A 1 572 ? 6.782  31.260  0.659  1.00 15.55 ? 572  ASP   A N    1 
ATOM   8809  C  CA   . ASP   A 1 572 ? 6.640  31.925  -0.664 1.00 15.32 ? 572  ASP   A CA   1 
ATOM   8810  C  C    . ASP   A 1 572 ? 5.765  33.167  -0.515 1.00 16.14 ? 572  ASP   A C    1 
ATOM   8811  O  O    . ASP   A 1 572 ? 5.988  34.137  -1.250 1.00 17.78 ? 572  ASP   A O    1 
ATOM   8812  C  CB   . ASP   A 1 572 ? 6.055  30.972  -1.707 1.00 17.38 ? 572  ASP   A CB   1 
ATOM   8813  C  CG   . ASP   A 1 572 ? 4.739  30.331  -1.300 1.00 20.74 ? 572  ASP   A CG   1 
ATOM   8814  O  OD1  . ASP   A 1 572 ? 4.415  30.355  -0.100 1.00 25.10 ? 572  ASP   A OD1  1 
ATOM   8815  O  OD2  . ASP   A 1 572 ? 4.048  29.811  -2.193 1.00 29.55 ? 572  ASP   A OD2  1 
ATOM   8816  H  H    . ASP   A 1 572 ? 6.536  30.436  0.674  1.00 18.67 ? 572  ASP   A H    1 
ATOM   8817  H  HA   . ASP   A 1 572 ? 7.520  32.188  -0.976 1.00 18.39 ? 572  ASP   A HA   1 
ATOM   8818  H  HB2  . ASP   A 1 572 ? 5.923  31.458  -2.536 1.00 20.86 ? 572  ASP   A HB2  1 
ATOM   8819  H  HB3  . ASP   A 1 572 ? 6.701  30.272  -1.888 1.00 20.86 ? 572  ASP   A HB3  1 
ATOM   8820  N  N    . VAL   A 1 573 ? 4.811  33.117  0.408  1.00 15.38 ? 573  VAL   A N    1 
ATOM   8821  C  CA   . VAL   A 1 573 ? 3.870  34.255  0.597  1.00 16.46 ? 573  VAL   A CA   1 
ATOM   8822  C  C    . VAL   A 1 573 ? 4.323  35.122  1.774  1.00 16.58 ? 573  VAL   A C    1 
ATOM   8823  O  O    . VAL   A 1 573 ? 4.124  36.342  1.709  1.00 18.23 ? 573  VAL   A O    1 
ATOM   8824  C  CB   . VAL   A 1 573 ? 2.449  33.711  0.834  1.00 21.81 ? 573  VAL   A CB   1 
ATOM   8825  C  CG1  . VAL   A 1 573 ? 1.508  34.780  1.364  1.00 29.06 ? 573  VAL   A CG1  1 
ATOM   8826  C  CG2  . VAL   A 1 573 ? 1.885  33.062  -0.419 1.00 22.31 ? 573  VAL   A CG2  1 
ATOM   8827  H  H    . VAL   A 1 573 ? 4.681  32.450  0.935  1.00 18.45 ? 573  VAL   A H    1 
ATOM   8828  H  HA   . VAL   A 1 573 ? 3.865  34.807  -0.200 1.00 19.76 ? 573  VAL   A HA   1 
ATOM   8829  H  HB   . VAL   A 1 573 ? 2.522  33.027  1.518  1.00 26.18 ? 573  VAL   A HB   1 
ATOM   8830  H  HG11 . VAL   A 1 573 ? 0.627  34.398  1.499  1.00 34.88 ? 573  VAL   A HG11 1 
ATOM   8831  H  HG12 . VAL   A 1 573 ? 1.846  35.119  2.208  1.00 34.88 ? 573  VAL   A HG12 1 
ATOM   8832  H  HG13 . VAL   A 1 573 ? 1.450  35.507  0.724  1.00 34.88 ? 573  VAL   A HG13 1 
ATOM   8833  H  HG21 . VAL   A 1 573 ? 0.992  32.730  -0.238 1.00 26.77 ? 573  VAL   A HG21 1 
ATOM   8834  H  HG22 . VAL   A 1 573 ? 1.848  33.717  -1.134 1.00 26.77 ? 573  VAL   A HG22 1 
ATOM   8835  H  HG23 . VAL   A 1 573 ? 2.455  32.324  -0.686 1.00 26.77 ? 573  VAL   A HG23 1 
ATOM   8836  N  N    . LEU   A 1 574 ? 4.954  34.521  2.786  1.00 14.77 ? 574  LEU   A N    1 
ATOM   8837  C  CA   . LEU   A 1 574 ? 5.265  35.280  3.993  1.00 14.09 ? 574  LEU   A CA   1 
ATOM   8838  C  C    . LEU   A 1 574 ? 6.537  36.115  3.857  1.00 11.48 ? 574  LEU   A C    1 
ATOM   8839  O  O    . LEU   A 1 574 ? 6.602  37.220  4.407  1.00 13.35 ? 574  LEU   A O    1 
ATOM   8840  C  CB   . LEU   A 1 574 ? 5.381  34.328  5.191  1.00 13.33 ? 574  LEU   A CB   1 
ATOM   8841  C  CG   . LEU   A 1 574 ? 4.091  33.590  5.566  1.00 11.54 ? 574  LEU   A CG   1 
ATOM   8842  C  CD1  . LEU   A 1 574 ? 4.377  32.494  6.587  1.00 13.00 ? 574  LEU   A CD1  1 
ATOM   8843  C  CD2  . LEU   A 1 574 ? 3.037  34.569  6.083  1.00 13.84 ? 574  LEU   A CD2  1 
ATOM   8844  H  H    . LEU   A 1 574 ? 5.203  33.698  2.793  1.00 17.73 ? 574  LEU   A H    1 
ATOM   8845  H  HA   . LEU   A 1 574 ? 4.535  35.903  4.135  1.00 16.91 ? 574  LEU   A HA   1 
ATOM   8846  H  HB2  . LEU   A 1 574 ? 6.068  33.671  4.998  1.00 16.00 ? 574  LEU   A HB2  1 
ATOM   8847  H  HB3  . LEU   A 1 574 ? 5.682  34.835  5.961  1.00 16.00 ? 574  LEU   A HB3  1 
ATOM   8848  H  HG   . LEU   A 1 574 ? 3.736  33.168  4.768  1.00 13.85 ? 574  LEU   A HG   1 
ATOM   8849  H  HD11 . LEU   A 1 574 ? 3.551  32.038  6.813  1.00 15.60 ? 574  LEU   A HD11 1 
ATOM   8850  H  HD12 . LEU   A 1 574 ? 5.005  31.857  6.211  1.00 15.60 ? 574  LEU   A HD12 1 
ATOM   8851  H  HD13 . LEU   A 1 574 ? 4.757  32.888  7.388  1.00 15.60 ? 574  LEU   A HD13 1 
ATOM   8852  H  HD21 . LEU   A 1 574 ? 2.230  34.083  6.314  1.00 16.61 ? 574  LEU   A HD21 1 
ATOM   8853  H  HD22 . LEU   A 1 574 ? 3.376  35.025  6.869  1.00 16.61 ? 574  LEU   A HD22 1 
ATOM   8854  H  HD23 . LEU   A 1 574 ? 2.835  35.221  5.394  1.00 16.61 ? 574  LEU   A HD23 1 
ATOM   8855  N  N    . LEU   A 1 575 ? 7.539  35.632  3.124  1.00 13.23 ? 575  LEU   A N    1 
ATOM   8856  C  CA   . LEU   A 1 575 ? 8.839  36.365  3.081  1.00 13.93 ? 575  LEU   A CA   1 
ATOM   8857  C  C    . LEU   A 1 575 ? 8.693  37.746  2.416  1.00 12.96 ? 575  LEU   A C    1 
ATOM   8858  O  O    . LEU   A 1 575 ? 9.197  38.722  2.986  1.00 13.09 ? 575  LEU   A O    1 
ATOM   8859  C  CB   . LEU   A 1 575 ? 9.883  35.506  2.360  1.00 15.79 ? 575  LEU   A CB   1 
ATOM   8860  C  CG   . LEU   A 1 575 ? 11.295 36.086  2.298  1.00 13.83 ? 575  LEU   A CG   1 
ATOM   8861  C  CD1  . LEU   A 1 575 ? 11.787 36.471  3.685  1.00 12.65 ? 575  LEU   A CD1  1 
ATOM   8862  C  CD2  . LEU   A 1 575 ? 12.250 35.096  1.653  1.00 13.25 ? 575  LEU   A CD2  1 
ATOM   8863  H  H    . LEU   A 1 575 ? 7.506  34.911  2.656  1.00 15.88 ? 575  LEU   A H    1 
ATOM   8864  H  HA   . LEU   A 1 575 ? 9.135  36.526  3.991  1.00 16.71 ? 575  LEU   A HA   1 
ATOM   8865  H  HB2  . LEU   A 1 575 ? 9.926  34.642  2.800  1.00 18.96 ? 575  LEU   A HB2  1 
ATOM   8866  H  HB3  . LEU   A 1 575 ? 9.577  35.348  1.453  1.00 18.96 ? 575  LEU   A HB3  1 
ATOM   8867  H  HG   . LEU   A 1 575 ? 11.266 36.888  1.754  1.00 16.60 ? 575  LEU   A HG   1 
ATOM   8868  H  HD11 . LEU   A 1 575 ? 12.683 36.836  3.621  1.00 15.19 ? 575  LEU   A HD11 1 
ATOM   8869  H  HD12 . LEU   A 1 575 ? 11.194 37.137  4.066  1.00 15.19 ? 575  LEU   A HD12 1 
ATOM   8870  H  HD13 . LEU   A 1 575 ? 11.798 35.686  4.254  1.00 15.19 ? 575  LEU   A HD13 1 
ATOM   8871  H  HD21 . LEU   A 1 575 ? 13.141 35.479  1.621  1.00 15.91 ? 575  LEU   A HD21 1 
ATOM   8872  H  HD22 . LEU   A 1 575 ? 12.269 34.278  2.174  1.00 15.91 ? 575  LEU   A HD22 1 
ATOM   8873  H  HD23 . LEU   A 1 575 ? 11.951 34.898  0.752  1.00 15.91 ? 575  LEU   A HD23 1 
ATOM   8874  N  N    . PRO   A 1 576 ? 8.054  37.878  1.236  1.00 16.64 ? 576  PRO   A N    1 
ATOM   8875  C  CA   . PRO   A 1 576 ? 7.899  39.192  0.620  1.00 15.79 ? 576  PRO   A CA   1 
ATOM   8876  C  C    . PRO   A 1 576 ? 7.164  40.162  1.556  1.00 14.97 ? 576  PRO   A C    1 
ATOM   8877  O  O    . PRO   A 1 576 ? 7.534  41.309  1.622  1.00 15.95 ? 576  PRO   A O    1 
ATOM   8878  C  CB   . PRO   A 1 576 ? 7.076  38.890  -0.644 1.00 16.30 ? 576  PRO   A CB   1 
ATOM   8879  C  CG   . PRO   A 1 576 ? 7.364  37.437  -0.939 1.00 17.51 ? 576  PRO   A CG   1 
ATOM   8880  C  CD   . PRO   A 1 576 ? 7.491  36.796  0.425  1.00 16.45 ? 576  PRO   A CD   1 
ATOM   8881  H  HA   . PRO   A 1 576 ? 8.745  39.625  0.424  1.00 18.95 ? 576  PRO   A HA   1 
ATOM   8882  H  HB2  . PRO   A 1 576 ? 6.129  39.040  -0.494 1.00 19.56 ? 576  PRO   A HB2  1 
ATOM   8883  H  HB3  . PRO   A 1 576 ? 7.340  39.460  -1.383 1.00 19.56 ? 576  PRO   A HB3  1 
ATOM   8884  H  HG2  . PRO   A 1 576 ? 6.649  37.032  -1.455 1.00 21.02 ? 576  PRO   A HG2  1 
ATOM   8885  H  HG3  . PRO   A 1 576 ? 8.179  37.335  -1.455 1.00 21.02 ? 576  PRO   A HG3  1 
ATOM   8886  H  HD2  . PRO   A 1 576 ? 6.632  36.499  0.765  1.00 19.74 ? 576  PRO   A HD2  1 
ATOM   8887  H  HD3  . PRO   A 1 576 ? 8.072  36.020  0.406  1.00 19.74 ? 576  PRO   A HD3  1 
ATOM   8888  N  N    . GLU   A 1 577 ? 6.139  39.669  2.248  1.00 16.78 ? 577  GLU   A N    1 
ATOM   8889  C  CA   . GLU   A 1 577 ? 5.383  40.519  3.202  1.00 17.14 ? 577  GLU   A CA   1 
ATOM   8890  C  C    . GLU   A 1 577 ? 6.299  40.919  4.366  1.00 14.90 ? 577  GLU   A C    1 
ATOM   8891  O  O    . GLU   A 1 577 ? 6.159  42.043  4.862  1.00 15.90 ? 577  GLU   A O    1 
ATOM   8892  C  CB   . GLU   A 1 577 ? 4.130  39.793  3.695  1.00 18.31 ? 577  GLU   A CB   1 
ATOM   8893  C  CG   . GLU   A 1 577 ? 3.260  40.639  4.605  1.00 23.88 ? 577  GLU   A CG   1 
ATOM   8894  C  CD   . GLU   A 1 577 ? 2.678  41.889  3.968  1.00 36.70 ? 577  GLU   A CD   1 
ATOM   8895  O  OE1  . GLU   A 1 577 ? 2.749  42.010  2.731  1.00 41.94 ? 577  GLU   A OE1  1 
ATOM   8896  O  OE2  . GLU   A 1 577 ? 2.153  42.739  4.712  1.00 43.55 ? 577  GLU   A OE2  1 
ATOM   8897  H  H    . GLU   A 1 577 ? 5.860  38.858  2.189  1.00 20.14 ? 577  GLU   A H    1 
ATOM   8898  H  HA   . GLU   A 1 577 ? 5.088  41.326  2.752  1.00 20.57 ? 577  GLU   A HA   1 
ATOM   8899  H  HB2  . GLU   A 1 577 ? 3.606  39.511  2.929  1.00 21.98 ? 577  GLU   A HB2  1 
ATOM   8900  H  HB3  . GLU   A 1 577 ? 4.396  38.989  4.169  1.00 21.98 ? 577  GLU   A HB3  1 
ATOM   8901  H  HG2  . GLU   A 1 577 ? 2.530  40.090  4.932  1.00 28.66 ? 577  GLU   A HG2  1 
ATOM   8902  H  HG3  . GLU   A 1 577 ? 3.785  40.902  5.377  1.00 28.66 ? 577  GLU   A HG3  1 
ATOM   8903  N  N    . TYR   A 1 578 ? 7.204  40.024  4.769  1.00 12.55 ? 578  TYR   A N    1 
ATOM   8904  C  CA   . TYR   A 1 578 ? 8.128  40.387  5.840  1.00 14.48 ? 578  TYR   A CA   1 
ATOM   8905  C  C    . TYR   A 1 578 ? 9.038  41.530  5.410  1.00 13.95 ? 578  TYR   A C    1 
ATOM   8906  O  O    . TYR   A 1 578 ? 9.211  42.509  6.148  1.00 13.58 ? 578  TYR   A O    1 
ATOM   8907  C  CB   . TYR   A 1 578 ? 8.958  39.177  6.283  1.00 14.03 ? 578  TYR   A CB   1 
ATOM   8908  C  CG   . TYR   A 1 578 ? 9.935  39.505  7.402  1.00 12.06 ? 578  TYR   A CG   1 
ATOM   8909  C  CD1  . TYR   A 1 578 ? 9.504  39.589  8.723  1.00 11.38 ? 578  TYR   A CD1  1 
ATOM   8910  C  CD2  . TYR   A 1 578 ? 11.286 39.746  7.132  1.00 12.10 ? 578  TYR   A CD2  1 
ATOM   8911  C  CE1  . TYR   A 1 578 ? 10.390 39.891  9.750  1.00 12.70 ? 578  TYR   A CE1  1 
ATOM   8912  C  CE2  . TYR   A 1 578 ? 12.179 40.047  8.160  1.00 13.50 ? 578  TYR   A CE2  1 
ATOM   8913  C  CZ   . TYR   A 1 578 ? 11.720 40.117  9.465  1.00 13.28 ? 578  TYR   A CZ   1 
ATOM   8914  O  OH   . TYR   A 1 578 ? 12.592 40.418  10.492 1.00 13.15 ? 578  TYR   A OH   1 
ATOM   8915  H  H    . TYR   A 1 578 ? 7.297  39.231  4.449  1.00 15.06 ? 578  TYR   A H    1 
ATOM   8916  H  HA   . TYR   A 1 578 ? 7.601  40.686  6.597  1.00 17.38 ? 578  TYR   A HA   1 
ATOM   8917  H  HB2  . TYR   A 1 578 ? 8.361  38.472  6.578  1.00 16.84 ? 578  TYR   A HB2  1 
ATOM   8918  H  HB3  . TYR   A 1 578 ? 9.450  38.832  5.521  1.00 16.84 ? 578  TYR   A HB3  1 
ATOM   8919  H  HD1  . TYR   A 1 578 ? 8.608  39.440  8.922  1.00 13.66 ? 578  TYR   A HD1  1 
ATOM   8920  H  HD2  . TYR   A 1 578 ? 11.593 39.705  6.255  1.00 14.52 ? 578  TYR   A HD2  1 
ATOM   8921  H  HE1  . TYR   A 1 578 ? 10.087 39.941  10.628 1.00 15.24 ? 578  TYR   A HE1  1 
ATOM   8922  H  HE2  . TYR   A 1 578 ? 13.077 40.200  7.971  1.00 16.21 ? 578  TYR   A HE2  1 
ATOM   8923  H  HH   . TYR   A 1 578 ? 12.272 40.146  11.220 1.00 15.78 ? 578  TYR   A HH   1 
ATOM   8924  N  N    . TYR   A 1 579 ? 9.644  41.423  4.223  1.00 14.15 ? 579  TYR   A N    1 
ATOM   8925  C  CA   . TYR   A 1 579 ? 10.440 42.541  3.715  1.00 15.25 ? 579  TYR   A CA   1 
ATOM   8926  C  C    . TYR   A 1 579 ? 9.606  43.819  3.644  1.00 16.55 ? 579  TYR   A C    1 
ATOM   8927  O  O    . TYR   A 1 579 ? 10.078 44.906  4.001  1.00 15.57 ? 579  TYR   A O    1 
ATOM   8928  C  CB   . TYR   A 1 579 ? 11.008 42.220  2.325  1.00 13.98 ? 579  TYR   A CB   1 
ATOM   8929  C  CG   . TYR   A 1 579 ? 12.012 41.077  2.253  1.00 13.75 ? 579  TYR   A CG   1 
ATOM   8930  C  CD1  . TYR   A 1 579 ? 12.749 40.682  3.363  1.00 13.61 ? 579  TYR   A CD1  1 
ATOM   8931  C  CD2  . TYR   A 1 579 ? 12.223 40.403  1.053  1.00 15.43 ? 579  TYR   A CD2  1 
ATOM   8932  C  CE1  . TYR   A 1 579 ? 13.665 39.632  3.281  1.00 14.40 ? 579  TYR   A CE1  1 
ATOM   8933  C  CE2  . TYR   A 1 579 ? 13.135 39.364  0.962  1.00 15.98 ? 579  TYR   A CE2  1 
ATOM   8934  C  CZ   . TYR   A 1 579 ? 13.851 38.981  2.075  1.00 14.19 ? 579  TYR   A CZ   1 
ATOM   8935  O  OH   . TYR   A 1 579 ? 14.750 37.942  1.974  1.00 14.88 ? 579  TYR   A OH   1 
ATOM   8936  H  H    . TYR   A 1 579 ? 9.608  40.733  3.711  1.00 16.98 ? 579  TYR   A H    1 
ATOM   8937  H  HA   . TYR   A 1 579 ? 11.175 42.680  4.332  1.00 18.31 ? 579  TYR   A HA   1 
ATOM   8938  H  HB2  . TYR   A 1 579 ? 10.267 42.012  1.734  1.00 16.77 ? 579  TYR   A HB2  1 
ATOM   8939  H  HB3  . TYR   A 1 579 ? 11.432 43.020  1.977  1.00 16.77 ? 579  TYR   A HB3  1 
ATOM   8940  H  HD1  . TYR   A 1 579 ? 12.630 41.124  4.173  1.00 16.33 ? 579  TYR   A HD1  1 
ATOM   8941  H  HD2  . TYR   A 1 579 ? 11.742 40.655  0.298  1.00 18.52 ? 579  TYR   A HD2  1 
ATOM   8942  H  HE1  . TYR   A 1 579 ? 14.147 39.372  4.032  1.00 17.28 ? 579  TYR   A HE1  1 
ATOM   8943  H  HE2  . TYR   A 1 579 ? 13.264 38.926  0.152  1.00 19.18 ? 579  TYR   A HE2  1 
ATOM   8944  H  HH   . TYR   A 1 579 ? 15.261 37.948  2.640  1.00 17.86 ? 579  TYR   A HH   1 
ATOM   8945  N  N    . SER   A 1 580 ? 8.356  43.704  3.194  1.00 15.42 ? 580  SER   A N    1 
ATOM   8946  C  CA   . SER   A 1 580 ? 7.524  44.888  3.012  1.00 16.02 ? 580  SER   A CA   1 
ATOM   8947  C  C    . SER   A 1 580 ? 7.226  45.573  4.341  1.00 15.73 ? 580  SER   A C    1 
ATOM   8948  O  O    . SER   A 1 580 ? 7.343  46.799  4.459  1.00 13.58 ? 580  SER   A O    1 
ATOM   8949  C  CB   . SER   A 1 580 ? 6.230  44.515  2.292  1.00 18.19 ? 580  SER   A CB   1 
ATOM   8950  O  OG   . SER   A 1 580 ? 5.405  45.657  2.152  1.00 22.01 ? 580  SER   A OG   1 
ATOM   8951  H  H    . SER   A 1 580 ? 7.977  42.959  2.991  1.00 18.50 ? 580  SER   A H    1 
ATOM   8952  H  HA   . SER   A 1 580 ? 8.016  45.520  2.465  1.00 19.22 ? 580  SER   A HA   1 
ATOM   8953  H  HB2  . SER   A 1 580 ? 6.433  44.144  1.419  1.00 21.83 ? 580  SER   A HB2  1 
ATOM   8954  H  HB3  . SER   A 1 580 ? 5.761  43.827  2.790  1.00 21.83 ? 580  SER   A HB3  1 
ATOM   8955  H  HG   . SER   A 1 580 ? 4.945  45.758  2.848  1.00 26.42 ? 580  SER   A HG   1 
ATOM   8956  N  N    . VAL   A 1 581 ? 6.845  44.800  5.364  1.00 15.38 ? 581  VAL   A N    1 
ATOM   8957  C  CA   . VAL   A 1 581 ? 6.524  45.427  6.643  1.00 16.70 ? 581  VAL   A CA   1 
ATOM   8958  C  C    . VAL   A 1 581 ? 7.777  45.958  7.331  1.00 15.03 ? 581  VAL   A C    1 
ATOM   8959  O  O    . VAL   A 1 581 ? 7.682  46.862  8.168  1.00 14.54 ? 581  VAL   A O    1 
ATOM   8960  C  CB   . VAL   A 1 581 ? 5.757  44.462  7.572  1.00 16.02 ? 581  VAL   A CB   1 
ATOM   8961  C  CG1  . VAL   A 1 581 ? 4.454  44.014  6.915  1.00 20.11 ? 581  VAL   A CG1  1 
ATOM   8962  C  CG2  . VAL   A 1 581 ? 6.623  43.276  7.962  1.00 16.00 ? 581  VAL   A CG2  1 
ATOM   8963  H  H    . VAL   A 1 581 ? 6.769  43.944  5.339  1.00 18.46 ? 581  VAL   A H    1 
ATOM   8964  H  HA   . VAL   A 1 581 ? 5.943  46.180  6.454  1.00 20.04 ? 581  VAL   A HA   1 
ATOM   8965  H  HB   . VAL   A 1 581 ? 5.532  44.935  8.389  1.00 19.23 ? 581  VAL   A HB   1 
ATOM   8966  H  HG11 . VAL   A 1 581 ? 3.983  43.409  7.509  1.00 24.13 ? 581  VAL   A HG11 1 
ATOM   8967  H  HG12 . VAL   A 1 581 ? 3.898  44.789  6.736  1.00 24.13 ? 581  VAL   A HG12 1 
ATOM   8968  H  HG13 . VAL   A 1 581 ? 4.651  43.559  6.081  1.00 24.13 ? 581  VAL   A HG13 1 
ATOM   8969  H  HG21 . VAL   A 1 581 ? 6.120  42.685  8.544  1.00 19.21 ? 581  VAL   A HG21 1 
ATOM   8970  H  HG22 . VAL   A 1 581 ? 6.889  42.793  7.164  1.00 19.21 ? 581  VAL   A HG22 1 
ATOM   8971  H  HG23 . VAL   A 1 581 ? 7.414  43.591  8.427  1.00 19.21 ? 581  VAL   A HG23 1 
ATOM   8972  N  N    . ARG   A 1 582 ? 8.955  45.432  6.988  1.00 15.10 ? 582  ARG   A N    1 
ATOM   8973  C  CA   . ARG   A 1 582 ? 10.204 45.969  7.514  1.00 14.37 ? 582  ARG   A CA   1 
ATOM   8974  C  C    . ARG   A 1 582 ? 10.615 47.277  6.842  1.00 14.63 ? 582  ARG   A C    1 
ATOM   8975  O  O    . ARG   A 1 582 ? 11.535 47.945  7.334  1.00 13.29 ? 582  ARG   A O    1 
ATOM   8976  C  CB   . ARG   A 1 582 ? 11.327 44.941  7.352  1.00 12.90 ? 582  ARG   A CB   1 
ATOM   8977  C  CG   . ARG   A 1 582 ? 11.263 43.750  8.320  1.00 13.36 ? 582  ARG   A CG   1 
ATOM   8978  C  CD   . ARG   A 1 582 ? 12.645 43.427  8.861  1.00 12.67 ? 582  ARG   A CD   1 
ATOM   8979  N  NE   . ARG   A 1 582 ? 13.071 44.395  9.867  1.00 13.66 ? 582  ARG   A NE   1 
ATOM   8980  C  CZ   . ARG   A 1 582 ? 12.995 44.197  11.177 1.00 12.03 ? 582  ARG   A CZ   1 
ATOM   8981  N  NH1  . ARG   A 1 582 ? 12.606 43.032  11.680 1.00 14.99 ? 582  ARG   A NH1  1 
ATOM   8982  N  NH2  . ARG   A 1 582 ? 13.337 45.182  12.002 1.00 12.41 ? 582  ARG   A NH2  1 
ATOM   8983  H  H    . ARG   A 1 582 ? 9.049  44.765  6.453  1.00 18.13 ? 582  ARG   A H    1 
ATOM   8984  H  HA   . ARG   A 1 582 ? 10.053 46.159  8.453  1.00 17.25 ? 582  ARG   A HA   1 
ATOM   8985  H  HB2  . ARG   A 1 582 ? 11.309 44.603  6.443  1.00 15.48 ? 582  ARG   A HB2  1 
ATOM   8986  H  HB3  . ARG   A 1 582 ? 12.178 45.391  7.470  1.00 15.48 ? 582  ARG   A HB3  1 
ATOM   8987  H  HG2  . ARG   A 1 582 ? 10.663 43.955  9.054  1.00 16.04 ? 582  ARG   A HG2  1 
ATOM   8988  H  HG3  . ARG   A 1 582 ? 10.899 42.975  7.864  1.00 16.04 ? 582  ARG   A HG3  1 
ATOM   8989  H  HD2  . ARG   A 1 582 ? 12.641 42.538  9.248  1.00 15.21 ? 582  ARG   A HD2  1 
ATOM   8990  H  HD3  . ARG   A 1 582 ? 13.284 43.416  8.131  1.00 15.21 ? 582  ARG   A HD3  1 
ATOM   8991  H  HE   . ARG   A 1 582 ? 13.393 45.144  9.592  1.00 16.40 ? 582  ARG   A HE   1 
ATOM   8992  H  HH11 . ARG   A 1 582 ? 12.396 42.385  11.154 1.00 17.99 ? 582  ARG   A HH11 1 
ATOM   8993  H  HH12 . ARG   A 1 582 ? 12.564 42.924  12.532 1.00 17.99 ? 582  ARG   A HH12 1 
ATOM   8994  H  HH21 . ARG   A 1 582 ? 13.603 45.936  11.685 1.00 14.90 ? 582  ARG   A HH21 1 
ATOM   8995  H  HH22 . ARG   A 1 582 ? 13.292 45.065  12.853 1.00 14.90 ? 582  ARG   A HH22 1 
ATOM   8996  N  N    . GLY   A 1 583 ? 9.962  47.664  5.749  1.00 17.34 ? 583  GLY   A N    1 
ATOM   8997  C  CA   . GLY   A 1 583 ? 10.421 48.805  4.978  1.00 16.76 ? 583  GLY   A CA   1 
ATOM   8998  C  C    . GLY   A 1 583 ? 11.651 48.504  4.150  1.00 18.15 ? 583  GLY   A C    1 
ATOM   8999  O  O    . GLY   A 1 583 ? 12.462 49.403  3.895  1.00 16.43 ? 583  GLY   A O    1 
ATOM   9000  H  H    . GLY   A 1 583 ? 9.256  47.280  5.442  1.00 20.81 ? 583  GLY   A H    1 
ATOM   9001  H  HA2  . GLY   A 1 583 ? 9.707  49.101  4.392  1.00 20.11 ? 583  GLY   A HA2  1 
ATOM   9002  H  HA3  . GLY   A 1 583 ? 10.615 49.539  5.581  1.00 20.11 ? 583  GLY   A HA3  1 
ATOM   9003  N  N    . TRP   A 1 584 ? 11.779 47.243  3.742  1.00 16.87 ? 584  TRP   A N    1 
ATOM   9004  C  CA   . TRP   A 1 584 ? 12.914 46.842  2.880  1.00 14.23 ? 584  TRP   A CA   1 
ATOM   9005  C  C    . TRP   A 1 584 ? 12.414 46.611  1.451  1.00 16.34 ? 584  TRP   A C    1 
ATOM   9006  O  O    . TRP   A 1 584 ? 11.192 46.503  1.265  1.00 17.21 ? 584  TRP   A O    1 
ATOM   9007  C  CB   . TRP   A 1 584 ? 13.602 45.581  3.418  1.00 14.98 ? 584  TRP   A CB   1 
ATOM   9008  C  CG   . TRP   A 1 584 ? 14.154 45.693  4.805  1.00 15.70 ? 584  TRP   A CG   1 
ATOM   9009  C  CD1  . TRP   A 1 584 ? 14.183 46.799  5.604  1.00 14.33 ? 584  TRP   A CD1  1 
ATOM   9010  C  CD2  . TRP   A 1 584 ? 14.768 44.637  5.565  1.00 15.40 ? 584  TRP   A CD2  1 
ATOM   9011  N  NE1  . TRP   A 1 584 ? 14.772 46.505  6.804  1.00 15.73 ? 584  TRP   A NE1  1 
ATOM   9012  C  CE2  . TRP   A 1 584 ? 15.141 45.186  6.810  1.00 14.53 ? 584  TRP   A CE2  1 
ATOM   9013  C  CE3  . TRP   A 1 584 ? 15.038 43.288  5.315  1.00 14.48 ? 584  TRP   A CE3  1 
ATOM   9014  C  CZ2  . TRP   A 1 584 ? 15.768 44.429  7.798  1.00 13.74 ? 584  TRP   A CZ2  1 
ATOM   9015  C  CZ3  . TRP   A 1 584 ? 15.657 42.542  6.291  1.00 12.79 ? 584  TRP   A CZ3  1 
ATOM   9016  C  CH2  . TRP   A 1 584 ? 16.014 43.106  7.515  1.00 15.94 ? 584  TRP   A CH2  1 
ATOM   9017  H  H    . TRP   A 1 584 ? 11.235 46.608  3.944  1.00 20.25 ? 584  TRP   A H    1 
ATOM   9018  H  HA   . TRP   A 1 584 ? 13.570 47.557  2.880  1.00 17.08 ? 584  TRP   A HA   1 
ATOM   9019  H  HB2  . TRP   A 1 584 ? 12.965 44.850  3.398  1.00 17.98 ? 584  TRP   A HB2  1 
ATOM   9020  H  HB3  . TRP   A 1 584 ? 14.325 45.344  2.817  1.00 17.98 ? 584  TRP   A HB3  1 
ATOM   9021  H  HD1  . TRP   A 1 584 ? 13.850 47.634  5.367  1.00 17.19 ? 584  TRP   A HD1  1 
ATOM   9022  H  HE1  . TRP   A 1 584 ? 14.891 47.059  7.450  1.00 18.88 ? 584  TRP   A HE1  1 
ATOM   9023  H  HE3  . TRP   A 1 584 ? 14.803 42.902  4.502  1.00 17.38 ? 584  TRP   A HE3  1 
ATOM   9024  H  HZ2  . TRP   A 1 584 ? 16.010 44.803  8.614  1.00 16.49 ? 584  TRP   A HZ2  1 
ATOM   9025  H  HZ3  . TRP   A 1 584 ? 15.841 41.644  6.131  1.00 15.35 ? 584  TRP   A HZ3  1 
ATOM   9026  H  HH2  . TRP   A 1 584 ? 16.429 42.575  8.156  1.00 19.13 ? 584  TRP   A HH2  1 
ATOM   9027  N  N    . SER   A 1 585 ? 13.338 46.484  0.507  1.00 15.17 ? 585  SER   A N    1 
ATOM   9028  C  CA   . SER   A 1 585 ? 12.993 46.253  -0.912 1.00 18.05 ? 585  SER   A CA   1 
ATOM   9029  C  C    . SER   A 1 585 ? 12.513 44.817  -1.129 1.00 16.31 ? 585  SER   A C    1 
ATOM   9030  O  O    . SER   A 1 585 ? 12.535 44.027  -0.171 1.00 15.40 ? 585  SER   A O    1 
ATOM   9031  C  CB   . SER   A 1 585 ? 14.200 46.520  -1.764 1.00 17.09 ? 585  SER   A CB   1 
ATOM   9032  O  OG   . SER   A 1 585 ? 15.044 45.384  -1.821 1.00 14.65 ? 585  SER   A OG   1 
ATOM   9033  H  H    . SER   A 1 585 ? 14.183 46.528  0.660  1.00 18.21 ? 585  SER   A H    1 
ATOM   9034  H  HA   . SER   A 1 585 ? 12.274 46.854  -1.161 1.00 21.66 ? 585  SER   A HA   1 
ATOM   9035  H  HB2  . SER   A 1 585 ? 13.920 46.764  -2.660 1.00 20.51 ? 585  SER   A HB2  1 
ATOM   9036  H  HB3  . SER   A 1 585 ? 14.692 47.275  -1.405 1.00 20.51 ? 585  SER   A HB3  1 
ATOM   9037  H  HG   . SER   A 1 585 ? 15.627 45.497  -2.415 1.00 17.58 ? 585  SER   A HG   1 
ATOM   9038  N  N    . LYS   A 1 586 ? 12.119 44.498  -2.361 1.00 15.41 ? 586  LYS   A N    1 
ATOM   9039  C  CA   . LYS   A 1 586 ? 11.713 43.107  -2.691 1.00 18.18 ? 586  LYS   A CA   1 
ATOM   9040  C  C    . LYS   A 1 586 ? 12.950 42.204  -2.646 1.00 17.74 ? 586  LYS   A C    1 
ATOM   9041  O  O    . LYS   A 1 586 ? 12.763 40.994  -2.470 1.00 22.46 ? 586  LYS   A O    1 
ATOM   9042  C  CB   . LYS   A 1 586 ? 10.994 43.075  -4.043 1.00 21.02 ? 586  LYS   A CB   1 
ATOM   9043  C  CG   . LYS   A 1 586 ? 9.542  43.532  -4.010 1.00 21.16 ? 586  LYS   A CG   1 
ATOM   9044  C  CD   . LYS   A 1 586 ? 8.764  43.123  -5.241 1.00 29.86 ? 586  LYS   A CD   1 
ATOM   9045  C  CE   . LYS   A 1 586 ? 8.116  44.294  -5.947 1.00 33.59 ? 586  LYS   A CE   1 
ATOM   9046  N  NZ   . LYS   A 1 586 ? 7.684  43.935  -7.318 1.00 39.98 ? 586  LYS   A NZ   1 
ATOM   9047  H  H    . LYS   A 1 586 ? 12.076 45.053  -3.017 1.00 18.50 ? 586  LYS   A H    1 
ATOM   9048  H  HA   . LYS   A 1 586 ? 11.080 42.770  -2.038 1.00 21.82 ? 586  LYS   A HA   1 
ATOM   9049  H  HB2  . LYS   A 1 586 ? 11.481 43.636  -4.667 1.00 25.22 ? 586  LYS   A HB2  1 
ATOM   9050  H  HB3  . LYS   A 1 586 ? 11.026 42.170  -4.390 1.00 25.22 ? 586  LYS   A HB3  1 
ATOM   9051  H  HG2  . LYS   A 1 586 ? 9.110  43.163  -3.224 1.00 25.39 ? 586  LYS   A HG2  1 
ATOM   9052  H  HG3  . LYS   A 1 586 ? 9.514  44.498  -3.922 1.00 25.39 ? 586  LYS   A HG3  1 
ATOM   9053  H  HD2  . LYS   A 1 586 ? 9.359  42.669  -5.858 1.00 35.84 ? 586  LYS   A HD2  1 
ATOM   9054  H  HD3  . LYS   A 1 586 ? 8.079  42.485  -4.987 1.00 35.84 ? 586  LYS   A HD3  1 
ATOM   9055  H  HE2  . LYS   A 1 586 ? 7.350  44.598  -5.435 1.00 40.32 ? 586  LYS   A HE2  1 
ATOM   9056  H  HE3  . LYS   A 1 586 ? 8.741  45.034  -5.988 1.00 40.32 ? 586  LYS   A HE3  1 
ATOM   9057  H  HZ1  . LYS   A 1 586 ? 7.308  44.642  -7.706 1.00 47.98 ? 586  LYS   A HZ1  1 
ATOM   9058  H  HZ2  . LYS   A 1 586 ? 8.390  43.677  -7.794 1.00 47.98 ? 586  LYS   A HZ2  1 
ATOM   9059  H  HZ3  . LYS   A 1 586 ? 7.094  43.270  -7.279 1.00 47.98 ? 586  LYS   A HZ3  1 
ATOM   9060  N  N    . GLU   A 1 587 ? 14.152 42.755  -2.857 1.00 19.81 ? 587  GLU   A N    1 
ATOM   9061  C  CA   . GLU   A 1 587 ? 15.362 41.976  -2.674 1.00 20.47 ? 587  GLU   A CA   1 
ATOM   9062  C  C    . GLU   A 1 587 ? 15.853 42.017  -1.232 1.00 19.66 ? 587  GLU   A C    1 
ATOM   9063  O  O    . GLU   A 1 587 ? 16.988 41.605  -0.960 1.00 16.15 ? 587  GLU   A O    1 
ATOM   9064  C  CB   . GLU   A 1 587 ? 16.457 42.472  -3.628 1.00 24.24 ? 587  GLU   A CB   1 
ATOM   9065  C  CG   . GLU   A 1 587 ? 16.133 42.361  -5.133 1.00 26.77 ? 587  GLU   A CG   1 
ATOM   9066  C  CD   . GLU   A 1 587 ? 14.985 43.252  -5.593 1.00 32.08 ? 587  GLU   A CD   1 
ATOM   9067  O  OE1  . GLU   A 1 587 ? 14.906 44.420  -5.145 1.00 25.94 ? 587  GLU   A OE1  1 
ATOM   9068  O  OE2  . GLU   A 1 587 ? 14.172 42.788  -6.420 1.00 32.05 ? 587  GLU   A OE2  1 
ATOM   9069  H  H    . GLU   A 1 587 ? 14.279 43.569  -3.103 1.00 23.78 ? 587  GLU   A H    1 
ATOM   9070  H  HA   . GLU   A 1 587 ? 15.152 41.052  -2.881 1.00 24.57 ? 587  GLU   A HA   1 
ATOM   9071  H  HB2  . GLU   A 1 587 ? 16.646 43.401  -3.422 1.00 29.09 ? 587  GLU   A HB2  1 
ATOM   9072  H  HB3  . GLU   A 1 587 ? 17.269 41.971  -3.451 1.00 29.09 ? 587  GLU   A HB3  1 
ATOM   9073  H  HG2  . GLU   A 1 587 ? 16.928 42.586  -5.642 1.00 32.13 ? 587  GLU   A HG2  1 
ATOM   9074  H  HG3  . GLU   A 1 587 ? 15.916 41.438  -5.339 1.00 32.13 ? 587  GLU   A HG3  1 
ATOM   9075  N  N    . GLY   A 1 588 ? 15.014 42.509  -0.317 1.00 14.98 ? 588  GLY   A N    1 
ATOM   9076  C  CA   . GLY   A 1 588 ? 15.361 42.502  1.121  1.00 15.56 ? 588  GLY   A CA   1 
ATOM   9077  C  C    . GLY   A 1 588 ? 16.400 43.543  1.500  1.00 16.08 ? 588  GLY   A C    1 
ATOM   9078  O  O    . GLY   A 1 588 ? 17.095 43.345  2.503  1.00 16.15 ? 588  GLY   A O    1 
ATOM   9079  H  H    . GLY   A 1 588 ? 14.245 42.849  -0.499 1.00 17.98 ? 588  GLY   A H    1 
ATOM   9080  H  HA2  . GLY   A 1 588 ? 14.556 42.655  1.641  1.00 18.68 ? 588  GLY   A HA2  1 
ATOM   9081  H  HA3  . GLY   A 1 588 ? 15.692 41.623  1.362  1.00 18.68 ? 588  GLY   A HA3  1 
ATOM   9082  N  N    . ILE   A 1 589 ? 16.480 44.627  0.732  1.00 14.88 ? 589  ILE   A N    1 
ATOM   9083  C  CA   . ILE   A 1 589 ? 17.489 45.689  1.004  1.00 15.07 ? 589  ILE   A CA   1 
ATOM   9084  C  C    . ILE   A 1 589 ? 16.793 46.859  1.704  1.00 13.54 ? 589  ILE   A C    1 
ATOM   9085  O  O    . ILE   A 1 589 ? 15.849 47.419  1.127  1.00 15.60 ? 589  ILE   A O    1 
ATOM   9086  C  CB   . ILE   A 1 589 ? 18.187 46.114  -0.302 1.00 15.38 ? 589  ILE   A CB   1 
ATOM   9087  C  CG1  . ILE   A 1 589 ? 18.681 44.907  -1.102 1.00 16.04 ? 589  ILE   A CG1  1 
ATOM   9088  C  CG2  . ILE   A 1 589 ? 19.311 47.097  -0.011 1.00 19.14 ? 589  ILE   A CG2  1 
ATOM   9089  C  CD1  . ILE   A 1 589 ? 19.725 44.084  -0.386 1.00 19.32 ? 589  ILE   A CD1  1 
ATOM   9090  H  H    . ILE   A 1 589 ? 15.973 44.778  0.054  1.00 17.86 ? 589  ILE   A H    1 
ATOM   9091  H  HA   . ILE   A 1 589 ? 18.184 45.354  1.591  1.00 18.08 ? 589  ILE   A HA   1 
ATOM   9092  H  HB   . ILE   A 1 589 ? 17.532 46.565  -0.858 1.00 18.46 ? 589  ILE   A HB   1 
ATOM   9093  H  HG12 . ILE   A 1 589 ? 17.924 44.339  -1.314 1.00 19.26 ? 589  ILE   A HG12 1 
ATOM   9094  H  HG13 . ILE   A 1 589 ? 19.048 45.217  -1.945 1.00 19.26 ? 589  ILE   A HG13 1 
ATOM   9095  H  HG21 . ILE   A 1 589 ? 19.740 47.354  -0.842 1.00 22.97 ? 589  ILE   A HG21 1 
ATOM   9096  H  HG22 . ILE   A 1 589 ? 18.948 47.885  0.422  1.00 22.97 ? 589  ILE   A HG22 1 
ATOM   9097  H  HG23 . ILE   A 1 589 ? 19.963 46.679  0.573  1.00 22.97 ? 589  ILE   A HG23 1 
ATOM   9098  H  HD11 . ILE   A 1 589 ? 19.992 43.339  -0.948 1.00 23.19 ? 589  ILE   A HD11 1 
ATOM   9099  H  HD12 . ILE   A 1 589 ? 20.498 44.637  -0.195 1.00 23.19 ? 589  ILE   A HD12 1 
ATOM   9100  H  HD13 . ILE   A 1 589 ? 19.357 43.746  0.445  1.00 23.19 ? 589  ILE   A HD13 1 
ATOM   9101  N  N    . PRO   A 1 590 ? 17.210 47.240  2.929  1.00 14.89 ? 590  PRO   A N    1 
ATOM   9102  C  CA   . PRO   A 1 590 ? 16.622 48.386  3.613  1.00 16.91 ? 590  PRO   A CA   1 
ATOM   9103  C  C    . PRO   A 1 590 ? 16.603 49.624  2.703  1.00 17.61 ? 590  PRO   A C    1 
ATOM   9104  O  O    . PRO   A 1 590 ? 17.598 49.903  2.078  1.00 17.64 ? 590  PRO   A O    1 
ATOM   9105  C  CB   . PRO   A 1 590 ? 17.549 48.585  4.818  1.00 17.04 ? 590  PRO   A CB   1 
ATOM   9106  C  CG   . PRO   A 1 590 ? 18.096 47.204  5.088  1.00 15.67 ? 590  PRO   A CG   1 
ATOM   9107  C  CD   . PRO   A 1 590 ? 18.257 46.585  3.715  1.00 15.45 ? 590  PRO   A CD   1 
ATOM   9108  H  HA   . PRO   A 1 590 ? 15.697 48.247  3.869  1.00 20.30 ? 590  PRO   A HA   1 
ATOM   9109  H  HB2  . PRO   A 1 590 ? 18.259 49.216  4.620  1.00 20.45 ? 590  PRO   A HB2  1 
ATOM   9110  H  HB3  . PRO   A 1 590 ? 17.066 48.932  5.584  1.00 20.45 ? 590  PRO   A HB3  1 
ATOM   9111  H  HG2  . PRO   A 1 590 ? 18.943 47.245  5.558  1.00 18.81 ? 590  PRO   A HG2  1 
ATOM   9112  H  HG3  . PRO   A 1 590 ? 17.490 46.686  5.640  1.00 18.81 ? 590  PRO   A HG3  1 
ATOM   9113  H  HD2  . PRO   A 1 590 ? 19.139 46.752  3.347  1.00 18.54 ? 590  PRO   A HD2  1 
ATOM   9114  H  HD3  . PRO   A 1 590 ? 18.138 45.623  3.739  1.00 18.54 ? 590  PRO   A HD3  1 
ATOM   9115  N  N    . THR   A 1 591 ? 15.464 50.318  2.659  1.00 15.60 ? 591  THR   A N    1 
ATOM   9116  C  CA   . THR   A 1 591 ? 15.323 51.483  1.754  1.00 18.91 ? 591  THR   A CA   1 
ATOM   9117  C  C    . THR   A 1 591 ? 15.945 52.740  2.354  1.00 17.92 ? 591  THR   A C    1 
ATOM   9118  O  O    . THR   A 1 591 ? 16.195 52.768  3.569  1.00 18.43 ? 591  THR   A O    1 
ATOM   9119  C  CB   . THR   A 1 591 ? 13.849 51.776  1.444  1.00 17.68 ? 591  THR   A CB   1 
ATOM   9120  O  OG1  . THR   A 1 591 ? 13.200 52.194  2.645  1.00 17.75 ? 591  THR   A OG1  1 
ATOM   9121  C  CG2  . THR   A 1 591 ? 13.132 50.581  0.855  1.00 20.57 ? 591  THR   A CG2  1 
ATOM   9122  H  H    . THR   A 1 591 ? 14.768 50.142  3.133  1.00 18.73 ? 591  THR   A H    1 
ATOM   9123  H  HA   . THR   A 1 591 ? 15.790 51.250  0.936  1.00 22.69 ? 591  THR   A HA   1 
ATOM   9124  H  HB   . THR   A 1 591 ? 13.816 52.479  0.776  1.00 21.22 ? 591  THR   A HB   1 
ATOM   9125  H  HG1  . THR   A 1 591 ? 13.154 51.547  3.179  1.00 21.31 ? 591  THR   A HG1  1 
ATOM   9126  H  HG21 . THR   A 1 591 ? 12.207 50.814  0.677  1.00 24.69 ? 591  THR   A HG21 1 
ATOM   9127  H  HG22 . THR   A 1 591 ? 13.565 50.319  0.027  1.00 24.69 ? 591  THR   A HG22 1 
ATOM   9128  H  HG23 . THR   A 1 591 ? 13.164 49.843  1.483  1.00 24.69 ? 591  THR   A HG23 1 
ATOM   9129  N  N    . GLU   A 1 592 ? 16.161 53.746  1.508  1.00 18.37 ? 592  GLU   A N    1 
ATOM   9130  C  CA   . GLU   A 1 592 ? 16.665 55.028  1.978  1.00 19.01 ? 592  GLU   A CA   1 
ATOM   9131  C  C    . GLU   A 1 592 ? 15.752 55.634  3.040  1.00 17.97 ? 592  GLU   A C    1 
ATOM   9132  O  O    . GLU   A 1 592 ? 16.236 56.136  4.061  1.00 16.88 ? 592  GLU   A O    1 
ATOM   9133  C  CB   . GLU   A 1 592 ? 16.844 55.977  0.785  1.00 21.26 ? 592  GLU   A CB   1 
ATOM   9134  C  CG   . GLU   A 1 592 ? 17.009 57.441  1.146  1.00 23.34 ? 592  GLU   A CG   1 
ATOM   9135  C  CD   . GLU   A 1 592 ? 17.227 58.324  -0.080 1.00 20.81 ? 592  GLU   A CD   1 
ATOM   9136  O  OE1  . GLU   A 1 592 ? 18.067 57.960  -0.933 1.00 21.14 ? 592  GLU   A OE1  1 
ATOM   9137  O  OE2  . GLU   A 1 592 ? 16.557 59.371  -0.203 1.00 21.54 ? 592  GLU   A OE2  1 
ATOM   9138  H  H    . GLU   A 1 592 ? 16.021 53.704  0.660  1.00 22.05 ? 592  GLU   A H    1 
ATOM   9139  H  HA   . GLU   A 1 592 ? 17.528 54.888  2.399  1.00 22.81 ? 592  GLU   A HA   1 
ATOM   9140  H  HB2  . GLU   A 1 592 ? 17.621 55.694  0.278  1.00 25.51 ? 592  GLU   A HB2  1 
ATOM   9141  H  HB3  . GLU   A 1 592 ? 16.075 55.887  0.200  1.00 25.51 ? 592  GLU   A HB3  1 
ATOM   9142  H  HG2  . GLU   A 1 592 ? 16.221 57.744  1.623  1.00 28.01 ? 592  GLU   A HG2  1 
ATOM   9143  H  HG3  . GLU   A 1 592 ? 17.762 57.539  1.750  1.00 28.01 ? 592  GLU   A HG3  1 
ATOM   9144  N  N    . GLU   A 1 593 ? 14.428 55.588  2.832  1.00 19.69 ? 593  GLU   A N    1 
ATOM   9145  C  CA   . GLU   A 1 593 ? 13.525 56.149  3.841  1.00 20.64 ? 593  GLU   A CA   1 
ATOM   9146  C  C    . GLU   A 1 593 ? 13.632 55.393  5.156  1.00 18.92 ? 593  GLU   A C    1 
ATOM   9147  O  O    . GLU   A 1 593 ? 13.608 56.001  6.233  1.00 18.56 ? 593  GLU   A O    1 
ATOM   9148  C  CB   . GLU   A 1 593 ? 12.066 56.148  3.371  1.00 22.08 ? 593  GLU   A CB   1 
ATOM   9149  C  CG   . GLU   A 1 593 ? 11.821 56.562  1.945  1.00 27.49 ? 593  GLU   A CG   1 
ATOM   9150  C  CD   . GLU   A 1 593 ? 10.373 56.368  1.532  1.00 28.73 ? 593  GLU   A CD   1 
ATOM   9151  O  OE1  . GLU   A 1 593 ? 9.506  57.112  2.045  1.00 30.25 ? 593  GLU   A OE1  1 
ATOM   9152  O  OE2  . GLU   A 1 593 ? 10.099 55.465  0.715  1.00 28.63 ? 593  GLU   A OE2  1 
ATOM   9153  H  H    . GLU   A 1 593 ? 14.046 55.249  2.140  1.00 23.64 ? 593  GLU   A H    1 
ATOM   9154  H  HA   . GLU   A 1 593 ? 13.802 57.069  3.977  1.00 24.77 ? 593  GLU   A HA   1 
ATOM   9155  H  HB2  . GLU   A 1 593 ? 11.708 55.255  3.494  1.00 26.51 ? 593  GLU   A HB2  1 
ATOM   9156  H  HB3  . GLU   A 1 593 ? 11.560 56.739  3.950  1.00 26.51 ? 593  GLU   A HB3  1 
ATOM   9157  H  HG2  . GLU   A 1 593 ? 12.065 57.494  1.834  1.00 32.99 ? 593  GLU   A HG2  1 
ATOM   9158  H  HG3  . GLU   A 1 593 ? 12.395 56.047  1.357  1.00 32.99 ? 593  GLU   A HG3  1 
ATOM   9159  N  N    . THR   A 1 594 ? 13.749 54.068  5.087  1.00 16.32 ? 594  THR   A N    1 
ATOM   9160  C  CA   . THR   A 1 594 ? 13.840 53.273  6.308  1.00 18.95 ? 594  THR   A CA   1 
ATOM   9161  C  C    . THR   A 1 594 ? 15.123 53.581  7.064  1.00 16.35 ? 594  THR   A C    1 
ATOM   9162  O  O    . THR   A 1 594 ? 15.107 53.764  8.288  1.00 15.39 ? 594  THR   A O    1 
ATOM   9163  C  CB   . THR   A 1 594 ? 13.748 51.784  5.978  1.00 17.85 ? 594  THR   A CB   1 
ATOM   9164  O  OG1  . THR   A 1 594 ? 12.484 51.531  5.357  1.00 17.03 ? 594  THR   A OG1  1 
ATOM   9165  C  CG2  . THR   A 1 594 ? 13.863 50.945  7.257  1.00 17.39 ? 594  THR   A CG2  1 
ATOM   9166  H  H    . THR   A 1 594 ? 13.777 53.617  4.355  1.00 19.58 ? 594  THR   A H    1 
ATOM   9167  H  HA   . THR   A 1 594 ? 13.094 53.508  6.882  1.00 22.74 ? 594  THR   A HA   1 
ATOM   9168  H  HB   . THR   A 1 594 ? 14.473 51.541  5.381  1.00 21.42 ? 594  THR   A HB   1 
ATOM   9169  H  HG1  . THR   A 1 594 ? 12.491 50.767  5.009  1.00 20.44 ? 594  THR   A HG1  1 
ATOM   9170  H  HG21 . THR   A 1 594 ? 13.803 50.003  7.033  1.00 20.87 ? 594  THR   A HG21 1 
ATOM   9171  H  HG22 . THR   A 1 594 ? 14.716 51.122  7.684  1.00 20.87 ? 594  THR   A HG22 1 
ATOM   9172  H  HG23 . THR   A 1 594 ? 13.143 51.179  7.864  1.00 20.87 ? 594  THR   A HG23 1 
ATOM   9173  N  N    . LEU   A 1 595 ? 16.247 53.654  6.351  1.00 17.65 ? 595  LEU   A N    1 
ATOM   9174  C  CA   . LEU   A 1 595 ? 17.507 53.967  7.015  1.00 16.14 ? 595  LEU   A CA   1 
ATOM   9175  C  C    . LEU   A 1 595 ? 17.454 55.341  7.681  1.00 16.79 ? 595  LEU   A C    1 
ATOM   9176  O  O    . LEU   A 1 595 ? 17.931 55.508  8.809  1.00 19.30 ? 595  LEU   A O    1 
ATOM   9177  C  CB   . LEU   A 1 595 ? 18.664 53.880  6.017  1.00 15.66 ? 595  LEU   A CB   1 
ATOM   9178  C  CG   . LEU   A 1 595 ? 18.936 52.464  5.501  1.00 16.96 ? 595  LEU   A CG   1 
ATOM   9179  C  CD1  . LEU   A 1 595 ? 20.027 52.470  4.438  1.00 20.76 ? 595  LEU   A CD1  1 
ATOM   9180  C  CD2  . LEU   A 1 595 ? 19.311 51.533  6.654  1.00 17.35 ? 595  LEU   A CD2  1 
ATOM   9181  H  H    . LEU   A 1 595 ? 16.300 53.529  5.502  1.00 21.19 ? 595  LEU   A H    1 
ATOM   9182  H  HA   . LEU   A 1 595 ? 17.656 53.312  7.715  1.00 19.38 ? 595  LEU   A HA   1 
ATOM   9183  H  HB2  . LEU   A 1 595 ? 18.472 54.458  5.262  1.00 18.80 ? 595  LEU   A HB2  1 
ATOM   9184  H  HB3  . LEU   A 1 595 ? 19.469 54.221  6.438  1.00 18.80 ? 595  LEU   A HB3  1 
ATOM   9185  H  HG   . LEU   A 1 595 ? 18.121 52.132  5.092  1.00 20.36 ? 595  LEU   A HG   1 
ATOM   9186  H  HD11 . LEU   A 1 595 ? 20.181 51.564  4.127  1.00 24.92 ? 595  LEU   A HD11 1 
ATOM   9187  H  HD12 . LEU   A 1 595 ? 19.749 53.024  3.692  1.00 24.92 ? 595  LEU   A HD12 1 
ATOM   9188  H  HD13 . LEU   A 1 595 ? 20.846 52.825  4.817  1.00 24.92 ? 595  LEU   A HD13 1 
ATOM   9189  H  HD21 . LEU   A 1 595 ? 19.479 50.642  6.309  1.00 20.82 ? 595  LEU   A HD21 1 
ATOM   9190  H  HD22 . LEU   A 1 595 ? 20.110 51.866  7.092  1.00 20.82 ? 595  LEU   A HD22 1 
ATOM   9191  H  HD23 . LEU   A 1 595 ? 18.582 51.499  7.293  1.00 20.82 ? 595  LEU   A HD23 1 
ATOM   9192  N  N    . LYS   A 1 596 ? 16.861 56.333  7.009  1.00 17.10 ? 596  LYS   A N    1 
ATOM   9193  C  CA   . LYS   A 1 596 ? 16.698 57.644  7.638  1.00 21.23 ? 596  LYS   A CA   1 
ATOM   9194  C  C    . LYS   A 1 596 ? 15.815 57.557  8.876  1.00 19.02 ? 596  LYS   A C    1 
ATOM   9195  O  O    . LYS   A 1 596 ? 16.156 58.102  9.933  1.00 21.62 ? 596  LYS   A O    1 
ATOM   9196  C  CB   . LYS   A 1 596 ? 16.125 58.664  6.650  1.00 21.74 ? 596  LYS   A CB   1 
ATOM   9197  C  CG   . LYS   A 1 596 ? 16.936 58.876  5.386  1.00 25.36 ? 596  LYS   A CG   1 
ATOM   9198  C  CD   . LYS   A 1 596 ? 16.076 59.458  4.273  1.00 29.44 ? 596  LYS   A CD   1 
ATOM   9199  C  CE   . LYS   A 1 596 ? 16.573 60.829  3.834  1.00 34.25 ? 596  LYS   A CE   1 
ATOM   9200  N  NZ   . LYS   A 1 596 ? 17.945 60.784  3.255  1.00 41.59 ? 596  LYS   A NZ   1 
ATOM   9201  H  H    . LYS   A 1 596 ? 16.554 56.269  6.208  1.00 20.53 ? 596  LYS   A H    1 
ATOM   9202  H  HA   . LYS   A 1 596 ? 17.579 57.944  7.912  1.00 25.48 ? 596  LYS   A HA   1 
ATOM   9203  H  HB2  . LYS   A 1 596 ? 15.232 58.381  6.399  1.00 26.10 ? 596  LYS   A HB2  1 
ATOM   9204  H  HB3  . LYS   A 1 596 ? 16.035 59.516  7.105  1.00 26.10 ? 596  LYS   A HB3  1 
ATOM   9205  H  HG2  . LYS   A 1 596 ? 17.678 59.473  5.571  1.00 30.43 ? 596  LYS   A HG2  1 
ATOM   9206  H  HG3  . LYS   A 1 596 ? 17.316 58.032  5.097  1.00 30.43 ? 596  LYS   A HG3  1 
ATOM   9207  H  HD2  . LYS   A 1 596 ? 16.078 58.855  3.513  1.00 35.33 ? 596  LYS   A HD2  1 
ATOM   9208  H  HD3  . LYS   A 1 596 ? 15.158 59.529  4.577  1.00 35.33 ? 596  LYS   A HD3  1 
ATOM   9209  H  HE2  . LYS   A 1 596 ? 15.961 61.196  3.177  1.00 41.10 ? 596  LYS   A HE2  1 
ATOM   9210  H  HE3  . LYS   A 1 596 ? 16.567 61.430  4.595  1.00 41.10 ? 596  LYS   A HE3  1 
ATOM   9211  H  HZ1  . LYS   A 1 596 ? 18.024 61.411  2.629  1.00 49.91 ? 596  LYS   A HZ1  1 
ATOM   9212  H  HZ2  . LYS   A 1 596 ? 18.543 60.930  3.897  1.00 49.91 ? 596  LYS   A HZ2  1 
ATOM   9213  H  HZ3  . LYS   A 1 596 ? 18.088 59.984  2.893  1.00 49.91 ? 596  LYS   A HZ3  1 
ATOM   9214  N  N    . LYS   A 1 597 ? 14.703 56.834  8.782  1.00 17.57 ? 597  LYS   A N    1 
ATOM   9215  C  CA   . LYS   A 1 597 ? 13.767 56.748  9.932  1.00 18.04 ? 597  LYS   A CA   1 
ATOM   9216  C  C    . LYS   A 1 597 ? 14.452 56.085  11.131 1.00 19.28 ? 597  LYS   A C    1 
ATOM   9217  O  O    . LYS   A 1 597 ? 14.160 56.496  12.266 1.00 20.14 ? 597  LYS   A O    1 
ATOM   9218  C  CB   . LYS   A 1 597 ? 12.522 55.943  9.546  1.00 20.10 ? 597  LYS   A CB   1 
ATOM   9219  C  CG   . LYS   A 1 597 ? 11.533 55.701  10.677 1.00 24.87 ? 597  LYS   A CG   1 
ATOM   9220  C  CD   . LYS   A 1 597 ? 10.503 54.642  10.356 1.00 31.63 ? 597  LYS   A CD   1 
ATOM   9221  C  CE   . LYS   A 1 597 ? 11.105 53.393  9.750  1.00 29.67 ? 597  LYS   A CE   1 
ATOM   9222  N  NZ   . LYS   A 1 597 ? 10.147 52.264  9.770  1.00 34.89 ? 597  LYS   A NZ   1 
ATOM   9223  H  H    . LYS   A 1 597 ? 14.465 56.391  8.084  1.00 21.09 ? 597  LYS   A H    1 
ATOM   9224  H  HA   . LYS   A 1 597 ? 13.502 57.649  10.176 1.00 21.66 ? 597  LYS   A HA   1 
ATOM   9225  H  HB2  . LYS   A 1 597 ? 12.064 56.407  8.828  1.00 24.13 ? 597  LYS   A HB2  1 
ATOM   9226  H  HB3  . LYS   A 1 597 ? 12.805 55.085  9.194  1.00 24.13 ? 597  LYS   A HB3  1 
ATOM   9227  H  HG2  . LYS   A 1 597 ? 12.020 55.438  11.473 1.00 29.85 ? 597  LYS   A HG2  1 
ATOM   9228  H  HG3  . LYS   A 1 597 ? 11.079 56.533  10.884 1.00 29.85 ? 597  LYS   A HG3  1 
ATOM   9229  H  HD2  . LYS   A 1 597 ? 10.028 54.404  11.167 1.00 37.96 ? 597  LYS   A HD2  1 
ATOM   9230  H  HD3  . LYS   A 1 597 ? 9.849  55.010  9.742  1.00 37.96 ? 597  LYS   A HD3  1 
ATOM   9231  H  HE2  . LYS   A 1 597 ? 11.375 53.573  8.836  1.00 35.61 ? 597  LYS   A HE2  1 
ATOM   9232  H  HE3  . LYS   A 1 597 ? 11.906 53.148  10.240 1.00 35.61 ? 597  LYS   A HE3  1 
ATOM   9233  H  HZ1  . LYS   A 1 597 ? 10.589 51.501  9.893  1.00 41.87 ? 597  LYS   A HZ1  1 
ATOM   9234  H  HZ2  . LYS   A 1 597 ? 9.565  52.380  10.433 1.00 41.87 ? 597  LYS   A HZ2  1 
ATOM   9235  H  HZ3  . LYS   A 1 597 ? 9.710  52.231  8.995  1.00 41.87 ? 597  LYS   A HZ3  1 
ATOM   9236  N  N    . LEU   A 1 598 ? 15.326 55.106  10.884 1.00 15.38 ? 598  LEU   A N    1 
ATOM   9237  C  CA   . LEU   A 1 598 ? 15.925 54.334  12.009 1.00 20.87 ? 598  LEU   A CA   1 
ATOM   9238  C  C    . LEU   A 1 598 ? 17.208 55.000  12.526 1.00 18.37 ? 598  LEU   A C    1 
ATOM   9239  O  O    . LEU   A 1 598 ? 17.809 54.454  13.461 1.00 20.18 ? 598  LEU   A O    1 
ATOM   9240  C  CB   . LEU   A 1 598 ? 16.217 52.914  11.519 1.00 17.97 ? 598  LEU   A CB   1 
ATOM   9241  C  CG   . LEU   A 1 598 ? 14.989 52.039  11.279 1.00 17.10 ? 598  LEU   A CG   1 
ATOM   9242  C  CD1  . LEU   A 1 598 ? 15.398 50.665  10.772 1.00 16.43 ? 598  LEU   A CD1  1 
ATOM   9243  C  CD2  . LEU   A 1 598 ? 14.158 51.916  12.546 1.00 20.02 ? 598  LEU   A CD2  1 
ATOM   9244  H  H    . LEU   A 1 598 ? 15.587 54.869  10.099 1.00 18.46 ? 598  LEU   A H    1 
ATOM   9245  H  HA   . LEU   A 1 598 ? 15.299 54.310  12.749 1.00 25.05 ? 598  LEU   A HA   1 
ATOM   9246  H  HB2  . LEU   A 1 598 ? 16.722 52.971  10.692 1.00 21.56 ? 598  LEU   A HB2  1 
ATOM   9247  H  HB3  . LEU   A 1 598 ? 16.787 52.474  12.170 1.00 21.56 ? 598  LEU   A HB3  1 
ATOM   9248  H  HG   . LEU   A 1 598 ? 14.444 52.465  10.599 1.00 20.53 ? 598  LEU   A HG   1 
ATOM   9249  H  HD11 . LEU   A 1 598 ? 14.606 50.125  10.626 1.00 19.71 ? 598  LEU   A HD11 1 
ATOM   9250  H  HD12 . LEU   A 1 598 ? 15.883 50.759  9.937  1.00 19.71 ? 598  LEU   A HD12 1 
ATOM   9251  H  HD13 . LEU   A 1 598 ? 15.966 50.233  11.429 1.00 19.71 ? 598  LEU   A HD13 1 
ATOM   9252  H  HD21 . LEU   A 1 598 ? 13.384 51.357  12.373 1.00 24.03 ? 598  LEU   A HD21 1 
ATOM   9253  H  HD22 . LEU   A 1 598 ? 14.695 51.515  13.248 1.00 24.03 ? 598  LEU   A HD22 1 
ATOM   9254  H  HD23 . LEU   A 1 598 ? 13.864 52.797  12.827 1.00 24.03 ? 598  LEU   A HD23 1 
ATOM   9255  N  N    . GLY   A 1 599 ? 17.605 56.127  11.937 1.00 21.07 ? 599  GLY   A N    1 
ATOM   9256  C  CA   . GLY   A 1 599 ? 18.855 56.790  12.355 1.00 20.07 ? 599  GLY   A CA   1 
ATOM   9257  C  C    . GLY   A 1 599 ? 20.087 56.058  11.853 1.00 23.57 ? 599  GLY   A C    1 
ATOM   9258  O  O    . GLY   A 1 599 ? 21.135 56.164  12.511 1.00 22.21 ? 599  GLY   A O    1 
ATOM   9259  H  H    . GLY   A 1 599 ? 17.178 56.523  11.304 1.00 25.29 ? 599  GLY   A H    1 
ATOM   9260  H  HA2  . GLY   A 1 599 ? 18.863 57.701  12.021 1.00 24.09 ? 599  GLY   A HA2  1 
ATOM   9261  H  HA3  . GLY   A 1 599 ? 18.884 56.842  13.323 1.00 24.09 ? 599  GLY   A HA3  1 
ATOM   9262  N  N    . LEU   A 1 600 ? 19.973 55.348  10.730 1.00 20.11 ? 600  LEU   A N    1 
ATOM   9263  C  CA   . LEU   A 1 600 ? 21.096 54.630  10.134 1.00 20.50 ? 600  LEU   A CA   1 
ATOM   9264  C  C    . LEU   A 1 600 ? 21.595 55.348  8.883  1.00 21.90 ? 600  LEU   A C    1 
ATOM   9265  O  O    . LEU   A 1 600 ? 21.911 54.719  7.868  1.00 18.72 ? 600  LEU   A O    1 
ATOM   9266  C  CB   . LEU   A 1 600 ? 20.708 53.188  9.815  1.00 18.71 ? 600  LEU   A CB   1 
ATOM   9267  C  CG   . LEU   A 1 600 ? 20.454 52.301  11.033 1.00 18.96 ? 600  LEU   A CG   1 
ATOM   9268  C  CD1  . LEU   A 1 600 ? 19.775 50.987  10.646 1.00 16.52 ? 600  LEU   A CD1  1 
ATOM   9269  C  CD2  . LEU   A 1 600 ? 21.764 52.037  11.778 1.00 19.38 ? 600  LEU   A CD2  1 
ATOM   9270  H  H    . LEU   A 1 600 ? 19.237 55.270  10.292 1.00 24.13 ? 600  LEU   A H    1 
ATOM   9271  H  HA   . LEU   A 1 600 ? 21.820 54.611  10.779 1.00 24.60 ? 600  LEU   A HA   1 
ATOM   9272  H  HB2  . LEU   A 1 600 ? 19.908 53.197  9.266  1.00 22.46 ? 600  LEU   A HB2  1 
ATOM   9273  H  HB3  . LEU   A 1 600 ? 21.413 52.788  9.282  1.00 22.46 ? 600  LEU   A HB3  1 
ATOM   9274  H  HG   . LEU   A 1 600 ? 19.848 52.774  11.624 1.00 22.75 ? 600  LEU   A HG   1 
ATOM   9275  H  HD11 . LEU   A 1 600 ? 19.630 50.451  11.441 1.00 19.83 ? 600  LEU   A HD11 1 
ATOM   9276  H  HD12 . LEU   A 1 600 ? 18.922 51.175  10.223 1.00 19.83 ? 600  LEU   A HD12 1 
ATOM   9277  H  HD13 . LEU   A 1 600 ? 20.341 50.500  10.027 1.00 19.83 ? 600  LEU   A HD13 1 
ATOM   9278  H  HD21 . LEU   A 1 600 ? 21.591 51.474  12.548 1.00 23.26 ? 600  LEU   A HD21 1 
ATOM   9279  H  HD22 . LEU   A 1 600 ? 22.389 51.591  11.186 1.00 23.26 ? 600  LEU   A HD22 1 
ATOM   9280  H  HD23 . LEU   A 1 600 ? 22.144 52.879  12.073 1.00 23.26 ? 600  LEU   A HD23 1 
ATOM   9281  N  N    . ASP   A 1 601 ? 21.683 56.679  8.962  1.00 23.12 ? 601  ASP   A N    1 
ATOM   9282  C  CA   . ASP   A 1 601 ? 21.976 57.486  7.782  1.00 22.12 ? 601  ASP   A CA   1 
ATOM   9283  C  C    . ASP   A 1 601 ? 23.358 57.196  7.219  1.00 18.15 ? 601  ASP   A C    1 
ATOM   9284  O  O    . ASP   A 1 601 ? 23.573 57.347  6.012  1.00 21.09 ? 601  ASP   A O    1 
ATOM   9285  C  CB   . ASP   A 1 601 ? 21.838 58.976  8.107  1.00 22.07 ? 601  ASP   A CB   1 
ATOM   9286  C  CG   . ASP   A 1 601 ? 20.494 59.313  8.718  1.00 23.23 ? 601  ASP   A CG   1 
ATOM   9287  O  OD1  . ASP   A 1 601 ? 20.256 58.914  9.877  1.00 24.31 ? 601  ASP   A OD1  1 
ATOM   9288  O  OD2  . ASP   A 1 601 ? 19.676 59.972  8.041  1.00 28.03 ? 601  ASP   A OD2  1 
ATOM   9289  H  H    . ASP   A 1 601 ? 21.576 57.129  9.687  1.00 27.74 ? 601  ASP   A H    1 
ATOM   9290  H  HA   . ASP   A 1 601 ? 21.329 57.246  7.101  1.00 26.55 ? 601  ASP   A HA   1 
ATOM   9291  H  HB2  . ASP   A 1 601 ? 22.543 59.237  8.720  1.00 26.49 ? 601  ASP   A HB2  1 
ATOM   9292  H  HB3  . ASP   A 1 601 ? 21.960 59.494  7.296  1.00 26.49 ? 601  ASP   A HB3  1 
ATOM   9293  N  N    . GLU   A 1 602 ? 24.291 56.779  8.071  1.00 20.39 ? 602  GLU   A N    1 
ATOM   9294  C  CA   . GLU   A 1 602 ? 25.681 56.533  7.611  1.00 25.36 ? 602  GLU   A CA   1 
ATOM   9295  C  C    . GLU   A 1 602 ? 25.727 55.378  6.602  1.00 22.55 ? 602  GLU   A C    1 
ATOM   9296  O  O    . GLU   A 1 602 ? 26.766 55.223  5.951  1.00 25.13 ? 602  GLU   A O    1 
ATOM   9297  C  CB   . GLU   A 1 602 ? 26.586 56.237  8.809  1.00 27.67 ? 602  GLU   A CB   1 
ATOM   9298  C  CG   . GLU   A 1 602 ? 26.092 55.095  9.677  1.00 27.17 ? 602  GLU   A CG   1 
ATOM   9299  C  CD   . GLU   A 1 602 ? 26.927 54.858  10.923 1.00 33.49 ? 602  GLU   A CD   1 
ATOM   9300  O  OE1  . GLU   A 1 602 ? 28.084 54.421  10.782 1.00 39.05 ? 602  GLU   A OE1  1 
ATOM   9301  O  OE2  . GLU   A 1 602 ? 26.419 55.111  12.030 1.00 34.99 ? 602  GLU   A OE2  1 
ATOM   9302  H  H    . GLU   A 1 602 ? 24.155 56.631  8.907  1.00 24.47 ? 602  GLU   A H    1 
ATOM   9303  H  HA   . GLU   A 1 602 ? 26.003 57.332  7.166  1.00 30.43 ? 602  GLU   A HA   1 
ATOM   9304  H  HB2  . GLU   A 1 602 ? 27.477 56.027  8.488  1.00 33.21 ? 602  GLU   A HB2  1 
ATOM   9305  H  HB3  . GLU   A 1 602 ? 26.662 57.037  9.353  1.00 33.21 ? 602  GLU   A HB3  1 
ATOM   9306  H  HG2  . GLU   A 1 602 ? 25.177 55.276  9.942  1.00 32.61 ? 602  GLU   A HG2  1 
ATOM   9307  H  HG3  . GLU   A 1 602 ? 26.079 54.282  9.148  1.00 32.61 ? 602  GLU   A HG3  1 
ATOM   9308  N  N    . TYR   A 1 603 ? 24.648 54.597  6.481  1.00 20.37 ? 603  TYR   A N    1 
ATOM   9309  C  CA   . TYR   A 1 603 ? 24.672 53.411  5.586  1.00 19.51 ? 603  TYR   A CA   1 
ATOM   9310  C  C    . TYR   A 1 603 ? 23.870 53.676  4.306  1.00 22.08 ? 603  TYR   A C    1 
ATOM   9311  O  O    . TYR   A 1 603 ? 23.765 52.766  3.471  1.00 23.84 ? 603  TYR   A O    1 
ATOM   9312  C  CB   . TYR   A 1 603 ? 24.140 52.174  6.314  1.00 19.11 ? 603  TYR   A CB   1 
ATOM   9313  C  CG   . TYR   A 1 603 ? 24.917 51.827  7.557  1.00 19.73 ? 603  TYR   A CG   1 
ATOM   9314  C  CD1  . TYR   A 1 603 ? 26.137 51.178  7.475  1.00 20.14 ? 603  TYR   A CD1  1 
ATOM   9315  C  CD2  . TYR   A 1 603 ? 24.447 52.169  8.813  1.00 20.34 ? 603  TYR   A CD2  1 
ATOM   9316  C  CE1  . TYR   A 1 603 ? 26.865 50.867  8.610  1.00 19.47 ? 603  TYR   A CE1  1 
ATOM   9317  C  CE2  . TYR   A 1 603 ? 25.162 51.864  9.959  1.00 17.72 ? 603  TYR   A CE2  1 
ATOM   9318  C  CZ   . TYR   A 1 603 ? 26.376 51.211  9.856  1.00 21.07 ? 603  TYR   A CZ   1 
ATOM   9319  O  OH   . TYR   A 1 603 ? 27.091 50.907  10.987 1.00 19.27 ? 603  TYR   A OH   1 
ATOM   9320  H  H    . TYR   A 1 603 ? 23.905 54.725  6.894  1.00 24.45 ? 603  TYR   A H    1 
ATOM   9321  H  HA   . TYR   A 1 603 ? 25.593 53.242  5.333  1.00 23.41 ? 603  TYR   A HA   1 
ATOM   9322  H  HB2  . TYR   A 1 603 ? 23.212 52.322  6.553  1.00 22.94 ? 603  TYR   A HB2  1 
ATOM   9323  H  HB3  . TYR   A 1 603 ? 24.159 51.417  5.707  1.00 22.94 ? 603  TYR   A HB3  1 
ATOM   9324  H  HD1  . TYR   A 1 603 ? 26.474 50.946  6.640  1.00 24.18 ? 603  TYR   A HD1  1 
ATOM   9325  H  HD2  . TYR   A 1 603 ? 23.633 52.613  8.889  1.00 24.41 ? 603  TYR   A HD2  1 
ATOM   9326  H  HE1  . TYR   A 1 603 ? 27.681 50.428  8.535  1.00 23.37 ? 603  TYR   A HE1  1 
ATOM   9327  H  HE2  . TYR   A 1 603 ? 24.827 52.098  10.794 1.00 21.27 ? 603  TYR   A HE2  1 
ATOM   9328  H  HH   . TYR   A 1 603 ? 27.767 50.455  10.778 1.00 23.12 ? 603  TYR   A HH   1 
ATOM   9329  N  N    . ILE   A 1 604 ? 23.341 54.892  4.156  1.00 20.54 ? 604  ILE   A N    1 
ATOM   9330  C  CA   . ILE   A 1 604 ? 22.527 55.237  2.951  1.00 23.03 ? 604  ILE   A CA   1 
ATOM   9331  C  C    . ILE   A 1 604 ? 23.416 55.221  1.703  1.00 25.02 ? 604  ILE   A C    1 
ATOM   9332  O  O    . ILE   A 1 604 ? 24.535 55.757  1.778  1.00 26.71 ? 604  ILE   A O    1 
ATOM   9333  C  CB   . ILE   A 1 604 ? 21.823 56.594  3.137  1.00 23.54 ? 604  ILE   A CB   1 
ATOM   9334  C  CG1  . ILE   A 1 604 ? 20.709 56.514  4.183  1.00 25.78 ? 604  ILE   A CG1  1 
ATOM   9335  C  CG2  . ILE   A 1 604 ? 21.312 57.127  1.808  1.00 25.69 ? 604  ILE   A CG2  1 
ATOM   9336  C  CD1  . ILE   A 1 604 ? 20.091 57.849  4.517  1.00 24.39 ? 604  ILE   A CD1  1 
ATOM   9337  H  H    . ILE   A 1 604 ? 23.432 55.532  4.723  1.00 24.65 ? 604  ILE   A H    1 
ATOM   9338  H  HA   . ILE   A 1 604 ? 21.832 54.571  2.834  1.00 27.64 ? 604  ILE   A HA   1 
ATOM   9339  H  HB   . ILE   A 1 604 ? 22.479 57.224  3.474  1.00 28.25 ? 604  ILE   A HB   1 
ATOM   9340  H  HG12 . ILE   A 1 604 ? 20.016 55.918  3.860  1.00 30.95 ? 604  ILE   A HG12 1 
ATOM   9341  H  HG13 . ILE   A 1 604 ? 21.066 56.120  4.994  1.00 30.95 ? 604  ILE   A HG13 1 
ATOM   9342  H  HG21 . ILE   A 1 604 ? 20.873 57.981  1.949  1.00 30.83 ? 604  ILE   A HG21 1 
ATOM   9343  H  HG22 . ILE   A 1 604 ? 22.057 57.244  1.198  1.00 30.83 ? 604  ILE   A HG22 1 
ATOM   9344  H  HG23 . ILE   A 1 604 ? 20.679 56.497  1.428  1.00 30.83 ? 604  ILE   A HG23 1 
ATOM   9345  H  HD11 . ILE   A 1 604 ? 19.396 57.727  5.182  1.00 29.27 ? 604  ILE   A HD11 1 
ATOM   9346  H  HD12 . ILE   A 1 604 ? 20.773 58.443  4.868  1.00 29.27 ? 604  ILE   A HD12 1 
ATOM   9347  H  HD13 . ILE   A 1 604 ? 19.706 58.237  3.716  1.00 29.27 ? 604  ILE   A HD13 1 
ATOM   9348  N  N    . GLY   A 1 605 ? 22.944 54.606  0.615  1.00 25.24 ? 605  GLY   A N    1 
ATOM   9349  C  CA   . GLY   A 1 605 ? 23.684 54.602  -0.663 1.00 33.37 ? 605  GLY   A CA   1 
ATOM   9350  C  C    . GLY   A 1 605 ? 24.776 53.552  -0.727 1.00 33.82 ? 605  GLY   A C    1 
ATOM   9351  O  O    . GLY   A 1 605 ? 25.468 53.492  -1.757 1.00 36.54 ? 605  GLY   A O    1 
ATOM   9352  H  H    . GLY   A 1 605 ? 22.196 54.183  0.591  1.00 30.29 ? 605  GLY   A H    1 
ATOM   9353  H  HA2  . GLY   A 1 605 ? 23.059 54.453  -1.390 1.00 40.05 ? 605  GLY   A HA2  1 
ATOM   9354  H  HA3  . GLY   A 1 605 ? 24.078 55.477  -0.803 1.00 40.05 ? 605  GLY   A HA3  1 
ATOM   9355  N  N    . LYS   A 1 606 ? 24.916 52.738  0.319  1.00 32.73 ? 606  LYS   A N    1 
ATOM   9356  C  CA   . LYS   A 1 606 ? 26.035 51.763  0.363  1.00 33.69 ? 606  LYS   A CA   1 
ATOM   9357  C  C    . LYS   A 1 606 ? 25.536 50.359  -0.007 1.00 33.67 ? 606  LYS   A C    1 
ATOM   9358  O  O    . LYS   A 1 606 ? 26.383 49.482  -0.251 1.00 36.35 ? 606  LYS   A O    1 
ATOM   9359  C  CB   . LYS   A 1 606 ? 26.690 51.817  1.747  1.00 37.68 ? 606  LYS   A CB   1 
ATOM   9360  C  CG   . LYS   A 1 606 ? 26.757 53.199  2.380  1.00 38.24 ? 606  LYS   A CG   1 
ATOM   9361  C  CD   . LYS   A 1 606 ? 28.120 53.839  2.256  1.00 43.46 ? 606  LYS   A CD   1 
ATOM   9362  C  CE   . LYS   A 1 606 ? 28.422 54.805  3.381  1.00 46.11 ? 606  LYS   A CE   1 
ATOM   9363  N  NZ   . LYS   A 1 606 ? 29.332 55.889  2.943  1.00 57.95 ? 606  LYS   A NZ   1 
ATOM   9364  H  H    . LYS   A 1 606 ? 24.394 52.725  1.002  1.00 39.28 ? 606  LYS   A H    1 
ATOM   9365  H  HA   . LYS   A 1 606 ? 26.711 51.994  -0.294 1.00 40.43 ? 606  LYS   A HA   1 
ATOM   9366  H  HB2  . LYS   A 1 606 ? 26.202 51.228  2.343  1.00 45.22 ? 606  LYS   A HB2  1 
ATOM   9367  H  HB3  . LYS   A 1 606 ? 27.591 51.466  1.676  1.00 45.22 ? 606  LYS   A HB3  1 
ATOM   9368  H  HG2  . LYS   A 1 606 ? 26.096 53.773  1.962  1.00 45.89 ? 606  LYS   A HG2  1 
ATOM   9369  H  HG3  . LYS   A 1 606 ? 26.521 53.131  3.318  1.00 45.89 ? 606  LYS   A HG3  1 
ATOM   9370  H  HD2  . LYS   A 1 606 ? 28.798 53.145  2.241  1.00 52.15 ? 606  LYS   A HD2  1 
ATOM   9371  H  HD3  . LYS   A 1 606 ? 28.176 54.309  1.409  1.00 52.15 ? 606  LYS   A HD3  1 
ATOM   9372  H  HE2  . LYS   A 1 606 ? 27.594 55.190  3.708  1.00 55.33 ? 606  LYS   A HE2  1 
ATOM   9373  H  HE3  . LYS   A 1 606 ? 28.824 54.324  4.122  1.00 55.33 ? 606  LYS   A HE3  1 
ATOM   9374  H  HZ1  . LYS   A 1 606 ? 29.490 56.438  3.625  1.00 69.54 ? 606  LYS   A HZ1  1 
ATOM   9375  H  HZ2  . LYS   A 1 606 ? 30.100 55.537  2.663  1.00 69.54 ? 606  LYS   A HZ2  1 
ATOM   9376  H  HZ3  . LYS   A 1 606 ? 28.954 56.344  2.278  1.00 69.54 ? 606  LYS   A HZ3  1 
ATOM   9377  N  N    . PHE   A 1 607 ? 24.222 50.129  -0.035 1.00 30.83 ? 607  PHE   A N    1 
ATOM   9378  C  CA   . PHE   A 1 607 ? 23.716 48.753  -0.291 1.00 31.52 ? 607  PHE   A CA   1 
ATOM   9379  C  C    . PHE   A 1 607 ? 22.679 48.764  -1.423 1.00 38.06 ? 607  PHE   A C    1 
ATOM   9380  O  O    . PHE   A 1 607 ? 22.423 47.722  -2.017 1.00 36.44 ? 607  PHE   A O    1 
ATOM   9381  C  CB   . PHE   A 1 607 ? 23.142 48.153  0.996  1.00 34.48 ? 607  PHE   A CB   1 
ATOM   9382  C  CG   . PHE   A 1 607 ? 24.129 48.072  2.132  1.00 28.60 ? 607  PHE   A CG   1 
ATOM   9383  C  CD1  . PHE   A 1 607 ? 24.333 49.153  2.973  1.00 33.59 ? 607  PHE   A CD1  1 
ATOM   9384  C  CD2  . PHE   A 1 607 ? 24.865 46.919  2.350  1.00 25.92 ? 607  PHE   A CD2  1 
ATOM   9385  C  CE1  . PHE   A 1 607 ? 25.246 49.080  4.013  1.00 28.08 ? 607  PHE   A CE1  1 
ATOM   9386  C  CE2  . PHE   A 1 607 ? 25.777 46.848  3.390  1.00 23.27 ? 607  PHE   A CE2  1 
ATOM   9387  C  CZ   . PHE   A 1 607 ? 25.964 47.928  4.220  1.00 26.17 ? 607  PHE   A CZ   1 
ATOM   9388  O  OXT  . PHE   A 1 607 ? 22.145 49.843  -1.681 1.00 29.21 ? 607  PHE   A OXT  1 
ATOM   9389  H  H    . PHE   A 1 607 ? 23.615 50.727  0.086  1.00 37.00 ? 607  PHE   A H    1 
ATOM   9390  H  HA   . PHE   A 1 607 ? 24.454 48.192  -0.577 1.00 37.83 ? 607  PHE   A HA   1 
ATOM   9391  H  HB2  . PHE   A 1 607 ? 22.382 48.685  1.278  1.00 41.38 ? 607  PHE   A HB2  1 
ATOM   9392  H  HB3  . PHE   A 1 607 ? 22.809 47.262  0.805  1.00 41.38 ? 607  PHE   A HB3  1 
ATOM   9393  H  HD1  . PHE   A 1 607 ? 23.852 49.937  2.838  1.00 40.31 ? 607  PHE   A HD1  1 
ATOM   9394  H  HD2  . PHE   A 1 607 ? 24.746 46.185  1.792  1.00 31.11 ? 607  PHE   A HD2  1 
ATOM   9395  H  HE1  . PHE   A 1 607 ? 25.373 49.813  4.572  1.00 33.70 ? 607  PHE   A HE1  1 
ATOM   9396  H  HE2  . PHE   A 1 607 ? 26.264 46.068  3.527  1.00 27.93 ? 607  PHE   A HE2  1 
ATOM   9397  H  HZ   . PHE   A 1 607 ? 26.575 47.878  4.919  1.00 31.41 ? 607  PHE   A HZ   1 
ATOM   9398  N  N    . MET   B 1 1   ? 31.187 -5.564  54.363 1.00 37.89 ? 1    MET   B N    1 
ATOM   9399  C  CA   . MET   B 1 1   ? 29.904 -5.946  55.008 1.00 36.84 ? 1    MET   B CA   1 
ATOM   9400  C  C    . MET   B 1 1   ? 28.747 -5.291  54.249 1.00 32.90 ? 1    MET   B C    1 
ATOM   9401  O  O    . MET   B 1 1   ? 29.030 -4.531  53.310 1.00 34.05 ? 1    MET   B O    1 
ATOM   9402  C  CB   . MET   B 1 1   ? 29.865 -5.477  56.465 1.00 32.92 ? 1    MET   B CB   1 
ATOM   9403  C  CG   . MET   B 1 1   ? 31.211 -5.487  57.148 1.00 34.93 ? 1    MET   B CG   1 
ATOM   9404  S  SD   . MET   B 1 1   ? 31.041 -5.049  58.890 1.00 35.36 ? 1    MET   B SD   1 
ATOM   9405  C  CE   . MET   B 1 1   ? 32.481 -5.860  59.583 1.00 35.24 ? 1    MET   B CE   1 
ATOM   9406  H  H1   . MET   B 1 1   ? 31.833 -6.110  54.640 1.00 45.47 ? 1    MET   B H1   1 
ATOM   9407  H  H2   . MET   B 1 1   ? 31.105 -5.627  53.479 1.00 45.47 ? 1    MET   B H2   1 
ATOM   9408  H  H3   . MET   B 1 1   ? 31.392 -4.726  54.583 1.00 45.47 ? 1    MET   B H3   1 
ATOM   9409  H  HA   . MET   B 1 1   ? 29.824 -6.912  54.987 1.00 44.21 ? 1    MET   B HA   1 
ATOM   9410  H  HB2  . MET   B 1 1   ? 29.503 -4.578  56.496 1.00 39.50 ? 1    MET   B HB2  1 
ATOM   9411  H  HB3  . MET   B 1 1   ? 29.256 -6.045  56.962 1.00 39.50 ? 1    MET   B HB3  1 
ATOM   9412  H  HG2  . MET   B 1 1   ? 31.614 -6.366  57.068 1.00 41.92 ? 1    MET   B HG2  1 
ATOM   9413  H  HG3  . MET   B 1 1   ? 31.807 -4.861  56.708 1.00 41.92 ? 1    MET   B HG3  1 
ATOM   9414  H  HE1  . MET   B 1 1   ? 32.513 -5.701  60.539 1.00 42.29 ? 1    MET   B HE1  1 
ATOM   9415  H  HE2  . MET   B 1 1   ? 32.427 -6.814  59.415 1.00 42.29 ? 1    MET   B HE2  1 
ATOM   9416  H  HE3  . MET   B 1 1   ? 33.283 -5.504  59.170 1.00 42.29 ? 1    MET   B HE3  1 
ATOM   9417  N  N    . TYR   B 1 2   ? 27.506 -5.551  54.666 1.00 28.77 ? 2    TYR   B N    1 
ATOM   9418  C  CA   . TYR   B 1 2   ? 26.327 -4.904  54.032 1.00 24.55 ? 2    TYR   B CA   1 
ATOM   9419  C  C    . TYR   B 1 2   ? 25.908 -3.684  54.865 1.00 22.91 ? 2    TYR   B C    1 
ATOM   9420  O  O    . TYR   B 1 2   ? 25.779 -3.819  56.091 1.00 21.62 ? 2    TYR   B O    1 
ATOM   9421  C  CB   . TYR   B 1 2   ? 25.192 -5.914  53.862 1.00 25.12 ? 2    TYR   B CB   1 
ATOM   9422  C  CG   . TYR   B 1 2   ? 25.526 -7.076  52.963 1.00 25.62 ? 2    TYR   B CG   1 
ATOM   9423  C  CD1  . TYR   B 1 2   ? 25.977 -6.870  51.670 1.00 25.15 ? 2    TYR   B CD1  1 
ATOM   9424  C  CD2  . TYR   B 1 2   ? 25.401 -8.381  53.406 1.00 26.00 ? 2    TYR   B CD2  1 
ATOM   9425  C  CE1  . TYR   B 1 2   ? 26.289 -7.930  50.837 1.00 24.61 ? 2    TYR   B CE1  1 
ATOM   9426  C  CE2  . TYR   B 1 2   ? 25.708 -9.454  52.586 1.00 27.91 ? 2    TYR   B CE2  1 
ATOM   9427  C  CZ   . TYR   B 1 2   ? 26.155 -9.228  51.297 1.00 25.56 ? 2    TYR   B CZ   1 
ATOM   9428  O  OH   . TYR   B 1 2   ? 26.464 -10.287 50.480 1.00 35.28 ? 2    TYR   B OH   1 
ATOM   9429  H  H    . TYR   B 1 2   ? 27.316 -6.092  55.307 1.00 34.53 ? 2    TYR   B H    1 
ATOM   9430  H  HA   . TYR   B 1 2   ? 26.557 -4.592  53.143 1.00 29.46 ? 2    TYR   B HA   1 
ATOM   9431  H  HB2  . TYR   B 1 2   ? 24.943 -6.255  54.735 1.00 30.14 ? 2    TYR   B HB2  1 
ATOM   9432  H  HB3  . TYR   B 1 2   ? 24.416 -5.455  53.505 1.00 30.14 ? 2    TYR   B HB3  1 
ATOM   9433  H  HD1  . TYR   B 1 2   ? 26.072 -6.000  51.355 1.00 30.18 ? 2    TYR   B HD1  1 
ATOM   9434  H  HD2  . TYR   B 1 2   ? 25.105 -8.541  54.273 1.00 31.20 ? 2    TYR   B HD2  1 
ATOM   9435  H  HE1  . TYR   B 1 2   ? 26.588 -7.770  49.971 1.00 29.53 ? 2    TYR   B HE1  1 
ATOM   9436  H  HE2  . TYR   B 1 2   ? 25.614 -10.324 52.901 1.00 33.49 ? 2    TYR   B HE2  1 
ATOM   9437  H  HH   . TYR   B 1 2   ? 26.335 -11.007 50.893 1.00 42.34 ? 2    TYR   B HH   1 
ATOM   9438  N  N    . GLY   B 1 3   ? 25.708 -2.542  54.208 1.00 22.54 ? 3    GLY   B N    1 
ATOM   9439  C  CA   . GLY   B 1 3   ? 25.373 -1.303  54.937 1.00 21.17 ? 3    GLY   B CA   1 
ATOM   9440  C  C    . GLY   B 1 3   ? 26.612 -0.809  55.648 1.00 17.58 ? 3    GLY   B C    1 
ATOM   9441  O  O    . GLY   B 1 3   ? 27.198 0.176   55.183 1.00 16.68 ? 3    GLY   B O    1 
ATOM   9442  H  H    . GLY   B 1 3   ? 25.759 -2.457  53.354 1.00 27.05 ? 3    GLY   B H    1 
ATOM   9443  H  HA2  . GLY   B 1 3   ? 25.047 -0.628  54.321 1.00 25.41 ? 3    GLY   B HA2  1 
ATOM   9444  H  HA3  . GLY   B 1 3   ? 24.663 -1.470  55.576 1.00 25.41 ? 3    GLY   B HA3  1 
ATOM   9445  N  N    . TYR   B 1 4   ? 26.989 -1.475  56.736 1.00 19.67 ? 4    TYR   B N    1 
ATOM   9446  C  CA   . TYR   B 1 4   ? 28.272 -1.143  57.397 1.00 20.08 ? 4    TYR   B CA   1 
ATOM   9447  C  C    . TYR   B 1 4   ? 29.403 -1.448  56.408 1.00 21.61 ? 4    TYR   B C    1 
ATOM   9448  O  O    . TYR   B 1 4   ? 29.234 -2.356  55.580 1.00 21.66 ? 4    TYR   B O    1 
ATOM   9449  C  CB   . TYR   B 1 4   ? 28.421 -1.952  58.687 1.00 19.10 ? 4    TYR   B CB   1 
ATOM   9450  C  CG   . TYR   B 1 4   ? 27.219 -1.920  59.598 1.00 19.67 ? 4    TYR   B CG   1 
ATOM   9451  C  CD1  . TYR   B 1 4   ? 27.065 -0.918  60.541 1.00 17.85 ? 4    TYR   B CD1  1 
ATOM   9452  C  CD2  . TYR   B 1 4   ? 26.235 -2.892  59.522 1.00 19.08 ? 4    TYR   B CD2  1 
ATOM   9453  C  CE1  . TYR   B 1 4   ? 25.967 -0.882  61.384 1.00 16.90 ? 4    TYR   B CE1  1 
ATOM   9454  C  CE2  . TYR   B 1 4   ? 25.129 -2.869  60.356 1.00 19.90 ? 4    TYR   B CE2  1 
ATOM   9455  C  CZ   . TYR   B 1 4   ? 24.994 -1.860  61.292 1.00 18.99 ? 4    TYR   B CZ   1 
ATOM   9456  O  OH   . TYR   B 1 4   ? 23.903 -1.826  62.125 1.00 17.82 ? 4    TYR   B OH   1 
ATOM   9457  H  H    . TYR   B 1 4   ? 26.538 -2.107  57.107 1.00 23.61 ? 4    TYR   B H    1 
ATOM   9458  H  HA   . TYR   B 1 4   ? 28.303 -0.205  57.642 1.00 24.10 ? 4    TYR   B HA   1 
ATOM   9459  H  HB2  . TYR   B 1 4   ? 28.610 -2.875  58.455 1.00 22.93 ? 4    TYR   B HB2  1 
ATOM   9460  H  HB3  . TYR   B 1 4   ? 29.190 -1.619  59.176 1.00 22.93 ? 4    TYR   B HB3  1 
ATOM   9461  H  HD1  . TYR   B 1 4   ? 27.713 -0.255  60.610 1.00 21.42 ? 4    TYR   B HD1  1 
ATOM   9462  H  HD2  . TYR   B 1 4   ? 26.319 -3.576  58.897 1.00 22.90 ? 4    TYR   B HD2  1 
ATOM   9463  H  HE1  . TYR   B 1 4   ? 25.884 -0.201  62.011 1.00 20.28 ? 4    TYR   B HE1  1 
ATOM   9464  H  HE2  . TYR   B 1 4   ? 24.479 -3.530  60.287 1.00 23.88 ? 4    TYR   B HE2  1 
ATOM   9465  H  HH   . TYR   B 1 4   ? 23.833 -1.061  62.465 1.00 21.39 ? 4    TYR   B HH   1 
ATOM   9466  N  N    . ASP   B 1 5   ? 30.495 -0.687  56.467 1.00 21.81 ? 5    ASP   B N    1 
ATOM   9467  C  CA   . ASP   B 1 5   ? 31.670 -0.962  55.599 1.00 21.96 ? 5    ASP   B CA   1 
ATOM   9468  C  C    . ASP   B 1 5   ? 32.523 -2.040  56.277 1.00 23.93 ? 5    ASP   B C    1 
ATOM   9469  O  O    . ASP   B 1 5   ? 32.917 -2.997  55.591 1.00 20.03 ? 5    ASP   B O    1 
ATOM   9470  C  CB   . ASP   B 1 5   ? 32.484 0.308   55.353 1.00 20.47 ? 5    ASP   B CB   1 
ATOM   9471  C  CG   . ASP   B 1 5   ? 31.827 1.308   54.419 1.00 21.50 ? 5    ASP   B CG   1 
ATOM   9472  O  OD1  . ASP   B 1 5   ? 30.825 0.946   53.779 1.00 18.99 ? 5    ASP   B OD1  1 
ATOM   9473  O  OD2  . ASP   B 1 5   ? 32.335 2.440   54.339 1.00 19.38 ? 5    ASP   B OD2  1 
ATOM   9474  H  H    . ASP   B 1 5   ? 30.587 -0.012  56.992 1.00 26.18 ? 5    ASP   B H    1 
ATOM   9475  H  HA   . ASP   B 1 5   ? 31.371 -1.275  54.731 1.00 26.35 ? 5    ASP   B HA   1 
ATOM   9476  H  HB2  . ASP   B 1 5   ? 32.652 0.741   56.205 1.00 24.57 ? 5    ASP   B HB2  1 
ATOM   9477  H  HB3  . ASP   B 1 5   ? 33.347 0.059   54.986 1.00 24.57 ? 5    ASP   B HB3  1 
ATOM   9478  N  N    . GLY   B 1 6   ? 32.800 -1.873  57.571 1.00 18.18 ? 6    GLY   B N    1 
ATOM   9479  C  CA   . GLY   B 1 6   ? 33.558 -2.887  58.328 1.00 19.58 ? 6    GLY   B CA   1 
ATOM   9480  C  C    . GLY   B 1 6   ? 34.867 -2.352  58.876 1.00 20.21 ? 6    GLY   B C    1 
ATOM   9481  O  O    . GLY   B 1 6   ? 35.605 -3.135  59.501 1.00 20.79 ? 6    GLY   B O    1 
ATOM   9482  H  H    . GLY   B 1 6   ? 32.562 -1.186  58.031 1.00 21.82 ? 6    GLY   B H    1 
ATOM   9483  H  HA2  . GLY   B 1 6   ? 33.013 -3.211  59.062 1.00 23.50 ? 6    GLY   B HA2  1 
ATOM   9484  H  HA3  . GLY   B 1 6   ? 33.739 -3.646  57.752 1.00 23.50 ? 6    GLY   B HA3  1 
ATOM   9485  N  N    . LYS   B 1 7   ? 35.141 -1.059  58.686 1.00 21.68 ? 7    LYS   B N    1 
ATOM   9486  C  CA   . LYS   B 1 7   ? 36.464 -0.529  59.100 1.00 18.20 ? 7    LYS   B CA   1 
ATOM   9487  C  C    . LYS   B 1 7   ? 36.359 0.759   59.917 1.00 16.18 ? 7    LYS   B C    1 
ATOM   9488  O  O    . LYS   B 1 7   ? 35.508 1.601   59.594 1.00 16.62 ? 7    LYS   B O    1 
ATOM   9489  C  CB   . LYS   B 1 7   ? 37.361 -0.275  57.884 1.00 17.89 ? 7    LYS   B CB   1 
ATOM   9490  C  CG   . LYS   B 1 7   ? 37.553 -1.467  56.957 1.00 16.79 ? 7    LYS   B CG   1 
ATOM   9491  C  CD   . LYS   B 1 7   ? 38.502 -2.506  57.513 1.00 20.09 ? 7    LYS   B CD   1 
ATOM   9492  C  CE   . LYS   B 1 7   ? 38.309 -3.870  56.886 1.00 23.81 ? 7    LYS   B CE   1 
ATOM   9493  N  NZ   . LYS   B 1 7   ? 39.352 -4.828  57.318 1.00 27.47 ? 7    LYS   B NZ   1 
ATOM   9494  H  H    . LYS   B 1 7   ? 34.605 -0.485  58.335 1.00 26.02 ? 7    LYS   B H    1 
ATOM   9495  H  HA   . LYS   B 1 7   ? 36.857 -1.212  59.665 1.00 21.85 ? 7    LYS   B HA   1 
ATOM   9496  H  HB2  . LYS   B 1 7   ? 36.986 0.458   57.371 1.00 21.47 ? 7    LYS   B HB2  1 
ATOM   9497  H  HB3  . LYS   B 1 7   ? 38.232 0.015   58.198 1.00 21.47 ? 7    LYS   B HB3  1 
ATOM   9498  H  HG2  . LYS   B 1 7   ? 36.692 -1.881  56.789 1.00 20.15 ? 7    LYS   B HG2  1 
ATOM   9499  H  HG3  . LYS   B 1 7   ? 37.889 -1.154  56.103 1.00 20.15 ? 7    LYS   B HG3  1 
ATOM   9500  H  HD2  . LYS   B 1 7   ? 39.416 -2.214  57.368 1.00 24.11 ? 7    LYS   B HD2  1 
ATOM   9501  H  HD3  . LYS   B 1 7   ? 38.375 -2.574  58.472 1.00 24.11 ? 7    LYS   B HD3  1 
ATOM   9502  H  HE2  . LYS   B 1 7   ? 37.434 -4.215  57.125 1.00 28.57 ? 7    LYS   B HE2  1 
ATOM   9503  H  HE3  . LYS   B 1 7   ? 38.327 -3.787  55.920 1.00 28.57 ? 7    LYS   B HE3  1 
ATOM   9504  H  HZ1  . LYS   B 1 7   ? 39.298 -5.568  56.827 1.00 32.96 ? 7    LYS   B HZ1  1 
ATOM   9505  H  HZ2  . LYS   B 1 7   ? 40.155 -4.460  57.212 1.00 32.96 ? 7    LYS   B HZ2  1 
ATOM   9506  H  HZ3  . LYS   B 1 7   ? 39.231 -5.032  58.176 1.00 32.96 ? 7    LYS   B HZ3  1 
ATOM   9507  N  N    . VAL   B 1 8   ? 37.225 0.894   60.911 1.00 15.68 ? 8    VAL   B N    1 
ATOM   9508  C  CA   . VAL   B 1 8   ? 37.312 2.085   61.747 1.00 15.82 ? 8    VAL   B CA   1 
ATOM   9509  C  C    . VAL   B 1 8   ? 38.694 2.701   61.575 1.00 16.47 ? 8    VAL   B C    1 
ATOM   9510  O  O    . VAL   B 1 8   ? 39.699 1.986   61.524 1.00 16.65 ? 8    VAL   B O    1 
ATOM   9511  C  CB   . VAL   B 1 8   ? 37.037 1.744   63.230 1.00 17.92 ? 8    VAL   B CB   1 
ATOM   9512  C  CG1  . VAL   B 1 8   ? 37.240 2.963   64.126 1.00 15.85 ? 8    VAL   B CG1  1 
ATOM   9513  C  CG2  . VAL   B 1 8   ? 35.628 1.187   63.394 1.00 19.97 ? 8    VAL   B CG2  1 
ATOM   9514  H  H    . VAL   B 1 8   ? 37.792 0.283   61.124 1.00 18.82 ? 8    VAL   B H    1 
ATOM   9515  H  HA   . VAL   B 1 8   ? 36.636 2.724   61.472 1.00 18.99 ? 8    VAL   B HA   1 
ATOM   9516  H  HB   . VAL   B 1 8   ? 37.674 1.066   63.504 1.00 21.50 ? 8    VAL   B HB   1 
ATOM   9517  H  HG11 . VAL   B 1 8   ? 37.061 2.721   65.048 1.00 19.03 ? 8    VAL   B HG11 1 
ATOM   9518  H  HG12 . VAL   B 1 8   ? 38.155 3.275   64.046 1.00 19.03 ? 8    VAL   B HG12 1 
ATOM   9519  H  HG13 . VAL   B 1 8   ? 36.633 3.669   63.854 1.00 19.03 ? 8    VAL   B HG13 1 
ATOM   9520  H  HG21 . VAL   B 1 8   ? 35.469 0.978   64.328 1.00 23.96 ? 8    VAL   B HG21 1 
ATOM   9521  H  HG22 . VAL   B 1 8   ? 34.982 1.847   63.097 1.00 23.96 ? 8    VAL   B HG22 1 
ATOM   9522  H  HG23 . VAL   B 1 8   ? 35.534 0.381   62.862 1.00 23.96 ? 8    VAL   B HG23 1 
ATOM   9523  N  N    . LEU   B 1 9   ? 38.740 4.032   61.470 1.00 14.65 ? 9    LEU   B N    1 
ATOM   9524  C  CA   . LEU   B 1 9   ? 40.029 4.752   61.310 1.00 14.52 ? 9    LEU   B CA   1 
ATOM   9525  C  C    . LEU   B 1 9   ? 40.399 5.401   62.647 1.00 18.60 ? 9    LEU   B C    1 
ATOM   9526  O  O    . LEU   B 1 9   ? 39.645 6.274   63.103 1.00 18.82 ? 9    LEU   B O    1 
ATOM   9527  C  CB   . LEU   B 1 9   ? 39.882 5.804   60.202 1.00 15.05 ? 9    LEU   B CB   1 
ATOM   9528  C  CG   . LEU   B 1 9   ? 41.065 6.749   60.007 1.00 14.10 ? 9    LEU   B CG   1 
ATOM   9529  C  CD1  . LEU   B 1 9   ? 42.326 5.972   59.665 1.00 16.89 ? 9    LEU   B CD1  1 
ATOM   9530  C  CD2  . LEU   B 1 9   ? 40.760 7.767   58.919 1.00 15.97 ? 9    LEU   B CD2  1 
ATOM   9531  H  H    . LEU   B 1 9   ? 38.047 4.541   61.488 1.00 17.58 ? 9    LEU   B H    1 
ATOM   9532  H  HA   . LEU   B 1 9   ? 40.737 4.140   61.056 1.00 17.42 ? 9    LEU   B HA   1 
ATOM   9533  H  HB2  . LEU   B 1 9   ? 39.719 5.343   59.364 1.00 18.06 ? 9    LEU   B HB2  1 
ATOM   9534  H  HB3  . LEU   B 1 9   ? 39.094 6.337   60.391 1.00 18.06 ? 9    LEU   B HB3  1 
ATOM   9535  H  HG   . LEU   B 1 9   ? 41.215 7.222   60.841 1.00 16.93 ? 9    LEU   B HG   1 
ATOM   9536  H  HD11 . LEU   B 1 9   ? 43.064 6.590   59.545 1.00 20.27 ? 9    LEU   B HD11 1 
ATOM   9537  H  HD12 . LEU   B 1 9   ? 42.533 5.357   60.386 1.00 20.27 ? 9    LEU   B HD12 1 
ATOM   9538  H  HD13 . LEU   B 1 9   ? 42.186 5.473   58.845 1.00 20.27 ? 9    LEU   B HD13 1 
ATOM   9539  H  HD21 . LEU   B 1 9   ? 41.520 8.359   58.807 1.00 19.16 ? 9    LEU   B HD21 1 
ATOM   9540  H  HD22 . LEU   B 1 9   ? 40.585 7.306   58.084 1.00 19.16 ? 9    LEU   B HD22 1 
ATOM   9541  H  HD23 . LEU   B 1 9   ? 39.980 8.286   59.171 1.00 19.16 ? 9    LEU   B HD23 1 
ATOM   9542  N  N    . ARG   B 1 10  ? 41.512 4.972   63.248 1.00 14.76 ? 10   ARG   B N    1 
ATOM   9543  C  CA   . ARG   B 1 10  ? 41.934 5.514   64.565 1.00 15.12 ? 10   ARG   B CA   1 
ATOM   9544  C  C    . ARG   B 1 10  ? 43.138 6.431   64.362 1.00 19.05 ? 10   ARG   B C    1 
ATOM   9545  O  O    . ARG   B 1 10  ? 44.183 5.930   63.914 1.00 17.54 ? 10   ARG   B O    1 
ATOM   9546  C  CB   . ARG   B 1 10  ? 42.287 4.392   65.549 1.00 18.20 ? 10   ARG   B CB   1 
ATOM   9547  C  CG   . ARG   B 1 10  ? 42.614 4.894   66.948 1.00 16.47 ? 10   ARG   B CG   1 
ATOM   9548  C  CD   . ARG   B 1 10  ? 42.897 3.777   67.934 1.00 20.32 ? 10   ARG   B CD   1 
ATOM   9549  N  NE   . ARG   B 1 10  ? 41.780 2.857   68.079 1.00 21.30 ? 10   ARG   B NE   1 
ATOM   9550  C  CZ   . ARG   B 1 10  ? 40.759 3.036   68.910 1.00 17.74 ? 10   ARG   B CZ   1 
ATOM   9551  N  NH1  . ARG   B 1 10  ? 40.704 4.114   69.670 1.00 17.29 ? 10   ARG   B NH1  1 
ATOM   9552  N  NH2  . ARG   B 1 10  ? 39.796 2.134   68.975 1.00 21.07 ? 10   ARG   B NH2  1 
ATOM   9553  H  H    . ARG   B 1 10  ? 42.038 4.375   62.922 1.00 17.72 ? 10   ARG   B H    1 
ATOM   9554  H  HA   . ARG   B 1 10  ? 41.195 6.013   64.945 1.00 18.15 ? 10   ARG   B HA   1 
ATOM   9555  H  HB2  . ARG   B 1 10  ? 41.543 3.771   65.601 1.00 21.85 ? 10   ARG   B HB2  1 
ATOM   9556  H  HB3  . ARG   B 1 10  ? 43.047 3.897   65.205 1.00 21.85 ? 10   ARG   B HB3  1 
ATOM   9557  H  HG2  . ARG   B 1 10  ? 43.385 5.480   66.903 1.00 19.77 ? 10   ARG   B HG2  1 
ATOM   9558  H  HG3  . ARG   B 1 10  ? 41.872 5.426   67.276 1.00 19.77 ? 10   ARG   B HG3  1 
ATOM   9559  H  HD2  . ARG   B 1 10  ? 43.680 3.285   67.643 1.00 24.38 ? 10   ARG   B HD2  1 
ATOM   9560  H  HD3  . ARG   B 1 10  ? 43.109 4.161   68.799 1.00 24.38 ? 10   ARG   B HD3  1 
ATOM   9561  H  HE   . ARG   B 1 10  ? 41.780 2.148   67.593 1.00 25.56 ? 10   ARG   B HE   1 
ATOM   9562  H  HH11 . ARG   B 1 10  ? 41.330 4.702   69.628 1.00 20.75 ? 10   ARG   B HH11 1 
ATOM   9563  H  HH12 . ARG   B 1 10  ? 40.042 4.228   70.207 1.00 20.75 ? 10   ARG   B HH12 1 
ATOM   9564  H  HH21 . ARG   B 1 10  ? 39.830 1.432   68.480 1.00 25.29 ? 10   ARG   B HH21 1 
ATOM   9565  H  HH22 . ARG   B 1 10  ? 39.135 2.249   69.513 1.00 25.29 ? 10   ARG   B HH22 1 
ATOM   9566  N  N    . ILE   B 1 11  ? 42.986 7.718   64.678 1.00 15.33 ? 11   ILE   B N    1 
ATOM   9567  C  CA   . ILE   B 1 11  ? 44.084 8.692   64.431 1.00 15.81 ? 11   ILE   B CA   1 
ATOM   9568  C  C    . ILE   B 1 11  ? 44.550 9.304   65.754 1.00 18.66 ? 11   ILE   B C    1 
ATOM   9569  O  O    . ILE   B 1 11  ? 43.725 9.934   66.434 1.00 20.69 ? 11   ILE   B O    1 
ATOM   9570  C  CB   . ILE   B 1 11  ? 43.643 9.771   63.416 1.00 16.24 ? 11   ILE   B CB   1 
ATOM   9571  C  CG1  . ILE   B 1 11  ? 43.268 9.147   62.071 1.00 17.41 ? 11   ILE   B CG1  1 
ATOM   9572  C  CG2  . ILE   B 1 11  ? 44.710 10.843  63.269 1.00 17.00 ? 11   ILE   B CG2  1 
ATOM   9573  C  CD1  . ILE   B 1 11  ? 42.606 10.105  61.111 1.00 18.41 ? 11   ILE   B CD1  1 
ATOM   9574  H  H    . ILE   B 1 11  ? 42.276 8.053   65.029 1.00 18.40 ? 11   ILE   B H    1 
ATOM   9575  H  HA   . ILE   B 1 11  ? 44.839 8.226   64.038 1.00 18.98 ? 11   ILE   B HA   1 
ATOM   9576  H  HB   . ILE   B 1 11  ? 42.845 10.202  63.760 1.00 19.49 ? 11   ILE   B HB   1 
ATOM   9577  H  HG12 . ILE   B 1 11  ? 44.069 8.790   61.656 1.00 20.90 ? 11   ILE   B HG12 1 
ATOM   9578  H  HG13 . ILE   B 1 11  ? 42.672 8.398   62.228 1.00 20.90 ? 11   ILE   B HG13 1 
ATOM   9579  H  HG21 . ILE   B 1 11  ? 44.414 11.509  62.629 1.00 20.40 ? 11   ILE   B HG21 1 
ATOM   9580  H  HG22 . ILE   B 1 11  ? 44.864 11.267  64.128 1.00 20.40 ? 11   ILE   B HG22 1 
ATOM   9581  H  HG23 . ILE   B 1 11  ? 45.534 10.439  62.956 1.00 20.40 ? 11   ILE   B HG23 1 
ATOM   9582  H  HD11 . ILE   B 1 11  ? 42.398 9.643   60.284 1.00 22.09 ? 11   ILE   B HD11 1 
ATOM   9583  H  HD12 . ILE   B 1 11  ? 41.788 10.445  61.506 1.00 22.09 ? 11   ILE   B HD12 1 
ATOM   9584  H  HD13 . ILE   B 1 11  ? 43.206 10.844  60.925 1.00 22.09 ? 11   ILE   B HD13 1 
ATOM   9585  N  N    . ASN   B 1 12  ? 45.814 9.085   66.115 1.00 17.83 ? 12   ASN   B N    1 
ATOM   9586  C  CA   . ASN   B 1 12  ? 46.387 9.741   67.316 1.00 18.78 ? 12   ASN   B CA   1 
ATOM   9587  C  C    . ASN   B 1 12  ? 47.146 10.962  66.803 1.00 18.98 ? 12   ASN   B C    1 
ATOM   9588  O  O    . ASN   B 1 12  ? 48.205 10.770  66.193 1.00 19.40 ? 12   ASN   B O    1 
ATOM   9589  C  CB   . ASN   B 1 12  ? 47.255 8.786   68.137 1.00 20.53 ? 12   ASN   B CB   1 
ATOM   9590  C  CG   . ASN   B 1 12  ? 47.731 9.400   69.434 1.00 23.99 ? 12   ASN   B CG   1 
ATOM   9591  O  OD1  . ASN   B 1 12  ? 48.501 10.356  69.427 1.00 21.52 ? 12   ASN   B OD1  1 
ATOM   9592  N  ND2  . ASN   B 1 12  ? 47.268 8.861   70.550 1.00 25.46 ? 12   ASN   B ND2  1 
ATOM   9593  H  H    . ASN   B 1 12  ? 46.357 8.570   65.692 1.00 21.40 ? 12   ASN   B H    1 
ATOM   9594  H  HA   . ASN   B 1 12  ? 45.694 10.013  67.938 1.00 22.54 ? 12   ASN   B HA   1 
ATOM   9595  H  HB2  . ASN   B 1 12  ? 46.750 7.981   68.331 1.00 24.64 ? 12   ASN   B HB2  1 
ATOM   9596  H  HB3  . ASN   B 1 12  ? 48.023 8.518   67.609 1.00 24.64 ? 12   ASN   B HB3  1 
ATOM   9597  H  HD21 . ASN   B 1 12  ? 47.505 9.180   71.312 1.00 30.55 ? 12   ASN   B HD21 1 
ATOM   9598  H  HD22 . ASN   B 1 12  ? 46.730 8.191   70.513 1.00 30.55 ? 12   ASN   B HD22 1 
ATOM   9599  N  N    . LEU   B 1 13  ? 46.774 12.154  67.276 1.00 18.90 ? 13   LEU   B N    1 
ATOM   9600  C  CA   . LEU   B 1 13  ? 47.411 13.400  66.768 1.00 19.03 ? 13   LEU   B CA   1 
ATOM   9601  C  C    . LEU   B 1 13  ? 48.763 13.647  67.452 1.00 21.77 ? 13   LEU   B C    1 
ATOM   9602  O  O    . LEU   B 1 13  ? 49.481 14.550  66.997 1.00 22.27 ? 13   LEU   B O    1 
ATOM   9603  C  CB   . LEU   B 1 13  ? 46.445 14.567  66.994 1.00 19.52 ? 13   LEU   B CB   1 
ATOM   9604  C  CG   . LEU   B 1 13  ? 45.198 14.542  66.111 1.00 18.25 ? 13   LEU   B CG   1 
ATOM   9605  C  CD1  . LEU   B 1 13  ? 44.376 15.809  66.293 1.00 18.04 ? 13   LEU   B CD1  1 
ATOM   9606  C  CD2  . LEU   B 1 13  ? 45.575 14.354  64.650 1.00 19.14 ? 13   LEU   B CD2  1 
ATOM   9607  H  H    . LEU   B 1 13  ? 46.170 12.274  67.877 1.00 22.68 ? 13   LEU   B H    1 
ATOM   9608  H  HA   . LEU   B 1 13  ? 47.592 13.313  65.819 1.00 22.84 ? 13   LEU   B HA   1 
ATOM   9609  H  HB2  . LEU   B 1 13  ? 46.168 14.567  67.924 1.00 23.43 ? 13   LEU   B HB2  1 
ATOM   9610  H  HB3  . LEU   B 1 13  ? 46.920 15.399  66.839 1.00 23.43 ? 13   LEU   B HB3  1 
ATOM   9611  H  HG   . LEU   B 1 13  ? 44.654 13.787  66.385 1.00 21.90 ? 13   LEU   B HG   1 
ATOM   9612  H  HD11 . LEU   B 1 13  ? 43.591 15.771  65.724 1.00 21.65 ? 13   LEU   B HD11 1 
ATOM   9613  H  HD12 . LEU   B 1 13  ? 44.099 15.885  67.220 1.00 21.65 ? 13   LEU   B HD12 1 
ATOM   9614  H  HD13 . LEU   B 1 13  ? 44.912 16.580  66.052 1.00 21.65 ? 13   LEU   B HD13 1 
ATOM   9615  H  HD21 . LEU   B 1 13  ? 44.771 14.341  64.107 1.00 22.97 ? 13   LEU   B HD21 1 
ATOM   9616  H  HD22 . LEU   B 1 13  ? 46.145 15.086  64.366 1.00 22.97 ? 13   LEU   B HD22 1 
ATOM   9617  H  HD23 . LEU   B 1 13  ? 46.050 13.515  64.544 1.00 22.97 ? 13   LEU   B HD23 1 
ATOM   9618  N  N    . LYS   B 1 14  ? 48.956 13.076  68.644 1.00 19.40 ? 14   LYS   B N    1 
ATOM   9619  C  CA   . LYS   B 1 14  ? 50.244 13.239  69.370 1.00 24.38 ? 14   LYS   B CA   1 
ATOM   9620  C  C    . LYS   B 1 14  ? 51.289 12.336  68.709 1.00 24.57 ? 14   LYS   B C    1 
ATOM   9621  O  O    . LYS   B 1 14  ? 52.356 12.853  68.349 1.00 27.46 ? 14   LYS   B O    1 
ATOM   9622  C  CB   . LYS   B 1 14  ? 50.093 12.925  70.861 1.00 26.01 ? 14   LYS   B CB   1 
ATOM   9623  C  CG   . LYS   B 1 14  ? 51.388 12.978  71.660 1.00 29.19 ? 14   LYS   B CG   1 
ATOM   9624  C  CD   . LYS   B 1 14  ? 51.174 12.917  73.157 1.00 36.51 ? 14   LYS   B CD   1 
ATOM   9625  C  CE   . LYS   B 1 14  ? 52.395 13.341  73.944 1.00 46.86 ? 14   LYS   B CE   1 
ATOM   9626  N  NZ   . LYS   B 1 14  ? 52.208 14.663  74.588 1.00 46.83 ? 14   LYS   B NZ   1 
ATOM   9627  H  H    . LYS   B 1 14  ? 48.371 12.596  69.052 1.00 23.28 ? 14   LYS   B H    1 
ATOM   9628  H  HA   . LYS   B 1 14  ? 50.532 14.164  69.315 1.00 29.26 ? 14   LYS   B HA   1 
ATOM   9629  H  HB2  . LYS   B 1 14  ? 49.463 13.553  71.248 1.00 31.22 ? 14   LYS   B HB2  1 
ATOM   9630  H  HB3  . LYS   B 1 14  ? 49.706 12.040  70.955 1.00 31.22 ? 14   LYS   B HB3  1 
ATOM   9631  H  HG2  . LYS   B 1 14  ? 51.957 12.240  71.391 1.00 35.03 ? 14   LYS   B HG2  1 
ATOM   9632  H  HG3  . LYS   B 1 14  ? 51.862 13.795  71.441 1.00 35.03 ? 14   LYS   B HG3  1 
ATOM   9633  H  HD2  . LYS   B 1 14  ? 50.427 13.488  73.396 1.00 43.82 ? 14   LYS   B HD2  1 
ATOM   9634  H  HD3  . LYS   B 1 14  ? 50.931 12.012  73.408 1.00 43.82 ? 14   LYS   B HD3  1 
ATOM   9635  H  HE2  . LYS   B 1 14  ? 52.588 12.676  74.623 1.00 56.24 ? 14   LYS   B HE2  1 
ATOM   9636  H  HE3  . LYS   B 1 14  ? 53.164 13.375  73.353 1.00 56.24 ? 14   LYS   B HE3  1 
ATOM   9637  H  HZ1  . LYS   B 1 14  ? 52.943 14.880  75.041 1.00 56.20 ? 14   LYS   B HZ1  1 
ATOM   9638  H  HZ2  . LYS   B 1 14  ? 52.052 15.278  73.964 1.00 56.20 ? 14   LYS   B HZ2  1 
ATOM   9639  H  HZ3  . LYS   B 1 14  ? 51.516 14.626  75.147 1.00 56.20 ? 14   LYS   B HZ3  1 
ATOM   9640  N  N    . GLU   B 1 15  ? 50.981 11.046  68.568 1.00 24.20 ? 15   GLU   B N    1 
ATOM   9641  C  CA   . GLU   B 1 15  ? 51.888 10.134  67.879 1.00 22.67 ? 15   GLU   B CA   1 
ATOM   9642  C  C    . GLU   B 1 15  ? 51.911 10.371  66.375 1.00 23.08 ? 15   GLU   B C    1 
ATOM   9643  O  O    . GLU   B 1 15  ? 52.859 9.941   65.709 1.00 28.24 ? 15   GLU   B O    1 
ATOM   9644  C  CB   . GLU   B 1 15  ? 51.482 8.683   68.152 1.00 23.91 ? 15   GLU   B CB   1 
ATOM   9645  C  CG   . GLU   B 1 15  ? 51.587 8.214   69.604 1.00 30.87 ? 15   GLU   B CG   1 
ATOM   9646  C  CD   . GLU   B 1 15  ? 52.870 8.642   70.291 1.00 37.93 ? 15   GLU   B CD   1 
ATOM   9647  O  OE1  . GLU   B 1 15  ? 53.956 8.440   69.710 1.00 38.18 ? 15   GLU   B OE1  1 
ATOM   9648  O  OE2  . GLU   B 1 15  ? 52.793 9.161   71.425 1.00 38.15 ? 15   GLU   B OE2  1 
ATOM   9649  H  H    . GLU   B 1 15  ? 50.258 10.684  68.862 1.00 29.05 ? 15   GLU   B H    1 
ATOM   9650  H  HA   . GLU   B 1 15  ? 52.779 10.305  68.224 1.00 27.21 ? 15   GLU   B HA   1 
ATOM   9651  H  HB2  . GLU   B 1 15  ? 50.565 8.562   67.858 1.00 28.69 ? 15   GLU   B HB2  1 
ATOM   9652  H  HB3  . GLU   B 1 15  ? 52.034 8.104   67.604 1.00 28.69 ? 15   GLU   B HB3  1 
ATOM   9653  H  HG2  . GLU   B 1 15  ? 50.831 8.561   70.103 1.00 37.05 ? 15   GLU   B HG2  1 
ATOM   9654  H  HG3  . GLU   B 1 15  ? 51.523 7.246   69.629 1.00 37.05 ? 15   GLU   B HG3  1 
ATOM   9655  N  N    . ARG   B 1 16  ? 50.905 11.087  65.857 1.00 23.07 ? 16   ARG   B N    1 
ATOM   9656  C  CA   . ARG   B 1 16  ? 50.783 11.316  64.391 1.00 23.47 ? 16   ARG   B CA   1 
ATOM   9657  C  C    . ARG   B 1 16  ? 50.642 9.953   63.709 1.00 22.59 ? 16   ARG   B C    1 
ATOM   9658  O  O    . ARG   B 1 16  ? 51.343 9.709   62.715 1.00 22.49 ? 16   ARG   B O    1 
ATOM   9659  C  CB   . ARG   B 1 16  ? 51.954 12.152  63.864 1.00 29.76 ? 16   ARG   B CB   1 
ATOM   9660  C  CG   . ARG   B 1 16  ? 52.066 13.526  64.509 1.00 31.12 ? 16   ARG   B CG   1 
ATOM   9661  C  CD   . ARG   B 1 16  ? 51.961 14.663  63.512 1.00 32.13 ? 16   ARG   B CD   1 
ATOM   9662  N  NE   . ARG   B 1 16  ? 51.890 15.959  64.173 1.00 34.23 ? 16   ARG   B NE   1 
ATOM   9663  C  CZ   . ARG   B 1 16  ? 52.020 17.127  63.557 1.00 33.93 ? 16   ARG   B CZ   1 
ATOM   9664  N  NH1  . ARG   B 1 16  ? 52.146 17.171  62.243 1.00 30.84 ? 16   ARG   B NH1  1 
ATOM   9665  N  NH2  . ARG   B 1 16  ? 52.022 18.248  64.259 1.00 32.85 ? 16   ARG   B NH2  1 
ATOM   9666  H  H    . ARG   B 1 16  ? 50.283 11.450  66.326 1.00 27.68 ? 16   ARG   B H    1 
ATOM   9667  H  HA   . ARG   B 1 16  ? 49.992 11.839  64.186 1.00 28.17 ? 16   ARG   B HA   1 
ATOM   9668  H  HB2  . ARG   B 1 16  ? 52.780 11.666  64.012 1.00 35.71 ? 16   ARG   B HB2  1 
ATOM   9669  H  HB3  . ARG   B 1 16  ? 51.857 12.261  62.905 1.00 35.71 ? 16   ARG   B HB3  1 
ATOM   9670  H  HG2  . ARG   B 1 16  ? 51.368 13.622  65.175 1.00 37.34 ? 16   ARG   B HG2  1 
ATOM   9671  H  HG3  . ARG   B 1 16  ? 52.914 13.590  64.976 1.00 37.34 ? 16   ARG   B HG3  1 
ATOM   9672  H  HD2  . ARG   B 1 16  ? 52.728 14.644  62.919 1.00 38.56 ? 16   ARG   B HD2  1 
ATOM   9673  H  HD3  . ARG   B 1 16  ? 51.173 14.538  62.961 1.00 38.56 ? 16   ARG   B HD3  1 
ATOM   9674  H  HE   . ARG   B 1 16  ? 51.754 15.968  65.022 1.00 41.08 ? 16   ARG   B HE   1 
ATOM   9675  H  HH11 . ARG   B 1 16  ? 52.144 16.442  61.786 1.00 37.01 ? 16   ARG   B HH11 1 
ATOM   9676  H  HH12 . ARG   B 1 16  ? 52.230 17.928  61.844 1.00 37.01 ? 16   ARG   B HH12 1 
ATOM   9677  H  HH21 . ARG   B 1 16  ? 51.939 18.220  65.115 1.00 39.42 ? 16   ARG   B HH21 1 
ATOM   9678  H  HH22 . ARG   B 1 16  ? 52.106 19.005  63.860 1.00 39.42 ? 16   ARG   B HH22 1 
ATOM   9679  N  N    . THR   B 1 17  ? 49.742 9.117   64.227 1.00 21.43 ? 17   THR   B N    1 
ATOM   9680  C  CA   . THR   B 1 17  ? 49.551 7.755   63.672 1.00 20.94 ? 17   THR   B CA   1 
ATOM   9681  C  C    . THR   B 1 17  ? 48.149 7.610   63.077 1.00 20.11 ? 17   THR   B C    1 
ATOM   9682  O  O    . THR   B 1 17  ? 47.213 8.172   63.660 1.00 19.16 ? 17   THR   B O    1 
ATOM   9683  C  CB   . THR   B 1 17  ? 49.772 6.690   64.754 1.00 19.83 ? 17   THR   B CB   1 
ATOM   9684  O  OG1  . THR   B 1 17  ? 48.983 7.026   65.895 1.00 21.52 ? 17   THR   B OG1  1 
ATOM   9685  C  CG2  . THR   B 1 17  ? 51.226 6.557   65.150 1.00 25.18 ? 17   THR   B CG2  1 
ATOM   9686  H  H    . THR   B 1 17  ? 49.232 9.308   64.893 1.00 25.72 ? 17   THR   B H    1 
ATOM   9687  H  HA   . THR   B 1 17  ? 50.206 7.623   62.969 1.00 25.13 ? 17   THR   B HA   1 
ATOM   9688  H  HB   . THR   B 1 17  ? 49.503 5.832   64.391 1.00 23.80 ? 17   THR   B HB   1 
ATOM   9689  H  HG1  . THR   B 1 17  ? 49.227 6.562   66.551 1.00 25.82 ? 17   THR   B HG1  1 
ATOM   9690  H  HG21 . THR   B 1 17  ? 51.314 5.875   65.834 1.00 30.23 ? 17   THR   B HG21 1 
ATOM   9691  H  HG22 . THR   B 1 17  ? 51.751 6.307   64.374 1.00 30.23 ? 17   THR   B HG22 1 
ATOM   9692  H  HG23 . THR   B 1 17  ? 51.546 7.405   65.497 1.00 30.23 ? 17   THR   B HG23 1 
ATOM   9693  N  N    . CYS   B 1 18  ? 48.025 6.882   61.966 1.00 19.05 ? 18   CYS   B N    1 
ATOM   9694  C  CA   . CYS   B 1 18  ? 46.705 6.618   61.333 1.00 17.79 ? 18   CYS   B CA   1 
ATOM   9695  C  C    . CYS   B 1 18  ? 46.565 5.106   61.163 1.00 18.89 ? 18   CYS   B C    1 
ATOM   9696  O  O    . CYS   B 1 18  ? 47.336 4.538   60.375 1.00 19.04 ? 18   CYS   B O    1 
ATOM   9697  C  CB   . CYS   B 1 18  ? 46.590 7.305   59.979 1.00 17.02 ? 18   CYS   B CB   1 
ATOM   9698  S  SG   . CYS   B 1 18  ? 46.684 9.111   60.086 1.00 20.32 ? 18   CYS   B SG   1 
ATOM   9699  H  H    . CYS   B 1 18  ? 48.690 6.526   61.553 1.00 22.86 ? 18   CYS   B H    1 
ATOM   9700  H  HA   . CYS   B 1 18  ? 45.999 6.972   61.897 1.00 21.35 ? 18   CYS   B HA   1 
ATOM   9701  H  HB2  . CYS   B 1 18  ? 47.298 6.984   59.399 1.00 20.42 ? 18   CYS   B HB2  1 
ATOM   9702  H  HB3  . CYS   B 1 18  ? 45.749 7.054   59.566 1.00 20.42 ? 18   CYS   B HB3  1 
ATOM   9703  H  HG   . CYS   B 1 18  ? 46.838 9.437   61.231 1.00 24.39 ? 18   CYS   B HG   1 
ATOM   9704  N  N    . LYS   B 1 19  ? 45.607 4.489   61.857 1.00 19.41 ? 19   LYS   B N    1 
ATOM   9705  C  CA   . LYS   B 1 19  ? 45.521 3.007   61.839 1.00 21.47 ? 19   LYS   B CA   1 
ATOM   9706  C  C    . LYS   B 1 19  ? 44.135 2.506   61.439 1.00 18.80 ? 19   LYS   B C    1 
ATOM   9707  O  O    . LYS   B 1 19  ? 43.147 3.186   61.755 1.00 18.84 ? 19   LYS   B O    1 
ATOM   9708  C  CB   . LYS   B 1 19  ? 45.845 2.463   63.234 1.00 23.46 ? 19   LYS   B CB   1 
ATOM   9709  C  CG   . LYS   B 1 19  ? 47.091 3.039   63.891 1.00 26.75 ? 19   LYS   B CG   1 
ATOM   9710  C  CD   . LYS   B 1 19  ? 47.328 2.501   65.285 1.00 28.94 ? 19   LYS   B CD   1 
ATOM   9711  C  CE   . LYS   B 1 19  ? 48.748 2.710   65.767 1.00 34.74 ? 19   LYS   B CE   1 
ATOM   9712  N  NZ   . LYS   B 1 19  ? 48.834 2.673   67.246 1.00 40.43 ? 19   LYS   B NZ   1 
ATOM   9713  H  H    . LYS   B 1 19  ? 45.011 4.886   62.333 1.00 23.30 ? 19   LYS   B H    1 
ATOM   9714  H  HA   . LYS   B 1 19  ? 46.158 2.692   61.179 1.00 25.77 ? 19   LYS   B HA   1 
ATOM   9715  H  HB2  . LYS   B 1 19  ? 45.086 2.632   63.814 1.00 28.15 ? 19   LYS   B HB2  1 
ATOM   9716  H  HB3  . LYS   B 1 19  ? 45.947 1.500   63.173 1.00 28.15 ? 19   LYS   B HB3  1 
ATOM   9717  H  HG2  . LYS   B 1 19  ? 47.863 2.841   63.338 1.00 32.10 ? 19   LYS   B HG2  1 
ATOM   9718  H  HG3  . LYS   B 1 19  ? 47.012 4.005   63.932 1.00 32.10 ? 19   LYS   B HG3  1 
ATOM   9719  H  HD2  . LYS   B 1 19  ? 46.716 2.933   65.901 1.00 34.73 ? 19   LYS   B HD2  1 
ATOM   9720  H  HD3  . LYS   B 1 19  ? 47.123 1.553   65.299 1.00 34.73 ? 19   LYS   B HD3  1 
ATOM   9721  H  HE2  . LYS   B 1 19  ? 49.322 2.024   65.392 1.00 41.69 ? 19   LYS   B HE2  1 
ATOM   9722  H  HE3  . LYS   B 1 19  ? 49.078 3.563   65.444 1.00 41.69 ? 19   LYS   B HE3  1 
ATOM   9723  H  HZ1  . LYS   B 1 19  ? 49.067 3.476   67.550 1.00 48.52 ? 19   LYS   B HZ1  1 
ATOM   9724  H  HZ2  . LYS   B 1 19  ? 48.042 2.447   67.584 1.00 48.52 ? 19   LYS   B HZ2  1 
ATOM   9725  H  HZ3  . LYS   B 1 19  ? 49.444 2.074   67.493 1.00 48.52 ? 19   LYS   B HZ3  1 
ATOM   9726  N  N    . SER   B 1 20  ? 44.082 1.334   60.806 1.00 17.94 ? 20   SER   B N    1 
ATOM   9727  C  CA   . SER   B 1 20  ? 42.780 0.712   60.470 1.00 18.33 ? 20   SER   B CA   1 
ATOM   9728  C  C    . SER   B 1 20  ? 42.468 -0.389  61.481 1.00 20.28 ? 20   SER   B C    1 
ATOM   9729  O  O    . SER   B 1 20  ? 43.377 -1.185  61.788 1.00 19.58 ? 20   SER   B O    1 
ATOM   9730  C  CB   . SER   B 1 20  ? 42.750 0.152   59.078 1.00 18.29 ? 20   SER   B CB   1 
ATOM   9731  O  OG   . SER   B 1 20  ? 41.516 -0.496  58.820 1.00 16.98 ? 20   SER   B OG   1 
ATOM   9732  H  H    . SER   B 1 20  ? 44.772 0.882   60.562 1.00 21.53 ? 20   SER   B H    1 
ATOM   9733  H  HA   . SER   B 1 20  ? 42.105 1.407   60.510 1.00 22.00 ? 20   SER   B HA   1 
ATOM   9734  H  HB2  . SER   B 1 20  ? 42.885 0.866   58.435 1.00 21.95 ? 20   SER   B HB2  1 
ATOM   9735  H  HB3  . SER   B 1 20  ? 43.480 -0.476  58.962 1.00 21.95 ? 20   SER   B HB3  1 
ATOM   9736  H  HG   . SER   B 1 20  ? 41.427 -0.611  57.993 1.00 20.37 ? 20   SER   B HG   1 
ATOM   9737  N  N    . GLU   B 1 21  ? 41.238 -0.412  61.983 1.00 17.32 ? 21   GLU   B N    1 
ATOM   9738  C  CA   . GLU   B 1 21  ? 40.801 -1.509  62.879 1.00 18.06 ? 21   GLU   B CA   1 
ATOM   9739  C  C    . GLU   B 1 21  ? 39.486 -2.018  62.291 1.00 17.82 ? 21   GLU   B C    1 
ATOM   9740  O  O    . GLU   B 1 21  ? 38.814 -1.238  61.605 1.00 20.32 ? 21   GLU   B O    1 
ATOM   9741  C  CB   . GLU   B 1 21  ? 40.647 -1.016  64.320 1.00 23.42 ? 21   GLU   B CB   1 
ATOM   9742  C  CG   . GLU   B 1 21  ? 41.924 -0.454  64.913 1.00 22.29 ? 21   GLU   B CG   1 
ATOM   9743  C  CD   . GLU   B 1 21  ? 41.770 0.106   66.317 1.00 24.01 ? 21   GLU   B CD   1 
ATOM   9744  O  OE1  . GLU   B 1 21  ? 40.622 0.212   66.785 1.00 26.18 ? 21   GLU   B OE1  1 
ATOM   9745  O  OE2  . GLU   B 1 21  ? 42.797 0.435   66.935 1.00 25.42 ? 21   GLU   B OE2  1 
ATOM   9746  H  H    . GLU   B 1 21  ? 40.639 0.185   61.826 1.00 20.79 ? 21   GLU   B H    1 
ATOM   9747  H  HA   . GLU   B 1 21  ? 41.455 -2.224  62.926 1.00 21.68 ? 21   GLU   B HA   1 
ATOM   9748  H  HB2  . GLU   B 1 21  ? 39.959 -0.333  64.348 1.00 28.11 ? 21   GLU   B HB2  1 
ATOM   9749  H  HB3  . GLU   B 1 21  ? 40.339 -1.751  64.873 1.00 28.11 ? 21   GLU   B HB3  1 
ATOM   9750  H  HG2  . GLU   B 1 21  ? 42.596 -1.153  64.927 1.00 26.75 ? 21   GLU   B HG2  1 
ATOM   9751  H  HG3  . GLU   B 1 21  ? 42.257 0.247   64.331 1.00 26.75 ? 21   GLU   B HG3  1 
ATOM   9752  N  N    . ASN   B 1 22  ? 39.155 -3.284  62.520 1.00 18.52 ? 22   ASN   B N    1 
ATOM   9753  C  CA   . ASN   B 1 22  ? 37.886 -3.813  62.041 1.00 18.68 ? 22   ASN   B CA   1 
ATOM   9754  C  C    . ASN   B 1 22  ? 36.744 -3.367  62.942 1.00 21.55 ? 22   ASN   B C    1 
ATOM   9755  O  O    . ASN   B 1 22  ? 36.857 -3.378  64.174 1.00 21.33 ? 22   ASN   B O    1 
ATOM   9756  C  CB   . ASN   B 1 22  ? 37.912 -5.336  61.971 1.00 22.45 ? 22   ASN   B CB   1 
ATOM   9757  C  CG   . ASN   B 1 22  ? 38.659 -5.849  60.759 1.00 20.19 ? 22   ASN   B CG   1 
ATOM   9758  O  OD1  . ASN   B 1 22  ? 39.276 -5.076  60.025 1.00 20.22 ? 22   ASN   B OD1  1 
ATOM   9759  N  ND2  . ASN   B 1 22  ? 38.583 -7.151  60.528 1.00 21.08 ? 22   ASN   B ND2  1 
ATOM   9760  H  H    . ASN   B 1 22  ? 39.646 -3.847  62.946 1.00 22.23 ? 22   ASN   B H    1 
ATOM   9761  H  HA   . ASN   B 1 22  ? 37.745 -3.463  61.147 1.00 22.42 ? 22   ASN   B HA   1 
ATOM   9762  H  HB2  . ASN   B 1 22  ? 38.327 -5.686  62.775 1.00 26.94 ? 22   ASN   B HB2  1 
ATOM   9763  H  HB3  . ASN   B 1 22  ? 37.002 -5.671  61.952 1.00 26.94 ? 22   ASN   B HB3  1 
ATOM   9764  H  HD21 . ASN   B 1 22  ? 38.975 -7.489  59.841 1.00 25.31 ? 22   ASN   B HD21 1 
ATOM   9765  H  HD22 . ASN   B 1 22  ? 38.142 -7.658  61.065 1.00 25.31 ? 22   ASN   B HD22 1 
ATOM   9766  N  N    . LEU   B 1 23  ? 35.621 -3.050  62.307 1.00 18.57 ? 23   LEU   B N    1 
ATOM   9767  C  CA   . LEU   B 1 23  ? 34.418 -2.677  63.083 1.00 19.16 ? 23   LEU   B CA   1 
ATOM   9768  C  C    . LEU   B 1 23  ? 33.883 -3.912  63.810 1.00 23.54 ? 23   LEU   B C    1 
ATOM   9769  O  O    . LEU   B 1 23  ? 33.923 -5.004  63.219 1.00 21.91 ? 23   LEU   B O    1 
ATOM   9770  C  CB   . LEU   B 1 23  ? 33.378 -2.150  62.094 1.00 19.69 ? 23   LEU   B CB   1 
ATOM   9771  C  CG   . LEU   B 1 23  ? 32.012 -1.800  62.682 1.00 18.57 ? 23   LEU   B CG   1 
ATOM   9772  C  CD1  . LEU   B 1 23  ? 32.050 -0.434  63.347 1.00 18.41 ? 23   LEU   B CD1  1 
ATOM   9773  C  CD2  . LEU   B 1 23  ? 30.941 -1.837  61.604 1.00 20.19 ? 23   LEU   B CD2  1 
ATOM   9774  H  H    . LEU   B 1 23  ? 35.524 -3.041  61.452 1.00 22.29 ? 23   LEU   B H    1 
ATOM   9775  H  HA   . LEU   B 1 23  ? 34.624 -1.998  63.744 1.00 22.99 ? 23   LEU   B HA   1 
ATOM   9776  H  HB2  . LEU   B 1 23  ? 33.738 -1.358  61.665 1.00 23.64 ? 23   LEU   B HB2  1 
ATOM   9777  H  HB3  . LEU   B 1 23  ? 33.251 -2.816  61.400 1.00 23.64 ? 23   LEU   B HB3  1 
ATOM   9778  H  HG   . LEU   B 1 23  ? 31.792 -2.462  63.356 1.00 22.29 ? 23   LEU   B HG   1 
ATOM   9779  H  HD11 . LEU   B 1 23  ? 31.176 -0.228  63.714 1.00 22.10 ? 23   LEU   B HD11 1 
ATOM   9780  H  HD12 . LEU   B 1 23  ? 32.707 -0.439  64.061 1.00 22.10 ? 23   LEU   B HD12 1 
ATOM   9781  H  HD13 . LEU   B 1 23  ? 32.291 0.239   62.691 1.00 22.10 ? 23   LEU   B HD13 1 
ATOM   9782  H  HD21 . LEU   B 1 23  ? 30.081 -1.613  61.994 1.00 24.23 ? 23   LEU   B HD21 1 
ATOM   9783  H  HD22 . LEU   B 1 23  ? 31.158 -1.195  60.910 1.00 24.23 ? 23   LEU   B HD22 1 
ATOM   9784  H  HD23 . LEU   B 1 23  ? 30.899 -2.727  61.220 1.00 24.23 ? 23   LEU   B HD23 1 
ATOM   9785  N  N    . ASP   B 1 24  ? 33.429 -3.742  65.051 1.00 21.27 ? 24   ASP   B N    1 
ATOM   9786  C  CA   . ASP   B 1 24  ? 32.762 -4.857  65.767 1.00 21.76 ? 24   ASP   B CA   1 
ATOM   9787  C  C    . ASP   B 1 24  ? 31.327 -4.906  65.242 1.00 22.39 ? 24   ASP   B C    1 
ATOM   9788  O  O    . ASP   B 1 24  ? 30.522 -4.077  65.697 1.00 22.14 ? 24   ASP   B O    1 
ATOM   9789  C  CB   . ASP   B 1 24  ? 32.831 -4.638  67.278 1.00 26.88 ? 24   ASP   B CB   1 
ATOM   9790  C  CG   . ASP   B 1 24  ? 32.203 -5.747  68.103 1.00 27.48 ? 24   ASP   B CG   1 
ATOM   9791  O  OD1  . ASP   B 1 24  ? 31.252 -6.383  67.615 1.00 26.00 ? 24   ASP   B OD1  1 
ATOM   9792  O  OD2  . ASP   B 1 24  ? 32.669 -5.956  69.235 1.00 31.90 ? 24   ASP   B OD2  1 
ATOM   9793  H  H    . ASP   B 1 24  ? 33.490 -3.009  65.497 1.00 25.52 ? 24   ASP   B H    1 
ATOM   9794  H  HA   . ASP   B 1 24  ? 33.200 -5.708  65.607 1.00 26.11 ? 24   ASP   B HA   1 
ATOM   9795  H  HB2  . ASP   B 1 24  ? 33.761 -4.544  67.538 1.00 32.27 ? 24   ASP   B HB2  1 
ATOM   9796  H  HB3  . ASP   B 1 24  ? 32.390 -3.801  67.493 1.00 32.27 ? 24   ASP   B HB3  1 
ATOM   9797  N  N    . LEU   B 1 25  ? 31.026 -5.808  64.305 1.00 20.51 ? 25   LEU   B N    1 
ATOM   9798  C  CA   . LEU   B 1 25  ? 29.675 -5.812  63.677 1.00 24.13 ? 25   LEU   B CA   1 
ATOM   9799  C  C    . LEU   B 1 25  ? 28.594 -6.076  64.733 1.00 22.90 ? 25   LEU   B C    1 
ATOM   9800  O  O    . LEU   B 1 25  ? 27.519 -5.469  64.636 1.00 20.15 ? 25   LEU   B O    1 
ATOM   9801  C  CB   . LEU   B 1 25  ? 29.616 -6.852  62.555 1.00 25.79 ? 25   LEU   B CB   1 
ATOM   9802  C  CG   . LEU   B 1 25  ? 28.299 -6.907  61.785 1.00 23.15 ? 25   LEU   B CG   1 
ATOM   9803  C  CD1  . LEU   B 1 25  ? 27.993 -5.563  61.143 1.00 21.86 ? 25   LEU   B CD1  1 
ATOM   9804  C  CD2  . LEU   B 1 25  ? 28.337 -8.003  60.733 1.00 28.71 ? 25   LEU   B CD2  1 
ATOM   9805  H  H    . LEU   B 1 25  ? 31.564 -6.414  64.018 1.00 24.61 ? 25   LEU   B H    1 
ATOM   9806  H  HA   . LEU   B 1 25  ? 29.507 -4.939  63.289 1.00 28.96 ? 25   LEU   B HA   1 
ATOM   9807  H  HB2  . LEU   B 1 25  ? 30.333 -6.670  61.928 1.00 30.95 ? 25   LEU   B HB2  1 
ATOM   9808  H  HB3  . LEU   B 1 25  ? 29.788 -7.727  62.936 1.00 30.95 ? 25   LEU   B HB3  1 
ATOM   9809  H  HG   . LEU   B 1 25  ? 27.590 -7.112  62.415 1.00 27.78 ? 25   LEU   B HG   1 
ATOM   9810  H  HD11 . LEU   B 1 25  ? 27.154 -5.619  60.659 1.00 26.24 ? 25   LEU   B HD11 1 
ATOM   9811  H  HD12 . LEU   B 1 25  ? 27.924 -4.883  61.832 1.00 26.24 ? 25   LEU   B HD12 1 
ATOM   9812  H  HD13 . LEU   B 1 25  ? 28.705 -5.328  60.528 1.00 26.24 ? 25   LEU   B HD13 1 
ATOM   9813  H  HD21 . LEU   B 1 25  ? 27.493 -8.022  60.255 1.00 34.45 ? 25   LEU   B HD21 1 
ATOM   9814  H  HD22 . LEU   B 1 25  ? 29.058 -7.827  60.108 1.00 34.45 ? 25   LEU   B HD22 1 
ATOM   9815  H  HD23 . LEU   B 1 25  ? 28.484 -8.860  61.163 1.00 34.45 ? 25   LEU   B HD23 1 
ATOM   9816  N  N    . ASP   B 1 26  ? 28.861 -6.981  65.676 1.00 23.99 ? 26   ASP   B N    1 
ATOM   9817  C  CA   . ASP   B 1 26  ? 27.832 -7.270  66.670 1.00 26.07 ? 26   ASP   B CA   1 
ATOM   9818  C  C    . ASP   B 1 26  ? 27.480 -6.020  67.471 1.00 26.15 ? 26   ASP   B C    1 
ATOM   9819  O  O    . ASP   B 1 26  ? 26.300 -5.764  67.744 1.00 20.98 ? 26   ASP   B O    1 
ATOM   9820  C  CB   . ASP   B 1 26  ? 28.289 -8.400  67.593 1.00 33.65 ? 26   ASP   B CB   1 
ATOM   9821  C  CG   . ASP   B 1 26  ? 28.141 -9.784  66.955 1.00 36.59 ? 26   ASP   B CG   1 
ATOM   9822  O  OD1  . ASP   B 1 26  ? 27.306 -9.947  66.039 1.00 35.99 ? 26   ASP   B OD1  1 
ATOM   9823  O  OD2  . ASP   B 1 26  ? 28.853 -10.716 67.385 1.00 41.98 ? 26   ASP   B OD2  1 
ATOM   9824  H  H    . ASP   B 1 26  ? 29.596 -7.420  65.756 1.00 28.79 ? 26   ASP   B H    1 
ATOM   9825  H  HA   . ASP   B 1 26  ? 27.030 -7.558  66.206 1.00 31.29 ? 26   ASP   B HA   1 
ATOM   9826  H  HB2  . ASP   B 1 26  ? 29.217 -8.258  67.836 1.00 40.38 ? 26   ASP   B HB2  1 
ATOM   9827  H  HB3  . ASP   B 1 26  ? 27.773 -8.370  68.414 1.00 40.38 ? 26   ASP   B HB3  1 
ATOM   9828  N  N    . LYS   B 1 27  ? 28.486 -5.213  67.820 1.00 25.87 ? 27   LYS   B N    1 
ATOM   9829  C  CA   . LYS   B 1 27  ? 28.238 -3.964  68.592 1.00 27.70 ? 27   LYS   B CA   1 
ATOM   9830  C  C    . LYS   B 1 27  ? 27.547 -2.934  67.692 1.00 20.04 ? 27   LYS   B C    1 
ATOM   9831  O  O    . LYS   B 1 27  ? 26.660 -2.222  68.178 1.00 20.92 ? 27   LYS   B O    1 
ATOM   9832  C  CB   . LYS   B 1 27  ? 29.541 -3.385  69.150 1.00 28.67 ? 27   LYS   B CB   1 
ATOM   9833  C  CG   . LYS   B 1 27  ? 29.435 -1.976  69.720 1.00 33.03 ? 27   LYS   B CG   1 
ATOM   9834  C  CD   . LYS   B 1 27  ? 30.775 -1.355  70.062 1.00 35.05 ? 27   LYS   B CD   1 
ATOM   9835  C  CE   . LYS   B 1 27  ? 31.687 -1.215  68.862 1.00 42.03 ? 27   LYS   B CE   1 
ATOM   9836  N  NZ   . LYS   B 1 27  ? 32.587 -0.043  68.980 1.00 42.78 ? 27   LYS   B NZ   1 
ATOM   9837  H  H    . LYS   B 1 27  ? 29.312 -5.358  67.628 1.00 31.04 ? 27   LYS   B H    1 
ATOM   9838  H  HA   . LYS   B 1 27  ? 27.664 -4.178  69.344 1.00 33.24 ? 27   LYS   B HA   1 
ATOM   9839  H  HB2  . LYS   B 1 27  ? 29.868 -3.976  69.846 1.00 34.41 ? 27   LYS   B HB2  1 
ATOM   9840  H  HB3  . LYS   B 1 27  ? 30.206 -3.383  68.444 1.00 34.41 ? 27   LYS   B HB3  1 
ATOM   9841  H  HG2  . LYS   B 1 27  ? 28.979 -1.409  69.078 1.00 39.63 ? 27   LYS   B HG2  1 
ATOM   9842  H  HG3  . LYS   B 1 27  ? 28.885 -1.999  70.519 1.00 39.63 ? 27   LYS   B HG3  1 
ATOM   9843  H  HD2  . LYS   B 1 27  ? 30.629 -0.480  70.455 1.00 42.06 ? 27   LYS   B HD2  1 
ATOM   9844  H  HD3  . LYS   B 1 27  ? 31.215 -1.898  70.735 1.00 42.06 ? 27   LYS   B HD3  1 
ATOM   9845  H  HE2  . LYS   B 1 27  ? 32.218 -2.021  68.765 1.00 50.44 ? 27   LYS   B HE2  1 
ATOM   9846  H  HE3  . LYS   B 1 27  ? 31.151 -1.130  68.058 1.00 50.44 ? 27   LYS   B HE3  1 
ATOM   9847  H  HZ1  . LYS   B 1 27  ? 33.174 -0.050  68.311 1.00 51.35 ? 27   LYS   B HZ1  1 
ATOM   9848  H  HZ2  . LYS   B 1 27  ? 32.107 0.705   68.945 1.00 51.35 ? 27   LYS   B HZ2  1 
ATOM   9849  H  HZ3  . LYS   B 1 27  ? 33.022 -0.079  69.756 1.00 51.35 ? 27   LYS   B HZ3  1 
ATOM   9850  N  N    . ALA   B 1 28  ? 27.948 -2.876  66.424 1.00 19.18 ? 28   ALA   B N    1 
ATOM   9851  C  CA   . ALA   B 1 28  ? 27.362 -1.905  65.475 1.00 20.28 ? 28   ALA   B CA   1 
ATOM   9852  C  C    . ALA   B 1 28  ? 25.872 -2.198  65.276 1.00 17.68 ? 28   ALA   B C    1 
ATOM   9853  O  O    . ALA   B 1 28  ? 25.083 -1.242  65.215 1.00 18.08 ? 28   ALA   B O    1 
ATOM   9854  C  CB   . ALA   B 1 28  ? 28.115 -1.966  64.168 1.00 20.33 ? 28   ALA   B CB   1 
ATOM   9855  H  H    . ALA   B 1 28  ? 28.555 -3.384  66.087 1.00 23.02 ? 28   ALA   B H    1 
ATOM   9856  H  HA   . ALA   B 1 28  ? 27.441 -1.007  65.833 1.00 24.34 ? 28   ALA   B HA   1 
ATOM   9857  H  HB1  . ALA   B 1 28  ? 27.732 -1.330  63.544 1.00 24.40 ? 28   ALA   B HB1  1 
ATOM   9858  H  HB2  . ALA   B 1 28  ? 29.048 -1.747  64.321 1.00 24.40 ? 28   ALA   B HB2  1 
ATOM   9859  H  HB3  . ALA   B 1 28  ? 28.050 -2.860  63.798 1.00 24.40 ? 28   ALA   B HB3  1 
ATOM   9860  N  N    . LYS   B 1 29  ? 25.512 -3.477  65.172 1.00 18.48 ? 29   LYS   B N    1 
ATOM   9861  C  CA   . LYS   B 1 29  ? 24.091 -3.863  64.976 1.00 18.38 ? 29   LYS   B CA   1 
ATOM   9862  C  C    . LYS   B 1 29  ? 23.319 -3.630  66.280 1.00 20.14 ? 29   LYS   B C    1 
ATOM   9863  O  O    . LYS   B 1 29  ? 22.174 -3.164  66.207 1.00 21.37 ? 29   LYS   B O    1 
ATOM   9864  C  CB   . LYS   B 1 29  ? 23.989 -5.326  64.536 1.00 21.54 ? 29   LYS   B CB   1 
ATOM   9865  C  CG   . LYS   B 1 29  ? 24.404 -5.611  63.100 1.00 21.77 ? 29   LYS   B CG   1 
ATOM   9866  C  CD   . LYS   B 1 29  ? 24.530 -7.090  62.808 1.00 29.04 ? 29   LYS   B CD   1 
ATOM   9867  C  CE   . LYS   B 1 29  ? 24.616 -7.404  61.330 1.00 29.96 ? 29   LYS   B CE   1 
ATOM   9868  N  NZ   . LYS   B 1 29  ? 24.561 -8.862  61.075 1.00 34.06 ? 29   LYS   B NZ   1 
ATOM   9869  H  H    . LYS   B 1 29  ? 26.061 -4.138  65.210 1.00 22.18 ? 29   LYS   B H    1 
ATOM   9870  H  HA   . LYS   B 1 29  ? 23.702 -3.316  64.276 1.00 22.06 ? 29   LYS   B HA   1 
ATOM   9871  H  HB2  . LYS   B 1 29  ? 24.538 -5.864  65.127 1.00 25.85 ? 29   LYS   B HB2  1 
ATOM   9872  H  HB3  . LYS   B 1 29  ? 23.072 -5.620  64.655 1.00 25.85 ? 29   LYS   B HB3  1 
ATOM   9873  H  HG2  . LYS   B 1 29  ? 23.753 -5.221  62.496 1.00 26.13 ? 29   LYS   B HG2  1 
ATOM   9874  H  HG3  . LYS   B 1 29  ? 25.253 -5.177  62.921 1.00 26.13 ? 29   LYS   B HG3  1 
ATOM   9875  H  HD2  . LYS   B 1 29  ? 25.321 -7.435  63.252 1.00 34.85 ? 29   LYS   B HD2  1 
ATOM   9876  H  HD3  . LYS   B 1 29  ? 23.767 -7.554  63.187 1.00 34.85 ? 29   LYS   B HD3  1 
ATOM   9877  H  HE2  . LYS   B 1 29  ? 23.887 -6.966  60.863 1.00 35.96 ? 29   LYS   B HE2  1 
ATOM   9878  H  HE3  . LYS   B 1 29  ? 25.441 -7.043  60.970 1.00 35.96 ? 29   LYS   B HE3  1 
ATOM   9879  H  HZ1  . LYS   B 1 29  ? 25.293 -9.115  60.636 1.00 40.88 ? 29   LYS   B HZ1  1 
ATOM   9880  H  HZ2  . LYS   B 1 29  ? 24.515 -9.298  61.850 1.00 40.88 ? 29   LYS   B HZ2  1 
ATOM   9881  H  HZ3  . LYS   B 1 29  ? 23.842 -9.051  60.586 1.00 40.88 ? 29   LYS   B HZ3  1 
ATOM   9882  N  N    . LYS   B 1 30  ? 23.928 -3.964  67.420 1.00 18.81 ? 30   LYS   B N    1 
ATOM   9883  C  CA   . LYS   B 1 30  ? 23.223 -3.819  68.691 1.00 20.62 ? 30   LYS   B CA   1 
ATOM   9884  C  C    . LYS   B 1 30  ? 22.869 -2.361  68.965 1.00 20.57 ? 30   LYS   B C    1 
ATOM   9885  O  O    . LYS   B 1 30  ? 21.772 -2.058  69.450 1.00 17.16 ? 30   LYS   B O    1 
ATOM   9886  C  CB   . LYS   B 1 30  ? 24.084 -4.390  69.817 1.00 21.67 ? 30   LYS   B CB   1 
ATOM   9887  C  CG   . LYS   B 1 30  ? 23.498 -4.256  71.208 1.00 23.12 ? 30   LYS   B CG   1 
ATOM   9888  C  CD   . LYS   B 1 30  ? 24.337 -5.041  72.206 1.00 20.44 ? 30   LYS   B CD   1 
ATOM   9889  C  CE   . LYS   B 1 30  ? 23.729 -5.018  73.601 1.00 20.21 ? 30   LYS   B CE   1 
ATOM   9890  N  NZ   . LYS   B 1 30  ? 24.528 -5.842  74.545 1.00 23.34 ? 30   LYS   B NZ   1 
ATOM   9891  H  H    . LYS   B 1 30  ? 24.730 -4.269  67.478 1.00 22.57 ? 30   LYS   B H    1 
ATOM   9892  H  HA   . LYS   B 1 30  ? 22.390 -4.313  68.644 1.00 24.75 ? 30   LYS   B HA   1 
ATOM   9893  H  HB2  . LYS   B 1 30  ? 24.244 -5.330  69.638 1.00 26.00 ? 30   LYS   B HB2  1 
ATOM   9894  H  HB3  . LYS   B 1 30  ? 24.947 -3.948  69.801 1.00 26.00 ? 30   LYS   B HB3  1 
ATOM   9895  H  HG2  . LYS   B 1 30  ? 23.467 -3.321  71.465 1.00 27.75 ? 30   LYS   B HG2  1 
ATOM   9896  H  HG3  . LYS   B 1 30  ? 22.585 -4.582  71.215 1.00 27.75 ? 30   LYS   B HG3  1 
ATOM   9897  H  HD2  . LYS   B 1 30  ? 24.421 -5.959  71.905 1.00 24.54 ? 30   LYS   B HD2  1 
ATOM   9898  H  HD3  . LYS   B 1 30  ? 25.233 -4.670  72.238 1.00 24.54 ? 30   LYS   B HD3  1 
ATOM   9899  H  HE2  . LYS   B 1 30  ? 23.684 -4.104  73.923 1.00 24.26 ? 30   LYS   B HE2  1 
ATOM   9900  H  HE3  . LYS   B 1 30  ? 22.819 -5.351  73.566 1.00 24.26 ? 30   LYS   B HE3  1 
ATOM   9901  H  HZ1  . LYS   B 1 30  ? 24.207 -5.745  75.369 1.00 28.01 ? 30   LYS   B HZ1  1 
ATOM   9902  H  HZ2  . LYS   B 1 30  ? 24.479 -6.698  74.307 1.00 28.01 ? 30   LYS   B HZ2  1 
ATOM   9903  H  HZ3  . LYS   B 1 30  ? 25.377 -5.577  74.525 1.00 28.01 ? 30   LYS   B HZ3  1 
ATOM   9904  N  N    . PHE   B 1 31  ? 23.795 -1.466  68.629 1.00 18.08 ? 31   PHE   B N    1 
ATOM   9905  C  CA   . PHE   B 1 31  ? 23.556 -0.013  68.834 1.00 17.60 ? 31   PHE   B CA   1 
ATOM   9906  C  C    . PHE   B 1 31  ? 23.198 0.634   67.488 1.00 17.91 ? 31   PHE   B C    1 
ATOM   9907  O  O    . PHE   B 1 31  ? 23.334 1.868   67.393 1.00 16.07 ? 31   PHE   B O    1 
ATOM   9908  C  CB   . PHE   B 1 31  ? 24.765 0.591   69.548 1.00 15.05 ? 31   PHE   B CB   1 
ATOM   9909  C  CG   . PHE   B 1 31  ? 25.011 0.016   70.920 1.00 16.32 ? 31   PHE   B CG   1 
ATOM   9910  C  CD1  . PHE   B 1 31  ? 24.374 0.540   72.033 1.00 16.83 ? 31   PHE   B CD1  1 
ATOM   9911  C  CD2  . PHE   B 1 31  ? 25.860 -1.064  71.096 1.00 19.06 ? 31   PHE   B CD2  1 
ATOM   9912  C  CE1  . PHE   B 1 31  ? 24.592 0.006   73.293 1.00 17.42 ? 31   PHE   B CE1  1 
ATOM   9913  C  CE2  . PHE   B 1 31  ? 26.078 -1.597  72.356 1.00 23.38 ? 31   PHE   B CE2  1 
ATOM   9914  C  CZ   . PHE   B 1 31  ? 25.443 -1.062  73.452 1.00 19.07 ? 31   PHE   B CZ   1 
ATOM   9915  H  H    . PHE   B 1 31  ? 24.559 -1.662  68.286 1.00 21.70 ? 31   PHE   B H    1 
ATOM   9916  H  HA   . PHE   B 1 31  ? 22.796 0.157   69.413 1.00 21.13 ? 31   PHE   B HA   1 
ATOM   9917  H  HB2  . PHE   B 1 31  ? 25.555 0.453   69.002 1.00 18.07 ? 31   PHE   B HB2  1 
ATOM   9918  H  HB3  . PHE   B 1 31  ? 24.638 1.550   69.626 1.00 18.07 ? 31   PHE   B HB3  1 
ATOM   9919  H  HD1  . PHE   B 1 31  ? 23.793 1.259   71.933 1.00 20.20 ? 31   PHE   B HD1  1 
ATOM   9920  H  HD2  . PHE   B 1 31  ? 26.289 -1.436  70.359 1.00 22.88 ? 31   PHE   B HD2  1 
ATOM   9921  H  HE1  . PHE   B 1 31  ? 24.162 0.371   74.032 1.00 20.91 ? 31   PHE   B HE1  1 
ATOM   9922  H  HE2  . PHE   B 1 31  ? 26.655 -2.319  72.461 1.00 28.06 ? 31   PHE   B HE2  1 
ATOM   9923  H  HZ   . PHE   B 1 31  ? 25.589 -1.421  74.297 1.00 22.89 ? 31   PHE   B HZ   1 
ATOM   9924  N  N    . ILE   B 1 32  ? 22.800 -0.166  66.492 1.00 15.96 ? 32   ILE   B N    1 
ATOM   9925  C  CA   . ILE   B 1 32  ? 22.325 0.336   65.160 1.00 14.52 ? 32   ILE   B CA   1 
ATOM   9926  C  C    . ILE   B 1 32  ? 23.450 0.988   64.345 1.00 16.91 ? 32   ILE   B C    1 
ATOM   9927  O  O    . ILE   B 1 32  ? 23.659 0.558   63.201 1.00 16.45 ? 32   ILE   B O    1 
ATOM   9928  C  CB   . ILE   B 1 32  ? 21.109 1.272   65.319 1.00 16.22 ? 32   ILE   B CB   1 
ATOM   9929  C  CG1  . ILE   B 1 32  ? 19.998 0.607   66.134 1.00 16.23 ? 32   ILE   B CG1  1 
ATOM   9930  C  CG2  . ILE   B 1 32  ? 20.610 1.734   63.960 1.00 17.55 ? 32   ILE   B CG2  1 
ATOM   9931  C  CD1  . ILE   B 1 32  ? 18.749 1.443   66.264 1.00 14.77 ? 32   ILE   B CD1  1 
ATOM   9932  H  H    . ILE   B 1 32  ? 22.793 -1.024  66.557 1.00 19.16 ? 32   ILE   B H    1 
ATOM   9933  H  HA   . ILE   B 1 32  ? 22.035 -0.437  64.650 1.00 17.43 ? 32   ILE   B HA   1 
ATOM   9934  H  HB   . ILE   B 1 32  ? 21.392 2.057   65.814 1.00 19.47 ? 32   ILE   B HB   1 
ATOM   9935  H  HG12 . ILE   B 1 32  ? 19.768 -0.239  65.720 1.00 19.48 ? 32   ILE   B HG12 1 
ATOM   9936  H  HG13 . ILE   B 1 32  ? 20.336 0.406   67.021 1.00 19.48 ? 32   ILE   B HG13 1 
ATOM   9937  H  HG21 . ILE   B 1 32  ? 19.847 2.321   64.078 1.00 21.07 ? 32   ILE   B HG21 1 
ATOM   9938  H  HG22 . ILE   B 1 32  ? 21.318 2.213   63.501 1.00 21.07 ? 32   ILE   B HG22 1 
ATOM   9939  H  HG23 . ILE   B 1 32  ? 20.347 0.964   63.433 1.00 21.07 ? 32   ILE   B HG23 1 
ATOM   9940  H  HD11 . ILE   B 1 32  ? 18.091 0.962   66.790 1.00 17.72 ? 32   ILE   B HD11 1 
ATOM   9941  H  HD12 . ILE   B 1 32  ? 18.964 2.281   66.703 1.00 17.72 ? 32   ILE   B HD12 1 
ATOM   9942  H  HD13 . ILE   B 1 32  ? 18.388 1.625   65.382 1.00 17.72 ? 32   ILE   B HD13 1 
ATOM   9943  N  N    . GLY   B 1 33  ? 24.148 1.963   64.917 1.00 16.85 ? 33   GLY   B N    1 
ATOM   9944  C  CA   . GLY   B 1 33  ? 25.199 2.669   64.166 1.00 15.15 ? 33   GLY   B CA   1 
ATOM   9945  C  C    . GLY   B 1 33  ? 25.207 4.139   64.520 1.00 15.86 ? 33   GLY   B C    1 
ATOM   9946  O  O    . GLY   B 1 33  ? 24.574 4.465   65.542 1.00 15.16 ? 33   GLY   B O    1 
ATOM   9947  H  H    . GLY   B 1 33  ? 24.036 2.233   65.726 1.00 20.23 ? 33   GLY   B H    1 
ATOM   9948  H  HA2  . GLY   B 1 33  ? 26.064 2.278   64.365 1.00 18.18 ? 33   GLY   B HA2  1 
ATOM   9949  H  HA3  . GLY   B 1 33  ? 25.051 2.561   63.213 1.00 18.18 ? 33   GLY   B HA3  1 
ATOM   9950  N  N    . CYS   B 1 34  ? 25.901 4.962   63.725 1.00 13.55 ? 34   CYS   B N    1 
ATOM   9951  C  CA   . CYS   B 1 34  ? 25.949 6.431   63.944 1.00 14.07 ? 34   CYS   B CA   1 
ATOM   9952  C  C    . CYS   B 1 34  ? 25.868 6.755   65.439 1.00 13.36 ? 34   CYS   B C    1 
ATOM   9953  O  O    . CYS   B 1 34  ? 26.774 6.344   66.180 1.00 14.10 ? 34   CYS   B O    1 
ATOM   9954  C  CB   . CYS   B 1 34  ? 24.790 7.085   63.201 1.00 16.03 ? 34   CYS   B CB   1 
ATOM   9955  S  SG   . CYS   B 1 34  ? 25.110 8.800   62.711 1.00 14.06 ? 34   CYS   B SG   1 
ATOM   9956  H  H    . CYS   B 1 34  ? 26.357 4.694   63.046 1.00 16.27 ? 34   CYS   B H    1 
ATOM   9957  H  HA   . CYS   B 1 34  ? 26.789 6.777   63.605 1.00 16.89 ? 34   CYS   B HA   1 
ATOM   9958  H  HB2  . CYS   B 1 34  ? 24.589 6.563   62.408 1.00 19.24 ? 34   CYS   B HB2  1 
ATOM   9959  H  HB3  . CYS   B 1 34  ? 24.001 7.060   63.764 1.00 19.24 ? 34   CYS   B HB3  1 
ATOM   9960  H  HG   . CYS   B 1 34  ? 26.272 8.929   62.441 1.00 16.88 ? 34   CYS   B HG   1 
ATOM   9961  N  N    . ARG   B 1 35  ? 24.814 7.462   65.853 1.00 15.00 ? 35   ARG   B N    1 
ATOM   9962  C  CA   . ARG   B 1 35  ? 24.653 7.882   67.274 1.00 13.53 ? 35   ARG   B CA   1 
ATOM   9963  C  C    . ARG   B 1 35  ? 25.022 6.771   68.262 1.00 14.43 ? 35   ARG   B C    1 
ATOM   9964  O  O    . ARG   B 1 35  ? 25.985 6.965   69.022 1.00 12.83 ? 35   ARG   B O    1 
ATOM   9965  C  CB   . ARG   B 1 35  ? 23.190 8.275   67.508 1.00 14.45 ? 35   ARG   B CB   1 
ATOM   9966  C  CG   . ARG   B 1 35  ? 22.917 8.933   68.852 1.00 13.03 ? 35   ARG   B CG   1 
ATOM   9967  C  CD   . ARG   B 1 35  ? 21.570 9.631   68.847 1.00 14.95 ? 35   ARG   B CD   1 
ATOM   9968  N  NE   . ARG   B 1 35  ? 21.005 9.818   70.175 1.00 13.30 ? 35   ARG   B NE   1 
ATOM   9969  C  CZ   . ARG   B 1 35  ? 19.765 10.228  70.412 1.00 14.59 ? 35   ARG   B CZ   1 
ATOM   9970  N  NH1  . ARG   B 1 35  ? 18.956 10.510  69.406 1.00 14.23 ? 35   ARG   B NH1  1 
ATOM   9971  N  NH2  . ARG   B 1 35  ? 19.336 10.357  71.656 1.00 13.78 ? 35   ARG   B NH2  1 
ATOM   9972  H  H    . ARG   B 1 35  ? 24.175 7.714   65.336 1.00 18.01 ? 35   ARG   B H    1 
ATOM   9973  H  HA   . ARG   B 1 35  ? 25.254 8.627   67.429 1.00 16.23 ? 35   ARG   B HA   1 
ATOM   9974  H  HB2  . ARG   B 1 35  ? 22.914 8.881   66.803 1.00 17.34 ? 35   ARG   B HB2  1 
ATOM   9975  H  HB3  . ARG   B 1 35  ? 22.638 7.481   67.432 1.00 17.34 ? 35   ARG   B HB3  1 
ATOM   9976  H  HG2  . ARG   B 1 35  ? 22.937 8.264   69.554 1.00 15.64 ? 35   ARG   B HG2  1 
ATOM   9977  H  HG3  . ARG   B 1 35  ? 23.617 9.574   69.051 1.00 15.64 ? 35   ARG   B HG3  1 
ATOM   9978  H  HD2  . ARG   B 1 35  ? 21.664 10.496  68.419 1.00 17.95 ? 35   ARG   B HD2  1 
ATOM   9979  H  HD3  . ARG   B 1 35  ? 20.949 9.115   68.309 1.00 17.95 ? 35   ARG   B HD3  1 
ATOM   9980  H  HE   . ARG   B 1 35  ? 21.509 9.652   70.852 1.00 15.97 ? 35   ARG   B HE   1 
ATOM   9981  H  HH11 . ARG   B 1 35  ? 19.233 10.428  68.596 1.00 17.08 ? 35   ARG   B HH11 1 
ATOM   9982  H  HH12 . ARG   B 1 35  ? 18.153 10.775  69.561 1.00 17.08 ? 35   ARG   B HH12 1 
ATOM   9983  H  HH21 . ARG   B 1 35  ? 19.861 10.175  72.313 1.00 16.53 ? 35   ARG   B HH21 1 
ATOM   9984  H  HH22 . ARG   B 1 35  ? 18.532 10.623  71.808 1.00 16.53 ? 35   ARG   B HH22 1 
ATOM   9985  N  N    . GLY   B 1 36  ? 24.274 5.667   68.265 1.00 14.10 ? 36   GLY   B N    1 
ATOM   9986  C  CA   . GLY   B 1 36  ? 24.480 4.609   69.276 1.00 15.31 ? 36   GLY   B CA   1 
ATOM   9987  C  C    . GLY   B 1 36  ? 25.880 4.026   69.221 1.00 12.43 ? 36   GLY   B C    1 
ATOM   9988  O  O    . GLY   B 1 36  ? 26.468 3.804   70.285 1.00 14.23 ? 36   GLY   B O    1 
ATOM   9989  H  H    . GLY   B 1 36  ? 23.647 5.506   67.699 1.00 16.92 ? 36   GLY   B H    1 
ATOM   9990  H  HA2  . GLY   B 1 36  ? 24.318 4.973   70.160 1.00 18.38 ? 36   GLY   B HA2  1 
ATOM   9991  H  HA3  . GLY   B 1 36  ? 23.831 3.901   69.138 1.00 18.38 ? 36   GLY   B HA3  1 
ATOM   9992  N  N    . LEU   B 1 37  ? 26.385 3.787   68.009 1.00 13.12 ? 37   LEU   B N    1 
ATOM   9993  C  CA   . LEU   B 1 37  ? 27.745 3.213   67.852 1.00 14.10 ? 37   LEU   B CA   1 
ATOM   9994  C  C    . LEU   B 1 37  ? 28.779 4.206   68.392 1.00 16.69 ? 37   LEU   B C    1 
ATOM   9995  O  O    . LEU   B 1 37  ? 29.708 3.775   69.090 1.00 15.48 ? 37   LEU   B O    1 
ATOM   9996  C  CB   . LEU   B 1 37  ? 27.993 2.904   66.372 1.00 14.45 ? 37   LEU   B CB   1 
ATOM   9997  C  CG   . LEU   B 1 37  ? 29.439 2.575   66.006 1.00 14.45 ? 37   LEU   B CG   1 
ATOM   9998  C  CD1  . LEU   B 1 37  ? 29.898 1.298   66.694 1.00 17.06 ? 37   LEU   B CD1  1 
ATOM   9999  C  CD2  . LEU   B 1 37  ? 29.605 2.459   64.499 1.00 14.57 ? 37   LEU   B CD2  1 
ATOM   10000 H  H    . LEU   B 1 37  ? 25.972 3.944   67.271 1.00 15.75 ? 37   LEU   B H    1 
ATOM   10001 H  HA   . LEU   B 1 37  ? 27.824 2.387   68.355 1.00 16.92 ? 37   LEU   B HA   1 
ATOM   10002 H  HB2  . LEU   B 1 37  ? 27.432 2.156   66.115 1.00 17.34 ? 37   LEU   B HB2  1 
ATOM   10003 H  HB3  . LEU   B 1 37  ? 27.707 3.667   65.845 1.00 17.34 ? 37   LEU   B HB3  1 
ATOM   10004 H  HG   . LEU   B 1 37  ? 29.997 3.304   66.318 1.00 17.34 ? 37   LEU   B HG   1 
ATOM   10005 H  HD11 . LEU   B 1 37  ? 30.817 1.110   66.447 1.00 20.47 ? 37   LEU   B HD11 1 
ATOM   10006 H  HD12 . LEU   B 1 37  ? 29.838 1.409   67.656 1.00 20.47 ? 37   LEU   B HD12 1 
ATOM   10007 H  HD13 . LEU   B 1 37  ? 29.332 0.560   66.418 1.00 20.47 ? 37   LEU   B HD13 1 
ATOM   10008 H  HD21 . LEU   B 1 37  ? 30.529 2.250   64.290 1.00 17.49 ? 37   LEU   B HD21 1 
ATOM   10009 H  HD22 . LEU   B 1 37  ? 29.031 1.753   64.163 1.00 17.49 ? 37   LEU   B HD22 1 
ATOM   10010 H  HD23 . LEU   B 1 37  ? 29.362 3.300   64.081 1.00 17.49 ? 37   LEU   B HD23 1 
ATOM   10011 N  N    . GLY   B 1 38  ? 28.642 5.490   68.070 1.00 14.16 ? 38   GLY   B N    1 
ATOM   10012 C  CA   . GLY   B 1 38  ? 29.596 6.494   68.570 1.00 14.44 ? 38   GLY   B CA   1 
ATOM   10013 C  C    . GLY   B 1 38  ? 29.591 6.603   70.089 1.00 13.70 ? 38   GLY   B C    1 
ATOM   10014 O  O    . GLY   B 1 38  ? 30.675 6.679   70.677 1.00 14.94 ? 38   GLY   B O    1 
ATOM   10015 H  H    . GLY   B 1 38  ? 28.015 5.803   67.571 1.00 17.00 ? 38   GLY   B H    1 
ATOM   10016 H  HA2  . GLY   B 1 38  ? 30.489 6.265   68.269 1.00 17.33 ? 38   GLY   B HA2  1 
ATOM   10017 H  HA3  . GLY   B 1 38  ? 29.381 7.359   68.187 1.00 17.33 ? 38   GLY   B HA3  1 
ATOM   10018 N  N    . VAL   B 1 39  ? 28.403 6.644   70.692 1.00 13.92 ? 39   VAL   B N    1 
ATOM   10019 C  CA   . VAL   B 1 39  ? 28.293 6.804   72.172 1.00 14.52 ? 39   VAL   B CA   1 
ATOM   10020 C  C    . VAL   B 1 39  ? 28.905 5.573   72.854 1.00 16.73 ? 39   VAL   B C    1 
ATOM   10021 O  O    . VAL   B 1 39  ? 29.691 5.749   73.794 1.00 16.65 ? 39   VAL   B O    1 
ATOM   10022 C  CB   . VAL   B 1 39  ? 26.828 7.014   72.599 1.00 13.76 ? 39   VAL   B CB   1 
ATOM   10023 C  CG1  . VAL   B 1 39  ? 26.677 7.059   74.112 1.00 15.60 ? 39   VAL   B CG1  1 
ATOM   10024 C  CG2  . VAL   B 1 39  ? 26.229 8.260   71.965 1.00 14.87 ? 39   VAL   B CG2  1 
ATOM   10025 H  H    . VAL   B 1 39  ? 27.650 6.583   70.281 1.00 16.71 ? 39   VAL   B H    1 
ATOM   10026 H  HA   . VAL   B 1 39  ? 28.783 7.595   72.448 1.00 17.42 ? 39   VAL   B HA   1 
ATOM   10027 H  HB   . VAL   B 1 39  ? 26.334 6.245   72.275 1.00 16.51 ? 39   VAL   B HB   1 
ATOM   10028 H  HG11 . VAL   B 1 39  ? 25.744 7.192   74.340 1.00 18.73 ? 39   VAL   B HG11 1 
ATOM   10029 H  HG12 . VAL   B 1 39  ? 26.987 6.223   74.493 1.00 18.73 ? 39   VAL   B HG12 1 
ATOM   10030 H  HG13 . VAL   B 1 39  ? 27.204 7.791   74.468 1.00 18.73 ? 39   VAL   B HG13 1 
ATOM   10031 H  HG21 . VAL   B 1 39  ? 25.309 8.360   72.255 1.00 17.84 ? 39   VAL   B HG21 1 
ATOM   10032 H  HG22 . VAL   B 1 39  ? 26.740 9.039   72.236 1.00 17.84 ? 39   VAL   B HG22 1 
ATOM   10033 H  HG23 . VAL   B 1 39  ? 26.256 8.177   70.999 1.00 17.84 ? 39   VAL   B HG23 1 
ATOM   10034 N  N    . LYS   B 1 40  ? 28.545 4.381   72.382 1.00 15.27 ? 40   LYS   B N    1 
ATOM   10035 C  CA   . LYS   B 1 40  ? 29.132 3.140   72.953 1.00 15.78 ? 40   LYS   B CA   1 
ATOM   10036 C  C    . LYS   B 1 40  ? 30.660 3.219   72.839 1.00 20.16 ? 40   LYS   B C    1 
ATOM   10037 O  O    . LYS   B 1 40  ? 31.349 2.952   73.836 1.00 17.89 ? 40   LYS   B O    1 
ATOM   10038 C  CB   . LYS   B 1 40  ? 28.566 1.912   72.239 1.00 16.35 ? 40   LYS   B CB   1 
ATOM   10039 C  CG   . LYS   B 1 40  ? 29.040 0.569   72.777 1.00 20.96 ? 40   LYS   B CG   1 
ATOM   10040 C  CD   . LYS   B 1 40  ? 28.778 0.392   74.257 1.00 21.84 ? 40   LYS   B CD   1 
ATOM   10041 C  CE   . LYS   B 1 40  ? 29.105 -1.002  74.751 1.00 27.30 ? 40   LYS   B CE   1 
ATOM   10042 N  NZ   . LYS   B 1 40  ? 29.838 -0.971  76.038 1.00 29.54 ? 40   LYS   B NZ   1 
ATOM   10043 H  H    . LYS   B 1 40  ? 27.978 4.257   71.748 1.00 18.33 ? 40   LYS   B H    1 
ATOM   10044 H  HA   . LYS   B 1 40  ? 28.898 3.056   73.891 1.00 18.93 ? 40   LYS   B HA   1 
ATOM   10045 H  HB2  . LYS   B 1 40  ? 27.598 1.942   72.294 1.00 19.62 ? 40   LYS   B HB2  1 
ATOM   10046 H  HB3  . LYS   B 1 40  ? 28.799 1.967   71.299 1.00 19.62 ? 40   LYS   B HB3  1 
ATOM   10047 H  HG2  . LYS   B 1 40  ? 28.597 -0.143  72.289 1.00 25.16 ? 40   LYS   B HG2  1 
ATOM   10048 H  HG3  . LYS   B 1 40  ? 29.991 0.478   72.610 1.00 25.16 ? 40   LYS   B HG3  1 
ATOM   10049 H  HD2  . LYS   B 1 40  ? 29.305 1.038   74.753 1.00 26.21 ? 40   LYS   B HD2  1 
ATOM   10050 H  HD3  . LYS   B 1 40  ? 27.845 0.585   74.441 1.00 26.21 ? 40   LYS   B HD3  1 
ATOM   10051 H  HE2  . LYS   B 1 40  ? 28.284 -1.508  74.858 1.00 32.77 ? 40   LYS   B HE2  1 
ATOM   10052 H  HE3  . LYS   B 1 40  ? 29.639 -1.464  74.086 1.00 32.77 ? 40   LYS   B HE3  1 
ATOM   10053 H  HZ1  . LYS   B 1 40  ? 29.862 -1.790  76.386 1.00 35.45 ? 40   LYS   B HZ1  1 
ATOM   10054 H  HZ2  . LYS   B 1 40  ? 30.669 -0.683  75.900 1.00 35.45 ? 40   LYS   B HZ2  1 
ATOM   10055 H  HZ3  . LYS   B 1 40  ? 29.424 -0.421  76.602 1.00 35.45 ? 40   LYS   B HZ3  1 
ATOM   10056 N  N    . THR   B 1 41  ? 31.158 3.574   71.655 1.00 15.50 ? 41   THR   B N    1 
ATOM   10057 C  CA   . THR   B 1 41  ? 32.626 3.646   71.434 1.00 18.74 ? 41   THR   B CA   1 
ATOM   10058 C  C    . THR   B 1 41  ? 33.248 4.652   72.414 1.00 18.27 ? 41   THR   B C    1 
ATOM   10059 O  O    . THR   B 1 41  ? 34.285 4.326   73.013 1.00 19.50 ? 41   THR   B O    1 
ATOM   10060 C  CB   . THR   B 1 41  ? 32.926 3.951   69.956 1.00 17.84 ? 41   THR   B CB   1 
ATOM   10061 O  OG1  . THR   B 1 41  ? 32.283 2.970   69.142 1.00 17.33 ? 41   THR   B OG1  1 
ATOM   10062 C  CG2  . THR   B 1 41  ? 34.409 3.987   69.661 1.00 22.85 ? 41   THR   B CG2  1 
ATOM   10063 H  H    . THR   B 1 41  ? 30.680 3.776   70.969 1.00 18.61 ? 41   THR   B H    1 
ATOM   10064 H  HA   . THR   B 1 41  ? 33.039 2.788   71.619 1.00 22.50 ? 41   THR   B HA   1 
ATOM   10065 H  HB   . THR   B 1 41  ? 32.582 4.835   69.755 1.00 21.41 ? 41   THR   B HB   1 
ATOM   10066 H  HG1  . THR   B 1 41  ? 31.465 3.152   69.077 1.00 20.80 ? 41   THR   B HG1  1 
ATOM   10067 H  HG21 . THR   B 1 41  ? 34.547 4.182   68.721 1.00 27.42 ? 41   THR   B HG21 1 
ATOM   10068 H  HG22 . THR   B 1 41  ? 34.830 4.676   70.199 1.00 27.42 ? 41   THR   B HG22 1 
ATOM   10069 H  HG23 . THR   B 1 41  ? 34.802 3.126   69.874 1.00 27.42 ? 41   THR   B HG23 1 
ATOM   10070 N  N    . LEU   B 1 42  ? 32.628 5.823   72.583 1.00 16.65 ? 42   LEU   B N    1 
ATOM   10071 C  CA   . LEU   B 1 42  ? 33.191 6.870   73.475 1.00 15.93 ? 42   LEU   B CA   1 
ATOM   10072 C  C    . LEU   B 1 42  ? 33.170 6.389   74.934 1.00 17.64 ? 42   LEU   B C    1 
ATOM   10073 O  O    . LEU   B 1 42  ? 34.201 6.525   75.609 1.00 18.14 ? 42   LEU   B O    1 
ATOM   10074 C  CB   . LEU   B 1 42  ? 32.360 8.148   73.322 1.00 15.69 ? 42   LEU   B CB   1 
ATOM   10075 C  CG   . LEU   B 1 42  ? 32.887 9.362   74.085 1.00 16.79 ? 42   LEU   B CG   1 
ATOM   10076 C  CD1  . LEU   B 1 42  ? 34.145 9.912   73.432 1.00 17.19 ? 42   LEU   B CD1  1 
ATOM   10077 C  CD2  . LEU   B 1 42  ? 31.824 10.443  74.183 1.00 14.02 ? 42   LEU   B CD2  1 
ATOM   10078 H  H    . LEU   B 1 42  ? 31.889 6.038   72.200 1.00 19.98 ? 42   LEU   B H    1 
ATOM   10079 H  HA   . LEU   B 1 42  ? 34.112 7.051   73.229 1.00 19.12 ? 42   LEU   B HA   1 
ATOM   10080 H  HB2  . LEU   B 1 42  ? 32.310 8.373   72.380 1.00 18.83 ? 42   LEU   B HB2  1 
ATOM   10081 H  HB3  . LEU   B 1 42  ? 31.455 7.965   73.619 1.00 18.83 ? 42   LEU   B HB3  1 
ATOM   10082 H  HG   . LEU   B 1 42  ? 33.113 9.073   74.983 1.00 20.15 ? 42   LEU   B HG   1 
ATOM   10083 H  HD11 . LEU   B 1 42  ? 34.460 10.681  73.933 1.00 20.64 ? 42   LEU   B HD11 1 
ATOM   10084 H  HD12 . LEU   B 1 42  ? 34.832 9.227   73.425 1.00 20.64 ? 42   LEU   B HD12 1 
ATOM   10085 H  HD13 . LEU   B 1 42  ? 33.946 10.180  72.521 1.00 20.64 ? 42   LEU   B HD13 1 
ATOM   10086 H  HD21 . LEU   B 1 42  ? 32.179 11.203  74.670 1.00 16.83 ? 42   LEU   B HD21 1 
ATOM   10087 H  HD22 . LEU   B 1 42  ? 31.564 10.724  73.291 1.00 16.83 ? 42   LEU   B HD22 1 
ATOM   10088 H  HD23 . LEU   B 1 42  ? 31.049 10.094  74.650 1.00 16.83 ? 42   LEU   B HD23 1 
ATOM   10089 N  N    . PHE   B 1 43  ? 32.028 5.869   75.387 1.00 16.20 ? 43   PHE   B N    1 
ATOM   10090 C  CA   . PHE   B 1 43  ? 31.889 5.382   76.785 1.00 17.76 ? 43   PHE   B CA   1 
ATOM   10091 C  C    . PHE   B 1 43  ? 32.945 4.305   77.056 1.00 21.39 ? 43   PHE   B C    1 
ATOM   10092 O  O    . PHE   B 1 43  ? 33.521 4.274   78.158 1.00 19.15 ? 43   PHE   B O    1 
ATOM   10093 C  CB   . PHE   B 1 43  ? 30.476 4.821   76.963 1.00 19.69 ? 43   PHE   B CB   1 
ATOM   10094 C  CG   . PHE   B 1 43  ? 29.912 4.849   78.361 1.00 17.29 ? 43   PHE   B CG   1 
ATOM   10095 C  CD1  . PHE   B 1 43  ? 30.703 5.176   79.450 1.00 19.82 ? 43   PHE   B CD1  1 
ATOM   10096 C  CD2  . PHE   B 1 43  ? 28.581 4.535   78.585 1.00 17.56 ? 43   PHE   B CD2  1 
ATOM   10097 C  CE1  . PHE   B 1 43  ? 30.172 5.190   80.730 1.00 21.12 ? 43   PHE   B CE1  1 
ATOM   10098 C  CE2  . PHE   B 1 43  ? 28.052 4.550   79.865 1.00 20.07 ? 43   PHE   B CE2  1 
ATOM   10099 C  CZ   . PHE   B 1 43  ? 28.849 4.877   80.935 1.00 20.63 ? 43   PHE   B CZ   1 
ATOM   10100 H  H    . PHE   B 1 43  ? 31.317 5.785   74.910 1.00 19.44 ? 43   PHE   B H    1 
ATOM   10101 H  HA   . PHE   B 1 43  ? 32.026 6.106   77.416 1.00 21.32 ? 43   PHE   B HA   1 
ATOM   10102 H  HB2  . PHE   B 1 43  ? 29.877 5.318   76.384 1.00 23.64 ? 43   PHE   B HB2  1 
ATOM   10103 H  HB3  . PHE   B 1 43  ? 30.473 3.902   76.653 1.00 23.64 ? 43   PHE   B HB3  1 
ATOM   10104 H  HD1  . PHE   B 1 43  ? 31.599 5.388   79.321 1.00 23.78 ? 43   PHE   B HD1  1 
ATOM   10105 H  HD2  . PHE   B 1 43  ? 28.035 4.311   77.866 1.00 21.08 ? 43   PHE   B HD2  1 
ATOM   10106 H  HE1  . PHE   B 1 43  ? 30.713 5.412   81.453 1.00 25.34 ? 43   PHE   B HE1  1 
ATOM   10107 H  HE2  . PHE   B 1 43  ? 27.157 4.339   80.000 1.00 24.08 ? 43   PHE   B HE2  1 
ATOM   10108 H  HZ   . PHE   B 1 43  ? 28.495 4.887   81.795 1.00 24.76 ? 43   PHE   B HZ   1 
ATOM   10109 N  N    . ASP   B 1 44  ? 33.190 3.448   76.068 1.00 20.07 ? 44   ASP   B N    1 
ATOM   10110 C  CA   . ASP   B 1 44  ? 34.137 2.320   76.262 1.00 19.21 ? 44   ASP   B CA   1 
ATOM   10111 C  C    . ASP   B 1 44  ? 35.587 2.797   76.286 1.00 21.01 ? 44   ASP   B C    1 
ATOM   10112 O  O    . ASP   B 1 44  ? 36.427 2.057   76.813 1.00 23.31 ? 44   ASP   B O    1 
ATOM   10113 C  CB   . ASP   B 1 44  ? 33.998 1.306   75.126 1.00 19.77 ? 44   ASP   B CB   1 
ATOM   10114 C  CG   . ASP   B 1 44  ? 32.771 0.420   75.218 1.00 21.01 ? 44   ASP   B CG   1 
ATOM   10115 O  OD1  . ASP   B 1 44  ? 32.107 0.450   76.267 1.00 23.87 ? 44   ASP   B OD1  1 
ATOM   10116 O  OD2  . ASP   B 1 44  ? 32.499 -0.297  74.240 1.00 22.36 ? 44   ASP   B OD2  1 
ATOM   10117 H  H    . ASP   B 1 44  ? 32.832 3.490   75.287 1.00 24.09 ? 44   ASP   B H    1 
ATOM   10118 H  HA   . ASP   B 1 44  ? 33.917 1.914   77.115 1.00 23.06 ? 44   ASP   B HA   1 
ATOM   10119 H  HB2  . ASP   B 1 44  ? 33.975 1.784   74.282 1.00 23.73 ? 44   ASP   B HB2  1 
ATOM   10120 H  HB3  . ASP   B 1 44  ? 34.788 0.744   75.112 1.00 23.73 ? 44   ASP   B HB3  1 
ATOM   10121 N  N    . GLU   B 1 45  ? 35.873 3.990   75.769 1.00 20.00 ? 45   GLU   B N    1 
ATOM   10122 C  CA   . GLU   B 1 45  ? 37.263 4.394   75.619 1.00 22.88 ? 45   GLU   B CA   1 
ATOM   10123 C  C    . GLU   B 1 45  ? 37.669 5.602   76.455 1.00 24.49 ? 45   GLU   B C    1 
ATOM   10124 O  O    . GLU   B 1 45  ? 38.868 5.879   76.545 1.00 23.48 ? 45   GLU   B O    1 
ATOM   10125 C  CB   . GLU   B 1 45  ? 37.569 4.668   74.138 1.00 22.31 ? 45   GLU   B CB   1 
ATOM   10126 C  CG   . GLU   B 1 45  ? 37.317 3.453   73.244 1.00 22.08 ? 45   GLU   B CG   1 
ATOM   10127 C  CD   . GLU   B 1 45  ? 38.021 3.530   71.900 1.00 22.93 ? 45   GLU   B CD   1 
ATOM   10128 O  OE1  . GLU   B 1 45  ? 38.678 4.556   71.621 1.00 22.55 ? 45   GLU   B OE1  1 
ATOM   10129 O  OE2  . GLU   B 1 45  ? 37.905 2.560   71.117 1.00 22.31 ? 45   GLU   B OE2  1 
ATOM   10130 H  H    . GLU   B 1 45  ? 35.291 4.566   75.505 1.00 24.01 ? 45   GLU   B H    1 
ATOM   10131 H  HA   . GLU   B 1 45  ? 37.788 3.650   75.954 1.00 27.46 ? 45   GLU   B HA   1 
ATOM   10132 H  HB2  . GLU   B 1 45  ? 37.023 5.409   73.831 1.00 26.78 ? 45   GLU   B HB2  1 
ATOM   10133 H  HB3  . GLU   B 1 45  ? 38.495 4.943   74.049 1.00 26.78 ? 45   GLU   B HB3  1 
ATOM   10134 H  HG2  . GLU   B 1 45  ? 37.609 2.653   73.708 1.00 26.51 ? 45   GLU   B HG2  1 
ATOM   10135 H  HG3  . GLU   B 1 45  ? 36.363 3.362   73.096 1.00 26.51 ? 45   GLU   B HG3  1 
ATOM   10136 N  N    . ILE   B 1 46  ? 36.727 6.325   77.069 1.00 20.37 ? 46   ILE   B N    1 
ATOM   10137 C  CA   . ILE   B 1 46  ? 37.083 7.463   77.909 1.00 20.92 ? 46   ILE   B CA   1 
ATOM   10138 C  C    . ILE   B 1 46  ? 36.446 7.325   79.287 1.00 24.22 ? 46   ILE   B C    1 
ATOM   10139 O  O    . ILE   B 1 46  ? 35.502 6.558   79.500 1.00 22.38 ? 46   ILE   B O    1 
ATOM   10140 C  CB   . ILE   B 1 46  ? 36.691 8.826   77.290 1.00 21.48 ? 46   ILE   B CB   1 
ATOM   10141 C  CG1  . ILE   B 1 46  ? 35.186 9.078   77.422 1.00 20.26 ? 46   ILE   B CG1  1 
ATOM   10142 C  CG2  . ILE   B 1 46  ? 37.159 8.927   75.840 1.00 22.61 ? 46   ILE   B CG2  1 
ATOM   10143 C  CD1  . ILE   B 1 46  ? 34.793 10.538  77.214 1.00 19.42 ? 46   ILE   B CD1  1 
ATOM   10144 H  H    . ILE   B 1 46  ? 35.883 6.171   77.010 1.00 24.45 ? 46   ILE   B H    1 
ATOM   10145 H  HA   . ILE   B 1 46  ? 38.050 7.452   77.985 1.00 25.11 ? 46   ILE   B HA   1 
ATOM   10146 H  HB   . ILE   B 1 46  ? 37.145 9.524   77.788 1.00 25.78 ? 46   ILE   B HB   1 
ATOM   10147 H  HG12 . ILE   B 1 46  ? 34.715 8.529   76.776 1.00 24.32 ? 46   ILE   B HG12 1 
ATOM   10148 H  HG13 . ILE   B 1 46  ? 34.894 8.794   78.302 1.00 24.32 ? 46   ILE   B HG13 1 
ATOM   10149 H  HG21 . ILE   B 1 46  ? 36.902 9.788   75.476 1.00 27.13 ? 46   ILE   B HG21 1 
ATOM   10150 H  HG22 . ILE   B 1 46  ? 38.124 8.837   75.804 1.00 27.13 ? 46   ILE   B HG22 1 
ATOM   10151 H  HG23 . ILE   B 1 46  ? 36.749 8.220   75.317 1.00 27.13 ? 46   ILE   B HG23 1 
ATOM   10152 H  HD11 . ILE   B 1 46  ? 33.832 10.632  77.310 1.00 23.31 ? 46   ILE   B HD11 1 
ATOM   10153 H  HD12 . ILE   B 1 46  ? 35.239 11.091  77.875 1.00 23.31 ? 46   ILE   B HD12 1 
ATOM   10154 H  HD13 . ILE   B 1 46  ? 35.058 10.821  76.325 1.00 23.31 ? 46   ILE   B HD13 1 
ATOM   10155 N  N    . ASP   B 1 47  ? 36.998 8.089   80.230 1.00 24.72 ? 47   ASP   B N    1 
ATOM   10156 C  CA   . ASP   B 1 47  ? 36.390 8.278   81.538 1.00 22.59 ? 47   ASP   B CA   1 
ATOM   10157 C  C    . ASP   B 1 47  ? 35.446 9.466   81.426 1.00 25.95 ? 47   ASP   B C    1 
ATOM   10158 O  O    . ASP   B 1 47  ? 35.918 10.602  81.247 1.00 20.23 ? 47   ASP   B O    1 
ATOM   10159 C  CB   . ASP   B 1 47  ? 37.466 8.519   82.593 1.00 27.18 ? 47   ASP   B CB   1 
ATOM   10160 C  CG   . ASP   B 1 47  ? 36.921 9.102   83.890 1.00 31.50 ? 47   ASP   B CG   1 
ATOM   10161 O  OD1  . ASP   B 1 47  ? 35.722 8.908   84.200 1.00 28.55 ? 47   ASP   B OD1  1 
ATOM   10162 O  OD2  . ASP   B 1 47  ? 37.721 9.727   84.626 1.00 35.93 ? 47   ASP   B OD2  1 
ATOM   10163 H  H    . ASP   B 1 47  ? 37.739 8.512   80.124 1.00 29.67 ? 47   ASP   B H    1 
ATOM   10164 H  HA   . ASP   B 1 47  ? 35.899 7.488   81.813 1.00 27.11 ? 47   ASP   B HA   1 
ATOM   10165 H  HB2  . ASP   B 1 47  ? 37.914 7.680   82.786 1.00 32.62 ? 47   ASP   B HB2  1 
ATOM   10166 H  HB3  . ASP   B 1 47  ? 38.135 9.121   82.231 1.00 32.62 ? 47   ASP   B HB3  1 
ATOM   10167 N  N    . PRO   B 1 48  ? 34.126 9.267   81.508 1.00 21.77 ? 48   PRO   B N    1 
ATOM   10168 C  CA   . PRO   B 1 48  ? 33.188 10.374  81.259 1.00 22.56 ? 48   PRO   B CA   1 
ATOM   10169 C  C    . PRO   B 1 48  ? 33.410 11.596  82.138 1.00 20.36 ? 48   PRO   B C    1 
ATOM   10170 O  O    . PRO   B 1 48  ? 32.905 12.674  81.813 1.00 20.87 ? 48   PRO   B O    1 
ATOM   10171 C  CB   . PRO   B 1 48  ? 31.818 9.736   81.524 1.00 17.63 ? 48   PRO   B CB   1 
ATOM   10172 C  CG   . PRO   B 1 48  ? 32.036 8.270   81.236 1.00 18.14 ? 48   PRO   B CG   1 
ATOM   10173 C  CD   . PRO   B 1 48  ? 33.430 7.985   81.723 1.00 22.50 ? 48   PRO   B CD   1 
ATOM   10174 H  HA   . PRO   B 1 48  ? 33.295 10.729  80.363 1.00 27.07 ? 48   PRO   B HA   1 
ATOM   10175 H  HB2  . PRO   B 1 48  ? 31.531 9.879   82.439 1.00 21.16 ? 48   PRO   B HB2  1 
ATOM   10176 H  HB3  . PRO   B 1 48  ? 31.133 10.113  80.949 1.00 21.16 ? 48   PRO   B HB3  1 
ATOM   10177 H  HG2  . PRO   B 1 48  ? 31.383 7.720   81.697 1.00 21.77 ? 48   PRO   B HG2  1 
ATOM   10178 H  HG3  . PRO   B 1 48  ? 31.949 8.081   80.289 1.00 21.77 ? 48   PRO   B HG3  1 
ATOM   10179 H  HD2  . PRO   B 1 48  ? 33.438 7.725   82.657 1.00 27.00 ? 48   PRO   B HD2  1 
ATOM   10180 H  HD3  . PRO   B 1 48  ? 33.844 7.264   81.224 1.00 27.00 ? 48   PRO   B HD3  1 
ATOM   10181 N  N    . LYS   B 1 49  ? 34.171 11.458  83.230 1.00 20.81 ? 49   LYS   B N    1 
ATOM   10182 C  CA   . LYS   B 1 49  ? 34.395 12.583  84.133 1.00 22.91 ? 49   LYS   B CA   1 
ATOM   10183 C  C    . LYS   B 1 49  ? 35.442 13.574  83.634 1.00 26.48 ? 49   LYS   B C    1 
ATOM   10184 O  O    . LYS   B 1 49  ? 35.587 14.640  84.240 1.00 22.05 ? 49   LYS   B O    1 
ATOM   10185 C  CB   . LYS   B 1 49  ? 34.807 12.082  85.522 1.00 25.05 ? 49   LYS   B CB   1 
ATOM   10186 C  CG   . LYS   B 1 49  ? 33.732 11.295  86.258 1.00 24.50 ? 49   LYS   B CG   1 
ATOM   10187 C  CD   . LYS   B 1 49  ? 34.219 10.779  87.616 1.00 25.93 ? 49   LYS   B CD   1 
ATOM   10188 C  CE   . LYS   B 1 49  ? 35.294 9.697   87.497 1.00 24.41 ? 49   LYS   B CE   1 
ATOM   10189 N  NZ   . LYS   B 1 49  ? 34.815 8.488   86.761 1.00 30.45 ? 49   LYS   B NZ   1 
ATOM   10190 H  H    . LYS   B 1 49  ? 34.561 10.727  83.461 1.00 24.97 ? 49   LYS   B H    1 
ATOM   10191 H  HA   . LYS   B 1 49  ? 33.549 13.056  84.175 1.00 27.49 ? 49   LYS   B HA   1 
ATOM   10192 H  HB2  . LYS   B 1 49  ? 35.594 11.523  85.431 1.00 30.06 ? 49   LYS   B HB2  1 
ATOM   10193 H  HB3  . LYS   B 1 49  ? 35.062 12.844  86.065 1.00 30.06 ? 49   LYS   B HB3  1 
ATOM   10194 H  HG2  . LYS   B 1 49  ? 32.953 11.858  86.388 1.00 29.40 ? 49   LYS   B HG2  1 
ATOM   10195 H  HG3  . LYS   B 1 49  ? 33.451 10.545  85.711 1.00 29.40 ? 49   LYS   B HG3  1 
ATOM   10196 H  HD2  . LYS   B 1 49  ? 34.571 11.522  88.131 1.00 31.13 ? 49   LYS   B HD2  1 
ATOM   10197 H  HD3  . LYS   B 1 49  ? 33.464 10.424  88.111 1.00 31.13 ? 49   LYS   B HD3  1 
ATOM   10198 H  HE2  . LYS   B 1 49  ? 36.068 10.064  87.041 1.00 29.29 ? 49   LYS   B HE2  1 
ATOM   10199 H  HE3  . LYS   B 1 49  ? 35.585 9.436   88.385 1.00 29.29 ? 49   LYS   B HE3  1 
ATOM   10200 H  HZ1  . LYS   B 1 49  ? 35.261 7.772   87.044 1.00 36.54 ? 49   LYS   B HZ1  1 
ATOM   10201 H  HZ2  . LYS   B 1 49  ? 33.945 8.374   86.911 1.00 36.54 ? 49   LYS   B HZ2  1 
ATOM   10202 H  HZ3  . LYS   B 1 49  ? 34.953 8.597   85.889 1.00 36.54 ? 49   LYS   B HZ3  1 
ATOM   10203 N  N    . ILE   B 1 50  ? 36.162 13.266  82.550 1.00 24.36 ? 50   ILE   B N    1 
ATOM   10204 C  CA   . ILE   B 1 50  ? 37.272 14.120  82.129 1.00 25.49 ? 50   ILE   B CA   1 
ATOM   10205 C  C    . ILE   B 1 50  ? 36.789 15.497  81.664 1.00 26.35 ? 50   ILE   B C    1 
ATOM   10206 O  O    . ILE   B 1 50  ? 35.628 15.694  81.284 1.00 24.22 ? 50   ILE   B O    1 
ATOM   10207 C  CB   . ILE   B 1 50  ? 38.084 13.438  81.018 1.00 28.84 ? 50   ILE   B CB   1 
ATOM   10208 C  CG1  . ILE   B 1 50  ? 37.199 13.221  79.793 1.00 27.73 ? 50   ILE   B CG1  1 
ATOM   10209 C  CG2  . ILE   B 1 50  ? 38.690 12.133  81.518 1.00 28.80 ? 50   ILE   B CG2  1 
ATOM   10210 C  CD1  . ILE   B 1 50  ? 37.960 12.835  78.576 1.00 29.30 ? 50   ILE   B CD1  1 
ATOM   10211 H  H    . ILE   B 1 50  ? 36.025 12.577  82.053 1.00 29.23 ? 50   ILE   B H    1 
ATOM   10212 H  HA   . ILE   B 1 50  ? 37.843 14.255  82.902 1.00 30.59 ? 50   ILE   B HA   1 
ATOM   10213 H  HB   . ILE   B 1 50  ? 38.821 14.013  80.759 1.00 34.61 ? 50   ILE   B HB   1 
ATOM   10214 H  HG12 . ILE   B 1 50  ? 36.547 12.530  79.991 1.00 33.28 ? 50   ILE   B HG12 1 
ATOM   10215 H  HG13 . ILE   B 1 50  ? 36.704 14.035  79.612 1.00 33.28 ? 50   ILE   B HG13 1 
ATOM   10216 H  HG21 . ILE   B 1 50  ? 39.198 11.717  80.804 1.00 34.56 ? 50   ILE   B HG21 1 
ATOM   10217 H  HG22 . ILE   B 1 50  ? 39.277 12.315  82.268 1.00 34.56 ? 50   ILE   B HG22 1 
ATOM   10218 H  HG23 . ILE   B 1 50  ? 37.981 11.534  81.801 1.00 34.56 ? 50   ILE   B HG23 1 
ATOM   10219 H  HD11 . ILE   B 1 50  ? 37.346 12.712  77.835 1.00 35.17 ? 50   ILE   B HD11 1 
ATOM   10220 H  HD12 . ILE   B 1 50  ? 38.595 13.534  78.356 1.00 35.17 ? 50   ILE   B HD12 1 
ATOM   10221 H  HD13 . ILE   B 1 50  ? 38.436 12.006  78.741 1.00 35.17 ? 50   ILE   B HD13 1 
ATOM   10222 N  N    . ASP   B 1 51  ? 37.709 16.462  81.714 1.00 22.73 ? 51   ASP   B N    1 
ATOM   10223 C  CA   . ASP   B 1 51  ? 37.560 17.731  81.010 1.00 25.22 ? 51   ASP   B CA   1 
ATOM   10224 C  C    . ASP   B 1 51  ? 37.383 17.491  79.519 1.00 21.34 ? 51   ASP   B C    1 
ATOM   10225 O  O    . ASP   B 1 51  ? 38.223 16.851  78.882 1.00 22.82 ? 51   ASP   B O    1 
ATOM   10226 C  CB   . ASP   B 1 51  ? 38.791 18.608  81.277 1.00 29.40 ? 51   ASP   B CB   1 
ATOM   10227 C  CG   . ASP   B 1 51  ? 38.679 20.005  80.673 1.00 34.64 ? 51   ASP   B CG   1 
ATOM   10228 O  OD1  . ASP   B 1 51  ? 37.663 20.324  80.020 1.00 27.54 ? 51   ASP   B OD1  1 
ATOM   10229 O  OD2  . ASP   B 1 51  ? 39.625 20.800  80.863 1.00 42.51 ? 51   ASP   B OD2  1 
ATOM   10230 H  H    . ASP   B 1 51  ? 38.441 16.396  82.161 1.00 27.28 ? 51   ASP   B H    1 
ATOM   10231 H  HA   . ASP   B 1 51  ? 36.769 18.189  81.335 1.00 30.27 ? 51   ASP   B HA   1 
ATOM   10232 H  HB2  . ASP   B 1 51  ? 38.923 18.686  82.235 1.00 35.28 ? 51   ASP   B HB2  1 
ATOM   10233 H  HB3  . ASP   B 1 51  ? 39.577 18.169  80.917 1.00 35.28 ? 51   ASP   B HB3  1 
ATOM   10234 N  N    . ALA   B 1 52  ? 36.284 18.012  78.964 1.00 22.68 ? 52   ALA   B N    1 
ATOM   10235 C  CA   . ALA   B 1 52  ? 35.991 17.802  77.550 1.00 18.62 ? 52   ALA   B CA   1 
ATOM   10236 C  C    . ALA   B 1 52  ? 37.009 18.467  76.631 1.00 18.49 ? 52   ALA   B C    1 
ATOM   10237 O  O    . ALA   B 1 52  ? 37.111 18.085  75.461 1.00 18.43 ? 52   ALA   B O    1 
ATOM   10238 C  CB   . ALA   B 1 52  ? 34.584 18.315  77.217 1.00 18.82 ? 52   ALA   B CB   1 
ATOM   10239 H  H    . ALA   B 1 52  ? 35.703 18.485  79.387 1.00 27.22 ? 52   ALA   B H    1 
ATOM   10240 H  HA   . ALA   B 1 52  ? 36.042 16.846  77.394 1.00 22.35 ? 52   ALA   B HA   1 
ATOM   10241 H  HB1  . ALA   B 1 52  ? 34.401 18.170  76.276 1.00 22.59 ? 52   ALA   B HB1  1 
ATOM   10242 H  HB2  . ALA   B 1 52  ? 33.930 17.837  77.750 1.00 22.59 ? 52   ALA   B HB2  1 
ATOM   10243 H  HB3  . ALA   B 1 52  ? 34.530 19.263  77.414 1.00 22.59 ? 52   ALA   B HB3  1 
ATOM   10244 N  N    . LEU   B 1 53  ? 37.760 19.450  77.122 1.00 21.34 ? 53   LEU   B N    1 
ATOM   10245 C  CA   . LEU   B 1 53  ? 38.797 20.094  76.329 1.00 21.21 ? 53   LEU   B CA   1 
ATOM   10246 C  C    . LEU   B 1 53  ? 40.180 19.510  76.584 1.00 20.50 ? 53   LEU   B C    1 
ATOM   10247 O  O    . LEU   B 1 53  ? 41.153 19.965  75.975 1.00 21.27 ? 53   LEU   B O    1 
ATOM   10248 C  CB   . LEU   B 1 53  ? 38.818 21.603  76.601 1.00 22.32 ? 53   LEU   B CB   1 
ATOM   10249 C  CG   . LEU   B 1 53  ? 37.518 22.355  76.306 1.00 21.65 ? 53   LEU   B CG   1 
ATOM   10250 C  CD1  . LEU   B 1 53  ? 37.681 23.839  76.609 1.00 23.36 ? 53   LEU   B CD1  1 
ATOM   10251 C  CD2  . LEU   B 1 53  ? 37.090 22.131  74.865 1.00 18.29 ? 53   LEU   B CD2  1 
ATOM   10252 H  H    . LEU   B 1 53  ? 37.682 19.759  77.921 1.00 25.61 ? 53   LEU   B H    1 
ATOM   10253 H  HA   . LEU   B 1 53  ? 38.578 19.929  75.399 1.00 25.45 ? 53   LEU   B HA   1 
ATOM   10254 H  HB2  . LEU   B 1 53  ? 39.047 21.743  77.533 1.00 26.78 ? 53   LEU   B HB2  1 
ATOM   10255 H  HB3  . LEU   B 1 53  ? 39.528 21.999  76.072 1.00 26.78 ? 53   LEU   B HB3  1 
ATOM   10256 H  HG   . LEU   B 1 53  ? 36.819 22.008  76.882 1.00 25.98 ? 53   LEU   B HG   1 
ATOM   10257 H  HD11 . LEU   B 1 53  ? 36.850 24.302  76.417 1.00 28.04 ? 53   LEU   B HD11 1 
ATOM   10258 H  HD12 . LEU   B 1 53  ? 37.907 23.955  77.545 1.00 28.04 ? 53   LEU   B HD12 1 
ATOM   10259 H  HD13 . LEU   B 1 53  ? 38.390 24.206  76.058 1.00 28.04 ? 53   LEU   B HD13 1 
ATOM   10260 H  HD21 . LEU   B 1 53  ? 36.266 22.613  74.693 1.00 21.95 ? 53   LEU   B HD21 1 
ATOM   10261 H  HD22 . LEU   B 1 53  ? 37.783 22.453  74.268 1.00 21.95 ? 53   LEU   B HD22 1 
ATOM   10262 H  HD23 . LEU   B 1 53  ? 36.948 21.184  74.713 1.00 21.95 ? 53   LEU   B HD23 1 
ATOM   10263 N  N    . SER   B 1 54  ? 40.292 18.518  77.460 1.00 20.73 ? 54   SER   B N    1 
ATOM   10264 C  CA   . SER   B 1 54  ? 41.574 17.878  77.695 1.00 20.84 ? 54   SER   B CA   1 
ATOM   10265 C  C    . SER   B 1 54  ? 41.910 16.925  76.551 1.00 20.99 ? 54   SER   B C    1 
ATOM   10266 O  O    . SER   B 1 54  ? 41.018 16.444  75.847 1.00 17.69 ? 54   SER   B O    1 
ATOM   10267 C  CB   . SER   B 1 54  ? 41.553 17.131  79.025 1.00 22.71 ? 54   SER   B CB   1 
ATOM   10268 O  OG   . SER   B 1 54  ? 40.792 15.942  78.932 1.00 24.65 ? 54   SER   B OG   1 
ATOM   10269 H  H    . SER   B 1 54  ? 39.640 18.204  77.925 1.00 24.88 ? 54   SER   B H    1 
ATOM   10270 H  HA   . SER   B 1 54  ? 42.261 18.562  77.735 1.00 25.01 ? 54   SER   B HA   1 
ATOM   10271 H  HB2  . SER   B 1 54  ? 42.460 16.917  79.293 1.00 27.26 ? 54   SER   B HB2  1 
ATOM   10272 H  HB3  . SER   B 1 54  ? 41.181 17.703  79.714 1.00 27.26 ? 54   SER   B HB3  1 
ATOM   10273 H  HG   . SER   B 1 54  ? 39.975 16.134  78.898 1.00 29.58 ? 54   SER   B HG   1 
ATOM   10274 N  N    . PRO   B 1 55  ? 43.199 16.644  76.342 1.00 24.09 ? 55   PRO   B N    1 
ATOM   10275 C  CA   . PRO   B 1 55  ? 43.590 15.713  75.270 1.00 22.37 ? 55   PRO   B CA   1 
ATOM   10276 C  C    . PRO   B 1 55  ? 42.935 14.340  75.361 1.00 21.62 ? 55   PRO   B C    1 
ATOM   10277 O  O    . PRO   B 1 55  ? 42.792 13.668  74.329 1.00 19.18 ? 55   PRO   B O    1 
ATOM   10278 C  CB   . PRO   B 1 55  ? 45.113 15.618  75.446 1.00 22.96 ? 55   PRO   B CB   1 
ATOM   10279 C  CG   . PRO   B 1 55  ? 45.493 16.928  76.058 1.00 25.14 ? 55   PRO   B CG   1 
ATOM   10280 C  CD   . PRO   B 1 55  ? 44.374 17.221  77.019 1.00 22.06 ? 55   PRO   B CD   1 
ATOM   10281 H  HA   . PRO   B 1 55  ? 43.304 16.032  74.400 1.00 26.85 ? 55   PRO   B HA   1 
ATOM   10282 H  HB2  . PRO   B 1 55  ? 45.358 14.875  76.019 1.00 27.56 ? 55   PRO   B HB2  1 
ATOM   10283 H  HB3  . PRO   B 1 55  ? 45.560 15.481  74.596 1.00 27.56 ? 55   PRO   B HB3  1 
ATOM   10284 H  HG2  . PRO   B 1 55  ? 46.347 16.872  76.514 1.00 30.17 ? 55   PRO   B HG2  1 
ATOM   10285 H  HG3  . PRO   B 1 55  ? 45.575 17.623  75.386 1.00 30.17 ? 55   PRO   B HG3  1 
ATOM   10286 H  HD2  . PRO   B 1 55  ? 44.527 16.811  77.885 1.00 26.48 ? 55   PRO   B HD2  1 
ATOM   10287 H  HD3  . PRO   B 1 55  ? 44.270 18.173  77.170 1.00 26.48 ? 55   PRO   B HD3  1 
ATOM   10288 N  N    . GLU   B 1 56  ? 42.521 13.910  76.557 1.00 18.64 ? 56   GLU   B N    1 
ATOM   10289 C  CA   . GLU   B 1 56  ? 42.008 12.554  76.733 1.00 22.76 ? 56   GLU   B CA   1 
ATOM   10290 C  C    . GLU   B 1 56  ? 40.590 12.373  76.200 1.00 19.31 ? 56   GLU   B C    1 
ATOM   10291 O  O    . GLU   B 1 56  ? 40.142 11.230  76.041 1.00 20.92 ? 56   GLU   B O    1 
ATOM   10292 C  CB   . GLU   B 1 56  ? 42.079 12.158  78.209 1.00 21.44 ? 56   GLU   B CB   1 
ATOM   10293 C  CG   . GLU   B 1 56  ? 43.503 11.926  78.705 1.00 27.89 ? 56   GLU   B CG   1 
ATOM   10294 C  CD   . GLU   B 1 56  ? 44.327 13.202  78.823 1.00 34.10 ? 56   GLU   B CD   1 
ATOM   10295 O  OE1  . GLU   B 1 56  ? 43.784 14.232  79.281 1.00 31.77 ? 56   GLU   B OE1  1 
ATOM   10296 O  OE2  . GLU   B 1 56  ? 45.518 13.173  78.445 1.00 36.39 ? 56   GLU   B OE2  1 
ATOM   10297 H  H    . GLU   B 1 56  ? 42.530 14.387  77.273 1.00 22.37 ? 56   GLU   B H    1 
ATOM   10298 H  HA   . GLU   B 1 56  ? 42.574 11.968  76.206 1.00 27.32 ? 56   GLU   B HA   1 
ATOM   10299 H  HB2  . GLU   B 1 56  ? 41.666 12.854  78.744 1.00 25.73 ? 56   GLU   B HB2  1 
ATOM   10300 H  HB3  . GLU   B 1 56  ? 41.560 11.350  78.346 1.00 25.73 ? 56   GLU   B HB3  1 
ATOM   10301 H  HG2  . GLU   B 1 56  ? 43.468 11.492  79.572 1.00 33.47 ? 56   GLU   B HG2  1 
ATOM   10302 H  HG3  . GLU   B 1 56  ? 43.952 11.315  78.100 1.00 33.47 ? 56   GLU   B HG3  1 
ATOM   10303 N  N    . ASN   B 1 57  ? 39.873 13.456  75.919 1.00 19.37 ? 57   ASN   B N    1 
ATOM   10304 C  CA   . ASN   B 1 57  ? 38.606 13.319  75.215 1.00 18.95 ? 57   ASN   B CA   1 
ATOM   10305 C  C    . ASN   B 1 57  ? 38.865 12.743  73.828 1.00 19.83 ? 57   ASN   B C    1 
ATOM   10306 O  O    . ASN   B 1 57  ? 39.949 12.898  73.259 1.00 21.17 ? 57   ASN   B O    1 
ATOM   10307 C  CB   . ASN   B 1 57  ? 37.897 14.678  75.122 1.00 18.33 ? 57   ASN   B CB   1 
ATOM   10308 C  CG   . ASN   B 1 57  ? 36.417 14.563  74.755 1.00 15.52 ? 57   ASN   B CG   1 
ATOM   10309 O  OD1  . ASN   B 1 57  ? 35.862 13.468  74.655 1.00 18.28 ? 57   ASN   B OD1  1 
ATOM   10310 N  ND2  . ASN   B 1 57  ? 35.769 15.711  74.565 1.00 16.59 ? 57   ASN   B ND2  1 
ATOM   10311 H  H    . ASN   B 1 57  ? 40.096 14.261  76.122 1.00 23.25 ? 57   ASN   B H    1 
ATOM   10312 H  HA   . ASN   B 1 57  ? 38.025 12.715  75.704 1.00 22.74 ? 57   ASN   B HA   1 
ATOM   10313 H  HB2  . ASN   B 1 57  ? 37.978 15.137  75.973 1.00 22.00 ? 57   ASN   B HB2  1 
ATOM   10314 H  HB3  . ASN   B 1 57  ? 38.347 15.226  74.460 1.00 22.00 ? 57   ASN   B HB3  1 
ATOM   10315 H  HD21 . ASN   B 1 57  ? 34.933 15.705  74.365 1.00 19.91 ? 57   ASN   B HD21 1 
ATOM   10316 H  HD22 . ASN   B 1 57  ? 36.187 16.459  74.643 1.00 19.91 ? 57   ASN   B HD22 1 
ATOM   10317 N  N    . LYS   B 1 58  ? 37.848 12.076  73.295 1.00 19.25 ? 58   LYS   B N    1 
ATOM   10318 C  CA   . LYS   B 1 58  ? 37.981 11.517  71.929 1.00 18.84 ? 58   LYS   B CA   1 
ATOM   10319 C  C    . LYS   B 1 58  ? 36.970 12.225  71.024 1.00 18.55 ? 58   LYS   B C    1 
ATOM   10320 O  O    . LYS   B 1 58  ? 35.835 12.452  71.477 1.00 17.08 ? 58   LYS   B O    1 
ATOM   10321 C  CB   . LYS   B 1 58  ? 37.814 9.994   71.939 1.00 17.28 ? 58   LYS   B CB   1 
ATOM   10322 C  CG   . LYS   B 1 58  ? 38.788 9.268   72.857 1.00 19.48 ? 58   LYS   B CG   1 
ATOM   10323 C  CD   . LYS   B 1 58  ? 39.365 8.000   72.275 1.00 19.12 ? 58   LYS   B CD   1 
ATOM   10324 C  CE   . LYS   B 1 58  ? 40.448 7.400   73.147 1.00 20.43 ? 58   LYS   B CE   1 
ATOM   10325 N  NZ   . LYS   B 1 58  ? 40.725 5.990   72.785 1.00 21.84 ? 58   LYS   B NZ   1 
ATOM   10326 H  H    . LYS   B 1 58  ? 37.093 11.933  73.682 1.00 23.10 ? 58   LYS   B H    1 
ATOM   10327 H  HA   . LYS   B 1 58  ? 38.872 11.677  71.580 1.00 22.62 ? 58   LYS   B HA   1 
ATOM   10328 H  HB2  . LYS   B 1 58  ? 36.908 9.779   72.210 1.00 20.74 ? 58   LYS   B HB2  1 
ATOM   10329 H  HB3  . LYS   B 1 58  ? 37.926 9.660   71.035 1.00 20.74 ? 58   LYS   B HB3  1 
ATOM   10330 H  HG2  . LYS   B 1 58  ? 39.516 9.870   73.079 1.00 23.38 ? 58   LYS   B HG2  1 
ATOM   10331 H  HG3  . LYS   B 1 58  ? 38.334 9.053   73.687 1.00 23.38 ? 58   LYS   B HG3  1 
ATOM   10332 H  HD2  . LYS   B 1 58  ? 38.654 7.351   72.155 1.00 22.94 ? 58   LYS   B HD2  1 
ATOM   10333 H  HD3  . LYS   B 1 58  ? 39.729 8.188   71.396 1.00 22.94 ? 58   LYS   B HD3  1 
ATOM   10334 H  HE2  . LYS   B 1 58  ? 41.261 7.922   73.060 1.00 24.52 ? 58   LYS   B HE2  1 
ATOM   10335 H  HE3  . LYS   B 1 58  ? 40.178 7.448   74.078 1.00 24.52 ? 58   LYS   B HE3  1 
ATOM   10336 H  HZ1  . LYS   B 1 58  ? 41.008 5.549   73.504 1.00 26.22 ? 58   LYS   B HZ1  1 
ATOM   10337 H  HZ2  . LYS   B 1 58  ? 39.981 5.610   72.479 1.00 26.22 ? 58   LYS   B HZ2  1 
ATOM   10338 H  HZ3  . LYS   B 1 58  ? 41.353 5.963   72.154 1.00 26.22 ? 58   LYS   B HZ3  1 
ATOM   10339 N  N    . PHE   B 1 59  ? 37.404 12.592  69.818 1.00 13.44 ? 59   PHE   B N    1 
ATOM   10340 C  CA   . PHE   B 1 59  ? 36.516 13.272  68.845 1.00 13.80 ? 59   PHE   B CA   1 
ATOM   10341 C  C    . PHE   B 1 59  ? 36.112 12.220  67.815 1.00 15.91 ? 59   PHE   B C    1 
ATOM   10342 O  O    . PHE   B 1 59  ? 36.962 11.839  66.996 1.00 15.47 ? 59   PHE   B O    1 
ATOM   10343 C  CB   . PHE   B 1 59  ? 37.246 14.467  68.235 1.00 14.27 ? 59   PHE   B CB   1 
ATOM   10344 C  CG   . PHE   B 1 59  ? 36.411 15.337  67.333 1.00 13.49 ? 59   PHE   B CG   1 
ATOM   10345 C  CD1  . PHE   B 1 59  ? 35.526 16.263  67.859 1.00 11.43 ? 59   PHE   B CD1  1 
ATOM   10346 C  CD2  . PHE   B 1 59  ? 36.518 15.236  65.956 1.00 15.73 ? 59   PHE   B CD2  1 
ATOM   10347 C  CE1  . PHE   B 1 59  ? 34.764 17.066  67.027 1.00 13.41 ? 59   PHE   B CE1  1 
ATOM   10348 C  CE2  . PHE   B 1 59  ? 35.753 16.038  65.125 1.00 15.24 ? 59   PHE   B CE2  1 
ATOM   10349 C  CZ   . PHE   B 1 59  ? 34.876 16.950  65.662 1.00 14.59 ? 59   PHE   B CZ   1 
ATOM   10350 H  H    . PHE   B 1 59  ? 38.206 12.461  69.536 1.00 16.13 ? 59   PHE   B H    1 
ATOM   10351 H  HA   . PHE   B 1 59  ? 35.715 13.632  69.257 1.00 16.57 ? 59   PHE   B HA   1 
ATOM   10352 H  HB2  . PHE   B 1 59  ? 37.597 15.015  68.954 1.00 17.13 ? 59   PHE   B HB2  1 
ATOM   10353 H  HB3  . PHE   B 1 59  ? 38.007 14.140  67.731 1.00 17.13 ? 59   PHE   B HB3  1 
ATOM   10354 H  HD1  . PHE   B 1 59  ? 35.442 16.347  68.781 1.00 13.72 ? 59   PHE   B HD1  1 
ATOM   10355 H  HD2  . PHE   B 1 59  ? 37.110 14.623  65.585 1.00 18.88 ? 59   PHE   B HD2  1 
ATOM   10356 H  HE1  . PHE   B 1 59  ? 34.175 17.686  67.393 1.00 16.10 ? 59   PHE   B HE1  1 
ATOM   10357 H  HE2  . PHE   B 1 59  ? 35.833 15.959  64.202 1.00 18.29 ? 59   PHE   B HE2  1 
ATOM   10358 H  HZ   . PHE   B 1 59  ? 34.360 17.486  65.104 1.00 17.51 ? 59   PHE   B HZ   1 
ATOM   10359 N  N    . ILE   B 1 60  ? 34.870 11.746  67.888 1.00 12.06 ? 60   ILE   B N    1 
ATOM   10360 C  CA   . ILE   B 1 60  ? 34.442 10.638  66.992 1.00 13.83 ? 60   ILE   B CA   1 
ATOM   10361 C  C    . ILE   B 1 60  ? 33.523 11.168  65.892 1.00 16.17 ? 60   ILE   B C    1 
ATOM   10362 O  O    . ILE   B 1 60  ? 32.578 11.903  66.218 1.00 14.67 ? 60   ILE   B O    1 
ATOM   10363 C  CB   . ILE   B 1 60  ? 33.741 9.531   67.804 1.00 14.26 ? 60   ILE   B CB   1 
ATOM   10364 C  CG1  . ILE   B 1 60  ? 34.684 8.914   68.839 1.00 14.20 ? 60   ILE   B CG1  1 
ATOM   10365 C  CG2  . ILE   B 1 60  ? 33.139 8.480   66.884 1.00 14.53 ? 60   ILE   B CG2  1 
ATOM   10366 C  CD1  . ILE   B 1 60  ? 34.018 7.907   69.745 1.00 17.49 ? 60   ILE   B CD1  1 
ATOM   10367 H  H    . ILE   B 1 60  ? 34.266 12.034  68.429 1.00 14.48 ? 60   ILE   B H    1 
ATOM   10368 H  HA   . ILE   B 1 60  ? 35.229 10.256  66.573 1.00 16.60 ? 60   ILE   B HA   1 
ATOM   10369 H  HB   . ILE   B 1 60  ? 33.011 9.938   68.296 1.00 17.12 ? 60   ILE   B HB   1 
ATOM   10370 H  HG12 . ILE   B 1 60  ? 35.421 8.484   68.377 1.00 17.05 ? 60   ILE   B HG12 1 
ATOM   10371 H  HG13 . ILE   B 1 60  ? 35.064 9.623   69.381 1.00 17.05 ? 60   ILE   B HG13 1 
ATOM   10372 H  HG21 . ILE   B 1 60  ? 32.704 7.795   67.416 1.00 17.44 ? 60   ILE   B HG21 1 
ATOM   10373 H  HG22 . ILE   B 1 60  ? 32.487 8.897   66.299 1.00 17.44 ? 60   ILE   B HG22 1 
ATOM   10374 H  HG23 . ILE   B 1 60  ? 33.841 8.077   66.350 1.00 17.44 ? 60   ILE   B HG23 1 
ATOM   10375 H  HD11 . ILE   B 1 60  ? 34.669 7.557   70.373 1.00 20.99 ? 60   ILE   B HD11 1 
ATOM   10376 H  HD12 . ILE   B 1 60  ? 33.297 8.336   70.232 1.00 20.99 ? 60   ILE   B HD12 1 
ATOM   10377 H  HD13 . ILE   B 1 60  ? 33.659 7.180   69.213 1.00 20.99 ? 60   ILE   B HD13 1 
ATOM   10378 N  N    . ILE   B 1 61  ? 33.815 10.811  64.643 1.00 12.55 ? 61   ILE   B N    1 
ATOM   10379 C  CA   . ILE   B 1 61  ? 32.903 11.159  63.520 1.00 15.84 ? 61   ILE   B CA   1 
ATOM   10380 C  C    . ILE   B 1 61  ? 32.347 9.819   63.047 1.00 13.79 ? 61   ILE   B C    1 
ATOM   10381 O  O    . ILE   B 1 61  ? 33.151 8.970   62.636 1.00 15.32 ? 61   ILE   B O    1 
ATOM   10382 C  CB   . ILE   B 1 61  ? 33.642 11.928  62.412 1.00 15.35 ? 61   ILE   B CB   1 
ATOM   10383 C  CG1  . ILE   B 1 61  ? 34.425 13.115  62.977 1.00 17.86 ? 61   ILE   B CG1  1 
ATOM   10384 C  CG2  . ILE   B 1 61  ? 32.666 12.361  61.331 1.00 17.52 ? 61   ILE   B CG2  1 
ATOM   10385 C  CD1  . ILE   B 1 61  ? 35.894 12.836  63.185 1.00 24.10 ? 61   ILE   B CD1  1 
ATOM   10386 H  H    . ILE   B 1 61  ? 34.520 10.375  64.414 1.00 15.06 ? 61   ILE   B H    1 
ATOM   10387 H  HA   . ILE   B 1 61  ? 32.189 11.758  63.790 1.00 19.01 ? 61   ILE   B HA   1 
ATOM   10388 H  HB   . ILE   B 1 61  ? 34.292 11.331  62.010 1.00 18.43 ? 61   ILE   B HB   1 
ATOM   10389 H  HG12 . ILE   B 1 61  ? 34.330 13.870  62.375 1.00 21.44 ? 61   ILE   B HG12 1 
ATOM   10390 H  HG13 . ILE   B 1 61  ? 34.032 13.377  63.824 1.00 21.44 ? 61   ILE   B HG13 1 
ATOM   10391 H  HG21 . ILE   B 1 61  ? 33.143 12.844  60.639 1.00 21.02 ? 61   ILE   B HG21 1 
ATOM   10392 H  HG22 . ILE   B 1 61  ? 32.242 11.578  60.945 1.00 21.02 ? 61   ILE   B HG22 1 
ATOM   10393 H  HG23 . ILE   B 1 61  ? 31.988 12.937  61.718 1.00 21.02 ? 61   ILE   B HG23 1 
ATOM   10394 H  HD11 . ILE   B 1 61  ? 36.326 13.627  63.543 1.00 28.92 ? 61   ILE   B HD11 1 
ATOM   10395 H  HD12 . ILE   B 1 61  ? 35.999 12.101  63.809 1.00 28.92 ? 61   ILE   B HD12 1 
ATOM   10396 H  HD13 . ILE   B 1 61  ? 36.302 12.601  62.337 1.00 28.92 ? 61   ILE   B HD13 1 
ATOM   10397 N  N    . VAL   B 1 62  ? 31.031 9.634   63.113 1.00 15.86 ? 62   VAL   B N    1 
ATOM   10398 C  CA   . VAL   B 1 62  ? 30.492 8.275   62.827 1.00 13.99 ? 62   VAL   B CA   1 
ATOM   10399 C  C    . VAL   B 1 62  ? 29.332 8.317   61.834 1.00 14.22 ? 62   VAL   B C    1 
ATOM   10400 O  O    . VAL   B 1 62  ? 28.524 9.256   61.894 1.00 14.74 ? 62   VAL   B O    1 
ATOM   10401 C  CB   . VAL   B 1 62  ? 30.081 7.583   64.144 1.00 15.11 ? 62   VAL   B CB   1 
ATOM   10402 C  CG1  . VAL   B 1 62  ? 29.094 8.423   64.940 1.00 15.14 ? 62   VAL   B CG1  1 
ATOM   10403 C  CG2  . VAL   B 1 62  ? 29.545 6.179   63.917 1.00 15.92 ? 62   VAL   B CG2  1 
ATOM   10404 H  H    . VAL   B 1 62  ? 30.449 10.236  63.309 1.00 19.03 ? 62   VAL   B H    1 
ATOM   10405 H  HA   . VAL   B 1 62  ? 31.195 7.754   62.408 1.00 16.79 ? 62   VAL   B HA   1 
ATOM   10406 H  HB   . VAL   B 1 62  ? 30.891 7.498   64.672 1.00 18.13 ? 62   VAL   B HB   1 
ATOM   10407 H  HG11 . VAL   B 1 62  ? 28.859 7.958   65.758 1.00 18.18 ? 62   VAL   B HG11 1 
ATOM   10408 H  HG12 . VAL   B 1 62  ? 29.498 9.277   65.159 1.00 18.18 ? 62   VAL   B HG12 1 
ATOM   10409 H  HG13 . VAL   B 1 62  ? 28.294 8.570   64.411 1.00 18.18 ? 62   VAL   B HG13 1 
ATOM   10410 H  HG21 . VAL   B 1 62  ? 29.300 5.784   64.769 1.00 19.11 ? 62   VAL   B HG21 1 
ATOM   10411 H  HG22 . VAL   B 1 62  ? 28.764 6.219   63.343 1.00 19.11 ? 62   VAL   B HG22 1 
ATOM   10412 H  HG23 . VAL   B 1 62  ? 30.228 5.636   63.494 1.00 19.11 ? 62   VAL   B HG23 1 
ATOM   10413 N  N    . THR   B 1 63  ? 29.260 7.303   60.977 1.00 13.12 ? 63   THR   B N    1 
ATOM   10414 C  CA   . THR   B 1 63  ? 28.162 7.209   59.991 1.00 13.81 ? 63   THR   B CA   1 
ATOM   10415 C  C    . THR   B 1 63  ? 27.185 6.119   60.423 1.00 14.35 ? 63   THR   B C    1 
ATOM   10416 O  O    . THR   B 1 63  ? 27.492 5.416   61.395 1.00 14.16 ? 63   THR   B O    1 
ATOM   10417 C  CB   . THR   B 1 63  ? 28.726 6.861   58.609 1.00 15.91 ? 63   THR   B CB   1 
ATOM   10418 O  OG1  . THR   B 1 63  ? 29.231 5.528   58.684 1.00 17.00 ? 63   THR   B OG1  1 
ATOM   10419 C  CG2  . THR   B 1 63  ? 29.827 7.798   58.166 1.00 17.29 ? 63   THR   B CG2  1 
ATOM   10420 H  H    . THR   B 1 63  ? 29.828 6.659   60.943 1.00 15.75 ? 63   THR   B H    1 
ATOM   10421 H  HA   . THR   B 1 63  ? 27.704 8.063   59.944 1.00 16.58 ? 63   THR   B HA   1 
ATOM   10422 H  HB   . THR   B 1 63  ? 28.017 6.948   57.952 1.00 19.10 ? 63   THR   B HB   1 
ATOM   10423 H  HG1  . THR   B 1 63  ? 29.885 5.505   59.211 1.00 20.41 ? 63   THR   B HG1  1 
ATOM   10424 H  HG21 . THR   B 1 63  ? 30.145 7.532   57.289 1.00 20.76 ? 63   THR   B HG21 1 
ATOM   10425 H  HG22 . THR   B 1 63  ? 29.483 8.704   58.124 1.00 20.76 ? 63   THR   B HG22 1 
ATOM   10426 H  HG23 . THR   B 1 63  ? 30.560 7.760   58.801 1.00 20.76 ? 63   THR   B HG23 1 
ATOM   10427 N  N    . GLY   B 1 64  ? 26.059 5.997   59.722 1.00 14.90 ? 64   GLY   B N    1 
ATOM   10428 C  CA   . GLY   B 1 64  ? 25.113 4.904   59.996 1.00 15.61 ? 64   GLY   B CA   1 
ATOM   10429 C  C    . GLY   B 1 64  ? 25.199 3.863   58.893 1.00 14.99 ? 64   GLY   B C    1 
ATOM   10430 O  O    . GLY   B 1 64  ? 25.811 4.158   57.856 1.00 16.22 ? 64   GLY   B O    1 
ATOM   10431 H  H    . GLY   B 1 64  ? 25.822 6.529   59.089 1.00 17.89 ? 64   GLY   B H    1 
ATOM   10432 H  HA2  . GLY   B 1 64  ? 25.315 4.497   60.853 1.00 18.73 ? 64   GLY   B HA2  1 
ATOM   10433 H  HA3  . GLY   B 1 64  ? 24.210 5.253   60.053 1.00 18.73 ? 64   GLY   B HA3  1 
ATOM   10434 N  N    . PRO   B 1 65  ? 24.623 2.651   59.067 1.00 15.20 ? 65   PRO   B N    1 
ATOM   10435 C  CA   . PRO   B 1 65  ? 24.634 1.632   58.011 1.00 17.74 ? 65   PRO   B CA   1 
ATOM   10436 C  C    . PRO   B 1 65  ? 23.951 2.125   56.728 1.00 15.22 ? 65   PRO   B C    1 
ATOM   10437 O  O    . PRO   B 1 65  ? 24.338 1.700   55.665 1.00 17.22 ? 65   PRO   B O    1 
ATOM   10438 C  CB   . PRO   B 1 65  ? 23.849 0.448   58.598 1.00 19.15 ? 65   PRO   B CB   1 
ATOM   10439 C  CG   . PRO   B 1 65  ? 23.050 1.048   59.731 1.00 16.22 ? 65   PRO   B CG   1 
ATOM   10440 C  CD   . PRO   B 1 65  ? 23.929 2.156   60.268 1.00 18.29 ? 65   PRO   B CD   1 
ATOM   10441 H  HA   . PRO   B 1 65  ? 25.542 1.401   57.761 1.00 21.29 ? 65   PRO   B HA   1 
ATOM   10442 H  HB2  . PRO   B 1 65  ? 23.270 0.044   57.933 1.00 22.98 ? 65   PRO   B HB2  1 
ATOM   10443 H  HB3  . PRO   B 1 65  ? 24.445 -0.248  58.916 1.00 22.98 ? 65   PRO   B HB3  1 
ATOM   10444 H  HG2  . PRO   B 1 65  ? 22.198 1.392   59.419 1.00 19.46 ? 65   PRO   B HG2  1 
ATOM   10445 H  HG3  . PRO   B 1 65  ? 22.856 0.388   60.415 1.00 19.46 ? 65   PRO   B HG3  1 
ATOM   10446 H  HD2  . PRO   B 1 65  ? 23.406 2.854   60.692 1.00 21.95 ? 65   PRO   B HD2  1 
ATOM   10447 H  HD3  . PRO   B 1 65  ? 24.554 1.827   60.932 1.00 21.95 ? 65   PRO   B HD3  1 
ATOM   10448 N  N    . LEU   B 1 66  ? 22.958 3.007   56.864 1.00 17.05 ? 66   LEU   B N    1 
ATOM   10449 C  CA   . LEU   B 1 66  ? 22.205 3.481   55.671 1.00 18.91 ? 66   LEU   B CA   1 
ATOM   10450 C  C    . LEU   B 1 66  ? 22.870 4.736   55.086 1.00 16.99 ? 66   LEU   B C    1 
ATOM   10451 O  O    . LEU   B 1 66  ? 22.485 5.130   53.976 1.00 18.16 ? 66   LEU   B O    1 
ATOM   10452 C  CB   . LEU   B 1 66  ? 20.747 3.750   56.060 1.00 17.64 ? 66   LEU   B CB   1 
ATOM   10453 C  CG   . LEU   B 1 66  ? 20.040 2.604   56.781 1.00 20.76 ? 66   LEU   B CG   1 
ATOM   10454 C  CD1  . LEU   B 1 66  ? 18.545 2.867   56.879 1.00 17.57 ? 66   LEU   B CD1  1 
ATOM   10455 C  CD2  . LEU   B 1 66  ? 20.301 1.280   56.081 1.00 21.64 ? 66   LEU   B CD2  1 
ATOM   10456 H  H    . LEU   B 1 66  ? 22.701 3.342   57.613 1.00 20.47 ? 66   LEU   B H    1 
ATOM   10457 H  HA   . LEU   B 1 66  ? 22.218 2.795   54.985 1.00 22.70 ? 66   LEU   B HA   1 
ATOM   10458 H  HB2  . LEU   B 1 66  ? 20.719 4.536   56.628 1.00 21.17 ? 66   LEU   B HB2  1 
ATOM   10459 H  HB3  . LEU   B 1 66  ? 20.248 3.963   55.256 1.00 21.17 ? 66   LEU   B HB3  1 
ATOM   10460 H  HG   . LEU   B 1 66  ? 20.401 2.550   57.680 1.00 24.91 ? 66   LEU   B HG   1 
ATOM   10461 H  HD11 . LEU   B 1 66  ? 18.116 2.129   57.339 1.00 21.09 ? 66   LEU   B HD11 1 
ATOM   10462 H  HD12 . LEU   B 1 66  ? 18.392 3.688   57.373 1.00 21.09 ? 66   LEU   B HD12 1 
ATOM   10463 H  HD13 . LEU   B 1 66  ? 18.172 2.952   55.988 1.00 21.09 ? 66   LEU   B HD13 1 
ATOM   10464 H  HD21 . LEU   B 1 66  ? 19.844 0.568   56.555 1.00 25.97 ? 66   LEU   B HD21 1 
ATOM   10465 H  HD22 . LEU   B 1 66  ? 19.972 1.325   55.170 1.00 25.97 ? 66   LEU   B HD22 1 
ATOM   10466 H  HD23 . LEU   B 1 66  ? 21.254 1.101   56.071 1.00 25.97 ? 66   LEU   B HD23 1 
ATOM   10467 N  N    . THR   B 1 67  ? 23.830 5.333   55.796 1.00 17.35 ? 67   THR   B N    1 
ATOM   10468 C  CA   . THR   B 1 67  ? 24.569 6.494   55.232 1.00 16.84 ? 67   THR   B CA   1 
ATOM   10469 C  C    . THR   B 1 67  ? 25.179 6.093   53.882 1.00 17.68 ? 67   THR   B C    1 
ATOM   10470 O  O    . THR   B 1 67  ? 25.918 5.102   53.847 1.00 17.05 ? 67   THR   B O    1 
ATOM   10471 C  CB   . THR   B 1 67  ? 25.635 7.022   56.202 1.00 15.19 ? 67   THR   B CB   1 
ATOM   10472 O  OG1  . THR   B 1 67  ? 25.014 7.379   57.436 1.00 14.24 ? 67   THR   B OG1  1 
ATOM   10473 C  CG2  . THR   B 1 67  ? 26.391 8.209   55.645 1.00 17.43 ? 67   THR   B CG2  1 
ATOM   10474 H  H    . THR   B 1 67  ? 24.072 5.097   56.587 1.00 20.82 ? 67   THR   B H    1 
ATOM   10475 H  HA   . THR   B 1 67  ? 23.946 7.225   55.094 1.00 20.21 ? 67   THR   B HA   1 
ATOM   10476 H  HB   . THR   B 1 67  ? 26.282 6.313   56.341 1.00 18.24 ? 67   THR   B HB   1 
ATOM   10477 H  HG1  . THR   B 1 67  ? 24.982 8.216   57.502 1.00 17.09 ? 67   THR   B HG1  1 
ATOM   10478 H  HG21 . THR   B 1 67  ? 27.050 8.505   56.292 1.00 20.92 ? 67   THR   B HG21 1 
ATOM   10479 H  HG22 . THR   B 1 67  ? 26.837 7.952   54.823 1.00 20.92 ? 67   THR   B HG22 1 
ATOM   10480 H  HG23 . THR   B 1 67  ? 25.770 8.932   55.463 1.00 20.92 ? 67   THR   B HG23 1 
ATOM   10481 N  N    . GLY   B 1 68  ? 24.865 6.838   52.820 1.00 18.01 ? 68   GLY   B N    1 
ATOM   10482 C  CA   . GLY   B 1 68  ? 25.450 6.567   51.492 1.00 20.37 ? 68   GLY   B CA   1 
ATOM   10483 C  C    . GLY   B 1 68  ? 24.677 5.522   50.703 1.00 21.34 ? 68   GLY   B C    1 
ATOM   10484 O  O    . GLY   B 1 68  ? 25.000 5.325   49.522 1.00 21.82 ? 68   GLY   B O    1 
ATOM   10485 H  H    . GLY   B 1 68  ? 24.319 7.502   52.841 1.00 21.62 ? 68   GLY   B H    1 
ATOM   10486 H  HA2  . GLY   B 1 68  ? 25.480 7.392   50.983 1.00 24.45 ? 68   GLY   B HA2  1 
ATOM   10487 H  HA3  . GLY   B 1 68  ? 26.366 6.269   51.603 1.00 24.45 ? 68   GLY   B HA3  1 
ATOM   10488 N  N    . ALA   B 1 69  ? 23.701 4.872   51.333 1.00 20.58 ? 69   ALA   B N    1 
ATOM   10489 C  CA   . ALA   B 1 69  ? 22.927 3.805   50.657 1.00 21.91 ? 69   ALA   B CA   1 
ATOM   10490 C  C    . ALA   B 1 69  ? 21.814 4.430   49.810 1.00 21.45 ? 69   ALA   B C    1 
ATOM   10491 O  O    . ALA   B 1 69  ? 21.390 5.556   50.121 1.00 19.78 ? 69   ALA   B O    1 
ATOM   10492 C  CB   . ALA   B 1 69  ? 22.376 2.838   51.672 1.00 22.46 ? 69   ALA   B CB   1 
ATOM   10493 H  H    . ALA   B 1 69  ? 23.465 5.025   52.146 1.00 24.70 ? 69   ALA   B H    1 
ATOM   10494 H  HA   . ALA   B 1 69  ? 23.511 3.306   50.065 1.00 26.29 ? 69   ALA   B HA   1 
ATOM   10495 H  HB1  . ALA   B 1 69  ? 21.872 2.145   51.218 1.00 26.95 ? 69   ALA   B HB1  1 
ATOM   10496 H  HB2  . ALA   B 1 69  ? 23.107 2.435   52.165 1.00 26.95 ? 69   ALA   B HB2  1 
ATOM   10497 H  HB3  . ALA   B 1 69  ? 21.794 3.311   52.287 1.00 26.95 ? 69   ALA   B HB3  1 
ATOM   10498 N  N    . PRO   B 1 70  ? 21.341 3.742   48.750 1.00 22.03 ? 70   PRO   B N    1 
ATOM   10499 C  CA   . PRO   B 1 70  ? 20.312 4.289   47.859 1.00 23.87 ? 70   PRO   B CA   1 
ATOM   10500 C  C    . PRO   B 1 70  ? 18.921 4.316   48.510 1.00 23.80 ? 70   PRO   B C    1 
ATOM   10501 O  O    . PRO   B 1 70  ? 18.014 3.717   47.980 1.00 19.97 ? 70   PRO   B O    1 
ATOM   10502 C  CB   . PRO   B 1 70  ? 20.388 3.352   46.644 1.00 25.50 ? 70   PRO   B CB   1 
ATOM   10503 C  CG   . PRO   B 1 70  ? 20.847 2.036   47.218 1.00 27.35 ? 70   PRO   B CG   1 
ATOM   10504 C  CD   . PRO   B 1 70  ? 21.791 2.410   48.340 1.00 22.59 ? 70   PRO   B CD   1 
ATOM   10505 H  HA   . PRO   B 1 70  ? 20.461 5.219   47.627 1.00 28.65 ? 70   PRO   B HA   1 
ATOM   10506 H  HB2  . PRO   B 1 70  ? 19.526 3.267   46.208 1.00 30.61 ? 70   PRO   B HB2  1 
ATOM   10507 H  HB3  . PRO   B 1 70  ? 21.011 3.685   45.979 1.00 30.61 ? 70   PRO   B HB3  1 
ATOM   10508 H  HG2  . PRO   B 1 70  ? 20.098 1.515   47.547 1.00 32.83 ? 70   PRO   B HG2  1 
ATOM   10509 H  HG3  . PRO   B 1 70  ? 21.294 1.496   46.547 1.00 32.83 ? 70   PRO   B HG3  1 
ATOM   10510 H  HD2  . PRO   B 1 70  ? 21.741 1.777   49.073 1.00 27.11 ? 70   PRO   B HD2  1 
ATOM   10511 H  HD3  . PRO   B 1 70  ? 22.713 2.423   48.039 1.00 27.11 ? 70   PRO   B HD3  1 
ATOM   10512 N  N    . VAL   B 1 71  ? 18.801 5.009   49.644 1.00 22.02 ? 71   VAL   B N    1 
ATOM   10513 C  CA   . VAL   B 1 71  ? 17.484 5.198   50.315 1.00 20.07 ? 71   VAL   B CA   1 
ATOM   10514 C  C    . VAL   B 1 71  ? 17.364 6.700   50.590 1.00 20.41 ? 71   VAL   B C    1 
ATOM   10515 O  O    . VAL   B 1 71  ? 18.403 7.379   50.597 1.00 19.23 ? 71   VAL   B O    1 
ATOM   10516 C  CB   . VAL   B 1 71  ? 17.379 4.386   51.618 1.00 21.19 ? 71   VAL   B CB   1 
ATOM   10517 C  CG1  . VAL   B 1 71  ? 17.234 2.897   51.345 1.00 24.69 ? 71   VAL   B CG1  1 
ATOM   10518 C  CG2  . VAL   B 1 71  ? 18.553 4.652   52.548 1.00 21.75 ? 71   VAL   B CG2  1 
ATOM   10519 H  H    . VAL   B 1 71  ? 19.462 5.382   50.050 1.00 26.42 ? 71   VAL   B H    1 
ATOM   10520 H  HA   . VAL   B 1 71  ? 16.762 4.879   49.751 1.00 24.09 ? 71   VAL   B HA   1 
ATOM   10521 H  HB   . VAL   B 1 71  ? 16.573 4.685   52.067 1.00 25.43 ? 71   VAL   B HB   1 
ATOM   10522 H  HG11 . VAL   B 1 71  ? 17.171 2.418   52.186 1.00 29.63 ? 71   VAL   B HG11 1 
ATOM   10523 H  HG12 . VAL   B 1 71  ? 16.432 2.740   50.823 1.00 29.63 ? 71   VAL   B HG12 1 
ATOM   10524 H  HG13 . VAL   B 1 71  ? 18.007 2.582   50.851 1.00 29.63 ? 71   VAL   B HG13 1 
ATOM   10525 H  HG21 . VAL   B 1 71  ? 18.452 4.124   53.356 1.00 26.10 ? 71   VAL   B HG21 1 
ATOM   10526 H  HG22 . VAL   B 1 71  ? 19.380 4.407   52.104 1.00 26.10 ? 71   VAL   B HG22 1 
ATOM   10527 H  HG23 . VAL   B 1 71  ? 18.577 5.594   52.778 1.00 26.10 ? 71   VAL   B HG23 1 
ATOM   10528 N  N    . PRO   B 1 72  ? 16.153 7.263   50.798 1.00 19.61 ? 72   PRO   B N    1 
ATOM   10529 C  CA   . PRO   B 1 72  ? 16.020 8.720   50.966 1.00 20.05 ? 72   PRO   B CA   1 
ATOM   10530 C  C    . PRO   B 1 72  ? 16.643 9.324   52.237 1.00 15.97 ? 72   PRO   B C    1 
ATOM   10531 O  O    . PRO   B 1 72  ? 16.481 8.736   53.280 1.00 17.21 ? 72   PRO   B O    1 
ATOM   10532 C  CB   . PRO   B 1 72  ? 14.496 8.931   50.965 1.00 19.95 ? 72   PRO   B CB   1 
ATOM   10533 C  CG   . PRO   B 1 72  ? 13.926 7.617   51.432 1.00 19.21 ? 72   PRO   B CG   1 
ATOM   10534 C  CD   . PRO   B 1 72  ? 14.849 6.582   50.830 1.00 21.76 ? 72   PRO   B CD   1 
ATOM   10535 H  HA   . PRO   B 1 72  ? 16.510 9.175   50.263 1.00 24.06 ? 72   PRO   B HA   1 
ATOM   10536 H  HB2  . PRO   B 1 72  ? 14.240 9.656   51.557 1.00 23.94 ? 72   PRO   B HB2  1 
ATOM   10537 H  HB3  . PRO   B 1 72  ? 14.173 9.160   50.080 1.00 23.94 ? 72   PRO   B HB3  1 
ATOM   10538 H  HG2  . PRO   B 1 72  ? 13.912 7.560   52.400 1.00 23.06 ? 72   PRO   B HG2  1 
ATOM   10539 H  HG3  . PRO   B 1 72  ? 13.013 7.498   51.128 1.00 23.06 ? 72   PRO   B HG3  1 
ATOM   10540 H  HD2  . PRO   B 1 72  ? 14.880 5.775   51.368 1.00 26.12 ? 72   PRO   B HD2  1 
ATOM   10541 H  HD3  . PRO   B 1 72  ? 14.561 6.320   49.942 1.00 26.12 ? 72   PRO   B HD3  1 
ATOM   10542 N  N    . THR   B 1 73  ? 17.335 10.462  52.102 1.00 16.08 ? 73   THR   B N    1 
ATOM   10543 C  CA   . THR   B 1 73  ? 17.953 11.192  53.250 1.00 16.26 ? 73   THR   B CA   1 
ATOM   10544 C  C    . THR   B 1 73  ? 19.139 10.416  53.831 1.00 16.14 ? 73   THR   B C    1 
ATOM   10545 O  O    . THR   B 1 73  ? 19.343 10.503  55.047 1.00 15.38 ? 73   THR   B O    1 
ATOM   10546 C  CB   . THR   B 1 73  ? 16.912 11.574  54.314 1.00 14.82 ? 73   THR   B CB   1 
ATOM   10547 O  OG1  . THR   B 1 73  ? 16.607 10.445  55.133 1.00 16.23 ? 73   THR   B OG1  1 
ATOM   10548 C  CG2  . THR   B 1 73  ? 15.647 12.137  53.700 1.00 17.91 ? 73   THR   B CG2  1 
ATOM   10549 H  H    . THR   B 1 73  ? 17.466 10.843  51.342 1.00 19.30 ? 73   THR   B H    1 
ATOM   10550 H  HA   . THR   B 1 73  ? 18.308 12.028  52.910 1.00 19.51 ? 73   THR   B HA   1 
ATOM   10551 H  HB   . THR   B 1 73  ? 17.301 12.273  54.863 1.00 17.79 ? 73   THR   B HB   1 
ATOM   10552 H  HG1  . THR   B 1 73  ? 16.277 9.835   54.659 1.00 19.48 ? 73   THR   B HG1  1 
ATOM   10553 H  HG21 . THR   B 1 73  ? 15.019 12.364  54.403 1.00 21.49 ? 73   THR   B HG21 1 
ATOM   10554 H  HG22 . THR   B 1 73  ? 15.862 12.933  53.189 1.00 21.49 ? 73   THR   B HG22 1 
ATOM   10555 H  HG23 . THR   B 1 73  ? 15.249 11.475  53.114 1.00 21.49 ? 73   THR   B HG23 1 
ATOM   10556 N  N    . SER   B 1 74  ? 19.934 9.769   52.973 1.00 13.73 ? 74   SER   B N    1 
ATOM   10557 C  CA   . SER   B 1 74  ? 21.072 8.937   53.445 1.00 17.52 ? 74   SER   B CA   1 
ATOM   10558 C  C    . SER   B 1 74  ? 22.377 9.737   53.576 1.00 14.84 ? 74   SER   B C    1 
ATOM   10559 O  O    . SER   B 1 74  ? 23.445 9.116   53.529 1.00 13.58 ? 74   SER   B O    1 
ATOM   10560 C  CB   . SER   B 1 74  ? 21.276 7.752   52.529 1.00 18.92 ? 74   SER   B CB   1 
ATOM   10561 O  OG   . SER   B 1 74  ? 21.580 8.181   51.212 1.00 18.47 ? 74   SER   B OG   1 
ATOM   10562 H  H    . SER   B 1 74  ? 19.840 9.793   52.118 1.00 16.48 ? 74   SER   B H    1 
ATOM   10563 H  HA   . SER   B 1 74  ? 20.840 8.623   54.333 1.00 21.03 ? 74   SER   B HA   1 
ATOM   10564 H  HB2  . SER   B 1 74  ? 21.996 7.196   52.867 1.00 22.71 ? 74   SER   B HB2  1 
ATOM   10565 H  HB3  . SER   B 1 74  ? 20.476 7.204   52.519 1.00 22.71 ? 74   SER   B HB3  1 
ATOM   10566 H  HG   . SER   B 1 74  ? 21.578 7.520   50.694 1.00 22.16 ? 74   SER   B HG   1 
ATOM   10567 N  N    . GLY   B 1 75  ? 22.297 11.054  53.765 1.00 13.37 ? 75   GLY   B N    1 
ATOM   10568 C  CA   . GLY   B 1 75  ? 23.529 11.860  53.849 1.00 13.95 ? 75   GLY   B CA   1 
ATOM   10569 C  C    . GLY   B 1 75  ? 23.877 12.220  55.284 1.00 13.20 ? 75   GLY   B C    1 
ATOM   10570 O  O    . GLY   B 1 75  ? 24.836 12.973  55.482 1.00 14.79 ? 75   GLY   B O    1 
ATOM   10571 H  H    . GLY   B 1 75  ? 21.563 11.495  53.846 1.00 16.05 ? 75   GLY   B H    1 
ATOM   10572 H  HA2  . GLY   B 1 75  ? 24.265 11.367  53.453 1.00 16.75 ? 75   GLY   B HA2  1 
ATOM   10573 H  HA3  . GLY   B 1 75  ? 23.419 12.672  53.330 1.00 16.75 ? 75   GLY   B HA3  1 
ATOM   10574 N  N    . ARG   B 1 76  ? 23.155 11.656  56.252 1.00 12.88 ? 76   ARG   B N    1 
ATOM   10575 C  CA   . ARG   B 1 76  ? 23.340 12.080  57.666 1.00 12.49 ? 76   ARG   B CA   1 
ATOM   10576 C  C    . ARG   B 1 76  ? 24.479 11.343  58.375 1.00 12.66 ? 76   ARG   B C    1 
ATOM   10577 O  O    . ARG   B 1 76  ? 24.671 10.145  58.119 1.00 15.08 ? 76   ARG   B O    1 
ATOM   10578 C  CB   . ARG   B 1 76  ? 22.028 11.910  58.439 1.00 13.03 ? 76   ARG   B CB   1 
ATOM   10579 C  CG   . ARG   B 1 76  ? 20.831 12.594  57.796 1.00 12.85 ? 76   ARG   B CG   1 
ATOM   10580 C  CD   . ARG   B 1 76  ? 21.034 14.079  57.556 1.00 13.02 ? 76   ARG   B CD   1 
ATOM   10581 N  NE   . ARG   B 1 76  ? 21.293 14.826  58.778 1.00 9.80  ? 76   ARG   B NE   1 
ATOM   10582 C  CZ   . ARG   B 1 76  ? 21.052 16.122  58.935 1.00 10.96 ? 76   ARG   B CZ   1 
ATOM   10583 N  NH1  . ARG   B 1 76  ? 20.446 16.802  57.979 1.00 12.92 ? 76   ARG   B NH1  1 
ATOM   10584 N  NH2  . ARG   B 1 76  ? 21.420 16.734  60.048 1.00 12.43 ? 76   ARG   B NH2  1 
ATOM   10585 H  H    . ARG   B 1 76  ? 22.566 11.042  56.129 1.00 15.45 ? 76   ARG   B H    1 
ATOM   10586 H  HA   . ARG   B 1 76  ? 23.592 13.016  57.648 1.00 14.99 ? 76   ARG   B HA   1 
ATOM   10587 H  HB2  . ARG   B 1 76  ? 21.837 10.963  58.528 1.00 15.64 ? 76   ARG   B HB2  1 
ATOM   10588 H  HB3  . ARG   B 1 76  ? 22.145 12.261  59.336 1.00 15.64 ? 76   ARG   B HB3  1 
ATOM   10589 H  HG2  . ARG   B 1 76  ? 20.637 12.161  56.950 1.00 15.42 ? 76   ARG   B HG2  1 
ATOM   10590 H  HG3  . ARG   B 1 76  ? 20.054 12.469  58.363 1.00 15.42 ? 76   ARG   B HG3  1 
ATOM   10591 H  HD2  . ARG   B 1 76  ? 21.776 14.203  56.944 1.00 15.63 ? 76   ARG   B HD2  1 
ATOM   10592 H  HD3  . ARG   B 1 76  ? 20.245 14.442  57.123 1.00 15.63 ? 76   ARG   B HD3  1 
ATOM   10593 H  HE   . ARG   B 1 76  ? 21.626 14.398  59.445 1.00 11.76 ? 76   ARG   B HE   1 
ATOM   10594 H  HH11 . ARG   B 1 76  ? 20.207 16.405  57.254 1.00 15.50 ? 76   ARG   B HH11 1 
ATOM   10595 H  HH12 . ARG   B 1 76  ? 20.290 17.642  58.081 1.00 15.50 ? 76   ARG   B HH12 1 
ATOM   10596 H  HH21 . ARG   B 1 76  ? 21.816 16.292  60.671 1.00 14.92 ? 76   ARG   B HH21 1 
ATOM   10597 H  HH22 . ARG   B 1 76  ? 21.264 17.574  60.149 1.00 14.92 ? 76   ARG   B HH22 1 
ATOM   10598 N  N    . PHE   B 1 77  ? 25.174 12.061  59.255 1.00 13.48 ? 77   PHE   B N    1 
ATOM   10599 C  CA   . PHE   B 1 77  ? 26.270 11.470  60.061 1.00 12.53 ? 77   PHE   B CA   1 
ATOM   10600 C  C    . PHE   B 1 77  ? 26.339 12.280  61.355 1.00 12.79 ? 77   PHE   B C    1 
ATOM   10601 O  O    . PHE   B 1 77  ? 25.629 13.295  61.459 1.00 11.18 ? 77   PHE   B O    1 
ATOM   10602 C  CB   . PHE   B 1 77  ? 27.602 11.500  59.311 1.00 13.61 ? 77   PHE   B CB   1 
ATOM   10603 C  CG   . PHE   B 1 77  ? 28.207 12.866  59.111 1.00 11.93 ? 77   PHE   B CG   1 
ATOM   10604 C  CD1  . PHE   B 1 77  ? 27.741 13.709  58.117 1.00 12.74 ? 77   PHE   B CD1  1 
ATOM   10605 C  CD2  . PHE   B 1 77  ? 29.254 13.299  59.906 1.00 11.78 ? 77   PHE   B CD2  1 
ATOM   10606 C  CE1  . PHE   B 1 77  ? 28.302 14.962  57.931 1.00 12.32 ? 77   PHE   B CE1  1 
ATOM   10607 C  CE2  . PHE   B 1 77  ? 29.816 14.551  59.718 1.00 11.83 ? 77   PHE   B CE2  1 
ATOM   10608 C  CZ   . PHE   B 1 77  ? 29.338 15.380  58.731 1.00 12.32 ? 77   PHE   B CZ   1 
ATOM   10609 H  H    . PHE   B 1 77  ? 25.034 12.896  59.408 1.00 16.18 ? 77   PHE   B H    1 
ATOM   10610 H  HA   . PHE   B 1 77  ? 26.095 10.534  60.246 1.00 15.04 ? 77   PHE   B HA   1 
ATOM   10611 H  HB2  . PHE   B 1 77  ? 28.239 10.950  59.793 1.00 16.34 ? 77   PHE   B HB2  1 
ATOM   10612 H  HB3  . PHE   B 1 77  ? 27.474 11.090  58.441 1.00 16.34 ? 77   PHE   B HB3  1 
ATOM   10613 H  HD1  . PHE   B 1 77  ? 27.044 13.431  57.568 1.00 15.29 ? 77   PHE   B HD1  1 
ATOM   10614 H  HD2  . PHE   B 1 77  ? 29.584 12.743  60.574 1.00 14.13 ? 77   PHE   B HD2  1 
ATOM   10615 H  HE1  . PHE   B 1 77  ? 27.977 15.521  57.263 1.00 14.79 ? 77   PHE   B HE1  1 
ATOM   10616 H  HE2  . PHE   B 1 77  ? 30.518 14.831  60.260 1.00 14.20 ? 77   PHE   B HE2  1 
ATOM   10617 H  HZ   . PHE   B 1 77  ? 29.715 16.221  58.605 1.00 14.79 ? 77   PHE   B HZ   1 
ATOM   10618 N  N    . MET   B 1 78  ? 27.176 11.861  62.298 1.00 12.29 ? 78   MET   B N    1 
ATOM   10619 C  CA   . MET   B 1 78  ? 27.148 12.579  63.594 1.00 11.46 ? 78   MET   B CA   1 
ATOM   10620 C  C    . MET   B 1 78  ? 28.536 12.760  64.202 1.00 11.48 ? 78   MET   B C    1 
ATOM   10621 O  O    . MET   B 1 78  ? 29.441 11.967  63.881 1.00 13.54 ? 78   MET   B O    1 
ATOM   10622 C  CB   . MET   B 1 78  ? 26.270 11.825  64.598 1.00 14.97 ? 78   MET   B CB   1 
ATOM   10623 C  CG   . MET   B 1 78  ? 24.798 11.905  64.263 1.00 14.26 ? 78   MET   B CG   1 
ATOM   10624 S  SD   . MET   B 1 78  ? 23.737 11.269  65.576 1.00 15.21 ? 78   MET   B SD   1 
ATOM   10625 C  CE   . MET   B 1 78  ? 24.391 12.168  66.980 1.00 17.12 ? 78   MET   B CE   1 
ATOM   10626 H  H    . MET   B 1 78  ? 27.735 11.211  62.230 1.00 14.75 ? 78   MET   B H    1 
ATOM   10627 H  HA   . MET   B 1 78  ? 26.784 13.459  63.410 1.00 13.76 ? 78   MET   B HA   1 
ATOM   10628 H  HB2  . MET   B 1 78  ? 26.542 10.894  64.624 1.00 17.97 ? 78   MET   B HB2  1 
ATOM   10629 H  HB3  . MET   B 1 78  ? 26.416 12.188  65.486 1.00 17.97 ? 78   MET   B HB3  1 
ATOM   10630 H  HG2  . MET   B 1 78  ? 24.563 12.829  64.083 1.00 17.12 ? 78   MET   B HG2  1 
ATOM   10631 H  HG3  . MET   B 1 78  ? 24.630 11.406  63.448 1.00 17.12 ? 78   MET   B HG3  1 
ATOM   10632 H  HE1  . MET   B 1 78  ? 23.902 11.919  67.780 1.00 20.54 ? 78   MET   B HE1  1 
ATOM   10633 H  HE2  . MET   B 1 78  ? 25.329 11.951  67.095 1.00 20.54 ? 78   MET   B HE2  1 
ATOM   10634 H  HE3  . MET   B 1 78  ? 24.296 13.121  66.827 1.00 20.54 ? 78   MET   B HE3  1 
ATOM   10635 N  N    . VAL   B 1 79  ? 28.684 13.802  65.016 1.00 11.65 ? 79   VAL   B N    1 
ATOM   10636 C  CA   . VAL   B 1 79  ? 29.934 13.984  65.796 1.00 12.09 ? 79   VAL   B CA   1 
ATOM   10637 C  C    . VAL   B 1 79  ? 29.581 13.537  67.216 1.00 14.02 ? 79   VAL   B C    1 
ATOM   10638 O  O    . VAL   B 1 79  ? 28.551 13.999  67.731 1.00 13.92 ? 79   VAL   B O    1 
ATOM   10639 C  CB   . VAL   B 1 79  ? 30.428 15.440  65.770 1.00 12.86 ? 79   VAL   B CB   1 
ATOM   10640 C  CG1  . VAL   B 1 79  ? 31.433 15.718  66.877 1.00 12.73 ? 79   VAL   B CG1  1 
ATOM   10641 C  CG2  . VAL   B 1 79  ? 30.999 15.821  64.413 1.00 10.45 ? 79   VAL   B CG2  1 
ATOM   10642 H  H    . VAL   B 1 79  ? 28.090 14.412  65.138 1.00 13.99 ? 79   VAL   B H    1 
ATOM   10643 H  HA   . VAL   B 1 79  ? 30.664 13.467  65.421 1.00 14.51 ? 79   VAL   B HA   1 
ATOM   10644 H  HB   . VAL   B 1 79  ? 29.651 15.998  65.930 1.00 15.44 ? 79   VAL   B HB   1 
ATOM   10645 H  HG11 . VAL   B 1 79  ? 31.721 16.643  66.828 1.00 15.28 ? 79   VAL   B HG11 1 
ATOM   10646 H  HG12 . VAL   B 1 79  ? 31.019 15.553  67.739 1.00 15.28 ? 79   VAL   B HG12 1 
ATOM   10647 H  HG13 . VAL   B 1 79  ? 32.201 15.135  66.771 1.00 15.28 ? 79   VAL   B HG13 1 
ATOM   10648 H  HG21 . VAL   B 1 79  ? 31.299 16.743  64.435 1.00 12.54 ? 79   VAL   B HG21 1 
ATOM   10649 H  HG22 . VAL   B 1 79  ? 31.749 15.242  64.203 1.00 12.54 ? 79   VAL   B HG22 1 
ATOM   10650 H  HG23 . VAL   B 1 79  ? 30.314 15.721  63.734 1.00 12.54 ? 79   VAL   B HG23 1 
ATOM   10651 N  N    . VAL   B 1 80  ? 30.357 12.613  67.775 1.00 11.65 ? 80   VAL   B N    1 
ATOM   10652 C  CA   . VAL   B 1 80  ? 30.114 12.126  69.163 1.00 11.75 ? 80   VAL   B CA   1 
ATOM   10653 C  C    . VAL   B 1 80  ? 31.378 12.391  69.982 1.00 12.36 ? 80   VAL   B C    1 
ATOM   10654 O  O    . VAL   B 1 80  ? 32.461 12.003  69.534 1.00 15.00 ? 80   VAL   B O    1 
ATOM   10655 C  CB   . VAL   B 1 80  ? 29.705 10.642  69.179 1.00 12.08 ? 80   VAL   B CB   1 
ATOM   10656 C  CG1  . VAL   B 1 80  ? 29.487 10.142  70.599 1.00 12.20 ? 80   VAL   B CG1  1 
ATOM   10657 C  CG2  . VAL   B 1 80  ? 28.465 10.396  68.335 1.00 12.53 ? 80   VAL   B CG2  1 
ATOM   10658 H  H    . VAL   B 1 80  ? 31.029 12.248  67.382 1.00 13.98 ? 80   VAL   B H    1 
ATOM   10659 H  HA   . VAL   B 1 80  ? 29.369 12.604  69.559 1.00 14.10 ? 80   VAL   B HA   1 
ATOM   10660 H  HB   . VAL   B 1 80  ? 30.439 10.141  68.790 1.00 14.50 ? 80   VAL   B HB   1 
ATOM   10661 H  HG11 . VAL   B 1 80  ? 29.231 9.207   70.577 1.00 14.65 ? 80   VAL   B HG11 1 
ATOM   10662 H  HG12 . VAL   B 1 80  ? 30.308 10.240  71.107 1.00 14.65 ? 80   VAL   B HG12 1 
ATOM   10663 H  HG13 . VAL   B 1 80  ? 28.783 10.660  71.020 1.00 14.65 ? 80   VAL   B HG13 1 
ATOM   10664 H  HG21 . VAL   B 1 80  ? 28.234 9.454   68.366 1.00 15.04 ? 80   VAL   B HG21 1 
ATOM   10665 H  HG22 . VAL   B 1 80  ? 27.727 10.921  68.683 1.00 15.04 ? 80   VAL   B HG22 1 
ATOM   10666 H  HG23 . VAL   B 1 80  ? 28.641 10.655  67.417 1.00 15.04 ? 80   VAL   B HG23 1 
ATOM   10667 N  N    . THR   B 1 81  ? 31.223 13.048  71.129 1.00 10.95 ? 81   THR   B N    1 
ATOM   10668 C  CA   . THR   B 1 81  ? 32.370 13.372  72.013 1.00 13.17 ? 81   THR   B CA   1 
ATOM   10669 C  C    . THR   B 1 81  ? 31.800 13.916  73.321 1.00 14.53 ? 81   THR   B C    1 
ATOM   10670 O  O    . THR   B 1 81  ? 30.580 14.114  73.385 1.00 12.05 ? 81   THR   B O    1 
ATOM   10671 C  CB   . THR   B 1 81  ? 33.290 14.433  71.400 1.00 11.93 ? 81   THR   B CB   1 
ATOM   10672 O  OG1  . THR   B 1 81  ? 34.434 14.613  72.235 1.00 17.91 ? 81   THR   B OG1  1 
ATOM   10673 C  CG2  . THR   B 1 81  ? 32.594 15.763  71.205 1.00 13.80 ? 81   THR   B CG2  1 
ATOM   10674 H  H    . THR   B 1 81  ? 30.463 13.321  71.424 1.00 13.14 ? 81   THR   B H    1 
ATOM   10675 H  HA   . THR   B 1 81  ? 32.898 12.569  72.148 1.00 15.80 ? 81   THR   B HA   1 
ATOM   10676 H  HB   . THR   B 1 81  ? 33.555 14.113  70.523 1.00 14.32 ? 81   THR   B HB   1 
ATOM   10677 H  HG1  . THR   B 1 81  ? 34.979 13.988  72.103 1.00 21.50 ? 81   THR   B HG1  1 
ATOM   10678 H  HG21 . THR   B 1 81  ? 33.214 16.399  70.816 1.00 16.57 ? 81   THR   B HG21 1 
ATOM   10679 H  HG22 . THR   B 1 81  ? 31.836 15.648  70.611 1.00 16.57 ? 81   THR   B HG22 1 
ATOM   10680 H  HG23 . THR   B 1 81  ? 32.285 16.096  72.062 1.00 16.57 ? 81   THR   B HG23 1 
ATOM   10681 N  N    . LYS   B 1 82  ? 32.649 14.146  74.320 1.00 12.61 ? 82   LYS   B N    1 
ATOM   10682 C  CA   . LYS   B 1 82  ? 32.098 14.795  75.535 1.00 13.81 ? 82   LYS   B CA   1 
ATOM   10683 C  C    . LYS   B 1 82  ? 31.852 16.265  75.187 1.00 12.89 ? 82   LYS   B C    1 
ATOM   10684 O  O    . LYS   B 1 82  ? 32.754 16.888  74.614 1.00 11.91 ? 82   LYS   B O    1 
ATOM   10685 C  CB   . LYS   B 1 82  ? 32.994 14.641  76.767 1.00 15.59 ? 82   LYS   B CB   1 
ATOM   10686 C  CG   . LYS   B 1 82  ? 32.347 15.186  78.034 1.00 15.72 ? 82   LYS   B CG   1 
ATOM   10687 C  CD   . LYS   B 1 82  ? 33.115 14.972  79.316 1.00 17.42 ? 82   LYS   B CD   1 
ATOM   10688 C  CE   . LYS   B 1 82  ? 32.411 15.611  80.495 1.00 17.63 ? 82   LYS   B CE   1 
ATOM   10689 N  NZ   . LYS   B 1 82  ? 33.120 15.365  81.771 1.00 20.16 ? 82   LYS   B NZ   1 
ATOM   10690 H  H    . LYS   B 1 82  ? 33.487 13.955  74.331 1.00 15.14 ? 82   LYS   B H    1 
ATOM   10691 H  HA   . LYS   B 1 82  ? 31.270 14.356  75.786 1.00 16.58 ? 82   LYS   B HA   1 
ATOM   10692 H  HB2  . LYS   B 1 82  ? 33.205 13.703  76.894 1.00 18.71 ? 82   LYS   B HB2  1 
ATOM   10693 H  HB3  . LYS   B 1 82  ? 33.833 15.102  76.612 1.00 18.71 ? 82   LYS   B HB3  1 
ATOM   10694 H  HG2  . LYS   B 1 82  ? 32.204 16.139  77.919 1.00 18.86 ? 82   LYS   B HG2  1 
ATOM   10695 H  HG3  . LYS   B 1 82  ? 31.472 14.778  78.130 1.00 18.86 ? 82   LYS   B HG3  1 
ATOM   10696 H  HD2  . LYS   B 1 82  ? 33.221 14.021  79.477 1.00 20.91 ? 82   LYS   B HD2  1 
ATOM   10697 H  HD3  . LYS   B 1 82  ? 34.006 15.346  79.228 1.00 20.91 ? 82   LYS   B HD3  1 
ATOM   10698 H  HE2  . LYS   B 1 82  ? 32.338 16.567  80.347 1.00 21.16 ? 82   LYS   B HE2  1 
ATOM   10699 H  HE3  . LYS   B 1 82  ? 31.507 15.264  80.557 1.00 21.16 ? 82   LYS   B HE3  1 
ATOM   10700 H  HZ1  . LYS   B 1 82  ? 32.844 15.950  82.382 1.00 24.20 ? 82   LYS   B HZ1  1 
ATOM   10701 H  HZ2  . LYS   B 1 82  ? 32.947 14.539  82.052 1.00 24.20 ? 82   LYS   B HZ2  1 
ATOM   10702 H  HZ3  . LYS   B 1 82  ? 33.996 15.458  81.647 1.00 24.20 ? 82   LYS   B HZ3  1 
ATOM   10703 N  N    . ALA   B 1 83  ? 30.675 16.782  75.538 1.00 11.54 ? 83   ALA   B N    1 
ATOM   10704 C  CA   . ALA   B 1 83  ? 30.300 18.165  75.170 1.00 13.62 ? 83   ALA   B CA   1 
ATOM   10705 C  C    . ALA   B 1 83  ? 30.840 19.174  76.188 1.00 13.87 ? 83   ALA   B C    1 
ATOM   10706 O  O    . ALA   B 1 83  ? 30.488 19.081  77.368 1.00 14.16 ? 83   ALA   B O    1 
ATOM   10707 C  CB   . ALA   B 1 83  ? 28.801 18.255  75.056 1.00 15.29 ? 83   ALA   B CB   1 
ATOM   10708 H  H    . ALA   B 1 83  ? 30.077 16.357  75.987 1.00 13.85 ? 83   ALA   B H    1 
ATOM   10709 H  HA   . ALA   B 1 83  ? 30.698 18.386  74.314 1.00 16.35 ? 83   ALA   B HA   1 
ATOM   10710 H  HB1  . ALA   B 1 83  ? 28.548 19.160  74.815 1.00 18.35 ? 83   ALA   B HB1  1 
ATOM   10711 H  HB2  . ALA   B 1 83  ? 28.491 17.640  74.373 1.00 18.35 ? 83   ALA   B HB2  1 
ATOM   10712 H  HB3  . ALA   B 1 83  ? 28.397 18.023  75.907 1.00 18.35 ? 83   ALA   B HB3  1 
ATOM   10713 N  N    . PRO   B 1 84  ? 31.680 20.137  75.767 1.00 13.53 ? 84   PRO   B N    1 
ATOM   10714 C  CA   . PRO   B 1 84  ? 32.216 21.168  76.665 1.00 15.03 ? 84   PRO   B CA   1 
ATOM   10715 C  C    . PRO   B 1 84  ? 31.168 22.146  77.220 1.00 12.91 ? 84   PRO   B C    1 
ATOM   10716 O  O    . PRO   B 1 84  ? 31.322 22.574  78.343 1.00 15.81 ? 84   PRO   B O    1 
ATOM   10717 C  CB   . PRO   B 1 84  ? 33.178 21.955  75.762 1.00 17.63 ? 84   PRO   B CB   1 
ATOM   10718 C  CG   . PRO   B 1 84  ? 33.478 21.024  74.609 1.00 16.89 ? 84   PRO   B CG   1 
ATOM   10719 C  CD   . PRO   B 1 84  ? 32.210 20.221  74.418 1.00 14.21 ? 84   PRO   B CD   1 
ATOM   10720 H  HA   . PRO   B 1 84  ? 32.609 20.751  77.448 1.00 18.04 ? 84   PRO   B HA   1 
ATOM   10721 H  HB2  . PRO   B 1 84  ? 32.773 22.780  75.452 1.00 21.16 ? 84   PRO   B HB2  1 
ATOM   10722 H  HB3  . PRO   B 1 84  ? 33.988 22.198  76.238 1.00 21.16 ? 84   PRO   B HB3  1 
ATOM   10723 H  HG2  . PRO   B 1 84  ? 33.705 21.520  73.807 1.00 20.27 ? 84   PRO   B HG2  1 
ATOM   10724 H  HG3  . PRO   B 1 84  ? 34.232 20.448  74.809 1.00 20.27 ? 84   PRO   B HG3  1 
ATOM   10725 H  HD2  . PRO   B 1 84  ? 31.592 20.662  73.815 1.00 17.06 ? 84   PRO   B HD2  1 
ATOM   10726 H  HD3  . PRO   B 1 84  ? 32.392 19.343  74.047 1.00 17.06 ? 84   PRO   B HD3  1 
ATOM   10727 N  N    . LEU   B 1 85  ? 30.158 22.500  76.422 1.00 11.94 ? 85   LEU   B N    1 
ATOM   10728 C  CA   . LEU   B 1 85  ? 29.170 23.512  76.883 1.00 12.84 ? 85   LEU   B CA   1 
ATOM   10729 C  C    . LEU   B 1 85  ? 28.321 22.950  78.025 1.00 14.16 ? 85   LEU   B C    1 
ATOM   10730 O  O    . LEU   B 1 85  ? 28.051 23.710  78.968 1.00 14.66 ? 85   LEU   B O    1 
ATOM   10731 C  CB   . LEU   B 1 85  ? 28.261 23.889  75.711 1.00 10.60 ? 85   LEU   B CB   1 
ATOM   10732 C  CG   . LEU   B 1 85  ? 27.128 24.857  76.045 1.00 12.44 ? 85   LEU   B CG   1 
ATOM   10733 C  CD1  . LEU   B 1 85  ? 27.681 26.231  76.389 1.00 14.33 ? 85   LEU   B CD1  1 
ATOM   10734 C  CD2  . LEU   B 1 85  ? 26.143 24.952  74.892 1.00 15.08 ? 85   LEU   B CD2  1 
ATOM   10735 H  H    . LEU   B 1 85  ? 30.020 22.184  75.634 1.00 14.33 ? 85   LEU   B H    1 
ATOM   10736 H  HA   . LEU   B 1 85  ? 29.644 24.295  77.205 1.00 15.41 ? 85   LEU   B HA   1 
ATOM   10737 H  HB2  . LEU   B 1 85  ? 28.807 24.282  75.012 1.00 12.72 ? 85   LEU   B HB2  1 
ATOM   10738 H  HB3  . LEU   B 1 85  ? 27.875 23.077  75.347 1.00 12.72 ? 85   LEU   B HB3  1 
ATOM   10739 H  HG   . LEU   B 1 85  ? 26.656 24.514  76.820 1.00 14.93 ? 85   LEU   B HG   1 
ATOM   10740 H  HD11 . LEU   B 1 85  ? 26.949 26.832  76.598 1.00 17.20 ? 85   LEU   B HD11 1 
ATOM   10741 H  HD12 . LEU   B 1 85  ? 28.270 26.160  77.157 1.00 17.20 ? 85   LEU   B HD12 1 
ATOM   10742 H  HD13 . LEU   B 1 85  ? 28.178 26.579  75.632 1.00 17.20 ? 85   LEU   B HD13 1 
ATOM   10743 H  HD21 . LEU   B 1 85  ? 25.432 25.570  75.123 1.00 18.10 ? 85   LEU   B HD21 1 
ATOM   10744 H  HD22 . LEU   B 1 85  ? 26.602 25.270  74.099 1.00 18.10 ? 85   LEU   B HD22 1 
ATOM   10745 H  HD23 . LEU   B 1 85  ? 25.765 24.076  74.717 1.00 18.10 ? 85   LEU   B HD23 1 
ATOM   10746 N  N    . THR   B 1 86  ? 27.967 21.668  77.966 1.00 14.40 ? 86   THR   B N    1 
ATOM   10747 C  CA   . THR   B 1 86  ? 26.992 21.105  78.935 1.00 12.52 ? 86   THR   B CA   1 
ATOM   10748 C  C    . THR   B 1 86  ? 27.609 20.136  79.942 1.00 12.14 ? 86   THR   B C    1 
ATOM   10749 O  O    . THR   B 1 86  ? 27.010 19.965  81.015 1.00 13.13 ? 86   THR   B O    1 
ATOM   10750 C  CB   . THR   B 1 86  ? 25.932 20.317  78.160 1.00 13.57 ? 86   THR   B CB   1 
ATOM   10751 O  OG1  . THR   B 1 86  ? 26.591 19.231  77.510 1.00 12.30 ? 86   THR   B OG1  1 
ATOM   10752 C  CG2  . THR   B 1 86  ? 25.212 21.166  77.135 1.00 11.35 ? 86   THR   B CG2  1 
ATOM   10753 H  H    . THR   B 1 86  ? 28.267 21.107  77.388 1.00 17.28 ? 86   THR   B H    1 
ATOM   10754 H  HA   . THR   B 1 86  ? 26.631 21.860  79.425 1.00 15.03 ? 86   THR   B HA   1 
ATOM   10755 H  HB   . THR   B 1 86  ? 25.258 20.004  78.783 1.00 16.29 ? 86   THR   B HB   1 
ATOM   10756 H  HG1  . THR   B 1 86  ? 26.094 18.554  77.523 1.00 14.76 ? 86   THR   B HG1  1 
ATOM   10757 H  HG21 . THR   B 1 86  ? 24.553 20.625  76.672 1.00 13.63 ? 86   THR   B HG21 1 
ATOM   10758 H  HG22 . THR   B 1 86  ? 24.768 21.904  77.581 1.00 13.63 ? 86   THR   B HG22 1 
ATOM   10759 H  HG23 . THR   B 1 86  ? 25.853 21.513  76.495 1.00 13.63 ? 86   THR   B HG23 1 
ATOM   10760 N  N    . GLY   B 1 87  ? 28.728 19.505  79.600 1.00 15.96 ? 87   GLY   B N    1 
ATOM   10761 C  CA   . GLY   B 1 87  ? 29.290 18.469  80.484 1.00 13.89 ? 87   GLY   B CA   1 
ATOM   10762 C  C    . GLY   B 1 87  ? 28.612 17.130  80.259 1.00 13.19 ? 87   GLY   B C    1 
ATOM   10763 O  O    . GLY   B 1 87  ? 28.963 16.164  80.946 1.00 15.38 ? 87   GLY   B O    1 
ATOM   10764 H  H    . GLY   B 1 87  ? 29.173 19.652  78.879 1.00 19.16 ? 87   GLY   B H    1 
ATOM   10765 H  HA2  . GLY   B 1 87  ? 30.243 18.384  80.322 1.00 16.68 ? 87   GLY   B HA2  1 
ATOM   10766 H  HA3  . GLY   B 1 87  ? 29.183 18.737  81.410 1.00 16.68 ? 87   GLY   B HA3  1 
ATOM   10767 N  N    . THR   B 1 88  ? 27.680 17.077  79.307 1.00 14.73 ? 88   THR   B N    1 
ATOM   10768 C  CA   . THR   B 1 88  ? 26.963 15.819  78.997 1.00 14.94 ? 88   THR   B CA   1 
ATOM   10769 C  C    . THR   B 1 88  ? 27.568 15.123  77.781 1.00 14.80 ? 88   THR   B C    1 
ATOM   10770 O  O    . THR   B 1 88  ? 28.622 15.563  77.295 1.00 14.45 ? 88   THR   B O    1 
ATOM   10771 C  CB   . THR   B 1 88  ? 25.500 16.088  78.631 1.00 13.33 ? 88   THR   B CB   1 
ATOM   10772 O  OG1  . THR   B 1 88  ? 25.475 16.757  77.369 1.00 12.79 ? 88   THR   B OG1  1 
ATOM   10773 C  CG2  . THR   B 1 88  ? 24.779 16.924  79.665 1.00 17.90 ? 88   THR   B CG2  1 
ATOM   10774 H  H    . THR   B 1 88  ? 27.443 17.750  78.827 1.00 17.67 ? 88   THR   B H    1 
ATOM   10775 H  HA   . THR   B 1 88  ? 27.035 15.270  79.794 1.00 17.93 ? 88   THR   B HA   1 
ATOM   10776 H  HB   . THR   B 1 88  ? 25.036 15.237  78.592 1.00 16.00 ? 88   THR   B HB   1 
ATOM   10777 H  HG1  . THR   B 1 88  ? 24.739 17.150  77.275 1.00 15.35 ? 88   THR   B HG1  1 
ATOM   10778 H  HG21 . THR   B 1 88  ? 23.861 17.064  79.385 1.00 21.48 ? 88   THR   B HG21 1 
ATOM   10779 H  HG22 . THR   B 1 88  ? 24.790 16.463  80.519 1.00 21.48 ? 88   THR   B HG22 1 
ATOM   10780 H  HG23 . THR   B 1 88  ? 25.223 17.782  79.755 1.00 21.48 ? 88   THR   B HG23 1 
ATOM   10781 N  N    . ILE   B 1 89  ? 26.907 14.062  77.333 1.00 14.79 ? 89   ILE   B N    1 
ATOM   10782 C  CA   . ILE   B 1 89  ? 27.337 13.413  76.071 1.00 13.77 ? 89   ILE   B CA   1 
ATOM   10783 C  C    . ILE   B 1 89  ? 27.105 14.431  74.958 1.00 14.99 ? 89   ILE   B C    1 
ATOM   10784 O  O    . ILE   B 1 89  ? 26.125 15.184  75.055 1.00 11.88 ? 89   ILE   B O    1 
ATOM   10785 C  CB   . ILE   B 1 89  ? 26.520 12.130  75.828 1.00 16.29 ? 89   ILE   B CB   1 
ATOM   10786 C  CG1  . ILE   B 1 89  ? 26.906 11.448  74.513 1.00 16.61 ? 89   ILE   B CG1  1 
ATOM   10787 C  CG2  . ILE   B 1 89  ? 25.028 12.414  75.901 1.00 12.98 ? 89   ILE   B CG2  1 
ATOM   10788 C  CD1  . ILE   B 1 89  ? 28.272 10.807  74.539 1.00 15.28 ? 89   ILE   B CD1  1 
ATOM   10789 H  H    . ILE   B 1 89  ? 26.228 13.703  77.720 1.00 17.75 ? 89   ILE   B H    1 
ATOM   10790 H  HA   . ILE   B 1 89  ? 28.271 13.152  76.106 1.00 16.53 ? 89   ILE   B HA   1 
ATOM   10791 H  HB   . ILE   B 1 89  ? 26.736 11.506  76.538 1.00 19.56 ? 89   ILE   B HB   1 
ATOM   10792 H  HG12 . ILE   B 1 89  ? 26.244 10.771  74.303 1.00 19.93 ? 89   ILE   B HG12 1 
ATOM   10793 H  HG13 . ILE   B 1 89  ? 26.879 12.103  73.798 1.00 19.93 ? 89   ILE   B HG13 1 
ATOM   10794 H  HG21 . ILE   B 1 89  ? 24.534 11.594  75.745 1.00 15.58 ? 89   ILE   B HG21 1 
ATOM   10795 H  HG22 . ILE   B 1 89  ? 24.807 12.762  76.779 1.00 15.58 ? 89   ILE   B HG22 1 
ATOM   10796 H  HG23 . ILE   B 1 89  ? 24.789 13.068  75.225 1.00 15.58 ? 89   ILE   B HG23 1 
ATOM   10797 H  HD11 . ILE   B 1 89  ? 28.453 10.395  73.680 1.00 18.34 ? 89   ILE   B HD11 1 
ATOM   10798 H  HD12 . ILE   B 1 89  ? 28.943 11.483  74.721 1.00 18.34 ? 89   ILE   B HD12 1 
ATOM   10799 H  HD13 . ILE   B 1 89  ? 28.299 10.130  75.233 1.00 18.34 ? 89   ILE   B HD13 1 
ATOM   10800 N  N    . GLY   B 1 90  ? 27.990 14.487  73.978 1.00 11.50 ? 90   GLY   B N    1 
ATOM   10801 C  CA   . GLY   B 1 90  ? 27.780 15.323  72.781 1.00 11.89 ? 90   GLY   B CA   1 
ATOM   10802 C  C    . GLY   B 1 90  ? 27.328 14.446  71.619 1.00 11.52 ? 90   GLY   B C    1 
ATOM   10803 O  O    . GLY   B 1 90  ? 27.969 13.452  71.368 1.00 13.57 ? 90   GLY   B O    1 
ATOM   10804 H  H    . GLY   B 1 90  ? 28.730 14.048  73.977 1.00 13.81 ? 90   GLY   B H    1 
ATOM   10805 H  HA2  . GLY   B 1 90  ? 27.113 16.004  72.963 1.00 14.27 ? 90   GLY   B HA2  1 
ATOM   10806 H  HA3  . GLY   B 1 90  ? 28.601 15.785  72.550 1.00 14.27 ? 90   GLY   B HA3  1 
ATOM   10807 N  N    . ILE   B 1 91  ? 26.212 14.796  71.010 1.00 10.13 ? 91   ILE   B N    1 
ATOM   10808 C  CA   . ILE   B 1 91  ? 25.626 13.992  69.908 1.00 12.56 ? 91   ILE   B CA   1 
ATOM   10809 C  C    . ILE   B 1 91  ? 25.042 15.001  68.909 1.00 11.83 ? 91   ILE   B C    1 
ATOM   10810 O  O    . ILE   B 1 91  ? 23.894 15.364  69.030 1.00 12.88 ? 91   ILE   B O    1 
ATOM   10811 C  CB   . ILE   B 1 91  ? 24.601 12.973  70.430 1.00 13.03 ? 91   ILE   B CB   1 
ATOM   10812 C  CG1  . ILE   B 1 91  ? 23.793 13.539  71.596 1.00 13.62 ? 91   ILE   B CG1  1 
ATOM   10813 C  CG2  . ILE   B 1 91  ? 25.304 11.682  70.809 1.00 13.44 ? 91   ILE   B CG2  1 
ATOM   10814 C  CD1  . ILE   B 1 91  ? 22.508 12.797  71.844 1.00 13.69 ? 91   ILE   B CD1  1 
ATOM   10815 H  H    . ILE   B 1 91  ? 25.761 15.500  71.210 1.00 12.16 ? 91   ILE   B H    1 
ATOM   10816 H  HA   . ILE   B 1 91  ? 26.294 13.444  69.467 1.00 15.07 ? 91   ILE   B HA   1 
ATOM   10817 H  HB   . ILE   B 1 91  ? 23.968 12.780  69.721 1.00 15.64 ? 91   ILE   B HB   1 
ATOM   10818 H  HG12 . ILE   B 1 91  ? 24.335 13.513  72.400 1.00 16.35 ? 91   ILE   B HG12 1 
ATOM   10819 H  HG13 . ILE   B 1 91  ? 23.592 14.471  71.420 1.00 16.35 ? 91   ILE   B HG13 1 
ATOM   10820 H  HG21 . ILE   B 1 91  ? 24.652 11.043  71.138 1.00 16.13 ? 91   ILE   B HG21 1 
ATOM   10821 H  HG22 . ILE   B 1 91  ? 25.751 11.316  70.030 1.00 16.13 ? 91   ILE   B HG22 1 
ATOM   10822 H  HG23 . ILE   B 1 91  ? 25.959 11.861  71.502 1.00 16.13 ? 91   ILE   B HG23 1 
ATOM   10823 H  HD11 . ILE   B 1 91  ? 22.041 13.200  72.592 1.00 16.43 ? 91   ILE   B HD11 1 
ATOM   10824 H  HD12 . ILE   B 1 91  ? 21.950 12.843  71.052 1.00 16.43 ? 91   ILE   B HD12 1 
ATOM   10825 H  HD13 . ILE   B 1 91  ? 22.704 11.869  72.048 1.00 16.43 ? 91   ILE   B HD13 1 
ATOM   10826 N  N    . SER   B 1 92  ? 25.887 15.433  67.986 1.00 10.83 ? 92   SER   B N    1 
ATOM   10827 C  CA   . SER   B 1 92  ? 25.493 16.489  67.034 1.00 9.66  ? 92   SER   B CA   1 
ATOM   10828 C  C    . SER   B 1 92  ? 25.400 15.903  65.620 1.00 11.79 ? 92   SER   B C    1 
ATOM   10829 O  O    . SER   B 1 92  ? 26.302 15.194  65.232 1.00 12.25 ? 92   SER   B O    1 
ATOM   10830 C  CB   . SER   B 1 92  ? 26.426 17.629  67.143 1.00 11.14 ? 92   SER   B CB   1 
ATOM   10831 O  OG   . SER   B 1 92  ? 26.522 18.091  68.477 1.00 13.60 ? 92   SER   B OG   1 
ATOM   10832 H  H    . SER   B 1 92  ? 26.688 15.138  67.886 1.00 12.99 ? 92   SER   B H    1 
ATOM   10833 H  HA   . SER   B 1 92  ? 24.611 16.832  67.248 1.00 11.59 ? 92   SER   B HA   1 
ATOM   10834 H  HB2  . SER   B 1 92  ? 27.304 17.362  66.827 1.00 13.37 ? 92   SER   B HB2  1 
ATOM   10835 H  HB3  . SER   B 1 92  ? 26.125 18.351  66.569 1.00 13.37 ? 92   SER   B HB3  1 
ATOM   10836 H  HG   . SER   B 1 92  ? 26.714 18.909  68.477 1.00 16.33 ? 92   SER   B HG   1 
ATOM   10837 N  N    . ASN   B 1 93  ? 24.315 16.225  64.918 1.00 12.14 ? 93   ASN   B N    1 
ATOM   10838 C  CA   . ASN   B 1 93  ? 24.060 15.566  63.616 1.00 10.21 ? 93   ASN   B CA   1 
ATOM   10839 C  C    . ASN   B 1 93  ? 24.267 16.565  62.476 1.00 11.52 ? 93   ASN   B C    1 
ATOM   10840 O  O    . ASN   B 1 93  ? 24.010 17.753  62.681 1.00 11.12 ? 93   ASN   B O    1 
ATOM   10841 C  CB   . ASN   B 1 93  ? 22.652 14.966  63.616 1.00 10.81 ? 93   ASN   B CB   1 
ATOM   10842 C  CG   . ASN   B 1 93  ? 22.351 14.049  62.452 1.00 8.74  ? 93   ASN   B CG   1 
ATOM   10843 O  OD1  . ASN   B 1 93  ? 22.341 14.478  61.303 1.00 11.43 ? 93   ASN   B OD1  1 
ATOM   10844 N  ND2  . ASN   B 1 93  ? 22.068 12.791  62.747 1.00 12.88 ? 93   ASN   B ND2  1 
ATOM   10845 H  H    . ASN   B 1 93  ? 23.725 16.803  65.160 1.00 14.57 ? 93   ASN   B H    1 
ATOM   10846 H  HA   . ASN   B 1 93  ? 24.689 14.841  63.479 1.00 12.26 ? 93   ASN   B HA   1 
ATOM   10847 H  HB2  . ASN   B 1 93  ? 22.525 14.472  64.441 1.00 12.97 ? 93   ASN   B HB2  1 
ATOM   10848 H  HB3  . ASN   B 1 93  ? 22.006 15.690  63.616 1.00 12.97 ? 93   ASN   B HB3  1 
ATOM   10849 H  HD21 . ASN   B 1 93  ? 21.867 12.237  62.121 1.00 15.45 ? 93   ASN   B HD21 1 
ATOM   10850 H  HD22 . ASN   B 1 93  ? 22.085 12.527  63.565 1.00 15.45 ? 93   ASN   B HD22 1 
ATOM   10851 N  N    . SER   B 1 94  ? 24.729 16.071  61.327 1.00 11.66 ? 94   SER   B N    1 
ATOM   10852 C  CA   . SER   B 1 94  ? 24.934 16.945  60.145 1.00 10.67 ? 94   SER   B CA   1 
ATOM   10853 C  C    . SER   B 1 94  ? 24.573 16.201  58.854 1.00 11.08 ? 94   SER   B C    1 
ATOM   10854 O  O    . SER   B 1 94  ? 24.639 14.966  58.836 1.00 11.76 ? 94   SER   B O    1 
ATOM   10855 C  CB   . SER   B 1 94  ? 26.339 17.476  60.078 1.00 9.61  ? 94   SER   B CB   1 
ATOM   10856 O  OG   . SER   B 1 94  ? 26.429 18.522  59.126 1.00 11.02 ? 94   SER   B OG   1 
ATOM   10857 H  H    . SER   B 1 94  ? 24.930 15.244  61.202 1.00 14.00 ? 94   SER   B H    1 
ATOM   10858 H  HA   . SER   B 1 94  ? 24.341 17.707  60.240 1.00 12.81 ? 94   SER   B HA   1 
ATOM   10859 H  HB2  . SER   B 1 94  ? 26.610 17.801  60.951 1.00 11.54 ? 94   SER   B HB2  1 
ATOM   10860 H  HB3  . SER   B 1 94  ? 26.950 16.761  59.840 1.00 11.54 ? 94   SER   B HB3  1 
ATOM   10861 H  HG   . SER   B 1 94  ? 27.099 18.398  58.635 1.00 13.23 ? 94   SER   B HG   1 
ATOM   10862 N  N    . GLY   B 1 95  ? 24.201 16.954  57.819 1.00 11.20 ? 95   GLY   B N    1 
ATOM   10863 C  CA   . GLY   B 1 95  ? 23.851 16.344  56.525 1.00 10.95 ? 95   GLY   B CA   1 
ATOM   10864 C  C    . GLY   B 1 95  ? 24.839 16.776  55.460 1.00 11.40 ? 95   GLY   B C    1 
ATOM   10865 O  O    . GLY   B 1 95  ? 26.048 16.652  55.693 1.00 12.15 ? 95   GLY   B O    1 
ATOM   10866 H  H    . GLY   B 1 95  ? 24.144 17.812  57.840 1.00 13.45 ? 95   GLY   B H    1 
ATOM   10867 H  HA2  . GLY   B 1 95  ? 23.853 15.377  56.604 1.00 13.14 ? 95   GLY   B HA2  1 
ATOM   10868 H  HA3  . GLY   B 1 95  ? 22.953 16.606  56.268 1.00 13.14 ? 95   GLY   B HA3  1 
ATOM   10869 N  N    . GLY   B 1 96  ? 24.333 17.277  54.333 1.00 11.76 ? 96   GLY   B N    1 
ATOM   10870 C  CA   . GLY   B 1 96  ? 25.219 17.648  53.221 1.00 12.69 ? 96   GLY   B CA   1 
ATOM   10871 C  C    . GLY   B 1 96  ? 25.712 16.432  52.454 1.00 12.66 ? 96   GLY   B C    1 
ATOM   10872 O  O    . GLY   B 1 96  ? 24.877 15.595  52.093 1.00 12.98 ? 96   GLY   B O    1 
ATOM   10873 H  H    . GLY   B 1 96  ? 23.495 17.409  54.190 1.00 14.12 ? 96   GLY   B H    1 
ATOM   10874 H  HA2  . GLY   B 1 96  ? 24.746 18.241  52.616 1.00 15.23 ? 96   GLY   B HA2  1 
ATOM   10875 H  HA3  . GLY   B 1 96  ? 25.979 18.142  53.566 1.00 15.23 ? 96   GLY   B HA3  1 
ATOM   10876 N  N    . LYS   B 1 97  ? 27.029 16.333  52.234 1.00 11.63 ? 97   LYS   B N    1 
ATOM   10877 C  CA   . LYS   B 1 97  ? 27.588 15.224  51.412 1.00 12.58 ? 97   LYS   B CA   1 
ATOM   10878 C  C    . LYS   B 1 97  ? 28.829 14.599  52.068 1.00 13.49 ? 97   LYS   B C    1 
ATOM   10879 O  O    . LYS   B 1 97  ? 29.119 13.439  51.751 1.00 14.46 ? 97   LYS   B O    1 
ATOM   10880 C  CB   . LYS   B 1 97  ? 27.961 15.762  50.027 1.00 14.60 ? 97   LYS   B CB   1 
ATOM   10881 C  CG   . LYS   B 1 97  ? 26.886 16.580  49.327 1.00 22.09 ? 97   LYS   B CG   1 
ATOM   10882 C  CD   . LYS   B 1 97  ? 25.833 15.726  48.657 1.00 23.77 ? 97   LYS   B CD   1 
ATOM   10883 C  CE   . LYS   B 1 97  ? 25.515 16.178  47.248 1.00 33.53 ? 97   LYS   B CE   1 
ATOM   10884 N  NZ   . LYS   B 1 97  ? 25.529 17.654  47.129 1.00 27.59 ? 97   LYS   B NZ   1 
ATOM   10885 H  H    . LYS   B 1 97  ? 27.614 16.883  52.542 1.00 13.96 ? 97   LYS   B H    1 
ATOM   10886 H  HA   . LYS   B 1 97  ? 26.911 14.534  51.337 1.00 15.10 ? 97   LYS   B HA   1 
ATOM   10887 H  HB2  . LYS   B 1 97  ? 28.756 16.310  50.114 1.00 17.52 ? 97   LYS   B HB2  1 
ATOM   10888 H  HB3  . LYS   B 1 97  ? 28.195 15.012  49.459 1.00 17.52 ? 97   LYS   B HB3  1 
ATOM   10889 H  HG2  . LYS   B 1 97  ? 26.458 17.163  49.974 1.00 26.52 ? 97   LYS   B HG2  1 
ATOM   10890 H  HG3  . LYS   B 1 97  ? 27.303 17.151  48.663 1.00 26.52 ? 97   LYS   B HG3  1 
ATOM   10891 H  HD2  . LYS   B 1 97  ? 26.136 14.805  48.635 1.00 28.53 ? 97   LYS   B HD2  1 
ATOM   10892 H  HD3  . LYS   B 1 97  ? 25.022 15.745  49.188 1.00 28.53 ? 97   LYS   B HD3  1 
ATOM   10893 H  HE2  . LYS   B 1 97  ? 26.161 15.798  46.632 1.00 40.24 ? 97   LYS   B HE2  1 
ATOM   10894 H  HE3  . LYS   B 1 97  ? 24.643 15.841  46.989 1.00 40.24 ? 97   LYS   B HE3  1 
ATOM   10895 H  HZ1  . LYS   B 1 97  ? 24.915 17.910  46.538 1.00 33.11 ? 97   LYS   B HZ1  1 
ATOM   10896 H  HZ2  . LYS   B 1 97  ? 25.347 18.018  47.921 1.00 33.11 ? 97   LYS   B HZ2  1 
ATOM   10897 H  HZ3  . LYS   B 1 97  ? 26.333 17.923  46.857 1.00 33.11 ? 97   LYS   B HZ3  1 
ATOM   10898 N  N    . TRP   B 1 98  ? 29.521 15.332  52.938 1.00 11.86 ? 98   TRP   B N    1 
ATOM   10899 C  CA   . TRP   B 1 98  ? 30.791 14.840  53.548 1.00 11.66 ? 98   TRP   B CA   1 
ATOM   10900 C  C    . TRP   B 1 98  ? 30.681 13.396  54.049 1.00 12.86 ? 98   TRP   B C    1 
ATOM   10901 O  O    . TRP   B 1 98  ? 31.576 12.596  53.734 1.00 12.44 ? 98   TRP   B O    1 
ATOM   10902 C  CB   . TRP   B 1 98  ? 31.214 15.775  54.691 1.00 12.57 ? 98   TRP   B CB   1 
ATOM   10903 C  CG   . TRP   B 1 98  ? 32.599 15.525  55.206 1.00 10.62 ? 98   TRP   B CG   1 
ATOM   10904 C  CD1  . TRP   B 1 98  ? 33.746 16.161  54.832 1.00 11.76 ? 98   TRP   B CD1  1 
ATOM   10905 C  CD2  . TRP   B 1 98  ? 32.984 14.565  56.205 1.00 11.03 ? 98   TRP   B CD2  1 
ATOM   10906 N  NE1  . TRP   B 1 98  ? 34.817 15.662  55.523 1.00 11.09 ? 98   TRP   B NE1  1 
ATOM   10907 C  CE2  . TRP   B 1 98  ? 34.380 14.682  56.374 1.00 11.63 ? 98   TRP   B CE2  1 
ATOM   10908 C  CE3  . TRP   B 1 98  ? 32.289 13.621  56.968 1.00 12.58 ? 98   TRP   B CE3  1 
ATOM   10909 C  CZ2  . TRP   B 1 98  ? 35.088 13.889  57.275 1.00 12.15 ? 98   TRP   B CZ2  1 
ATOM   10910 C  CZ3  . TRP   B 1 98  ? 32.990 12.837  57.855 1.00 10.34 ? 98   TRP   B CZ3  1 
ATOM   10911 C  CH2  . TRP   B 1 98  ? 34.370 12.971  58.005 1.00 12.08 ? 98   TRP   B CH2  1 
ATOM   10912 H  H    . TRP   B 1 98  ? 29.285 16.117  53.197 1.00 14.24 ? 98   TRP   B H    1 
ATOM   10913 H  HA   . TRP   B 1 98  ? 31.469 14.844  52.854 1.00 14.00 ? 98   TRP   B HA   1 
ATOM   10914 H  HB2  . TRP   B 1 98  ? 31.155 16.693  54.384 1.00 15.09 ? 98   TRP   B HB2  1 
ATOM   10915 H  HB3  . TRP   B 1 98  ? 30.585 15.680  55.423 1.00 15.09 ? 98   TRP   B HB3  1 
ATOM   10916 H  HD1  . TRP   B 1 98  ? 33.794 16.839  54.197 1.00 14.12 ? 98   TRP   B HD1  1 
ATOM   10917 H  HE1  . TRP   B 1 98  ? 35.632 15.922  55.437 1.00 13.31 ? 98   TRP   B HE1  1 
ATOM   10918 H  HE3  . TRP   B 1 98  ? 31.368 13.525  56.877 1.00 15.09 ? 98   TRP   B HE3  1 
ATOM   10919 H  HZ2  . TRP   B 1 98  ? 36.008 13.977  57.378 1.00 14.59 ? 98   TRP   B HZ2  1 
ATOM   10920 H  HZ3  . TRP   B 1 98  ? 32.535 12.206  58.364 1.00 12.41 ? 98   TRP   B HZ3  1 
ATOM   10921 H  HH2  . TRP   B 1 98  ? 34.815 12.426  58.613 1.00 14.50 ? 98   TRP   B HH2  1 
ATOM   10922 N  N    . GLY   B 1 99  ? 29.649 13.082  54.828 1.00 13.92 ? 99   GLY   B N    1 
ATOM   10923 C  CA   . GLY   B 1 99  ? 29.545 11.740  55.435 1.00 13.47 ? 99   GLY   B CA   1 
ATOM   10924 C  C    . GLY   B 1 99  ? 29.445 10.639  54.397 1.00 14.32 ? 99   GLY   B C    1 
ATOM   10925 O  O    . GLY   B 1 99  ? 29.881 9.515   54.685 1.00 15.41 ? 99   GLY   B O    1 
ATOM   10926 H  H    . GLY   B 1 99  ? 29.004 13.617  55.020 1.00 16.71 ? 99   GLY   B H    1 
ATOM   10927 H  HA2  . GLY   B 1 99  ? 30.320 11.581  55.997 1.00 16.17 ? 99   GLY   B HA2  1 
ATOM   10928 H  HA3  . GLY   B 1 99  ? 28.766 11.709  56.012 1.00 16.17 ? 99   GLY   B HA3  1 
ATOM   10929 N  N    . VAL   B 1 100 ? 28.881 10.959  53.237 1.00 15.19 ? 100  VAL   B N    1 
ATOM   10930 C  CA   . VAL   B 1 100 ? 28.676 9.927   52.183 1.00 15.23 ? 100  VAL   B CA   1 
ATOM   10931 C  C    . VAL   B 1 100 ? 30.036 9.586   51.562 1.00 14.78 ? 100  VAL   B C    1 
ATOM   10932 O  O    . VAL   B 1 100 ? 30.267 8.408   51.257 1.00 14.92 ? 100  VAL   B O    1 
ATOM   10933 C  CB   . VAL   B 1 100 ? 27.651 10.407  51.138 1.00 15.62 ? 100  VAL   B CB   1 
ATOM   10934 C  CG1  . VAL   B 1 100 ? 27.563 9.462   49.949 1.00 16.03 ? 100  VAL   B CG1  1 
ATOM   10935 C  CG2  . VAL   B 1 100 ? 26.280 10.618  51.758 1.00 16.70 ? 100  VAL   B CG2  1 
ATOM   10936 H  H    . VAL   B 1 100 ? 28.610 11.748  53.029 1.00 18.23 ? 100  VAL   B H    1 
ATOM   10937 H  HA   . VAL   B 1 100 ? 28.305 9.119   52.571 1.00 18.28 ? 100  VAL   B HA   1 
ATOM   10938 H  HB   . VAL   B 1 100 ? 27.969 11.263  50.809 1.00 18.75 ? 100  VAL   B HB   1 
ATOM   10939 H  HG11 . VAL   B 1 100 ? 26.909 9.798   49.316 1.00 19.24 ? 100  VAL   B HG11 1 
ATOM   10940 H  HG12 . VAL   B 1 100 ? 28.430 9.403   49.517 1.00 19.24 ? 100  VAL   B HG12 1 
ATOM   10941 H  HG13 . VAL   B 1 100 ? 27.294 8.582   50.254 1.00 19.24 ? 100  VAL   B HG13 1 
ATOM   10942 H  HG21 . VAL   B 1 100 ? 25.659 10.919  51.076 1.00 20.05 ? 100  VAL   B HG21 1 
ATOM   10943 H  HG22 . VAL   B 1 100 ? 25.964 9.783   52.136 1.00 20.05 ? 100  VAL   B HG22 1 
ATOM   10944 H  HG23 . VAL   B 1 100 ? 26.341 11.287  52.458 1.00 20.05 ? 100  VAL   B HG23 1 
ATOM   10945 N  N    . ASP   B 1 101 ? 30.900 10.585  51.403 1.00 14.48 ? 101  ASP   B N    1 
ATOM   10946 C  CA   . ASP   B 1 101 ? 32.262 10.322  50.865 1.00 13.59 ? 101  ASP   B CA   1 
ATOM   10947 C  C    . ASP   B 1 101 ? 33.068 9.481   51.866 1.00 14.54 ? 101  ASP   B C    1 
ATOM   10948 O  O    . ASP   B 1 101 ? 33.825 8.608   51.427 1.00 12.95 ? 101  ASP   B O    1 
ATOM   10949 C  CB   . ASP   B 1 101 ? 32.989 11.614  50.491 1.00 12.59 ? 101  ASP   B CB   1 
ATOM   10950 C  CG   . ASP   B 1 101 ? 32.837 11.963  49.021 1.00 16.66 ? 101  ASP   B CG   1 
ATOM   10951 O  OD1  . ASP   B 1 101 ? 33.645 11.465  48.217 1.00 17.30 ? 101  ASP   B OD1  1 
ATOM   10952 O  OD2  . ASP   B 1 101 ? 31.903 12.715  48.693 1.00 18.94 ? 101  ASP   B OD2  1 
ATOM   10953 H  H    . ASP   B 1 101 ? 30.736 11.408  51.592 1.00 17.38 ? 101  ASP   B H    1 
ATOM   10954 H  HA   . ASP   B 1 101 ? 32.171 9.815   50.043 1.00 16.31 ? 101  ASP   B HA   1 
ATOM   10955 H  HB2  . ASP   B 1 101 ? 32.645 12.343  51.031 1.00 15.12 ? 101  ASP   B HB2  1 
ATOM   10956 H  HB3  . ASP   B 1 101 ? 33.931 11.524  50.703 1.00 15.12 ? 101  ASP   B HB3  1 
ATOM   10957 N  N    . LEU   B 1 102 ? 32.922 9.756   53.166 1.00 13.45 ? 102  LEU   B N    1 
ATOM   10958 C  CA   . LEU   B 1 102 ? 33.625 8.919   54.176 1.00 11.88 ? 102  LEU   B CA   1 
ATOM   10959 C  C    . LEU   B 1 102 ? 33.181 7.463   54.005 1.00 13.97 ? 102  LEU   B C    1 
ATOM   10960 O  O    . LEU   B 1 102 ? 34.043 6.569   54.034 1.00 13.83 ? 102  LEU   B O    1 
ATOM   10961 C  CB   . LEU   B 1 102 ? 33.317 9.438   55.585 1.00 13.71 ? 102  LEU   B CB   1 
ATOM   10962 C  CG   . LEU   B 1 102 ? 33.976 8.648   56.715 1.00 12.08 ? 102  LEU   B CG   1 
ATOM   10963 C  CD1  . LEU   B 1 102 ? 35.489 8.744   56.623 1.00 13.69 ? 102  LEU   B CD1  1 
ATOM   10964 C  CD2  . LEU   B 1 102 ? 33.490 9.126   58.074 1.00 13.71 ? 102  LEU   B CD2  1 
ATOM   10965 H  H    . LEU   B 1 102 ? 32.442 10.395  53.485 1.00 16.15 ? 102  LEU   B H    1 
ATOM   10966 H  HA   . LEU   B 1 102 ? 34.585 8.968   54.047 1.00 14.26 ? 102  LEU   B HA   1 
ATOM   10967 H  HB2  . LEU   B 1 102 ? 33.602 10.363  55.645 1.00 16.45 ? 102  LEU   B HB2  1 
ATOM   10968 H  HB3  . LEU   B 1 102 ? 32.356 9.428   55.717 1.00 16.45 ? 102  LEU   B HB3  1 
ATOM   10969 H  HG   . LEU   B 1 102 ? 33.721 7.717   56.617 1.00 14.50 ? 102  LEU   B HG   1 
ATOM   10970 H  HD11 . LEU   B 1 102 ? 35.890 8.238   57.347 1.00 16.43 ? 102  LEU   B HD11 1 
ATOM   10971 H  HD12 . LEU   B 1 102 ? 35.785 8.383   55.773 1.00 16.43 ? 102  LEU   B HD12 1 
ATOM   10972 H  HD13 . LEU   B 1 102 ? 35.759 9.673   56.691 1.00 16.43 ? 102  LEU   B HD13 1 
ATOM   10973 H  HD21 . LEU   B 1 102 ? 33.922 8.610   58.772 1.00 16.46 ? 102  LEU   B HD21 1 
ATOM   10974 H  HD22 . LEU   B 1 102 ? 33.708 10.065  58.184 1.00 16.46 ? 102  LEU   B HD22 1 
ATOM   10975 H  HD23 . LEU   B 1 102 ? 32.529 9.009   58.134 1.00 16.46 ? 102  LEU   B HD23 1 
ATOM   10976 N  N    . LYS   B 1 103 ? 31.878 7.243   53.839 1.00 14.40 ? 103  LYS   B N    1 
ATOM   10977 C  CA   . LYS   B 1 103 ? 31.345 5.864   53.702 1.00 13.19 ? 103  LYS   B CA   1 
ATOM   10978 C  C    . LYS   B 1 103 ? 31.875 5.251   52.402 1.00 17.84 ? 103  LYS   B C    1 
ATOM   10979 O  O    . LYS   B 1 103 ? 32.253 4.070   52.412 1.00 18.78 ? 103  LYS   B O    1 
ATOM   10980 C  CB   . LYS   B 1 103 ? 29.815 5.899   53.732 1.00 19.20 ? 103  LYS   B CB   1 
ATOM   10981 C  CG   . LYS   B 1 103 ? 29.140 4.553   53.931 1.00 26.00 ? 103  LYS   B CG   1 
ATOM   10982 C  CD   . LYS   B 1 103 ? 29.133 4.097   55.368 1.00 20.29 ? 103  LYS   B CD   1 
ATOM   10983 C  CE   . LYS   B 1 103 ? 28.376 2.800   55.545 1.00 19.97 ? 103  LYS   B CE   1 
ATOM   10984 N  NZ   . LYS   B 1 103 ? 26.911 3.001   55.461 1.00 18.65 ? 103  LYS   B NZ   1 
ATOM   10985 H  H    . LYS   B 1 103 ? 31.283 7.863   53.802 1.00 17.29 ? 103  LYS   B H    1 
ATOM   10986 H  HA   . LYS   B 1 103 ? 31.641 5.310   54.442 1.00 15.83 ? 103  LYS   B HA   1 
ATOM   10987 H  HB2  . LYS   B 1 103 ? 29.534 6.494   54.444 1.00 23.05 ? 103  LYS   B HB2  1 
ATOM   10988 H  HB3  . LYS   B 1 103 ? 29.498 6.283   52.900 1.00 23.05 ? 103  LYS   B HB3  1 
ATOM   10989 H  HG2  . LYS   B 1 103 ? 28.226 4.606   53.610 1.00 31.20 ? 103  LYS   B HG2  1 
ATOM   10990 H  HG3  . LYS   B 1 103 ? 29.593 3.888   53.389 1.00 31.20 ? 103  LYS   B HG3  1 
ATOM   10991 H  HD2  . LYS   B 1 103 ? 30.046 3.983   55.675 1.00 24.35 ? 103  LYS   B HD2  1 
ATOM   10992 H  HD3  . LYS   B 1 103 ? 28.731 4.784   55.923 1.00 24.35 ? 103  LYS   B HD3  1 
ATOM   10993 H  HE2  . LYS   B 1 103 ? 28.655 2.167   54.865 1.00 23.97 ? 103  LYS   B HE2  1 
ATOM   10994 H  HE3  . LYS   B 1 103 ? 28.600 2.410   56.404 1.00 23.97 ? 103  LYS   B HE3  1 
ATOM   10995 H  HZ1  . LYS   B 1 103 ? 26.511 2.218   55.321 1.00 22.38 ? 103  LYS   B HZ1  1 
ATOM   10996 H  HZ2  . LYS   B 1 103 ? 26.615 3.353   56.223 1.00 22.38 ? 103  LYS   B HZ2  1 
ATOM   10997 H  HZ3  . LYS   B 1 103 ? 26.725 3.553   54.788 1.00 22.38 ? 103  LYS   B HZ3  1 
ATOM   10998 N  N    . LYS   B 1 104 ? 31.909 6.041   51.329 1.00 17.42 ? 104  LYS   B N    1 
ATOM   10999 C  CA   . LYS   B 1 104 ? 32.410 5.535   50.024 1.00 18.60 ? 104  LYS   B CA   1 
ATOM   11000 C  C    . LYS   B 1 104 ? 33.929 5.336   50.081 1.00 18.75 ? 104  LYS   B C    1 
ATOM   11001 O  O    . LYS   B 1 104 ? 34.447 4.617   49.222 1.00 22.41 ? 104  LYS   B O    1 
ATOM   11002 C  CB   . LYS   B 1 104 ? 31.993 6.483   48.896 1.00 19.36 ? 104  LYS   B CB   1 
ATOM   11003 C  CG   . LYS   B 1 104 ? 30.488 6.577   48.687 1.00 19.43 ? 104  LYS   B CG   1 
ATOM   11004 C  CD   . LYS   B 1 104 ? 30.073 7.399   47.490 1.00 24.06 ? 104  LYS   B CD   1 
ATOM   11005 C  CE   . LYS   B 1 104 ? 28.694 7.021   46.992 1.00 35.90 ? 104  LYS   B CE   1 
ATOM   11006 N  NZ   . LYS   B 1 104 ? 27.918 8.200   46.540 1.00 36.69 ? 104  LYS   B NZ   1 
ATOM   11007 H  H    . LYS   B 1 104 ? 31.653 6.862   51.323 1.00 20.91 ? 104  LYS   B H    1 
ATOM   11008 H  HA   . LYS   B 1 104 ? 32.012 4.670   49.838 1.00 22.33 ? 104  LYS   B HA   1 
ATOM   11009 H  HB2  . LYS   B 1 104 ? 32.339 7.369   49.087 1.00 23.23 ? 104  LYS   B HB2  1 
ATOM   11010 H  HB3  . LYS   B 1 104 ? 32.407 6.188   48.070 1.00 23.23 ? 104  LYS   B HB3  1 
ATOM   11011 H  HG2  . LYS   B 1 104 ? 30.130 5.681   48.590 1.00 23.32 ? 104  LYS   B HG2  1 
ATOM   11012 H  HG3  . LYS   B 1 104 ? 30.085 6.959   49.483 1.00 23.32 ? 104  LYS   B HG3  1 
ATOM   11013 H  HD2  . LYS   B 1 104 ? 30.084 8.340   47.725 1.00 28.88 ? 104  LYS   B HD2  1 
ATOM   11014 H  HD3  . LYS   B 1 104 ? 30.718 7.278   46.776 1.00 28.88 ? 104  LYS   B HD3  1 
ATOM   11015 H  HE2  . LYS   B 1 104 ? 28.778 6.391   46.259 1.00 43.09 ? 104  LYS   B HE2  1 
ATOM   11016 H  HE3  . LYS   B 1 104 ? 28.209 6.569   47.700 1.00 43.09 ? 104  LYS   B HE3  1 
ATOM   11017 H  HZ1  . LYS   B 1 104 ? 27.196 8.295   47.052 1.00 44.04 ? 104  LYS   B HZ1  1 
ATOM   11018 H  HZ2  . LYS   B 1 104 ? 28.423 8.930   46.602 1.00 44.04 ? 104  LYS   B HZ2  1 
ATOM   11019 H  HZ3  . LYS   B 1 104 ? 27.667 8.084   45.694 1.00 44.04 ? 104  LYS   B HZ3  1 
ATOM   11020 N  N    . ALA   B 1 105 ? 34.601 5.935   51.065 1.00 16.37 ? 105  ALA   B N    1 
ATOM   11021 C  CA   . ALA   B 1 105 ? 36.064 5.744   51.217 1.00 16.07 ? 105  ALA   B CA   1 
ATOM   11022 C  C    . ALA   B 1 105 ? 36.354 4.449   51.993 1.00 17.25 ? 105  ALA   B C    1 
ATOM   11023 O  O    . ALA   B 1 105 ? 37.535 4.105   52.112 1.00 18.34 ? 105  ALA   B O    1 
ATOM   11024 C  CB   . ALA   B 1 105 ? 36.680 6.950   51.878 1.00 17.45 ? 105  ALA   B CB   1 
ATOM   11025 H  H    . ALA   B 1 105 ? 34.243 6.451   51.652 1.00 19.64 ? 105  ALA   B H    1 
ATOM   11026 H  HA   . ALA   B 1 105 ? 36.469 5.654   50.340 1.00 19.29 ? 105  ALA   B HA   1 
ATOM   11027 H  HB1  . ALA   B 1 105 ? 37.636 6.815   51.972 1.00 20.94 ? 105  ALA   B HB1  1 
ATOM   11028 H  HB2  . ALA   B 1 105 ? 36.517 7.736   51.333 1.00 20.94 ? 105  ALA   B HB2  1 
ATOM   11029 H  HB3  . ALA   B 1 105 ? 36.284 7.077   52.754 1.00 20.94 ? 105  ALA   B HB3  1 
ATOM   11030 N  N    . GLY   B 1 106 ? 35.315 3.775   52.498 1.00 16.59 ? 106  GLY   B N    1 
ATOM   11031 C  CA   . GLY   B 1 106 ? 35.495 2.477   53.181 1.00 16.05 ? 106  GLY   B CA   1 
ATOM   11032 C  C    . GLY   B 1 106 ? 35.508 2.577   54.697 1.00 16.55 ? 106  GLY   B C    1 
ATOM   11033 O  O    . GLY   B 1 106 ? 35.808 1.563   55.346 1.00 16.46 ? 106  GLY   B O    1 
ATOM   11034 H  H    . GLY   B 1 106 ? 34.500 4.047   52.458 1.00 19.91 ? 106  GLY   B H    1 
ATOM   11035 H  HA2  . GLY   B 1 106 ? 34.782 1.878   52.911 1.00 19.27 ? 106  GLY   B HA2  1 
ATOM   11036 H  HA3  . GLY   B 1 106 ? 36.328 2.078   52.885 1.00 19.27 ? 106  GLY   B HA3  1 
ATOM   11037 N  N    . TRP   B 1 107 ? 35.179 3.744   55.250 1.00 14.99 ? 107  TRP   B N    1 
ATOM   11038 C  CA   . TRP   B 1 107 ? 35.264 3.940   56.719 1.00 14.07 ? 107  TRP   B CA   1 
ATOM   11039 C  C    . TRP   B 1 107 ? 33.874 4.182   57.307 1.00 15.41 ? 107  TRP   B C    1 
ATOM   11040 O  O    . TRP   B 1 107 ? 33.133 5.005   56.753 1.00 16.41 ? 107  TRP   B O    1 
ATOM   11041 C  CB   . TRP   B 1 107 ? 36.186 5.116   57.041 1.00 13.73 ? 107  TRP   B CB   1 
ATOM   11042 C  CG   . TRP   B 1 107 ? 37.554 5.037   56.442 1.00 17.40 ? 107  TRP   B CG   1 
ATOM   11043 C  CD1  . TRP   B 1 107 ? 38.030 5.745   55.377 1.00 16.57 ? 107  TRP   B CD1  1 
ATOM   11044 C  CD2  . TRP   B 1 107 ? 38.644 4.221   56.902 1.00 15.86 ? 107  TRP   B CD2  1 
ATOM   11045 N  NE1  . TRP   B 1 107 ? 39.337 5.418   55.137 1.00 17.25 ? 107  TRP   B NE1  1 
ATOM   11046 C  CE2  . TRP   B 1 107 ? 39.741 4.485   56.055 1.00 17.05 ? 107  TRP   B CE2  1 
ATOM   11047 C  CE3  . TRP   B 1 107 ? 38.797 3.293   57.937 1.00 13.85 ? 107  TRP   B CE3  1 
ATOM   11048 C  CZ2  . TRP   B 1 107 ? 40.972 3.853   56.216 1.00 13.79 ? 107  TRP   B CZ2  1 
ATOM   11049 C  CZ3  . TRP   B 1 107 ? 40.014 2.670   58.096 1.00 17.99 ? 107  TRP   B CZ3  1 
ATOM   11050 C  CH2  . TRP   B 1 107 ? 41.084 2.947   57.246 1.00 19.03 ? 107  TRP   B CH2  1 
ATOM   11051 H  H    . TRP   B 1 107 ? 34.907 4.431   54.809 1.00 17.99 ? 107  TRP   B H    1 
ATOM   11052 H  HA   . TRP   B 1 107 ? 35.631 3.136   57.118 1.00 16.89 ? 107  TRP   B HA   1 
ATOM   11053 H  HB2  . TRP   B 1 107 ? 35.762 5.933   56.736 1.00 16.48 ? 107  TRP   B HB2  1 
ATOM   11054 H  HB3  . TRP   B 1 107 ? 36.274 5.185   58.005 1.00 16.48 ? 107  TRP   B HB3  1 
ATOM   11055 H  HD1  . TRP   B 1 107 ? 37.537 6.361   54.885 1.00 19.89 ? 107  TRP   B HD1  1 
ATOM   11056 H  HE1  . TRP   B 1 107 ? 39.826 5.746   54.510 1.00 20.70 ? 107  TRP   B HE1  1 
ATOM   11057 H  HE3  . TRP   B 1 107 ? 38.089 3.100   58.508 1.00 16.63 ? 107  TRP   B HE3  1 
ATOM   11058 H  HZ2  . TRP   B 1 107 ? 41.688 4.036   55.651 1.00 16.56 ? 107  TRP   B HZ2  1 
ATOM   11059 H  HZ3  . TRP   B 1 107 ? 40.125 2.053   58.783 1.00 21.59 ? 107  TRP   B HZ3  1 
ATOM   11060 H  HH2  . TRP   B 1 107 ? 41.893 2.509   57.378 1.00 22.84 ? 107  TRP   B HH2  1 
ATOM   11061 N  N    . ASP   B 1 108 ? 33.553 3.492   58.400 1.00 15.43 ? 108  ASP   B N    1 
ATOM   11062 C  CA   . ASP   B 1 108 ? 32.261 3.733   59.086 1.00 12.84 ? 108  ASP   B CA   1 
ATOM   11063 C  C    . ASP   B 1 108 ? 32.440 4.797   60.162 1.00 13.73 ? 108  ASP   B C    1 
ATOM   11064 O  O    . ASP   B 1 108 ? 31.453 5.471   60.486 1.00 13.83 ? 108  ASP   B O    1 
ATOM   11065 C  CB   . ASP   B 1 108 ? 31.781 2.476   59.801 1.00 17.61 ? 108  ASP   B CB   1 
ATOM   11066 C  CG   . ASP   B 1 108 ? 31.553 1.298   58.873 1.00 20.61 ? 108  ASP   B CG   1 
ATOM   11067 O  OD1  . ASP   B 1 108 ? 30.567 1.336   58.118 1.00 19.84 ? 108  ASP   B OD1  1 
ATOM   11068 O  OD2  . ASP   B 1 108 ? 32.362 0.355   58.923 1.00 18.14 ? 108  ASP   B OD2  1 
ATOM   11069 H  H    . ASP   B 1 108 ? 34.050 2.891   58.762 1.00 18.52 ? 108  ASP   B H    1 
ATOM   11070 H  HA   . ASP   B 1 108 ? 31.622 4.007   58.410 1.00 15.42 ? 108  ASP   B HA   1 
ATOM   11071 H  HB2  . ASP   B 1 108 ? 32.434 2.226   60.473 1.00 21.14 ? 108  ASP   B HB2  1 
ATOM   11072 H  HB3  . ASP   B 1 108 ? 30.954 2.675   60.268 1.00 21.14 ? 108  ASP   B HB3  1 
ATOM   11073 N  N    . MET   B 1 109 ? 33.660 4.951   60.668 1.00 12.47 ? 109  MET   B N    1 
ATOM   11074 C  CA   . MET   B 1 109 ? 33.846 5.853   61.829 1.00 13.14 ? 109  MET   B CA   1 
ATOM   11075 C  C    . MET   B 1 109 ? 35.297 6.316   61.936 1.00 16.25 ? 109  MET   B C    1 
ATOM   11076 O  O    . MET   B 1 109 ? 36.194 5.536   61.564 1.00 15.53 ? 109  MET   B O    1 
ATOM   11077 C  CB   . MET   B 1 109 ? 33.469 5.091   63.107 1.00 14.86 ? 109  MET   B CB   1 
ATOM   11078 C  CG   . MET   B 1 109 ? 33.730 5.846   64.391 1.00 16.29 ? 109  MET   B CG   1 
ATOM   11079 S  SD   . MET   B 1 109 ? 32.975 5.005   65.811 1.00 15.89 ? 109  MET   B SD   1 
ATOM   11080 C  CE   . MET   B 1 109 ? 33.687 3.368   65.651 1.00 16.51 ? 109  MET   B CE   1 
ATOM   11081 H  H    . MET   B 1 109 ? 34.372 4.566   60.377 1.00 14.97 ? 109  MET   B H    1 
ATOM   11082 H  HA   . MET   B 1 109 ? 33.282 6.634   61.713 1.00 15.77 ? 109  MET   B HA   1 
ATOM   11083 H  HB2  . MET   B 1 109 ? 32.527 4.861   63.067 1.00 17.84 ? 109  MET   B HB2  1 
ATOM   11084 H  HB3  . MET   B 1 109 ? 33.964 4.257   63.130 1.00 17.84 ? 109  MET   B HB3  1 
ATOM   11085 H  HG2  . MET   B 1 109 ? 34.686 5.929   64.532 1.00 19.56 ? 109  MET   B HG2  1 
ATOM   11086 H  HG3  . MET   B 1 109 ? 33.375 6.746   64.318 1.00 19.56 ? 109  MET   B HG3  1 
ATOM   11087 H  HE1  . MET   B 1 109 ? 33.359 2.801   66.366 1.00 19.81 ? 109  MET   B HE1  1 
ATOM   11088 H  HE2  . MET   B 1 109 ? 33.435 2.987   64.795 1.00 19.81 ? 109  MET   B HE2  1 
ATOM   11089 H  HE3  . MET   B 1 109 ? 34.654 3.429   65.705 1.00 19.81 ? 109  MET   B HE3  1 
ATOM   11090 N  N    . ILE   B 1 110 ? 35.498 7.546   62.402 1.00 16.32 ? 110  ILE   B N    1 
ATOM   11091 C  CA   . ILE   B 1 110 ? 36.871 8.047   62.673 1.00 15.34 ? 110  ILE   B CA   1 
ATOM   11092 C  C    . ILE   B 1 110 ? 36.967 8.326   64.176 1.00 14.24 ? 110  ILE   B C    1 
ATOM   11093 O  O    . ILE   B 1 110 ? 36.045 8.962   64.710 1.00 13.18 ? 110  ILE   B O    1 
ATOM   11094 C  CB   . ILE   B 1 110 ? 37.192 9.314   61.856 1.00 14.07 ? 110  ILE   B CB   1 
ATOM   11095 C  CG1  . ILE   B 1 110 ? 36.893 9.132   60.367 1.00 16.17 ? 110  ILE   B CG1  1 
ATOM   11096 C  CG2  . ILE   B 1 110 ? 38.629 9.750   62.093 1.00 15.15 ? 110  ILE   B CG2  1 
ATOM   11097 C  CD1  . ILE   B 1 110 ? 37.229 10.344  59.533 1.00 14.62 ? 110  ILE   B CD1  1 
ATOM   11098 H  H    . ILE   B 1 110 ? 34.870 8.109   62.570 1.00 19.59 ? 110  ILE   B H    1 
ATOM   11099 H  HA   . ILE   B 1 110 ? 37.523 7.381   62.404 1.00 18.41 ? 110  ILE   B HA   1 
ATOM   11100 H  HB   . ILE   B 1 110 ? 36.606 10.022  62.167 1.00 16.88 ? 110  ILE   B HB   1 
ATOM   11101 H  HG12 . ILE   B 1 110 ? 37.394 8.371   60.035 1.00 19.41 ? 110  ILE   B HG12 1 
ATOM   11102 H  HG13 . ILE   B 1 110 ? 35.952 8.923   60.257 1.00 19.41 ? 110  ILE   B HG13 1 
ATOM   11103 H  HG21 . ILE   B 1 110 ? 38.815 10.547  61.573 1.00 18.18 ? 110  ILE   B HG21 1 
ATOM   11104 H  HG22 . ILE   B 1 110 ? 38.758 9.942   63.035 1.00 18.18 ? 110  ILE   B HG22 1 
ATOM   11105 H  HG23 . ILE   B 1 110 ? 39.232 9.040   61.822 1.00 18.18 ? 110  ILE   B HG23 1 
ATOM   11106 H  HD11 . ILE   B 1 110 ? 37.018 10.166  58.603 1.00 17.55 ? 110  ILE   B HD11 1 
ATOM   11107 H  HD12 . ILE   B 1 110 ? 36.711 11.104  59.842 1.00 17.55 ? 110  ILE   B HD12 1 
ATOM   11108 H  HD13 . ILE   B 1 110 ? 38.175 10.543  59.617 1.00 17.55 ? 110  ILE   B HD13 1 
ATOM   11109 N  N    . ILE   B 1 111 ? 38.023 7.838   64.827 1.00 13.28 ? 111  ILE   B N    1 
ATOM   11110 C  CA   . ILE   B 1 111 ? 38.254 8.164   66.262 1.00 13.85 ? 111  ILE   B CA   1 
ATOM   11111 C  C    . ILE   B 1 111 ? 39.516 9.026   66.329 1.00 15.47 ? 111  ILE   B C    1 
ATOM   11112 O  O    . ILE   B 1 111 ? 40.605 8.500   66.051 1.00 17.67 ? 111  ILE   B O    1 
ATOM   11113 C  CB   . ILE   B 1 111 ? 38.398 6.891   67.117 1.00 18.69 ? 111  ILE   B CB   1 
ATOM   11114 C  CG1  . ILE   B 1 111 ? 37.207 5.945   66.948 1.00 17.34 ? 111  ILE   B CG1  1 
ATOM   11115 C  CG2  . ILE   B 1 111 ? 38.630 7.252   68.576 1.00 17.90 ? 111  ILE   B CG2  1 
ATOM   11116 C  CD1  . ILE   B 1 111 ? 37.382 4.624   67.658 1.00 19.10 ? 111  ILE   B CD1  1 
ATOM   11117 H  H    . ILE   B 1 111 ? 38.615 7.324   64.474 1.00 15.94 ? 111  ILE   B H    1 
ATOM   11118 H  HA   . ILE   B 1 111 ? 37.493 8.644   66.625 1.00 16.63 ? 111  ILE   B HA   1 
ATOM   11119 H  HB   . ILE   B 1 111 ? 39.177 6.408   66.799 1.00 22.44 ? 111  ILE   B HB   1 
ATOM   11120 H  HG12 . ILE   B 1 111 ? 36.407 6.380   67.282 1.00 20.81 ? 111  ILE   B HG12 1 
ATOM   11121 H  HG13 . ILE   B 1 111 ? 37.066 5.780   66.003 1.00 20.81 ? 111  ILE   B HG13 1 
ATOM   11122 H  HG21 . ILE   B 1 111 ? 38.718 6.441   69.100 1.00 21.49 ? 111  ILE   B HG21 1 
ATOM   11123 H  HG22 . ILE   B 1 111 ? 39.442 7.777   68.654 1.00 21.49 ? 111  ILE   B HG22 1 
ATOM   11124 H  HG23 . ILE   B 1 111 ? 37.878 7.769   68.905 1.00 21.49 ? 111  ILE   B HG23 1 
ATOM   11125 H  HD11 . ILE   B 1 111 ? 36.597 4.072   67.513 1.00 22.92 ? 111  ILE   B HD11 1 
ATOM   11126 H  HD12 . ILE   B 1 111 ? 38.165 4.170   67.309 1.00 22.92 ? 111  ILE   B HD12 1 
ATOM   11127 H  HD13 . ILE   B 1 111 ? 37.496 4.780   68.609 1.00 22.92 ? 111  ILE   B HD13 1 
ATOM   11128 N  N    . VAL   B 1 112 ? 39.367 10.304  66.675 1.00 15.65 ? 112  VAL   B N    1 
ATOM   11129 C  CA   . VAL   B 1 112 ? 40.541 11.218  66.777 1.00 16.65 ? 112  VAL   B CA   1 
ATOM   11130 C  C    . VAL   B 1 112 ? 40.976 11.289  68.243 1.00 16.41 ? 112  VAL   B C    1 
ATOM   11131 O  O    . VAL   B 1 112 ? 40.129 11.605  69.089 1.00 17.07 ? 112  VAL   B O    1 
ATOM   11132 C  CB   . VAL   B 1 112 ? 40.240 12.612  66.196 1.00 14.98 ? 112  VAL   B CB   1 
ATOM   11133 C  CG1  . VAL   B 1 112 ? 41.464 13.511  66.238 1.00 16.79 ? 112  VAL   B CG1  1 
ATOM   11134 C  CG2  . VAL   B 1 112 ? 39.693 12.514  64.780 1.00 16.22 ? 112  VAL   B CG2  1 
ATOM   11135 H  H    . VAL   B 1 112 ? 38.610 10.671  66.855 1.00 18.78 ? 112  VAL   B H    1 
ATOM   11136 H  HA   . VAL   B 1 112 ? 41.270 10.865  66.243 1.00 19.99 ? 112  VAL   B HA   1 
ATOM   11137 H  HB   . VAL   B 1 112 ? 39.557 13.014  66.756 1.00 17.98 ? 112  VAL   B HB   1 
ATOM   11138 H  HG11 . VAL   B 1 112 ? 41.241 14.379  65.866 1.00 20.15 ? 112  VAL   B HG11 1 
ATOM   11139 H  HG12 . VAL   B 1 112 ? 41.755 13.619  67.157 1.00 20.15 ? 112  VAL   B HG12 1 
ATOM   11140 H  HG13 . VAL   B 1 112 ? 42.178 13.110  65.718 1.00 20.15 ? 112  VAL   B HG13 1 
ATOM   11141 H  HG21 . VAL   B 1 112 ? 39.513 13.404  64.440 1.00 19.47 ? 112  VAL   B HG21 1 
ATOM   11142 H  HG22 . VAL   B 1 112 ? 40.345 12.077  64.210 1.00 19.47 ? 112  VAL   B HG22 1 
ATOM   11143 H  HG23 . VAL   B 1 112 ? 38.872 11.998  64.785 1.00 19.47 ? 112  VAL   B HG23 1 
ATOM   11144 N  N    . GLU   B 1 113 ? 42.257 11.027  68.507 1.00 18.43 ? 113  GLU   B N    1 
ATOM   11145 C  CA   . GLU   B 1 113 ? 42.745 10.969  69.907 1.00 17.25 ? 113  GLU   B CA   1 
ATOM   11146 C  C    . GLU   B 1 113 ? 43.813 12.021  70.195 1.00 18.14 ? 113  GLU   B C    1 
ATOM   11147 O  O    . GLU   B 1 113 ? 44.520 12.412  69.258 1.00 18.26 ? 113  GLU   B O    1 
ATOM   11148 C  CB   . GLU   B 1 113 ? 43.387 9.609   70.177 1.00 17.83 ? 113  GLU   B CB   1 
ATOM   11149 C  CG   . GLU   B 1 113 ? 42.463 8.431   69.947 1.00 19.33 ? 113  GLU   B CG   1 
ATOM   11150 C  CD   . GLU   B 1 113 ? 43.159 7.093   70.115 1.00 22.28 ? 113  GLU   B CD   1 
ATOM   11151 O  OE1  . GLU   B 1 113 ? 44.355 7.010   69.776 1.00 21.89 ? 113  GLU   B OE1  1 
ATOM   11152 O  OE2  . GLU   B 1 113 ? 42.508 6.145   70.582 1.00 20.03 ? 113  GLU   B OE2  1 
ATOM   11153 H  H    . GLU   B 1 113 ? 42.857 10.881  67.908 1.00 22.12 ? 113  GLU   B H    1 
ATOM   11154 H  HA   . GLU   B 1 113 ? 41.972 11.127  70.472 1.00 20.71 ? 113  GLU   B HA   1 
ATOM   11155 H  HB2  . GLU   B 1 113 ? 44.167 9.512   69.608 1.00 21.40 ? 113  GLU   B HB2  1 
ATOM   11156 H  HB3  . GLU   B 1 113 ? 43.701 9.587   71.095 1.00 21.40 ? 113  GLU   B HB3  1 
ATOM   11157 H  HG2  . GLU   B 1 113 ? 41.719 8.483   70.567 1.00 23.20 ? 113  GLU   B HG2  1 
ATOM   11158 H  HG3  . GLU   B 1 113 ? 42.091 8.487   69.053 1.00 23.20 ? 113  GLU   B HG3  1 
ATOM   11159 N  N    . ASP   B 1 114 ? 43.908 12.452  71.451 1.00 18.78 ? 114  ASP   B N    1 
ATOM   11160 C  CA   . ASP   B 1 114 ? 44.992 13.370  71.888 1.00 19.95 ? 114  ASP   B CA   1 
ATOM   11161 C  C    . ASP   B 1 114 ? 44.969 14.727  71.185 1.00 19.70 ? 114  ASP   B C    1 
ATOM   11162 O  O    . ASP   B 1 114 ? 43.886 15.171  70.786 1.00 16.58 ? 114  ASP   B O    1 
ATOM   11163 C  CB   . ASP   B 1 114 ? 46.363 12.692  71.783 1.00 19.89 ? 114  ASP   B CB   1 
ATOM   11164 C  CG   . ASP   B 1 114 ? 47.277 13.065  72.936 1.00 24.03 ? 114  ASP   B CG   1 
ATOM   11165 O  OD1  . ASP   B 1 114 ? 47.632 14.252  73.039 1.00 20.94 ? 114  ASP   B OD1  1 
ATOM   11166 O  OD2  . ASP   B 1 114 ? 47.615 12.166  73.728 1.00 25.48 ? 114  ASP   B OD2  1 
ATOM   11167 H  H    . ASP   B 1 114 ? 43.359 12.231  72.075 1.00 22.54 ? 114  ASP   B H    1 
ATOM   11168 H  HA   . ASP   B 1 114 ? 44.822 13.566  72.823 1.00 23.95 ? 114  ASP   B HA   1 
ATOM   11169 H  HB2  . ASP   B 1 114 ? 46.245 11.729  71.764 1.00 23.87 ? 114  ASP   B HB2  1 
ATOM   11170 H  HB3  . ASP   B 1 114 ? 46.783 12.943  70.945 1.00 23.87 ? 114  ASP   B HB3  1 
ATOM   11171 N  N    . LYS   B 1 115 ? 46.141 15.340  71.041 1.00 20.60 ? 115  LYS   B N    1 
ATOM   11172 C  CA   . LYS   B 1 115 ? 46.215 16.704  70.465 1.00 19.31 ? 115  LYS   B CA   1 
ATOM   11173 C  C    . LYS   B 1 115 ? 47.519 16.853  69.676 1.00 20.77 ? 115  LYS   B C    1 
ATOM   11174 O  O    . LYS   B 1 115 ? 48.540 16.315  70.129 1.00 19.47 ? 115  LYS   B O    1 
ATOM   11175 C  CB   . LYS   B 1 115 ? 46.151 17.751  71.580 1.00 19.31 ? 115  LYS   B CB   1 
ATOM   11176 C  CG   . LYS   B 1 115 ? 46.631 19.144  71.202 1.00 21.67 ? 115  LYS   B CG   1 
ATOM   11177 C  CD   . LYS   B 1 115 ? 46.668 20.089  72.380 1.00 23.71 ? 115  LYS   B CD   1 
ATOM   11178 C  CE   . LYS   B 1 115 ? 46.778 21.540  71.967 1.00 26.09 ? 115  LYS   B CE   1 
ATOM   11179 N  NZ   . LYS   B 1 115 ? 47.079 22.415  73.125 1.00 30.13 ? 115  LYS   B NZ   1 
ATOM   11180 H  H    . LYS   B 1 115 ? 46.899 14.999  71.263 1.00 24.72 ? 115  LYS   B H    1 
ATOM   11181 H  HA   . LYS   B 1 115 ? 45.462 16.842  69.869 1.00 23.18 ? 115  LYS   B HA   1 
ATOM   11182 H  HB2  . LYS   B 1 115 ? 45.234 17.815  71.889 1.00 23.17 ? 115  LYS   B HB2  1 
ATOM   11183 H  HB3  . LYS   B 1 115 ? 46.681 17.436  72.329 1.00 23.17 ? 115  LYS   B HB3  1 
ATOM   11184 H  HG2  . LYS   B 1 115 ? 47.518 19.082  70.814 1.00 26.00 ? 115  LYS   B HG2  1 
ATOM   11185 H  HG3  . LYS   B 1 115 ? 46.047 19.508  70.518 1.00 26.00 ? 115  LYS   B HG3  1 
ATOM   11186 H  HD2  . LYS   B 1 115 ? 45.865 19.969  72.911 1.00 28.45 ? 115  LYS   B HD2  1 
ATOM   11187 H  HD3  . LYS   B 1 115 ? 47.421 19.861  72.948 1.00 28.45 ? 115  LYS   B HD3  1 
ATOM   11188 H  HE2  . LYS   B 1 115 ? 47.475 21.635  71.299 1.00 31.31 ? 115  LYS   B HE2  1 
ATOM   11189 H  HE3  . LYS   B 1 115 ? 45.948 21.823  71.553 1.00 31.31 ? 115  LYS   B HE3  1 
ATOM   11190 H  HZ1  . LYS   B 1 115 ? 47.585 23.097  72.859 1.00 36.16 ? 115  LYS   B HZ1  1 
ATOM   11191 H  HZ2  . LYS   B 1 115 ? 46.319 22.726  73.467 1.00 36.16 ? 115  LYS   B HZ2  1 
ATOM   11192 H  HZ3  . LYS   B 1 115 ? 47.514 21.948  73.745 1.00 36.16 ? 115  LYS   B HZ3  1 
ATOM   11193 N  N    . ALA   B 1 116 ? 47.471 17.553  68.543 1.00 17.82 ? 116  ALA   B N    1 
ATOM   11194 C  CA   . ALA   B 1 116 ? 48.697 17.813  67.755 1.00 19.87 ? 116  ALA   B CA   1 
ATOM   11195 C  C    . ALA   B 1 116 ? 49.455 18.991  68.371 1.00 20.99 ? 116  ALA   B C    1 
ATOM   11196 O  O    . ALA   B 1 116 ? 48.812 19.895  68.916 1.00 19.56 ? 116  ALA   B O    1 
ATOM   11197 C  CB   . ALA   B 1 116 ? 48.338 18.101  66.324 1.00 21.52 ? 116  ALA   B CB   1 
ATOM   11198 H  H    . ALA   B 1 116 ? 46.752 17.886  68.209 1.00 21.39 ? 116  ALA   B H    1 
ATOM   11199 H  HA   . ALA   B 1 116 ? 49.268 17.029  67.772 1.00 23.85 ? 116  ALA   B HA   1 
ATOM   11200 H  HB1  . ALA   B 1 116 ? 49.146 18.270  65.815 1.00 25.83 ? 116  ALA   B HB1  1 
ATOM   11201 H  HB2  . ALA   B 1 116 ? 47.873 17.338  65.947 1.00 25.83 ? 116  ALA   B HB2  1 
ATOM   11202 H  HB3  . ALA   B 1 116 ? 47.763 18.881  66.285 1.00 25.83 ? 116  ALA   B HB3  1 
ATOM   11203 N  N    . ASP   B 1 117 ? 50.784 18.973  68.258 1.00 24.53 ? 117  ASP   B N    1 
ATOM   11204 C  CA   . ASP   B 1 117 ? 51.613 20.049  68.858 1.00 24.43 ? 117  ASP   B CA   1 
ATOM   11205 C  C    . ASP   B 1 117 ? 51.429 21.325  68.042 1.00 24.05 ? 117  ASP   B C    1 
ATOM   11206 O  O    . ASP   B 1 117 ? 51.990 22.354  68.434 1.00 28.59 ? 117  ASP   B O    1 
ATOM   11207 C  CB   . ASP   B 1 117 ? 53.077 19.615  68.945 1.00 29.16 ? 117  ASP   B CB   1 
ATOM   11208 C  CG   . ASP   B 1 117 ? 53.585 18.944  67.681 1.00 32.18 ? 117  ASP   B CG   1 
ATOM   11209 O  OD1  . ASP   B 1 117 ? 52.898 19.040  66.647 1.00 35.31 ? 117  ASP   B OD1  1 
ATOM   11210 O  OD2  . ASP   B 1 117 ? 54.665 18.331  67.744 1.00 45.23 ? 117  ASP   B OD2  1 
ATOM   11211 H  H    . ASP   B 1 117 ? 51.228 18.362  67.847 1.00 29.44 ? 117  ASP   B H    1 
ATOM   11212 H  HA   . ASP   B 1 117 ? 51.326 20.226  69.767 1.00 29.32 ? 117  ASP   B HA   1 
ATOM   11213 H  HB2  . ASP   B 1 117 ? 53.627 20.392  69.134 1.00 35.00 ? 117  ASP   B HB2  1 
ATOM   11214 H  HB3  . ASP   B 1 117 ? 53.182 19.005  69.692 1.00 35.00 ? 117  ASP   B HB3  1 
ATOM   11215 N  N    A SER   B 1 118 ? 50.885 21.192  66.829 0.37 22.35 ? 118  SER   B N    1 
ATOM   11216 N  N    B SER   B 1 118 ? 50.882 21.193  66.830 0.63 22.32 ? 118  SER   B N    1 
ATOM   11217 C  CA   A SER   B 1 118 ? 50.663 22.371  65.954 0.37 20.62 ? 118  SER   B CA   1 
ATOM   11218 C  CA   B SER   B 1 118 ? 50.658 22.373  65.958 0.63 20.62 ? 118  SER   B CA   1 
ATOM   11219 C  C    A SER   B 1 118 ? 49.399 22.142  65.120 0.37 20.76 ? 118  SER   B C    1 
ATOM   11220 C  C    B SER   B 1 118 ? 49.396 22.141  65.121 0.63 20.74 ? 118  SER   B C    1 
ATOM   11221 O  O    A SER   B 1 118 ? 49.019 20.976  64.916 0.37 21.50 ? 118  SER   B O    1 
ATOM   11222 O  O    B SER   B 1 118 ? 49.023 20.977  64.910 0.63 21.53 ? 118  SER   B O    1 
ATOM   11223 C  CB   A SER   B 1 118 ? 51.864 22.615  65.076 0.37 22.32 ? 118  SER   B CB   1 
ATOM   11224 C  CB   B SER   B 1 118 ? 51.859 22.624  65.081 0.63 22.24 ? 118  SER   B CB   1 
ATOM   11225 O  OG   A SER   B 1 118 ? 51.870 23.948  64.589 0.37 24.04 ? 118  SER   B OG   1 
ATOM   11226 O  OG   B SER   B 1 118 ? 52.144 21.479  64.294 0.63 22.17 ? 118  SER   B OG   1 
ATOM   11227 H  H    A SER   B 1 118 ? 50.637 20.442  66.490 0.37 26.83 ? 118  SER   B H    1 
ATOM   11228 H  H    B SER   B 1 118 ? 50.634 20.443  66.490 0.63 26.79 ? 118  SER   B H    1 
ATOM   11229 H  HA   A SER   B 1 118 ? 50.540 23.164  66.499 0.37 24.75 ? 118  SER   B HA   1 
ATOM   11230 H  HA   B SER   B 1 118 ? 50.533 23.164  66.506 0.63 24.75 ? 118  SER   B HA   1 
ATOM   11231 H  HB2  A SER   B 1 118 ? 52.677 22.446  65.578 0.37 26.78 ? 118  SER   B HB2  1 
ATOM   11232 H  HB2  B SER   B 1 118 ? 51.693 23.386  64.505 0.63 26.69 ? 118  SER   B HB2  1 
ATOM   11233 H  HB3  A SER   B 1 118 ? 51.857 21.994  64.331 0.37 26.78 ? 118  SER   B HB3  1 
ATOM   11234 H  HB3  B SER   B 1 118 ? 52.627 22.846  65.630 0.63 26.69 ? 118  SER   B HB3  1 
ATOM   11235 H  HG   A SER   B 1 118 ? 51.534 23.967  63.819 0.37 28.85 ? 118  SER   B HG   1 
ATOM   11236 H  HG   B SER   B 1 118 ? 51.933 21.628  63.495 0.63 26.61 ? 118  SER   B HG   1 
ATOM   11237 N  N    . PRO   B 1 119 ? 48.774 23.204  64.565 1.00 19.75 ? 119  PRO   B N    1 
ATOM   11238 C  CA   . PRO   B 1 119 ? 47.533 23.019  63.825 1.00 20.27 ? 119  PRO   B CA   1 
ATOM   11239 C  C    . PRO   B 1 119 ? 47.769 22.051  62.657 1.00 19.31 ? 119  PRO   B C    1 
ATOM   11240 O  O    . PRO   B 1 119 ? 48.732 22.217  61.936 1.00 17.72 ? 119  PRO   B O    1 
ATOM   11241 C  CB   . PRO   B 1 119 ? 47.210 24.434  63.335 1.00 20.87 ? 119  PRO   B CB   1 
ATOM   11242 C  CG   . PRO   B 1 119 ? 47.651 25.306  64.480 1.00 19.74 ? 119  PRO   B CG   1 
ATOM   11243 C  CD   . PRO   B 1 119 ? 48.799 24.558  65.128 1.00 23.28 ? 119  PRO   B CD   1 
ATOM   11244 H  HA   . PRO   B 1 119 ? 46.810 22.637  64.346 1.00 24.33 ? 119  PRO   B HA   1 
ATOM   11245 H  HB2  . PRO   B 1 119 ? 47.687 24.648  62.518 1.00 25.05 ? 119  PRO   B HB2  1 
ATOM   11246 H  HB3  . PRO   B 1 119 ? 46.264 24.541  63.147 1.00 25.05 ? 119  PRO   B HB3  1 
ATOM   11247 H  HG2  . PRO   B 1 119 ? 47.934 26.179  64.167 1.00 23.69 ? 119  PRO   B HG2  1 
ATOM   11248 H  HG3  . PRO   B 1 119 ? 46.927 25.451  65.109 1.00 23.69 ? 119  PRO   B HG3  1 
ATOM   11249 H  HD2  . PRO   B 1 119 ? 49.645 24.995  64.943 1.00 27.94 ? 119  PRO   B HD2  1 
ATOM   11250 H  HD3  . PRO   B 1 119 ? 48.697 24.534  66.092 1.00 27.94 ? 119  PRO   B HD3  1 
ATOM   11251 N  N    . VAL   B 1 120 ? 46.875 21.072  62.503 1.00 17.05 ? 120  VAL   B N    1 
ATOM   11252 C  CA   . VAL   B 1 120 ? 47.010 20.079  61.400 1.00 15.83 ? 120  VAL   B CA   1 
ATOM   11253 C  C    . VAL   B 1 120 ? 45.652 19.808  60.754 1.00 16.18 ? 120  VAL   B C    1 
ATOM   11254 O  O    . VAL   B 1 120 ? 44.624 20.209  61.329 1.00 16.07 ? 120  VAL   B O    1 
ATOM   11255 C  CB   . VAL   B 1 120 ? 47.600 18.752  61.911 1.00 18.59 ? 120  VAL   B CB   1 
ATOM   11256 C  CG1  . VAL   B 1 120 ? 49.018 18.922  62.430 1.00 19.30 ? 120  VAL   B CG1  1 
ATOM   11257 C  CG2  . VAL   B 1 120 ? 46.710 18.113  62.964 1.00 18.69 ? 120  VAL   B CG2  1 
ATOM   11258 H  H    . VAL   B 1 120 ? 46.190 20.956  63.011 1.00 20.47 ? 120  VAL   B H    1 
ATOM   11259 H  HA   . VAL   B 1 120 ? 47.614 20.457  60.742 1.00 19.00 ? 120  VAL   B HA   1 
ATOM   11260 H  HB   . VAL   B 1 120 ? 47.639 18.152  61.150 1.00 22.31 ? 120  VAL   B HB   1 
ATOM   11261 H  HG11 . VAL   B 1 120 ? 49.353 18.067  62.742 1.00 23.17 ? 120  VAL   B HG11 1 
ATOM   11262 H  HG12 . VAL   B 1 120 ? 49.587 19.251  61.716 1.00 23.17 ? 120  VAL   B HG12 1 
ATOM   11263 H  HG13 . VAL   B 1 120 ? 49.020 19.557  63.164 1.00 23.17 ? 120  VAL   B HG13 1 
ATOM   11264 H  HG21 . VAL   B 1 120 ? 47.109 17.281  63.264 1.00 22.43 ? 120  VAL   B HG21 1 
ATOM   11265 H  HG22 . VAL   B 1 120 ? 46.616 18.716  63.718 1.00 22.43 ? 120  VAL   B HG22 1 
ATOM   11266 H  HG23 . VAL   B 1 120 ? 45.836 17.933  62.583 1.00 22.43 ? 120  VAL   B HG23 1 
ATOM   11267 N  N    . TYR   B 1 121 ? 45.665 19.164  59.590 1.00 16.61 ? 121  TYR   B N    1 
ATOM   11268 C  CA   . TYR   B 1 121 ? 44.401 18.714  58.961 1.00 13.84 ? 121  TYR   B CA   1 
ATOM   11269 C  C    . TYR   B 1 121 ? 44.602 17.263  58.515 1.00 16.23 ? 121  TYR   B C    1 
ATOM   11270 O  O    . TYR   B 1 121 ? 45.756 16.859  58.293 1.00 17.11 ? 121  TYR   B O    1 
ATOM   11271 C  CB   . TYR   B 1 121 ? 43.954 19.643  57.827 1.00 13.93 ? 121  TYR   B CB   1 
ATOM   11272 C  CG   . TYR   B 1 121 ? 44.790 19.651  56.573 1.00 14.49 ? 121  TYR   B CG   1 
ATOM   11273 C  CD1  . TYR   B 1 121 ? 44.523 18.785  55.527 1.00 14.14 ? 121  TYR   B CD1  1 
ATOM   11274 C  CD2  . TYR   B 1 121 ? 45.811 20.570  56.408 1.00 16.58 ? 121  TYR   B CD2  1 
ATOM   11275 C  CE1  . TYR   B 1 121 ? 45.272 18.808  54.362 1.00 16.50 ? 121  TYR   B CE1  1 
ATOM   11276 C  CE2  . TYR   B 1 121 ? 46.568 20.609  55.250 1.00 18.64 ? 121  TYR   B CE2  1 
ATOM   11277 C  CZ   . TYR   B 1 121 ? 46.297 19.726  54.223 1.00 16.30 ? 121  TYR   B CZ   1 
ATOM   11278 O  OH   . TYR   B 1 121 ? 47.048 19.765  53.073 1.00 18.38 ? 121  TYR   B OH   1 
ATOM   11279 H  H    . TYR   B 1 121 ? 46.377 18.975  59.146 1.00 19.94 ? 121  TYR   B H    1 
ATOM   11280 H  HA   . TYR   B 1 121 ? 43.672 18.754  59.600 1.00 16.61 ? 121  TYR   B HA   1 
ATOM   11281 H  HB2  . TYR   B 1 121 ? 43.047 19.403  57.582 1.00 16.72 ? 121  TYR   B HB2  1 
ATOM   11282 H  HB3  . TYR   B 1 121 ? 43.924 20.548  58.174 1.00 16.72 ? 121  TYR   B HB3  1 
ATOM   11283 H  HD1  . TYR   B 1 121 ? 43.826 18.175  55.608 1.00 16.97 ? 121  TYR   B HD1  1 
ATOM   11284 H  HD2  . TYR   B 1 121 ? 45.993 21.175  57.090 1.00 19.90 ? 121  TYR   B HD2  1 
ATOM   11285 H  HE1  . TYR   B 1 121 ? 45.086 18.208  53.676 1.00 19.81 ? 121  TYR   B HE1  1 
ATOM   11286 H  HE2  . TYR   B 1 121 ? 47.257 21.228  55.164 1.00 22.37 ? 121  TYR   B HE2  1 
ATOM   11287 H  HH   . TYR   B 1 121 ? 46.701 19.264  52.495 1.00 22.06 ? 121  TYR   B HH   1 
ATOM   11288 N  N    . ILE   B 1 122 ? 43.515 16.509  58.434 1.00 16.42 ? 122  ILE   B N    1 
ATOM   11289 C  CA   . ILE   B 1 122 ? 43.590 15.091  57.993 1.00 13.05 ? 122  ILE   B CA   1 
ATOM   11290 C  C    . ILE   B 1 122 ? 43.088 15.029  56.552 1.00 14.30 ? 122  ILE   B C    1 
ATOM   11291 O  O    . ILE   B 1 122 ? 42.045 15.644  56.271 1.00 14.05 ? 122  ILE   B O    1 
ATOM   11292 C  CB   . ILE   B 1 122 ? 42.766 14.186  58.929 1.00 12.91 ? 122  ILE   B CB   1 
ATOM   11293 C  CG1  . ILE   B 1 122 ? 43.281 14.258  60.368 1.00 14.69 ? 122  ILE   B CG1  1 
ATOM   11294 C  CG2  . ILE   B 1 122 ? 42.732 12.758  58.411 1.00 13.42 ? 122  ILE   B CG2  1 
ATOM   11295 C  CD1  . ILE   B 1 122 ? 42.336 13.677  61.390 1.00 14.57 ? 122  ILE   B CD1  1 
ATOM   11296 H  H    . ILE   B 1 122 ? 42.722 16.783  58.625 1.00 19.71 ? 122  ILE   B H    1 
ATOM   11297 H  HA   . ILE   B 1 122 ? 44.503 14.766  58.032 1.00 15.66 ? 122  ILE   B HA   1 
ATOM   11298 H  HB   . ILE   B 1 122 ? 41.853 14.514  58.938 1.00 15.50 ? 122  ILE   B HB   1 
ATOM   11299 H  HG12 . ILE   B 1 122 ? 44.128 13.789  60.422 1.00 17.63 ? 122  ILE   B HG12 1 
ATOM   11300 H  HG13 . ILE   B 1 122 ? 43.455 15.185  60.593 1.00 17.63 ? 122  ILE   B HG13 1 
ATOM   11301 H  HG21 . ILE   B 1 122 ? 42.209 12.207  59.014 1.00 16.11 ? 122  ILE   B HG21 1 
ATOM   11302 H  HG22 . ILE   B 1 122 ? 42.329 12.743  57.529 1.00 16.11 ? 122  ILE   B HG22 1 
ATOM   11303 H  HG23 . ILE   B 1 122 ? 43.636 12.411  58.359 1.00 16.11 ? 122  ILE   B HG23 1 
ATOM   11304 H  HD11 . ILE   B 1 122 ? 42.726 13.757  62.274 1.00 17.49 ? 122  ILE   B HD11 1 
ATOM   11305 H  HD12 . ILE   B 1 122 ? 41.495 14.159  61.364 1.00 17.49 ? 122  ILE   B HD12 1 
ATOM   11306 H  HD13 . ILE   B 1 122 ? 42.178 12.741  61.190 1.00 17.49 ? 122  ILE   B HD13 1 
ATOM   11307 N  N    . GLU   B 1 123 ? 43.815 14.316  55.692 1.00 14.04 ? 123  GLU   B N    1 
ATOM   11308 C  CA   . GLU   B 1 123 ? 43.444 14.208  54.262 1.00 14.25 ? 123  GLU   B CA   1 
ATOM   11309 C  C    . GLU   B 1 123 ? 43.186 12.737  53.937 1.00 14.39 ? 123  GLU   B C    1 
ATOM   11310 O  O    . GLU   B 1 123 ? 44.124 11.939  54.053 1.00 15.63 ? 123  GLU   B O    1 
ATOM   11311 C  CB   . GLU   B 1 123 ? 44.559 14.795  53.398 1.00 17.63 ? 123  GLU   B CB   1 
ATOM   11312 C  CG   . GLU   B 1 123 ? 44.319 14.633  51.909 1.00 16.63 ? 123  GLU   B CG   1 
ATOM   11313 C  CD   . GLU   B 1 123 ? 45.333 15.352  51.037 1.00 21.75 ? 123  GLU   B CD   1 
ATOM   11314 O  OE1  . GLU   B 1 123 ? 46.212 16.030  51.593 1.00 21.05 ? 123  GLU   B OE1  1 
ATOM   11315 O  OE2  . GLU   B 1 123 ? 45.235 15.231  49.805 1.00 23.01 ? 123  GLU   B OE2  1 
ATOM   11316 H  H    . GLU   B 1 123 ? 44.527 13.885  55.908 1.00 16.86 ? 123  GLU   B H    1 
ATOM   11317 H  HA   . GLU   B 1 123 ? 42.636 14.711  54.076 1.00 17.11 ? 123  GLU   B HA   1 
ATOM   11318 H  HB2  . GLU   B 1 123 ? 44.654 15.738  53.602 1.00 21.16 ? 123  GLU   B HB2  1 
ATOM   11319 H  HB3  . GLU   B 1 123 ? 45.398 14.368  53.631 1.00 21.16 ? 123  GLU   B HB3  1 
ATOM   11320 H  HG2  . GLU   B 1 123 ? 44.330 13.688  51.690 1.00 19.96 ? 123  GLU   B HG2  1 
ATOM   11321 H  HG3  . GLU   B 1 123 ? 43.432 14.963  51.696 1.00 19.96 ? 123  GLU   B HG3  1 
ATOM   11322 N  N    . ILE   B 1 124 ? 41.960 12.413  53.540 1.00 16.09 ? 124  ILE   B N    1 
ATOM   11323 C  CA   . ILE   B 1 124 ? 41.600 10.992  53.285 1.00 16.13 ? 124  ILE   B CA   1 
ATOM   11324 C  C    . ILE   B 1 124 ? 41.169 10.788  51.834 1.00 14.80 ? 124  ILE   B C    1 
ATOM   11325 O  O    . ILE   B 1 124 ? 40.288 11.531  51.368 1.00 13.74 ? 124  ILE   B O    1 
ATOM   11326 C  CB   . ILE   B 1 124 ? 40.473 10.520  54.226 1.00 15.85 ? 124  ILE   B CB   1 
ATOM   11327 C  CG1  . ILE   B 1 124 ? 40.826 10.733  55.699 1.00 14.66 ? 124  ILE   B CG1  1 
ATOM   11328 C  CG2  . ILE   B 1 124 ? 40.104 9.074   53.935 1.00 15.76 ? 124  ILE   B CG2  1 
ATOM   11329 C  CD1  . ILE   B 1 124 ? 39.628 10.690  56.615 1.00 16.74 ? 124  ILE   B CD1  1 
ATOM   11330 H  H    . ILE   B 1 124 ? 41.324 12.977  53.411 1.00 19.31 ? 124  ILE   B H    1 
ATOM   11331 H  HA   . ILE   B 1 124 ? 42.393 10.462  53.458 1.00 19.36 ? 124  ILE   B HA   1 
ATOM   11332 H  HB   . ILE   B 1 124 ? 39.693 11.069  54.051 1.00 19.03 ? 124  ILE   B HB   1 
ATOM   11333 H  HG12 . ILE   B 1 124 ? 41.460 10.052  55.974 1.00 17.60 ? 124  ILE   B HG12 1 
ATOM   11334 H  HG13 . ILE   B 1 124 ? 41.269 11.590  55.798 1.00 17.60 ? 124  ILE   B HG13 1 
ATOM   11335 H  HG21 . ILE   B 1 124 ? 39.395 8.794   54.535 1.00 18.92 ? 124  ILE   B HG21 1 
ATOM   11336 H  HG22 . ILE   B 1 124 ? 39.800 8.996   53.017 1.00 18.92 ? 124  ILE   B HG22 1 
ATOM   11337 H  HG23 . ILE   B 1 124 ? 40.881 8.509   54.067 1.00 18.92 ? 124  ILE   B HG23 1 
ATOM   11338 H  HD11 . ILE   B 1 124 ? 39.915 10.831  57.531 1.00 20.09 ? 124  ILE   B HD11 1 
ATOM   11339 H  HD12 . ILE   B 1 124 ? 39.002 11.387  56.362 1.00 20.09 ? 124  ILE   B HD12 1 
ATOM   11340 H  HD13 . ILE   B 1 124 ? 39.195 9.825   56.542 1.00 20.09 ? 124  ILE   B HD13 1 
ATOM   11341 N  N    . VAL   B 1 125 ? 41.798 9.837   51.148 1.00 14.56 ? 125  VAL   B N    1 
ATOM   11342 C  CA   . VAL   B 1 125 ? 41.317 9.436   49.798 1.00 17.03 ? 125  VAL   B CA   1 
ATOM   11343 C  C    . VAL   B 1 125 ? 41.190 7.917   49.892 1.00 17.44 ? 125  VAL   B C    1 
ATOM   11344 O  O    . VAL   B 1 125 ? 42.236 7.252   49.902 1.00 17.76 ? 125  VAL   B O    1 
ATOM   11345 C  CB   . VAL   B 1 125 ? 42.245 9.864   48.648 1.00 19.44 ? 125  VAL   B CB   1 
ATOM   11346 C  CG1  . VAL   B 1 125 ? 41.669 9.446   47.304 1.00 20.05 ? 125  VAL   B CG1  1 
ATOM   11347 C  CG2  . VAL   B 1 125 ? 42.507 11.360  48.667 1.00 20.48 ? 125  VAL   B CG2  1 
ATOM   11348 H  H    . VAL   B 1 125 ? 42.491 9.412   51.427 1.00 17.48 ? 125  VAL   B H    1 
ATOM   11349 H  HA   . VAL   B 1 125 ? 40.482 9.879   49.579 1.00 20.44 ? 125  VAL   B HA   1 
ATOM   11350 H  HB   . VAL   B 1 125 ? 43.093 9.411   48.778 1.00 23.33 ? 125  VAL   B HB   1 
ATOM   11351 H  HG11 . VAL   B 1 125 ? 42.268 9.725   46.594 1.00 24.06 ? 125  VAL   B HG11 1 
ATOM   11352 H  HG12 . VAL   B 1 125 ? 41.568 8.482   47.281 1.00 24.06 ? 125  VAL   B HG12 1 
ATOM   11353 H  HG13 . VAL   B 1 125 ? 40.803 9.865   47.179 1.00 24.06 ? 125  VAL   B HG13 1 
ATOM   11354 H  HG21 . VAL   B 1 125 ? 43.094 11.595  47.931 1.00 24.58 ? 125  VAL   B HG21 1 
ATOM   11355 H  HG22 . VAL   B 1 125 ? 41.667 11.837  48.576 1.00 24.58 ? 125  VAL   B HG22 1 
ATOM   11356 H  HG23 . VAL   B 1 125 ? 42.928 11.604  49.506 1.00 24.58 ? 125  VAL   B HG23 1 
ATOM   11357 N  N    . ASP   B 1 126 ? 39.967 7.411   50.029 1.00 15.75 ? 126  ASP   B N    1 
ATOM   11358 C  CA   . ASP   B 1 126 ? 39.771 5.954   50.252 1.00 18.65 ? 126  ASP   B CA   1 
ATOM   11359 C  C    . ASP   B 1 126 ? 40.617 5.521   51.456 1.00 18.27 ? 126  ASP   B C    1 
ATOM   11360 O  O    . ASP   B 1 126 ? 40.409 6.078   52.540 1.00 16.48 ? 126  ASP   B O    1 
ATOM   11361 C  CB   . ASP   B 1 126 ? 40.047 5.155   48.977 1.00 21.53 ? 126  ASP   B CB   1 
ATOM   11362 C  CG   . ASP   B 1 126 ? 39.034 5.449   47.885 1.00 23.02 ? 126  ASP   B CG   1 
ATOM   11363 O  OD1  . ASP   B 1 126 ? 37.829 5.455   48.193 1.00 18.61 ? 126  ASP   B OD1  1 
ATOM   11364 O  OD2  . ASP   B 1 126 ? 39.459 5.679   46.739 1.00 23.07 ? 126  ASP   B OD2  1 
ATOM   11365 H  H    . ASP   B 1 126 ? 39.243 7.873   49.999 1.00 18.91 ? 126  ASP   B H    1 
ATOM   11366 H  HA   . ASP   B 1 126 ? 38.844 5.766   50.465 1.00 22.38 ? 126  ASP   B HA   1 
ATOM   11367 H  HB2  . ASP   B 1 126 ? 40.938 5.362   48.654 1.00 25.84 ? 126  ASP   B HB2  1 
ATOM   11368 H  HB3  . ASP   B 1 126 ? 40.033 4.207   49.182 1.00 25.84 ? 126  ASP   B HB3  1 
ATOM   11369 N  N    . ASP   B 1 127 ? 41.557 4.593   51.263 1.00 19.21 ? 127  ASP   B N    1 
ATOM   11370 C  CA   . ASP   B 1 127 ? 42.336 4.050   52.409 1.00 19.78 ? 127  ASP   B CA   1 
ATOM   11371 C  C    . ASP   B 1 127 ? 43.616 4.850   52.668 1.00 19.66 ? 127  ASP   B C    1 
ATOM   11372 O  O    . ASP   B 1 127 ? 44.295 4.546   53.655 1.00 23.52 ? 127  ASP   B O    1 
ATOM   11373 C  CB   . ASP   B 1 127 ? 42.683 2.578   52.180 1.00 20.96 ? 127  ASP   B CB   1 
ATOM   11374 C  CG   . ASP   B 1 127 ? 43.529 2.358   50.939 1.00 25.58 ? 127  ASP   B CG   1 
ATOM   11375 O  OD1  . ASP   B 1 127 ? 43.222 2.977   49.904 1.00 27.50 ? 127  ASP   B OD1  1 
ATOM   11376 O  OD2  . ASP   B 1 127 ? 44.486 1.570   51.021 1.00 31.49 ? 127  ASP   B OD2  1 
ATOM   11377 H  H    . ASP   B 1 127 ? 41.764 4.263   50.496 1.00 23.05 ? 127  ASP   B H    1 
ATOM   11378 H  HA   . ASP   B 1 127 ? 41.772 4.129   53.194 1.00 23.74 ? 127  ASP   B HA   1 
ATOM   11379 H  HB2  . ASP   B 1 127 ? 43.158 2.238   52.954 1.00 25.16 ? 127  ASP   B HB2  1 
ATOM   11380 H  HB3  . ASP   B 1 127 ? 41.863 2.065   52.102 1.00 25.16 ? 127  ASP   B HB3  1 
ATOM   11381 N  N    . LYS   B 1 128 ? 43.927 5.836   51.825 1.00 18.70 ? 128  LYS   B N    1 
ATOM   11382 C  CA   . LYS   B 1 128 ? 45.120 6.686   52.069 1.00 18.77 ? 128  LYS   B CA   1 
ATOM   11383 C  C    . LYS   B 1 128 ? 44.751 7.807   53.047 1.00 20.69 ? 128  LYS   B C    1 
ATOM   11384 O  O    . LYS   B 1 128 ? 43.835 8.581   52.736 1.00 15.45 ? 128  LYS   B O    1 
ATOM   11385 C  CB   . LYS   B 1 128 ? 45.681 7.252   50.762 1.00 22.55 ? 128  LYS   B CB   1 
ATOM   11386 C  CG   . LYS   B 1 128 ? 46.967 8.051   50.919 1.00 28.40 ? 128  LYS   B CG   1 
ATOM   11387 C  CD   . LYS   B 1 128 ? 47.342 8.844   49.688 1.00 37.64 ? 128  LYS   B CD   1 
ATOM   11388 C  CE   . LYS   B 1 128 ? 48.723 9.457   49.784 1.00 41.36 ? 128  LYS   B CE   1 
ATOM   11389 N  NZ   . LYS   B 1 128 ? 49.161 10.033  48.491 1.00 44.34 ? 128  LYS   B NZ   1 
ATOM   11390 H  H    . LYS   B 1 128 ? 43.478 6.034   51.119 1.00 22.45 ? 128  LYS   B H    1 
ATOM   11391 H  HA   . LYS   B 1 128 ? 45.819 6.140   52.461 1.00 22.52 ? 128  LYS   B HA   1 
ATOM   11392 H  HB2  . LYS   B 1 128 ? 45.843 6.518   50.148 1.00 27.07 ? 128  LYS   B HB2  1 
ATOM   11393 H  HB3  . LYS   B 1 128 ? 45.009 7.820   50.354 1.00 27.07 ? 128  LYS   B HB3  1 
ATOM   11394 H  HG2  . LYS   B 1 128 ? 46.872 8.659   51.669 1.00 34.09 ? 128  LYS   B HG2  1 
ATOM   11395 H  HG3  . LYS   B 1 128 ? 47.692 7.444   51.136 1.00 34.09 ? 128  LYS   B HG3  1 
ATOM   11396 H  HD2  . LYS   B 1 128 ? 47.303 8.265   48.911 1.00 45.17 ? 128  LYS   B HD2  1 
ATOM   11397 H  HD3  . LYS   B 1 128 ? 46.689 9.548   49.550 1.00 45.17 ? 128  LYS   B HD3  1 
ATOM   11398 H  HE2  . LYS   B 1 128 ? 48.723 10.150  50.463 1.00 49.64 ? 128  LYS   B HE2  1 
ATOM   11399 H  HE3  . LYS   B 1 128 ? 49.358 8.781   50.068 1.00 49.64 ? 128  LYS   B HE3  1 
ATOM   11400 H  HZ1  . LYS   B 1 128 ? 49.974 10.384  48.582 1.00 53.21 ? 128  LYS   B HZ1  1 
ATOM   11401 H  HZ2  . LYS   B 1 128 ? 49.182 9.393   47.873 1.00 53.21 ? 128  LYS   B HZ2  1 
ATOM   11402 H  HZ3  . LYS   B 1 128 ? 48.591 10.668  48.240 1.00 53.21 ? 128  LYS   B HZ3  1 
ATOM   11403 N  N    . VAL   B 1 129 ? 45.453 7.870   54.180 1.00 19.31 ? 129  VAL   B N    1 
ATOM   11404 C  CA   . VAL   B 1 129 ? 45.155 8.899   55.213 1.00 17.33 ? 129  VAL   B CA   1 
ATOM   11405 C  C    . VAL   B 1 129 ? 46.470 9.576   55.594 1.00 17.88 ? 129  VAL   B C    1 
ATOM   11406 O  O    . VAL   B 1 129 ? 47.461 8.860   55.812 1.00 18.32 ? 129  VAL   B O    1 
ATOM   11407 C  CB   . VAL   B 1 129 ? 44.455 8.272   56.436 1.00 17.31 ? 129  VAL   B CB   1 
ATOM   11408 C  CG1  . VAL   B 1 129 ? 44.093 9.318   57.477 1.00 18.76 ? 129  VAL   B CG1  1 
ATOM   11409 C  CG2  . VAL   B 1 129 ? 43.232 7.462   56.034 1.00 14.95 ? 129  VAL   B CG2  1 
ATOM   11410 H  H    . VAL   B 1 129 ? 46.100 7.339   54.379 1.00 23.18 ? 129  VAL   B H    1 
ATOM   11411 H  HA   . VAL   B 1 129 ? 44.540 9.562   54.861 1.00 20.80 ? 129  VAL   B HA   1 
ATOM   11412 H  HB   . VAL   B 1 129 ? 45.093 7.663   56.839 1.00 20.78 ? 129  VAL   B HB   1 
ATOM   11413 H  HG11 . VAL   B 1 129 ? 43.656 8.889   58.229 1.00 22.51 ? 129  VAL   B HG11 1 
ATOM   11414 H  HG12 . VAL   B 1 129 ? 44.899 9.763   57.783 1.00 22.51 ? 129  VAL   B HG12 1 
ATOM   11415 H  HG13 . VAL   B 1 129 ? 43.493 9.971   57.085 1.00 22.51 ? 129  VAL   B HG13 1 
ATOM   11416 H  HG21 . VAL   B 1 129 ? 42.819 7.084   56.826 1.00 17.94 ? 129  VAL   B HG21 1 
ATOM   11417 H  HG22 . VAL   B 1 129 ? 42.596 8.038   55.582 1.00 17.94 ? 129  VAL   B HG22 1 
ATOM   11418 H  HG23 . VAL   B 1 129 ? 43.500 6.746   55.437 1.00 17.94 ? 129  VAL   B HG23 1 
ATOM   11419 N  N    . GLU   B 1 130 ? 46.473 10.906  55.643 1.00 17.02 ? 130  GLU   B N    1 
ATOM   11420 C  CA   . GLU   B 1 130 ? 47.712 11.651  55.975 1.00 17.47 ? 130  GLU   B CA   1 
ATOM   11421 C  C    . GLU   B 1 130 ? 47.419 12.804  56.934 1.00 18.20 ? 130  GLU   B C    1 
ATOM   11422 O  O    . GLU   B 1 130 ? 46.310 13.356  56.871 1.00 18.92 ? 130  GLU   B O    1 
ATOM   11423 C  CB   . GLU   B 1 130 ? 48.358 12.238  54.721 1.00 20.29 ? 130  GLU   B CB   1 
ATOM   11424 C  CG   . GLU   B 1 130 ? 48.509 11.254  53.580 1.00 23.48 ? 130  GLU   B CG   1 
ATOM   11425 C  CD   . GLU   B 1 130 ? 48.837 11.936  52.264 1.00 31.95 ? 130  GLU   B CD   1 
ATOM   11426 O  OE1  . GLU   B 1 130 ? 47.892 12.341  51.561 1.00 32.45 ? 130  GLU   B OE1  1 
ATOM   11427 O  OE2  . GLU   B 1 130 ? 50.034 12.078  51.959 1.00 33.39 ? 130  GLU   B OE2  1 
ATOM   11428 H  H    . GLU   B 1 130 ? 45.785 11.399  55.492 1.00 20.42 ? 130  GLU   B H    1 
ATOM   11429 H  HA   . GLU   B 1 130 ? 48.315 11.016  56.391 1.00 20.97 ? 130  GLU   B HA   1 
ATOM   11430 H  HB2  . GLU   B 1 130 ? 47.826 12.990  54.417 1.00 24.35 ? 130  GLU   B HB2  1 
ATOM   11431 H  HB3  . GLU   B 1 130 ? 49.234 12.585  54.953 1.00 24.35 ? 130  GLU   B HB3  1 
ATOM   11432 H  HG2  . GLU   B 1 130 ? 49.210 10.619  53.795 1.00 28.19 ? 130  GLU   B HG2  1 
ATOM   11433 H  HG3  . GLU   B 1 130 ? 47.687 10.748  53.483 1.00 28.19 ? 130  GLU   B HG3  1 
ATOM   11434 N  N    . ILE   B 1 131 ? 48.393 13.146  57.776 1.00 19.27 ? 131  ILE   B N    1 
ATOM   11435 C  CA   . ILE   B 1 131 ? 48.245 14.324  58.674 1.00 18.16 ? 131  ILE   B CA   1 
ATOM   11436 C  C    . ILE   B 1 131 ? 49.158 15.417  58.121 1.00 18.33 ? 131  ILE   B C    1 
ATOM   11437 O  O    . ILE   B 1 131 ? 50.353 15.136  57.935 1.00 18.80 ? 131  ILE   B O    1 
ATOM   11438 C  CB   . ILE   B 1 131 ? 48.578 13.957  60.130 1.00 18.72 ? 131  ILE   B CB   1 
ATOM   11439 C  CG1  . ILE   B 1 131 ? 47.718 12.791  60.625 1.00 18.85 ? 131  ILE   B CG1  1 
ATOM   11440 C  CG2  . ILE   B 1 131 ? 48.458 15.176  61.032 1.00 19.18 ? 131  ILE   B CG2  1 
ATOM   11441 C  CD1  . ILE   B 1 131 ? 48.293 12.070  61.820 1.00 21.69 ? 131  ILE   B CD1  1 
ATOM   11442 H  H    . ILE   B 1 131 ? 49.139 12.726  57.852 1.00 23.13 ? 131  ILE   B H    1 
ATOM   11443 H  HA   . ILE   B 1 131 ? 47.328 14.640  58.693 1.00 21.80 ? 131  ILE   B HA   1 
ATOM   11444 H  HB   . ILE   B 1 131 ? 49.500 13.657  60.163 1.00 22.47 ? 131  ILE   B HB   1 
ATOM   11445 H  HG12 . ILE   B 1 131 ? 46.837 13.125  60.854 1.00 22.63 ? 131  ILE   B HG12 1 
ATOM   11446 H  HG13 . ILE   B 1 131 ? 47.602 12.156  59.901 1.00 22.63 ? 131  ILE   B HG13 1 
ATOM   11447 H  HG21 . ILE   B 1 131 ? 48.671 14.926  61.945 1.00 23.02 ? 131  ILE   B HG21 1 
ATOM   11448 H  HG22 . ILE   B 1 131 ? 49.075 15.862  60.733 1.00 23.02 ? 131  ILE   B HG22 1 
ATOM   11449 H  HG23 . ILE   B 1 131 ? 47.551 15.518  60.995 1.00 23.02 ? 131  ILE   B HG23 1 
ATOM   11450 H  HD11 . ILE   B 1 131 ? 47.700 11.347  62.078 1.00 26.03 ? 131  ILE   B HD11 1 
ATOM   11451 H  HD12 . ILE   B 1 131 ? 49.163 11.707  61.592 1.00 26.03 ? 131  ILE   B HD12 1 
ATOM   11452 H  HD13 . ILE   B 1 131 ? 48.386 12.691  62.559 1.00 26.03 ? 131  ILE   B HD13 1 
ATOM   11453 N  N    . LYS   B 1 132 ? 48.613 16.606  57.855 1.00 19.97 ? 132  LYS   B N    1 
ATOM   11454 C  CA   . LYS   B 1 132 ? 49.426 17.658  57.192 1.00 22.81 ? 132  LYS   B CA   1 
ATOM   11455 C  C    . LYS   B 1 132 ? 49.394 18.979  57.968 1.00 19.02 ? 132  LYS   B C    1 
ATOM   11456 O  O    . LYS   B 1 132 ? 48.426 19.205  58.712 1.00 18.71 ? 132  LYS   B O    1 
ATOM   11457 C  CB   . LYS   B 1 132 ? 48.913 17.870  55.767 1.00 21.40 ? 132  LYS   B CB   1 
ATOM   11458 C  CG   . LYS   B 1 132 ? 48.915 16.619  54.897 1.00 22.34 ? 132  LYS   B CG   1 
ATOM   11459 C  CD   . LYS   B 1 132 ? 48.898 16.898  53.411 1.00 23.78 ? 132  LYS   B CD   1 
ATOM   11460 C  CE   . LYS   B 1 132 ? 49.289 15.692  52.583 1.00 28.58 ? 132  LYS   B CE   1 
ATOM   11461 N  NZ   . LYS   B 1 132 ? 49.005 15.893  51.142 1.00 28.50 ? 132  LYS   B NZ   1 
ATOM   11462 H  H    . LYS   B 1 132 ? 47.803 16.829  58.039 1.00 23.97 ? 132  LYS   B H    1 
ATOM   11463 H  HA   . LYS   B 1 132 ? 50.349 17.359  57.171 1.00 27.37 ? 132  LYS   B HA   1 
ATOM   11464 H  HB2  . LYS   B 1 132 ? 48.008 18.218  55.810 1.00 25.68 ? 132  LYS   B HB2  1 
ATOM   11465 H  HB3  . LYS   B 1 132 ? 49.457 18.548  55.338 1.00 25.68 ? 132  LYS   B HB3  1 
ATOM   11466 H  HG2  . LYS   B 1 132 ? 49.701 16.092  55.108 1.00 26.81 ? 132  LYS   B HG2  1 
ATOM   11467 H  HG3  . LYS   B 1 132 ? 48.142 16.079  55.123 1.00 26.81 ? 132  LYS   B HG3  1 
ATOM   11468 H  HD2  . LYS   B 1 132 ? 48.010 17.189  53.151 1.00 28.55 ? 132  LYS   B HD2  1 
ATOM   11469 H  HD3  . LYS   B 1 132 ? 49.505 17.629  53.216 1.00 28.55 ? 132  LYS   B HD3  1 
ATOM   11470 H  HE2  . LYS   B 1 132 ? 50.234 15.511  52.703 1.00 34.30 ? 132  LYS   B HE2  1 
ATOM   11471 H  HE3  . LYS   B 1 132 ? 48.808 14.912  52.901 1.00 34.30 ? 132  LYS   B HE3  1 
ATOM   11472 H  HZ1  . LYS   B 1 132 ? 49.325 15.205  50.677 1.00 34.20 ? 132  LYS   B HZ1  1 
ATOM   11473 H  HZ2  . LYS   B 1 132 ? 48.126 15.951  51.018 1.00 34.20 ? 132  LYS   B HZ2  1 
ATOM   11474 H  HZ3  . LYS   B 1 132 ? 49.394 16.644  50.865 1.00 34.20 ? 132  LYS   B HZ3  1 
ATOM   11475 N  N    . ASP   B 1 133 ? 50.413 19.815  57.772 1.00 19.12 ? 133  ASP   B N    1 
ATOM   11476 C  CA   . ASP   B 1 133 ? 50.501 21.131  58.455 1.00 20.23 ? 133  ASP   B CA   1 
ATOM   11477 C  C    . ASP   B 1 133 ? 49.345 22.039  58.019 1.00 20.99 ? 133  ASP   B C    1 
ATOM   11478 O  O    . ASP   B 1 133 ? 49.149 22.202  56.808 1.00 18.23 ? 133  ASP   B O    1 
ATOM   11479 C  CB   . ASP   B 1 133 ? 51.857 21.787  58.183 1.00 25.80 ? 133  ASP   B CB   1 
ATOM   11480 C  CG   . ASP   B 1 133 ? 51.972 23.199  58.726 1.00 30.67 ? 133  ASP   B CG   1 
ATOM   11481 O  OD1  . ASP   B 1 133 ? 51.249 23.517  59.682 1.00 30.44 ? 133  ASP   B OD1  1 
ATOM   11482 O  OD2  . ASP   B 1 133 ? 52.790 23.965  58.189 1.00 42.79 ? 133  ASP   B OD2  1 
ATOM   11483 H  H    . ASP   B 1 133 ? 51.073 19.647  57.246 1.00 22.95 ? 133  ASP   B H    1 
ATOM   11484 H  HA   . ASP   B 1 133 ? 50.426 20.991  59.412 1.00 24.28 ? 133  ASP   B HA   1 
ATOM   11485 H  HB2  . ASP   B 1 133 ? 52.556 21.240  58.575 1.00 30.96 ? 133  ASP   B HB2  1 
ATOM   11486 H  HB3  . ASP   B 1 133 ? 52.013 21.804  57.226 1.00 30.96 ? 133  ASP   B HB3  1 
ATOM   11487 N  N    . ALA   B 1 134 ? 48.641 22.626  58.990 1.00 17.65 ? 134  ALA   B N    1 
ATOM   11488 C  CA   . ALA   B 1 134 ? 47.489 23.504  58.676 1.00 18.17 ? 134  ALA   B CA   1 
ATOM   11489 C  C    . ALA   B 1 134 ? 47.808 24.971  58.996 1.00 20.65 ? 134  ALA   B C    1 
ATOM   11490 O  O    . ALA   B 1 134 ? 46.862 25.767  59.086 1.00 18.69 ? 134  ALA   B O    1 
ATOM   11491 C  CB   . ALA   B 1 134 ? 46.276 23.027  59.439 1.00 16.85 ? 134  ALA   B CB   1 
ATOM   11492 H  H    . ALA   B 1 134 ? 48.805 22.535  59.829 1.00 21.18 ? 134  ALA   B H    1 
ATOM   11493 H  HA   . ALA   B 1 134 ? 47.302 23.455  57.725 1.00 21.81 ? 134  ALA   B HA   1 
ATOM   11494 H  HB1  . ALA   B 1 134 ? 45.520 23.600  59.236 1.00 20.23 ? 134  ALA   B HB1  1 
ATOM   11495 H  HB2  . ALA   B 1 134 ? 46.069 22.115  59.181 1.00 20.23 ? 134  ALA   B HB2  1 
ATOM   11496 H  HB3  . ALA   B 1 134 ? 46.459 23.059  60.391 1.00 20.23 ? 134  ALA   B HB3  1 
ATOM   11497 N  N    . SER   B 1 135 ? 49.092 25.318  59.120 1.00 18.73 ? 135  SER   B N    1 
ATOM   11498 C  CA   . SER   B 1 135 ? 49.477 26.698  59.513 1.00 24.38 ? 135  SER   B CA   1 
ATOM   11499 C  C    . SER   B 1 135 ? 48.932 27.731  58.519 1.00 21.80 ? 135  SER   B C    1 
ATOM   11500 O  O    . SER   B 1 135 ? 48.659 28.860  58.943 1.00 23.11 ? 135  SER   B O    1 
ATOM   11501 C  CB   . SER   B 1 135 ? 50.973 26.811  59.636 1.00 25.97 ? 135  SER   B CB   1 
ATOM   11502 O  OG   . SER   B 1 135 ? 51.589 26.648  58.369 1.00 30.15 ? 135  SER   B OG   1 
ATOM   11503 H  H    . SER   B 1 135 ? 49.753 24.785  58.985 1.00 22.48 ? 135  SER   B H    1 
ATOM   11504 H  HA   . SER   B 1 135 ? 49.082 26.886  60.379 1.00 29.27 ? 135  SER   B HA   1 
ATOM   11505 H  HB2  . SER   B 1 135 ? 51.208 27.676  60.007 1.00 31.17 ? 135  SER   B HB2  1 
ATOM   11506 H  HB3  . SER   B 1 135 ? 51.304 26.139  60.252 1.00 31.17 ? 135  SER   B HB3  1 
ATOM   11507 H  HG   . SER   B 1 135 ? 51.955 25.893  58.330 1.00 36.18 ? 135  SER   B HG   1 
ATOM   11508 N  N    . GLN   B 1 136 ? 48.799 27.358  57.246 1.00 22.56 ? 136  GLN   B N    1 
ATOM   11509 C  CA   . GLN   B 1 136 ? 48.361 28.328  56.209 1.00 23.16 ? 136  GLN   B CA   1 
ATOM   11510 C  C    . GLN   B 1 136 ? 46.829 28.393  56.155 1.00 21.46 ? 136  GLN   B C    1 
ATOM   11511 O  O    . GLN   B 1 136 ? 46.307 29.181  55.350 1.00 21.38 ? 136  GLN   B O    1 
ATOM   11512 C  CB   . GLN   B 1 136 ? 48.924 27.933  54.843 1.00 21.07 ? 136  GLN   B CB   1 
ATOM   11513 C  CG   . GLN   B 1 136 ? 50.443 27.888  54.811 1.00 27.01 ? 136  GLN   B CG   1 
ATOM   11514 C  CD   . GLN   B 1 136 ? 51.053 29.100  55.471 1.00 34.74 ? 136  GLN   B CD   1 
ATOM   11515 O  OE1  . GLN   B 1 136 ? 50.830 30.234  55.055 1.00 38.24 ? 136  GLN   B OE1  1 
ATOM   11516 N  NE2  . GLN   B 1 136 ? 51.831 28.867  56.514 1.00 37.00 ? 136  GLN   B NE2  1 
ATOM   11517 H  H    . GLN   B 1 136 ? 48.952 26.563  56.955 1.00 27.08 ? 136  GLN   B H    1 
ATOM   11518 H  HA   . GLN   B 1 136 ? 48.700 29.206  56.442 1.00 27.79 ? 136  GLN   B HA   1 
ATOM   11519 H  HB2  . GLN   B 1 136 ? 48.575 27.062  54.596 1.00 25.29 ? 136  GLN   B HB2  1 
ATOM   11520 H  HB3  . GLN   B 1 136 ? 48.611 28.564  54.176 1.00 25.29 ? 136  GLN   B HB3  1 
ATOM   11521 H  HG2  . GLN   B 1 136 ? 50.752 27.085  55.259 1.00 32.41 ? 136  GLN   B HG2  1 
ATOM   11522 H  HG3  . GLN   B 1 136 ? 50.746 27.834  53.891 1.00 32.41 ? 136  GLN   B HG3  1 
ATOM   11523 H  HE21 . GLN   B 1 136 ? 51.965 28.060  56.778 1.00 44.41 ? 136  GLN   B HE21 1 
ATOM   11524 H  HE22 . GLN   B 1 136 ? 52.203 29.523  56.928 1.00 44.41 ? 136  GLN   B HE22 1 
ATOM   11525 N  N    . LEU   B 1 137 ? 46.150 27.588  56.975 1.00 19.37 ? 137  LEU   B N    1 
ATOM   11526 C  CA   . LEU   B 1 137 ? 44.663 27.576  56.994 1.00 18.55 ? 137  LEU   B CA   1 
ATOM   11527 C  C    . LEU   B 1 137 ? 44.154 28.138  58.326 1.00 21.50 ? 137  LEU   B C    1 
ATOM   11528 O  O    . LEU   B 1 137 ? 43.040 28.695  58.341 1.00 16.00 ? 137  LEU   B O    1 
ATOM   11529 C  CB   . LEU   B 1 137 ? 44.183 26.132  56.827 1.00 19.83 ? 137  LEU   B CB   1 
ATOM   11530 C  CG   . LEU   B 1 137 ? 44.570 25.443  55.521 1.00 19.20 ? 137  LEU   B CG   1 
ATOM   11531 C  CD1  . LEU   B 1 137 ? 44.280 23.952  55.600 1.00 19.50 ? 137  LEU   B CD1  1 
ATOM   11532 C  CD2  . LEU   B 1 137 ? 43.831 26.063  54.347 1.00 20.72 ? 137  LEU   B CD2  1 
ATOM   11533 H  H    . LEU   B 1 137 ? 46.518 27.042  57.528 1.00 23.25 ? 137  LEU   B H    1 
ATOM   11534 H  HA   . LEU   B 1 137 ? 44.321 28.126  56.272 1.00 22.26 ? 137  LEU   B HA   1 
ATOM   11535 H  HB2  . LEU   B 1 137 ? 44.532 25.607  57.564 1.00 23.80 ? 137  LEU   B HB2  1 
ATOM   11536 H  HB3  . LEU   B 1 137 ? 43.216 26.121  56.903 1.00 23.80 ? 137  LEU   B HB3  1 
ATOM   11537 H  HG   . LEU   B 1 137 ? 45.522 25.567  55.383 1.00 23.04 ? 137  LEU   B HG   1 
ATOM   11538 H  HD11 . LEU   B 1 137 ? 44.531 23.529  54.764 1.00 23.40 ? 137  LEU   B HD11 1 
ATOM   11539 H  HD12 . LEU   B 1 137 ? 44.791 23.561  56.326 1.00 23.40 ? 137  LEU   B HD12 1 
ATOM   11540 H  HD13 . LEU   B 1 137 ? 43.333 23.814  55.760 1.00 23.40 ? 137  LEU   B HD13 1 
ATOM   11541 H  HD21 . LEU   B 1 137 ? 44.089 25.613  53.528 1.00 24.86 ? 137  LEU   B HD21 1 
ATOM   11542 H  HD22 . LEU   B 1 137 ? 42.875 25.968  54.480 1.00 24.86 ? 137  LEU   B HD22 1 
ATOM   11543 H  HD23 . LEU   B 1 137 ? 44.056 27.004  54.283 1.00 24.86 ? 137  LEU   B HD23 1 
ATOM   11544 N  N    . TRP   B 1 138 ? 44.931 27.973  59.398 1.00 17.26 ? 138  TRP   B N    1 
ATOM   11545 C  CA   . TRP   B 1 138 ? 44.493 28.411  60.751 1.00 21.32 ? 138  TRP   B CA   1 
ATOM   11546 C  C    . TRP   B 1 138 ? 44.034 29.873  60.722 1.00 17.86 ? 138  TRP   B C    1 
ATOM   11547 O  O    . TRP   B 1 138 ? 44.801 30.720  60.232 1.00 17.92 ? 138  TRP   B O    1 
ATOM   11548 C  CB   . TRP   B 1 138 ? 45.624 28.178  61.760 1.00 17.10 ? 138  TRP   B CB   1 
ATOM   11549 C  CG   . TRP   B 1 138 ? 45.195 27.960  63.179 1.00 17.87 ? 138  TRP   B CG   1 
ATOM   11550 C  CD1  . TRP   B 1 138 ? 45.423 28.792  64.236 1.00 20.44 ? 138  TRP   B CD1  1 
ATOM   11551 C  CD2  . TRP   B 1 138 ? 44.503 26.817  63.715 1.00 18.11 ? 138  TRP   B CD2  1 
ATOM   11552 N  NE1  . TRP   B 1 138 ? 44.910 28.256  65.385 1.00 19.31 ? 138  TRP   B NE1  1 
ATOM   11553 C  CE2  . TRP   B 1 138 ? 44.341 27.045  65.098 1.00 17.23 ? 138  TRP   B CE2  1 
ATOM   11554 C  CE3  . TRP   B 1 138 ? 44.000 25.633  63.167 1.00 18.91 ? 138  TRP   B CE3  1 
ATOM   11555 C  CZ2  . TRP   B 1 138 ? 43.700 26.132  65.933 1.00 19.42 ? 138  TRP   B CZ2  1 
ATOM   11556 C  CZ3  . TRP   B 1 138 ? 43.368 24.732  63.993 1.00 18.33 ? 138  TRP   B CZ3  1 
ATOM   11557 C  CH2  . TRP   B 1 138 ? 43.219 24.980  65.356 1.00 19.23 ? 138  TRP   B CH2  1 
ATOM   11558 H  H    . TRP   B 1 138 ? 45.712 27.613  59.375 1.00 20.72 ? 138  TRP   B H    1 
ATOM   11559 H  HA   . TRP   B 1 138 ? 43.730 27.882  61.032 1.00 25.59 ? 138  TRP   B HA   1 
ATOM   11560 H  HB2  . TRP   B 1 138 ? 46.138 27.407  61.473 1.00 20.52 ? 138  TRP   B HB2  1 
ATOM   11561 H  HB3  . TRP   B 1 138 ? 46.221 28.942  61.734 1.00 20.52 ? 138  TRP   B HB3  1 
ATOM   11562 H  HD1  . TRP   B 1 138 ? 45.865 29.609  64.183 1.00 24.53 ? 138  TRP   B HD1  1 
ATOM   11563 H  HE1  . TRP   B 1 138 ? 44.940 28.621  66.163 1.00 23.17 ? 138  TRP   B HE1  1 
ATOM   11564 H  HE3  . TRP   B 1 138 ? 44.091 25.457  62.258 1.00 22.69 ? 138  TRP   B HE3  1 
ATOM   11565 H  HZ2  . TRP   B 1 138 ? 43.601 26.295  66.843 1.00 23.30 ? 138  TRP   B HZ2  1 
ATOM   11566 H  HZ3  . TRP   B 1 138 ? 43.034 23.942  63.634 1.00 22.00 ? 138  TRP   B HZ3  1 
ATOM   11567 H  HH2  . TRP   B 1 138 ? 42.785 24.352  65.887 1.00 23.08 ? 138  TRP   B HH2  1 
ATOM   11568 N  N    . GLY   B 1 139 ? 42.831 30.144  61.234 1.00 14.41 ? 139  GLY   B N    1 
ATOM   11569 C  CA   . GLY   B 1 139 ? 42.309 31.521  61.284 1.00 15.99 ? 139  GLY   B CA   1 
ATOM   11570 C  C    . GLY   B 1 139 ? 41.283 31.795  60.197 1.00 18.49 ? 139  GLY   B C    1 
ATOM   11571 O  O    . GLY   B 1 139 ? 40.562 32.797  60.317 1.00 16.13 ? 139  GLY   B O    1 
ATOM   11572 H  H    . GLY   B 1 139 ? 42.300 29.550  61.557 1.00 17.30 ? 139  GLY   B H    1 
ATOM   11573 H  HA2  . GLY   B 1 139 ? 41.906 31.680  62.152 1.00 19.19 ? 139  GLY   B HA2  1 
ATOM   11574 H  HA3  . GLY   B 1 139 ? 43.045 32.146  61.195 1.00 19.19 ? 139  GLY   B HA3  1 
ATOM   11575 N  N    . LYS   B 1 140 ? 41.207 30.935  59.182 1.00 14.52 ? 140  LYS   B N    1 
ATOM   11576 C  CA   . LYS   B 1 140 ? 40.309 31.220  58.034 1.00 17.35 ? 140  LYS   B CA   1 
ATOM   11577 C  C    . LYS   B 1 140 ? 38.874 30.800  58.355 1.00 16.89 ? 140  LYS   B C    1 
ATOM   11578 O  O    . LYS   B 1 140 ? 38.686 29.816  59.085 1.00 15.69 ? 140  LYS   B O    1 
ATOM   11579 C  CB   . LYS   B 1 140 ? 40.793 30.521  56.762 1.00 15.91 ? 140  LYS   B CB   1 
ATOM   11580 C  CG   . LYS   B 1 140 ? 42.063 31.100  56.156 1.00 15.65 ? 140  LYS   B CG   1 
ATOM   11581 C  CD   . LYS   B 1 140 ? 42.524 30.364  54.920 1.00 16.09 ? 140  LYS   B CD   1 
ATOM   11582 C  CE   . LYS   B 1 140 ? 43.768 30.971  54.308 1.00 19.43 ? 140  LYS   B CE   1 
ATOM   11583 N  NZ   . LYS   B 1 140 ? 43.535 32.367  53.871 1.00 22.78 ? 140  LYS   B NZ   1 
ATOM   11584 H  H    . LYS   B 1 140 ? 41.649 30.199  59.128 1.00 17.43 ? 140  LYS   B H    1 
ATOM   11585 H  HA   . LYS   B 1 140 ? 40.327 32.177  57.877 1.00 20.82 ? 140  LYS   B HA   1 
ATOM   11586 H  HB2  . LYS   B 1 140 ? 40.944 29.584  56.961 1.00 19.10 ? 140  LYS   B HB2  1 
ATOM   11587 H  HB3  . LYS   B 1 140 ? 40.087 30.560  56.098 1.00 19.10 ? 140  LYS   B HB3  1 
ATOM   11588 H  HG2  . LYS   B 1 140 ? 41.912 32.032  55.933 1.00 18.79 ? 140  LYS   B HG2  1 
ATOM   11589 H  HG3  . LYS   B 1 140 ? 42.770 31.079  56.820 1.00 18.79 ? 140  LYS   B HG3  1 
ATOM   11590 H  HD2  . LYS   B 1 140 ? 42.699 29.437  55.147 1.00 19.31 ? 140  LYS   B HD2  1 
ATOM   11591 H  HD3  . LYS   B 1 140 ? 41.811 30.366  54.262 1.00 19.31 ? 140  LYS   B HD3  1 
ATOM   11592 H  HE2  . LYS   B 1 140 ? 44.491 30.950  54.954 1.00 23.32 ? 140  LYS   B HE2  1 
ATOM   11593 H  HE3  . LYS   B 1 140 ? 44.050 30.436  53.549 1.00 23.32 ? 140  LYS   B HE3  1 
ATOM   11594 H  HZ1  . LYS   B 1 140 ? 44.253 32.667  53.439 1.00 27.34 ? 140  LYS   B HZ1  1 
ATOM   11595 H  HZ2  . LYS   B 1 140 ? 42.830 32.395  53.329 1.00 27.34 ? 140  LYS   B HZ2  1 
ATOM   11596 H  HZ3  . LYS   B 1 140 ? 43.382 32.879  54.582 1.00 27.34 ? 140  LYS   B HZ3  1 
ATOM   11597 N  N    . VAL   B 1 141 ? 37.915 31.538  57.801 1.00 18.27 ? 141  VAL   B N    1 
ATOM   11598 C  CA   . VAL   B 1 141 ? 36.487 31.171  57.990 1.00 15.08 ? 141  VAL   B CA   1 
ATOM   11599 C  C    . VAL   B 1 141 ? 36.208 29.880  57.214 1.00 14.92 ? 141  VAL   B C    1 
ATOM   11600 O  O    . VAL   B 1 141 ? 37.060 29.467  56.410 1.00 14.05 ? 141  VAL   B O    1 
ATOM   11601 C  CB   . VAL   B 1 141 ? 35.554 32.326  57.573 1.00 15.83 ? 141  VAL   B CB   1 
ATOM   11602 C  CG1  . VAL   B 1 141 ? 35.703 33.522  58.499 1.00 17.09 ? 141  VAL   B CG1  1 
ATOM   11603 C  CG2  . VAL   B 1 141 ? 35.773 32.734  56.125 1.00 17.26 ? 141  VAL   B CG2  1 
ATOM   11604 H  H    . VAL   B 1 141 ? 38.051 32.239  57.322 1.00 21.92 ? 141  VAL   B H    1 
ATOM   11605 H  HA   . VAL   B 1 141 ? 36.307 31.012  58.930 1.00 18.10 ? 141  VAL   B HA   1 
ATOM   11606 H  HB   . VAL   B 1 141 ? 34.645 31.997  57.651 1.00 19.00 ? 141  VAL   B HB   1 
ATOM   11607 H  HG11 . VAL   B 1 141 ? 35.105 34.230  58.212 1.00 20.51 ? 141  VAL   B HG11 1 
ATOM   11608 H  HG12 . VAL   B 1 141 ? 35.480 33.259  59.406 1.00 20.51 ? 141  VAL   B HG12 1 
ATOM   11609 H  HG13 . VAL   B 1 141 ? 36.619 33.841  58.471 1.00 20.51 ? 141  VAL   B HG13 1 
ATOM   11610 H  HG21 . VAL   B 1 141 ? 35.171 33.460  55.899 1.00 20.72 ? 141  VAL   B HG21 1 
ATOM   11611 H  HG22 . VAL   B 1 141 ? 36.690 33.026  56.006 1.00 20.72 ? 141  VAL   B HG22 1 
ATOM   11612 H  HG23 . VAL   B 1 141 ? 35.597 31.977  55.545 1.00 20.72 ? 141  VAL   B HG23 1 
ATOM   11613 N  N    . THR   B 1 142 ? 35.044 29.285  57.447 1.00 13.96 ? 142  THR   B N    1 
ATOM   11614 C  CA   . THR   B 1 142 ? 34.696 27.987  56.817 1.00 14.65 ? 142  THR   B CA   1 
ATOM   11615 C  C    . THR   B 1 142 ? 34.832 28.053  55.289 1.00 15.11 ? 142  THR   B C    1 
ATOM   11616 O  O    . THR   B 1 142 ? 35.506 27.178  54.728 1.00 13.47 ? 142  THR   B O    1 
ATOM   11617 C  CB   . THR   B 1 142 ? 33.290 27.568  57.266 1.00 14.78 ? 142  THR   B CB   1 
ATOM   11618 O  OG1  . THR   B 1 142 ? 33.238 27.641  58.691 1.00 15.08 ? 142  THR   B OG1  1 
ATOM   11619 C  CG2  . THR   B 1 142 ? 32.905 26.183  56.797 1.00 16.50 ? 142  THR   B CG2  1 
ATOM   11620 H  H    . THR   B 1 142 ? 34.435 29.605  57.963 1.00 16.76 ? 142  THR   B H    1 
ATOM   11621 H  HA   . THR   B 1 142 ? 35.322 27.307  57.110 1.00 17.59 ? 142  THR   B HA   1 
ATOM   11622 H  HB   . THR   B 1 142 ? 32.650 28.174  56.861 1.00 17.73 ? 142  THR   B HB   1 
ATOM   11623 H  HG1  . THR   B 1 142 ? 32.493 27.947  58.929 1.00 18.10 ? 142  THR   B HG1  1 
ATOM   11624 H  HG21 . THR   B 1 142 ? 32.011 25.973  57.109 1.00 19.81 ? 142  THR   B HG21 1 
ATOM   11625 H  HG22 . THR   B 1 142 ? 32.925 26.152  55.828 1.00 19.81 ? 142  THR   B HG22 1 
ATOM   11626 H  HG23 . THR   B 1 142 ? 33.532 25.534  57.153 1.00 19.81 ? 142  THR   B HG23 1 
ATOM   11627 N  N    . SER   B 1 143 ? 34.196 29.033  54.647 1.00 13.96 ? 143  SER   B N    1 
ATOM   11628 C  CA   . SER   B 1 143 ? 34.202 29.094  53.160 1.00 15.99 ? 143  SER   B CA   1 
ATOM   11629 C  C    . SER   B 1 143 ? 35.639 29.155  52.633 1.00 16.25 ? 143  SER   B C    1 
ATOM   11630 O  O    . SER   B 1 143 ? 35.937 28.452  51.660 1.00 14.13 ? 143  SER   B O    1 
ATOM   11631 C  CB   . SER   B 1 143 ? 33.389 30.270  52.660 1.00 16.69 ? 143  SER   B CB   1 
ATOM   11632 O  OG   . SER   B 1 143 ? 33.988 31.498  53.041 1.00 17.19 ? 143  SER   B OG   1 
ATOM   11633 H  H    . SER   B 1 143 ? 33.760 29.666  55.034 1.00 16.76 ? 143  SER   B H    1 
ATOM   11634 H  HA   . SER   B 1 143 ? 33.788 28.285  52.821 1.00 19.19 ? 143  SER   B HA   1 
ATOM   11635 H  HB2  . SER   B 1 143 ? 33.314 30.229  51.694 1.00 20.03 ? 143  SER   B HB2  1 
ATOM   11636 H  HB3  . SER   B 1 143 ? 32.488 30.221  53.017 1.00 20.03 ? 143  SER   B HB3  1 
ATOM   11637 H  HG   . SER   B 1 143 ? 33.396 32.025  53.319 1.00 20.63 ? 143  SER   B HG   1 
ATOM   11638 N  N    . GLU   B 1 144 ? 36.466 29.998  53.245 1.00 14.55 ? 144  GLU   B N    1 
ATOM   11639 C  CA   . GLU   B 1 144 ? 37.860 30.172  52.764 1.00 15.85 ? 144  GLU   B CA   1 
ATOM   11640 C  C    . GLU   B 1 144 ? 38.651 28.889  53.038 1.00 13.95 ? 144  GLU   B C    1 
ATOM   11641 O  O    . GLU   B 1 144 ? 39.390 28.446  52.143 1.00 15.44 ? 144  GLU   B O    1 
ATOM   11642 C  CB   . GLU   B 1 144 ? 38.487 31.400  53.424 1.00 15.85 ? 144  GLU   B CB   1 
ATOM   11643 C  CG   . GLU   B 1 144 ? 37.918 32.705  52.901 1.00 20.11 ? 144  GLU   B CG   1 
ATOM   11644 C  CD   . GLU   B 1 144 ? 38.255 32.985  51.446 1.00 25.34 ? 144  GLU   B CD   1 
ATOM   11645 O  OE1  . GLU   B 1 144 ? 39.454 33.054  51.127 1.00 26.55 ? 144  GLU   B OE1  1 
ATOM   11646 O  OE2  . GLU   B 1 144 ? 37.321 33.133  50.640 1.00 26.56 ? 144  GLU   B OE2  1 
ATOM   11647 H  H    . GLU   B 1 144 ? 36.256 30.476  53.929 1.00 17.46 ? 144  GLU   B H    1 
ATOM   11648 H  HA   . GLU   B 1 144 ? 37.873 30.327  51.807 1.00 19.03 ? 144  GLU   B HA   1 
ATOM   11649 H  HB2  . GLU   B 1 144 ? 38.348 31.353  54.383 1.00 19.02 ? 144  GLU   B HB2  1 
ATOM   11650 H  HB3  . GLU   B 1 144 ? 39.445 31.388  53.275 1.00 19.02 ? 144  GLU   B HB3  1 
ATOM   11651 H  HG2  . GLU   B 1 144 ? 36.954 32.691  53.003 1.00 24.13 ? 144  GLU   B HG2  1 
ATOM   11652 H  HG3  . GLU   B 1 144 ? 38.251 33.434  53.447 1.00 24.13 ? 144  GLU   B HG3  1 
ATOM   11653 N  N    . THR   B 1 145 ? 38.501 28.322  54.232 1.00 12.59 ? 145  THR   B N    1 
ATOM   11654 C  CA   . THR   B 1 145 ? 39.179 27.036  54.540 1.00 15.38 ? 145  THR   B CA   1 
ATOM   11655 C  C    . THR   B 1 145 ? 38.813 26.005  53.467 1.00 15.78 ? 145  THR   B C    1 
ATOM   11656 O  O    . THR   B 1 145 ? 39.718 25.317  52.967 1.00 15.87 ? 145  THR   B O    1 
ATOM   11657 C  CB   . THR   B 1 145 ? 38.780 26.546  55.940 1.00 15.37 ? 145  THR   B CB   1 
ATOM   11658 O  OG1  . THR   B 1 145 ? 39.136 27.550  56.891 1.00 13.64 ? 145  THR   B OG1  1 
ATOM   11659 C  CG2  . THR   B 1 145 ? 39.425 25.228  56.310 1.00 15.87 ? 145  THR   B CG2  1 
ATOM   11660 H  H    . THR   B 1 145 ? 38.026 28.646  54.871 1.00 15.11 ? 145  THR   B H    1 
ATOM   11661 H  HA   . THR   B 1 145 ? 40.141 27.163  54.536 1.00 18.45 ? 145  THR   B HA   1 
ATOM   11662 H  HB   . THR   B 1 145 ? 37.822 26.391  55.941 1.00 18.45 ? 145  THR   B HB   1 
ATOM   11663 H  HG1  . THR   B 1 145 ? 38.596 28.191  56.837 1.00 16.38 ? 145  THR   B HG1  1 
ATOM   11664 H  HG21 . THR   B 1 145 ? 39.140 24.967  57.200 1.00 19.04 ? 145  THR   B HG21 1 
ATOM   11665 H  HG22 . THR   B 1 145 ? 39.159 24.547  55.672 1.00 19.04 ? 145  THR   B HG22 1 
ATOM   11666 H  HG23 . THR   B 1 145 ? 40.390 25.324  56.295 1.00 19.04 ? 145  THR   B HG23 1 
ATOM   11667 N  N    . THR   B 1 146 ? 37.527 25.912  53.132 1.00 15.11 ? 146  THR   B N    1 
ATOM   11668 C  CA   . THR   B 1 146 ? 37.065 24.890  52.156 1.00 14.92 ? 146  THR   B CA   1 
ATOM   11669 C  C    . THR   B 1 146 ? 37.649 25.187  50.769 1.00 13.56 ? 146  THR   B C    1 
ATOM   11670 O  O    . THR   B 1 146 ? 38.152 24.256  50.135 1.00 14.12 ? 146  THR   B O    1 
ATOM   11671 C  CB   . THR   B 1 146 ? 35.534 24.830  52.128 1.00 14.13 ? 146  THR   B CB   1 
ATOM   11672 O  OG1  . THR   B 1 146 ? 35.076 24.632  53.466 1.00 13.36 ? 146  THR   B OG1  1 
ATOM   11673 C  CG2  . THR   B 1 146 ? 35.001 23.743  51.222 1.00 14.73 ? 146  THR   B CG2  1 
ATOM   11674 H  H    . THR   B 1 146 ? 36.906 26.417  53.446 1.00 18.14 ? 146  THR   B H    1 
ATOM   11675 H  HA   . THR   B 1 146 ? 37.384 24.017  52.432 1.00 17.91 ? 146  THR   B HA   1 
ATOM   11676 H  HB   . THR   B 1 146 ? 35.201 25.666  51.764 1.00 16.96 ? 146  THR   B HB   1 
ATOM   11677 H  HG1  . THR   B 1 146 ? 35.134 25.354  53.892 1.00 16.04 ? 146  THR   B HG1  1 
ATOM   11678 H  HG21 . THR   B 1 146 ? 34.031 23.751  51.243 1.00 17.67 ? 146  THR   B HG21 1 
ATOM   11679 H  HG22 . THR   B 1 146 ? 35.306 23.899  50.315 1.00 17.67 ? 146  THR   B HG22 1 
ATOM   11680 H  HG23 . THR   B 1 146 ? 35.324 22.880  51.527 1.00 17.67 ? 146  THR   B HG23 1 
ATOM   11681 N  N    . LYS   B 1 147 ? 37.554 26.442  50.319 1.00 13.48 ? 147  LYS   B N    1 
ATOM   11682 C  CA   . LYS   B 1 147 ? 38.086 26.829  48.986 1.00 15.50 ? 147  LYS   B CA   1 
ATOM   11683 C  C    . LYS   B 1 147 ? 39.575 26.477  48.899 1.00 16.90 ? 147  LYS   B C    1 
ATOM   11684 O  O    . LYS   B 1 147 ? 39.993 25.915  47.869 1.00 16.30 ? 147  LYS   B O    1 
ATOM   11685 C  CB   . LYS   B 1 147 ? 37.900 28.331  48.748 1.00 14.25 ? 147  LYS   B CB   1 
ATOM   11686 C  CG   . LYS   B 1 147 ? 36.542 28.759  48.211 1.00 16.09 ? 147  LYS   B CG   1 
ATOM   11687 C  CD   . LYS   B 1 147 ? 36.503 30.234  47.871 1.00 21.51 ? 147  LYS   B CD   1 
ATOM   11688 C  CE   . LYS   B 1 147 ? 35.099 30.780  47.730 1.00 28.47 ? 147  LYS   B CE   1 
ATOM   11689 N  NZ   . LYS   B 1 147 ? 34.336 30.059  46.687 1.00 27.40 ? 147  LYS   B NZ   1 
ATOM   11690 H  H    . LYS   B 1 147 ? 37.190 27.085  50.759 1.00 16.18 ? 147  LYS   B H    1 
ATOM   11691 H  HA   . LYS   B 1 147 ? 37.596 26.341  48.305 1.00 18.60 ? 147  LYS   B HA   1 
ATOM   11692 H  HB2  . LYS   B 1 147 ? 38.058 28.795  49.585 1.00 17.10 ? 147  LYS   B HB2  1 
ATOM   11693 H  HB3  . LYS   B 1 147 ? 38.582 28.629  48.126 1.00 17.10 ? 147  LYS   B HB3  1 
ATOM   11694 H  HG2  . LYS   B 1 147 ? 36.331 28.240  47.419 1.00 19.31 ? 147  LYS   B HG2  1 
ATOM   11695 H  HG3  . LYS   B 1 147 ? 35.858 28.562  48.870 1.00 19.31 ? 147  LYS   B HG3  1 
ATOM   11696 H  HD2  . LYS   B 1 147 ? 36.968 30.731  48.562 1.00 25.81 ? 147  LYS   B HD2  1 
ATOM   11697 H  HD3  . LYS   B 1 147 ? 36.985 30.381  47.042 1.00 25.81 ? 147  LYS   B HD3  1 
ATOM   11698 H  HE2  . LYS   B 1 147 ? 34.636 30.707  48.579 1.00 34.17 ? 147  LYS   B HE2  1 
ATOM   11699 H  HE3  . LYS   B 1 147 ? 35.139 31.724  47.509 1.00 34.17 ? 147  LYS   B HE3  1 
ATOM   11700 H  HZ1  . LYS   B 1 147 ? 33.522 30.411  46.618 1.00 32.88 ? 147  LYS   B HZ1  1 
ATOM   11701 H  HZ2  . LYS   B 1 147 ? 34.758 30.132  45.907 1.00 32.88 ? 147  LYS   B HZ2  1 
ATOM   11702 H  HZ3  . LYS   B 1 147 ? 34.269 29.200  46.909 1.00 32.88 ? 147  LYS   B HZ3  1 
ATOM   11703 N  N    . GLU   B 1 148 ? 40.338 26.802  49.940 1.00 15.03 ? 148  GLU   B N    1 
ATOM   11704 C  CA   . GLU   B 1 148 ? 41.806 26.569  49.900 1.00 15.64 ? 148  GLU   B CA   1 
ATOM   11705 C  C    . GLU   B 1 148 ? 42.100 25.064  49.864 1.00 14.53 ? 148  GLU   B C    1 
ATOM   11706 O  O    . GLU   B 1 148 ? 42.992 24.651  49.098 1.00 16.59 ? 148  GLU   B O    1 
ATOM   11707 C  CB   . GLU   B 1 148 ? 42.474 27.237  51.102 1.00 16.28 ? 148  GLU   B CB   1 
ATOM   11708 C  CG   . GLU   B 1 148 ? 42.444 28.755  51.054 1.00 18.56 ? 148  GLU   B CG   1 
ATOM   11709 C  CD   . GLU   B 1 148 ? 42.966 29.408  49.783 1.00 19.37 ? 148  GLU   B CD   1 
ATOM   11710 O  OE1  . GLU   B 1 148 ? 43.788 28.786  49.083 1.00 18.37 ? 148  GLU   B OE1  1 
ATOM   11711 O  OE2  . GLU   B 1 148 ? 42.552 30.547  49.502 1.00 20.54 ? 148  GLU   B OE2  1 
ATOM   11712 H  H    . GLU   B 1 148 ? 40.045 27.151  50.669 1.00 18.04 ? 148  GLU   B H    1 
ATOM   11713 H  HA   . GLU   B 1 148 ? 42.172 26.965  49.094 1.00 18.77 ? 148  GLU   B HA   1 
ATOM   11714 H  HB2  . GLU   B 1 148 ? 42.034 26.939  51.913 1.00 19.53 ? 148  GLU   B HB2  1 
ATOM   11715 H  HB3  . GLU   B 1 148 ? 43.396 26.941  51.154 1.00 19.53 ? 148  GLU   B HB3  1 
ATOM   11716 H  HG2  . GLU   B 1 148 ? 41.528 29.044  51.189 1.00 22.28 ? 148  GLU   B HG2  1 
ATOM   11717 H  HG3  . GLU   B 1 148 ? 42.961 29.092  51.802 1.00 22.28 ? 148  GLU   B HG3  1 
ATOM   11718 N  N    . LEU   B 1 149 ? 41.385 24.280  50.671 1.00 13.41 ? 149  LEU   B N    1 
ATOM   11719 C  CA   . LEU   B 1 149 ? 41.640 22.818  50.731 1.00 13.98 ? 149  LEU   B CA   1 
ATOM   11720 C  C    . LEU   B 1 149 ? 41.251 22.169  49.398 1.00 14.45 ? 149  LEU   B C    1 
ATOM   11721 O  O    . LEU   B 1 149 ? 41.918 21.206  49.004 1.00 14.99 ? 149  LEU   B O    1 
ATOM   11722 C  CB   . LEU   B 1 149 ? 40.848 22.221  51.899 1.00 13.28 ? 149  LEU   B CB   1 
ATOM   11723 C  CG   . LEU   B 1 149 ? 41.572 22.259  53.244 1.00 15.13 ? 149  LEU   B CG   1 
ATOM   11724 C  CD1  . LEU   B 1 149 ? 40.635 21.883  54.379 1.00 17.29 ? 149  LEU   B CD1  1 
ATOM   11725 C  CD2  . LEU   B 1 149 ? 42.790 21.349  53.228 1.00 16.23 ? 149  LEU   B CD2  1 
ATOM   11726 H  H    . LEU   B 1 149 ? 40.756 24.559  51.187 1.00 16.09 ? 149  LEU   B H    1 
ATOM   11727 H  HA   . LEU   B 1 149 ? 42.583 22.647  50.879 1.00 16.78 ? 149  LEU   B HA   1 
ATOM   11728 H  HB2  . LEU   B 1 149 ? 40.009 22.700  51.983 1.00 15.93 ? 149  LEU   B HB2  1 
ATOM   11729 H  HB3  . LEU   B 1 149 ? 40.629 21.300  51.689 1.00 15.93 ? 149  LEU   B HB3  1 
ATOM   11730 H  HG   . LEU   B 1 149 ? 41.874 23.168  53.394 1.00 18.16 ? 149  LEU   B HG   1 
ATOM   11731 H  HD11 . LEU   B 1 149 ? 41.117 21.914  55.220 1.00 20.75 ? 149  LEU   B HD11 1 
ATOM   11732 H  HD12 . LEU   B 1 149 ? 39.894 22.508  54.408 1.00 20.75 ? 149  LEU   B HD12 1 
ATOM   11733 H  HD13 . LEU   B 1 149 ? 40.295 20.986  54.235 1.00 20.75 ? 149  LEU   B HD13 1 
ATOM   11734 H  HD21 . LEU   B 1 149 ? 43.234 21.388  54.089 1.00 19.47 ? 149  LEU   B HD21 1 
ATOM   11735 H  HD22 . LEU   B 1 149 ? 42.511 20.437  53.049 1.00 19.47 ? 149  LEU   B HD22 1 
ATOM   11736 H  HD23 . LEU   B 1 149 ? 43.403 21.641  52.535 1.00 19.47 ? 149  LEU   B HD23 1 
ATOM   11737 N  N    . GLU   B 1 150 ? 40.213 22.687  48.739 1.00 15.40 ? 150  GLU   B N    1 
ATOM   11738 C  CA   . GLU   B 1 150 ? 39.729 22.081  47.470 1.00 14.62 ? 150  GLU   B CA   1 
ATOM   11739 C  C    . GLU   B 1 150 ? 40.823 22.212  46.403 1.00 18.27 ? 150  GLU   B C    1 
ATOM   11740 O  O    . GLU   B 1 150 ? 40.885 21.356  45.505 1.00 16.17 ? 150  GLU   B O    1 
ATOM   11741 C  CB   . GLU   B 1 150 ? 38.419 22.745  47.038 1.00 14.06 ? 150  GLU   B CB   1 
ATOM   11742 C  CG   . GLU   B 1 150 ? 37.215 22.231  47.804 1.00 13.95 ? 150  GLU   B CG   1 
ATOM   11743 C  CD   . GLU   B 1 150 ? 35.870 22.628  47.222 1.00 20.65 ? 150  GLU   B CD   1 
ATOM   11744 O  OE1  . GLU   B 1 150 ? 35.846 23.118  46.079 1.00 20.60 ? 150  GLU   B OE1  1 
ATOM   11745 O  OE2  . GLU   B 1 150 ? 34.852 22.442  47.914 1.00 15.98 ? 150  GLU   B OE2  1 
ATOM   11746 H  H    . GLU   B 1 150 ? 39.773 23.380  48.997 1.00 18.49 ? 150  GLU   B H    1 
ATOM   11747 H  HA   . GLU   B 1 150 ? 39.543 21.138  47.597 1.00 17.55 ? 150  GLU   B HA   1 
ATOM   11748 H  HB2  . GLU   B 1 150 ? 38.491 23.704  47.164 1.00 16.88 ? 150  GLU   B HB2  1 
ATOM   11749 H  HB3  . GLU   B 1 150 ? 38.282 22.593  46.090 1.00 16.88 ? 150  GLU   B HB3  1 
ATOM   11750 H  HG2  . GLU   B 1 150 ? 37.262 21.263  47.844 1.00 16.74 ? 150  GLU   B HG2  1 
ATOM   11751 H  HG3  . GLU   B 1 150 ? 37.266 22.555  48.717 1.00 16.74 ? 150  GLU   B HG3  1 
ATOM   11752 N  N    . LYS   B 1 151 ? 41.655 23.241  46.531 1.00 15.65 ? 151  LYS   B N    1 
ATOM   11753 C  CA   . LYS   B 1 151 ? 42.723 23.464  45.527 1.00 15.46 ? 151  LYS   B CA   1 
ATOM   11754 C  C    . LYS   B 1 151 ? 43.843 22.441  45.702 1.00 19.07 ? 151  LYS   B C    1 
ATOM   11755 O  O    . LYS   B 1 151 ? 44.501 22.126  44.695 1.00 17.67 ? 151  LYS   B O    1 
ATOM   11756 C  CB   . LYS   B 1 151 ? 43.364 24.836  45.728 1.00 14.42 ? 151  LYS   B CB   1 
ATOM   11757 C  CG   . LYS   B 1 151 ? 42.460 26.037  45.489 1.00 15.83 ? 151  LYS   B CG   1 
ATOM   11758 C  CD   . LYS   B 1 151 ? 43.145 27.346  45.815 1.00 18.48 ? 151  LYS   B CD   1 
ATOM   11759 C  CE   . LYS   B 1 151 ? 42.197 28.524  45.876 1.00 16.34 ? 151  LYS   B CE   1 
ATOM   11760 N  NZ   . LYS   B 1 151 ? 42.872 29.745  46.376 1.00 18.23 ? 151  LYS   B NZ   1 
ATOM   11761 H  H    . LYS   B 1 151 ? 41.630 23.815  47.171 1.00 18.79 ? 151  LYS   B H    1 
ATOM   11762 H  HA   . LYS   B 1 151 ? 42.313 23.390  44.651 1.00 18.56 ? 151  LYS   B HA   1 
ATOM   11763 H  HB2  . LYS   B 1 151 ? 43.703 24.885  46.635 1.00 17.31 ? 151  LYS   B HB2  1 
ATOM   11764 H  HB3  . LYS   B 1 151 ? 44.128 24.906  45.135 1.00 17.31 ? 151  LYS   B HB3  1 
ATOM   11765 H  HG2  . LYS   B 1 151 ? 42.176 26.045  44.562 1.00 19.00 ? 151  LYS   B HG2  1 
ATOM   11766 H  HG3  . LYS   B 1 151 ? 41.660 25.950  46.030 1.00 19.00 ? 151  LYS   B HG3  1 
ATOM   11767 H  HD2  . LYS   B 1 151 ? 43.600 27.261  46.668 1.00 22.18 ? 151  LYS   B HD2  1 
ATOM   11768 H  HD3  . LYS   B 1 151 ? 43.826 27.522  45.147 1.00 22.18 ? 151  LYS   B HD3  1 
ATOM   11769 H  HE2  . LYS   B 1 151 ? 41.834 28.693  44.993 1.00 19.61 ? 151  LYS   B HE2  1 
ATOM   11770 H  HE3  . LYS   B 1 151 ? 41.449 28.308  46.454 1.00 19.61 ? 151  LYS   B HE3  1 
ATOM   11771 H  HZ1  . LYS   B 1 151 ? 42.268 30.385  46.510 1.00 21.88 ? 151  LYS   B HZ1  1 
ATOM   11772 H  HZ2  . LYS   B 1 151 ? 43.286 29.563  47.143 1.00 21.88 ? 151  LYS   B HZ2  1 
ATOM   11773 H  HZ3  . LYS   B 1 151 ? 43.468 30.022  45.776 1.00 21.88 ? 151  LYS   B HZ3  1 
ATOM   11774 N  N    . ILE   B 1 152 ? 44.050 21.944  46.921 1.00 18.70 ? 152  ILE   B N    1 
ATOM   11775 C  CA   . ILE   B 1 152 ? 45.252 21.088  47.166 1.00 18.09 ? 152  ILE   B CA   1 
ATOM   11776 C  C    . ILE   B 1 152 ? 44.859 19.673  47.594 1.00 17.73 ? 152  ILE   B C    1 
ATOM   11777 O  O    . ILE   B 1 152 ? 45.708 18.981  48.171 1.00 18.43 ? 152  ILE   B O    1 
ATOM   11778 C  CB   . ILE   B 1 152 ? 46.154 21.778  48.203 1.00 18.75 ? 152  ILE   B CB   1 
ATOM   11779 C  CG1  . ILE   B 1 152 ? 45.458 21.862  49.564 1.00 19.26 ? 152  ILE   B CG1  1 
ATOM   11780 C  CG2  . ILE   B 1 152 ? 46.591 23.145  47.706 1.00 21.49 ? 152  ILE   B CG2  1 
ATOM   11781 C  CD1  . ILE   B 1 152 ? 46.185 22.710  50.578 1.00 17.19 ? 152  ILE   B CD1  1 
ATOM   11782 H  H    . ILE   B 1 152 ? 43.541 22.073  47.602 1.00 22.45 ? 152  ILE   B H    1 
ATOM   11783 H  HA   . ILE   B 1 152 ? 45.748 20.988  46.339 1.00 21.71 ? 152  ILE   B HA   1 
ATOM   11784 H  HB   . ILE   B 1 152 ? 46.953 21.241  48.322 1.00 22.51 ? 152  ILE   B HB   1 
ATOM   11785 H  HG12 . ILE   B 1 152 ? 44.565 22.220  49.438 1.00 23.12 ? 152  ILE   B HG12 1 
ATOM   11786 H  HG13 . ILE   B 1 152 ? 45.356 20.965  49.920 1.00 23.12 ? 152  ILE   B HG13 1 
ATOM   11787 H  HG21 . ILE   B 1 152 ? 47.158 23.565  48.371 1.00 25.80 ? 152  ILE   B HG21 1 
ATOM   11788 H  HG22 . ILE   B 1 152 ? 47.085 23.045  46.877 1.00 25.80 ? 152  ILE   B HG22 1 
ATOM   11789 H  HG23 . ILE   B 1 152 ? 45.809 23.699  47.552 1.00 25.80 ? 152  ILE   B HG23 1 
ATOM   11790 H  HD11 . ILE   B 1 152 ? 45.688 22.716  51.411 1.00 20.64 ? 152  ILE   B HD11 1 
ATOM   11791 H  HD12 . ILE   B 1 152 ? 47.069 22.343  50.733 1.00 20.64 ? 152  ILE   B HD12 1 
ATOM   11792 H  HD13 . ILE   B 1 152 ? 46.266 23.617  50.243 1.00 20.64 ? 152  ILE   B HD13 1 
ATOM   11793 N  N    . THR   B 1 153 ? 43.627 19.266  47.310 1.00 19.69 ? 153  THR   B N    1 
ATOM   11794 C  CA   . THR   B 1 153 ? 43.194 17.878  47.591 1.00 18.01 ? 153  THR   B CA   1 
ATOM   11795 C  C    . THR   B 1 153 ? 42.610 17.315  46.294 1.00 18.15 ? 153  THR   B C    1 
ATOM   11796 O  O    . THR   B 1 153 ? 42.361 18.101  45.372 1.00 17.54 ? 153  THR   B O    1 
ATOM   11797 C  CB   . THR   B 1 153 ? 42.198 17.821  48.758 1.00 15.39 ? 153  THR   B CB   1 
ATOM   11798 O  OG1  . THR   B 1 153 ? 41.080 18.645  48.429 1.00 15.87 ? 153  THR   B OG1  1 
ATOM   11799 C  CG2  . THR   B 1 153 ? 42.803 18.269  50.070 1.00 17.14 ? 153  THR   B CG2  1 
ATOM   11800 H  H    . THR   B 1 153 ? 43.023 19.765  46.957 1.00 23.63 ? 153  THR   B H    1 
ATOM   11801 H  HA   . THR   B 1 153 ? 43.947 17.335  47.874 1.00 21.61 ? 153  THR   B HA   1 
ATOM   11802 H  HB   . THR   B 1 153 ? 41.929 16.898  48.883 1.00 18.47 ? 153  THR   B HB   1 
ATOM   11803 H  HG1  . THR   B 1 153 ? 41.269 19.449  48.583 1.00 19.05 ? 153  THR   B HG1  1 
ATOM   11804 H  HG21 . THR   B 1 153 ? 42.134 18.214  50.771 1.00 20.57 ? 153  THR   B HG21 1 
ATOM   11805 H  HG22 . THR   B 1 153 ? 43.553 17.696  50.293 1.00 20.57 ? 153  THR   B HG22 1 
ATOM   11806 H  HG23 . THR   B 1 153 ? 43.110 19.185  49.989 1.00 20.57 ? 153  THR   B HG23 1 
ATOM   11807 N  N    . GLU   B 1 154 ? 42.406 16.001  46.238 1.00 17.62 ? 154  GLU   B N    1 
ATOM   11808 C  CA   . GLU   B 1 154 ? 41.858 15.362  45.017 1.00 17.65 ? 154  GLU   B CA   1 
ATOM   11809 C  C    . GLU   B 1 154 ? 40.482 15.952  44.711 1.00 17.77 ? 154  GLU   B C    1 
ATOM   11810 O  O    . GLU   B 1 154 ? 39.736 16.237  45.658 1.00 20.40 ? 154  GLU   B O    1 
ATOM   11811 C  CB   . GLU   B 1 154 ? 41.746 13.851  45.197 1.00 21.22 ? 154  GLU   B CB   1 
ATOM   11812 C  CG   . GLU   B 1 154 ? 41.601 13.093  43.893 1.00 30.63 ? 154  GLU   B CG   1 
ATOM   11813 C  CD   . GLU   B 1 154 ? 41.962 11.622  44.001 1.00 28.75 ? 154  GLU   B CD   1 
ATOM   11814 O  OE1  . GLU   B 1 154 ? 43.043 11.321  44.539 1.00 30.55 ? 154  GLU   B OE1  1 
ATOM   11815 O  OE2  . GLU   B 1 154 ? 41.157 10.785  43.554 1.00 32.67 ? 154  GLU   B OE2  1 
ATOM   11816 H  H    . GLU   B 1 154 ? 42.573 15.458  46.883 1.00 21.15 ? 154  GLU   B H    1 
ATOM   11817 H  HA   . GLU   B 1 154 ? 42.461 15.535  44.277 1.00 21.19 ? 154  GLU   B HA   1 
ATOM   11818 H  HB2  . GLU   B 1 154 ? 42.533 13.529  45.663 1.00 25.47 ? 154  GLU   B HB2  1 
ATOM   11819 H  HB3  . GLU   B 1 154 ? 40.982 13.656  45.762 1.00 25.47 ? 154  GLU   B HB3  1 
ATOM   11820 H  HG2  . GLU   B 1 154 ? 40.686 13.172  43.582 1.00 36.76 ? 154  GLU   B HG2  1 
ATOM   11821 H  HG3  . GLU   B 1 154 ? 42.165 13.508  43.222 1.00 36.76 ? 154  GLU   B HG3  1 
ATOM   11822 N  N    . ASN   B 1 155 ? 40.149 16.093  43.428 1.00 20.66 ? 155  ASN   B N    1 
ATOM   11823 C  CA   . ASN   B 1 155 ? 38.831 16.653  43.026 1.00 22.95 ? 155  ASN   B CA   1 
ATOM   11824 C  C    . ASN   B 1 155 ? 37.694 15.835  43.655 1.00 20.62 ? 155  ASN   B C    1 
ATOM   11825 O  O    . ASN   B 1 155 ? 37.854 14.608  43.752 1.00 21.64 ? 155  ASN   B O    1 
ATOM   11826 C  CB   . ASN   B 1 155 ? 38.708 16.734  41.502 1.00 27.84 ? 155  ASN   B CB   1 
ATOM   11827 C  CG   . ASN   B 1 155 ? 37.453 17.448  41.045 1.00 31.96 ? 155  ASN   B CG   1 
ATOM   11828 O  OD1  . ASN   B 1 155 ? 37.120 18.516  41.552 1.00 31.80 ? 155  ASN   B OD1  1 
ATOM   11829 N  ND2  . ASN   B 1 155 ? 36.749 16.864  40.089 1.00 32.27 ? 155  ASN   B ND2  1 
ATOM   11830 H  H    . ASN   B 1 155 ? 40.660 15.876  42.771 1.00 24.80 ? 155  ASN   B H    1 
ATOM   11831 H  HA   . ASN   B 1 155 ? 38.762 17.561  43.360 1.00 27.54 ? 155  ASN   B HA   1 
ATOM   11832 H  HB2  . ASN   B 1 155 ? 39.484 17.194  41.144 1.00 33.42 ? 155  ASN   B HB2  1 
ATOM   11833 H  HB3  . ASN   B 1 155 ? 38.715 15.837  41.134 1.00 33.42 ? 155  ASN   B HB3  1 
ATOM   11834 H  HD21 . ASN   B 1 155 ? 36.028 17.233  39.800 1.00 38.73 ? 155  ASN   B HD21 1 
ATOM   11835 H  HD22 . ASN   B 1 155 ? 37.013 16.116  39.757 1.00 38.73 ? 155  ASN   B HD22 1 
ATOM   11836 N  N    . LYS   B 1 156 ? 36.600 16.495  44.055 1.00 18.12 ? 156  LYS   B N    1 
ATOM   11837 C  CA   . LYS   B 1 156 ? 35.415 15.824  44.671 1.00 20.36 ? 156  LYS   B CA   1 
ATOM   11838 C  C    . LYS   B 1 156 ? 35.654 15.593  46.175 1.00 14.19 ? 156  LYS   B C    1 
ATOM   11839 O  O    . LYS   B 1 156 ? 34.751 15.039  46.820 1.00 19.13 ? 156  LYS   B O    1 
ATOM   11840 C  CB   . LYS   B 1 156 ? 35.004 14.550  43.913 1.00 23.17 ? 156  LYS   B CB   1 
ATOM   11841 C  CG   . LYS   B 1 156 ? 34.781 14.723  42.417 1.00 29.65 ? 156  LYS   B CG   1 
ATOM   11842 C  CD   . LYS   B 1 156 ? 34.021 13.573  41.797 1.00 34.24 ? 156  LYS   B CD   1 
ATOM   11843 C  CE   . LYS   B 1 156 ? 32.530 13.824  41.726 1.00 41.13 ? 156  LYS   B CE   1 
ATOM   11844 N  NZ   . LYS   B 1 156 ? 32.213 14.999  40.881 1.00 42.10 ? 156  LYS   B NZ   1 
ATOM   11845 H  H    . LYS   B 1 156 ? 36.513 17.347  43.981 1.00 21.74 ? 156  LYS   B H    1 
ATOM   11846 H  HA   . LYS   B 1 156 ? 34.652 16.417  44.591 1.00 24.44 ? 156  LYS   B HA   1 
ATOM   11847 H  HB2  . LYS   B 1 156 ? 35.690 13.877  44.047 1.00 27.81 ? 156  LYS   B HB2  1 
ATOM   11848 H  HB3  . LYS   B 1 156 ? 34.188 14.206  44.309 1.00 27.81 ? 156  LYS   B HB3  1 
ATOM   11849 H  HG2  . LYS   B 1 156 ? 34.294 15.547  42.261 1.00 35.58 ? 156  LYS   B HG2  1 
ATOM   11850 H  HG3  . LYS   B 1 156 ? 35.640 14.812  41.975 1.00 35.58 ? 156  LYS   B HG3  1 
ATOM   11851 H  HD2  . LYS   B 1 156 ? 34.360 13.412  40.903 1.00 41.09 ? 156  LYS   B HD2  1 
ATOM   11852 H  HD3  . LYS   B 1 156 ? 34.185 12.768  42.312 1.00 41.09 ? 156  LYS   B HD3  1 
ATOM   11853 H  HE2  . LYS   B 1 156 ? 32.086 13.039  41.369 1.00 49.36 ? 156  LYS   B HE2  1 
ATOM   11854 H  HE3  . LYS   B 1 156 ? 32.182 13.965  42.620 1.00 49.36 ? 156  LYS   B HE3  1 
ATOM   11855 H  HZ1  . LYS   B 1 156 ? 31.337 15.027  40.728 1.00 50.53 ? 156  LYS   B HZ1  1 
ATOM   11856 H  HZ2  . LYS   B 1 156 ? 32.465 15.743  41.300 1.00 50.53 ? 156  LYS   B HZ2  1 
ATOM   11857 H  HZ3  . LYS   B 1 156 ? 32.647 14.934  40.107 1.00 50.53 ? 156  LYS   B HZ3  1 
ATOM   11858 N  N    . SER   B 1 157 ? 36.794 16.041  46.717 1.00 15.59 ? 157  SER   B N    1 
ATOM   11859 C  CA   . SER   B 1 157 ? 37.031 15.915  48.177 1.00 15.45 ? 157  SER   B CA   1 
ATOM   11860 C  C    . SER   B 1 157 ? 36.026 16.804  48.918 1.00 15.36 ? 157  SER   B C    1 
ATOM   11861 O  O    . SER   B 1 157 ? 35.803 17.939  48.466 1.00 15.74 ? 157  SER   B O    1 
ATOM   11862 C  CB   . SER   B 1 157 ? 38.446 16.262  48.551 1.00 14.79 ? 157  SER   B CB   1 
ATOM   11863 O  OG   . SER   B 1 157 ? 39.335 15.216  48.192 1.00 14.27 ? 157  SER   B OG   1 
ATOM   11864 H  H    . SER   B 1 157 ? 37.432 16.413  46.276 1.00 18.71 ? 157  SER   B H    1 
ATOM   11865 H  HA   . SER   B 1 157 ? 36.901 14.989  48.437 1.00 18.55 ? 157  SER   B HA   1 
ATOM   11866 H  HB2  . SER   B 1 157 ? 38.710 17.083  48.107 1.00 17.75 ? 157  SER   B HB2  1 
ATOM   11867 H  HB3  . SER   B 1 157 ? 38.502 16.426  49.505 1.00 17.75 ? 157  SER   B HB3  1 
ATOM   11868 H  HG   . SER   B 1 157 ? 39.610 15.339  47.408 1.00 17.13 ? 157  SER   B HG   1 
ATOM   11869 N  N    . LYS   B 1 158 ? 35.446 16.288  50.000 1.00 14.05 ? 158  LYS   B N    1 
ATOM   11870 C  CA   . LYS   B 1 158 ? 34.505 17.088  50.828 1.00 12.79 ? 158  LYS   B CA   1 
ATOM   11871 C  C    . LYS   B 1 158 ? 35.261 17.631  52.045 1.00 14.20 ? 158  LYS   B C    1 
ATOM   11872 O  O    . LYS   B 1 158 ? 36.233 16.985  52.474 1.00 12.44 ? 158  LYS   B O    1 
ATOM   11873 C  CB   . LYS   B 1 158 ? 33.304 16.229  51.218 1.00 14.40 ? 158  LYS   B CB   1 
ATOM   11874 C  CG   . LYS   B 1 158 ? 32.548 15.616  50.048 1.00 16.01 ? 158  LYS   B CG   1 
ATOM   11875 C  CD   . LYS   B 1 158 ? 32.127 16.640  49.016 1.00 13.81 ? 158  LYS   B CD   1 
ATOM   11876 C  CE   . LYS   B 1 158 ? 31.251 16.058  47.927 1.00 15.92 ? 158  LYS   B CE   1 
ATOM   11877 N  NZ   . LYS   B 1 158 ? 31.962 15.013  47.154 1.00 17.54 ? 158  LYS   B NZ   1 
ATOM   11878 H  H    . LYS   B 1 158 ? 35.575 15.485  50.280 1.00 16.86 ? 158  LYS   B H    1 
ATOM   11879 H  HA   . LYS   B 1 158 ? 34.160 17.845  50.328 1.00 15.35 ? 158  LYS   B HA   1 
ATOM   11880 H  HB2  . LYS   B 1 158 ? 33.609 15.515  51.799 1.00 17.29 ? 158  LYS   B HB2  1 
ATOM   11881 H  HB3  . LYS   B 1 158 ? 32.689 16.772  51.735 1.00 17.29 ? 158  LYS   B HB3  1 
ATOM   11882 H  HG2  . LYS   B 1 158 ? 33.107 14.947  49.623 1.00 19.22 ? 158  LYS   B HG2  1 
ATOM   11883 H  HG3  . LYS   B 1 158 ? 31.761 15.158  50.382 1.00 19.22 ? 158  LYS   B HG3  1 
ATOM   11884 H  HD2  . LYS   B 1 158 ? 31.650 17.360  49.458 1.00 16.58 ? 158  LYS   B HD2  1 
ATOM   11885 H  HD3  . LYS   B 1 158 ? 32.919 17.030  48.613 1.00 16.58 ? 158  LYS   B HD3  1 
ATOM   11886 H  HE2  . LYS   B 1 158 ? 30.450 15.680  48.323 1.00 19.10 ? 158  LYS   B HE2  1 
ATOM   11887 H  HE3  . LYS   B 1 158 ? 30.965 16.766  47.328 1.00 19.10 ? 158  LYS   B HE3  1 
ATOM   11888 H  HZ1  . LYS   B 1 158 ? 31.550 14.888  46.375 1.00 21.06 ? 158  LYS   B HZ1  1 
ATOM   11889 H  HZ2  . LYS   B 1 158 ? 32.801 15.271  47.007 1.00 21.06 ? 158  LYS   B HZ2  1 
ATOM   11890 H  HZ3  . LYS   B 1 158 ? 31.963 14.252  47.615 1.00 21.06 ? 158  LYS   B HZ3  1 
ATOM   11891 N  N    . VAL   B 1 159 ? 34.816 18.767  52.586 1.00 10.11 ? 159  VAL   B N    1 
ATOM   11892 C  CA   . VAL   B 1 159 ? 35.605 19.398  53.684 1.00 11.32 ? 159  VAL   B CA   1 
ATOM   11893 C  C    . VAL   B 1 159 ? 34.786 19.512  54.970 1.00 11.95 ? 159  VAL   B C    1 
ATOM   11894 O  O    . VAL   B 1 159 ? 33.687 20.081  54.922 1.00 11.19 ? 159  VAL   B O    1 
ATOM   11895 C  CB   . VAL   B 1 159 ? 36.152 20.779  53.273 1.00 13.26 ? 159  VAL   B CB   1 
ATOM   11896 C  CG1  . VAL   B 1 159 ? 36.813 21.495  54.441 1.00 13.97 ? 159  VAL   B CG1  1 
ATOM   11897 C  CG2  . VAL   B 1 159 ? 37.105 20.683  52.092 1.00 12.69 ? 159  VAL   B CG2  1 
ATOM   11898 H  H    . VAL   B 1 159 ? 34.098 19.181  52.356 1.00 12.14 ? 159  VAL   B H    1 
ATOM   11899 H  HA   . VAL   B 1 159 ? 36.361 18.815  53.856 1.00 13.59 ? 159  VAL   B HA   1 
ATOM   11900 H  HB   . VAL   B 1 159 ? 35.388 21.307  52.994 1.00 15.92 ? 159  VAL   B HB   1 
ATOM   11901 H  HG11 . VAL   B 1 159 ? 37.144 22.358  54.146 1.00 16.77 ? 159  VAL   B HG11 1 
ATOM   11902 H  HG12 . VAL   B 1 159 ? 36.165 21.623  55.151 1.00 16.77 ? 159  VAL   B HG12 1 
ATOM   11903 H  HG13 . VAL   B 1 159 ? 37.552 20.961  54.772 1.00 16.77 ? 159  VAL   B HG13 1 
ATOM   11904 H  HG21 . VAL   B 1 159 ? 37.427 21.569  51.863 1.00 15.23 ? 159  VAL   B HG21 1 
ATOM   11905 H  HG22 . VAL   B 1 159 ? 37.857 20.117  52.328 1.00 15.23 ? 159  VAL   B HG22 1 
ATOM   11906 H  HG23 . VAL   B 1 159 ? 36.640 20.302  51.331 1.00 15.23 ? 159  VAL   B HG23 1 
ATOM   11907 N  N    . LEU   B 1 160 ? 35.319 18.969  56.059 1.00 10.04 ? 160  LEU   B N    1 
ATOM   11908 C  CA   . LEU   B 1 160 ? 34.684 19.148  57.385 1.00 10.36 ? 160  LEU   B CA   1 
ATOM   11909 C  C    . LEU   B 1 160 ? 35.698 19.954  58.195 1.00 10.44 ? 160  LEU   B C    1 
ATOM   11910 O  O    . LEU   B 1 160 ? 36.874 19.585  58.180 1.00 14.12 ? 160  LEU   B O    1 
ATOM   11911 C  CB   . LEU   B 1 160 ? 34.431 17.768  57.991 1.00 9.19  ? 160  LEU   B CB   1 
ATOM   11912 C  CG   . LEU   B 1 160 ? 33.947 17.737  59.440 1.00 11.47 ? 160  LEU   B CG   1 
ATOM   11913 C  CD1  . LEU   B 1 160 ? 32.954 16.603  59.639 1.00 12.19 ? 160  LEU   B CD1  1 
ATOM   11914 C  CD2  . LEU   B 1 160 ? 35.117 17.583  60.399 1.00 13.45 ? 160  LEU   B CD2  1 
ATOM   11915 H  H    . LEU   B 1 160 ? 36.038 18.497  56.064 1.00 12.05 ? 160  LEU   B H    1 
ATOM   11916 H  HA   . LEU   B 1 160 ? 33.829 19.606  57.356 1.00 12.44 ? 160  LEU   B HA   1 
ATOM   11917 H  HB2  . LEU   B 1 160 ? 33.775 17.311  57.442 1.00 11.03 ? 160  LEU   B HB2  1 
ATOM   11918 H  HB3  . LEU   B 1 160 ? 35.253 17.256  57.935 1.00 11.03 ? 160  LEU   B HB3  1 
ATOM   11919 H  HG   . LEU   B 1 160 ? 33.506 18.580  59.630 1.00 13.76 ? 160  LEU   B HG   1 
ATOM   11920 H  HD11 . LEU   B 1 160 ? 32.654 16.593  60.561 1.00 14.63 ? 160  LEU   B HD11 1 
ATOM   11921 H  HD12 . LEU   B 1 160 ? 32.192 16.733  59.053 1.00 14.63 ? 160  LEU   B HD12 1 
ATOM   11922 H  HD13 . LEU   B 1 160 ? 33.381 15.758  59.430 1.00 14.63 ? 160  LEU   B HD13 1 
ATOM   11923 H  HD21 . LEU   B 1 160 ? 34.788 17.566  61.311 1.00 16.15 ? 160  LEU   B HD21 1 
ATOM   11924 H  HD22 . LEU   B 1 160 ? 35.585 16.755  60.209 1.00 16.15 ? 160  LEU   B HD22 1 
ATOM   11925 H  HD23 . LEU   B 1 160 ? 35.726 18.330  60.290 1.00 16.15 ? 160  LEU   B HD23 1 
ATOM   11926 N  N    . CYS   B 1 161 ? 35.268 21.040  58.835 1.00 12.97 ? 161  CYS   B N    1 
ATOM   11927 C  CA   . CYS   B 1 161 ? 36.288 21.879  59.506 1.00 10.54 ? 161  CYS   B CA   1 
ATOM   11928 C  C    . CYS   B 1 161 ? 35.706 22.711  60.646 1.00 12.91 ? 161  CYS   B C    1 
ATOM   11929 O  O    . CYS   B 1 161 ? 34.488 22.640  60.883 1.00 12.84 ? 161  CYS   B O    1 
ATOM   11930 C  CB   . CYS   B 1 161 ? 36.908 22.850  58.510 1.00 11.33 ? 161  CYS   B CB   1 
ATOM   11931 S  SG   . CYS   B 1 161 ? 35.723 24.058  57.850 1.00 13.98 ? 161  CYS   B SG   1 
ATOM   11932 H  H    . CYS   B 1 161 ? 34.452 21.304  58.898 1.00 15.57 ? 161  CYS   B H    1 
ATOM   11933 H  HA   . CYS   B 1 161 ? 36.948 21.265  59.865 1.00 12.65 ? 161  CYS   B HA   1 
ATOM   11934 H  HB2  . CYS   B 1 161 ? 37.637 23.324  58.941 1.00 13.60 ? 161  CYS   B HB2  1 
ATOM   11935 H  HB3  . CYS   B 1 161 ? 37.292 22.348  57.774 1.00 13.60 ? 161  CYS   B HB3  1 
ATOM   11936 H  HG   . CYS   B 1 161 ? 36.282 24.787  57.078 1.00 16.78 ? 161  CYS   B HG   1 
ATOM   11937 N  N    . ILE   B 1 162 ? 36.584 23.429  61.339 1.00 13.20 ? 162  ILE   B N    1 
ATOM   11938 C  CA   . ILE   B 1 162 ? 36.119 24.379  62.379 1.00 13.60 ? 162  ILE   B CA   1 
ATOM   11939 C  C    . ILE   B 1 162 ? 36.485 25.778  61.888 1.00 15.37 ? 162  ILE   B C    1 
ATOM   11940 O  O    . ILE   B 1 162 ? 37.406 25.897  61.063 1.00 14.03 ? 162  ILE   B O    1 
ATOM   11941 C  CB   . ILE   B 1 162 ? 36.774 24.081  63.741 1.00 12.86 ? 162  ILE   B CB   1 
ATOM   11942 C  CG1  . ILE   B 1 162 ? 38.291 23.924  63.614 1.00 15.82 ? 162  ILE   B CG1  1 
ATOM   11943 C  CG2  . ILE   B 1 162 ? 36.132 22.871  64.400 1.00 15.31 ? 162  ILE   B CG2  1 
ATOM   11944 C  CD1  . ILE   B 1 162 ? 39.034 24.100  64.915 1.00 15.13 ? 162  ILE   B CD1  1 
ATOM   11945 H  H    . ILE   B 1 162 ? 37.437 23.392  61.235 1.00 15.84 ? 162  ILE   B H    1 
ATOM   11946 H  HA   . ILE   B 1 162 ? 35.162 24.299  62.514 1.00 16.33 ? 162  ILE   B HA   1 
ATOM   11947 H  HB   . ILE   B 1 162 ? 36.618 24.844  64.319 1.00 15.43 ? 162  ILE   B HB   1 
ATOM   11948 H  HG12 . ILE   B 1 162 ? 38.487 23.044  63.256 1.00 18.99 ? 162  ILE   B HG12 1 
ATOM   11949 H  HG13 . ILE   B 1 162 ? 38.622 24.572  62.972 1.00 18.99 ? 162  ILE   B HG13 1 
ATOM   11950 H  HG21 . ILE   B 1 162 ? 36.560 22.703  65.254 1.00 18.38 ? 162  ILE   B HG21 1 
ATOM   11951 H  HG22 . ILE   B 1 162 ? 35.187 23.042  64.540 1.00 18.38 ? 162  ILE   B HG22 1 
ATOM   11952 H  HG23 . ILE   B 1 162 ? 36.239 22.096  63.827 1.00 18.38 ? 162  ILE   B HG23 1 
ATOM   11953 H  HD11 . ILE   B 1 162 ? 39.985 23.988  64.762 1.00 18.16 ? 162  ILE   B HD11 1 
ATOM   11954 H  HD12 . ILE   B 1 162 ? 38.866 24.988  65.266 1.00 18.16 ? 162  ILE   B HD12 1 
ATOM   11955 H  HD13 . ILE   B 1 162 ? 38.729 23.437  65.554 1.00 18.16 ? 162  ILE   B HD13 1 
ATOM   11956 N  N    . GLY   B 1 163 ? 35.758 26.789  62.353 1.00 16.59 ? 163  GLY   B N    1 
ATOM   11957 C  CA   . GLY   B 1 163 ? 36.122 28.174  62.023 1.00 13.50 ? 163  GLY   B CA   1 
ATOM   11958 C  C    . GLY   B 1 163 ? 36.938 28.769  63.157 1.00 14.66 ? 163  GLY   B C    1 
ATOM   11959 O  O    . GLY   B 1 163 ? 37.303 28.028  64.082 1.00 14.17 ? 163  GLY   B O    1 
ATOM   11960 H  H    . GLY   B 1 163 ? 35.063 26.703  62.852 1.00 19.91 ? 163  GLY   B H    1 
ATOM   11961 H  HA2  . GLY   B 1 163 ? 36.632 28.196  61.198 1.00 16.20 ? 163  GLY   B HA2  1 
ATOM   11962 H  HA3  . GLY   B 1 163 ? 35.322 28.702  61.876 1.00 16.20 ? 163  GLY   B HA3  1 
ATOM   11963 N  N    . PRO   B 1 164 ? 37.221 30.084  63.130 1.00 14.90 ? 164  PRO   B N    1 
ATOM   11964 C  CA   . PRO   B 1 164 ? 37.975 30.733  64.207 1.00 16.18 ? 164  PRO   B CA   1 
ATOM   11965 C  C    . PRO   B 1 164 ? 37.419 30.497  65.629 1.00 15.52 ? 164  PRO   B C    1 
ATOM   11966 O  O    . PRO   B 1 164 ? 38.190 30.468  66.554 1.00 17.27 ? 164  PRO   B O    1 
ATOM   11967 C  CB   . PRO   B 1 164 ? 37.878 32.216  63.811 1.00 19.61 ? 164  PRO   B CB   1 
ATOM   11968 C  CG   . PRO   B 1 164 ? 37.754 32.191  62.306 1.00 20.77 ? 164  PRO   B CG   1 
ATOM   11969 C  CD   . PRO   B 1 164 ? 36.874 30.992  62.035 1.00 14.76 ? 164  PRO   B CD   1 
ATOM   11970 H  HA   . PRO   B 1 164 ? 38.875 30.379  64.276 1.00 19.41 ? 164  PRO   B HA   1 
ATOM   11971 H  HB2  . PRO   B 1 164 ? 37.111 32.643  64.223 1.00 23.53 ? 164  PRO   B HB2  1 
ATOM   11972 H  HB3  . PRO   B 1 164 ? 38.663 32.710  64.094 1.00 23.53 ? 164  PRO   B HB3  1 
ATOM   11973 H  HG2  . PRO   B 1 164 ? 37.356 33.008  61.968 1.00 24.93 ? 164  PRO   B HG2  1 
ATOM   11974 H  HG3  . PRO   B 1 164 ? 38.620 32.100  61.879 1.00 24.93 ? 164  PRO   B HG3  1 
ATOM   11975 H  HD2  . PRO   B 1 164 ? 35.933 31.226  62.046 1.00 17.72 ? 164  PRO   B HD2  1 
ATOM   11976 H  HD3  . PRO   B 1 164 ? 37.059 30.598  61.168 1.00 17.72 ? 164  PRO   B HD3  1 
ATOM   11977 N  N    . ALA   B 1 165 ? 36.101 30.310  65.758 1.00 16.71 ? 165  ALA   B N    1 
ATOM   11978 C  CA   . ALA   B 1 165 ? 35.489 30.120  67.097 1.00 15.08 ? 165  ALA   B CA   1 
ATOM   11979 C  C    . ALA   B 1 165 ? 35.965 28.801  67.714 1.00 12.57 ? 165  ALA   B C    1 
ATOM   11980 O  O    . ALA   B 1 165 ? 36.287 28.785  68.906 1.00 13.56 ? 165  ALA   B O    1 
ATOM   11981 C  CB   . ALA   B 1 165 ? 33.984 30.150  66.996 1.00 12.19 ? 165  ALA   B CB   1 
ATOM   11982 H  H    . ALA   B 1 165 ? 35.546 30.289  65.101 1.00 20.05 ? 165  ALA   B H    1 
ATOM   11983 H  HA   . ALA   B 1 165 ? 35.769 30.847  67.675 1.00 18.10 ? 165  ALA   B HA   1 
ATOM   11984 H  HB1  . ALA   B 1 165 ? 33.598 30.025  67.877 1.00 14.63 ? 165  ALA   B HB1  1 
ATOM   11985 H  HB2  . ALA   B 1 165 ? 33.701 31.006  66.638 1.00 14.63 ? 165  ALA   B HB2  1 
ATOM   11986 H  HB3  . ALA   B 1 165 ? 33.685 29.439  66.408 1.00 14.63 ? 165  ALA   B HB3  1 
ATOM   11987 N  N    . GLY   B 1 166 ? 35.966 27.731  66.920 1.00 12.71 ? 166  GLY   B N    1 
ATOM   11988 C  CA   . GLY   B 1 166 ? 36.463 26.437  67.419 1.00 15.35 ? 166  GLY   B CA   1 
ATOM   11989 C  C    . GLY   B 1 166 ? 37.946 26.504  67.735 1.00 15.49 ? 166  GLY   B C    1 
ATOM   11990 O  O    . GLY   B 1 166 ? 38.364 25.914  68.740 1.00 13.61 ? 166  GLY   B O    1 
ATOM   11991 H  H    . GLY   B 1 166 ? 35.690 27.726  66.105 1.00 15.26 ? 166  GLY   B H    1 
ATOM   11992 H  HA2  . GLY   B 1 166 ? 35.971 26.184  68.216 1.00 18.42 ? 166  GLY   B HA2  1 
ATOM   11993 H  HA3  . GLY   B 1 166 ? 36.302 25.748  66.755 1.00 18.42 ? 166  GLY   B HA3  1 
ATOM   11994 N  N    . GLU   B 1 167 ? 38.710 27.199  66.888 1.00 14.21 ? 167  GLU   B N    1 
ATOM   11995 C  CA   . GLU   B 1 167 ? 40.164 27.366  67.137 1.00 14.48 ? 167  GLU   B CA   1 
ATOM   11996 C  C    . GLU   B 1 167 ? 40.362 28.046  68.495 1.00 13.94 ? 167  GLU   B C    1 
ATOM   11997 O  O    . GLU   B 1 167 ? 41.332 27.703  69.184 1.00 16.34 ? 167  GLU   B O    1 
ATOM   11998 C  CB   . GLU   B 1 167 ? 40.810 28.202  66.029 1.00 15.18 ? 167  GLU   B CB   1 
ATOM   11999 C  CG   . GLU   B 1 167 ? 40.643 27.640  64.630 1.00 16.92 ? 167  GLU   B CG   1 
ATOM   12000 C  CD   . GLU   B 1 167 ? 41.151 28.578  63.548 1.00 18.37 ? 167  GLU   B CD   1 
ATOM   12001 O  OE1  . GLU   B 1 167 ? 41.421 29.750  63.869 1.00 16.35 ? 167  GLU   B OE1  1 
ATOM   12002 O  OE2  . GLU   B 1 167 ? 41.273 28.139  62.389 1.00 16.97 ? 167  GLU   B OE2  1 
ATOM   12003 H  H    . GLU   B 1 167 ? 38.420 27.579  66.173 1.00 17.05 ? 167  GLU   B H    1 
ATOM   12004 H  HA   . GLU   B 1 167 ? 40.589 26.494  67.142 1.00 17.38 ? 167  GLU   B HA   1 
ATOM   12005 H  HB2  . GLU   B 1 167 ? 40.432 29.095  66.053 1.00 18.21 ? 167  GLU   B HB2  1 
ATOM   12006 H  HB3  . GLU   B 1 167 ? 41.757 28.290  66.218 1.00 18.21 ? 167  GLU   B HB3  1 
ATOM   12007 H  HG2  . GLU   B 1 167 ? 41.117 26.796  64.567 1.00 20.30 ? 167  GLU   B HG2  1 
ATOM   12008 H  HG3  . GLU   B 1 167 ? 39.705 27.451  64.473 1.00 20.30 ? 167  GLU   B HG3  1 
ATOM   12009 N  N    . ARG   B 1 168 ? 39.458 28.961  68.867 1.00 14.84 ? 168  ARG   B N    1 
ATOM   12010 C  CA   . ARG   B 1 168 ? 39.612 29.726  70.139 1.00 15.58 ? 168  ARG   B CA   1 
ATOM   12011 C  C    . ARG   B 1 168 ? 38.891 29.010  71.289 1.00 13.47 ? 168  ARG   B C    1 
ATOM   12012 O  O    . ARG   B 1 168 ? 38.832 29.597  72.379 1.00 17.39 ? 168  ARG   B O    1 
ATOM   12013 C  CB   . ARG   B 1 168 ? 39.122 31.166  69.945 1.00 16.71 ? 168  ARG   B CB   1 
ATOM   12014 C  CG   . ARG   B 1 168 ? 40.035 32.005  69.062 1.00 18.80 ? 168  ARG   B CG   1 
ATOM   12015 C  CD   . ARG   B 1 168 ? 39.338 33.208  68.459 1.00 22.06 ? 168  ARG   B CD   1 
ATOM   12016 N  NE   . ARG   B 1 168 ? 40.217 33.954  67.572 1.00 24.69 ? 168  ARG   B NE   1 
ATOM   12017 C  CZ   . ARG   B 1 168 ? 41.044 34.916  67.964 1.00 29.86 ? 168  ARG   B CZ   1 
ATOM   12018 N  NH1  . ARG   B 1 168 ? 41.085 35.280  69.233 1.00 29.32 ? 168  ARG   B NH1  1 
ATOM   12019 N  NH2  . ARG   B 1 168 ? 41.823 35.516  67.081 1.00 36.11 ? 168  ARG   B NH2  1 
ATOM   12020 H  H    . ARG   B 1 168 ? 38.755 29.159  68.412 1.00 17.81 ? 168  ARG   B H    1 
ATOM   12021 H  HA   . ARG   B 1 168 ? 40.551 29.768  70.380 1.00 18.69 ? 168  ARG   B HA   1 
ATOM   12022 H  HB2  . ARG   B 1 168 ? 38.234 31.148  69.555 1.00 20.05 ? 168  ARG   B HB2  1 
ATOM   12023 H  HB3  . ARG   B 1 168 ? 39.042 31.592  70.813 1.00 20.05 ? 168  ARG   B HB3  1 
ATOM   12024 H  HG2  . ARG   B 1 168 ? 40.794 32.307  69.585 1.00 22.57 ? 168  ARG   B HG2  1 
ATOM   12025 H  HG3  . ARG   B 1 168 ? 40.385 31.449  68.348 1.00 22.57 ? 168  ARG   B HG3  1 
ATOM   12026 H  HD2  . ARG   B 1 168 ? 38.555 32.915  67.967 1.00 26.47 ? 168  ARG   B HD2  1 
ATOM   12027 H  HD3  . ARG   B 1 168 ? 39.025 33.790  69.169 1.00 26.47 ? 168  ARG   B HD3  1 
ATOM   12028 H  HE   . ARG   B 1 168 ? 40.200 33.758  66.735 1.00 29.64 ? 168  ARG   B HE   1 
ATOM   12029 H  HH11 . ARG   B 1 168 ? 40.575 34.894  69.808 1.00 35.19 ? 168  ARG   B HH11 1 
ATOM   12030 H  HH12 . ARG   B 1 168 ? 41.622 35.903  69.484 1.00 35.19 ? 168  ARG   B HH12 1 
ATOM   12031 H  HH21 . ARG   B 1 168 ? 41.794 35.283  66.254 1.00 43.33 ? 168  ARG   B HH21 1 
ATOM   12032 H  HH22 . ARG   B 1 168 ? 42.359 36.139  67.334 1.00 43.33 ? 168  ARG   B HH22 1 
ATOM   12033 N  N    . LEU   B 1 169 ? 38.349 27.815  71.049 1.00 13.11 ? 169  LEU   B N    1 
ATOM   12034 C  CA   . LEU   B 1 169 ? 37.733 26.990  72.129 1.00 15.89 ? 169  LEU   B CA   1 
ATOM   12035 C  C    . LEU   B 1 169 ? 36.432 27.601  72.670 1.00 16.43 ? 169  LEU   B C    1 
ATOM   12036 O  O    . LEU   B 1 169 ? 36.097 27.295  73.824 1.00 15.26 ? 169  LEU   B O    1 
ATOM   12037 C  CB   . LEU   B 1 169 ? 38.755 26.787  73.253 1.00 16.20 ? 169  LEU   B CB   1 
ATOM   12038 C  CG   . LEU   B 1 169 ? 40.083 26.166  72.824 1.00 18.19 ? 169  LEU   B CG   1 
ATOM   12039 C  CD1  . LEU   B 1 169 ? 40.860 25.664  74.030 1.00 16.70 ? 169  LEU   B CD1  1 
ATOM   12040 C  CD2  . LEU   B 1 169 ? 39.859 25.037  71.830 1.00 18.75 ? 169  LEU   B CD2  1 
ATOM   12041 H  H    . LEU   B 1 169 ? 38.321 27.452  70.270 1.00 15.74 ? 169  LEU   B H    1 
ATOM   12042 H  HA   . LEU   B 1 169 ? 37.489 26.131  71.749 1.00 19.07 ? 169  LEU   B HA   1 
ATOM   12043 H  HB2  . LEU   B 1 169 ? 38.935 27.646  73.665 1.00 19.44 ? 169  LEU   B HB2  1 
ATOM   12044 H  HB3  . LEU   B 1 169 ? 38.356 26.223  73.934 1.00 19.44 ? 169  LEU   B HB3  1 
ATOM   12045 H  HG   . LEU   B 1 169 ? 40.607 26.856  72.388 1.00 21.83 ? 169  LEU   B HG   1 
ATOM   12046 H  HD11 . LEU   B 1 169 ? 41.698 25.274  73.736 1.00 20.05 ? 169  LEU   B HD11 1 
ATOM   12047 H  HD12 . LEU   B 1 169 ? 41.041 26.405  74.630 1.00 20.05 ? 169  LEU   B HD12 1 
ATOM   12048 H  HD13 . LEU   B 1 169 ? 40.337 24.992  74.495 1.00 20.05 ? 169  LEU   B HD13 1 
ATOM   12049 H  HD21 . LEU   B 1 169 ? 40.714 24.658  71.572 1.00 22.50 ? 169  LEU   B HD21 1 
ATOM   12050 H  HD22 . LEU   B 1 169 ? 39.311 24.349  72.239 1.00 22.50 ? 169  LEU   B HD22 1 
ATOM   12051 H  HD23 . LEU   B 1 169 ? 39.409 25.383  71.044 1.00 22.50 ? 169  LEU   B HD23 1 
ATOM   12052 N  N    . SER   B 1 170 ? 35.720 28.394  71.870 1.00 14.17 ? 170  SER   B N    1 
ATOM   12053 C  CA   . SER   B 1 170 ? 34.398 28.906  72.323 1.00 14.71 ? 170  SER   B CA   1 
ATOM   12054 C  C    . SER   B 1 170 ? 33.459 27.724  72.598 1.00 11.73 ? 170  SER   B C    1 
ATOM   12055 O  O    . SER   B 1 170 ? 33.411 26.807  71.778 1.00 15.00 ? 170  SER   B O    1 
ATOM   12056 C  CB   . SER   B 1 170 ? 33.792 29.857  71.325 1.00 16.00 ? 170  SER   B CB   1 
ATOM   12057 O  OG   . SER   B 1 170 ? 32.422 30.092  71.607 1.00 15.95 ? 170  SER   B OG   1 
ATOM   12058 H  H    . SER   B 1 170 ? 35.963 28.648  71.085 1.00 17.01 ? 170  SER   B H    1 
ATOM   12059 H  HA   . SER   B 1 170 ? 34.529 29.408  73.142 1.00 17.66 ? 170  SER   B HA   1 
ATOM   12060 H  HB2  . SER   B 1 170 ? 34.277 30.697  71.340 1.00 19.20 ? 170  SER   B HB2  1 
ATOM   12061 H  HB3  . SER   B 1 170 ? 33.883 29.493  70.431 1.00 19.20 ? 170  SER   B HB3  1 
ATOM   12062 H  HG   . SER   B 1 170 ? 32.355 30.580  72.287 1.00 19.15 ? 170  SER   B HG   1 
ATOM   12063 N  N    . LEU   B 1 171 ? 32.730 27.769  73.716 1.00 14.11 ? 171  LEU   B N    1 
ATOM   12064 C  CA   . LEU   B 1 171 ? 31.834 26.642  74.090 1.00 12.94 ? 171  LEU   B CA   1 
ATOM   12065 C  C    . LEU   B 1 171 ? 30.586 26.633  73.198 1.00 14.04 ? 171  LEU   B C    1 
ATOM   12066 O  O    . LEU   B 1 171 ? 29.754 25.745  73.394 1.00 11.96 ? 171  LEU   B O    1 
ATOM   12067 C  CB   . LEU   B 1 171 ? 31.452 26.765  75.570 1.00 14.01 ? 171  LEU   B CB   1 
ATOM   12068 C  CG   . LEU   B 1 171 ? 32.611 26.688  76.563 1.00 16.11 ? 171  LEU   B CG   1 
ATOM   12069 C  CD1  . LEU   B 1 171 ? 32.092 26.569  77.988 1.00 17.79 ? 171  LEU   B CD1  1 
ATOM   12070 C  CD2  . LEU   B 1 171 ? 33.530 25.523  76.234 1.00 18.58 ? 171  LEU   B CD2  1 
ATOM   12071 H  H    . LEU   B 1 171 ? 32.732 28.427  74.270 1.00 16.94 ? 171  LEU   B H    1 
ATOM   12072 H  HA   . LEU   B 1 171 ? 32.299 25.801  73.956 1.00 15.53 ? 171  LEU   B HA   1 
ATOM   12073 H  HB2  . LEU   B 1 171 ? 30.993 27.610  75.699 1.00 16.82 ? 171  LEU   B HB2  1 
ATOM   12074 H  HB3  . LEU   B 1 171 ? 30.818 26.062  75.783 1.00 16.82 ? 171  LEU   B HB3  1 
ATOM   12075 H  HG   . LEU   B 1 171 ? 33.123 27.509  76.490 1.00 19.34 ? 171  LEU   B HG   1 
ATOM   12076 H  HD11 . LEU   B 1 171 ? 32.841 26.521  78.602 1.00 21.35 ? 171  LEU   B HD11 1 
ATOM   12077 H  HD12 . LEU   B 1 171 ? 31.549 27.344  78.200 1.00 21.35 ? 171  LEU   B HD12 1 
ATOM   12078 H  HD13 . LEU   B 1 171 ? 31.555 25.766  78.071 1.00 21.35 ? 171  LEU   B HD13 1 
ATOM   12079 H  HD21 . LEU   B 1 171 ? 34.257 25.493  76.875 1.00 22.30 ? 171  LEU   B HD21 1 
ATOM   12080 H  HD22 . LEU   B 1 171 ? 33.029 24.694  76.275 1.00 22.30 ? 171  LEU   B HD22 1 
ATOM   12081 H  HD23 . LEU   B 1 171 ? 33.892 25.638  75.341 1.00 22.30 ? 171  LEU   B HD23 1 
ATOM   12082 N  N    . MET   B 1 172 ? 30.462 27.582  72.265 1.00 13.17 ? 172  MET   B N    1 
ATOM   12083 C  CA   . MET   B 1 172 ? 29.334 27.525  71.294 1.00 12.20 ? 172  MET   B CA   1 
ATOM   12084 C  C    . MET   B 1 172 ? 29.887 27.214  69.893 1.00 14.77 ? 172  MET   B C    1 
ATOM   12085 O  O    . MET   B 1 172 ? 29.149 27.385  68.911 1.00 13.98 ? 172  MET   B O    1 
ATOM   12086 C  CB   . MET   B 1 172 ? 28.510 28.818  71.286 1.00 12.35 ? 172  MET   B CB   1 
ATOM   12087 C  CG   . MET   B 1 172 ? 29.244 30.038  70.783 1.00 13.82 ? 172  MET   B CG   1 
ATOM   12088 S  SD   . MET   B 1 172 ? 28.099 31.440  70.664 1.00 15.57 ? 172  MET   B SD   1 
ATOM   12089 C  CE   . MET   B 1 172 ? 27.822 31.782  72.401 1.00 17.13 ? 172  MET   B CE   1 
ATOM   12090 H  H    . MET   B 1 172 ? 30.995 28.250  72.169 1.00 15.80 ? 172  MET   B H    1 
ATOM   12091 H  HA   . MET   B 1 172 ? 28.730 26.817  71.569 1.00 14.64 ? 172  MET   B HA   1 
ATOM   12092 H  HB2  . MET   B 1 172 ? 27.723 28.681  70.736 1.00 14.82 ? 172  MET   B HB2  1 
ATOM   12093 H  HB3  . MET   B 1 172 ? 28.199 28.993  72.188 1.00 14.82 ? 172  MET   B HB3  1 
ATOM   12094 H  HG2  . MET   B 1 172 ? 29.974 30.256  71.383 1.00 16.59 ? 172  MET   B HG2  1 
ATOM   12095 H  HG3  . MET   B 1 172 ? 29.635 29.855  69.915 1.00 16.59 ? 172  MET   B HG3  1 
ATOM   12096 H  HE1  . MET   B 1 172 ? 27.211 32.530  72.490 1.00 20.56 ? 172  MET   B HE1  1 
ATOM   12097 H  HE2  . MET   B 1 172 ? 27.439 31.000  72.828 1.00 20.56 ? 172  MET   B HE2  1 
ATOM   12098 H  HE3  . MET   B 1 172 ? 28.666 32.001  72.826 1.00 20.56 ? 172  MET   B HE3  1 
ATOM   12099 N  N    . ALA   B 1 173 ? 31.121 26.711  69.835 1.00 11.43 ? 173  ALA   B N    1 
ATOM   12100 C  CA   . ALA   B 1 173 ? 31.762 26.379  68.541 1.00 14.27 ? 173  ALA   B CA   1 
ATOM   12101 C  C    . ALA   B 1 173 ? 31.099 25.168  67.886 1.00 15.97 ? 173  ALA   B C    1 
ATOM   12102 O  O    . ALA   B 1 173 ? 30.741 24.219  68.595 1.00 14.18 ? 173  ALA   B O    1 
ATOM   12103 C  CB   . ALA   B 1 173 ? 33.229 26.135  68.749 1.00 13.70 ? 173  ALA   B CB   1 
ATOM   12104 H  H    . ALA   B 1 173 ? 31.609 26.552  70.525 1.00 13.71 ? 173  ALA   B H    1 
ATOM   12105 H  HA   . ALA   B 1 173 ? 31.648 27.132  67.940 1.00 17.13 ? 173  ALA   B HA   1 
ATOM   12106 H  HB1  . ALA   B 1 173 ? 33.645 25.918  67.900 1.00 16.44 ? 173  ALA   B HB1  1 
ATOM   12107 H  HB2  . ALA   B 1 173 ? 33.641 26.933  69.116 1.00 16.44 ? 173  ALA   B HB2  1 
ATOM   12108 H  HB3  . ALA   B 1 173 ? 33.350 25.396  69.366 1.00 16.44 ? 173  ALA   B HB3  1 
ATOM   12109 N  N    . ALA   B 1 174 ? 31.020 25.194  66.559 1.00 11.74 ? 174  ALA   B N    1 
ATOM   12110 C  CA   . ALA   B 1 174 ? 30.339 24.121  65.818 1.00 12.29 ? 174  ALA   B CA   1 
ATOM   12111 C  C    . ALA   B 1 174 ? 31.331 23.382  64.920 1.00 14.18 ? 174  ALA   B C    1 
ATOM   12112 O  O    . ALA   B 1 174 ? 32.448 23.884  64.735 1.00 13.86 ? 174  ALA   B O    1 
ATOM   12113 C  CB   . ALA   B 1 174 ? 29.271 24.753  64.968 1.00 14.46 ? 174  ALA   B CB   1 
ATOM   12114 H  H    . ALA   B 1 174 ? 31.350 25.817  66.067 1.00 14.09 ? 174  ALA   B H    1 
ATOM   12115 H  HA   . ALA   B 1 174 ? 29.954 23.483  66.439 1.00 14.75 ? 174  ALA   B HA   1 
ATOM   12116 H  HB1  . ALA   B 1 174 ? 28.806 24.064  64.468 1.00 17.36 ? 174  ALA   B HB1  1 
ATOM   12117 H  HB2  . ALA   B 1 174 ? 28.640 25.221  65.536 1.00 17.36 ? 174  ALA   B HB2  1 
ATOM   12118 H  HB3  . ALA   B 1 174 ? 29.678 25.381  64.351 1.00 17.36 ? 174  ALA   B HB3  1 
ATOM   12119 N  N    . VAL   B 1 175 ? 30.916 22.227  64.409 1.00 11.49 ? 175  VAL   B N    1 
ATOM   12120 C  CA   . VAL   B 1 175 ? 31.739 21.499  63.404 1.00 14.32 ? 175  VAL   B CA   1 
ATOM   12121 C  C    . VAL   B 1 175 ? 31.030 21.706  62.063 1.00 13.63 ? 175  VAL   B C    1 
ATOM   12122 O  O    . VAL   B 1 175 ? 29.851 21.347  61.959 1.00 12.12 ? 175  VAL   B O    1 
ATOM   12123 C  CB   . VAL   B 1 175 ? 31.883 20.010  63.750 1.00 12.29 ? 175  VAL   B CB   1 
ATOM   12124 C  CG1  . VAL   B 1 175 ? 32.553 19.240  62.624 1.00 12.51 ? 175  VAL   B CG1  1 
ATOM   12125 C  CG2  . VAL   B 1 175 ? 32.633 19.817  65.059 1.00 15.35 ? 175  VAL   B CG2  1 
ATOM   12126 H  H    . VAL   B 1 175 ? 30.176 21.842  64.617 1.00 13.80 ? 175  VAL   B H    1 
ATOM   12127 H  HA   . VAL   B 1 175 ? 32.647 21.839  63.380 1.00 17.19 ? 175  VAL   B HA   1 
ATOM   12128 H  HB   . VAL   B 1 175 ? 30.988 19.652  63.862 1.00 14.76 ? 175  VAL   B HB   1 
ATOM   12129 H  HG11 . VAL   B 1 175 ? 32.630 18.305  62.872 1.00 15.02 ? 175  VAL   B HG11 1 
ATOM   12130 H  HG12 . VAL   B 1 175 ? 32.020 19.318  61.817 1.00 15.02 ? 175  VAL   B HG12 1 
ATOM   12131 H  HG13 . VAL   B 1 175 ? 33.437 19.605  62.464 1.00 15.02 ? 175  VAL   B HG13 1 
ATOM   12132 H  HG21 . VAL   B 1 175 ? 32.709 18.869  65.252 1.00 18.42 ? 175  VAL   B HG21 1 
ATOM   12133 H  HG22 . VAL   B 1 175 ? 33.520 20.203  64.984 1.00 18.42 ? 175  VAL   B HG22 1 
ATOM   12134 H  HG23 . VAL   B 1 175 ? 32.149 20.255  65.777 1.00 18.42 ? 175  VAL   B HG23 1 
ATOM   12135 N  N    . MET   B 1 176 ? 31.729 22.273  61.083 1.00 13.79 ? 176  MET   B N    1 
ATOM   12136 C  CA   . MET   B 1 176 ? 31.069 22.619  59.802 1.00 13.30 ? 176  MET   B CA   1 
ATOM   12137 C  C    . MET   B 1 176 ? 31.448 21.618  58.710 1.00 11.33 ? 176  MET   B C    1 
ATOM   12138 O  O    . MET   B 1 176 ? 32.551 21.065  58.778 1.00 11.73 ? 176  MET   B O    1 
ATOM   12139 C  CB   . MET   B 1 176 ? 31.509 24.023  59.372 1.00 12.30 ? 176  MET   B CB   1 
ATOM   12140 C  CG   . MET   B 1 176 ? 31.424 25.046  60.486 1.00 12.47 ? 176  MET   B CG   1 
ATOM   12141 S  SD   . MET   B 1 176 ? 29.707 25.440  60.900 1.00 14.20 ? 176  MET   B SD   1 
ATOM   12142 C  CE   . MET   B 1 176 ? 28.991 25.551  59.261 1.00 16.19 ? 176  MET   B CE   1 
ATOM   12143 H  H    . MET   B 1 176 ? 32.566 22.466  61.126 1.00 16.55 ? 176  MET   B H    1 
ATOM   12144 H  HA   . MET   B 1 176 ? 30.108 22.592  59.930 1.00 15.96 ? 176  MET   B HA   1 
ATOM   12145 H  HB2  . MET   B 1 176 ? 32.422 23.983  59.047 1.00 14.77 ? 176  MET   B HB2  1 
ATOM   12146 H  HB3  . MET   B 1 176 ? 30.956 24.315  58.630 1.00 14.77 ? 176  MET   B HB3  1 
ATOM   12147 H  HG2  . MET   B 1 176 ? 31.878 24.706  61.273 1.00 14.97 ? 176  MET   B HG2  1 
ATOM   12148 H  HG3  . MET   B 1 176 ? 31.887 25.855  60.219 1.00 14.97 ? 176  MET   B HG3  1 
ATOM   12149 H  HE1  . MET   B 1 176 ? 28.047 25.763  59.334 1.00 19.43 ? 176  MET   B HE1  1 
ATOM   12150 H  HE2  . MET   B 1 176 ? 29.441 26.248  58.758 1.00 19.43 ? 176  MET   B HE2  1 
ATOM   12151 H  HE3  . MET   B 1 176 ? 29.097 24.702  58.803 1.00 19.43 ? 176  MET   B HE3  1 
ATOM   12152 N  N    . ASN   B 1 177 ? 30.544 21.396  57.756 1.00 12.32 ? 177  ASN   B N    1 
ATOM   12153 C  CA   . ASN   B 1 177 ? 30.884 20.541  56.588 1.00 10.17 ? 177  ASN   B CA   1 
ATOM   12154 C  C    . ASN   B 1 177 ? 30.100 21.062  55.378 1.00 10.51 ? 177  ASN   B C    1 
ATOM   12155 O  O    . ASN   B 1 177 ? 29.004 21.599  55.567 1.00 10.05 ? 177  ASN   B O    1 
ATOM   12156 C  CB   . ASN   B 1 177 ? 30.665 19.051  56.868 1.00 13.55 ? 177  ASN   B CB   1 
ATOM   12157 C  CG   . ASN   B 1 177 ? 29.228 18.704  57.182 1.00 10.95 ? 177  ASN   B CG   1 
ATOM   12158 O  OD1  . ASN   B 1 177 ? 28.796 18.835  58.323 1.00 11.00 ? 177  ASN   B OD1  1 
ATOM   12159 N  ND2  . ASN   B 1 177 ? 28.490 18.254  56.181 1.00 13.73 ? 177  ASN   B ND2  1 
ATOM   12160 H  H    . ASN   B 1 177 ? 29.746 21.716  57.754 1.00 14.78 ? 177  ASN   B H    1 
ATOM   12161 H  HA   . ASN   B 1 177 ? 31.833 20.603  56.396 1.00 12.20 ? 177  ASN   B HA   1 
ATOM   12162 H  HB2  . ASN   B 1 177 ? 30.953 18.538  56.097 1.00 16.26 ? 177  ASN   B HB2  1 
ATOM   12163 H  HB3  . ASN   B 1 177 ? 31.226 18.783  57.613 1.00 16.26 ? 177  ASN   B HB3  1 
ATOM   12164 H  HD21 . ASN   B 1 177 ? 27.668 18.038  56.316 1.00 16.48 ? 177  ASN   B HD21 1 
ATOM   12165 H  HD22 . ASN   B 1 177 ? 28.832 18.177  55.396 1.00 16.48 ? 177  ASN   B HD22 1 
ATOM   12166 N  N    . ASP   B 1 178 ? 30.685 20.931  54.190 1.00 10.84 ? 178  ASP   B N    1 
ATOM   12167 C  CA   . ASP   B 1 178 ? 30.010 21.406  52.955 1.00 10.81 ? 178  ASP   B CA   1 
ATOM   12168 C  C    . ASP   B 1 178 ? 29.664 22.896  53.118 1.00 12.43 ? 178  ASP   B C    1 
ATOM   12169 O  O    . ASP   B 1 178 ? 28.574 23.285  52.674 1.00 13.20 ? 178  ASP   B O    1 
ATOM   12170 C  CB   . ASP   B 1 178 ? 28.867 20.460  52.577 1.00 13.61 ? 178  ASP   B CB   1 
ATOM   12171 C  CG   . ASP   B 1 178 ? 29.334 19.014  52.493 1.00 14.01 ? 178  ASP   B CG   1 
ATOM   12172 O  OD1  . ASP   B 1 178 ? 30.191 18.726  51.636 1.00 13.83 ? 178  ASP   B OD1  1 
ATOM   12173 O  OD2  . ASP   B 1 178 ? 28.853 18.191  53.294 1.00 12.75 ? 178  ASP   B OD2  1 
ATOM   12174 H  H    . ASP   B 1 178 ? 31.459 20.578  54.066 1.00 13.01 ? 178  ASP   B H    1 
ATOM   12175 H  HA   . ASP   B 1 178 ? 30.591 21.371  52.179 1.00 12.98 ? 178  ASP   B HA   1 
ATOM   12176 H  HB2  . ASP   B 1 178 ? 28.157 20.533  53.233 1.00 16.34 ? 178  ASP   B HB2  1 
ATOM   12177 H  HB3  . ASP   B 1 178 ? 28.493 20.729  51.723 1.00 16.34 ? 178  ASP   B HB3  1 
ATOM   12178 N  N    . VAL   B 1 179 ? 30.546 23.666  53.759 1.00 12.32 ? 179  VAL   B N    1 
ATOM   12179 C  CA   . VAL   B 1 179 ? 30.402 25.153  53.871 1.00 11.48 ? 179  VAL   B CA   1 
ATOM   12180 C  C    . VAL   B 1 179 ? 29.277 25.588  54.819 1.00 14.10 ? 179  VAL   B C    1 
ATOM   12181 O  O    . VAL   B 1 179 ? 29.554 26.430  55.682 1.00 12.41 ? 179  VAL   B O    1 
ATOM   12182 C  CB   . VAL   B 1 179 ? 30.242 25.807  52.482 1.00 13.16 ? 179  VAL   B CB   1 
ATOM   12183 C  CG1  . VAL   B 1 179 ? 30.181 27.323  52.587 1.00 15.03 ? 179  VAL   B CG1  1 
ATOM   12184 C  CG2  . VAL   B 1 179 ? 31.360 25.390  51.539 1.00 13.11 ? 179  VAL   B CG2  1 
ATOM   12185 H  H    . VAL   B 1 179 ? 31.249 23.356  54.146 1.00 14.79 ? 179  VAL   B H    1 
ATOM   12186 H  HA   . VAL   B 1 179 ? 31.228 25.471  54.269 1.00 13.78 ? 179  VAL   B HA   1 
ATOM   12187 H  HB   . VAL   B 1 179 ? 29.401 25.492  52.115 1.00 15.79 ? 179  VAL   B HB   1 
ATOM   12188 H  HG11 . VAL   B 1 179 ? 30.081 27.705  51.701 1.00 18.04 ? 179  VAL   B HG11 1 
ATOM   12189 H  HG12 . VAL   B 1 179 ? 29.424 27.579  53.137 1.00 18.04 ? 179  VAL   B HG12 1 
ATOM   12190 H  HG13 . VAL   B 1 179 ? 30.999 27.653  52.990 1.00 18.04 ? 179  VAL   B HG13 1 
ATOM   12191 H  HG21 . VAL   B 1 179 ? 31.232 25.816  50.677 1.00 15.74 ? 179  VAL   B HG21 1 
ATOM   12192 H  HG22 . VAL   B 1 179 ? 32.214 25.661  51.910 1.00 15.74 ? 179  VAL   B HG22 1 
ATOM   12193 H  HG23 . VAL   B 1 179 ? 31.348 24.426  51.428 1.00 15.74 ? 179  VAL   B HG23 1 
ATOM   12194 N  N    . ASP   B 1 180 ? 28.070 25.046  54.665 1.00 11.06 ? 180  ASP   B N    1 
ATOM   12195 C  CA   . ASP   B 1 180 ? 26.933 25.601  55.446 1.00 11.93 ? 180  ASP   B CA   1 
ATOM   12196 C  C    . ASP   B 1 180 ? 26.124 24.527  56.182 1.00 13.37 ? 180  ASP   B C    1 
ATOM   12197 O  O    . ASP   B 1 180 ? 25.035 24.858  56.667 1.00 13.20 ? 180  ASP   B O    1 
ATOM   12198 C  CB   . ASP   B 1 180 ? 26.029 26.411  54.515 1.00 12.20 ? 180  ASP   B CB   1 
ATOM   12199 C  CG   . ASP   B 1 180 ? 25.759 25.704  53.198 1.00 12.36 ? 180  ASP   B CG   1 
ATOM   12200 O  OD1  . ASP   B 1 180 ? 25.250 24.571  53.241 1.00 13.60 ? 180  ASP   B OD1  1 
ATOM   12201 O  OD2  . ASP   B 1 180 ? 26.061 26.293  52.144 1.00 13.99 ? 180  ASP   B OD2  1 
ATOM   12202 H  H    . ASP   B 1 180 ? 27.881 24.389  54.144 1.00 13.28 ? 180  ASP   B H    1 
ATOM   12203 H  HA   . ASP   B 1 180 ? 27.306 26.174  56.134 1.00 14.32 ? 180  ASP   B HA   1 
ATOM   12204 H  HB2  . ASP   B 1 180 ? 25.186 26.587  54.962 1.00 14.65 ? 180  ASP   B HB2  1 
ATOM   12205 H  HB3  . ASP   B 1 180 ? 26.441 27.271  54.337 1.00 14.65 ? 180  ASP   B HB3  1 
ATOM   12206 N  N    . ARG   B 1 181 ? 26.621 23.292  56.248 1.00 12.09 ? 181  ARG   B N    1 
ATOM   12207 C  CA   . ARG   B 1 181 ? 25.931 22.246  57.050 1.00 12.88 ? 181  ARG   B CA   1 
ATOM   12208 C  C    . ARG   B 1 181 ? 26.728 22.093  58.349 1.00 11.41 ? 181  ARG   B C    1 
ATOM   12209 O  O    . ARG   B 1 181 ? 27.919 22.425  58.338 1.00 11.79 ? 181  ARG   B O    1 
ATOM   12210 C  CB   . ARG   B 1 181 ? 25.810 20.942  56.258 1.00 10.72 ? 181  ARG   B CB   1 
ATOM   12211 C  CG   . ARG   B 1 181 ? 25.170 21.109  54.888 1.00 10.87 ? 181  ARG   B CG   1 
ATOM   12212 C  CD   . ARG   B 1 181 ? 23.863 21.876  54.948 1.00 12.22 ? 181  ARG   B CD   1 
ATOM   12213 N  NE   . ARG   B 1 181 ? 22.799 21.117  55.587 1.00 11.24 ? 181  ARG   B NE   1 
ATOM   12214 C  CZ   . ARG   B 1 181 ? 21.505 21.388  55.468 1.00 9.05  ? 181  ARG   B CZ   1 
ATOM   12215 N  NH1  . ARG   B 1 181 ? 21.106 22.389  54.705 1.00 13.90 ? 181  ARG   B NH1  1 
ATOM   12216 N  NH2  . ARG   B 1 181 ? 20.613 20.650  56.104 1.00 13.54 ? 181  ARG   B NH2  1 
ATOM   12217 H  H    . ARG   B 1 181 ? 27.338 23.032  55.851 1.00 14.52 ? 181  ARG   B H    1 
ATOM   12218 H  HA   . ARG   B 1 181 ? 25.018 22.497  57.260 1.00 15.45 ? 181  ARG   B HA   1 
ATOM   12219 H  HB2  . ARG   B 1 181 ? 26.694 20.558  56.147 1.00 12.87 ? 181  ARG   B HB2  1 
ATOM   12220 H  HB3  . ARG   B 1 181 ? 25.288 20.308  56.774 1.00 12.87 ? 181  ARG   B HB3  1 
ATOM   12221 H  HG2  . ARG   B 1 181 ? 25.787 21.572  54.300 1.00 13.04 ? 181  ARG   B HG2  1 
ATOM   12222 H  HG3  . ARG   B 1 181 ? 25.011 20.234  54.500 1.00 13.04 ? 181  ARG   B HG3  1 
ATOM   12223 H  HD2  . ARG   B 1 181 ? 24.000 22.705  55.432 1.00 14.67 ? 181  ARG   B HD2  1 
ATOM   12224 H  HD3  . ARG   B 1 181 ? 23.590 22.115  54.048 1.00 14.67 ? 181  ARG   B HD3  1 
ATOM   12225 H  HE   . ARG   B 1 181 ? 23.024 20.446  56.076 1.00 13.49 ? 181  ARG   B HE   1 
ATOM   12226 H  HH11 . ARG   B 1 181 ? 21.685 22.866  54.284 1.00 16.69 ? 181  ARG   B HH11 1 
ATOM   12227 H  HH12 . ARG   B 1 181 ? 20.267 22.564  54.629 1.00 16.69 ? 181  ARG   B HH12 1 
ATOM   12228 H  HH21 . ARG   B 1 181 ? 20.870 19.993  56.596 1.00 16.25 ? 181  ARG   B HH21 1 
ATOM   12229 H  HH22 . ARG   B 1 181 ? 19.775 20.826  56.026 1.00 16.25 ? 181  ARG   B HH22 1 
ATOM   12230 N  N    . THR   B 1 182 ? 26.103 21.614  59.431 1.00 9.54  ? 182  THR   B N    1 
ATOM   12231 C  CA   . THR   B 1 182 ? 26.890 21.585  60.692 1.00 10.63 ? 182  THR   B CA   1 
ATOM   12232 C  C    . THR   B 1 182 ? 26.391 20.642  61.785 1.00 10.91 ? 182  THR   B C    1 
ATOM   12233 O  O    . THR   B 1 182 ? 25.170 20.480  61.906 1.00 10.83 ? 182  THR   B O    1 
ATOM   12234 C  CB   . THR   B 1 182 ? 26.946 22.970  61.359 1.00 10.65 ? 182  THR   B CB   1 
ATOM   12235 O  OG1  . THR   B 1 182 ? 27.569 22.848  62.637 1.00 11.76 ? 182  THR   B OG1  1 
ATOM   12236 C  CG2  . THR   B 1 182 ? 25.580 23.603  61.517 1.00 11.12 ? 182  THR   B CG2  1 
ATOM   12237 H  H    . THR   B 1 182 ? 25.295 21.322  59.470 1.00 11.46 ? 182  THR   B H    1 
ATOM   12238 H  HA   . THR   B 1 182 ? 27.750 21.267  60.376 1.00 12.75 ? 182  THR   B HA   1 
ATOM   12239 H  HB   . THR   B 1 182 ? 27.461 23.552  60.778 1.00 12.79 ? 182  THR   B HB   1 
ATOM   12240 H  HG1  . THR   B 1 182 ? 28.279 22.406  62.562 1.00 14.12 ? 182  THR   B HG1  1 
ATOM   12241 H  HG21 . THR   B 1 182 ? 25.672 24.471  61.941 1.00 13.35 ? 182  THR   B HG21 1 
ATOM   12242 H  HG22 . THR   B 1 182 ? 25.171 23.712  60.644 1.00 13.35 ? 182  THR   B HG22 1 
ATOM   12243 H  HG23 . THR   B 1 182 ? 25.021 23.033  62.067 1.00 13.35 ? 182  THR   B HG23 1 
ATOM   12244 N  N    . ALA   B 1 183 ? 27.329 19.999  62.484 1.00 11.01 ? 183  ALA   B N    1 
ATOM   12245 C  CA   . ALA   B 1 183 ? 27.007 19.279  63.733 1.00 10.34 ? 183  ALA   B CA   1 
ATOM   12246 C  C    . ALA   B 1 183 ? 27.332 20.413  64.695 1.00 10.75 ? 183  ALA   B C    1 
ATOM   12247 O  O    . ALA   B 1 183 ? 28.518 20.604  64.983 1.00 11.47 ? 183  ALA   B O    1 
ATOM   12248 C  CB   . ALA   B 1 183 ? 27.916 18.095  63.894 1.00 11.47 ? 183  ALA   B CB   1 
ATOM   12249 H  H    . ALA   B 1 183 ? 28.158 19.964  62.257 1.00 13.21 ? 183  ALA   B H    1 
ATOM   12250 H  HA   . ALA   B 1 183 ? 26.119 18.899  63.824 1.00 12.41 ? 183  ALA   B HA   1 
ATOM   12251 H  HB1  . ALA   B 1 183 ? 27.698 17.629  64.716 1.00 13.76 ? 183  ALA   B HB1  1 
ATOM   12252 H  HB2  . ALA   B 1 183 ? 27.801 17.494  63.141 1.00 13.76 ? 183  ALA   B HB2  1 
ATOM   12253 H  HB3  . ALA   B 1 183 ? 28.837 18.396  63.929 1.00 13.76 ? 183  ALA   B HB3  1 
ATOM   12254 N  N    . ALA   B 1 184 ? 26.322 21.153  65.156 1.00 11.13 ? 184  ALA   B N    1 
ATOM   12255 C  CA   . ALA   B 1 184 ? 26.620 22.446  65.817 1.00 11.93 ? 184  ALA   B CA   1 
ATOM   12256 C  C    . ALA   B 1 184 ? 26.571 22.551  67.340 1.00 12.15 ? 184  ALA   B C    1 
ATOM   12257 O  O    . ALA   B 1 184 ? 27.370 23.321  67.877 1.00 13.85 ? 184  ALA   B O    1 
ATOM   12258 C  CB   . ALA   B 1 184 ? 25.613 23.431  65.265 1.00 13.04 ? 184  ALA   B CB   1 
ATOM   12259 H  H    . ALA   B 1 184 ? 25.489 20.944  65.104 1.00 13.36 ? 184  ALA   B H    1 
ATOM   12260 H  HA   . ALA   B 1 184 ? 27.557 22.605  65.623 1.00 14.32 ? 184  ALA   B HA   1 
ATOM   12261 H  HB1  . ALA   B 1 184 ? 25.760 24.303  65.665 1.00 15.65 ? 184  ALA   B HB1  1 
ATOM   12262 H  HB2  . ALA   B 1 184 ? 25.717 23.495  64.303 1.00 15.65 ? 184  ALA   B HB2  1 
ATOM   12263 H  HB3  . ALA   B 1 184 ? 24.716 23.128  65.473 1.00 15.65 ? 184  ALA   B HB3  1 
ATOM   12264 N  N    . ARG   B 1 185 ? 25.667 21.839  68.000 1.00 13.55 ? 185  ARG   B N    1 
ATOM   12265 C  CA   . ARG   B 1 185 ? 25.459 22.146  69.443 1.00 11.19 ? 185  ARG   B CA   1 
ATOM   12266 C  C    . ARG   B 1 185 ? 26.391 21.390  70.400 1.00 12.73 ? 185  ARG   B C    1 
ATOM   12267 O  O    . ARG   B 1 185 ? 26.982 20.383  69.998 1.00 12.27 ? 185  ARG   B O    1 
ATOM   12268 C  CB   . ARG   B 1 185 ? 23.969 21.973  69.778 1.00 12.81 ? 185  ARG   B CB   1 
ATOM   12269 C  CG   . ARG   B 1 185 ? 23.030 22.580  68.745 1.00 15.57 ? 185  ARG   B CG   1 
ATOM   12270 C  CD   . ARG   B 1 185 ? 21.708 23.019  69.344 1.00 11.77 ? 185  ARG   B CD   1 
ATOM   12271 N  NE   . ARG   B 1 185 ? 21.834 24.234  70.135 1.00 10.49 ? 185  ARG   B NE   1 
ATOM   12272 C  CZ   . ARG   B 1 185 ? 21.053 24.551  71.160 1.00 12.81 ? 185  ARG   B CZ   1 
ATOM   12273 N  NH1  . ARG   B 1 185 ? 19.969 23.840  71.409 1.00 12.50 ? 185  ARG   B NH1  1 
ATOM   12274 N  NH2  . ARG   B 1 185 ? 21.362 25.577  71.932 1.00 10.45 ? 185  ARG   B NH2  1 
ATOM   12275 H  H    . ARG   B 1 185 ? 25.183 21.209  67.671 1.00 16.27 ? 185  ARG   B H    1 
ATOM   12276 H  HA   . ARG   B 1 185 ? 25.713 23.071  69.588 1.00 13.44 ? 185  ARG   B HA   1 
ATOM   12277 H  HB2  . ARG   B 1 185 ? 23.774 21.027  69.863 1.00 15.37 ? 185  ARG   B HB2  1 
ATOM   12278 H  HB3  . ARG   B 1 185 ? 23.791 22.378  70.641 1.00 15.37 ? 185  ARG   B HB3  1 
ATOM   12279 H  HG2  . ARG   B 1 185 ? 23.462 23.343  68.329 1.00 18.69 ? 185  ARG   B HG2  1 
ATOM   12280 H  HG3  . ARG   B 1 185 ? 22.864 21.931  68.044 1.00 18.69 ? 185  ARG   B HG3  1 
ATOM   12281 H  HD2  . ARG   B 1 185 ? 21.066 23.165  68.632 1.00 14.13 ? 185  ARG   B HD2  1 
ATOM   12282 H  HD3  . ARG   B 1 185 ? 21.356 22.308  69.902 1.00 14.13 ? 185  ARG   B HD3  1 
ATOM   12283 H  HE   . ARG   B 1 185 ? 22.459 24.786  69.923 1.00 12.60 ? 185  ARG   B HE   1 
ATOM   12284 H  HH11 . ARG   B 1 185 ? 19.769 23.171  70.907 1.00 15.01 ? 185  ARG   B HH11 1 
ATOM   12285 H  HH12 . ARG   B 1 185 ? 19.463 24.046  72.073 1.00 15.01 ? 185  ARG   B HH12 1 
ATOM   12286 H  HH21 . ARG   B 1 185 ? 22.069 26.039  71.770 1.00 12.55 ? 185  ARG   B HH21 1 
ATOM   12287 H  HH22 . ARG   B 1 185 ? 20.856 25.783  72.596 1.00 12.55 ? 185  ARG   B HH22 1 
ATOM   12288 N  N    . GLY   B 1 186 ? 26.517 21.910  71.628 1.00 12.33 ? 186  GLY   B N    1 
ATOM   12289 C  CA   . GLY   B 1 186 ? 27.327 21.248  72.669 1.00 9.80  ? 186  GLY   B CA   1 
ATOM   12290 C  C    . GLY   B 1 186 ? 28.743 21.775  72.764 1.00 11.21 ? 186  GLY   B C    1 
ATOM   12291 O  O    . GLY   B 1 186 ? 29.451 21.370  73.694 1.00 12.29 ? 186  GLY   B O    1 
ATOM   12292 H  H    . GLY   B 1 186 ? 26.144 22.643  71.880 1.00 14.80 ? 186  GLY   B H    1 
ATOM   12293 H  HA2  . GLY   B 1 186 ? 26.890 21.360  73.528 1.00 11.77 ? 186  GLY   B HA2  1 
ATOM   12294 H  HA3  . GLY   B 1 186 ? 27.356 20.295  72.488 1.00 11.77 ? 186  GLY   B HA3  1 
ATOM   12295 N  N    . GLY   B 1 187 ? 29.145 22.639  71.830 1.00 13.36 ? 187  GLY   B N    1 
ATOM   12296 C  CA   . GLY   B 1 187 ? 30.545 23.108  71.803 1.00 12.93 ? 187  GLY   B CA   1 
ATOM   12297 C  C    . GLY   B 1 187 ? 31.454 22.057  71.187 1.00 12.68 ? 187  GLY   B C    1 
ATOM   12298 O  O    . GLY   B 1 187 ? 32.656 22.072  71.483 1.00 16.02 ? 187  GLY   B O    1 
ATOM   12299 H  H    . GLY   B 1 187 ? 28.640 22.963  71.214 1.00 16.03 ? 187  GLY   B H    1 
ATOM   12300 H  HA2  . GLY   B 1 187 ? 30.605 23.932  71.294 1.00 15.52 ? 187  GLY   B HA2  1 
ATOM   12301 H  HA3  . GLY   B 1 187 ? 30.841 23.309  72.705 1.00 15.52 ? 187  GLY   B HA3  1 
ATOM   12302 N  N    . VAL   B 1 188 ? 30.894 21.176  70.359 1.00 13.04 ? 188  VAL   B N    1 
ATOM   12303 C  CA   . VAL   B 1 188 ? 31.688 20.056  69.776 1.00 13.49 ? 188  VAL   B CA   1 
ATOM   12304 C  C    . VAL   B 1 188 ? 32.863 20.626  68.971 1.00 14.24 ? 188  VAL   B C    1 
ATOM   12305 O  O    . VAL   B 1 188 ? 33.914 19.970  68.905 1.00 13.41 ? 188  VAL   B O    1 
ATOM   12306 C  CB   . VAL   B 1 188 ? 30.794 19.132  68.927 1.00 15.13 ? 188  VAL   B CB   1 
ATOM   12307 C  CG1  . VAL   B 1 188 ? 29.897 18.276  69.807 1.00 13.37 ? 188  VAL   B CG1  1 
ATOM   12308 C  CG2  . VAL   B 1 188 ? 29.966 19.912  67.918 1.00 15.97 ? 188  VAL   B CG2  1 
ATOM   12309 H  H    . VAL   B 1 188 ? 30.069 21.196  70.117 1.00 15.65 ? 188  VAL   B H    1 
ATOM   12310 H  HA   . VAL   B 1 188 ? 32.050 19.510  70.491 1.00 16.19 ? 188  VAL   B HA   1 
ATOM   12311 H  HB   . VAL   B 1 188 ? 31.385 18.546  68.430 1.00 18.16 ? 188  VAL   B HB   1 
ATOM   12312 H  HG11 . VAL   B 1 188 ? 29.346 17.705  69.249 1.00 16.04 ? 188  VAL   B HG11 1 
ATOM   12313 H  HG12 . VAL   B 1 188 ? 30.444 17.727  70.390 1.00 16.04 ? 188  VAL   B HG12 1 
ATOM   12314 H  HG13 . VAL   B 1 188 ? 29.328 18.849  70.344 1.00 16.04 ? 188  VAL   B HG13 1 
ATOM   12315 H  HG21 . VAL   B 1 188 ? 29.418 19.298  67.405 1.00 19.16 ? 188  VAL   B HG21 1 
ATOM   12316 H  HG22 . VAL   B 1 188 ? 29.394 20.541  68.385 1.00 19.16 ? 188  VAL   B HG22 1 
ATOM   12317 H  HG23 . VAL   B 1 188 ? 30.556 20.396  67.319 1.00 19.16 ? 188  VAL   B HG23 1 
ATOM   12318 N  N    . GLY   B 1 189 ? 32.684 21.813  68.397 1.00 12.23 ? 189  GLY   B N    1 
ATOM   12319 C  CA   . GLY   B 1 189 ? 33.768 22.436  67.615 1.00 13.14 ? 189  GLY   B CA   1 
ATOM   12320 C  C    . GLY   B 1 189 ? 34.970 22.779  68.478 1.00 14.74 ? 189  GLY   B C    1 
ATOM   12321 O  O    . GLY   B 1 189 ? 36.093 22.792  67.955 1.00 13.14 ? 189  GLY   B O    1 
ATOM   12322 H  H    . GLY   B 1 189 ? 31.959 22.273  68.443 1.00 14.67 ? 189  GLY   B H    1 
ATOM   12323 H  HA2  . GLY   B 1 189 ? 34.042 21.833  66.906 1.00 15.77 ? 189  GLY   B HA2  1 
ATOM   12324 H  HA3  . GLY   B 1 189 ? 33.436 23.242  67.189 1.00 15.77 ? 189  GLY   B HA3  1 
ATOM   12325 N  N    . ALA   B 1 190 ? 34.733 23.069  69.758 1.00 14.05 ? 190  ALA   B N    1 
ATOM   12326 C  CA   . ALA   B 1 190 ? 35.833 23.417  70.685 1.00 14.97 ? 190  ALA   B CA   1 
ATOM   12327 C  C    . ALA   B 1 190 ? 36.685 22.177  70.982 1.00 15.22 ? 190  ALA   B C    1 
ATOM   12328 O  O    . ALA   B 1 190 ? 37.886 22.335  71.230 1.00 14.49 ? 190  ALA   B O    1 
ATOM   12329 C  CB   . ALA   B 1 190 ? 35.274 24.007  71.953 1.00 13.61 ? 190  ALA   B CB   1 
ATOM   12330 H  H    . ALA   B 1 190 ? 33.951 23.072  70.115 1.00 16.87 ? 190  ALA   B H    1 
ATOM   12331 H  HA   . ALA   B 1 190 ? 36.403 24.082  70.268 1.00 17.96 ? 190  ALA   B HA   1 
ATOM   12332 H  HB1  . ALA   B 1 190 ? 36.002 24.232  72.554 1.00 16.34 ? 190  ALA   B HB1  1 
ATOM   12333 H  HB2  . ALA   B 1 190 ? 34.770 24.808  71.742 1.00 16.34 ? 190  ALA   B HB2  1 
ATOM   12334 H  HB3  . ALA   B 1 190 ? 34.690 23.361  72.381 1.00 16.34 ? 190  ALA   B HB3  1 
ATOM   12335 N  N    . VAL   B 1 191 ? 36.074 20.994  70.961 1.00 15.60 ? 191  VAL   B N    1 
ATOM   12336 C  CA   . VAL   B 1 191 ? 36.864 19.745  71.159 1.00 14.54 ? 191  VAL   B CA   1 
ATOM   12337 C  C    . VAL   B 1 191 ? 37.821 19.584  69.974 1.00 15.07 ? 191  VAL   B C    1 
ATOM   12338 O  O    . VAL   B 1 191 ? 39.004 19.300  70.195 1.00 17.57 ? 191  VAL   B O    1 
ATOM   12339 C  CB   . VAL   B 1 191 ? 35.955 18.511  71.312 1.00 15.93 ? 191  VAL   B CB   1 
ATOM   12340 C  CG1  . VAL   B 1 191 ? 36.766 17.235  71.480 1.00 13.63 ? 191  VAL   B CG1  1 
ATOM   12341 C  CG2  . VAL   B 1 191 ? 34.974 18.675  72.460 1.00 13.88 ? 191  VAL   B CG2  1 
ATOM   12342 H  H    . VAL   B 1 191 ? 35.231 20.879  70.839 1.00 18.72 ? 191  VAL   B H    1 
ATOM   12343 H  HA   . VAL   B 1 191 ? 37.370 19.815  71.984 1.00 17.45 ? 191  VAL   B HA   1 
ATOM   12344 H  HB   . VAL   B 1 191 ? 35.444 18.436  70.491 1.00 19.12 ? 191  VAL   B HB   1 
ATOM   12345 H  HG11 . VAL   B 1 191 ? 36.165 16.479  71.573 1.00 16.36 ? 191  VAL   B HG11 1 
ATOM   12346 H  HG12 . VAL   B 1 191 ? 37.330 17.105  70.702 1.00 16.36 ? 191  VAL   B HG12 1 
ATOM   12347 H  HG13 . VAL   B 1 191 ? 37.321 17.306  72.272 1.00 16.36 ? 191  VAL   B HG13 1 
ATOM   12348 H  HG21 . VAL   B 1 191 ? 34.419 17.882  72.527 1.00 16.66 ? 191  VAL   B HG21 1 
ATOM   12349 H  HG22 . VAL   B 1 191 ? 35.463 18.798  73.289 1.00 16.66 ? 191  VAL   B HG22 1 
ATOM   12350 H  HG23 . VAL   B 1 191 ? 34.413 19.449  72.298 1.00 16.66 ? 191  VAL   B HG23 1 
ATOM   12351 N  N    . MET   B 1 192 ? 37.300 19.757  68.760 1.00 14.46 ? 192  MET   B N    1 
ATOM   12352 C  CA   . MET   B 1 192 ? 38.171 19.670  67.559 1.00 13.90 ? 192  MET   B CA   1 
ATOM   12353 C  C    . MET   B 1 192 ? 39.290 20.707  67.693 1.00 18.99 ? 192  MET   B C    1 
ATOM   12354 O  O    . MET   B 1 192 ? 40.455 20.350  67.484 1.00 14.98 ? 192  MET   B O    1 
ATOM   12355 C  CB   . MET   B 1 192 ? 37.370 19.933  66.283 1.00 16.79 ? 192  MET   B CB   1 
ATOM   12356 C  CG   . MET   B 1 192 ? 37.998 19.360  65.032 1.00 15.73 ? 192  MET   B CG   1 
ATOM   12357 S  SD   . MET   B 1 192 ? 36.802 19.251  63.676 1.00 16.39 ? 192  MET   B SD   1 
ATOM   12358 C  CE   . MET   B 1 192 ? 37.850 19.677  62.286 1.00 14.68 ? 192  MET   B CE   1 
ATOM   12359 H  H    . MET   B 1 192 ? 36.471 19.921  68.600 1.00 17.36 ? 192  MET   B H    1 
ATOM   12360 H  HA   . MET   B 1 192 ? 38.544 18.777  67.499 1.00 16.68 ? 192  MET   B HA   1 
ATOM   12361 H  HB2  . MET   B 1 192 ? 36.481 19.559  66.388 1.00 20.15 ? 192  MET   B HB2  1 
ATOM   12362 H  HB3  . MET   B 1 192 ? 37.264 20.891  66.171 1.00 20.15 ? 192  MET   B HB3  1 
ATOM   12363 H  HG2  . MET   B 1 192 ? 38.746 19.915  64.761 1.00 18.87 ? 192  MET   B HG2  1 
ATOM   12364 H  HG3  . MET   B 1 192 ? 38.354 18.478  65.222 1.00 18.87 ? 192  MET   B HG3  1 
ATOM   12365 H  HE1  . MET   B 1 192 ? 37.328 19.658  61.469 1.00 17.62 ? 192  MET   B HE1  1 
ATOM   12366 H  HE2  . MET   B 1 192 ? 38.214 20.567  62.416 1.00 17.62 ? 192  MET   B HE2  1 
ATOM   12367 H  HE3  . MET   B 1 192 ? 38.576 19.037  62.220 1.00 17.62 ? 192  MET   B HE3  1 
ATOM   12368 N  N    . GLY   B 1 193 ? 38.932 21.947  68.043 1.00 16.57 ? 193  GLY   B N    1 
ATOM   12369 C  CA   . GLY   B 1 193 ? 39.952 22.991  68.245 1.00 16.09 ? 193  GLY   B CA   1 
ATOM   12370 C  C    . GLY   B 1 193 ? 40.939 22.607  69.334 1.00 15.95 ? 193  GLY   B C    1 
ATOM   12371 O  O    . GLY   B 1 193 ? 42.127 22.920  69.182 1.00 17.41 ? 193  GLY   B O    1 
ATOM   12372 H  H    . GLY   B 1 193 ? 38.121 22.204  68.167 1.00 19.88 ? 193  GLY   B H    1 
ATOM   12373 H  HA2  . GLY   B 1 193 ? 40.429 23.143  67.414 1.00 19.31 ? 193  GLY   B HA2  1 
ATOM   12374 H  HA3  . GLY   B 1 193 ? 39.519 23.826  68.480 1.00 19.31 ? 193  GLY   B HA3  1 
ATOM   12375 N  N    . SER   B 1 194 ? 40.459 21.953  70.395 1.00 16.30 ? 194  SER   B N    1 
ATOM   12376 C  CA   . SER   B 1 194 ? 41.326 21.558  71.537 1.00 16.41 ? 194  SER   B CA   1 
ATOM   12377 C  C    . SER   B 1 194 ? 42.400 20.567  71.082 1.00 17.25 ? 194  SER   B C    1 
ATOM   12378 O  O    . SER   B 1 194 ? 43.387 20.413  71.814 1.00 17.60 ? 194  SER   B O    1 
ATOM   12379 C  CB   . SER   B 1 194 ? 40.509 20.959  72.658 1.00 16.44 ? 194  SER   B CB   1 
ATOM   12380 O  OG   . SER   B 1 194 ? 40.174 19.611  72.388 1.00 18.44 ? 194  SER   B OG   1 
ATOM   12381 H  H    . SER   B 1 194 ? 39.635 21.724  70.482 1.00 19.56 ? 194  SER   B H    1 
ATOM   12382 H  HA   . SER   B 1 194 ? 41.760 22.359  71.870 1.00 19.69 ? 194  SER   B HA   1 
ATOM   12383 H  HB2  . SER   B 1 194 ? 41.009 21.010  73.488 1.00 19.73 ? 194  SER   B HB2  1 
ATOM   12384 H  HB3  . SER   B 1 194 ? 39.698 21.477  72.783 1.00 19.73 ? 194  SER   B HB3  1 
ATOM   12385 H  HG   . SER   B 1 194 ? 39.911 19.541  71.593 1.00 22.13 ? 194  SER   B HG   1 
ATOM   12386 N  N    . LYS   B 1 195 ? 42.196 19.920  69.933 1.00 16.55 ? 195  LYS   B N    1 
ATOM   12387 C  CA   . LYS   B 1 195 ? 43.156 18.888  69.455 1.00 17.28 ? 195  LYS   B CA   1 
ATOM   12388 C  C    . LYS   B 1 195 ? 44.055 19.486  68.365 1.00 18.08 ? 195  LYS   B C    1 
ATOM   12389 O  O    . LYS   B 1 195 ? 44.860 18.731  67.800 1.00 15.72 ? 195  LYS   B O    1 
ATOM   12390 C  CB   . LYS   B 1 195 ? 42.393 17.661  68.950 1.00 15.37 ? 195  LYS   B CB   1 
ATOM   12391 C  CG   . LYS   B 1 195 ? 41.476 16.994  69.968 1.00 13.93 ? 195  LYS   B CG   1 
ATOM   12392 C  CD   . LYS   B 1 195 ? 40.929 15.658  69.500 1.00 15.61 ? 195  LYS   B CD   1 
ATOM   12393 C  CE   . LYS   B 1 195 ? 40.426 14.780  70.627 1.00 16.83 ? 195  LYS   B CE   1 
ATOM   12394 N  NZ   . LYS   B 1 195 ? 41.358 14.772  71.779 1.00 18.28 ? 195  LYS   B NZ   1 
ATOM   12395 H  H    . LYS   B 1 195 ? 41.523 20.053  69.415 1.00 19.87 ? 195  LYS   B H    1 
ATOM   12396 H  HA   . LYS   B 1 195 ? 43.724 18.601  70.187 1.00 20.74 ? 195  LYS   B HA   1 
ATOM   12397 H  HB2  . LYS   B 1 195 ? 41.861 17.923  68.182 1.00 18.44 ? 195  LYS   B HB2  1 
ATOM   12398 H  HB3  . LYS   B 1 195 ? 43.036 17.005  68.639 1.00 18.44 ? 195  LYS   B HB3  1 
ATOM   12399 H  HG2  . LYS   B 1 195 ? 41.963 16.864  70.797 1.00 16.72 ? 195  LYS   B HG2  1 
ATOM   12400 H  HG3  . LYS   B 1 195 ? 40.735 17.588  70.165 1.00 16.72 ? 195  LYS   B HG3  1 
ATOM   12401 H  HD2  . LYS   B 1 195 ? 40.204 15.815  68.874 1.00 18.74 ? 195  LYS   B HD2  1 
ATOM   12402 H  HD3  . LYS   B 1 195 ? 41.624 15.184  69.016 1.00 18.74 ? 195  LYS   B HD3  1 
ATOM   12403 H  HE2  . LYS   B 1 195 ? 39.556 15.094  70.918 1.00 20.19 ? 195  LYS   B HE2  1 
ATOM   12404 H  HE3  . LYS   B 1 195 ? 40.306 13.874  70.302 1.00 20.19 ? 195  LYS   B HE3  1 
ATOM   12405 H  HZ1  . LYS   B 1 195 ? 41.202 14.055  72.283 1.00 21.94 ? 195  LYS   B HZ1  1 
ATOM   12406 H  HZ2  . LYS   B 1 195 ? 42.197 14.749  71.482 1.00 21.94 ? 195  LYS   B HZ2  1 
ATOM   12407 H  HZ3  . LYS   B 1 195 ? 41.236 15.508  72.265 1.00 21.94 ? 195  LYS   B HZ3  1 
ATOM   12408 N  N    . ASN   B 1 196 ? 43.919 20.788  68.100 1.00 16.83 ? 196  ASN   B N    1 
ATOM   12409 C  CA   . ASN   B 1 196 ? 44.726 21.467  67.052 1.00 16.08 ? 196  ASN   B CA   1 
ATOM   12410 C  C    . ASN   B 1 196 ? 44.348 20.905  65.678 1.00 15.47 ? 196  ASN   B C    1 
ATOM   12411 O  O    . ASN   B 1 196 ? 45.217 20.895  64.799 1.00 15.67 ? 196  ASN   B O    1 
ATOM   12412 C  CB   . ASN   B 1 196 ? 46.229 21.365  67.333 1.00 16.44 ? 196  ASN   B CB   1 
ATOM   12413 C  CG   . ASN   B 1 196 ? 46.811 22.657  67.866 1.00 21.33 ? 196  ASN   B CG   1 
ATOM   12414 O  OD1  . ASN   B 1 196 ? 46.272 23.733  67.620 1.00 19.55 ? 196  ASN   B OD1  1 
ATOM   12415 N  ND2  . ASN   B 1 196 ? 47.908 22.562  68.599 1.00 19.31 ? 196  ASN   B ND2  1 
ATOM   12416 H  H    . ASN   B 1 196 ? 43.367 21.304  68.511 1.00 20.20 ? 196  ASN   B H    1 
ATOM   12417 H  HA   . ASN   B 1 196 ? 44.522 22.415  67.061 1.00 19.29 ? 196  ASN   B HA   1 
ATOM   12418 H  HB2  . ASN   B 1 196 ? 46.387 20.654  67.974 1.00 19.73 ? 196  ASN   B HB2  1 
ATOM   12419 H  HB3  . ASN   B 1 196 ? 46.691 21.119  66.517 1.00 19.73 ? 196  ASN   B HB3  1 
ATOM   12420 H  HD21 . ASN   B 1 196 ? 48.271 23.271  68.924 1.00 23.18 ? 196  ASN   B HD21 1 
ATOM   12421 H  HD22 . ASN   B 1 196 ? 48.258 21.791  68.751 1.00 23.18 ? 196  ASN   B HD22 1 
ATOM   12422 N  N    . LEU   B 1 197 ? 43.095 20.469  65.517 1.00 14.82 ? 197  LEU   B N    1 
ATOM   12423 C  CA   . LEU   B 1 197 ? 42.630 19.904  64.223 1.00 15.50 ? 197  LEU   B CA   1 
ATOM   12424 C  C    . LEU   B 1 197 ? 41.763 20.937  63.498 1.00 15.81 ? 197  LEU   B C    1 
ATOM   12425 O  O    . LEU   B 1 197 ? 40.682 21.263  64.009 1.00 12.65 ? 197  LEU   B O    1 
ATOM   12426 C  CB   . LEU   B 1 197 ? 41.856 18.609  64.471 1.00 12.92 ? 197  LEU   B CB   1 
ATOM   12427 C  CG   . LEU   B 1 197 ? 41.319 17.919  63.219 1.00 12.73 ? 197  LEU   B CG   1 
ATOM   12428 C  CD1  . LEU   B 1 197 ? 42.453 17.568  62.267 1.00 12.43 ? 197  LEU   B CD1  1 
ATOM   12429 C  CD2  . LEU   B 1 197 ? 40.525 16.676  63.588 1.00 16.16 ? 197  LEU   B CD2  1 
ATOM   12430 H  H    . LEU   B 1 197 ? 42.496 20.487  66.134 1.00 17.79 ? 197  LEU   B H    1 
ATOM   12431 H  HA   . LEU   B 1 197 ? 43.393 19.695  63.661 1.00 18.60 ? 197  LEU   B HA   1 
ATOM   12432 H  HB2  . LEU   B 1 197 ? 42.435 17.989  64.941 1.00 15.51 ? 197  LEU   B HB2  1 
ATOM   12433 H  HB3  . LEU   B 1 197 ? 41.110 18.803  65.060 1.00 15.51 ? 197  LEU   B HB3  1 
ATOM   12434 H  HG   . LEU   B 1 197 ? 40.724 18.537  62.766 1.00 15.28 ? 197  LEU   B HG   1 
ATOM   12435 H  HD11 . LEU   B 1 197 ? 42.092 17.131  61.480 1.00 14.92 ? 197  LEU   B HD11 1 
ATOM   12436 H  HD12 . LEU   B 1 197 ? 42.916 18.378  62.003 1.00 14.92 ? 197  LEU   B HD12 1 
ATOM   12437 H  HD13 . LEU   B 1 197 ? 43.075 16.970  62.711 1.00 14.92 ? 197  LEU   B HD13 1 
ATOM   12438 H  HD21 . LEU   B 1 197 ? 40.193 16.253  62.781 1.00 19.40 ? 197  LEU   B HD21 1 
ATOM   12439 H  HD22 . LEU   B 1 197 ? 41.098 16.056  64.066 1.00 19.40 ? 197  LEU   B HD22 1 
ATOM   12440 H  HD23 . LEU   B 1 197 ? 39.777 16.925  64.153 1.00 19.40 ? 197  LEU   B HD23 1 
ATOM   12441 N  N    . LYS   B 1 198 ? 42.228 21.405  62.342 1.00 14.17 ? 198  LYS   B N    1 
ATOM   12442 C  CA   . LYS   B 1 198 ? 41.501 22.466  61.601 1.00 12.82 ? 198  LYS   B CA   1 
ATOM   12443 C  C    . LYS   B 1 198 ? 40.466 21.831  60.676 1.00 12.96 ? 198  LYS   B C    1 
ATOM   12444 O  O    . LYS   B 1 198 ? 39.387 22.418  60.518 1.00 16.20 ? 198  LYS   B O    1 
ATOM   12445 C  CB   . LYS   B 1 198 ? 42.498 23.291  60.782 1.00 14.44 ? 198  LYS   B CB   1 
ATOM   12446 C  CG   . LYS   B 1 198 ? 41.890 24.327  59.845 1.00 14.66 ? 198  LYS   B CG   1 
ATOM   12447 C  CD   . LYS   B 1 198 ? 41.099 25.400  60.564 1.00 14.06 ? 198  LYS   B CD   1 
ATOM   12448 C  CE   . LYS   B 1 198 ? 40.678 26.534  59.654 1.00 14.49 ? 198  LYS   B CE   1 
ATOM   12449 N  NZ   . LYS   B 1 198 ? 39.671 27.414  60.295 1.00 14.40 ? 198  LYS   B NZ   1 
ATOM   12450 H  H    . LYS   B 1 198 ? 42.951 21.133  61.965 1.00 17.01 ? 198  LYS   B H    1 
ATOM   12451 H  HA   . LYS   B 1 198 ? 41.047 23.047  62.231 1.00 15.38 ? 198  LYS   B HA   1 
ATOM   12452 H  HB2  . LYS   B 1 198 ? 43.096 23.746  61.395 1.00 17.33 ? 198  LYS   B HB2  1 
ATOM   12453 H  HB3  . LYS   B 1 198 ? 43.040 22.683  60.256 1.00 17.33 ? 198  LYS   B HB3  1 
ATOM   12454 H  HG2  . LYS   B 1 198 ? 42.600 24.746  59.333 1.00 17.59 ? 198  LYS   B HG2  1 
ATOM   12455 H  HG3  . LYS   B 1 198 ? 41.310 23.878  59.210 1.00 17.59 ? 198  LYS   B HG3  1 
ATOM   12456 H  HD2  . LYS   B 1 198 ? 40.309 25.001  60.962 1.00 16.88 ? 198  LYS   B HD2  1 
ATOM   12457 H  HD3  . LYS   B 1 198 ? 41.633 25.756  61.291 1.00 16.88 ? 198  LYS   B HD3  1 
ATOM   12458 H  HE2  . LYS   B 1 198 ? 41.457 27.058  59.410 1.00 17.39 ? 198  LYS   B HE2  1 
ATOM   12459 H  HE3  . LYS   B 1 198 ? 40.313 26.170  58.832 1.00 17.39 ? 198  LYS   B HE3  1 
ATOM   12460 H  HZ1  . LYS   B 1 198 ? 39.447 28.067  59.734 1.00 17.29 ? 198  LYS   B HZ1  1 
ATOM   12461 H  HZ2  . LYS   B 1 198 ? 38.947 26.938  60.499 1.00 17.29 ? 198  LYS   B HZ2  1 
ATOM   12462 H  HZ3  . LYS   B 1 198 ? 40.013 27.766  61.037 1.00 17.29 ? 198  LYS   B HZ3  1 
ATOM   12463 N  N    . ALA   B 1 199 ? 40.784 20.669  60.104 1.00 14.92 ? 199  ALA   B N    1 
ATOM   12464 C  CA   . ALA   B 1 199 ? 39.842 20.109  59.113 1.00 13.15 ? 199  ALA   B CA   1 
ATOM   12465 C  C    . ALA   B 1 199 ? 40.085 18.634  58.795 1.00 13.41 ? 199  ALA   B C    1 
ATOM   12466 O  O    . ALA   B 1 199 ? 41.160 18.118  59.133 1.00 14.17 ? 199  ALA   B O    1 
ATOM   12467 C  CB   . ALA   B 1 199 ? 39.943 20.921  57.843 1.00 12.39 ? 199  ALA   B CB   1 
ATOM   12468 H  H    . ALA   B 1 199 ? 41.493 20.208  60.258 1.00 17.91 ? 199  ALA   B H    1 
ATOM   12469 H  HA   . ALA   B 1 199 ? 38.955 20.159  59.501 1.00 15.78 ? 199  ALA   B HA   1 
ATOM   12470 H  HB1  . ALA   B 1 199 ? 39.329 20.565  57.181 1.00 14.88 ? 199  ALA   B HB1  1 
ATOM   12471 H  HB2  . ALA   B 1 199 ? 39.715 21.845  58.031 1.00 14.88 ? 199  ALA   B HB2  1 
ATOM   12472 H  HB3  . ALA   B 1 199 ? 40.849 20.875  57.501 1.00 14.88 ? 199  ALA   B HB3  1 
ATOM   12473 N  N    . ILE   B 1 200 ? 39.079 17.996  58.204 1.00 13.24 ? 200  ILE   B N    1 
ATOM   12474 C  CA   . ILE   B 1 200 ? 39.230 16.605  57.704 1.00 14.81 ? 200  ILE   B CA   1 
ATOM   12475 C  C    . ILE   B 1 200 ? 38.656 16.615  56.284 1.00 13.35 ? 200  ILE   B C    1 
ATOM   12476 O  O    . ILE   B 1 200 ? 37.460 16.913  56.137 1.00 14.07 ? 200  ILE   B O    1 
ATOM   12477 C  CB   . ILE   B 1 200 ? 38.495 15.583  58.588 1.00 12.89 ? 200  ILE   B CB   1 
ATOM   12478 C  CG1  . ILE   B 1 200 ? 38.934 15.670  60.050 1.00 13.28 ? 200  ILE   B CG1  1 
ATOM   12479 C  CG2  . ILE   B 1 200 ? 38.677 14.182  58.026 1.00 13.94 ? 200  ILE   B CG2  1 
ATOM   12480 C  CD1  . ILE   B 1 200 ? 38.253 14.666  60.946 1.00 16.72 ? 200  ILE   B CD1  1 
ATOM   12481 H  H    . ILE   B 1 200 ? 38.300 18.338  58.077 1.00 15.89 ? 200  ILE   B H    1 
ATOM   12482 H  HA   . ILE   B 1 200 ? 40.161 16.333  57.720 1.00 17.78 ? 200  ILE   B HA   1 
ATOM   12483 H  HB   . ILE   B 1 200 ? 37.549 15.797  58.575 1.00 15.47 ? 200  ILE   B HB   1 
ATOM   12484 H  HG12 . ILE   B 1 200 ? 39.894 15.538  60.100 1.00 15.94 ? 200  ILE   B HG12 1 
ATOM   12485 H  HG13 . ILE   B 1 200 ? 38.753 16.563  60.382 1.00 15.94 ? 200  ILE   B HG13 1 
ATOM   12486 H  HG21 . ILE   B 1 200 ? 38.211 13.544  58.589 1.00 16.74 ? 200  ILE   B HG21 1 
ATOM   12487 H  HG22 . ILE   B 1 200 ? 38.315 14.144  57.127 1.00 16.74 ? 200  ILE   B HG22 1 
ATOM   12488 H  HG23 . ILE   B 1 200 ? 39.622 13.962  58.003 1.00 16.74 ? 200  ILE   B HG23 1 
ATOM   12489 H  HD11 . ILE   B 1 200 ? 38.574 14.773  61.855 1.00 20.07 ? 200  ILE   B HD11 1 
ATOM   12490 H  HD12 . ILE   B 1 200 ? 37.294 14.810  60.923 1.00 20.07 ? 200  ILE   B HD12 1 
ATOM   12491 H  HD13 . ILE   B 1 200 ? 38.453 13.768  60.637 1.00 20.07 ? 200  ILE   B HD13 1 
ATOM   12492 N  N    . THR   B 1 201 ? 39.491 16.341  55.283 1.00 13.22 ? 201  THR   B N    1 
ATOM   12493 C  CA   . THR   B 1 201 ? 38.989 16.239  53.891 1.00 13.62 ? 201  THR   B CA   1 
ATOM   12494 C  C    . THR   B 1 201 ? 38.769 14.755  53.588 1.00 13.81 ? 201  THR   B C    1 
ATOM   12495 O  O    . THR   B 1 201 ? 39.552 13.932  54.082 1.00 12.62 ? 201  THR   B O    1 
ATOM   12496 C  CB   . THR   B 1 201 ? 39.944 16.931  52.910 1.00 15.85 ? 201  THR   B CB   1 
ATOM   12497 O  OG1  . THR   B 1 201 ? 41.073 16.085  52.693 1.00 15.70 ? 201  THR   B OG1  1 
ATOM   12498 C  CG2  . THR   B 1 201 ? 40.401 18.285  53.405 1.00 19.08 ? 201  THR   B CG2  1 
ATOM   12499 H  H    . THR   B 1 201 ? 40.336 16.211  55.374 1.00 15.87 ? 201  THR   B H    1 
ATOM   12500 H  HA   . THR   B 1 201 ? 38.144 16.704  53.787 1.00 16.35 ? 201  THR   B HA   1 
ATOM   12501 H  HB   . THR   B 1 201 ? 39.465 17.082  52.080 1.00 19.02 ? 201  THR   B HB   1 
ATOM   12502 H  HG1  . THR   B 1 201 ? 40.925 15.583  52.036 1.00 18.85 ? 201  THR   B HG1  1 
ATOM   12503 H  HG21 . THR   B 1 201 ? 41.001 18.682  52.754 1.00 22.90 ? 201  THR   B HG21 1 
ATOM   12504 H  HG22 . THR   B 1 201 ? 39.631 18.861  53.529 1.00 22.90 ? 201  THR   B HG22 1 
ATOM   12505 H  HG23 . THR   B 1 201 ? 40.865 18.181  54.250 1.00 22.90 ? 201  THR   B HG23 1 
ATOM   12506 N  N    . VAL   B 1 202 ? 37.727 14.439  52.826 1.00 13.27 ? 202  VAL   B N    1 
ATOM   12507 C  CA   . VAL   B 1 202 ? 37.530 13.013  52.460 1.00 14.30 ? 202  VAL   B CA   1 
ATOM   12508 C  C    . VAL   B 1 202 ? 36.980 12.871  51.040 1.00 16.87 ? 202  VAL   B C    1 
ATOM   12509 O  O    . VAL   B 1 202 ? 36.063 13.626  50.672 1.00 15.67 ? 202  VAL   B O    1 
ATOM   12510 C  CB   . VAL   B 1 202 ? 36.629 12.281  53.475 1.00 14.17 ? 202  VAL   B CB   1 
ATOM   12511 C  CG1  . VAL   B 1 202 ? 35.198 12.797  53.455 1.00 14.60 ? 202  VAL   B CG1  1 
ATOM   12512 C  CG2  . VAL   B 1 202 ? 36.660 10.775  53.267 1.00 17.29 ? 202  VAL   B CG2  1 
ATOM   12513 H  H    . VAL   B 1 202 ? 37.144 14.992  52.518 1.00 15.92 ? 202  VAL   B H    1 
ATOM   12514 H  HA   . VAL   B 1 202 ? 38.403 12.591  52.486 1.00 17.17 ? 202  VAL   B HA   1 
ATOM   12515 H  HB   . VAL   B 1 202 ? 36.994 12.473  54.353 1.00 17.01 ? 202  VAL   B HB   1 
ATOM   12516 H  HG11 . VAL   B 1 202 ? 34.669 12.310  54.106 1.00 17.53 ? 202  VAL   B HG11 1 
ATOM   12517 H  HG12 . VAL   B 1 202 ? 35.191 13.742  53.675 1.00 17.53 ? 202  VAL   B HG12 1 
ATOM   12518 H  HG13 . VAL   B 1 202 ? 34.820 12.669  52.571 1.00 17.53 ? 202  VAL   B HG13 1 
ATOM   12519 H  HG21 . VAL   B 1 202 ? 36.085 10.346  53.920 1.00 20.75 ? 202  VAL   B HG21 1 
ATOM   12520 H  HG22 . VAL   B 1 202 ? 36.347 10.565  52.373 1.00 20.75 ? 202  VAL   B HG22 1 
ATOM   12521 H  HG23 . VAL   B 1 202 ? 37.568 10.452  53.375 1.00 20.75 ? 202  VAL   B HG23 1 
ATOM   12522 N  N    . LYS   B 1 203 ? 37.569 11.958  50.271 1.00 15.56 ? 203  LYS   B N    1 
ATOM   12523 C  CA   . LYS   B 1 203 ? 37.023 11.617  48.936 1.00 14.91 ? 203  LYS   B CA   1 
ATOM   12524 C  C    . LYS   B 1 203 ? 36.862 10.095  48.926 1.00 17.37 ? 203  LYS   B C    1 
ATOM   12525 O  O    . LYS   B 1 203 ? 37.815 9.406   49.327 1.00 17.98 ? 203  LYS   B O    1 
ATOM   12526 C  CB   . LYS   B 1 203 ? 37.947 12.057  47.800 1.00 18.04 ? 203  LYS   B CB   1 
ATOM   12527 C  CG   . LYS   B 1 203 ? 37.656 11.378  46.468 1.00 18.96 ? 203  LYS   B CG   1 
ATOM   12528 C  CD   . LYS   B 1 203 ? 38.449 11.926  45.308 1.00 24.18 ? 203  LYS   B CD   1 
ATOM   12529 C  CE   . LYS   B 1 203 ? 37.896 11.481  43.971 1.00 24.91 ? 203  LYS   B CE   1 
ATOM   12530 N  NZ   . LYS   B 1 203 ? 38.664 12.048  42.839 1.00 28.67 ? 203  LYS   B NZ   1 
ATOM   12531 H  H    . LYS   B 1 203 ? 38.278 11.524  50.491 1.00 18.67 ? 203  LYS   B H    1 
ATOM   12532 H  HA   . LYS   B 1 203 ? 36.183 12.079  48.789 1.00 17.90 ? 203  LYS   B HA   1 
ATOM   12533 H  HB2  . LYS   B 1 203 ? 37.871 13.017  47.687 1.00 21.65 ? 203  LYS   B HB2  1 
ATOM   12534 H  HB3  . LYS   B 1 203 ? 38.865 11.873  48.053 1.00 21.65 ? 203  LYS   B HB3  1 
ATOM   12535 H  HG2  . LYS   B 1 203 ? 37.840 10.429  46.553 1.00 22.75 ? 203  LYS   B HG2  1 
ATOM   12536 H  HG3  . LYS   B 1 203 ? 36.710 11.467  46.271 1.00 22.75 ? 203  LYS   B HG3  1 
ATOM   12537 H  HD2  . LYS   B 1 203 ? 38.450 12.895  45.349 1.00 29.02 ? 203  LYS   B HD2  1 
ATOM   12538 H  HD3  . LYS   B 1 203 ? 39.372 11.638  45.386 1.00 29.02 ? 203  LYS   B HD3  1 
ATOM   12539 H  HE2  . LYS   B 1 203 ? 37.914 10.512  43.920 1.00 29.89 ? 203  LYS   B HE2  1 
ATOM   12540 H  HE3  . LYS   B 1 203 ? 36.967 11.752  43.899 1.00 29.89 ? 203  LYS   B HE3  1 
ATOM   12541 H  HZ1  . LYS   B 1 203 ? 38.278 11.814  42.072 1.00 34.40 ? 203  LYS   B HZ1  1 
ATOM   12542 H  HZ2  . LYS   B 1 203 ? 38.679 12.935  42.905 1.00 34.40 ? 203  LYS   B HZ2  1 
ATOM   12543 H  HZ3  . LYS   B 1 203 ? 39.497 11.736  42.859 1.00 34.40 ? 203  LYS   B HZ3  1 
ATOM   12544 N  N    . GLY   B 1 204 ? 35.700 9.604   48.511 1.00 15.89 ? 204  GLY   B N    1 
ATOM   12545 C  CA   . GLY   B 1 204 ? 35.450 8.155   48.457 1.00 18.35 ? 204  GLY   B CA   1 
ATOM   12546 C  C    . GLY   B 1 204 ? 35.083 7.709   47.054 1.00 20.22 ? 204  GLY   B C    1 
ATOM   12547 O  O    . GLY   B 1 204 ? 34.280 8.398   46.411 1.00 19.82 ? 204  GLY   B O    1 
ATOM   12548 H  H    . GLY   B 1 204 ? 35.038 10.089  48.254 1.00 19.08 ? 204  GLY   B H    1 
ATOM   12549 H  HA2  . GLY   B 1 204 ? 36.240 7.677   48.754 1.00 22.02 ? 204  GLY   B HA2  1 
ATOM   12550 H  HA3  . GLY   B 1 204 ? 34.733 7.926   49.069 1.00 22.02 ? 204  GLY   B HA3  1 
ATOM   12551 N  N    . THR   B 1 205 ? 35.649 6.586   46.605 1.00 21.56 ? 205  THR   B N    1 
ATOM   12552 C  CA   . THR   B 1 205 ? 35.406 6.106   45.219 1.00 22.83 ? 205  THR   B CA   1 
ATOM   12553 C  C    . THR   B 1 205 ? 34.807 4.697   45.264 1.00 22.24 ? 205  THR   B C    1 
ATOM   12554 O  O    . THR   B 1 205 ? 34.626 4.100   44.189 1.00 21.96 ? 205  THR   B O    1 
ATOM   12555 C  CB   . THR   B 1 205 ? 36.698 6.143   44.393 1.00 25.67 ? 205  THR   B CB   1 
ATOM   12556 O  OG1  . THR   B 1 205 ? 37.579 5.140   44.901 1.00 22.96 ? 205  THR   B OG1  1 
ATOM   12557 C  CG2  . THR   B 1 205 ? 37.379 7.494   44.426 1.00 26.06 ? 205  THR   B CG2  1 
ATOM   12558 H  H    . THR   B 1 205 ? 36.171 6.087   47.072 1.00 25.87 ? 205  THR   B H    1 
ATOM   12559 H  HA   . THR   B 1 205 ? 34.772 6.697   44.783 1.00 27.40 ? 205  THR   B HA   1 
ATOM   12560 H  HB   . THR   B 1 205 ? 36.471 5.974   43.465 1.00 30.81 ? 205  THR   B HB   1 
ATOM   12561 H  HG1  . THR   B 1 205 ? 38.135 5.493   45.422 1.00 27.55 ? 205  THR   B HG1  1 
ATOM   12562 H  HG21 . THR   B 1 205 ? 38.187 7.462   43.890 1.00 31.28 ? 205  THR   B HG21 1 
ATOM   12563 H  HG22 . THR   B 1 205 ? 36.780 8.167   44.068 1.00 31.28 ? 205  THR   B HG22 1 
ATOM   12564 H  HG23 . THR   B 1 205 ? 37.607 7.719   45.341 1.00 31.28 ? 205  THR   B HG23 1 
ATOM   12565 N  N    . GLY   B 1 206 ? 34.513 4.195   46.463 1.00 24.97 ? 206  GLY   B N    1 
ATOM   12566 C  CA   . GLY   B 1 206 ? 33.900 2.865   46.610 1.00 26.95 ? 206  GLY   B CA   1 
ATOM   12567 C  C    . GLY   B 1 206 ? 32.391 2.940   46.728 1.00 24.42 ? 206  GLY   B C    1 
ATOM   12568 O  O    . GLY   B 1 206 ? 31.837 4.025   46.508 1.00 24.20 ? 206  GLY   B O    1 
ATOM   12569 H  H    . GLY   B 1 206 ? 34.659 4.604   47.205 1.00 29.96 ? 206  GLY   B H    1 
ATOM   12570 H  HA2  . GLY   B 1 206 ? 34.136 2.316   45.846 1.00 32.34 ? 206  GLY   B HA2  1 
ATOM   12571 H  HA3  . GLY   B 1 206 ? 34.263 2.428   47.396 1.00 32.34 ? 206  GLY   B HA3  1 
ATOM   12572 N  N    . LYS   B 1 207 ? 31.753 1.814   47.054 1.00 26.48 ? 207  LYS   B N    1 
ATOM   12573 C  CA   . LYS   B 1 207 ? 30.272 1.770   47.118 1.00 25.10 ? 207  LYS   B CA   1 
ATOM   12574 C  C    . LYS   B 1 207 ? 29.817 1.163   48.443 1.00 26.45 ? 207  LYS   B C    1 
ATOM   12575 O  O    . LYS   B 1 207 ? 30.626 0.476   49.088 1.00 26.99 ? 207  LYS   B O    1 
ATOM   12576 C  CB   . LYS   B 1 207 ? 29.700 0.913   45.988 1.00 31.19 ? 207  LYS   B CB   1 
ATOM   12577 C  CG   . LYS   B 1 207 ? 30.213 1.253   44.596 1.00 38.53 ? 207  LYS   B CG   1 
ATOM   12578 C  CD   . LYS   B 1 207 ? 29.157 1.117   43.525 1.00 46.20 ? 207  LYS   B CD   1 
ATOM   12579 C  CE   . LYS   B 1 207 ? 29.682 0.463   42.266 1.00 48.26 ? 207  LYS   B CE   1 
ATOM   12580 N  NZ   . LYS   B 1 207 ? 30.948 1.086   41.816 1.00 55.63 ? 207  LYS   B NZ   1 
ATOM   12581 H  H    . LYS   B 1 207 ? 32.144 1.071   47.240 1.00 31.79 ? 207  LYS   B H    1 
ATOM   12582 H  HA   . LYS   B 1 207 ? 29.951 2.682   47.034 1.00 30.12 ? 207  LYS   B HA   1 
ATOM   12583 H  HB2  . LYS   B 1 207 ? 29.901 -0.018  46.173 1.00 37.43 ? 207  LYS   B HB2  1 
ATOM   12584 H  HB3  . LYS   B 1 207 ? 28.734 1.001   45.992 1.00 37.43 ? 207  LYS   B HB3  1 
ATOM   12585 H  HG2  . LYS   B 1 207 ? 30.551 2.162   44.595 1.00 46.24 ? 207  LYS   B HG2  1 
ATOM   12586 H  HG3  . LYS   B 1 207 ? 30.960 0.672   44.382 1.00 46.24 ? 207  LYS   B HG3  1 
ATOM   12587 H  HD2  . LYS   B 1 207 ? 28.416 0.595   43.871 1.00 55.44 ? 207  LYS   B HD2  1 
ATOM   12588 H  HD3  . LYS   B 1 207 ? 28.808 1.995   43.307 1.00 55.44 ? 207  LYS   B HD3  1 
ATOM   12589 H  HE2  . LYS   B 1 207 ? 29.825 -0.483  42.427 1.00 57.91 ? 207  LYS   B HE2  1 
ATOM   12590 H  HE3  . LYS   B 1 207 ? 29.018 0.533   41.563 1.00 57.91 ? 207  LYS   B HE3  1 
ATOM   12591 H  HZ1  . LYS   B 1 207 ? 31.024 1.000   40.933 1.00 66.75 ? 207  LYS   B HZ1  1 
ATOM   12592 H  HZ2  . LYS   B 1 207 ? 30.947 1.950   42.031 1.00 66.75 ? 207  LYS   B HZ2  1 
ATOM   12593 H  HZ3  . LYS   B 1 207 ? 31.635 0.683   42.213 1.00 66.75 ? 207  LYS   B HZ3  1 
ATOM   12594 N  N    . ILE   B 1 208 ? 28.570 1.430   48.822 1.00 25.08 ? 208  ILE   B N    1 
ATOM   12595 C  CA   . ILE   B 1 208 ? 28.003 0.797   50.044 1.00 23.86 ? 208  ILE   B CA   1 
ATOM   12596 C  C    . ILE   B 1 208 ? 27.394 -0.536  49.601 1.00 24.74 ? 208  ILE   B C    1 
ATOM   12597 O  O    . ILE   B 1 208 ? 26.474 -0.513  48.769 1.00 27.34 ? 208  ILE   B O    1 
ATOM   12598 C  CB   . ILE   B 1 208 ? 26.964 1.710   50.731 1.00 23.93 ? 208  ILE   B CB   1 
ATOM   12599 C  CG1  . ILE   B 1 208 ? 27.628 2.866   51.484 1.00 28.04 ? 208  ILE   B CG1  1 
ATOM   12600 C  CG2  . ILE   B 1 208 ? 26.049 0.903   51.640 1.00 21.56 ? 208  ILE   B CG2  1 
ATOM   12601 C  CD1  . ILE   B 1 208 ? 28.135 3.980   50.596 1.00 25.56 ? 208  ILE   B CD1  1 
ATOM   12602 H  H    . ILE   B 1 208 ? 28.036 1.960   48.406 1.00 30.10 ? 208  ILE   B H    1 
ATOM   12603 H  HA   . ILE   B 1 208 ? 28.693 0.651   50.710 1.00 28.64 ? 208  ILE   B HA   1 
ATOM   12604 H  HB   . ILE   B 1 208 ? 26.418 2.106   50.034 1.00 28.72 ? 208  ILE   B HB   1 
ATOM   12605 H  HG12 . ILE   B 1 208 ? 26.991 3.235   52.115 1.00 33.66 ? 208  ILE   B HG12 1 
ATOM   12606 H  HG13 . ILE   B 1 208 ? 28.370 2.517   52.002 1.00 33.66 ? 208  ILE   B HG13 1 
ATOM   12607 H  HG21 . ILE   B 1 208 ? 25.406 1.495   52.060 1.00 25.88 ? 208  ILE   B HG21 1 
ATOM   12608 H  HG22 . ILE   B 1 208 ? 25.579 0.235   51.116 1.00 25.88 ? 208  ILE   B HG22 1 
ATOM   12609 H  HG23 . ILE   B 1 208 ? 26.578 0.463   52.324 1.00 25.88 ? 208  ILE   B HG23 1 
ATOM   12610 H  HD11 . ILE   B 1 208 ? 28.540 4.671   51.143 1.00 30.68 ? 208  ILE   B HD11 1 
ATOM   12611 H  HD12 . ILE   B 1 208 ? 28.796 3.627   49.980 1.00 30.68 ? 208  ILE   B HD12 1 
ATOM   12612 H  HD13 . ILE   B 1 208 ? 27.395 4.357   50.095 1.00 30.68 ? 208  ILE   B HD13 1 
ATOM   12613 N  N    . ALA   B 1 209 ? 27.919 -1.643  50.125 1.00 22.17 ? 209  ALA   B N    1 
ATOM   12614 C  CA   . ALA   B 1 209 ? 27.416 -2.982  49.743 1.00 26.78 ? 209  ALA   B CA   1 
ATOM   12615 C  C    . ALA   B 1 209 ? 25.990 -3.189  50.268 1.00 28.09 ? 209  ALA   B C    1 
ATOM   12616 O  O    . ALA   B 1 209 ? 25.722 -2.794  51.414 1.00 24.81 ? 209  ALA   B O    1 
ATOM   12617 C  CB   . ALA   B 1 209 ? 28.357 -4.042  50.256 1.00 26.36 ? 209  ALA   B CB   1 
ATOM   12618 H  H    . ALA   B 1 209 ? 28.560 -1.650  50.698 1.00 26.61 ? 209  ALA   B H    1 
ATOM   12619 H  HA   . ALA   B 1 209 ? 27.381 -3.050  48.776 1.00 32.14 ? 209  ALA   B HA   1 
ATOM   12620 H  HB1  . ALA   B 1 209 ? 28.026 -4.918  50.005 1.00 31.64 ? 209  ALA   B HB1  1 
ATOM   12621 H  HB2  . ALA   B 1 209 ? 29.237 -3.907  49.871 1.00 31.64 ? 209  ALA   B HB2  1 
ATOM   12622 H  HB3  . ALA   B 1 209 ? 28.415 -3.984  51.223 1.00 31.64 ? 209  ALA   B HB3  1 
ATOM   12623 N  N    . LEU   B 1 210 ? 25.127 -3.808  49.458 1.00 25.36 ? 210  LEU   B N    1 
ATOM   12624 C  CA   . LEU   B 1 210 ? 23.711 -4.024  49.851 1.00 24.97 ? 210  LEU   B CA   1 
ATOM   12625 C  C    . LEU   B 1 210 ? 23.412 -5.524  49.931 1.00 26.00 ? 210  LEU   B C    1 
ATOM   12626 O  O    . LEU   B 1 210 ? 23.840 -6.258  49.024 1.00 25.58 ? 210  LEU   B O    1 
ATOM   12627 C  CB   . LEU   B 1 210 ? 22.804 -3.352  48.817 1.00 27.65 ? 210  LEU   B CB   1 
ATOM   12628 C  CG   . LEU   B 1 210 ? 23.120 -1.891  48.508 1.00 28.81 ? 210  LEU   B CG   1 
ATOM   12629 C  CD1  . LEU   B 1 210 ? 22.186 -1.358  47.433 1.00 29.21 ? 210  LEU   B CD1  1 
ATOM   12630 C  CD2  . LEU   B 1 210 ? 23.027 -1.042  49.766 1.00 23.03 ? 210  LEU   B CD2  1 
ATOM   12631 H  H    . LEU   B 1 210 ? 25.331 -4.112  48.680 1.00 30.43 ? 210  LEU   B H    1 
ATOM   12632 H  HA   . LEU   B 1 210 ? 23.548 -3.635  50.725 1.00 29.97 ? 210  LEU   B HA   1 
ATOM   12633 H  HB2  . LEU   B 1 210 ? 22.853 -3.858  47.991 1.00 33.18 ? 210  LEU   B HB2  1 
ATOM   12634 H  HB3  . LEU   B 1 210 ? 21.888 -3.408  49.130 1.00 33.18 ? 210  LEU   B HB3  1 
ATOM   12635 H  HG   . LEU   B 1 210 ? 24.030 -1.841  48.175 1.00 34.58 ? 210  LEU   B HG   1 
ATOM   12636 H  HD11 . LEU   B 1 210 ? 22.400 -0.430  47.249 1.00 35.06 ? 210  LEU   B HD11 1 
ATOM   12637 H  HD12 . LEU   B 1 210 ? 22.293 -1.881  46.623 1.00 35.06 ? 210  LEU   B HD12 1 
ATOM   12638 H  HD13 . LEU   B 1 210 ? 21.268 -1.423  47.740 1.00 35.06 ? 210  LEU   B HD13 1 
ATOM   12639 H  HD21 . LEU   B 1 210 ? 23.231 -0.119  49.549 1.00 27.64 ? 210  LEU   B HD21 1 
ATOM   12640 H  HD22 . LEU   B 1 210 ? 22.129 -1.098  50.129 1.00 27.64 ? 210  LEU   B HD22 1 
ATOM   12641 H  HD23 . LEU   B 1 210 ? 23.662 -1.367  50.424 1.00 27.64 ? 210  LEU   B HD23 1 
ATOM   12642 N  N    . ALA   B 1 211 ? 22.694 -5.948  50.969 1.00 24.74 ? 211  ALA   B N    1 
ATOM   12643 C  CA   . ALA   B 1 211 ? 22.307 -7.371  51.096 1.00 28.03 ? 211  ALA   B CA   1 
ATOM   12644 C  C    . ALA   B 1 211 ? 21.411 -7.765  49.917 1.00 28.91 ? 211  ALA   B C    1 
ATOM   12645 O  O    . ALA   B 1 211 ? 21.574 -8.886  49.415 1.00 28.06 ? 211  ALA   B O    1 
ATOM   12646 C  CB   . ALA   B 1 211 ? 21.618 -7.602  52.413 1.00 28.74 ? 211  ALA   B CB   1 
ATOM   12647 H  H    . ALA   B 1 211 ? 22.420 -5.442  51.608 1.00 29.70 ? 211  ALA   B H    1 
ATOM   12648 H  HA   . ALA   B 1 211 ? 23.100 -7.930  51.075 1.00 33.64 ? 211  ALA   B HA   1 
ATOM   12649 H  HB1  . ALA   B 1 211 ? 21.368 -8.536  52.488 1.00 34.49 ? 211  ALA   B HB1  1 
ATOM   12650 H  HB2  . ALA   B 1 211 ? 22.219 -7.369  53.138 1.00 34.49 ? 211  ALA   B HB2  1 
ATOM   12651 H  HB3  . ALA   B 1 211 ? 20.822 -7.050  52.463 1.00 34.49 ? 211  ALA   B HB3  1 
ATOM   12652 N  N    . ASP   B 1 212 ? 20.509 -6.874  49.494 1.00 30.76 ? 212  ASP   B N    1 
ATOM   12653 C  CA   . ASP   B 1 212 ? 19.557 -7.182  48.393 1.00 33.20 ? 212  ASP   B CA   1 
ATOM   12654 C  C    . ASP   B 1 212 ? 19.308 -5.909  47.583 1.00 32.68 ? 212  ASP   B C    1 
ATOM   12655 O  O    . ASP   B 1 212 ? 18.338 -5.195  47.897 1.00 29.99 ? 212  ASP   B O    1 
ATOM   12656 C  CB   . ASP   B 1 212 ? 18.257 -7.779  48.935 1.00 35.77 ? 212  ASP   B CB   1 
ATOM   12657 C  CG   . ASP   B 1 212 ? 17.333 -8.336  47.865 1.00 39.98 ? 212  ASP   B CG   1 
ATOM   12658 O  OD1  . ASP   B 1 212 ? 17.434 -7.891  46.705 1.00 39.70 ? 212  ASP   B OD1  1 
ATOM   12659 O  OD2  . ASP   B 1 212 ? 16.512 -9.206  48.205 1.00 38.72 ? 212  ASP   B OD2  1 
ATOM   12660 H  H    . ASP   B 1 212 ? 20.424 -6.085  49.824 1.00 36.92 ? 212  ASP   B H    1 
ATOM   12661 H  HA   . ASP   B 1 212 ? 19.943 -7.854  47.809 1.00 39.84 ? 212  ASP   B HA   1 
ATOM   12662 H  HB2  . ASP   B 1 212 ? 18.475 -8.487  49.561 1.00 42.93 ? 212  ASP   B HB2  1 
ATOM   12663 H  HB3  . ASP   B 1 212 ? 17.783 -7.096  49.434 1.00 42.93 ? 212  ASP   B HB3  1 
ATOM   12664 N  N    . LYS   B 1 213 ? 20.130 -5.661  46.565 1.00 30.36 ? 213  LYS   B N    1 
ATOM   12665 C  CA   . LYS   B 1 213 ? 20.024 -4.413  45.764 1.00 35.54 ? 213  LYS   B CA   1 
ATOM   12666 C  C    . LYS   B 1 213 ? 18.598 -4.223  45.239 1.00 34.11 ? 213  LYS   B C    1 
ATOM   12667 O  O    . LYS   B 1 213 ? 18.075 -3.101  45.338 1.00 32.12 ? 213  LYS   B O    1 
ATOM   12668 C  CB   . LYS   B 1 213 ? 21.023 -4.463  44.606 1.00 42.27 ? 213  LYS   B CB   1 
ATOM   12669 C  CG   . LYS   B 1 213 ? 20.720 -3.536  43.438 1.00 53.79 ? 213  LYS   B CG   1 
ATOM   12670 C  CD   . LYS   B 1 213 ? 21.251 -4.059  42.122 1.00 54.15 ? 213  LYS   B CD   1 
ATOM   12671 C  CE   . LYS   B 1 213 ? 20.897 -3.173  40.947 1.00 60.07 ? 213  LYS   B CE   1 
ATOM   12672 N  NZ   . LYS   B 1 213 ? 22.107 -2.602  40.311 1.00 63.72 ? 213  LYS   B NZ   1 
ATOM   12673 H  H    . LYS   B 1 213 ? 20.757 -6.193  46.313 1.00 36.44 ? 213  LYS   B H    1 
ATOM   12674 H  HA   . LYS   B 1 213 ? 20.234 -3.655  46.332 1.00 42.65 ? 213  LYS   B HA   1 
ATOM   12675 H  HB2  . LYS   B 1 213 ? 21.904 -4.247  44.950 1.00 50.73 ? 213  LYS   B HB2  1 
ATOM   12676 H  HB3  . LYS   B 1 213 ? 21.064 -5.373  44.274 1.00 50.73 ? 213  LYS   B HB3  1 
ATOM   12677 H  HG2  . LYS   B 1 213 ? 19.760 -3.413  43.369 1.00 64.55 ? 213  LYS   B HG2  1 
ATOM   12678 H  HG3  . LYS   B 1 213 ? 21.106 -2.664  43.614 1.00 64.55 ? 213  LYS   B HG3  1 
ATOM   12679 H  HD2  . LYS   B 1 213 ? 22.216 -4.142  42.179 1.00 64.99 ? 213  LYS   B HD2  1 
ATOM   12680 H  HD3  . LYS   B 1 213 ? 20.898 -4.949  41.967 1.00 64.99 ? 213  LYS   B HD3  1 
ATOM   12681 H  HE2  . LYS   B 1 213 ? 20.398 -3.686  40.292 1.00 72.09 ? 213  LYS   B HE2  1 
ATOM   12682 H  HE3  . LYS   B 1 213 ? 20.318 -2.455  41.245 1.00 72.09 ? 213  LYS   B HE3  1 
ATOM   12683 H  HZ1  . LYS   B 1 213 ? 21.868 -2.087  39.626 1.00 76.46 ? 213  LYS   B HZ1  1 
ATOM   12684 H  HZ2  . LYS   B 1 213 ? 22.553 -2.114  40.906 1.00 76.46 ? 213  LYS   B HZ2  1 
ATOM   12685 H  HZ3  . LYS   B 1 213 ? 22.628 -3.261  40.018 1.00 76.46 ? 213  LYS   B HZ3  1 
ATOM   12686 N  N    . GLU   B 1 214 ? 17.998 -5.280  44.696 1.00 34.70 ? 214  GLU   B N    1 
ATOM   12687 C  CA   . GLU   B 1 214 ? 16.650 -5.149  44.088 1.00 36.35 ? 214  GLU   B CA   1 
ATOM   12688 C  C    . GLU   B 1 214 ? 15.637 -4.741  45.162 1.00 33.25 ? 214  GLU   B C    1 
ATOM   12689 O  O    . GLU   B 1 214 ? 14.800 -3.863  44.889 1.00 32.99 ? 214  GLU   B O    1 
ATOM   12690 C  CB   . GLU   B 1 214 ? 16.267 -6.472  43.424 1.00 40.32 ? 214  GLU   B CB   1 
ATOM   12691 C  CG   . GLU   B 1 214 ? 17.154 -6.837  42.249 1.00 58.39 ? 214  GLU   B CG   1 
ATOM   12692 C  CD   . GLU   B 1 214 ? 17.190 -5.807  41.135 1.00 59.73 ? 214  GLU   B CD   1 
ATOM   12693 O  OE1  . GLU   B 1 214 ? 16.125 -5.238  40.820 1.00 53.73 ? 214  GLU   B OE1  1 
ATOM   12694 O  OE2  . GLU   B 1 214 ? 18.284 -5.575  40.587 1.00 61.93 ? 214  GLU   B OE2  1 
ATOM   12695 H  H    . GLU   B 1 214 ? 18.336 -6.070  44.664 1.00 41.65 ? 214  GLU   B H    1 
ATOM   12696 H  HA   . GLU   B 1 214 ? 16.654 -4.458  43.407 1.00 43.62 ? 214  GLU   B HA   1 
ATOM   12697 H  HB2  . GLU   B 1 214 ? 16.309 -7.181  44.084 1.00 48.38 ? 214  GLU   B HB2  1 
ATOM   12698 H  HB3  . GLU   B 1 214 ? 15.347 -6.420  43.122 1.00 48.38 ? 214  GLU   B HB3  1 
ATOM   12699 H  HG2  . GLU   B 1 214 ? 18.058 -6.976  42.573 1.00 70.07 ? 214  GLU   B HG2  1 
ATOM   12700 H  HG3  . GLU   B 1 214 ? 16.851 -7.682  41.881 1.00 70.07 ? 214  GLU   B HG3  1 
ATOM   12701 N  N    . LYS   B 1 215 ? 15.714 -5.377  46.329 1.00 30.91 ? 215  LYS   B N    1 
ATOM   12702 C  CA   . LYS   B 1 215 ? 14.760 -5.060  47.421 1.00 33.95 ? 215  LYS   B CA   1 
ATOM   12703 C  C    . LYS   B 1 215 ? 14.991 -3.615  47.873 1.00 28.75 ? 215  LYS   B C    1 
ATOM   12704 O  O    . LYS   B 1 215 ? 14.005 -2.900  48.105 1.00 28.55 ? 215  LYS   B O    1 
ATOM   12705 C  CB   . LYS   B 1 215 ? 14.936 -6.032  48.588 1.00 32.83 ? 215  LYS   B CB   1 
ATOM   12706 C  CG   . LYS   B 1 215 ? 14.025 -5.777  49.780 1.00 35.45 ? 215  LYS   B CG   1 
ATOM   12707 C  CD   . LYS   B 1 215 ? 13.811 -6.997  50.645 1.00 41.80 ? 215  LYS   B CD   1 
ATOM   12708 C  CE   . LYS   B 1 215 ? 12.445 -7.025  51.296 1.00 45.36 ? 215  LYS   B CE   1 
ATOM   12709 N  NZ   . LYS   B 1 215 ? 11.778 -5.703  51.236 1.00 47.58 ? 215  LYS   B NZ   1 
ATOM   12710 H  H    . LYS   B 1 215 ? 16.294 -5.984  46.517 1.00 37.10 ? 215  LYS   B H    1 
ATOM   12711 H  HA   . LYS   B 1 215 ? 13.850 -5.154  47.098 1.00 40.75 ? 215  LYS   B HA   1 
ATOM   12712 H  HB2  . LYS   B 1 215 ? 14.781 -6.934  48.266 1.00 39.40 ? 215  LYS   B HB2  1 
ATOM   12713 H  HB3  . LYS   B 1 215 ? 15.858 -5.993  48.888 1.00 39.40 ? 215  LYS   B HB3  1 
ATOM   12714 H  HG2  . LYS   B 1 215 ? 14.404 -5.067  50.322 1.00 42.54 ? 215  LYS   B HG2  1 
ATOM   12715 H  HG3  . LYS   B 1 215 ? 13.166 -5.461  49.460 1.00 42.54 ? 215  LYS   B HG3  1 
ATOM   12716 H  HD2  . LYS   B 1 215 ? 13.923 -7.795  50.105 1.00 50.17 ? 215  LYS   B HD2  1 
ATOM   12717 H  HD3  . LYS   B 1 215 ? 14.493 -7.023  51.334 1.00 50.17 ? 215  LYS   B HD3  1 
ATOM   12718 H  HE2  . LYS   B 1 215 ? 11.890 -7.687  50.855 1.00 54.44 ? 215  LYS   B HE2  1 
ATOM   12719 H  HE3  . LYS   B 1 215 ? 12.534 -7.301  52.222 1.00 54.44 ? 215  LYS   B HE3  1 
ATOM   12720 H  HZ1  . LYS   B 1 215 ? 11.083 -5.695  51.792 1.00 57.10 ? 215  LYS   B HZ1  1 
ATOM   12721 H  HZ2  . LYS   B 1 215 ? 12.355 -5.068  51.473 1.00 57.10 ? 215  LYS   B HZ2  1 
ATOM   12722 H  HZ3  . LYS   B 1 215 ? 11.495 -5.551  50.406 1.00 57.10 ? 215  LYS   B HZ3  1 
ATOM   12723 N  N    . VAL   B 1 216 ? 16.257 -3.216  47.970 1.00 29.59 ? 216  VAL   B N    1 
ATOM   12724 C  CA   . VAL   B 1 216 ? 16.581 -1.825  48.395 1.00 26.14 ? 216  VAL   B CA   1 
ATOM   12725 C  C    . VAL   B 1 216 ? 15.911 -0.858  47.415 1.00 25.99 ? 216  VAL   B C    1 
ATOM   12726 O  O    . VAL   B 1 216 ? 15.259 0.089   47.874 1.00 27.52 ? 216  VAL   B O    1 
ATOM   12727 C  CB   . VAL   B 1 216 ? 18.103 -1.603  48.471 1.00 27.44 ? 216  VAL   B CB   1 
ATOM   12728 C  CG1  . VAL   B 1 216 ? 18.447 -0.144  48.727 1.00 26.80 ? 216  VAL   B CG1  1 
ATOM   12729 C  CG2  . VAL   B 1 216 ? 18.756 -2.500  49.509 1.00 26.25 ? 216  VAL   B CG2  1 
ATOM   12730 H  H    . VAL   B 1 216 ? 16.939 -3.712  47.801 1.00 35.51 ? 216  VAL   B H    1 
ATOM   12731 H  HA   . VAL   B 1 216 ? 16.241 -1.664  49.289 1.00 31.38 ? 216  VAL   B HA   1 
ATOM   12732 H  HB   . VAL   B 1 216 ? 18.462 -1.846  47.603 1.00 32.93 ? 216  VAL   B HB   1 
ATOM   12733 H  HG11 . VAL   B 1 216 ? 19.411 -0.041  48.769 1.00 32.17 ? 216  VAL   B HG11 1 
ATOM   12734 H  HG12 . VAL   B 1 216 ? 18.095 0.403   48.007 1.00 32.17 ? 216  VAL   B HG12 1 
ATOM   12735 H  HG13 . VAL   B 1 216 ? 18.055 0.138   49.568 1.00 32.17 ? 216  VAL   B HG13 1 
ATOM   12736 H  HG21 . VAL   B 1 216 ? 19.711 -2.332  49.527 1.00 31.50 ? 216  VAL   B HG21 1 
ATOM   12737 H  HG22 . VAL   B 1 216 ? 18.378 -2.313  50.383 1.00 31.50 ? 216  VAL   B HG22 1 
ATOM   12738 H  HG23 . VAL   B 1 216 ? 18.596 -3.429  49.281 1.00 31.50 ? 216  VAL   B HG23 1 
ATOM   12739 N  N    . LYS   B 1 217 ? 16.048 -1.116  46.112 1.00 25.44 ? 217  LYS   B N    1 
ATOM   12740 C  CA   . LYS   B 1 217 ? 15.484 -0.200  45.084 1.00 26.32 ? 217  LYS   B CA   1 
ATOM   12741 C  C    . LYS   B 1 217 ? 13.960 -0.128  45.221 1.00 26.55 ? 217  LYS   B C    1 
ATOM   12742 O  O    . LYS   B 1 217 ? 13.409 0.981   45.147 1.00 26.91 ? 217  LYS   B O    1 
ATOM   12743 C  CB   . LYS   B 1 217 ? 15.879 -0.683  43.687 1.00 33.14 ? 217  LYS   B CB   1 
ATOM   12744 C  CG   . LYS   B 1 217 ? 15.422 0.212   42.544 1.00 40.59 ? 217  LYS   B CG   1 
ATOM   12745 C  CD   . LYS   B 1 217 ? 15.879 -0.285  41.192 1.00 50.14 ? 217  LYS   B CD   1 
ATOM   12746 C  CE   . LYS   B 1 217 ? 15.408 0.587   40.048 1.00 58.01 ? 217  LYS   B CE   1 
ATOM   12747 N  NZ   . LYS   B 1 217 ? 15.875 0.069   38.741 1.00 61.79 ? 217  LYS   B NZ   1 
ATOM   12748 H  H    . LYS   B 1 217 ? 16.456 -1.803  45.795 1.00 30.53 ? 217  LYS   B H    1 
ATOM   12749 H  HA   . LYS   B 1 217 ? 15.844 0.691   45.218 1.00 31.58 ? 217  LYS   B HA   1 
ATOM   12750 H  HB2  . LYS   B 1 217 ? 16.845 -0.765  43.649 1.00 39.77 ? 217  LYS   B HB2  1 
ATOM   12751 H  HB3  . LYS   B 1 217 ? 15.513 -1.571  43.551 1.00 39.77 ? 217  LYS   B HB3  1 
ATOM   12752 H  HG2  . LYS   B 1 217 ? 14.454 0.271   42.552 1.00 48.71 ? 217  LYS   B HG2  1 
ATOM   12753 H  HG3  . LYS   B 1 217 ? 15.762 1.109   42.686 1.00 48.71 ? 217  LYS   B HG3  1 
ATOM   12754 H  HD2  . LYS   B 1 217 ? 16.848 -0.329  41.180 1.00 60.17 ? 217  LYS   B HD2  1 
ATOM   12755 H  HD3  . LYS   B 1 217 ? 15.552 -1.189  41.058 1.00 60.17 ? 217  LYS   B HD3  1 
ATOM   12756 H  HE2  . LYS   B 1 217 ? 14.439 0.632   40.052 1.00 69.62 ? 217  LYS   B HE2  1 
ATOM   12757 H  HE3  . LYS   B 1 217 ? 15.734 1.492   40.174 1.00 69.62 ? 217  LYS   B HE3  1 
ATOM   12758 H  HZ1  . LYS   B 1 217 ? 15.584 0.601   38.089 1.00 74.16 ? 217  LYS   B HZ1  1 
ATOM   12759 H  HZ2  . LYS   B 1 217 ? 16.765 0.048   38.731 1.00 74.16 ? 217  LYS   B HZ2  1 
ATOM   12760 H  HZ3  . LYS   B 1 217 ? 15.558 -0.753  38.617 1.00 74.16 ? 217  LYS   B HZ3  1 
ATOM   12761 N  N    . LYS   B 1 218 ? 13.317 -1.275  45.436 1.00 26.76 ? 218  LYS   B N    1 
ATOM   12762 C  CA   . LYS   B 1 218 ? 11.835 -1.309  45.521 1.00 30.13 ? 218  LYS   B CA   1 
ATOM   12763 C  C    . LYS   B 1 218 ? 11.396 -0.586  46.800 1.00 29.18 ? 218  LYS   B C    1 
ATOM   12764 O  O    . LYS   B 1 218 ? 10.458 0.228   46.733 1.00 30.07 ? 218  LYS   B O    1 
ATOM   12765 C  CB   . LYS   B 1 218 ? 11.356 -2.763  45.490 1.00 34.74 ? 218  LYS   B CB   1 
ATOM   12766 C  CG   . LYS   B 1 218 ? 9.899  -2.975  45.875 1.00 49.94 ? 218  LYS   B CG   1 
ATOM   12767 C  CD   . LYS   B 1 218 ? 9.387  -4.365  45.564 1.00 50.18 ? 218  LYS   B CD   1 
ATOM   12768 C  CE   . LYS   B 1 218 ? 7.877  -4.465  45.622 1.00 44.76 ? 218  LYS   B CE   1 
ATOM   12769 N  NZ   . LYS   B 1 218 ? 7.257  -3.182  46.033 1.00 50.59 ? 218  LYS   B NZ   1 
ATOM   12770 H  H    . LYS   B 1 218 ? 13.702 -2.037  45.535 1.00 32.12 ? 218  LYS   B H    1 
ATOM   12771 H  HA   . LYS   B 1 218 ? 11.436 -0.853  44.764 1.00 36.16 ? 218  LYS   B HA   1 
ATOM   12772 H  HB2  . LYS   B 1 218 ? 11.494 -3.115  44.597 1.00 41.69 ? 218  LYS   B HB2  1 
ATOM   12773 H  HB3  . LYS   B 1 218 ? 11.913 -3.285  46.089 1.00 41.69 ? 218  LYS   B HB3  1 
ATOM   12774 H  HG2  . LYS   B 1 218 ? 9.795  -2.805  46.824 1.00 59.94 ? 218  LYS   B HG2  1 
ATOM   12775 H  HG3  . LYS   B 1 218 ? 9.351  -2.325  45.409 1.00 59.94 ? 218  LYS   B HG3  1 
ATOM   12776 H  HD2  . LYS   B 1 218 ? 9.690  -4.626  44.680 1.00 60.22 ? 218  LYS   B HD2  1 
ATOM   12777 H  HD3  . LYS   B 1 218 ? 9.772  -4.995  46.193 1.00 60.22 ? 218  LYS   B HD3  1 
ATOM   12778 H  HE2  . LYS   B 1 218 ? 7.536  -4.725  44.752 1.00 53.72 ? 218  LYS   B HE2  1 
ATOM   12779 H  HE3  . LYS   B 1 218 ? 7.622  -5.162  46.246 1.00 53.72 ? 218  LYS   B HE3  1 
ATOM   12780 H  HZ1  . LYS   B 1 218 ? 6.383  -3.300  46.156 1.00 60.72 ? 218  LYS   B HZ1  1 
ATOM   12781 H  HZ2  . LYS   B 1 218 ? 7.628  -2.903  46.792 1.00 60.72 ? 218  LYS   B HZ2  1 
ATOM   12782 H  HZ3  . LYS   B 1 218 ? 7.387  -2.572  45.398 1.00 60.72 ? 218  LYS   B HZ3  1 
ATOM   12783 N  N    . VAL   B 1 219 ? 12.076 -0.870  47.907 1.00 25.71 ? 219  VAL   B N    1 
ATOM   12784 C  CA   . VAL   B 1 219 ? 11.732 -0.228  49.209 1.00 26.73 ? 219  VAL   B CA   1 
ATOM   12785 C  C    . VAL   B 1 219 ? 11.893 1.290   49.061 1.00 26.35 ? 219  VAL   B C    1 
ATOM   12786 O  O    . VAL   B 1 219 ? 10.990 2.021   49.496 1.00 26.80 ? 219  VAL   B O    1 
ATOM   12787 C  CB   . VAL   B 1 219 ? 12.607 -0.793  50.343 1.00 25.97 ? 219  VAL   B CB   1 
ATOM   12788 C  CG1  . VAL   B 1 219 ? 12.554 0.078   51.588 1.00 27.65 ? 219  VAL   B CG1  1 
ATOM   12789 C  CG2  . VAL   B 1 219 ? 12.234 -2.227  50.681 1.00 31.28 ? 219  VAL   B CG2  1 
ATOM   12790 H  H    . VAL   B 1 219 ? 12.734 -1.422  47.942 1.00 30.86 ? 219  VAL   B H    1 
ATOM   12791 H  HA   . VAL   B 1 219 ? 10.812 -0.424  49.446 1.00 32.08 ? 219  VAL   B HA   1 
ATOM   12792 H  HB   . VAL   B 1 219 ? 13.520 -0.789  50.015 1.00 31.16 ? 219  VAL   B HB   1 
ATOM   12793 H  HG11 . VAL   B 1 219 ? 13.116 -0.309  52.278 1.00 33.18 ? 219  VAL   B HG11 1 
ATOM   12794 H  HG12 . VAL   B 1 219 ? 12.873 0.969   51.374 1.00 33.18 ? 219  VAL   B HG12 1 
ATOM   12795 H  HG13 . VAL   B 1 219 ? 11.640 0.131   51.908 1.00 33.18 ? 219  VAL   B HG13 1 
ATOM   12796 H  HG21 . VAL   B 1 219 ? 12.804 -2.550  51.397 1.00 37.54 ? 219  VAL   B HG21 1 
ATOM   12797 H  HG22 . VAL   B 1 219 ? 11.307 -2.262  50.965 1.00 37.54 ? 219  VAL   B HG22 1 
ATOM   12798 H  HG23 . VAL   B 1 219 ? 12.353 -2.786  49.897 1.00 37.54 ? 219  VAL   B HG23 1 
ATOM   12799 N  N    . SER   B 1 220 ? 12.991 1.736   48.443 1.00 27.59 ? 220  SER   B N    1 
ATOM   12800 C  CA   . SER   B 1 220 ? 13.258 3.194   48.305 1.00 25.07 ? 220  SER   B CA   1 
ATOM   12801 C  C    . SER   B 1 220 ? 12.125 3.880   47.535 1.00 22.31 ? 220  SER   B C    1 
ATOM   12802 O  O    . SER   B 1 220 ? 11.658 4.931   47.989 1.00 26.82 ? 220  SER   B O    1 
ATOM   12803 C  CB   . SER   B 1 220 ? 14.591 3.450   47.659 1.00 27.39 ? 220  SER   B CB   1 
ATOM   12804 O  OG   . SER   B 1 220 ? 14.720 4.809   47.275 1.00 25.10 ? 220  SER   B OG   1 
ATOM   12805 H  H    . SER   B 1 220 ? 13.592 1.227   48.098 1.00 33.11 ? 220  SER   B H    1 
ATOM   12806 H  HA   . SER   B 1 220 ? 13.292 3.577   49.195 1.00 30.09 ? 220  SER   B HA   1 
ATOM   12807 H  HB2  . SER   B 1 220 ? 15.303 3.216   48.275 1.00 32.88 ? 220  SER   B HB2  1 
ATOM   12808 H  HB3  . SER   B 1 220 ? 14.691 2.880   46.881 1.00 32.88 ? 220  SER   B HB3  1 
ATOM   12809 H  HG   . SER   B 1 220 ? 14.385 4.918   46.512 1.00 30.13 ? 220  SER   B HG   1 
ATOM   12810 N  N    . VAL   B 1 221 ? 11.720 3.304   46.402 1.00 29.92 ? 221  VAL   B N    1 
ATOM   12811 C  CA   . VAL   B 1 221 ? 10.649 3.922   45.565 1.00 30.94 ? 221  VAL   B CA   1 
ATOM   12812 C  C    . VAL   B 1 221 ? 9.395  4.077   46.429 1.00 29.65 ? 221  VAL   B C    1 
ATOM   12813 O  O    . VAL   B 1 221 ? 8.763  5.144   46.378 1.00 29.28 ? 221  VAL   B O    1 
ATOM   12814 C  CB   . VAL   B 1 221 ? 10.372 3.080   44.303 1.00 35.57 ? 221  VAL   B CB   1 
ATOM   12815 C  CG1  . VAL   B 1 221 ? 8.973  3.317   43.755 1.00 36.60 ? 221  VAL   B CG1  1 
ATOM   12816 C  CG2  . VAL   B 1 221 ? 11.420 3.318   43.230 1.00 30.91 ? 221  VAL   B CG2  1 
ATOM   12817 H  H    . VAL   B 1 221 ? 12.038 2.567   46.093 1.00 35.90 ? 221  VAL   B H    1 
ATOM   12818 H  HA   . VAL   B 1 221 ? 10.935 4.795   45.253 1.00 37.13 ? 221  VAL   B HA   1 
ATOM   12819 H  HB   . VAL   B 1 221 ? 10.426 2.150   44.572 1.00 42.68 ? 221  VAL   B HB   1 
ATOM   12820 H  HG11 . VAL   B 1 221 ? 8.838  2.771   42.964 1.00 43.93 ? 221  VAL   B HG11 1 
ATOM   12821 H  HG12 . VAL   B 1 221 ? 8.317  3.078   44.428 1.00 43.93 ? 221  VAL   B HG12 1 
ATOM   12822 H  HG13 . VAL   B 1 221 ? 8.871  4.253   43.522 1.00 43.93 ? 221  VAL   B HG13 1 
ATOM   12823 H  HG21 . VAL   B 1 221 ? 11.217 2.775   42.453 1.00 37.09 ? 221  VAL   B HG21 1 
ATOM   12824 H  HG22 . VAL   B 1 221 ? 11.419 4.255   42.979 1.00 37.09 ? 221  VAL   B HG22 1 
ATOM   12825 H  HG23 . VAL   B 1 221 ? 12.295 3.077   43.573 1.00 37.09 ? 221  VAL   B HG23 1 
ATOM   12826 N  N    . GLU   B 1 222 ? 9.072  3.045   47.205 1.00 27.36 ? 222  GLU   B N    1 
ATOM   12827 C  CA   . GLU   B 1 222 ? 7.858  3.084   48.055 1.00 27.59 ? 222  GLU   B CA   1 
ATOM   12828 C  C    . GLU   B 1 222 ? 7.969  4.233   49.064 1.00 24.85 ? 222  GLU   B C    1 
ATOM   12829 O  O    . GLU   B 1 222 ? 7.029  5.041   49.149 1.00 21.02 ? 222  GLU   B O    1 
ATOM   12830 C  CB   . GLU   B 1 222 ? 7.689  1.743   48.768 1.00 30.50 ? 222  GLU   B CB   1 
ATOM   12831 C  CG   . GLU   B 1 222 ? 6.618  1.763   49.840 1.00 32.41 ? 222  GLU   B CG   1 
ATOM   12832 C  CD   . GLU   B 1 222 ? 6.441  0.439   50.560 1.00 37.92 ? 222  GLU   B CD   1 
ATOM   12833 O  OE1  . GLU   B 1 222 ? 6.476  -0.606  49.884 1.00 43.20 ? 222  GLU   B OE1  1 
ATOM   12834 O  OE2  . GLU   B 1 222 ? 6.272  0.456   51.792 1.00 44.23 ? 222  GLU   B OE2  1 
ATOM   12835 H  H    . GLU   B 1 222 ? 9.528  2.318   47.261 1.00 32.84 ? 222  GLU   B H    1 
ATOM   12836 H  HA   . GLU   B 1 222 ? 7.076  3.239   47.503 1.00 33.11 ? 222  GLU   B HA   1 
ATOM   12837 H  HB2  . GLU   B 1 222 ? 7.470  1.062   48.113 1.00 36.60 ? 222  GLU   B HB2  1 
ATOM   12838 H  HB3  . GLU   B 1 222 ? 8.535  1.489   49.170 1.00 36.60 ? 222  GLU   B HB3  1 
ATOM   12839 H  HG2  . GLU   B 1 222 ? 6.838  2.448   50.491 1.00 38.90 ? 222  GLU   B HG2  1 
ATOM   12840 H  HG3  . GLU   B 1 222 ? 5.773  2.016   49.436 1.00 38.90 ? 222  GLU   B HG3  1 
ATOM   12841 N  N    . LYS   B 1 223 ? 9.083  4.293   49.800 1.00 26.66 ? 223  LYS   B N    1 
ATOM   12842 C  CA   . LYS   B 1 223 ? 9.216  5.325   50.866 1.00 22.26 ? 223  LYS   B CA   1 
ATOM   12843 C  C    . LYS   B 1 223 ? 9.208  6.727   50.238 1.00 23.30 ? 223  LYS   B C    1 
ATOM   12844 O  O    . LYS   B 1 223 ? 8.568  7.625   50.806 1.00 25.31 ? 223  LYS   B O    1 
ATOM   12845 C  CB   . LYS   B 1 223 ? 10.470 5.071   51.709 1.00 20.15 ? 223  LYS   B CB   1 
ATOM   12846 C  CG   . LYS   B 1 223 ? 10.600 3.667   52.285 1.00 22.71 ? 223  LYS   B CG   1 
ATOM   12847 C  CD   . LYS   B 1 223 ? 9.288  3.087   52.768 1.00 24.95 ? 223  LYS   B CD   1 
ATOM   12848 C  CE   . LYS   B 1 223 ? 9.426  1.667   53.275 1.00 25.76 ? 223  LYS   B CE   1 
ATOM   12849 N  NZ   . LYS   B 1 223 ? 8.114  1.078   53.625 1.00 28.97 ? 223  LYS   B NZ   1 
ATOM   12850 H  H    . LYS   B 1 223 ? 9.759  3.769   49.711 1.00 31.99 ? 223  LYS   B H    1 
ATOM   12851 H  HA   . LYS   B 1 223 ? 8.457  5.268   51.468 1.00 26.71 ? 223  LYS   B HA   1 
ATOM   12852 H  HB2  . LYS   B 1 223 ? 11.250 5.253   51.162 1.00 24.18 ? 223  LYS   B HB2  1 
ATOM   12853 H  HB3  . LYS   B 1 223 ? 10.482 5.707   52.442 1.00 24.18 ? 223  LYS   B HB3  1 
ATOM   12854 H  HG2  . LYS   B 1 223 ? 10.974 3.081   51.609 1.00 27.25 ? 223  LYS   B HG2  1 
ATOM   12855 H  HG3  . LYS   B 1 223 ? 11.228 3.685   53.024 1.00 27.25 ? 223  LYS   B HG3  1 
ATOM   12856 H  HD2  . LYS   B 1 223 ? 8.933  3.646   53.477 1.00 29.95 ? 223  LYS   B HD2  1 
ATOM   12857 H  HD3  . LYS   B 1 223 ? 8.644  3.106   52.043 1.00 29.95 ? 223  LYS   B HD3  1 
ATOM   12858 H  HE2  . LYS   B 1 223 ? 9.855  1.122   52.597 1.00 30.92 ? 223  LYS   B HE2  1 
ATOM   12859 H  HE3  . LYS   B 1 223 ? 10.003 1.657   54.054 1.00 30.92 ? 223  LYS   B HE3  1 
ATOM   12860 H  HZ1  . LYS   B 1 223 ? 8.238  0.286   54.012 1.00 34.77 ? 223  LYS   B HZ1  1 
ATOM   12861 H  HZ2  . LYS   B 1 223 ? 7.686  1.619   54.187 1.00 34.77 ? 223  LYS   B HZ2  1 
ATOM   12862 H  HZ3  . LYS   B 1 223 ? 7.629  0.974   52.886 1.00 34.77 ? 223  LYS   B HZ3  1 
ATOM   12863 N  N    . ILE   B 1 224 ? 9.900  6.900   49.111 1.00 24.96 ? 224  ILE   B N    1 
ATOM   12864 C  CA   . ILE   B 1 224 ? 9.962  8.244   48.465 1.00 24.41 ? 224  ILE   B CA   1 
ATOM   12865 C  C    . ILE   B 1 224 ? 8.535  8.636   48.063 1.00 27.02 ? 224  ILE   B C    1 
ATOM   12866 O  O    . ILE   B 1 224 ? 8.158  9.802   48.258 1.00 24.35 ? 224  ILE   B O    1 
ATOM   12867 C  CB   . ILE   B 1 224 ? 10.956 8.256   47.288 1.00 25.70 ? 224  ILE   B CB   1 
ATOM   12868 C  CG1  . ILE   B 1 224 ? 12.404 8.194   47.782 1.00 25.77 ? 224  ILE   B CG1  1 
ATOM   12869 C  CG2  . ILE   B 1 224 ? 10.719 9.454   46.385 1.00 27.22 ? 224  ILE   B CG2  1 
ATOM   12870 C  CD1  . ILE   B 1 224 ? 13.417 7.947   46.692 1.00 25.30 ? 224  ILE   B CD1  1 
ATOM   12871 H  H    . ILE   B 1 224 ? 10.334 6.279   48.703 1.00 29.95 ? 224  ILE   B H    1 
ATOM   12872 H  HA   . ILE   B 1 224 ? 10.303 8.909   49.084 1.00 29.29 ? 224  ILE   B HA   1 
ATOM   12873 H  HB   . ILE   B 1 224 ? 10.800 7.459   46.758 1.00 30.85 ? 224  ILE   B HB   1 
ATOM   12874 H  HG12 . ILE   B 1 224 ? 12.620 9.028   48.227 1.00 30.93 ? 224  ILE   B HG12 1 
ATOM   12875 H  HG13 . ILE   B 1 224 ? 12.479 7.490   48.446 1.00 30.93 ? 224  ILE   B HG13 1 
ATOM   12876 H  HG21 . ILE   B 1 224 ? 11.356 9.439   45.653 1.00 32.66 ? 224  ILE   B HG21 1 
ATOM   12877 H  HG22 . ILE   B 1 224 ? 9.817  9.418   46.029 1.00 32.66 ? 224  ILE   B HG22 1 
ATOM   12878 H  HG23 . ILE   B 1 224 ? 10.832 10.271  46.895 1.00 32.66 ? 224  ILE   B HG23 1 
ATOM   12879 H  HD11 . ILE   B 1 224 ? 14.307 7.920   47.077 1.00 30.36 ? 224  ILE   B HD11 1 
ATOM   12880 H  HD12 . ILE   B 1 224 ? 13.227 7.100   46.259 1.00 30.36 ? 224  ILE   B HD12 1 
ATOM   12881 H  HD13 . ILE   B 1 224 ? 13.369 8.662   46.038 1.00 30.36 ? 224  ILE   B HD13 1 
ATOM   12882 N  N    . THR   B 1 225 ? 7.771  7.678   47.531 1.00 29.15 ? 225  THR   B N    1 
ATOM   12883 C  CA   . THR   B 1 225 ? 6.374  7.963   47.111 1.00 27.89 ? 225  THR   B CA   1 
ATOM   12884 C  C    . THR   B 1 225 ? 5.570  8.492   48.307 1.00 26.68 ? 225  THR   B C    1 
ATOM   12885 O  O    . THR   B 1 225 ? 4.870  9.507   48.145 1.00 25.67 ? 225  THR   B O    1 
ATOM   12886 C  CB   . THR   B 1 225 ? 5.743  6.732   46.443 1.00 31.35 ? 225  THR   B CB   1 
ATOM   12887 O  OG1  . THR   B 1 225 ? 6.443  6.476   45.225 1.00 35.06 ? 225  THR   B OG1  1 
ATOM   12888 C  CG2  . THR   B 1 225 ? 4.267  6.909   46.167 1.00 28.42 ? 225  THR   B CG2  1 
ATOM   12889 H  H    . THR   B 1 225 ? 8.028  6.867   47.403 1.00 34.99 ? 225  THR   B H    1 
ATOM   12890 H  HA   . THR   B 1 225 ? 6.368  8.660   46.437 1.00 33.47 ? 225  THR   B HA   1 
ATOM   12891 H  HB   . THR   B 1 225 ? 5.819  5.982   47.053 1.00 37.62 ? 225  THR   B HB   1 
ATOM   12892 H  HG1  . THR   B 1 225 ? 7.158  6.069   45.393 1.00 42.08 ? 225  THR   B HG1  1 
ATOM   12893 H  HG21 . THR   B 1 225 ? 3.918  6.108   45.747 1.00 34.11 ? 225  THR   B HG21 1 
ATOM   12894 H  HG22 . THR   B 1 225 ? 3.798  7.067   47.001 1.00 34.11 ? 225  THR   B HG22 1 
ATOM   12895 H  HG23 . THR   B 1 225 ? 4.137  7.667   45.576 1.00 34.11 ? 225  THR   B HG23 1 
ATOM   12896 N  N    . THR   B 1 226 ? 5.693  7.839   49.465 1.00 24.31 ? 226  THR   B N    1 
ATOM   12897 C  CA   . THR   B 1 226 ? 4.970  8.291   50.685 1.00 25.27 ? 226  THR   B CA   1 
ATOM   12898 C  C    . THR   B 1 226 ? 5.387  9.723   51.042 1.00 23.46 ? 226  THR   B C    1 
ATOM   12899 O  O    . THR   B 1 226 ? 4.501  10.540  51.335 1.00 23.32 ? 226  THR   B O    1 
ATOM   12900 C  CB   . THR   B 1 226 ? 5.219  7.338   51.860 1.00 25.80 ? 226  THR   B CB   1 
ATOM   12901 O  OG1  . THR   B 1 226 ? 4.904  6.014   51.427 1.00 26.68 ? 226  THR   B OG1  1 
ATOM   12902 C  CG2  . THR   B 1 226 ? 4.406  7.689   53.085 1.00 24.90 ? 226  THR   B CG2  1 
ATOM   12903 H  H    . THR   B 1 226 ? 6.181  7.140   49.576 1.00 29.18 ? 226  THR   B H    1 
ATOM   12904 H  HA   . THR   B 1 226 ? 4.018  8.282   50.499 1.00 30.33 ? 226  THR   B HA   1 
ATOM   12905 H  HB   . THR   B 1 226 ? 6.150  7.412   52.122 1.00 30.96 ? 226  THR   B HB   1 
ATOM   12906 H  HG1  . THR   B 1 226 ? 5.527  5.721   50.946 1.00 32.02 ? 226  THR   B HG1  1 
ATOM   12907 H  HG21 . THR   B 1 226 ? 4.601  7.057   53.795 1.00 29.88 ? 226  THR   B HG21 1 
ATOM   12908 H  HG22 . THR   B 1 226 ? 4.633  8.585   53.379 1.00 29.88 ? 226  THR   B HG22 1 
ATOM   12909 H  HG23 . THR   B 1 226 ? 3.461  7.650   52.869 1.00 29.88 ? 226  THR   B HG23 1 
ATOM   12910 N  N    . LEU   B 1 227 ? 6.687  10.011  50.998 1.00 22.28 ? 227  LEU   B N    1 
ATOM   12911 C  CA   . LEU   B 1 227 ? 7.186  11.360  51.380 1.00 20.48 ? 227  LEU   B CA   1 
ATOM   12912 C  C    . LEU   B 1 227 ? 6.671  12.403  50.382 1.00 19.38 ? 227  LEU   B C    1 
ATOM   12913 O  O    . LEU   B 1 227 ? 6.198  13.458  50.823 1.00 19.44 ? 227  LEU   B O    1 
ATOM   12914 C  CB   . LEU   B 1 227 ? 8.718  11.327  51.420 1.00 20.96 ? 227  LEU   B CB   1 
ATOM   12915 C  CG   . LEU   B 1 227 ? 9.320  10.480  52.540 1.00 17.84 ? 227  LEU   B CG   1 
ATOM   12916 C  CD1  . LEU   B 1 227 ? 10.829 10.370  52.389 1.00 23.00 ? 227  LEU   B CD1  1 
ATOM   12917 C  CD2  . LEU   B 1 227 ? 8.961  11.051  53.904 1.00 18.14 ? 227  LEU   B CD2  1 
ATOM   12918 H  H    . LEU   B 1 227 ? 7.298  9.457   50.755 1.00 26.74 ? 227  LEU   B H    1 
ATOM   12919 H  HA   . LEU   B 1 227 ? 6.859  11.607  52.259 1.00 24.58 ? 227  LEU   B HA   1 
ATOM   12920 H  HB2  . LEU   B 1 227 ? 9.043  10.991  50.570 1.00 25.15 ? 227  LEU   B HB2  1 
ATOM   12921 H  HB3  . LEU   B 1 227 ? 9.045  12.236  51.510 1.00 25.15 ? 227  LEU   B HB3  1 
ATOM   12922 H  HG   . LEU   B 1 227 ? 8.943  9.589   52.473 1.00 21.42 ? 227  LEU   B HG   1 
ATOM   12923 H  HD11 . LEU   B 1 227 ? 11.188 9.829   53.110 1.00 27.60 ? 227  LEU   B HD11 1 
ATOM   12924 H  HD12 . LEU   B 1 227 ? 11.040 9.955   51.538 1.00 27.60 ? 227  LEU   B HD12 1 
ATOM   12925 H  HD13 . LEU   B 1 227 ? 11.223 11.256  52.423 1.00 27.60 ? 227  LEU   B HD13 1 
ATOM   12926 H  HD21 . LEU   B 1 227 ? 9.352  10.499  54.599 1.00 21.78 ? 227  LEU   B HD21 1 
ATOM   12927 H  HD22 . LEU   B 1 227 ? 9.305  11.955  53.977 1.00 21.78 ? 227  LEU   B HD22 1 
ATOM   12928 H  HD23 . LEU   B 1 227 ? 7.996  11.063  54.006 1.00 21.78 ? 227  LEU   B HD23 1 
ATOM   12929 N  N    . LYS   B 1 228 ? 6.743  12.095  49.087 1.00 20.13 ? 228  LYS   B N    1 
ATOM   12930 C  CA   . LYS   B 1 228 ? 6.347  13.082  48.050 1.00 23.17 ? 228  LYS   B CA   1 
ATOM   12931 C  C    . LYS   B 1 228 ? 4.844  13.369  48.141 1.00 20.02 ? 228  LYS   B C    1 
ATOM   12932 O  O    . LYS   B 1 228 ? 4.435  14.472  47.757 1.00 19.63 ? 228  LYS   B O    1 
ATOM   12933 C  CB   . LYS   B 1 228 ? 6.744  12.563  46.665 1.00 24.74 ? 228  LYS   B CB   1 
ATOM   12934 C  CG   . LYS   B 1 228 ? 8.240  12.361  46.464 1.00 29.86 ? 228  LYS   B CG   1 
ATOM   12935 C  CD   . LYS   B 1 228 ? 8.700  12.515  45.032 1.00 32.35 ? 228  LYS   B CD   1 
ATOM   12936 C  CE   . LYS   B 1 228 ? 10.191 12.759  44.920 1.00 34.85 ? 228  LYS   B CE   1 
ATOM   12937 N  NZ   . LYS   B 1 228 ? 10.705 12.482  43.558 1.00 41.77 ? 228  LYS   B NZ   1 
ATOM   12938 H  H    . LYS   B 1 228 ? 7.012  11.337  48.781 1.00 24.16 ? 228  LYS   B H    1 
ATOM   12939 H  HA   . LYS   B 1 228 ? 6.813  13.919  48.201 1.00 27.81 ? 228  LYS   B HA   1 
ATOM   12940 H  HB2  . LYS   B 1 228 ? 6.292  11.719  46.508 1.00 29.69 ? 228  LYS   B HB2  1 
ATOM   12941 H  HB3  . LYS   B 1 228 ? 6.422  13.186  45.995 1.00 29.69 ? 228  LYS   B HB3  1 
ATOM   12942 H  HG2  . LYS   B 1 228 ? 8.719  12.998  47.017 1.00 35.83 ? 228  LYS   B HG2  1 
ATOM   12943 H  HG3  . LYS   B 1 228 ? 8.481  11.475  46.777 1.00 35.83 ? 228  LYS   B HG3  1 
ATOM   12944 H  HD2  . LYS   B 1 228 ? 8.469  11.715  44.534 1.00 38.83 ? 228  LYS   B HD2  1 
ATOM   12945 H  HD3  . LYS   B 1 228 ? 8.223  13.253  44.621 1.00 38.83 ? 228  LYS   B HD3  1 
ATOM   12946 H  HE2  . LYS   B 1 228 ? 10.385 13.680  45.155 1.00 41.83 ? 228  LYS   B HE2  1 
ATOM   12947 H  HE3  . LYS   B 1 228 ? 10.657 12.199  45.560 1.00 41.83 ? 228  LYS   B HE3  1 
ATOM   12948 H  HZ1  . LYS   B 1 228 ? 11.581 12.637  43.534 1.00 50.13 ? 228  LYS   B HZ1  1 
ATOM   12949 H  HZ2  . LYS   B 1 228 ? 10.549 11.631  43.349 1.00 50.13 ? 228  LYS   B HZ2  1 
ATOM   12950 H  HZ3  . LYS   B 1 228 ? 10.294 13.011  42.972 1.00 50.13 ? 228  LYS   B HZ3  1 
ATOM   12951 N  N    . ASN   B 1 229 ? 4.069  12.401  48.631 1.00 22.22 ? 229  ASN   B N    1 
ATOM   12952 C  CA   . ASN   B 1 229 ? 2.600  12.586  48.760 1.00 23.08 ? 229  ASN   B CA   1 
ATOM   12953 C  C    . ASN   B 1 229 ? 2.246  13.194  50.125 1.00 19.97 ? 229  ASN   B C    1 
ATOM   12954 O  O    . ASN   B 1 229 ? 1.071  13.532  50.322 1.00 22.86 ? 229  ASN   B O    1 
ATOM   12955 C  CB   . ASN   B 1 229 ? 1.844  11.274  48.542 1.00 26.25 ? 229  ASN   B CB   1 
ATOM   12956 C  CG   . ASN   B 1 229 ? 2.000  10.736  47.136 1.00 30.87 ? 229  ASN   B CG   1 
ATOM   12957 O  OD1  . ASN   B 1 229 ? 2.258  11.491  46.203 1.00 30.46 ? 229  ASN   B OD1  1 
ATOM   12958 N  ND2  . ASN   B 1 229 ? 1.845  9.432   46.976 1.00 34.07 ? 229  ASN   B ND2  1 
ATOM   12959 H  H    . ASN   B 1 229 ? 4.359  11.635  48.894 1.00 26.67 ? 229  ASN   B H    1 
ATOM   12960 H  HA   . ASN   B 1 229 ? 2.322  13.203  48.065 1.00 27.70 ? 229  ASN   B HA   1 
ATOM   12961 H  HB2  . ASN   B 1 229 ? 2.164  10.612  49.175 1.00 31.50 ? 229  ASN   B HB2  1 
ATOM   12962 H  HB3  . ASN   B 1 229 ? 0.902  11.413  48.728 1.00 31.50 ? 229  ASN   B HB3  1 
ATOM   12963 H  HD21 . ASN   B 1 229 ? 1.925  9.082   46.194 1.00 40.89 ? 229  ASN   B HD21 1 
ATOM   12964 H  HD22 . ASN   B 1 229 ? 1.665  8.934   47.654 1.00 40.89 ? 229  ASN   B HD22 1 
ATOM   12965 N  N    . ASP   B 1 230 ? 3.220  13.325  51.028 1.00 20.29 ? 230  ASP   B N    1 
ATOM   12966 C  CA   . ASP   B 1 230 ? 2.938  13.977  52.334 1.00 20.85 ? 230  ASP   B CA   1 
ATOM   12967 C  C    . ASP   B 1 230 ? 2.888  15.495  52.141 1.00 19.97 ? 230  ASP   B C    1 
ATOM   12968 O  O    . ASP   B 1 230 ? 3.725  16.026  51.415 1.00 20.46 ? 230  ASP   B O    1 
ATOM   12969 C  CB   . ASP   B 1 230 ? 3.951  13.578  53.407 1.00 17.89 ? 230  ASP   B CB   1 
ATOM   12970 C  CG   . ASP   B 1 230 ? 3.660  14.210  54.756 1.00 22.16 ? 230  ASP   B CG   1 
ATOM   12971 O  OD1  . ASP   B 1 230 ? 2.792  13.678  55.470 1.00 24.61 ? 230  ASP   B OD1  1 
ATOM   12972 O  OD2  . ASP   B 1 230 ? 4.292  15.233  55.073 1.00 21.46 ? 230  ASP   B OD2  1 
ATOM   12973 H  H    . ASP   B 1 230 ? 4.030  13.056  50.920 1.00 24.35 ? 230  ASP   B H    1 
ATOM   12974 H  HA   . ASP   B 1 230 ? 2.075  13.670  52.653 1.00 25.03 ? 230  ASP   B HA   1 
ATOM   12975 H  HB2  . ASP   B 1 230 ? 3.953  12.613  53.501 1.00 21.47 ? 230  ASP   B HB2  1 
ATOM   12976 H  HB3  . ASP   B 1 230 ? 4.840  13.837  53.118 1.00 21.47 ? 230  ASP   B HB3  1 
ATOM   12977 N  N    . PRO   B 1 231 ? 1.925  16.201  52.765 1.00 23.49 ? 231  PRO   B N    1 
ATOM   12978 C  CA   . PRO   B 1 231 ? 1.817  17.658  52.635 1.00 24.18 ? 231  PRO   B CA   1 
ATOM   12979 C  C    . PRO   B 1 231 ? 3.042  18.418  53.166 1.00 23.26 ? 231  PRO   B C    1 
ATOM   12980 O  O    . PRO   B 1 231 ? 3.370  19.439  52.612 1.00 22.39 ? 231  PRO   B O    1 
ATOM   12981 C  CB   . PRO   B 1 231 ? 0.612  18.009  53.513 1.00 26.06 ? 231  PRO   B CB   1 
ATOM   12982 C  CG   . PRO   B 1 231 ? -0.187 16.729  53.574 1.00 29.52 ? 231  PRO   B CG   1 
ATOM   12983 C  CD   . PRO   B 1 231 ? 0.855  15.632  53.583 1.00 26.35 ? 231  PRO   B CD   1 
ATOM   12984 H  HA   . PRO   B 1 231 ? 1.739  17.908  51.701 1.00 29.02 ? 231  PRO   B HA   1 
ATOM   12985 H  HB2  . PRO   B 1 231 ? 0.889  18.296  54.397 1.00 31.27 ? 231  PRO   B HB2  1 
ATOM   12986 H  HB3  . PRO   B 1 231 ? 0.093  18.733  53.129 1.00 31.27 ? 231  PRO   B HB3  1 
ATOM   12987 H  HG2  . PRO   B 1 231 ? -0.741 16.696  54.369 1.00 35.42 ? 231  PRO   B HG2  1 
ATOM   12988 H  HG3  . PRO   B 1 231 ? -0.780 16.646  52.811 1.00 35.42 ? 231  PRO   B HG3  1 
ATOM   12989 H  HD2  . PRO   B 1 231 ? 1.157  15.429  54.482 1.00 31.62 ? 231  PRO   B HD2  1 
ATOM   12990 H  HD3  . PRO   B 1 231 ? 0.513  14.806  53.206 1.00 31.62 ? 231  PRO   B HD3  1 
ATOM   12991 N  N    . VAL   B 1 232 ? 3.663  17.905  54.232 1.00 19.51 ? 232  VAL   B N    1 
ATOM   12992 C  CA   . VAL   B 1 232 ? 4.859  18.583  54.811 1.00 19.22 ? 232  VAL   B CA   1 
ATOM   12993 C  C    . VAL   B 1 232 ? 6.108  18.152  54.030 1.00 20.07 ? 232  VAL   B C    1 
ATOM   12994 O  O    . VAL   B 1 232 ? 6.820  19.033  53.526 1.00 18.09 ? 232  VAL   B O    1 
ATOM   12995 C  CB   . VAL   B 1 232 ? 5.000  18.294  56.318 1.00 20.53 ? 232  VAL   B CB   1 
ATOM   12996 C  CG1  . VAL   B 1 232 ? 6.274  18.892  56.893 1.00 17.10 ? 232  VAL   B CG1  1 
ATOM   12997 C  CG2  . VAL   B 1 232 ? 3.783  18.762  57.099 1.00 22.29 ? 232  VAL   B CG2  1 
ATOM   12998 H  H    . VAL   B 1 232 ? 3.424  17.184  54.635 1.00 23.41 ? 232  VAL   B H    1 
ATOM   12999 H  HA   . VAL   B 1 232 ? 4.751  19.543  54.727 1.00 23.06 ? 232  VAL   B HA   1 
ATOM   13000 H  HB   . VAL   B 1 232 ? 5.059  17.330  56.411 1.00 24.64 ? 232  VAL   B HB   1 
ATOM   13001 H  HG11 . VAL   B 1 232 ? 6.328  18.690  57.840 1.00 20.52 ? 232  VAL   B HG11 1 
ATOM   13002 H  HG12 . VAL   B 1 232 ? 7.043  18.514  56.438 1.00 20.52 ? 232  VAL   B HG12 1 
ATOM   13003 H  HG13 . VAL   B 1 232 ? 6.265  19.854  56.768 1.00 20.52 ? 232  VAL   B HG13 1 
ATOM   13004 H  HG21 . VAL   B 1 232 ? 3.907  18.564  58.041 1.00 26.75 ? 232  VAL   B HG21 1 
ATOM   13005 H  HG22 . VAL   B 1 232 ? 3.671  19.718  56.982 1.00 26.75 ? 232  VAL   B HG22 1 
ATOM   13006 H  HG23 . VAL   B 1 232 ? 2.993  18.302  56.774 1.00 26.75 ? 232  VAL   B HG23 1 
ATOM   13007 N  N    . ALA   B 1 233 ? 6.361  16.842  53.955 1.00 17.98 ? 233  ALA   B N    1 
ATOM   13008 C  CA   . ALA   B 1 233 ? 7.584  16.347  53.284 1.00 18.26 ? 233  ALA   B CA   1 
ATOM   13009 C  C    . ALA   B 1 233 ? 7.504  16.603  51.776 1.00 20.40 ? 233  ALA   B C    1 
ATOM   13010 O  O    . ALA   B 1 233 ? 8.562  16.783  51.165 1.00 21.78 ? 233  ALA   B O    1 
ATOM   13011 C  CB   . ALA   B 1 233 ? 7.770  14.877  53.574 1.00 20.51 ? 233  ALA   B CB   1 
ATOM   13012 H  H    . ALA   B 1 233 ? 5.852  16.229  54.278 1.00 21.58 ? 233  ALA   B H    1 
ATOM   13013 H  HA   . ALA   B 1 233 ? 8.353  16.827  53.629 1.00 21.92 ? 233  ALA   B HA   1 
ATOM   13014 H  HB1  . ALA   B 1 233 ? 8.573  14.559  53.132 1.00 24.61 ? 233  ALA   B HB1  1 
ATOM   13015 H  HB2  . ALA   B 1 233 ? 7.854  14.744  54.531 1.00 24.61 ? 233  ALA   B HB2  1 
ATOM   13016 H  HB3  . ALA   B 1 233 ? 7.003  14.383  53.246 1.00 24.61 ? 233  ALA   B HB3  1 
ATOM   13017 N  N    . GLY   B 1 234 ? 6.295  16.625  51.211 1.00 15.96 ? 234  GLY   B N    1 
ATOM   13018 C  CA   . GLY   B 1 234 ? 6.168  16.747  49.746 1.00 21.18 ? 234  GLY   B CA   1 
ATOM   13019 C  C    . GLY   B 1 234 ? 5.904  18.154  49.239 1.00 21.74 ? 234  GLY   B C    1 
ATOM   13020 O  O    . GLY   B 1 234 ? 6.028  18.355  48.024 1.00 19.40 ? 234  GLY   B O    1 
ATOM   13021 H  H    . GLY   B 1 234 ? 5.552  16.572  51.640 1.00 19.16 ? 234  GLY   B H    1 
ATOM   13022 H  HA2  . GLY   B 1 234 ? 6.983  16.418  49.336 1.00 25.42 ? 234  GLY   B HA2  1 
ATOM   13023 H  HA3  . GLY   B 1 234 ? 5.447  16.170  49.448 1.00 25.42 ? 234  GLY   B HA3  1 
ATOM   13024 N  N    . GLN   B 1 235 ? 5.556  19.098  50.116 1.00 22.57 ? 235  GLN   B N    1 
ATOM   13025 C  CA   . GLN   B 1 235 ? 5.185  20.448  49.618 1.00 22.95 ? 235  GLN   B CA   1 
ATOM   13026 C  C    . GLN   B 1 235 ? 5.708  21.563  50.526 1.00 18.31 ? 235  GLN   B C    1 
ATOM   13027 O  O    . GLN   B 1 235 ? 6.421  22.436  50.024 1.00 19.89 ? 235  GLN   B O    1 
ATOM   13028 C  CB   . GLN   B 1 235 ? 3.662  20.566  49.537 1.00 23.90 ? 235  GLN   B CB   1 
ATOM   13029 C  CG   . GLN   B 1 235 ? 3.015  19.564  48.595 1.00 28.31 ? 235  GLN   B CG   1 
ATOM   13030 C  CD   . GLN   B 1 235 ? 3.411  19.796  47.158 1.00 31.11 ? 235  GLN   B CD   1 
ATOM   13031 O  OE1  . GLN   B 1 235 ? 3.856  20.878  46.782 1.00 33.14 ? 235  GLN   B OE1  1 
ATOM   13032 N  NE2  . GLN   B 1 235 ? 3.248  18.771  46.339 1.00 32.68 ? 235  GLN   B NE2  1 
ATOM   13033 H  H    . GLN   B 1 235 ? 5.525  18.995  50.969 1.00 27.09 ? 235  GLN   B H    1 
ATOM   13034 H  HA   . GLN   B 1 235 ? 5.589  20.551  48.742 1.00 27.54 ? 235  GLN   B HA   1 
ATOM   13035 H  HB2  . GLN   B 1 235 ? 3.290  20.448  50.425 1.00 28.68 ? 235  GLN   B HB2  1 
ATOM   13036 H  HB3  . GLN   B 1 235 ? 3.431  21.463  49.249 1.00 28.68 ? 235  GLN   B HB3  1 
ATOM   13037 H  HG2  . GLN   B 1 235 ? 3.268  18.665  48.858 1.00 33.97 ? 235  GLN   B HG2  1 
ATOM   13038 H  HG3  . GLN   B 1 235 ? 2.050  19.622  48.676 1.00 33.97 ? 235  GLN   B HG3  1 
ATOM   13039 H  HE21 . GLN   B 1 235 ? 2.934  18.028  46.637 1.00 39.21 ? 235  GLN   B HE21 1 
ATOM   13040 H  HE22 . GLN   B 1 235 ? 3.456  18.847  45.508 1.00 39.21 ? 235  GLN   B HE22 1 
ATOM   13041 N  N    . GLY   B 1 236 ? 5.356  21.532  51.810 1.00 20.36 ? 236  GLY   B N    1 
ATOM   13042 C  CA   . GLY   B 1 236 ? 5.714  22.655  52.697 1.00 19.76 ? 236  GLY   B CA   1 
ATOM   13043 C  C    . GLY   B 1 236 ? 7.200  22.834  52.937 1.00 18.37 ? 236  GLY   B C    1 
ATOM   13044 O  O    . GLY   B 1 236 ? 7.685  23.960  52.828 1.00 14.52 ? 236  GLY   B O    1 
ATOM   13045 H  H    . GLY   B 1 236 ? 4.922  20.892  52.185 1.00 24.43 ? 236  GLY   B H    1 
ATOM   13046 H  HA2  . GLY   B 1 236 ? 5.360  23.475  52.317 1.00 23.72 ? 236  GLY   B HA2  1 
ATOM   13047 H  HA3  . GLY   B 1 236 ? 5.275  22.526  53.552 1.00 23.72 ? 236  GLY   B HA3  1 
ATOM   13048 N  N    A MET   B 1 237 ? 7.922  21.730  53.151 0.54 19.11 ? 237  MET   B N    1 
ATOM   13049 N  N    B MET   B 1 237 ? 7.921  21.730  53.150 0.46 19.11 ? 237  MET   B N    1 
ATOM   13050 C  CA   A MET   B 1 237 ? 9.374  21.823  53.465 0.54 19.02 ? 237  MET   B CA   1 
ATOM   13051 C  CA   B MET   B 1 237 ? 9.373  21.818  53.462 0.46 19.02 ? 237  MET   B CA   1 
ATOM   13052 C  C    A MET   B 1 237 ? 10.193 22.118  52.201 0.54 17.00 ? 237  MET   B C    1 
ATOM   13053 C  C    B MET   B 1 237 ? 10.191 22.119  52.200 0.46 17.00 ? 237  MET   B C    1 
ATOM   13054 O  O    A MET   B 1 237 ? 11.002 23.053  52.240 0.54 15.92 ? 237  MET   B O    1 
ATOM   13055 O  O    B MET   B 1 237 ? 10.996 23.060  52.240 0.46 15.93 ? 237  MET   B O    1 
ATOM   13056 C  CB   A MET   B 1 237 ? 9.877  20.530  54.116 0.54 19.96 ? 237  MET   B CB   1 
ATOM   13057 C  CB   B MET   B 1 237 ? 9.868  20.510  54.087 0.46 19.95 ? 237  MET   B CB   1 
ATOM   13058 C  CG   A MET   B 1 237 ? 9.369  20.333  55.529 0.54 20.51 ? 237  MET   B CG   1 
ATOM   13059 C  CG   B MET   B 1 237 ? 9.321  20.273  55.473 0.46 20.65 ? 237  MET   B CG   1 
ATOM   13060 S  SD   A MET   B 1 237 ? 10.482 19.298  56.510 0.54 19.79 ? 237  MET   B SD   1 
ATOM   13061 S  SD   B MET   B 1 237 ? 10.144 21.338  56.672 0.46 23.57 ? 237  MET   B SD   1 
ATOM   13062 C  CE   A MET   B 1 237 ? 11.495 20.557  57.283 0.54 22.68 ? 237  MET   B CE   1 
ATOM   13063 C  CE   B MET   B 1 237 ? 11.456 20.248  57.220 0.46 22.43 ? 237  MET   B CE   1 
ATOM   13064 H  H    A MET   B 1 237 ? 7.608  20.930  53.122 0.54 22.94 ? 237  MET   B H    1 
ATOM   13065 H  H    B MET   B 1 237 ? 7.605  20.930  53.122 0.46 22.93 ? 237  MET   B H    1 
ATOM   13066 H  HA   A MET   B 1 237 ? 9.491  22.555  54.090 0.54 22.83 ? 237  MET   B HA   1 
ATOM   13067 H  HA   B MET   B 1 237 ? 9.494  22.544  54.094 0.46 22.83 ? 237  MET   B HA   1 
ATOM   13068 H  HB2  A MET   B 1 237 ? 9.604  19.774  53.573 0.54 23.95 ? 237  MET   B HB2  1 
ATOM   13069 H  HB2  B MET   B 1 237 ? 9.616  19.769  53.515 0.46 23.94 ? 237  MET   B HB2  1 
ATOM   13070 H  HB3  A MET   B 1 237 ? 10.847 20.536  54.126 0.54 23.95 ? 237  MET   B HB3  1 
ATOM   13071 H  HB3  B MET   B 1 237 ? 10.837 20.522  54.125 0.46 23.94 ? 237  MET   B HB3  1 
ATOM   13072 H  HG2  A MET   B 1 237 ? 9.268  21.197  55.959 0.54 24.62 ? 237  MET   B HG2  1 
ATOM   13073 H  HG2  B MET   B 1 237 ? 8.366  20.444  55.483 0.46 24.78 ? 237  MET   B HG2  1 
ATOM   13074 H  HG3  A MET   B 1 237 ? 8.489  19.925  55.502 0.54 24.62 ? 237  MET   B HG3  1 
ATOM   13075 H  HG3  B MET   B 1 237 ? 9.445  19.343  55.720 0.46 24.78 ? 237  MET   B HG3  1 
ATOM   13076 H  HE1  A MET   B 1 237 ? 12.155 20.135  57.855 0.54 27.22 ? 237  MET   B HE1  1 
ATOM   13077 H  HE1  B MET   B 1 237 ? 11.996 20.701  57.886 0.46 26.92 ? 237  MET   B HE1  1 
ATOM   13078 H  HE2  A MET   B 1 237 ? 11.945 21.076  56.598 0.54 27.22 ? 237  MET   B HE2  1 
ATOM   13079 H  HE2  B MET   B 1 237 ? 11.071 19.446  57.607 0.46 26.92 ? 237  MET   B HE2  1 
ATOM   13080 H  HE3  A MET   B 1 237 ? 10.934 21.142  57.815 0.54 27.22 ? 237  MET   B HE3  1 
ATOM   13081 H  HE3  B MET   B 1 237 ? 12.013 20.006  56.464 0.46 26.92 ? 237  MET   B HE3  1 
ATOM   13082 N  N    . PRO   B 1 238 ? 9.842  21.542  51.030 1.00 17.33 ? 238  PRO   B N    1 
ATOM   13083 C  CA   . PRO   B 1 238 ? 10.568 21.879  49.809 1.00 17.56 ? 238  PRO   B CA   1 
ATOM   13084 C  C    . PRO   B 1 238 ? 10.323 23.355  49.456 1.00 16.95 ? 238  PRO   B C    1 
ATOM   13085 O  O    . PRO   B 1 238 ? 11.254 24.042  49.107 1.00 16.22 ? 238  PRO   B O    1 
ATOM   13086 C  CB   . PRO   B 1 238 ? 10.002 20.935  48.736 1.00 18.03 ? 238  PRO   B CB   1 
ATOM   13087 C  CG   . PRO   B 1 238 ? 8.940  20.123  49.440 1.00 20.17 ? 238  PRO   B CG   1 
ATOM   13088 C  CD   . PRO   B 1 238 ? 9.331  20.176  50.897 1.00 18.34 ? 238  PRO   B CD   1 
ATOM   13089 H  HA   . PRO   B 1 238 ? 11.528 21.771  49.895 1.00 21.08 ? 238  PRO   B HA   1 
ATOM   13090 H  HB2  . PRO   B 1 238 ? 9.627  21.434  47.994 1.00 21.64 ? 238  PRO   B HB2  1 
ATOM   13091 H  HB3  . PRO   B 1 238 ? 10.696 20.363  48.372 1.00 21.64 ? 238  PRO   B HB3  1 
ATOM   13092 H  HG2  . PRO   B 1 238 ? 8.056  20.497  49.297 1.00 24.21 ? 238  PRO   B HG2  1 
ATOM   13093 H  HG3  . PRO   B 1 238 ? 8.918  19.210  49.113 1.00 24.21 ? 238  PRO   B HG3  1 
ATOM   13094 H  HD2  . PRO   B 1 238 ? 8.574  20.014  51.481 1.00 22.01 ? 238  PRO   B HD2  1 
ATOM   13095 H  HD3  . PRO   B 1 238 ? 10.005 19.514  51.116 1.00 22.01 ? 238  PRO   B HD3  1 
ATOM   13096 N  N    . THR   B 1 239 ? 9.079  23.807  49.597 1.00 16.28 ? 239  THR   B N    1 
ATOM   13097 C  CA   . THR   B 1 239 ? 8.732  25.193  49.190 1.00 18.92 ? 239  THR   B CA   1 
ATOM   13098 C  C    . THR   B 1 239 ? 9.170  26.236  50.224 1.00 15.95 ? 239  THR   B C    1 
ATOM   13099 O  O    . THR   B 1 239 ? 9.746  27.247  49.807 1.00 17.50 ? 239  THR   B O    1 
ATOM   13100 C  CB   . THR   B 1 239 ? 7.222  25.304  48.933 1.00 19.04 ? 239  THR   B CB   1 
ATOM   13101 O  OG1  . THR   B 1 239 ? 6.842  24.277  48.018 1.00 20.39 ? 239  THR   B OG1  1 
ATOM   13102 C  CG2  . THR   B 1 239 ? 6.810  26.660  48.403 1.00 21.06 ? 239  THR   B CG2  1 
ATOM   13103 H  H    . THR   B 1 239 ? 8.426  23.348  49.918 1.00 19.54 ? 239  THR   B H    1 
ATOM   13104 H  HA   . THR   B 1 239 ? 9.218  25.382  48.372 1.00 22.71 ? 239  THR   B HA   1 
ATOM   13105 H  HB   . THR   B 1 239 ? 6.764  25.197  49.781 1.00 22.85 ? 239  THR   B HB   1 
ATOM   13106 H  HG1  . THR   B 1 239 ? 6.699  23.565  48.440 1.00 24.48 ? 239  THR   B HG1  1 
ATOM   13107 H  HG21 . THR   B 1 239 ? 5.851  26.674  48.259 1.00 25.27 ? 239  THR   B HG21 1 
ATOM   13108 H  HG22 . THR   B 1 239 ? 7.050  27.346  49.046 1.00 25.27 ? 239  THR   B HG22 1 
ATOM   13109 H  HG23 . THR   B 1 239 ? 7.265  26.831  47.563 1.00 25.27 ? 239  THR   B HG23 1 
ATOM   13110 N  N    . TYR   B 1 240 ? 8.942  25.991  51.518 1.00 16.54 ? 240  TYR   B N    1 
ATOM   13111 C  CA   . TYR   B 1 240 ? 9.190  27.044  52.542 1.00 14.70 ? 240  TYR   B CA   1 
ATOM   13112 C  C    . TYR   B 1 240 ? 10.349 26.709  53.488 1.00 17.05 ? 240  TYR   B C    1 
ATOM   13113 O  O    . TYR   B 1 240 ? 10.799 27.611  54.207 1.00 18.73 ? 240  TYR   B O    1 
ATOM   13114 C  CB   . TYR   B 1 240 ? 7.897  27.255  53.331 1.00 15.61 ? 240  TYR   B CB   1 
ATOM   13115 C  CG   . TYR   B 1 240 ? 6.747  27.686  52.459 1.00 16.38 ? 240  TYR   B CG   1 
ATOM   13116 C  CD1  . TYR   B 1 240 ? 6.782  28.900  51.796 1.00 15.10 ? 240  TYR   B CD1  1 
ATOM   13117 C  CD2  . TYR   B 1 240 ? 5.647  26.869  52.263 1.00 17.60 ? 240  TYR   B CD2  1 
ATOM   13118 C  CE1  . TYR   B 1 240 ? 5.741  29.306  50.980 1.00 16.18 ? 240  TYR   B CE1  1 
ATOM   13119 C  CE2  . TYR   B 1 240 ? 4.598  27.259  51.449 1.00 19.81 ? 240  TYR   B CE2  1 
ATOM   13120 C  CZ   . TYR   B 1 240 ? 4.644  28.483  50.806 1.00 20.04 ? 240  TYR   B CZ   1 
ATOM   13121 O  OH   . TYR   B 1 240 ? 3.613  28.883  49.993 1.00 20.67 ? 240  TYR   B OH   1 
ATOM   13122 H  H    . TYR   B 1 240 ? 8.651  25.244  51.829 1.00 19.85 ? 240  TYR   B H    1 
ATOM   13123 H  HA   . TYR   B 1 240 ? 9.454  27.856  52.082 1.00 17.65 ? 240  TYR   B HA   1 
ATOM   13124 H  HB2  . TYR   B 1 240 ? 7.662  26.431  53.786 1.00 18.74 ? 240  TYR   B HB2  1 
ATOM   13125 H  HB3  . TYR   B 1 240 ? 8.047  27.925  54.017 1.00 18.74 ? 240  TYR   B HB3  1 
ATOM   13126 H  HD1  . TYR   B 1 240 ? 7.521  29.455  51.901 1.00 18.12 ? 240  TYR   B HD1  1 
ATOM   13127 H  HD2  . TYR   B 1 240 ? 5.612  26.042  52.687 1.00 21.13 ? 240  TYR   B HD2  1 
ATOM   13128 H  HE1  . TYR   B 1 240 ? 5.779  30.130  50.550 1.00 19.42 ? 240  TYR   B HE1  1 
ATOM   13129 H  HE2  . TYR   B 1 240 ? 3.864  26.700  51.335 1.00 23.78 ? 240  TYR   B HE2  1 
ATOM   13130 H  HH   . TYR   B 1 240 ? 3.912  29.379  49.385 1.00 24.81 ? 240  TYR   B HH   1 
ATOM   13131 N  N    . GLY   B 1 241 ? 10.803 25.458  53.485 1.00 14.12 ? 241  GLY   B N    1 
ATOM   13132 C  CA   . GLY   B 1 241 ? 11.881 25.042  54.403 1.00 14.23 ? 241  GLY   B CA   1 
ATOM   13133 C  C    . GLY   B 1 241 ? 11.398 24.878  55.835 1.00 12.98 ? 241  GLY   B C    1 
ATOM   13134 O  O    . GLY   B 1 241 ? 10.180 24.960  56.058 1.00 13.76 ? 241  GLY   B O    1 
ATOM   13135 H  H    . GLY   B 1 241 ? 10.509 24.836  52.969 1.00 16.95 ? 241  GLY   B H    1 
ATOM   13136 H  HA2  . GLY   B 1 241 ? 12.258 24.203  54.094 1.00 17.07 ? 241  GLY   B HA2  1 
ATOM   13137 H  HA3  . GLY   B 1 241 ? 12.594 25.700  54.379 1.00 17.07 ? 241  GLY   B HA3  1 
ATOM   13138 N  N    . THR   B 1 242 ? 12.324 24.653  56.770 1.00 12.41 ? 242  THR   B N    1 
ATOM   13139 C  CA   . THR   B 1 242 ? 11.962 24.551  58.207 1.00 12.92 ? 242  THR   B CA   1 
ATOM   13140 C  C    . THR   B 1 242 ? 11.275 25.853  58.626 1.00 14.62 ? 242  THR   B C    1 
ATOM   13141 O  O    . THR   B 1 242 ? 10.468 25.818  59.559 1.00 14.13 ? 242  THR   B O    1 
ATOM   13142 C  CB   . THR   B 1 242 ? 13.202 24.296  59.076 1.00 11.16 ? 242  THR   B CB   1 
ATOM   13143 O  OG1  . THR   B 1 242 ? 14.171 25.318  58.850 1.00 11.37 ? 242  THR   B OG1  1 
ATOM   13144 C  CG2  . THR   B 1 242 ? 13.819 22.939  58.813 1.00 13.98 ? 242  THR   B CG2  1 
ATOM   13145 H  H    . THR   B 1 242 ? 13.162 24.556  56.605 1.00 14.90 ? 242  THR   B H    1 
ATOM   13146 H  HA   . THR   B 1 242 ? 11.361 23.800  58.334 1.00 15.51 ? 242  THR   B HA   1 
ATOM   13147 H  HB   . THR   B 1 242 ? 12.914 24.310  60.002 1.00 13.40 ? 242  THR   B HB   1 
ATOM   13148 H  HG1  . THR   B 1 242 ? 14.917 24.967  58.691 1.00 13.64 ? 242  THR   B HG1  1 
ATOM   13149 H  HG21 . THR   B 1 242 ? 14.596 22.821  59.381 1.00 16.78 ? 242  THR   B HG21 1 
ATOM   13150 H  HG22 . THR   B 1 242 ? 13.169 22.245  59.006 1.00 16.78 ? 242  THR   B HG22 1 
ATOM   13151 H  HG23 . THR   B 1 242 ? 14.087 22.880  57.883 1.00 16.78 ? 242  THR   B HG23 1 
ATOM   13152 N  N    . ALA   B 1 243 ? 11.591 26.950  57.932 1.00 14.83 ? 243  ALA   B N    1 
ATOM   13153 C  CA   . ALA   B 1 243 ? 11.004 28.274  58.255 1.00 14.85 ? 243  ALA   B CA   1 
ATOM   13154 C  C    . ALA   B 1 243 ? 9.474  28.254  58.152 1.00 14.47 ? 243  ALA   B C    1 
ATOM   13155 O  O    . ALA   B 1 243 ? 8.849  29.208  58.633 1.00 17.56 ? 243  ALA   B O    1 
ATOM   13156 C  CB   . ALA   B 1 243 ? 11.590 29.302  57.328 1.00 11.30 ? 243  ALA   B CB   1 
ATOM   13157 H  H    . ALA   B 1 243 ? 12.141 26.957  57.271 1.00 17.80 ? 243  ALA   B H    1 
ATOM   13158 H  HA   . ALA   B 1 243 ? 11.220 28.500  59.173 1.00 17.82 ? 243  ALA   B HA   1 
ATOM   13159 H  HB1  . ALA   B 1 243 ? 11.213 30.173  57.530 1.00 13.57 ? 243  ALA   B HB1  1 
ATOM   13160 H  HB2  . ALA   B 1 243 ? 12.553 29.332  57.445 1.00 13.57 ? 243  ALA   B HB2  1 
ATOM   13161 H  HB3  . ALA   B 1 243 ? 11.383 29.066  56.410 1.00 13.57 ? 243  ALA   B HB3  1 
ATOM   13162 N  N    . ILE   B 1 244 ? 8.900  27.229  57.523 1.00 14.64 ? 244  ILE   B N    1 
ATOM   13163 C  CA   . ILE   B 1 244 ? 7.413  27.106  57.480 1.00 13.68 ? 244  ILE   B CA   1 
ATOM   13164 C  C    . ILE   B 1 244 ? 6.866  27.123  58.912 1.00 15.49 ? 244  ILE   B C    1 
ATOM   13165 O  O    . ILE   B 1 244 ? 5.681  27.443  59.073 1.00 14.56 ? 244  ILE   B O    1 
ATOM   13166 C  CB   . ILE   B 1 244 ? 7.000  25.818  56.741 1.00 13.30 ? 244  ILE   B CB   1 
ATOM   13167 C  CG1  . ILE   B 1 244 ? 5.532  25.854  56.311 1.00 17.67 ? 244  ILE   B CG1  1 
ATOM   13168 C  CG2  . ILE   B 1 244 ? 7.314  24.590  57.581 1.00 13.80 ? 244  ILE   B CG2  1 
ATOM   13169 C  CD1  . ILE   B 1 244 ? 5.112  24.672  55.476 1.00 16.71 ? 244  ILE   B CD1  1 
ATOM   13170 H  H    . ILE   B 1 244 ? 9.328  26.602  57.120 1.00 17.57 ? 244  ILE   B H    1 
ATOM   13171 H  HA   . ILE   B 1 244 ? 7.038  27.856  56.992 1.00 16.42 ? 244  ILE   B HA   1 
ATOM   13172 H  HB   . ILE   B 1 244 ? 7.525  25.762  55.928 1.00 15.97 ? 244  ILE   B HB   1 
ATOM   13173 H  HG12 . ILE   B 1 244 ? 4.973  25.895  57.103 1.00 21.21 ? 244  ILE   B HG12 1 
ATOM   13174 H  HG13 . ILE   B 1 244 ? 5.371  26.668  55.808 1.00 21.21 ? 244  ILE   B HG13 1 
ATOM   13175 H  HG21 . ILE   B 1 244 ? 7.047  23.791  57.099 1.00 16.57 ? 244  ILE   B HG21 1 
ATOM   13176 H  HG22 . ILE   B 1 244 ? 8.267  24.556  57.761 1.00 16.57 ? 244  ILE   B HG22 1 
ATOM   13177 H  HG23 . ILE   B 1 244 ? 6.829  24.639  58.420 1.00 16.57 ? 244  ILE   B HG23 1 
ATOM   13178 H  HD11 . ILE   B 1 244 ? 4.175  24.759  55.240 1.00 20.05 ? 244  ILE   B HD11 1 
ATOM   13179 H  HD12 . ILE   B 1 244 ? 5.647  24.640  54.668 1.00 20.05 ? 244  ILE   B HD12 1 
ATOM   13180 H  HD13 . ILE   B 1 244 ? 5.243  23.855  55.982 1.00 20.05 ? 244  ILE   B HD13 1 
ATOM   13181 N  N    . LEU   B 1 245 ? 7.707  26.827  59.907 1.00 15.51 ? 245  LEU   B N    1 
ATOM   13182 C  CA   . LEU   B 1 245 ? 7.235  26.705  61.315 1.00 12.61 ? 245  LEU   B CA   1 
ATOM   13183 C  C    . LEU   B 1 245 ? 6.971  28.067  61.968 1.00 15.22 ? 245  LEU   B C    1 
ATOM   13184 O  O    . LEU   B 1 245 ? 6.233  28.094  62.960 1.00 14.44 ? 245  LEU   B O    1 
ATOM   13185 C  CB   . LEU   B 1 245 ? 8.296  25.945  62.117 1.00 10.44 ? 245  LEU   B CB   1 
ATOM   13186 C  CG   . LEU   B 1 245 ? 8.412  24.455  61.808 1.00 13.96 ? 245  LEU   B CG   1 
ATOM   13187 C  CD1  . LEU   B 1 245 ? 9.739  23.908  62.309 1.00 14.78 ? 245  LEU   B CD1  1 
ATOM   13188 C  CD2  . LEU   B 1 245 ? 7.254  23.687  62.423 1.00 16.19 ? 245  LEU   B CD2  1 
ATOM   13189 H  H    . LEU   B 1 245 ? 8.550  26.692  59.801 1.00 18.62 ? 245  LEU   B H    1 
ATOM   13190 H  HA   . LEU   B 1 245 ? 6.391  26.227  61.311 1.00 15.14 ? 245  LEU   B HA   1 
ATOM   13191 H  HB2  . LEU   B 1 245 ? 9.158  26.360  61.958 1.00 12.53 ? 245  LEU   B HB2  1 
ATOM   13192 H  HB3  . LEU   B 1 245 ? 8.101  26.049  63.061 1.00 12.53 ? 245  LEU   B HB3  1 
ATOM   13193 H  HG   . LEU   B 1 245 ? 8.376  24.341  60.845 1.00 16.75 ? 245  LEU   B HG   1 
ATOM   13194 H  HD11 . LEU   B 1 245 ? 9.797  22.961  62.105 1.00 17.74 ? 245  LEU   B HD11 1 
ATOM   13195 H  HD12 . LEU   B 1 245 ? 10.468 24.377  61.873 1.00 17.74 ? 245  LEU   B HD12 1 
ATOM   13196 H  HD13 . LEU   B 1 245 ? 9.800  24.036  63.269 1.00 17.74 ? 245  LEU   B HD13 1 
ATOM   13197 H  HD21 . LEU   B 1 245 ? 7.345  22.744  62.216 1.00 19.43 ? 245  LEU   B HD21 1 
ATOM   13198 H  HD22 . LEU   B 1 245 ? 7.260  23.809  63.385 1.00 19.43 ? 245  LEU   B HD22 1 
ATOM   13199 H  HD23 . LEU   B 1 245 ? 6.417  24.018  62.061 1.00 19.43 ? 245  LEU   B HD23 1 
ATOM   13200 N  N    . VAL   B 1 246 ? 7.554  29.144  61.446 1.00 12.69 ? 246  VAL   B N    1 
ATOM   13201 C  CA   . VAL   B 1 246 ? 7.412  30.464  62.132 1.00 14.71 ? 246  VAL   B CA   1 
ATOM   13202 C  C    . VAL   B 1 246 ? 5.932  30.756  62.416 1.00 17.07 ? 246  VAL   B C    1 
ATOM   13203 O  O    . VAL   B 1 246 ? 5.592  30.963  63.591 1.00 14.05 ? 246  VAL   B O    1 
ATOM   13204 C  CB   . VAL   B 1 246 ? 8.056  31.594  61.306 1.00 14.82 ? 246  VAL   B CB   1 
ATOM   13205 C  CG1  . VAL   B 1 246 ? 7.745  32.964  61.888 1.00 15.60 ? 246  VAL   B CG1  1 
ATOM   13206 C  CG2  . VAL   B 1 246 ? 9.557  31.402  61.161 1.00 16.98 ? 246  VAL   B CG2  1 
ATOM   13207 H  H    . VAL   B 1 246 ? 8.022  29.151  60.724 1.00 15.24 ? 246  VAL   B H    1 
ATOM   13208 H  HA   . VAL   B 1 246 ? 7.883  30.422  62.979 1.00 17.66 ? 246  VAL   B HA   1 
ATOM   13209 H  HB   . VAL   B 1 246 ? 7.663  31.550  60.420 1.00 17.79 ? 246  VAL   B HB   1 
ATOM   13210 H  HG11 . VAL   B 1 246 ? 8.165  33.649  61.345 1.00 18.73 ? 246  VAL   B HG11 1 
ATOM   13211 H  HG12 . VAL   B 1 246 ? 6.785  33.102  61.897 1.00 18.73 ? 246  VAL   B HG12 1 
ATOM   13212 H  HG13 . VAL   B 1 246 ? 8.087  33.016  62.794 1.00 18.73 ? 246  VAL   B HG13 1 
ATOM   13213 H  HG21 . VAL   B 1 246 ? 9.927  32.129  60.637 1.00 20.38 ? 246  VAL   B HG21 1 
ATOM   13214 H  HG22 . VAL   B 1 246 ? 9.969  31.394  62.039 1.00 20.38 ? 246  VAL   B HG22 1 
ATOM   13215 H  HG23 . VAL   B 1 246 ? 9.734  30.559  60.714 1.00 20.38 ? 246  VAL   B HG23 1 
ATOM   13216 N  N    . ASN   B 1 247 ? 5.091  30.761  61.382 1.00 17.57 ? 247  ASN   B N    1 
ATOM   13217 C  CA   . ASN   B 1 247 ? 3.673  31.173  61.575 1.00 19.69 ? 247  ASN   B CA   1 
ATOM   13218 C  C    . ASN   B 1 247 ? 2.893  30.094  62.326 1.00 16.34 ? 247  ASN   B C    1 
ATOM   13219 O  O    . ASN   B 1 247 ? 1.977  30.448  63.075 1.00 18.47 ? 247  ASN   B O    1 
ATOM   13220 C  CB   . ASN   B 1 247 ? 3.001  31.530  60.246 1.00 20.17 ? 247  ASN   B CB   1 
ATOM   13221 C  CG   . ASN   B 1 247 ? 3.533  32.823  59.662 1.00 22.47 ? 247  ASN   B CG   1 
ATOM   13222 O  OD1  . ASN   B 1 247 ? 4.016  33.685  60.392 1.00 23.41 ? 247  ASN   B OD1  1 
ATOM   13223 N  ND2  . ASN   B 1 247 ? 3.453  32.966  58.350 1.00 19.24 ? 247  ASN   B ND2  1 
ATOM   13224 H  H    . ASN   B 1 247 ? 5.301  30.538  60.578 1.00 21.08 ? 247  ASN   B H    1 
ATOM   13225 H  HA   . ASN   B 1 247 ? 3.670  31.977  62.118 1.00 23.63 ? 247  ASN   B HA   1 
ATOM   13226 H  HB2  . ASN   B 1 247 ? 3.140  30.810  59.612 1.00 24.20 ? 247  ASN   B HB2  1 
ATOM   13227 H  HB3  . ASN   B 1 247 ? 2.044  31.608  60.381 1.00 24.20 ? 247  ASN   B HB3  1 
ATOM   13228 H  HD21 . ASN   B 1 247 ? 3.746  33.684  57.977 1.00 23.09 ? 247  ASN   B HD21 1 
ATOM   13229 H  HD22 . ASN   B 1 247 ? 3.108  32.341  57.870 1.00 23.09 ? 247  ASN   B HD22 1 
ATOM   13230 N  N    . ILE   B 1 248 ? 3.258  28.832  62.118 1.00 13.63 ? 248  ILE   B N    1 
ATOM   13231 C  CA   . ILE   B 1 248 ? 2.564  27.716  62.818 1.00 14.82 ? 248  ILE   B CA   1 
ATOM   13232 C  C    . ILE   B 1 248 ? 2.801  27.869  64.326 1.00 17.23 ? 248  ILE   B C    1 
ATOM   13233 O  O    . ILE   B 1 248 ? 1.817  27.843  65.091 1.00 16.37 ? 248  ILE   B O    1 
ATOM   13234 C  CB   . ILE   B 1 248 ? 3.053  26.357  62.278 1.00 16.46 ? 248  ILE   B CB   1 
ATOM   13235 C  CG1  . ILE   B 1 248 ? 2.805  26.222  60.774 1.00 17.96 ? 248  ILE   B CG1  1 
ATOM   13236 C  CG2  . ILE   B 1 248 ? 2.431  25.211  63.061 1.00 19.82 ? 248  ILE   B CG2  1 
ATOM   13237 C  CD1  . ILE   B 1 248 ? 3.448  25.004  60.156 1.00 20.43 ? 248  ILE   B CD1  1 
ATOM   13238 H  H    . ILE   B 1 248 ? 3.891  28.589  61.589 1.00 16.36 ? 248  ILE   B H    1 
ATOM   13239 H  HA   . ILE   B 1 248 ? 1.609  27.749  62.652 1.00 17.79 ? 248  ILE   B HA   1 
ATOM   13240 H  HB   . ILE   B 1 248 ? 4.014  26.314  62.405 1.00 19.75 ? 248  ILE   B HB   1 
ATOM   13241 H  HG12 . ILE   B 1 248 ? 1.849  26.188  60.614 1.00 21.56 ? 248  ILE   B HG12 1 
ATOM   13242 H  HG13 . ILE   B 1 248 ? 3.139  27.015  60.327 1.00 21.56 ? 248  ILE   B HG13 1 
ATOM   13243 H  HG21 . ILE   B 1 248 ? 2.750  24.366  62.707 1.00 23.79 ? 248  ILE   B HG21 1 
ATOM   13244 H  HG22 . ILE   B 1 248 ? 2.680  25.284  63.996 1.00 23.79 ? 248  ILE   B HG22 1 
ATOM   13245 H  HG23 . ILE   B 1 248 ? 1.465  25.250  62.980 1.00 23.79 ? 248  ILE   B HG23 1 
ATOM   13246 H  HD11 . ILE   B 1 248 ? 3.252  24.981  59.206 1.00 24.52 ? 248  ILE   B HD11 1 
ATOM   13247 H  HD12 . ILE   B 1 248 ? 4.408  25.044  60.286 1.00 24.52 ? 248  ILE   B HD12 1 
ATOM   13248 H  HD13 . ILE   B 1 248 ? 3.098  24.204  60.578 1.00 24.52 ? 248  ILE   B HD13 1 
ATOM   13249 N  N    . ILE   B 1 249 ? 4.058  28.046  64.731 1.00 16.50 ? 249  ILE   B N    1 
ATOM   13250 C  CA   . ILE   B 1 249 ? 4.369  28.125  66.188 1.00 15.47 ? 249  ILE   B CA   1 
ATOM   13251 C  C    . ILE   B 1 249 ? 3.788  29.432  66.745 1.00 14.62 ? 249  ILE   B C    1 
ATOM   13252 O  O    . ILE   B 1 249 ? 3.195  29.400  67.836 1.00 17.15 ? 249  ILE   B O    1 
ATOM   13253 C  CB   . ILE   B 1 249 ? 5.885  28.008  66.441 1.00 13.87 ? 249  ILE   B CB   1 
ATOM   13254 C  CG1  . ILE   B 1 249 ? 6.454  26.716  65.851 1.00 14.60 ? 249  ILE   B CG1  1 
ATOM   13255 C  CG2  . ILE   B 1 249 ? 6.198  28.131  67.924 1.00 14.55 ? 249  ILE   B CG2  1 
ATOM   13256 C  CD1  . ILE   B 1 249 ? 5.690  25.475  66.250 1.00 15.58 ? 249  ILE   B CD1  1 
ATOM   13257 H  H    . ILE   B 1 249 ? 4.736  28.122  64.207 1.00 19.81 ? 249  ILE   B H    1 
ATOM   13258 H  HA   . ILE   B 1 249 ? 3.959  27.378  66.652 1.00 18.57 ? 249  ILE   B HA   1 
ATOM   13259 H  HB   . ILE   B 1 249 ? 6.320  28.745  65.985 1.00 16.65 ? 249  ILE   B HB   1 
ATOM   13260 H  HG12 . ILE   B 1 249 ? 6.458  26.786  64.884 1.00 17.52 ? 249  ILE   B HG12 1 
ATOM   13261 H  HG13 . ILE   B 1 249 ? 7.378  26.621  66.132 1.00 17.52 ? 249  ILE   B HG13 1 
ATOM   13262 H  HG21 . ILE   B 1 249 ? 7.155  28.055  68.060 1.00 17.46 ? 249  ILE   B HG21 1 
ATOM   13263 H  HG22 . ILE   B 1 249 ? 5.893  28.993  68.249 1.00 17.46 ? 249  ILE   B HG22 1 
ATOM   13264 H  HG23 . ILE   B 1 249 ? 5.745  27.424  68.410 1.00 17.46 ? 249  ILE   B HG23 1 
ATOM   13265 H  HD11 . ILE   B 1 249 ? 6.102  24.697  65.844 1.00 18.70 ? 249  ILE   B HD11 1 
ATOM   13266 H  HD12 . ILE   B 1 249 ? 5.706  25.382  67.215 1.00 18.70 ? 249  ILE   B HD12 1 
ATOM   13267 H  HD13 . ILE   B 1 249 ? 4.771  25.549  65.948 1.00 18.70 ? 249  ILE   B HD13 1 
ATOM   13268 N  N    . ASN   B 1 250 ? 3.959  30.534  66.014 1.00 16.40 ? 250  ASN   B N    1 
ATOM   13269 C  CA   . ASN   B 1 250 ? 3.475  31.853  66.508 1.00 14.79 ? 250  ASN   B CA   1 
ATOM   13270 C  C    . ASN   B 1 250 ? 1.951  31.827  66.671 1.00 15.78 ? 250  ASN   B C    1 
ATOM   13271 O  O    . ASN   B 1 250 ? 1.467  32.365  67.672 1.00 17.99 ? 250  ASN   B O    1 
ATOM   13272 C  CB   . ASN   B 1 250 ? 3.914  33.000  65.597 1.00 15.71 ? 250  ASN   B CB   1 
ATOM   13273 C  CG   . ASN   B 1 250 ? 3.667  34.361  66.211 1.00 15.52 ? 250  ASN   B CG   1 
ATOM   13274 O  OD1  . ASN   B 1 250 ? 4.208  34.680  67.266 1.00 15.20 ? 250  ASN   B OD1  1 
ATOM   13275 N  ND2  . ASN   B 1 250 ? 2.851  35.168  65.554 1.00 18.63 ? 250  ASN   B ND2  1 
ATOM   13276 H  H    . ASN   B 1 250 ? 4.343  30.554  65.245 1.00 19.68 ? 250  ASN   B H    1 
ATOM   13277 H  HA   . ASN   B 1 250 ? 3.879  32.014  67.375 1.00 17.75 ? 250  ASN   B HA   1 
ATOM   13278 H  HB2  . ASN   B 1 250 ? 4.859  32.906  65.397 1.00 18.85 ? 250  ASN   B HB2  1 
ATOM   13279 H  HB3  . ASN   B 1 250 ? 3.438  32.939  64.754 1.00 18.85 ? 250  ASN   B HB3  1 
ATOM   13280 H  HD21 . ASN   B 1 250 ? 2.681  35.952  65.863 1.00 22.36 ? 250  ASN   B HD21 1 
ATOM   13281 H  HD22 . ASN   B 1 250 ? 2.491  34.909  64.817 1.00 22.36 ? 250  ASN   B HD22 1 
ATOM   13282 N  N    . GLU   B 1 251 ? 1.232  31.225  65.722 1.00 17.35 ? 251  GLU   B N    1 
ATOM   13283 C  CA   . GLU   B 1 251 ? -0.255 31.220  65.777 1.00 21.50 ? 251  GLU   B CA   1 
ATOM   13284 C  C    . GLU   B 1 251 ? -0.729 30.393  66.979 1.00 21.67 ? 251  GLU   B C    1 
ATOM   13285 O  O    . GLU   B 1 251 ? -1.855 30.627  67.435 1.00 20.23 ? 251  GLU   B O    1 
ATOM   13286 C  CB   . GLU   B 1 251 ? -0.851 30.703  64.469 1.00 23.03 ? 251  GLU   B CB   1 
ATOM   13287 C  CG   . GLU   B 1 251 ? -0.822 31.732  63.354 1.00 32.08 ? 251  GLU   B CG   1 
ATOM   13288 C  CD   . GLU   B 1 251 ? -1.082 31.168  61.968 1.00 43.30 ? 251  GLU   B CD   1 
ATOM   13289 O  OE1  . GLU   B 1 251 ? -1.572 30.026  61.879 1.00 44.46 ? 251  GLU   B OE1  1 
ATOM   13290 O  OE2  . GLU   B 1 251 ? -0.798 31.874  60.981 1.00 41.09 ? 251  GLU   B OE2  1 
ATOM   13291 H  H    . GLU   B 1 251 ? 1.569  30.817  65.044 1.00 20.83 ? 251  GLU   B H    1 
ATOM   13292 H  HA   . GLU   B 1 251 ? -0.568 32.131  65.891 1.00 25.80 ? 251  GLU   B HA   1 
ATOM   13293 H  HB2  . GLU   B 1 251 ? -0.362 29.914  64.187 1.00 27.64 ? 251  GLU   B HB2  1 
ATOM   13294 H  HB3  . GLU   B 1 251 ? -1.768 30.428  64.624 1.00 27.64 ? 251  GLU   B HB3  1 
ATOM   13295 H  HG2  . GLU   B 1 251 ? -1.485 32.415  63.542 1.00 38.49 ? 251  GLU   B HG2  1 
ATOM   13296 H  HG3  . GLU   B 1 251 ? 0.044  32.169  63.355 1.00 38.49 ? 251  GLU   B HG3  1 
ATOM   13297 N  N    . ASN   B 1 252 ? 0.102  29.470  67.465 1.00 19.81 ? 252  ASN   B N    1 
ATOM   13298 C  CA   . ASN   B 1 252 ? -0.242 28.674  68.673 1.00 19.71 ? 252  ASN   B CA   1 
ATOM   13299 C  C    . ASN   B 1 252 ? 0.185  29.436  69.933 1.00 18.49 ? 252  ASN   B C    1 
ATOM   13300 O  O    . ASN   B 1 252 ? -0.077 28.936  71.036 1.00 18.40 ? 252  ASN   B O    1 
ATOM   13301 C  CB   . ASN   B 1 252 ? 0.396  27.283  68.622 1.00 18.92 ? 252  ASN   B CB   1 
ATOM   13302 C  CG   . ASN   B 1 252 ? -0.370 26.316  67.746 1.00 21.31 ? 252  ASN   B CG   1 
ATOM   13303 O  OD1  . ASN   B 1 252 ? -1.417 25.812  68.141 1.00 25.06 ? 252  ASN   B OD1  1 
ATOM   13304 N  ND2  . ASN   B 1 252 ? 0.143  26.053  66.556 1.00 23.89 ? 252  ASN   B ND2  1 
ATOM   13305 H  H    . ASN   B 1 252 ? 0.867  29.282  67.120 1.00 23.77 ? 252  ASN   B H    1 
ATOM   13306 H  HA   . ASN   B 1 252 ? -1.203 28.546  68.698 1.00 23.66 ? 252  ASN   B HA   1 
ATOM   13307 H  HB2  . ASN   B 1 252 ? 1.305  27.361  68.292 1.00 22.71 ? 252  ASN   B HB2  1 
ATOM   13308 H  HB3  . ASN   B 1 252 ? 0.451  26.924  69.521 1.00 22.71 ? 252  ASN   B HB3  1 
ATOM   13309 H  HD21 . ASN   B 1 252 ? -0.260 25.510  66.025 1.00 28.67 ? 252  ASN   B HD21 1 
ATOM   13310 H  HD22 . ASN   B 1 252 ? 0.879  26.425  66.313 1.00 28.67 ? 252  ASN   B HD22 1 
ATOM   13311 N  N    . GLY   B 1 253 ? 0.828  30.593  69.768 1.00 15.01 ? 253  GLY   B N    1 
ATOM   13312 C  CA   . GLY   B 1 253 ? 1.232  31.420  70.920 1.00 14.11 ? 253  GLY   B CA   1 
ATOM   13313 C  C    . GLY   B 1 253 ? 2.309  30.768  71.767 1.00 17.10 ? 253  GLY   B C    1 
ATOM   13314 O  O    . GLY   B 1 253 ? 2.309  30.974  72.987 1.00 14.79 ? 253  GLY   B O    1 
ATOM   13315 H  H    . GLY   B 1 253 ? 1.041  30.920  69.002 1.00 18.02 ? 253  GLY   B H    1 
ATOM   13316 H  HA2  . GLY   B 1 253 ? 1.554  32.277  70.600 1.00 16.94 ? 253  GLY   B HA2  1 
ATOM   13317 H  HA3  . GLY   B 1 253 ? 0.455  31.597  71.473 1.00 16.94 ? 253  GLY   B HA3  1 
ATOM   13318 N  N    . VAL   B 1 254 ? 3.212  30.022  71.130 1.00 17.14 ? 254  VAL   B N    1 
ATOM   13319 C  CA   . VAL   B 1 254 ? 4.323  29.351  71.867 1.00 15.01 ? 254  VAL   B CA   1 
ATOM   13320 C  C    . VAL   B 1 254 ? 5.640  29.684  71.157 1.00 14.84 ? 254  VAL   B C    1 
ATOM   13321 O  O    . VAL   B 1 254 ? 6.563  28.858  71.213 1.00 13.21 ? 254  VAL   B O    1 
ATOM   13322 C  CB   . VAL   B 1 254 ? 4.083  27.833  71.982 1.00 15.08 ? 254  VAL   B CB   1 
ATOM   13323 C  CG1  . VAL   B 1 254 ? 3.116  27.516  73.112 1.00 16.46 ? 254  VAL   B CG1  1 
ATOM   13324 C  CG2  . VAL   B 1 254 ? 3.585  27.240  70.674 1.00 14.42 ? 254  VAL   B CG2  1 
ATOM   13325 H  H    . VAL   B 1 254 ? 3.212  29.884  70.281 1.00 20.58 ? 254  VAL   B H    1 
ATOM   13326 H  HA   . VAL   B 1 254 ? 4.365  29.680  72.779 1.00 18.01 ? 254  VAL   B HA   1 
ATOM   13327 H  HB   . VAL   B 1 254 ? 4.939  27.424  72.185 1.00 18.10 ? 254  VAL   B HB   1 
ATOM   13328 H  HG11 . VAL   B 1 254 ? 2.982  26.557  73.164 1.00 19.75 ? 254  VAL   B HG11 1 
ATOM   13329 H  HG12 . VAL   B 1 254 ? 3.482  27.836  73.951 1.00 19.75 ? 254  VAL   B HG12 1 
ATOM   13330 H  HG13 . VAL   B 1 254 ? 2.266  27.952  72.943 1.00 19.75 ? 254  VAL   B HG13 1 
ATOM   13331 H  HG21 . VAL   B 1 254 ? 3.445  26.286  70.783 1.00 17.31 ? 254  VAL   B HG21 1 
ATOM   13332 H  HG22 . VAL   B 1 254 ? 2.748  27.662  70.425 1.00 17.31 ? 254  VAL   B HG22 1 
ATOM   13333 H  HG23 . VAL   B 1 254 ? 4.243  27.392  69.978 1.00 17.31 ? 254  VAL   B HG23 1 
ATOM   13334 N  N    . HIS   B 1 255 ? 5.698  30.851  70.513 1.00 14.51 ? 255  HIS   B N    1 
ATOM   13335 C  CA   . HIS   B 1 255 ? 6.935  31.311  69.829 1.00 15.73 ? 255  HIS   B CA   1 
ATOM   13336 C  C    . HIS   B 1 255 ? 7.657  32.252  70.796 1.00 13.94 ? 255  HIS   B C    1 
ATOM   13337 O  O    . HIS   B 1 255 ? 7.174  33.373  71.022 1.00 15.95 ? 255  HIS   B O    1 
ATOM   13338 C  CB   . HIS   B 1 255 ? 6.571  31.958  68.490 1.00 13.90 ? 255  HIS   B CB   1 
ATOM   13339 C  CG   . HIS   B 1 255 ? 7.745  32.389  67.680 1.00 14.22 ? 255  HIS   B CG   1 
ATOM   13340 N  ND1  . HIS   B 1 255 ? 8.522  31.506  66.963 1.00 14.03 ? 255  HIS   B ND1  1 
ATOM   13341 C  CD2  . HIS   B 1 255 ? 8.269  33.601  67.468 1.00 16.83 ? 255  HIS   B CD2  1 
ATOM   13342 C  CE1  . HIS   B 1 255 ? 9.482  32.175  66.343 1.00 16.09 ? 255  HIS   B CE1  1 
ATOM   13343 N  NE2  . HIS   B 1 255 ? 9.347  33.449  66.636 1.00 15.11 ? 255  HIS   B NE2  1 
ATOM   13344 H  H    . HIS   B 1 255 ? 5.037  31.398  70.455 1.00 17.41 ? 255  HIS   B H    1 
ATOM   13345 H  HA   . HIS   B 1 255 ? 7.535  30.581  69.611 1.00 18.88 ? 255  HIS   B HA   1 
ATOM   13346 H  HB2  . HIS   B 1 255 ? 6.046  31.329  67.971 1.00 16.69 ? 255  HIS   B HB2  1 
ATOM   13347 H  HB3  . HIS   B 1 255 ? 6.006  32.729  68.658 1.00 16.69 ? 255  HIS   B HB3  1 
ATOM   13348 H  HD1  . HIS   B 1 255 ? 8.403  30.655  66.924 1.00 16.84 ? 255  HIS   B HD1  1 
ATOM   13349 H  HD2  . HIS   B 1 255 ? 7.958  34.403  67.822 1.00 20.19 ? 255  HIS   B HD2  1 
ATOM   13350 H  HE1  . HIS   B 1 255 ? 10.138 31.807  65.795 1.00 19.32 ? 255  HIS   B HE1  1 
ATOM   13351 N  N    . PRO   B 1 256 ? 8.798  31.851  71.391 1.00 15.42 ? 256  PRO   B N    1 
ATOM   13352 C  CA   . PRO   B 1 256 ? 9.448  32.672  72.409 1.00 13.18 ? 256  PRO   B CA   1 
ATOM   13353 C  C    . PRO   B 1 256 ? 9.821  34.064  71.886 1.00 12.13 ? 256  PRO   B C    1 
ATOM   13354 O  O    . PRO   B 1 256 ? 10.360 34.166  70.807 1.00 15.22 ? 256  PRO   B O    1 
ATOM   13355 C  CB   . PRO   B 1 256 ? 10.695 31.869  72.813 1.00 13.90 ? 256  PRO   B CB   1 
ATOM   13356 C  CG   . PRO   B 1 256 ? 10.398 30.457  72.348 1.00 12.87 ? 256  PRO   B CG   1 
ATOM   13357 C  CD   . PRO   B 1 256 ? 9.520  30.610  71.124 1.00 15.85 ? 256  PRO   B CD   1 
ATOM   13358 H  HA   . PRO   B 1 256 ? 8.858  32.843  73.160 1.00 15.81 ? 256  PRO   B HA   1 
ATOM   13359 H  HB2  . PRO   B 1 256 ? 11.494 32.220  72.390 1.00 16.69 ? 256  PRO   B HB2  1 
ATOM   13360 H  HB3  . PRO   B 1 256 ? 10.843 31.903  73.771 1.00 16.69 ? 256  PRO   B HB3  1 
ATOM   13361 H  HG2  . PRO   B 1 256 ? 11.215 29.981  72.134 1.00 15.45 ? 256  PRO   B HG2  1 
ATOM   13362 H  HG3  . PRO   B 1 256 ? 9.947  29.949  73.040 1.00 15.45 ? 256  PRO   B HG3  1 
ATOM   13363 H  HD2  . PRO   B 1 256 ? 10.045 30.668  70.310 1.00 19.03 ? 256  PRO   B HD2  1 
ATOM   13364 H  HD3  . PRO   B 1 256 ? 8.916  29.858  71.019 1.00 19.03 ? 256  PRO   B HD3  1 
ATOM   13365 N  N    . VAL   B 1 257 ? 9.524  35.089  72.684 1.00 14.60 ? 257  VAL   B N    1 
ATOM   13366 C  CA   . VAL   B 1 257 ? 9.845  36.486  72.283 1.00 13.01 ? 257  VAL   B CA   1 
ATOM   13367 C  C    . VAL   B 1 257 ? 10.628 37.152  73.416 1.00 14.30 ? 257  VAL   B C    1 
ATOM   13368 O  O    . VAL   B 1 257 ? 10.254 36.962  74.581 1.00 14.98 ? 257  VAL   B O    1 
ATOM   13369 C  CB   . VAL   B 1 257 ? 8.564  37.268  71.928 1.00 16.62 ? 257  VAL   B CB   1 
ATOM   13370 C  CG1  . VAL   B 1 257 ? 8.828  38.759  71.793 1.00 16.90 ? 257  VAL   B CG1  1 
ATOM   13371 C  CG2  . VAL   B 1 257 ? 7.903  36.723  70.672 1.00 14.41 ? 257  VAL   B CG2  1 
ATOM   13372 H  H    . VAL   B 1 257 ? 9.143  35.012  73.451 1.00 17.53 ? 257  VAL   B H    1 
ATOM   13373 H  HA   . VAL   B 1 257 ? 10.393 36.482  71.483 1.00 15.61 ? 257  VAL   B HA   1 
ATOM   13374 H  HB   . VAL   B 1 257 ? 7.949  37.143  72.668 1.00 19.95 ? 257  VAL   B HB   1 
ATOM   13375 H  HG11 . VAL   B 1 257 ? 8.002  39.215  71.570 1.00 20.28 ? 257  VAL   B HG11 1 
ATOM   13376 H  HG12 . VAL   B 1 257 ? 9.171  39.104  72.632 1.00 20.28 ? 257  VAL   B HG12 1 
ATOM   13377 H  HG13 . VAL   B 1 257 ? 9.480  38.910  71.091 1.00 20.28 ? 257  VAL   B HG13 1 
ATOM   13378 H  HG21 . VAL   B 1 257 ? 7.103  37.236  70.478 1.00 17.29 ? 257  VAL   B HG21 1 
ATOM   13379 H  HG22 . VAL   B 1 257 ? 8.519  36.792  69.926 1.00 17.29 ? 257  VAL   B HG22 1 
ATOM   13380 H  HG23 . VAL   B 1 257 ? 7.665  35.793  70.809 1.00 17.29 ? 257  VAL   B HG23 1 
ATOM   13381 N  N    . LYS   B 1 258 ? 11.691 37.879  73.067 1.00 14.35 ? 258  LYS   B N    1 
ATOM   13382 C  CA   . LYS   B 1 258 ? 12.524 38.592  74.073 1.00 13.43 ? 258  LYS   B CA   1 
ATOM   13383 C  C    . LYS   B 1 258 ? 12.939 37.645  75.202 1.00 13.10 ? 258  LYS   B C    1 
ATOM   13384 O  O    . LYS   B 1 258 ? 12.529 37.877  76.345 1.00 14.80 ? 258  LYS   B O    1 
ATOM   13385 C  CB   . LYS   B 1 258 ? 11.791 39.841  74.572 1.00 16.03 ? 258  LYS   B CB   1 
ATOM   13386 C  CG   . LYS   B 1 258 ? 11.658 40.945  73.532 1.00 17.21 ? 258  LYS   B CG   1 
ATOM   13387 C  CD   . LYS   B 1 258 ? 10.662 42.014  73.922 1.00 20.52 ? 258  LYS   B CD   1 
ATOM   13388 C  CE   . LYS   B 1 258 ? 10.904 43.333  73.222 1.00 23.43 ? 258  LYS   B CE   1 
ATOM   13389 N  NZ   . LYS   B 1 258 ? 10.047 44.406  73.779 1.00 28.75 ? 258  LYS   B NZ   1 
ATOM   13390 H  H    . LYS   B 1 258 ? 11.956 37.979  72.255 1.00 17.23 ? 258  LYS   B H    1 
ATOM   13391 H  HA   . LYS   B 1 258 ? 13.347 38.895  73.658 1.00 16.12 ? 258  LYS   B HA   1 
ATOM   13392 H  HB2  . LYS   B 1 258 ? 10.905 39.585  74.872 1.00 19.23 ? 258  LYS   B HB2  1 
ATOM   13393 H  HB3  . LYS   B 1 258 ? 12.261 40.193  75.344 1.00 19.23 ? 258  LYS   B HB3  1 
ATOM   13394 H  HG2  . LYS   B 1 258 ? 12.526 41.355  73.392 1.00 20.66 ? 258  LYS   B HG2  1 
ATOM   13395 H  HG3  . LYS   B 1 258 ? 11.389 40.554  72.686 1.00 20.66 ? 258  LYS   B HG3  1 
ATOM   13396 H  HD2  . LYS   B 1 258 ? 9.766  41.704  73.716 1.00 24.63 ? 258  LYS   B HD2  1 
ATOM   13397 H  HD3  . LYS   B 1 258 ? 10.702 42.151  74.881 1.00 24.63 ? 258  LYS   B HD3  1 
ATOM   13398 H  HE2  . LYS   B 1 258 ? 11.837 43.582  73.312 1.00 28.12 ? 258  LYS   B HE2  1 
ATOM   13399 H  HE3  . LYS   B 1 258 ? 10.727 43.235  72.273 1.00 28.12 ? 258  LYS   B HE3  1 
ATOM   13400 H  HZ1  . LYS   B 1 258 ? 10.123 45.137  73.278 1.00 34.50 ? 258  LYS   B HZ1  1 
ATOM   13401 H  HZ2  . LYS   B 1 258 ? 9.199  44.137  73.783 1.00 34.50 ? 258  LYS   B HZ2  1 
ATOM   13402 H  HZ3  . LYS   B 1 258 ? 10.304 44.589  74.611 1.00 34.50 ? 258  LYS   B HZ3  1 
ATOM   13403 N  N    . ASN   B 1 259 ? 13.744 36.631  74.882 1.00 14.20 ? 259  ASN   B N    1 
ATOM   13404 C  CA   . ASN   B 1 259 ? 14.278 35.713  75.925 1.00 13.90 ? 259  ASN   B CA   1 
ATOM   13405 C  C    . ASN   B 1 259 ? 13.133 35.023  76.679 1.00 14.55 ? 259  ASN   B C    1 
ATOM   13406 O  O    . ASN   B 1 259 ? 13.287 34.820  77.891 1.00 13.62 ? 259  ASN   B O    1 
ATOM   13407 C  CB   . ASN   B 1 259 ? 15.276 36.420  76.845 1.00 14.46 ? 259  ASN   B CB   1 
ATOM   13408 C  CG   . ASN   B 1 259 ? 16.249 35.470  77.509 1.00 14.29 ? 259  ASN   B CG   1 
ATOM   13409 O  OD1  . ASN   B 1 259 ? 16.670 34.487  76.906 1.00 14.25 ? 259  ASN   B OD1  1 
ATOM   13410 N  ND2  . ASN   B 1 259 ? 16.609 35.755  78.749 1.00 13.59 ? 259  ASN   B ND2  1 
ATOM   13411 H  H    . ASN   B 1 259 ? 13.997 36.449  74.080 1.00 17.05 ? 259  ASN   B H    1 
ATOM   13412 H  HA   . ASN   B 1 259 ? 14.784 35.010  75.487 1.00 16.68 ? 259  ASN   B HA   1 
ATOM   13413 H  HB2  . ASN   B 1 259 ? 15.773 37.076  76.331 1.00 17.36 ? 259  ASN   B HB2  1 
ATOM   13414 H  HB3  . ASN   B 1 259 ? 14.789 36.906  77.529 1.00 17.36 ? 259  ASN   B HB3  1 
ATOM   13415 H  HD21 . ASN   B 1 259 ? 17.160 35.242  79.166 1.00 16.31 ? 259  ASN   B HD21 1 
ATOM   13416 H  HD22 . ASN   B 1 259 ? 16.293 36.453  79.139 1.00 16.31 ? 259  ASN   B HD22 1 
ATOM   13417 N  N    . PHE   B 1 260 ? 12.057 34.665  75.975 1.00 14.16 ? 260  PHE   B N    1 
ATOM   13418 C  CA   . PHE   B 1 260 ? 10.918 33.915  76.579 1.00 14.85 ? 260  PHE   B CA   1 
ATOM   13419 C  C    . PHE   B 1 260 ? 10.077 34.817  77.492 1.00 15.97 ? 260  PHE   B C    1 
ATOM   13420 O  O    . PHE   B 1 260 ? 9.184  34.294  78.174 1.00 16.35 ? 260  PHE   B O    1 
ATOM   13421 C  CB   . PHE   B 1 260 ? 11.402 32.670  77.331 1.00 14.74 ? 260  PHE   B CB   1 
ATOM   13422 C  CG   . PHE   B 1 260 ? 11.884 31.536  76.461 1.00 13.54 ? 260  PHE   B CG   1 
ATOM   13423 C  CD1  . PHE   B 1 260 ? 13.095 31.617  75.794 1.00 14.43 ? 260  PHE   B CD1  1 
ATOM   13424 C  CD2  . PHE   B 1 260 ? 11.135 30.379  76.322 1.00 14.77 ? 260  PHE   B CD2  1 
ATOM   13425 C  CE1  . PHE   B 1 260 ? 13.540 30.573  75.000 1.00 13.57 ? 260  PHE   B CE1  1 
ATOM   13426 C  CE2  . PHE   B 1 260 ? 11.581 29.335  75.528 1.00 12.12 ? 260  PHE   B CE2  1 
ATOM   13427 C  CZ   . PHE   B 1 260 ? 12.783 29.433  74.869 1.00 11.76 ? 260  PHE   B CZ   1 
ATOM   13428 H  H    . PHE   B 1 260 ? 11.955 34.843  75.140 1.00 16.99 ? 260  PHE   B H    1 
ATOM   13429 H  HA   . PHE   B 1 260 ? 10.350 33.617  75.851 1.00 17.83 ? 260  PHE   B HA   1 
ATOM   13430 H  HB2  . PHE   B 1 260 ? 12.123 32.930  77.926 1.00 17.70 ? 260  PHE   B HB2  1 
ATOM   13431 H  HB3  . PHE   B 1 260 ? 10.677 32.345  77.888 1.00 17.70 ? 260  PHE   B HB3  1 
ATOM   13432 H  HD1  . PHE   B 1 260 ? 13.616 32.382  75.880 1.00 17.31 ? 260  PHE   B HD1  1 
ATOM   13433 H  HD2  . PHE   B 1 260 ? 10.322 30.302  76.767 1.00 17.73 ? 260  PHE   B HD2  1 
ATOM   13434 H  HE1  . PHE   B 1 260 ? 14.353 30.643  74.554 1.00 16.29 ? 260  PHE   B HE1  1 
ATOM   13435 H  HE2  . PHE   B 1 260 ? 11.066 28.566  75.441 1.00 14.55 ? 260  PHE   B HE2  1 
ATOM   13436 H  HZ   . PHE   B 1 260 ? 13.083 28.732  74.337 1.00 14.12 ? 260  PHE   B HZ   1 
ATOM   13437 N  N    . GLN   B 1 261 ? 10.341 36.124  77.491 1.00 16.05 ? 261  GLN   B N    1 
ATOM   13438 C  CA   . GLN   B 1 261 ? 9.474  37.021  78.298 1.00 15.90 ? 261  GLN   B CA   1 
ATOM   13439 C  C    . GLN   B 1 261 ? 8.068  37.003  77.694 1.00 16.40 ? 261  GLN   B C    1 
ATOM   13440 O  O    . GLN   B 1 261 ? 7.104  37.175  78.457 1.00 19.25 ? 261  GLN   B O    1 
ATOM   13441 C  CB   . GLN   B 1 261 ? 10.063 38.431  78.371 1.00 16.74 ? 261  GLN   B CB   1 
ATOM   13442 C  CG   . GLN   B 1 261 ? 11.259 38.536  79.303 1.00 17.10 ? 261  GLN   B CG   1 
ATOM   13443 C  CD   . GLN   B 1 261 ? 11.756 39.956  79.405 1.00 20.22 ? 261  GLN   B CD   1 
ATOM   13444 O  OE1  . GLN   B 1 261 ? 11.398 40.693  80.319 1.00 17.38 ? 261  GLN   B OE1  1 
ATOM   13445 N  NE2  . GLN   B 1 261 ? 12.586 40.351  78.454 1.00 17.78 ? 261  GLN   B NE2  1 
ATOM   13446 H  H    . GLN   B 1 261 ? 10.979 36.506  77.059 1.00 19.27 ? 261  GLN   B H    1 
ATOM   13447 H  HA   . GLN   B 1 261 ? 9.423  36.706  79.214 1.00 19.09 ? 261  GLN   B HA   1 
ATOM   13448 H  HB2  . GLN   B 1 261 ? 10.329 38.710  77.481 1.00 20.09 ? 261  GLN   B HB2  1 
ATOM   13449 H  HB3  . GLN   B 1 261 ? 9.375  39.047  78.667 1.00 20.09 ? 261  GLN   B HB3  1 
ATOM   13450 H  HG2  . GLN   B 1 261 ? 11.013 38.214  80.184 1.00 20.52 ? 261  GLN   B HG2  1 
ATOM   13451 H  HG3  . GLN   B 1 261 ? 11.973 37.964  78.981 1.00 20.52 ? 261  GLN   B HG3  1 
ATOM   13452 H  HE21 . GLN   B 1 261 ? 12.815 39.806  77.829 1.00 21.34 ? 261  GLN   B HE21 1 
ATOM   13453 H  HE22 . GLN   B 1 261 ? 12.897 41.153  78.461 1.00 21.34 ? 261  GLN   B HE22 1 
ATOM   13454 N  N    . GLU   B 1 262 ? 7.966  36.806  76.380 1.00 17.43 ? 262  GLU   B N    1 
ATOM   13455 C  CA   . GLU   B 1 262 ? 6.634  36.703  75.722 1.00 18.64 ? 262  GLU   B CA   1 
ATOM   13456 C  C    . GLU   B 1 262 ? 6.587  35.446  74.845 1.00 14.33 ? 262  GLU   B C    1 
ATOM   13457 O  O    . GLU   B 1 262 ? 7.637  34.815  74.670 1.00 13.86 ? 262  GLU   B O    1 
ATOM   13458 C  CB   . GLU   B 1 262 ? 6.308  37.971  74.930 1.00 17.58 ? 262  GLU   B CB   1 
ATOM   13459 C  CG   . GLU   B 1 262 ? 6.088  39.188  75.807 1.00 19.14 ? 262  GLU   B CG   1 
ATOM   13460 C  CD   . GLU   B 1 262 ? 6.012  40.493  75.034 1.00 27.50 ? 262  GLU   B CD   1 
ATOM   13461 O  OE1  . GLU   B 1 262 ? 5.118  40.615  74.177 1.00 26.88 ? 262  GLU   B OE1  1 
ATOM   13462 O  OE2  . GLU   B 1 262 ? 6.851  41.376  75.285 1.00 25.61 ? 262  GLU   B OE2  1 
ATOM   13463 H  H    . GLU   B 1 262 ? 8.637  36.729  75.848 1.00 20.92 ? 262  GLU   B H    1 
ATOM   13464 H  HA   . GLU   B 1 262 ? 5.949  36.621  76.404 1.00 22.37 ? 262  GLU   B HA   1 
ATOM   13465 H  HB2  . GLU   B 1 262 ? 7.032  38.153  74.311 1.00 21.10 ? 262  GLU   B HB2  1 
ATOM   13466 H  HB3  . GLU   B 1 262 ? 5.512  37.816  74.397 1.00 21.10 ? 262  GLU   B HB3  1 
ATOM   13467 H  HG2  . GLU   B 1 262 ? 5.266  39.071  76.309 1.00 22.97 ? 262  GLU   B HG2  1 
ATOM   13468 H  HG3  . GLU   B 1 262 ? 6.809  39.246  76.453 1.00 22.97 ? 262  GLU   B HG3  1 
ATOM   13469 N  N    . SER   B 1 263 ? 5.410  35.112  74.315 1.00 16.98 ? 263  SER   B N    1 
ATOM   13470 C  CA   . SER   B 1 263 ? 5.249  33.840  73.563 1.00 14.54 ? 263  SER   B CA   1 
ATOM   13471 C  C    . SER   B 1 263 ? 4.504  34.082  72.250 1.00 15.22 ? 263  SER   B C    1 
ATOM   13472 O  O    . SER   B 1 263 ? 4.068  33.103  71.629 1.00 16.01 ? 263  SER   B O    1 
ATOM   13473 C  CB   . SER   B 1 263 ? 4.522  32.839  74.426 1.00 15.92 ? 263  SER   B CB   1 
ATOM   13474 O  OG   . SER   B 1 263 ? 4.966  32.914  75.772 1.00 16.25 ? 263  SER   B OG   1 
ATOM   13475 H  H    . SER   B 1 263 ? 4.698  35.591  74.372 1.00 20.38 ? 263  SER   B H    1 
ATOM   13476 H  HA   . SER   B 1 263 ? 6.123  33.484  73.340 1.00 17.46 ? 263  SER   B HA   1 
ATOM   13477 H  HB2  . SER   B 1 263 ? 3.567  33.005  74.387 1.00 19.11 ? 263  SER   B HB2  1 
ATOM   13478 H  HB3  . SER   B 1 263 ? 4.668  31.944  74.083 1.00 19.11 ? 263  SER   B HB3  1 
ATOM   13479 H  HG   . SER   B 1 263 ? 5.430  32.238  75.952 1.00 19.50 ? 263  SER   B HG   1 
ATOM   13480 N  N    . TYR   B 1 264 ? 4.357  35.350  71.861 1.00 16.60 ? 264  TYR   B N    1 
ATOM   13481 C  CA   . TYR   B 1 264 ? 3.608  35.696  70.629 1.00 17.32 ? 264  TYR   B CA   1 
ATOM   13482 C  C    . TYR   B 1 264 ? 4.060  37.065  70.119 1.00 17.60 ? 264  TYR   B C    1 
ATOM   13483 O  O    . TYR   B 1 264 ? 4.337  37.944  70.944 1.00 14.81 ? 264  TYR   B O    1 
ATOM   13484 C  CB   . TYR   B 1 264 ? 2.101  35.757  70.889 1.00 20.23 ? 264  TYR   B CB   1 
ATOM   13485 C  CG   . TYR   B 1 264 ? 1.304  36.270  69.718 1.00 21.13 ? 264  TYR   B CG   1 
ATOM   13486 C  CD1  . TYR   B 1 264 ? 0.912  35.421  68.699 1.00 18.98 ? 264  TYR   B CD1  1 
ATOM   13487 C  CD2  . TYR   B 1 264 ? 0.962  37.608  69.617 1.00 26.68 ? 264  TYR   B CD2  1 
ATOM   13488 C  CE1  . TYR   B 1 264 ? 0.191  35.885  67.612 1.00 23.05 ? 264  TYR   B CE1  1 
ATOM   13489 C  CE2  . TYR   B 1 264 ? 0.246  38.090  68.535 1.00 27.88 ? 264  TYR   B CE2  1 
ATOM   13490 C  CZ   . TYR   B 1 264 ? -0.144 37.224  67.531 1.00 26.75 ? 264  TYR   B CZ   1 
ATOM   13491 O  OH   . TYR   B 1 264 ? -0.859 37.690  66.457 1.00 31.39 ? 264  TYR   B OH   1 
ATOM   13492 H  H    . TYR   B 1 264 ? 4.677  36.025  72.286 1.00 19.93 ? 264  TYR   B H    1 
ATOM   13493 H  HA   . TYR   B 1 264 ? 3.789  35.005  69.972 1.00 20.79 ? 264  TYR   B HA   1 
ATOM   13494 H  HB2  . TYR   B 1 264 ? 1.785  34.870  71.121 1.00 24.28 ? 264  TYR   B HB2  1 
ATOM   13495 H  HB3  . TYR   B 1 264 ? 1.936  36.327  71.657 1.00 24.28 ? 264  TYR   B HB3  1 
ATOM   13496 H  HD1  . TYR   B 1 264 ? 1.137  34.520  68.745 1.00 22.78 ? 264  TYR   B HD1  1 
ATOM   13497 H  HD2  . TYR   B 1 264 ? 1.219  38.195  70.291 1.00 32.02 ? 264  TYR   B HD2  1 
ATOM   13498 H  HE1  . TYR   B 1 264 ? -0.067 35.298  66.938 1.00 27.67 ? 264  TYR   B HE1  1 
ATOM   13499 H  HE2  . TYR   B 1 264 ? 0.028  38.993  68.484 1.00 33.46 ? 264  TYR   B HE2  1 
ATOM   13500 H  HH   . TYR   B 1 264 ? -0.989 38.515  66.543 1.00 37.68 ? 264  TYR   B HH   1 
ATOM   13501 N  N    . THR   B 1 265 ? 4.138  37.212  68.797 1.00 17.66 ? 265  THR   B N    1 
ATOM   13502 C  CA   . THR   B 1 265 ? 4.488  38.528  68.205 1.00 19.39 ? 265  THR   B CA   1 
ATOM   13503 C  C    . THR   B 1 265 ? 3.711  38.713  66.901 1.00 20.89 ? 265  THR   B C    1 
ATOM   13504 O  O    . THR   B 1 265 ? 3.629  37.756  66.117 1.00 18.69 ? 265  THR   B O    1 
ATOM   13505 C  CB   . THR   B 1 265 ? 5.995  38.704  67.987 1.00 15.44 ? 265  THR   B CB   1 
ATOM   13506 O  OG1  . THR   B 1 265 ? 6.172  39.912  67.248 1.00 17.41 ? 265  THR   B OG1  1 
ATOM   13507 C  CG2  . THR   B 1 265 ? 6.622  37.547  67.240 1.00 17.06 ? 265  THR   B CG2  1 
ATOM   13508 H  H    . THR   B 1 265 ? 3.997  36.583  68.227 1.00 21.20 ? 265  THR   B H    1 
ATOM   13509 H  HA   . THR   B 1 265 ? 4.234  39.218  68.838 1.00 23.27 ? 265  THR   B HA   1 
ATOM   13510 H  HB   . THR   B 1 265 ? 6.437  38.737  68.850 1.00 18.53 ? 265  THR   B HB   1 
ATOM   13511 H  HG1  . THR   B 1 265 ? 6.250  40.557  67.780 1.00 20.89 ? 265  THR   B HG1  1 
ATOM   13512 H  HG21 . THR   B 1 265 ? 7.572  37.709  67.130 1.00 20.47 ? 265  THR   B HG21 1 
ATOM   13513 H  HG22 . THR   B 1 265 ? 6.490  36.728  67.743 1.00 20.47 ? 265  THR   B HG22 1 
ATOM   13514 H  HG23 . THR   B 1 265 ? 6.206  37.461  66.368 1.00 20.47 ? 265  THR   B HG23 1 
ATOM   13515 N  N    . ASN   B 1 266 ? 3.159  39.909  66.702 1.00 16.79 ? 266  ASN   B N    1 
ATOM   13516 C  CA   . ASN   B 1 266 ? 2.416  40.220  65.457 1.00 22.75 ? 266  ASN   B CA   1 
ATOM   13517 C  C    . ASN   B 1 266 ? 3.407  40.554  64.330 1.00 19.43 ? 266  ASN   B C    1 
ATOM   13518 O  O    . ASN   B 1 266 ? 2.947  40.906  63.236 1.00 20.98 ? 266  ASN   B O    1 
ATOM   13519 C  CB   . ASN   B 1 266 ? 1.425  41.361  65.707 1.00 24.56 ? 266  ASN   B CB   1 
ATOM   13520 C  CG   . ASN   B 1 266 ? 2.050  42.517  66.459 1.00 29.05 ? 266  ASN   B CG   1 
ATOM   13521 O  OD1  . ASN   B 1 266 ? 3.265  42.698  66.429 1.00 25.59 ? 266  ASN   B OD1  1 
ATOM   13522 N  ND2  . ASN   B 1 266 ? 1.232  43.303  67.138 1.00 35.30 ? 266  ASN   B ND2  1 
ATOM   13523 H  H    . ASN   B 1 266 ? 3.197  40.557  67.266 1.00 20.15 ? 266  ASN   B H    1 
ATOM   13524 H  HA   . ASN   B 1 266 ? 1.903  39.445  65.179 1.00 27.31 ? 266  ASN   B HA   1 
ATOM   13525 H  HB2  . ASN   B 1 266 ? 1.082  41.679  64.857 1.00 29.48 ? 266  ASN   B HB2  1 
ATOM   13526 H  HB3  . ASN   B 1 266 ? 0.668  41.023  66.210 1.00 29.48 ? 266  ASN   B HB3  1 
ATOM   13527 H  HD21 . ASN   B 1 266 ? 1.546  43.970  67.581 1.00 42.36 ? 266  ASN   B HD21 1 
ATOM   13528 H  HD22 . ASN   B 1 266 ? 0.386  43.147  67.137 1.00 42.36 ? 266  ASN   B HD22 1 
ATOM   13529 N  N    . GLN   B 1 267 ? 4.714  40.428  64.591 1.00 17.60 ? 267  GLN   B N    1 
ATOM   13530 C  CA   . GLN   B 1 267 ? 5.750  40.727  63.562 1.00 18.89 ? 267  GLN   B CA   1 
ATOM   13531 C  C    . GLN   B 1 267 ? 6.349  39.436  62.988 1.00 18.78 ? 267  GLN   B C    1 
ATOM   13532 O  O    . GLN   B 1 267 ? 7.241  39.542  62.137 1.00 16.05 ? 267  GLN   B O    1 
ATOM   13533 C  CB   . GLN   B 1 267 ? 6.883  41.551  64.171 1.00 15.71 ? 267  GLN   B CB   1 
ATOM   13534 C  CG   . GLN   B 1 267 ? 6.416  42.812  64.881 1.00 18.44 ? 267  GLN   B CG   1 
ATOM   13535 C  CD   . GLN   B 1 267 ? 5.681  43.722  63.930 1.00 16.37 ? 267  GLN   B CD   1 
ATOM   13536 O  OE1  . GLN   B 1 267 ? 6.177  44.058  62.858 1.00 16.43 ? 267  GLN   B OE1  1 
ATOM   13537 N  NE2  . GLN   B 1 267 ? 4.480  44.118  64.315 1.00 17.78 ? 267  GLN   B NE2  1 
ATOM   13538 H  H    . GLN   B 1 267 ? 5.030  40.173  65.349 1.00 21.13 ? 267  GLN   B H    1 
ATOM   13539 H  HA   . GLN   B 1 267 ? 5.316  41.226  62.852 1.00 22.67 ? 267  GLN   B HA   1 
ATOM   13540 H  HB2  . GLN   B 1 267 ? 7.371  40.998  64.801 1.00 18.85 ? 267  GLN   B HB2  1 
ATOM   13541 H  HB3  . GLN   B 1 267 ? 7.505  41.797  63.469 1.00 18.85 ? 267  GLN   B HB3  1 
ATOM   13542 H  HG2  . GLN   B 1 267 ? 5.836  42.575  65.622 1.00 22.14 ? 267  GLN   B HG2  1 
ATOM   13543 H  HG3  . GLN   B 1 267 ? 7.179  43.278  65.256 1.00 22.14 ? 267  GLN   B HG3  1 
ATOM   13544 H  HE21 . GLN   B 1 267 ? 4.165  43.862  65.073 1.00 21.34 ? 267  GLN   B HE21 1 
ATOM   13545 H  HE22 . GLN   B 1 267 ? 4.013  44.632  63.807 1.00 21.34 ? 267  GLN   B HE22 1 
ATOM   13546 N  N    . ALA   B 1 268 ? 5.853  38.275  63.409 1.00 17.19 ? 268  ALA   B N    1 
ATOM   13547 C  CA   . ALA   B 1 268 ? 6.461  36.988  62.988 1.00 16.05 ? 268  ALA   B CA   1 
ATOM   13548 C  C    . ALA   B 1 268 ? 6.402  36.785  61.468 1.00 14.50 ? 268  ALA   B C    1 
ATOM   13549 O  O    . ALA   B 1 268 ? 7.356  36.215  60.926 1.00 15.17 ? 268  ALA   B O    1 
ATOM   13550 C  CB   . ALA   B 1 268 ? 5.786  35.851  63.713 1.00 16.25 ? 268  ALA   B CB   1 
ATOM   13551 H  H    . ALA   B 1 268 ? 5.174  38.199  63.932 1.00 20.64 ? 268  ALA   B H    1 
ATOM   13552 H  HA   . ALA   B 1 268 ? 7.401  37.008  63.225 1.00 19.27 ? 268  ALA   B HA   1 
ATOM   13553 H  HB1  . ALA   B 1 268 ? 6.183  35.010  63.438 1.00 19.51 ? 268  ALA   B HB1  1 
ATOM   13554 H  HB2  . ALA   B 1 268 ? 5.900  35.964  64.670 1.00 19.51 ? 268  ALA   B HB2  1 
ATOM   13555 H  HB3  . ALA   B 1 268 ? 4.840  35.846  63.499 1.00 19.51 ? 268  ALA   B HB3  1 
ATOM   13556 N  N    . ASP   B 1 269 ? 5.328  37.217  60.805 1.00 15.07 ? 269  ASP   B N    1 
ATOM   13557 C  CA   . ASP   B 1 269 ? 5.194  36.928  59.350 1.00 17.10 ? 269  ASP   B CA   1 
ATOM   13558 C  C    . ASP   B 1 269 ? 6.361  37.542  58.568 1.00 19.56 ? 269  ASP   B C    1 
ATOM   13559 O  O    . ASP   B 1 269 ? 6.615  37.085  57.446 1.00 18.80 ? 269  ASP   B O    1 
ATOM   13560 C  CB   . ASP   B 1 269 ? 3.859  37.405  58.775 1.00 22.37 ? 269  ASP   B CB   1 
ATOM   13561 C  CG   . ASP   B 1 269 ? 3.629  36.888  57.365 1.00 28.51 ? 269  ASP   B CG   1 
ATOM   13562 O  OD1  . ASP   B 1 269 ? 3.915  35.700  57.123 1.00 24.23 ? 269  ASP   B OD1  1 
ATOM   13563 O  OD2  . ASP   B 1 269 ? 3.188  37.683  56.517 1.00 33.66 ? 269  ASP   B OD2  1 
ATOM   13564 H  H    . ASP   B 1 269 ? 4.681  37.664  61.153 1.00 18.08 ? 269  ASP   B H    1 
ATOM   13565 H  HA   . ASP   B 1 269 ? 5.217  35.963  59.253 1.00 20.53 ? 269  ASP   B HA   1 
ATOM   13566 H  HB2  . ASP   B 1 269 ? 3.136  37.108  59.349 1.00 26.85 ? 269  ASP   B HB2  1 
ATOM   13567 H  HB3  . ASP   B 1 269 ? 3.838  38.375  58.770 1.00 26.85 ? 269  ASP   B HB3  1 
ATOM   13568 N  N    . LYS   B 1 270 ? 7.030  38.535  59.149 1.00 14.05 ? 270  LYS   B N    1 
ATOM   13569 C  CA   . LYS   B 1 270 ? 8.138  39.219  58.433 1.00 17.07 ? 270  LYS   B CA   1 
ATOM   13570 C  C    . LYS   B 1 270 ? 9.320  38.260  58.267 1.00 15.50 ? 270  LYS   B C    1 
ATOM   13571 O  O    . LYS   B 1 270 ? 10.118 38.479  57.344 1.00 14.82 ? 270  LYS   B O    1 
ATOM   13572 C  CB   . LYS   B 1 270 ? 8.595  40.453  59.212 1.00 18.24 ? 270  LYS   B CB   1 
ATOM   13573 C  CG   . LYS   B 1 270 ? 7.555  41.556  59.348 1.00 17.00 ? 270  LYS   B CG   1 
ATOM   13574 C  CD   . LYS   B 1 270 ? 8.087  42.764  60.079 1.00 17.79 ? 270  LYS   B CD   1 
ATOM   13575 C  CE   . LYS   B 1 270 ? 9.254  43.409  59.364 1.00 17.53 ? 270  LYS   B CE   1 
ATOM   13576 N  NZ   . LYS   B 1 270 ? 9.572  44.743  59.924 1.00 18.91 ? 270  LYS   B NZ   1 
ATOM   13577 H  H    . LYS   B 1 270 ? 6.872  38.832  59.940 1.00 16.86 ? 270  LYS   B H    1 
ATOM   13578 H  HA   . LYS   B 1 270 ? 7.817  39.495  57.561 1.00 20.49 ? 270  LYS   B HA   1 
ATOM   13579 H  HB2  . LYS   B 1 270 ? 8.868  40.174  60.100 1.00 21.90 ? 270  LYS   B HB2  1 
ATOM   13580 H  HB3  . LYS   B 1 270 ? 9.380  40.820  58.776 1.00 21.90 ? 270  LYS   B HB3  1 
ATOM   13581 H  HG2  . LYS   B 1 270 ? 7.253  41.823  58.466 1.00 20.40 ? 270  LYS   B HG2  1 
ATOM   13582 H  HG3  . LYS   B 1 270 ? 6.781  41.211  59.820 1.00 20.40 ? 270  LYS   B HG3  1 
ATOM   13583 H  HD2  . LYS   B 1 270 ? 7.375  43.415  60.182 1.00 21.35 ? 270  LYS   B HD2  1 
ATOM   13584 H  HD3  . LYS   B 1 270 ? 8.363  42.502  60.971 1.00 21.35 ? 270  LYS   B HD3  1 
ATOM   13585 H  HE2  . LYS   B 1 270 ? 10.033 42.835  59.433 1.00 21.04 ? 270  LYS   B HE2  1 
ATOM   13586 H  HE3  . LYS   B 1 270 ? 9.048  43.495  58.420 1.00 21.04 ? 270  LYS   B HE3  1 
ATOM   13587 H  HZ1  . LYS   B 1 270 ? 10.430 44.930  59.778 1.00 22.69 ? 270  LYS   B HZ1  1 
ATOM   13588 H  HZ2  . LYS   B 1 270 ? 9.063  45.359  59.531 1.00 22.69 ? 270  LYS   B HZ2  1 
ATOM   13589 H  HZ3  . LYS   B 1 270 ? 9.414  44.743  60.800 1.00 22.69 ? 270  LYS   B HZ3  1 
ATOM   13590 N  N    . ILE   B 1 271 ? 9.432  37.264  59.150 1.00 16.33 ? 271  ILE   B N    1 
ATOM   13591 C  CA   . ILE   B 1 271 ? 10.605 36.337  59.100 1.00 14.64 ? 271  ILE   B CA   1 
ATOM   13592 C  C    . ILE   B 1 271 ? 10.100 34.912  58.841 1.00 15.98 ? 271  ILE   B C    1 
ATOM   13593 O  O    . ILE   B 1 271 ? 10.795 33.962  59.234 1.00 14.57 ? 271  ILE   B O    1 
ATOM   13594 C  CB   . ILE   B 1 271 ? 11.438 36.444  60.391 1.00 16.73 ? 271  ILE   B CB   1 
ATOM   13595 C  CG1  . ILE   B 1 271 ? 10.598 36.152  61.636 1.00 16.88 ? 271  ILE   B CG1  1 
ATOM   13596 C  CG2  . ILE   B 1 271 ? 12.115 37.804  60.475 1.00 16.97 ? 271  ILE   B CG2  1 
ATOM   13597 C  CD1  . ILE   B 1 271 ? 11.386 36.189  62.923 1.00 16.24 ? 271  ILE   B CD1  1 
ATOM   13598 H  H    . ILE   B 1 271 ? 8.864  37.099  59.775 1.00 19.60 ? 271  ILE   B H    1 
ATOM   13599 H  HA   . ILE   B 1 271 ? 11.197 36.585  58.373 1.00 17.58 ? 271  ILE   B HA   1 
ATOM   13600 H  HB   . ILE   B 1 271 ? 12.130 35.765  60.358 1.00 20.08 ? 271  ILE   B HB   1 
ATOM   13601 H  HG12 . ILE   B 1 271 ? 9.877  36.799  61.689 1.00 20.26 ? 271  ILE   B HG12 1 
ATOM   13602 H  HG13 . ILE   B 1 271 ? 10.188 35.278  61.542 1.00 20.26 ? 271  ILE   B HG13 1 
ATOM   13603 H  HG21 . ILE   B 1 271 ? 12.635 37.857  61.292 1.00 20.37 ? 271  ILE   B HG21 1 
ATOM   13604 H  HG22 . ILE   B 1 271 ? 12.701 37.922  59.711 1.00 20.37 ? 271  ILE   B HG22 1 
ATOM   13605 H  HG23 . ILE   B 1 271 ? 11.441 38.502  60.476 1.00 20.37 ? 271  ILE   B HG23 1 
ATOM   13606 H  HD11 . ILE   B 1 271 ? 10.797 35.996  63.669 1.00 19.49 ? 271  ILE   B HD11 1 
ATOM   13607 H  HD12 . ILE   B 1 271 ? 12.092 35.525  62.889 1.00 19.49 ? 271  ILE   B HD12 1 
ATOM   13608 H  HD13 . ILE   B 1 271 ? 11.776 37.070  63.039 1.00 19.49 ? 271  ILE   B HD13 1 
ATOM   13609 N  N    . SER   B 1 272 ? 8.950  34.791  58.182 1.00 16.02 ? 272  SER   B N    1 
ATOM   13610 C  CA   . SER   B 1 272 ? 8.361  33.466  57.869 1.00 15.21 ? 272  SER   B CA   1 
ATOM   13611 C  C    . SER   B 1 272 ? 9.007  32.834  56.633 1.00 14.96 ? 272  SER   B C    1 
ATOM   13612 O  O    . SER   B 1 272 ? 9.601  33.570  55.830 1.00 12.67 ? 272  SER   B O    1 
ATOM   13613 C  CB   . SER   B 1 272 ? 6.882  33.604  57.649 1.00 16.00 ? 272  SER   B CB   1 
ATOM   13614 O  OG   . SER   B 1 272 ? 6.613  34.327  56.461 1.00 18.35 ? 272  SER   B OG   1 
ATOM   13615 H  H    . SER   B 1 272 ? 8.486  35.459  57.902 1.00 19.23 ? 272  SER   B H    1 
ATOM   13616 H  HA   . SER   B 1 272 ? 8.530  32.883  58.626 1.00 18.26 ? 272  SER   B HA   1 
ATOM   13617 H  HB2  . SER   B 1 272 ? 6.476  32.725  57.596 1.00 19.21 ? 272  SER   B HB2  1 
ATOM   13618 H  HB3  . SER   B 1 272 ? 6.479  34.057  58.406 1.00 19.21 ? 272  SER   B HB3  1 
ATOM   13619 H  HG   . SER   B 1 272 ? 6.576  35.148  56.635 1.00 22.02 ? 272  SER   B HG   1 
ATOM   13620 N  N    . GLY   B 1 273 ? 8.860  31.514  56.486 1.00 17.99 ? 273  GLY   B N    1 
ATOM   13621 C  CA   . GLY   B 1 273 ? 9.364  30.838  55.276 1.00 16.11 ? 273  GLY   B CA   1 
ATOM   13622 C  C    . GLY   B 1 273 ? 8.581  31.304  54.062 1.00 15.37 ? 273  GLY   B C    1 
ATOM   13623 O  O    . GLY   B 1 273 ? 9.141  31.313  52.965 1.00 15.28 ? 273  GLY   B O    1 
ATOM   13624 H  H    . GLY   B 1 273 ? 8.480  30.998  57.060 1.00 21.59 ? 273  GLY   B H    1 
ATOM   13625 H  HA2  . GLY   B 1 273 ? 10.307 31.031  55.157 1.00 19.33 ? 273  GLY   B HA2  1 
ATOM   13626 H  HA3  . GLY   B 1 273 ? 9.282  29.877  55.375 1.00 19.33 ? 273  GLY   B HA3  1 
ATOM   13627 N  N    . GLU   B 1 274 ? 7.320  31.685  54.281 1.00 14.85 ? 274  GLU   B N    1 
ATOM   13628 C  CA   . GLU   B 1 274 ? 6.486  32.212  53.173 1.00 17.04 ? 274  GLU   B CA   1 
ATOM   13629 C  C    . GLU   B 1 274 ? 7.134  33.499  52.654 1.00 15.77 ? 274  GLU   B C    1 
ATOM   13630 O  O    . GLU   B 1 274 ? 7.270  33.642  51.430 1.00 15.52 ? 274  GLU   B O    1 
ATOM   13631 C  CB   . GLU   B 1 274 ? 5.065  32.446  53.679 1.00 16.99 ? 274  GLU   B CB   1 
ATOM   13632 C  CG   . GLU   B 1 274 ? 4.294  31.157  53.898 1.00 18.33 ? 274  GLU   B CG   1 
ATOM   13633 C  CD   . GLU   B 1 274 ? 4.339  30.607  55.313 1.00 20.18 ? 274  GLU   B CD   1 
ATOM   13634 O  OE1  . GLU   B 1 274 ? 5.168  31.083  56.108 1.00 17.63 ? 274  GLU   B OE1  1 
ATOM   13635 O  OE2  . GLU   B 1 274 ? 3.540  29.702  55.613 1.00 24.54 ? 274  GLU   B OE2  1 
ATOM   13636 H  H    . GLU   B 1 274 ? 6.927  31.651  55.045 1.00 17.82 ? 274  GLU   B H    1 
ATOM   13637 H  HA   . GLU   B 1 274 ? 6.432  31.579  52.440 1.00 20.45 ? 274  GLU   B HA   1 
ATOM   13638 H  HB2  . GLU   B 1 274 ? 5.101  32.941  54.512 1.00 20.39 ? 274  GLU   B HB2  1 
ATOM   13639 H  HB3  . GLU   B 1 274 ? 4.587  32.999  53.041 1.00 20.39 ? 274  GLU   B HB3  1 
ATOM   13640 H  HG2  . GLU   B 1 274 ? 3.367  31.306  53.654 1.00 22.00 ? 274  GLU   B HG2  1 
ATOM   13641 H  HG3  . GLU   B 1 274 ? 4.641  30.483  53.293 1.00 22.00 ? 274  GLU   B HG3  1 
ATOM   13642 N  N    . THR   B 1 275 ? 7.521  34.385  53.570 1.00 16.85 ? 275  THR   B N    1 
ATOM   13643 C  CA   . THR   B 1 275 ? 8.176  35.657  53.170 1.00 15.09 ? 275  THR   B CA   1 
ATOM   13644 C  C    . THR   B 1 275 ? 9.518  35.354  52.501 1.00 14.58 ? 275  THR   B C    1 
ATOM   13645 O  O    . THR   B 1 275 ? 9.815  35.966  51.468 1.00 18.16 ? 275  THR   B O    1 
ATOM   13646 C  CB   . THR   B 1 275 ? 8.364  36.578  54.377 1.00 15.67 ? 275  THR   B CB   1 
ATOM   13647 O  OG1  . THR   B 1 275 ? 7.062  36.894  54.868 1.00 16.59 ? 275  THR   B OG1  1 
ATOM   13648 C  CG2  . THR   B 1 275 ? 9.119  37.846  54.048 1.00 14.36 ? 275  THR   B CG2  1 
ATOM   13649 H  H    . THR   B 1 275 ? 7.421  34.282  54.418 1.00 20.23 ? 275  THR   B H    1 
ATOM   13650 H  HA   . THR   B 1 275 ? 7.605  36.119  52.536 1.00 18.11 ? 275  THR   B HA   1 
ATOM   13651 H  HB   . THR   B 1 275 ? 8.901  36.119  55.041 1.00 18.81 ? 275  THR   B HB   1 
ATOM   13652 H  HG1  . THR   B 1 275 ? 7.092  36.985  55.703 1.00 19.91 ? 275  THR   B HG1  1 
ATOM   13653 H  HG21 . THR   B 1 275 ? 9.207  38.387  54.848 1.00 17.24 ? 275  THR   B HG21 1 
ATOM   13654 H  HG22 . THR   B 1 275 ? 10.001 37.620  53.712 1.00 17.24 ? 275  THR   B HG22 1 
ATOM   13655 H  HG23 . THR   B 1 275 ? 8.634  38.345  53.372 1.00 17.24 ? 275  THR   B HG23 1 
ATOM   13656 N  N    . LEU   B 1 276 ? 10.298 34.446  53.093 1.00 14.01 ? 276  LEU   B N    1 
ATOM   13657 C  CA   . LEU   B 1 276 ? 11.640 34.141  52.527 1.00 14.03 ? 276  LEU   B CA   1 
ATOM   13658 C  C    . LEU   B 1 276 ? 11.455 33.589  51.111 1.00 13.22 ? 276  LEU   B C    1 
ATOM   13659 O  O    . LEU   B 1 276 ? 12.156 34.048  50.203 1.00 14.96 ? 276  LEU   B O    1 
ATOM   13660 C  CB   . LEU   B 1 276 ? 12.362 33.137  53.434 1.00 15.60 ? 276  LEU   B CB   1 
ATOM   13661 C  CG   . LEU   B 1 276 ? 13.758 32.720  52.976 1.00 16.60 ? 276  LEU   B CG   1 
ATOM   13662 C  CD1  . LEU   B 1 276 ? 14.750 33.859  53.155 1.00 15.13 ? 276  LEU   B CD1  1 
ATOM   13663 C  CD2  . LEU   B 1 276 ? 14.226 31.484  53.728 1.00 16.56 ? 276  LEU   B CD2  1 
ATOM   13664 H  H    . LEU   B 1 276 ? 10.088 34.003  53.800 1.00 16.82 ? 276  LEU   B H    1 
ATOM   13665 H  HA   . LEU   B 1 276 ? 12.185 34.942  52.481 1.00 16.83 ? 276  LEU   B HA   1 
ATOM   13666 H  HB2  . LEU   B 1 276 ? 12.431 33.520  54.323 1.00 18.73 ? 276  LEU   B HB2  1 
ATOM   13667 H  HB3  . LEU   B 1 276 ? 11.813 32.341  53.510 1.00 18.73 ? 276  LEU   B HB3  1 
ATOM   13668 H  HG   . LEU   B 1 276 ? 13.710 32.504  52.032 1.00 19.92 ? 276  LEU   B HG   1 
ATOM   13669 H  HD11 . LEU   B 1 276 ? 15.628 33.573  52.859 1.00 18.16 ? 276  LEU   B HD11 1 
ATOM   13670 H  HD12 . LEU   B 1 276 ? 14.465 34.623  52.629 1.00 18.16 ? 276  LEU   B HD12 1 
ATOM   13671 H  HD13 . LEU   B 1 276 ? 14.791 34.109  54.091 1.00 18.16 ? 276  LEU   B HD13 1 
ATOM   13672 H  HD21 . LEU   B 1 276 ? 15.113 31.236  53.423 1.00 19.87 ? 276  LEU   B HD21 1 
ATOM   13673 H  HD22 . LEU   B 1 276 ? 14.253 31.674  54.679 1.00 19.87 ? 276  LEU   B HD22 1 
ATOM   13674 H  HD23 . LEU   B 1 276 ? 13.611 30.752  53.562 1.00 19.87 ? 276  LEU   B HD23 1 
ATOM   13675 N  N    . THR   B 1 277 ? 10.508 32.670  50.944 1.00 17.44 ? 277  THR   B N    1 
ATOM   13676 C  CA   . THR   B 1 277 ? 10.256 32.059  49.614 1.00 17.93 ? 277  THR   B CA   1 
ATOM   13677 C  C    . THR   B 1 277 ? 9.842  33.151  48.619 1.00 18.20 ? 277  THR   B C    1 
ATOM   13678 O  O    . THR   B 1 277 ? 10.214 33.038  47.444 1.00 20.91 ? 277  THR   B O    1 
ATOM   13679 C  CB   . THR   B 1 277 ? 9.233  30.921  49.736 1.00 16.90 ? 277  THR   B CB   1 
ATOM   13680 O  OG1  . THR   B 1 277 ? 9.850  29.848  50.447 1.00 16.67 ? 277  THR   B OG1  1 
ATOM   13681 C  CG2  . THR   B 1 277 ? 8.730  30.425  48.398 1.00 19.60 ? 277  THR   B CG2  1 
ATOM   13682 H  H    . THR   B 1 277 ? 9.999  32.381  51.574 1.00 20.93 ? 277  THR   B H    1 
ATOM   13683 H  HA   . THR   B 1 277 ? 11.067 31.655  49.268 1.00 21.52 ? 277  THR   B HA   1 
ATOM   13684 H  HB   . THR   B 1 277 ? 8.457  31.263  50.207 1.00 20.28 ? 277  THR   B HB   1 
ATOM   13685 H  HG1  . THR   B 1 277 ? 9.668  29.120  50.069 1.00 20.00 ? 277  THR   B HG1  1 
ATOM   13686 H  HG21 . THR   B 1 277 ? 8.090  29.710  48.538 1.00 23.53 ? 277  THR   B HG21 1 
ATOM   13687 H  HG22 . THR   B 1 277 ? 8.301  31.154  47.923 1.00 23.53 ? 277  THR   B HG22 1 
ATOM   13688 H  HG23 . THR   B 1 277 ? 9.476  30.093  47.875 1.00 23.53 ? 277  THR   B HG23 1 
ATOM   13689 N  N    . ALA   B 1 278 ? 9.113  34.170  49.082 1.00 16.58 ? 278  ALA   B N    1 
ATOM   13690 C  CA   . ALA   B 1 278 ? 8.623  35.234  48.172 1.00 18.78 ? 278  ALA   B CA   1 
ATOM   13691 C  C    . ALA   B 1 278 ? 9.723  36.257  47.881 1.00 16.78 ? 278  ALA   B C    1 
ATOM   13692 O  O    . ALA   B 1 278 ? 9.522  37.068  46.962 1.00 22.04 ? 278  ALA   B O    1 
ATOM   13693 C  CB   . ALA   B 1 278 ? 7.435  35.932  48.782 1.00 20.39 ? 278  ALA   B CB   1 
ATOM   13694 H  H    . ALA   B 1 278 ? 8.889  34.271  49.906 1.00 19.89 ? 278  ALA   B H    1 
ATOM   13695 H  HA   . ALA   B 1 278 ? 8.360  34.816  47.337 1.00 22.54 ? 278  ALA   B HA   1 
ATOM   13696 H  HB1  . ALA   B 1 278 ? 7.122  36.625  48.180 1.00 24.48 ? 278  ALA   B HB1  1 
ATOM   13697 H  HB2  . ALA   B 1 278 ? 6.724  35.290  48.932 1.00 24.48 ? 278  ALA   B HB2  1 
ATOM   13698 H  HB3  . ALA   B 1 278 ? 7.693  36.331  49.628 1.00 24.48 ? 278  ALA   B HB3  1 
ATOM   13699 N  N    . ASN   B 1 279 ? 10.828 36.227  48.627 1.00 18.06 ? 279  ASN   B N    1 
ATOM   13700 C  CA   . ASN   B 1 279 ? 11.847 37.295  48.442 1.00 19.11 ? 279  ASN   B CA   1 
ATOM   13701 C  C    . ASN   B 1 279 ? 13.259 36.756  48.165 1.00 18.83 ? 279  ASN   B C    1 
ATOM   13702 O  O    . ASN   B 1 279 ? 13.628 36.690  46.982 1.00 20.98 ? 279  ASN   B O    1 
ATOM   13703 C  CB   . ASN   B 1 279 ? 11.849 38.252  49.636 1.00 18.96 ? 279  ASN   B CB   1 
ATOM   13704 C  CG   . ASN   B 1 279 ? 10.558 39.038  49.723 1.00 21.86 ? 279  ASN   B CG   1 
ATOM   13705 O  OD1  . ASN   B 1 279 ? 10.441 40.113  49.140 1.00 21.88 ? 279  ASN   B OD1  1 
ATOM   13706 N  ND2  . ASN   B 1 279 ? 9.572  38.499  50.421 1.00 20.93 ? 279  ASN   B ND2  1 
ATOM   13707 H  H    . ASN   B 1 279 ? 11.013 35.633  49.221 1.00 21.68 ? 279  ASN   B H    1 
ATOM   13708 H  HA   . ASN   B 1 279 ? 11.588 37.783  47.645 1.00 22.93 ? 279  ASN   B HA   1 
ATOM   13709 H  HB2  . ASN   B 1 279 ? 11.978 37.748  50.455 1.00 22.76 ? 279  ASN   B HB2  1 
ATOM   13710 H  HB3  . ASN   B 1 279 ? 12.597 38.865  49.559 1.00 22.76 ? 279  ASN   B HB3  1 
ATOM   13711 H  HD21 . ASN   B 1 279 ? 8.815  38.903  50.479 1.00 25.12 ? 279  ASN   B HD21 1 
ATOM   13712 H  HD22 . ASN   B 1 279 ? 9.688  37.744  50.817 1.00 25.12 ? 279  ASN   B HD22 1 
ATOM   13713 N  N    . GLN   B 1 280 ? 14.016 36.389  49.201 1.00 18.21 ? 280  GLN   B N    1 
ATOM   13714 C  CA   . GLN   B 1 280 ? 15.455 36.043  49.009 1.00 18.60 ? 280  GLN   B CA   1 
ATOM   13715 C  C    . GLN   B 1 280 ? 15.702 34.578  48.612 1.00 16.94 ? 280  GLN   B C    1 
ATOM   13716 O  O    . GLN   B 1 280 ? 16.856 34.266  48.285 1.00 15.57 ? 280  GLN   B O    1 
ATOM   13717 C  CB   . GLN   B 1 280 ? 16.229 36.409  50.277 1.00 18.44 ? 280  GLN   B CB   1 
ATOM   13718 C  CG   . GLN   B 1 280 ? 15.973 37.833  50.755 1.00 18.17 ? 280  GLN   B CG   1 
ATOM   13719 C  CD   . GLN   B 1 280 ? 14.864 37.937  51.776 1.00 20.17 ? 280  GLN   B CD   1 
ATOM   13720 O  OE1  . GLN   B 1 280 ? 13.929 37.141  51.792 1.00 16.98 ? 280  GLN   B OE1  1 
ATOM   13721 N  NE2  . GLN   B 1 280 ? 14.960 38.934  52.639 1.00 18.75 ? 280  GLN   B NE2  1 
ATOM   13722 H  H    . GLN   B 1 280 ? 13.735 36.331  50.012 1.00 21.86 ? 280  GLN   B H    1 
ATOM   13723 H  HA   . GLN   B 1 280 ? 15.776 36.562  48.255 1.00 22.33 ? 280  GLN   B HA   1 
ATOM   13724 H  HB2  . GLN   B 1 280 ? 15.989 35.790  50.984 1.00 22.13 ? 280  GLN   B HB2  1 
ATOM   13725 H  HB3  . GLN   B 1 280 ? 17.178 36.297  50.112 1.00 22.13 ? 280  GLN   B HB3  1 
ATOM   13726 H  HG2  . GLN   B 1 280 ? 16.790 38.190  51.138 1.00 21.81 ? 280  GLN   B HG2  1 
ATOM   13727 H  HG3  . GLN   B 1 280 ? 15.752 38.388  49.991 1.00 21.81 ? 280  GLN   B HG3  1 
ATOM   13728 H  HE21 . GLN   B 1 280 ? 15.628 39.474  52.600 1.00 22.51 ? 280  GLN   B HE21 1 
ATOM   13729 H  HE22 . GLN   B 1 280 ? 14.354 39.043  53.239 1.00 22.51 ? 280  GLN   B HE22 1 
ATOM   13730 N  N    . LEU   B 1 281 ? 14.684 33.724  48.625 1.00 16.68 ? 281  LEU   B N    1 
ATOM   13731 C  CA   . LEU   B 1 281 ? 14.973 32.303  48.315 1.00 14.46 ? 281  LEU   B CA   1 
ATOM   13732 C  C    . LEU   B 1 281 ? 15.374 32.171  46.835 1.00 17.50 ? 281  LEU   B C    1 
ATOM   13733 O  O    . LEU   B 1 281 ? 14.621 32.650  45.968 1.00 16.65 ? 281  LEU   B O    1 
ATOM   13734 C  CB   . LEU   B 1 281 ? 13.784 31.402  48.656 1.00 17.20 ? 281  LEU   B CB   1 
ATOM   13735 C  CG   . LEU   B 1 281 ? 14.033 29.912  48.446 1.00 15.69 ? 281  LEU   B CG   1 
ATOM   13736 C  CD1  . LEU   B 1 281 ? 14.941 29.367  49.534 1.00 15.53 ? 281  LEU   B CD1  1 
ATOM   13737 C  CD2  . LEU   B 1 281 ? 12.719 29.148  48.400 1.00 18.64 ? 281  LEU   B CD2  1 
ATOM   13738 H  H    . LEU   B 1 281 ? 13.864 33.917  48.798 1.00 20.02 ? 281  LEU   B H    1 
ATOM   13739 H  HA   . LEU   B 1 281 ? 15.714 32.007  48.867 1.00 17.36 ? 281  LEU   B HA   1 
ATOM   13740 H  HB2  . LEU   B 1 281 ? 13.538 31.549  49.583 1.00 20.64 ? 281  LEU   B HB2  1 
ATOM   13741 H  HB3  . LEU   B 1 281 ? 13.025 31.670  48.115 1.00 20.64 ? 281  LEU   B HB3  1 
ATOM   13742 H  HG   . LEU   B 1 281 ? 14.478 29.792  47.592 1.00 18.83 ? 281  LEU   B HG   1 
ATOM   13743 H  HD11 . LEU   B 1 281 ? 15.090 28.420  49.387 1.00 18.63 ? 281  LEU   B HD11 1 
ATOM   13744 H  HD12 . LEU   B 1 281 ? 15.790 29.835  49.511 1.00 18.63 ? 281  LEU   B HD12 1 
ATOM   13745 H  HD13 . LEU   B 1 281 ? 14.524 29.498  50.400 1.00 18.63 ? 281  LEU   B HD13 1 
ATOM   13746 H  HD21 . LEU   B 1 281 ? 12.898 28.204  48.266 1.00 22.37 ? 281  LEU   B HD21 1 
ATOM   13747 H  HD22 . LEU   B 1 281 ? 12.243 29.271  49.236 1.00 22.37 ? 281  LEU   B HD22 1 
ATOM   13748 H  HD23 . LEU   B 1 281 ? 12.176 29.481  47.668 1.00 22.37 ? 281  LEU   B HD23 1 
ATOM   13749 N  N    . VAL   B 1 282 ? 16.501 31.506  46.582 1.00 15.32 ? 282  VAL   B N    1 
ATOM   13750 C  CA   . VAL   B 1 282 ? 16.967 31.276  45.180 1.00 14.78 ? 282  VAL   B CA   1 
ATOM   13751 C  C    . VAL   B 1 282 ? 16.540 29.874  44.755 1.00 14.54 ? 282  VAL   B C    1 
ATOM   13752 O  O    . VAL   B 1 282 ? 16.028 29.717  43.651 1.00 15.82 ? 282  VAL   B O    1 
ATOM   13753 C  CB   . VAL   B 1 282 ? 18.491 31.437  45.112 1.00 13.94 ? 282  VAL   B CB   1 
ATOM   13754 C  CG1  . VAL   B 1 282 ? 19.050 30.992  43.770 1.00 16.47 ? 282  VAL   B CG1  1 
ATOM   13755 C  CG2  . VAL   B 1 282 ? 18.954 32.835  45.480 1.00 15.44 ? 282  VAL   B CG2  1 
ATOM   13756 H  H    . VAL   B 1 282 ? 17.015 31.178  47.189 1.00 18.39 ? 282  VAL   B H    1 
ATOM   13757 H  HA   . VAL   B 1 282 ? 16.572 31.924  44.576 1.00 17.74 ? 282  VAL   B HA   1 
ATOM   13758 H  HB   . VAL   B 1 282 ? 18.855 30.844  45.788 1.00 16.73 ? 282  VAL   B HB   1 
ATOM   13759 H  HG11 . VAL   B 1 282 ? 20.013 31.109  43.766 1.00 19.77 ? 282  VAL   B HG11 1 
ATOM   13760 H  HG12 . VAL   B 1 282 ? 18.837 30.057  43.625 1.00 19.77 ? 282  VAL   B HG12 1 
ATOM   13761 H  HG13 . VAL   B 1 282 ? 18.657 31.526  43.062 1.00 19.77 ? 282  VAL   B HG13 1 
ATOM   13762 H  HG21 . VAL   B 1 282 ? 19.921 32.882  45.421 1.00 18.54 ? 282  VAL   B HG21 1 
ATOM   13763 H  HG22 . VAL   B 1 282 ? 18.562 33.478  44.868 1.00 18.54 ? 282  VAL   B HG22 1 
ATOM   13764 H  HG23 . VAL   B 1 282 ? 18.676 33.040  46.386 1.00 18.54 ? 282  VAL   B HG23 1 
ATOM   13765 N  N    . ARG   B 1 283 ? 16.734 28.901  45.649 1.00 13.19 ? 283  ARG   B N    1 
ATOM   13766 C  CA   . ARG   B 1 283 ? 16.406 27.496  45.341 1.00 15.03 ? 283  ARG   B CA   1 
ATOM   13767 C  C    . ARG   B 1 283 ? 16.536 26.651  46.614 1.00 12.50 ? 283  ARG   B C    1 
ATOM   13768 O  O    . ARG   B 1 283 ? 16.961 27.174  47.623 1.00 15.05 ? 283  ARG   B O    1 
ATOM   13769 C  CB   . ARG   B 1 283 ? 17.365 26.927  44.286 1.00 15.32 ? 283  ARG   B CB   1 
ATOM   13770 C  CG   . ARG   B 1 283 ? 18.837 27.057  44.647 1.00 13.31 ? 283  ARG   B CG   1 
ATOM   13771 C  CD   . ARG   B 1 283 ? 19.660 25.974  43.976 1.00 15.76 ? 283  ARG   B CD   1 
ATOM   13772 N  NE   . ARG   B 1 283 ? 21.092 26.176  44.120 1.00 14.77 ? 283  ARG   B NE   1 
ATOM   13773 C  CZ   . ARG   B 1 283 ? 21.809 25.745  45.149 1.00 15.27 ? 283  ARG   B CZ   1 
ATOM   13774 N  NH1  . ARG   B 1 283 ? 21.224 25.077  46.126 1.00 14.50 ? 283  ARG   B NH1  1 
ATOM   13775 N  NH2  . ARG   B 1 283 ? 23.106 25.983  45.199 1.00 18.00 ? 283  ARG   B NH2  1 
ATOM   13776 H  H    . ARG   B 1 283 ? 17.053 29.028  46.437 1.00 15.83 ? 283  ARG   B H    1 
ATOM   13777 H  HA   . ARG   B 1 283 ? 15.499 27.466  44.999 1.00 18.03 ? 283  ARG   B HA   1 
ATOM   13778 H  HB2  . ARG   B 1 283 ? 17.158 25.990  44.147 1.00 18.39 ? 283  ARG   B HB2  1 
ATOM   13779 H  HB3  . ARG   B 1 283 ? 17.208 27.380  43.443 1.00 18.39 ? 283  ARG   B HB3  1 
ATOM   13780 H  HG2  . ARG   B 1 283 ? 19.164 27.930  44.377 1.00 15.98 ? 283  ARG   B HG2  1 
ATOM   13781 H  HG3  . ARG   B 1 283 ? 18.944 26.999  45.609 1.00 15.98 ? 283  ARG   B HG3  1 
ATOM   13782 H  HD2  . ARG   B 1 283 ? 19.421 25.113  44.353 1.00 18.92 ? 283  ARG   B HD2  1 
ATOM   13783 H  HD3  . ARG   B 1 283 ? 19.436 25.943  43.033 1.00 18.92 ? 283  ARG   B HD3  1 
ATOM   13784 H  HE   . ARG   B 1 283 ? 21.502 26.604  43.496 1.00 17.72 ? 283  ARG   B HE   1 
ATOM   13785 H  HH11 . ARG   B 1 283 ? 20.379 24.922  46.095 1.00 17.40 ? 283  ARG   B HH11 1 
ATOM   13786 H  HH12 . ARG   B 1 283 ? 21.688 24.797  46.794 1.00 17.40 ? 283  ARG   B HH12 1 
ATOM   13787 H  HH21 . ARG   B 1 283 ? 23.488 26.418  44.563 1.00 21.61 ? 283  ARG   B HH21 1 
ATOM   13788 H  HH22 . ARG   B 1 283 ? 23.569 25.703  45.867 1.00 21.61 ? 283  ARG   B HH22 1 
ATOM   13789 N  N    . LYS   B 1 284 ? 16.157 25.380  46.490 1.00 16.85 ? 284  LYS   B N    1 
ATOM   13790 C  CA   . LYS   B 1 284 ? 16.369 24.441  47.621 1.00 14.00 ? 284  LYS   B CA   1 
ATOM   13791 C  C    . LYS   B 1 284 ? 17.840 24.025  47.639 1.00 14.79 ? 284  LYS   B C    1 
ATOM   13792 O  O    . LYS   B 1 284 ? 18.530 24.286  46.637 1.00 13.73 ? 284  LYS   B O    1 
ATOM   13793 C  CB   . LYS   B 1 284 ? 15.473 23.211  47.464 1.00 16.11 ? 284  LYS   B CB   1 
ATOM   13794 C  CG   . LYS   B 1 284 ? 14.027 23.502  47.090 1.00 15.44 ? 284  LYS   B CG   1 
ATOM   13795 C  CD   . LYS   B 1 284 ? 13.117 22.307  47.262 1.00 25.29 ? 284  LYS   B CD   1 
ATOM   13796 C  CE   . LYS   B 1 284 ? 13.523 21.119  46.417 1.00 27.56 ? 284  LYS   B CE   1 
ATOM   13797 N  NZ   . LYS   B 1 284 ? 13.467 21.435  44.970 1.00 29.89 ? 284  LYS   B NZ   1 
ATOM   13798 H  H    . LYS   B 1 284 ? 15.788 25.040  45.792 1.00 20.22 ? 284  LYS   B H    1 
ATOM   13799 H  HA   . LYS   B 1 284 ? 16.140 24.876  48.457 1.00 16.81 ? 284  LYS   B HA   1 
ATOM   13800 H  HB2  . LYS   B 1 284 ? 15.857 22.634  46.785 1.00 19.34 ? 284  LYS   B HB2  1 
ATOM   13801 H  HB3  . LYS   B 1 284 ? 15.482 22.714  48.297 1.00 19.34 ? 284  LYS   B HB3  1 
ATOM   13802 H  HG2  . LYS   B 1 284 ? 13.698 24.233  47.636 1.00 18.53 ? 284  LYS   B HG2  1 
ATOM   13803 H  HG3  . LYS   B 1 284 ? 13.991 23.799  46.167 1.00 18.53 ? 284  LYS   B HG3  1 
ATOM   13804 H  HD2  . LYS   B 1 284 ? 13.111 22.045  48.196 1.00 30.35 ? 284  LYS   B HD2  1 
ATOM   13805 H  HD3  . LYS   B 1 284 ? 12.210 22.564  47.034 1.00 30.35 ? 284  LYS   B HD3  1 
ATOM   13806 H  HE2  . LYS   B 1 284 ? 14.422 20.844  46.654 1.00 33.08 ? 284  LYS   B HE2  1 
ATOM   13807 H  HE3  . LYS   B 1 284 ? 12.938 20.370  46.608 1.00 33.08 ? 284  LYS   B HE3  1 
ATOM   13808 H  HZ1  . LYS   B 1 284 ? 13.625 20.697  44.498 1.00 35.87 ? 284  LYS   B HZ1  1 
ATOM   13809 H  HZ2  . LYS   B 1 284 ? 12.660 21.750  44.766 1.00 35.87 ? 284  LYS   B HZ2  1 
ATOM   13810 H  HZ3  . LYS   B 1 284 ? 14.082 22.048  44.776 1.00 35.87 ? 284  LYS   B HZ3  1 
ATOM   13811 N  N    . ASN   B 1 285 ? 18.353 23.670  48.819 1.00 13.24 ? 285  ASN   B N    1 
ATOM   13812 C  CA   . ASN   B 1 285 ? 19.768 23.224  48.939 1.00 13.28 ? 285  ASN   B CA   1 
ATOM   13813 C  C    . ASN   B 1 285 ? 19.722 21.828  49.554 1.00 11.75 ? 285  ASN   B C    1 
ATOM   13814 O  O    . ASN   B 1 285 ? 20.052 21.689  50.739 1.00 12.86 ? 285  ASN   B O    1 
ATOM   13815 C  CB   . ASN   B 1 285 ? 20.595 24.224  49.745 1.00 14.58 ? 285  ASN   B CB   1 
ATOM   13816 C  CG   . ASN   B 1 285 ? 22.084 24.033  49.567 1.00 14.45 ? 285  ASN   B CG   1 
ATOM   13817 O  OD1  . ASN   B 1 285 ? 22.536 23.614  48.505 1.00 13.93 ? 285  ASN   B OD1  1 
ATOM   13818 N  ND2  . ASN   B 1 285 ? 22.850 24.338  50.601 1.00 14.03 ? 285  ASN   B ND2  1 
ATOM   13819 H  H    . ASN   B 1 285 ? 17.914 23.676  49.559 1.00 15.89 ? 285  ASN   B H    1 
ATOM   13820 H  HA   . ASN   B 1 285 ? 20.213 23.184  48.078 1.00 15.93 ? 285  ASN   B HA   1 
ATOM   13821 H  HB2  . ASN   B 1 285 ? 20.355 25.125  49.478 1.00 17.50 ? 285  ASN   B HB2  1 
ATOM   13822 H  HB3  . ASN   B 1 285 ? 20.372 24.138  50.685 1.00 17.50 ? 285  ASN   B HB3  1 
ATOM   13823 H  HD21 . ASN   B 1 285 ? 23.703 24.246  50.546 1.00 16.84 ? 285  ASN   B HD21 1 
ATOM   13824 H  HD22 . ASN   B 1 285 ? 22.495 24.629  51.328 1.00 16.84 ? 285  ASN   B HD22 1 
ATOM   13825 N  N    . PRO   B 1 286 ? 19.305 20.797  48.796 1.00 12.21 ? 286  PRO   B N    1 
ATOM   13826 C  CA   . PRO   B 1 286 ? 19.106 19.466  49.365 1.00 14.46 ? 286  PRO   B CA   1 
ATOM   13827 C  C    . PRO   B 1 286 ? 20.376 18.720  49.778 1.00 15.94 ? 286  PRO   B C    1 
ATOM   13828 O  O    . PRO   B 1 286 ? 21.390 18.860  49.130 1.00 15.05 ? 286  PRO   B O    1 
ATOM   13829 C  CB   . PRO   B 1 286 ? 18.457 18.658  48.227 1.00 18.09 ? 286  PRO   B CB   1 
ATOM   13830 C  CG   . PRO   B 1 286 ? 18.012 19.700  47.220 1.00 24.33 ? 286  PRO   B CG   1 
ATOM   13831 C  CD   . PRO   B 1 286 ? 18.989 20.846  47.371 1.00 16.44 ? 286  PRO   B CD   1 
ATOM   13832 H  HA   . PRO   B 1 286 ? 18.589 19.563  50.180 1.00 17.36 ? 286  PRO   B HA   1 
ATOM   13833 H  HB2  . PRO   B 1 286 ? 19.087 18.035  47.834 1.00 21.71 ? 286  PRO   B HB2  1 
ATOM   13834 H  HB3  . PRO   B 1 286 ? 17.706 18.136  48.549 1.00 21.71 ? 286  PRO   B HB3  1 
ATOM   13835 H  HG2  . PRO   B 1 286 ? 18.027 19.344  46.318 1.00 29.21 ? 286  PRO   B HG2  1 
ATOM   13836 H  HG3  . PRO   B 1 286 ? 17.103 19.990  47.395 1.00 29.21 ? 286  PRO   B HG3  1 
ATOM   13837 H  HD2  . PRO   B 1 286 ? 19.778 20.724  46.821 1.00 19.73 ? 286  PRO   B HD2  1 
ATOM   13838 H  HD3  . PRO   B 1 286 ? 18.594 21.695  47.116 1.00 19.73 ? 286  PRO   B HD3  1 
ATOM   13839 N  N    . CYS   B 1 287 ? 20.261 17.956  50.856 1.00 15.15 ? 287  CYS   B N    1 
ATOM   13840 C  CA   . CYS   B 1 287 ? 21.394 17.098  51.265 1.00 14.04 ? 287  CYS   B CA   1 
ATOM   13841 C  C    . CYS   B 1 287 ? 21.480 15.931  50.279 1.00 13.65 ? 287  CYS   B C    1 
ATOM   13842 O  O    . CYS   B 1 287 ? 20.658 15.867  49.360 1.00 15.09 ? 287  CYS   B O    1 
ATOM   13843 C  CB   . CYS   B 1 287 ? 21.159 16.536  52.658 1.00 13.41 ? 287  CYS   B CB   1 
ATOM   13844 S  SG   . CYS   B 1 287 ? 21.027 17.809  53.941 1.00 11.97 ? 287  CYS   B SG   1 
ATOM   13845 H  H    . CYS   B 1 287 ? 19.564 17.911  51.358 1.00 18.19 ? 287  CYS   B H    1 
ATOM   13846 H  HA   . CYS   B 1 287 ? 22.211 17.620  51.269 1.00 16.85 ? 287  CYS   B HA   1 
ATOM   13847 H  HB2  . CYS   B 1 287 ? 20.346 16.008  52.652 1.00 16.10 ? 287  CYS   B HB2  1 
ATOM   13848 H  HB3  . CYS   B 1 287 ? 21.886 15.935  52.883 1.00 16.10 ? 287  CYS   B HB3  1 
ATOM   13849 N  N    . TYR   B 1 288 ? 22.431 15.025  50.501 1.00 15.85 ? 288  TYR   B N    1 
ATOM   13850 C  CA   . TYR   B 1 288 ? 22.598 13.853  49.604 1.00 13.87 ? 288  TYR   B CA   1 
ATOM   13851 C  C    . TYR   B 1 288 ? 21.320 13.015  49.482 1.00 16.76 ? 288  TYR   B C    1 
ATOM   13852 O  O    . TYR   B 1 288 ? 20.705 12.710  50.516 1.00 16.32 ? 288  TYR   B O    1 
ATOM   13853 C  CB   . TYR   B 1 288 ? 23.729 12.957  50.110 1.00 16.43 ? 288  TYR   B CB   1 
ATOM   13854 C  CG   . TYR   B 1 288 ? 23.983 11.745  49.252 1.00 17.00 ? 288  TYR   B CG   1 
ATOM   13855 C  CD1  . TYR   B 1 288 ? 24.673 11.851  48.058 1.00 19.05 ? 288  TYR   B CD1  1 
ATOM   13856 C  CD2  . TYR   B 1 288 ? 23.521 10.494  49.625 1.00 19.08 ? 288  TYR   B CD2  1 
ATOM   13857 C  CE1  . TYR   B 1 288 ? 24.906 10.746  47.258 1.00 21.68 ? 288  TYR   B CE1  1 
ATOM   13858 C  CE2  . TYR   B 1 288 ? 23.746 9.378   48.838 1.00 20.25 ? 288  TYR   B CE2  1 
ATOM   13859 C  CZ   . TYR   B 1 288 ? 24.441 9.504   47.650 1.00 23.31 ? 288  TYR   B CZ   1 
ATOM   13860 O  OH   . TYR   B 1 288 ? 24.668 8.404   46.862 1.00 24.40 ? 288  TYR   B OH   1 
ATOM   13861 H  H    . TYR   B 1 288 ? 22.989 15.059  51.154 1.00 19.02 ? 288  TYR   B H    1 
ATOM   13862 H  HA   . TYR   B 1 288 ? 22.810 14.206  48.726 1.00 16.65 ? 288  TYR   B HA   1 
ATOM   13863 H  HB2  . TYR   B 1 288 ? 24.544 13.480  50.163 1.00 19.72 ? 288  TYR   B HB2  1 
ATOM   13864 H  HB3  . TYR   B 1 288 ? 23.519 12.665  51.011 1.00 19.72 ? 288  TYR   B HB3  1 
ATOM   13865 H  HD1  . TYR   B 1 288 ? 24.987 12.683  47.787 1.00 22.87 ? 288  TYR   B HD1  1 
ATOM   13866 H  HD2  . TYR   B 1 288 ? 23.049 10.402  50.421 1.00 22.90 ? 288  TYR   B HD2  1 
ATOM   13867 H  HE1  . TYR   B 1 288 ? 25.374 10.838  46.459 1.00 26.02 ? 288  TYR   B HE1  1 
ATOM   13868 H  HE2  . TYR   B 1 288 ? 23.430 8.546   49.108 1.00 24.31 ? 288  TYR   B HE2  1 
ATOM   13869 H  HH   . TYR   B 1 288 ? 25.241 8.592   46.277 1.00 29.29 ? 288  TYR   B HH   1 
ATOM   13870 N  N    . SER   B 1 289 ? 20.949 12.642  48.254 1.00 16.79 ? 289  SER   B N    1 
ATOM   13871 C  CA   . SER   B 1 289 ? 19.799 11.727  48.013 1.00 20.84 ? 289  SER   B CA   1 
ATOM   13872 C  C    . SER   B 1 289 ? 18.580 12.107  48.856 1.00 17.42 ? 289  SER   B C    1 
ATOM   13873 O  O    . SER   B 1 289 ? 18.032 11.226  49.530 1.00 19.13 ? 289  SER   B O    1 
ATOM   13874 C  CB   . SER   B 1 289 ? 20.198 10.293  48.244 1.00 26.41 ? 289  SER   B CB   1 
ATOM   13875 O  OG   . SER   B 1 289 ? 19.102 9.415   48.049 1.00 32.98 ? 289  SER   B OG   1 
ATOM   13876 H  H    . SER   B 1 289 ? 21.346 12.903  47.537 1.00 20.15 ? 289  SER   B H    1 
ATOM   13877 H  HA   . SER   B 1 289 ? 19.541 11.823  47.083 1.00 25.02 ? 289  SER   B HA   1 
ATOM   13878 H  HB2  . SER   B 1 289 ? 20.918 10.054  47.639 1.00 31.70 ? 289  SER   B HB2  1 
ATOM   13879 H  HB3  . SER   B 1 289 ? 20.540 10.192  49.146 1.00 31.70 ? 289  SER   B HB3  1 
ATOM   13880 H  HG   . SER   B 1 289 ? 18.516 9.564   48.632 1.00 39.57 ? 289  SER   B HG   1 
ATOM   13881 N  N    . CYS   B 1 290 ? 18.155 13.364  48.761 1.00 17.55 ? 290  CYS   B N    1 
ATOM   13882 C  CA   . CYS   B 1 290 ? 17.004 13.829  49.575 1.00 17.86 ? 290  CYS   B CA   1 
ATOM   13883 C  C    . CYS   B 1 290 ? 15.847 14.277  48.678 1.00 16.06 ? 290  CYS   B C    1 
ATOM   13884 O  O    . CYS   B 1 290 ? 16.032 15.230  47.913 1.00 15.45 ? 290  CYS   B O    1 
ATOM   13885 C  CB   . CYS   B 1 290 ? 17.409 14.998  50.457 1.00 16.47 ? 290  CYS   B CB   1 
ATOM   13886 S  SG   . CYS   B 1 290 ? 16.023 15.525  51.495 1.00 17.06 ? 290  CYS   B SG   1 
ATOM   13887 H  H    . CYS   B 1 290 ? 18.502 13.960  48.247 1.00 21.07 ? 290  CYS   B H    1 
ATOM   13888 H  HA   . CYS   B 1 290 ? 16.719 13.084  50.126 1.00 21.44 ? 290  CYS   B HA   1 
ATOM   13889 H  HB2  . CYS   B 1 290 ? 18.159 14.743  51.016 1.00 19.77 ? 290  CYS   B HB2  1 
ATOM   13890 H  HB3  . CYS   B 1 290 ? 17.706 15.738  49.905 1.00 19.77 ? 290  CYS   B HB3  1 
ATOM   13891 N  N    . PRO   B 1 291 ? 14.666 13.629  48.764 1.00 19.69 ? 291  PRO   B N    1 
ATOM   13892 C  CA   . PRO   B 1 291 ? 13.507 14.036  47.977 1.00 17.60 ? 291  PRO   B CA   1 
ATOM   13893 C  C    . PRO   B 1 291 ? 12.683 15.145  48.651 1.00 18.72 ? 291  PRO   B C    1 
ATOM   13894 O  O    . PRO   B 1 291 ? 11.719 15.575  48.067 1.00 19.65 ? 291  PRO   B O    1 
ATOM   13895 C  CB   . PRO   B 1 291 ? 12.693 12.736  47.923 1.00 20.32 ? 291  PRO   B CB   1 
ATOM   13896 C  CG   . PRO   B 1 291 ? 12.960 12.091  49.264 1.00 18.62 ? 291  PRO   B CG   1 
ATOM   13897 C  CD   . PRO   B 1 291 ? 14.396 12.449  49.589 1.00 21.74 ? 291  PRO   B CD   1 
ATOM   13898 H  HA   . PRO   B 1 291 ? 13.756 14.406  47.115 1.00 21.12 ? 291  PRO   B HA   1 
ATOM   13899 H  HB2  . PRO   B 1 291 ? 11.748 12.912  47.794 1.00 24.39 ? 291  PRO   B HB2  1 
ATOM   13900 H  HB3  . PRO   B 1 291 ? 12.978 12.167  47.191 1.00 24.39 ? 291  PRO   B HB3  1 
ATOM   13901 H  HG2  . PRO   B 1 291 ? 12.352 12.425  49.942 1.00 22.35 ? 291  PRO   B HG2  1 
ATOM   13902 H  HG3  . PRO   B 1 291 ? 12.838 11.130  49.222 1.00 22.35 ? 291  PRO   B HG3  1 
ATOM   13903 H  HD2  . PRO   B 1 291 ? 14.508 12.643  50.533 1.00 26.10 ? 291  PRO   B HD2  1 
ATOM   13904 H  HD3  . PRO   B 1 291 ? 15.000 11.721  49.375 1.00 26.10 ? 291  PRO   B HD3  1 
ATOM   13905 N  N    . ILE   B 1 292 ? 13.086 15.573  49.849 1.00 16.30 ? 292  ILE   B N    1 
ATOM   13906 C  CA   . ILE   B 1 292 ? 12.358 16.646  50.593 1.00 16.98 ? 292  ILE   B CA   1 
ATOM   13907 C  C    . ILE   B 1 292 ? 12.971 18.009  50.251 1.00 17.39 ? 292  ILE   B C    1 
ATOM   13908 O  O    . ILE   B 1 292 ? 12.213 18.910  49.878 1.00 18.01 ? 292  ILE   B O    1 
ATOM   13909 C  CB   . ILE   B 1 292 ? 12.385 16.356  52.108 1.00 17.48 ? 292  ILE   B CB   1 
ATOM   13910 C  CG1  . ILE   B 1 292 ? 11.827 14.966  52.421 1.00 20.93 ? 292  ILE   B CG1  1 
ATOM   13911 C  CG2  . ILE   B 1 292 ? 11.660 17.447  52.881 1.00 17.57 ? 292  ILE   B CG2  1 
ATOM   13912 C  CD1  . ILE   B 1 292 ? 11.938 14.573  53.876 1.00 19.10 ? 292  ILE   B CD1  1 
ATOM   13913 H  H    . ILE   B 1 292 ? 13.776 15.264  50.260 1.00 19.57 ? 292  ILE   B H    1 
ATOM   13914 H  HA   . ILE   B 1 292 ? 11.426 16.663  50.324 1.00 20.38 ? 292  ILE   B HA   1 
ATOM   13915 H  HB   . ILE   B 1 292 ? 13.311 16.359  52.398 1.00 20.98 ? 292  ILE   B HB   1 
ATOM   13916 H  HG12 . ILE   B 1 292 ? 10.894 14.935  52.157 1.00 25.12 ? 292  ILE   B HG12 1 
ATOM   13917 H  HG13 . ILE   B 1 292 ? 12.296 14.310  51.882 1.00 25.12 ? 292  ILE   B HG13 1 
ATOM   13918 H  HG21 . ILE   B 1 292 ? 11.689 17.246  53.829 1.00 21.09 ? 292  ILE   B HG21 1 
ATOM   13919 H  HG22 . ILE   B 1 292 ? 12.092 18.300  52.719 1.00 21.09 ? 292  ILE   B HG22 1 
ATOM   13920 H  HG23 . ILE   B 1 292 ? 10.736 17.492  52.588 1.00 21.09 ? 292  ILE   B HG23 1 
ATOM   13921 H  HD11 . ILE   B 1 292 ? 11.567 13.686  54.001 1.00 22.92 ? 292  ILE   B HD11 1 
ATOM   13922 H  HD12 . ILE   B 1 292 ? 12.871 14.573  54.141 1.00 22.92 ? 292  ILE   B HD12 1 
ATOM   13923 H  HD13 . ILE   B 1 292 ? 11.447 15.208  54.421 1.00 22.92 ? 292  ILE   B HD13 1 
ATOM   13924 N  N    . GLY   B 1 293 ? 14.290 18.150  50.377 1.00 14.74 ? 293  GLY   B N    1 
ATOM   13925 C  CA   . GLY   B 1 293 ? 14.959 19.406  49.983 1.00 16.11 ? 293  GLY   B CA   1 
ATOM   13926 C  C    . GLY   B 1 293 ? 14.538 20.604  50.824 1.00 13.43 ? 293  GLY   B C    1 
ATOM   13927 O  O    . GLY   B 1 293 ? 14.266 21.666  50.256 1.00 13.85 ? 293  GLY   B O    1 
ATOM   13928 H  H    . GLY   B 1 293 ? 14.816 17.543  50.684 1.00 17.70 ? 293  GLY   B H    1 
ATOM   13929 H  HA2  . GLY   B 1 293 ? 15.919 19.290  50.055 1.00 19.34 ? 293  GLY   B HA2  1 
ATOM   13930 H  HA3  . GLY   B 1 293 ? 14.765 19.589  49.050 1.00 19.34 ? 293  GLY   B HA3  1 
ATOM   13931 N  N    . CYS   B 1 294 ? 14.521 20.443  52.144 1.00 15.17 ? 294  CYS   B N    1 
ATOM   13932 C  CA   . CYS   B 1 294 ? 14.149 21.566  53.047 1.00 15.31 ? 294  CYS   B CA   1 
ATOM   13933 C  C    . CYS   B 1 294 ? 15.276 22.607  53.082 1.00 10.03 ? 294  CYS   B C    1 
ATOM   13934 O  O    . CYS   B 1 294 ? 14.999 23.764  53.426 1.00 13.06 ? 294  CYS   B O    1 
ATOM   13935 C  CB   . CYS   B 1 294 ? 13.816 21.063  54.448 1.00 15.64 ? 294  CYS   B CB   1 
ATOM   13936 S  SG   . CYS   B 1 294 ? 15.254 20.737  55.505 1.00 11.88 ? 294  CYS   B SG   1 
ATOM   13937 H  H    . CYS   B 1 294 ? 14.716 19.708  52.545 1.00 18.21 ? 294  CYS   B H    1 
ATOM   13938 H  HA   . CYS   B 1 294 ? 13.349 21.990  52.698 1.00 18.37 ? 294  CYS   B HA   1 
ATOM   13939 H  HB2  . CYS   B 1 294 ? 13.251 21.718  54.887 1.00 18.78 ? 294  CYS   B HB2  1 
ATOM   13940 H  HB3  . CYS   B 1 294 ? 13.297 20.247  54.370 1.00 18.78 ? 294  CYS   B HB3  1 
ATOM   13941 N  N    . GLY   B 1 295 ? 16.496 22.205  52.722 1.00 11.92 ? 295  GLY   B N    1 
ATOM   13942 C  CA   . GLY   B 1 295 ? 17.639 23.132  52.770 1.00 9.72  ? 295  GLY   B CA   1 
ATOM   13943 C  C    . GLY   B 1 295 ? 17.362 24.419  52.014 1.00 15.81 ? 295  GLY   B C    1 
ATOM   13944 O  O    . GLY   B 1 295 ? 16.677 24.358  50.983 1.00 14.21 ? 295  GLY   B O    1 
ATOM   13945 H  H    . GLY   B 1 295 ? 16.686 21.412  52.450 1.00 14.30 ? 295  GLY   B H    1 
ATOM   13946 H  HA2  . GLY   B 1 295 ? 17.847 23.340  53.694 1.00 11.67 ? 295  GLY   B HA2  1 
ATOM   13947 H  HA3  . GLY   B 1 295 ? 18.421 22.699  52.394 1.00 11.67 ? 295  GLY   B HA3  1 
ATOM   13948 N  N    . ARG   B 1 296 ? 17.914 25.535  52.492 1.00 11.22 ? 296  ARG   B N    1 
ATOM   13949 C  CA   . ARG   B 1 296 ? 17.609 26.842  51.859 1.00 12.31 ? 296  ARG   B CA   1 
ATOM   13950 C  C    . ARG   B 1 296 ? 18.850 27.429  51.182 1.00 14.65 ? 296  ARG   B C    1 
ATOM   13951 O  O    . ARG   B 1 296 ? 19.934 27.346  51.771 1.00 13.31 ? 296  ARG   B O    1 
ATOM   13952 C  CB   . ARG   B 1 296 ? 17.080 27.840  52.896 1.00 14.27 ? 296  ARG   B CB   1 
ATOM   13953 C  CG   . ARG   B 1 296 ? 15.849 27.374  53.658 1.00 13.77 ? 296  ARG   B CG   1 
ATOM   13954 C  CD   . ARG   B 1 296 ? 14.597 27.358  52.803 1.00 14.72 ? 296  ARG   B CD   1 
ATOM   13955 N  NE   . ARG   B 1 296 ? 14.458 26.103  52.082 1.00 11.69 ? 296  ARG   B NE   1 
ATOM   13956 C  CZ   . ARG   B 1 296 ? 13.477 25.820  51.236 1.00 16.25 ? 296  ARG   B CZ   1 
ATOM   13957 N  NH1  . ARG   B 1 296 ? 12.547 26.721  50.973 1.00 14.36 ? 296  ARG   B NH1  1 
ATOM   13958 N  NH2  . ARG   B 1 296 ? 13.431 24.634  50.655 1.00 14.95 ? 296  ARG   B NH2  1 
ATOM   13959 H  H    . ARG   B 1 296 ? 18.453 25.569  53.161 1.00 13.46 ? 296  ARG   B H    1 
ATOM   13960 H  HA   . ARG   B 1 296 ? 16.927 26.686  51.188 1.00 14.78 ? 296  ARG   B HA   1 
ATOM   13961 H  HB2  . ARG   B 1 296 ? 17.786 28.031  53.533 1.00 17.13 ? 296  ARG   B HB2  1 
ATOM   13962 H  HB3  . ARG   B 1 296 ? 16.871 28.674  52.447 1.00 17.13 ? 296  ARG   B HB3  1 
ATOM   13963 H  HG2  . ARG   B 1 296 ? 16.008 26.483  54.007 1.00 16.53 ? 296  ARG   B HG2  1 
ATOM   13964 H  HG3  . ARG   B 1 296 ? 15.707 27.956  54.421 1.00 16.53 ? 296  ARG   B HG3  1 
ATOM   13965 H  HD2  . ARG   B 1 296 ? 13.819 27.497  53.365 1.00 17.66 ? 296  ARG   B HD2  1 
ATOM   13966 H  HD3  . ARG   B 1 296 ? 14.626 28.094  52.171 1.00 17.66 ? 296  ARG   B HD3  1 
ATOM   13967 H  HE   . ARG   B 1 296 ? 15.056 25.500  52.214 1.00 14.03 ? 296  ARG   B HE   1 
ATOM   13968 H  HH11 . ARG   B 1 296 ? 12.577 27.493  51.351 1.00 17.24 ? 296  ARG   B HH11 1 
ATOM   13969 H  HH12 . ARG   B 1 296 ? 11.912 26.535  50.424 1.00 17.24 ? 296  ARG   B HH12 1 
ATOM   13970 H  HH21 . ARG   B 1 296 ? 14.036 24.048  50.826 1.00 17.95 ? 296  ARG   B HH21 1 
ATOM   13971 H  HH22 . ARG   B 1 296 ? 12.796 24.448  50.106 1.00 17.95 ? 296  ARG   B HH22 1 
ATOM   13972 N  N    . TRP   B 1 297 ? 18.677 27.981  49.981 1.00 13.95 ? 297  TRP   B N    1 
ATOM   13973 C  CA   . TRP   B 1 297 ? 19.774 28.704  49.292 1.00 13.36 ? 297  TRP   B CA   1 
ATOM   13974 C  C    . TRP   B 1 297 ? 19.240 30.122  49.093 1.00 17.67 ? 297  TRP   B C    1 
ATOM   13975 O  O    . TRP   B 1 297 ? 18.224 30.258  48.397 1.00 14.40 ? 297  TRP   B O    1 
ATOM   13976 C  CB   . TRP   B 1 297 ? 20.127 28.008  47.974 1.00 13.95 ? 297  TRP   B CB   1 
ATOM   13977 C  CG   . TRP   B 1 297 ? 21.392 28.500  47.345 1.00 14.65 ? 297  TRP   B CG   1 
ATOM   13978 C  CD1  . TRP   B 1 297 ? 21.515 29.224  46.194 1.00 15.03 ? 297  TRP   B CD1  1 
ATOM   13979 C  CD2  . TRP   B 1 297 ? 22.729 28.299  47.836 1.00 15.28 ? 297  TRP   B CD2  1 
ATOM   13980 N  NE1  . TRP   B 1 297 ? 22.834 29.485  45.936 1.00 15.98 ? 297  TRP   B NE1  1 
ATOM   13981 C  CE2  . TRP   B 1 297 ? 23.601 28.932  46.926 1.00 15.20 ? 297  TRP   B CE2  1 
ATOM   13982 C  CE3  . TRP   B 1 297 ? 23.270 27.645  48.947 1.00 18.18 ? 297  TRP   B CE3  1 
ATOM   13983 C  CZ2  . TRP   B 1 297 ? 24.983 28.930  47.100 1.00 18.54 ? 297  TRP   B CZ2  1 
ATOM   13984 C  CZ3  . TRP   B 1 297 ? 24.636 27.646  49.118 1.00 15.83 ? 297  TRP   B CZ3  1 
ATOM   13985 C  CH2  . TRP   B 1 297 ? 25.478 28.281  48.207 1.00 18.93 ? 297  TRP   B CH2  1 
ATOM   13986 H  H    . TRP   B 1 297 ? 17.938 27.954  49.542 1.00 16.75 ? 297  TRP   B H    1 
ATOM   13987 H  HA   . TRP   B 1 297 ? 20.601 28.717  49.799 1.00 16.04 ? 297  TRP   B HA   1 
ATOM   13988 H  HB2  . TRP   B 1 297 ? 20.206 27.054  48.134 1.00 16.75 ? 297  TRP   B HB2  1 
ATOM   13989 H  HB3  . TRP   B 1 297 ? 19.396 28.131  47.348 1.00 16.75 ? 297  TRP   B HB3  1 
ATOM   13990 H  HD1  . TRP   B 1 297 ? 20.804 29.500  45.661 1.00 18.03 ? 297  TRP   B HD1  1 
ATOM   13991 H  HE1  . TRP   B 1 297 ? 23.133 29.926  45.261 1.00 19.17 ? 297  TRP   B HE1  1 
ATOM   13992 H  HE3  . TRP   B 1 297 ? 22.717 27.217  49.560 1.00 21.82 ? 297  TRP   B HE3  1 
ATOM   13993 H  HZ2  . TRP   B 1 297 ? 25.548 29.350  46.492 1.00 22.25 ? 297  TRP   B HZ2  1 
ATOM   13994 H  HZ3  . TRP   B 1 297 ? 25.004 27.215  49.855 1.00 18.99 ? 297  TRP   B HZ3  1 
ATOM   13995 H  HH2  . TRP   B 1 297 ? 26.397 28.266  48.351 1.00 22.72 ? 297  TRP   B HH2  1 
ATOM   13996 N  N    . VAL   B 1 298 ? 19.885 31.125  49.691 1.00 12.73 ? 298  VAL   B N    1 
ATOM   13997 C  CA   . VAL   B 1 298 ? 19.285 32.489  49.671 1.00 16.28 ? 298  VAL   B CA   1 
ATOM   13998 C  C    . VAL   B 1 298 ? 20.196 33.522  49.009 1.00 15.14 ? 298  VAL   B C    1 
ATOM   13999 O  O    . VAL   B 1 298 ? 21.396 33.261  48.854 1.00 15.76 ? 298  VAL   B O    1 
ATOM   14000 C  CB   . VAL   B 1 298 ? 18.908 32.931  51.101 1.00 14.61 ? 298  VAL   B CB   1 
ATOM   14001 C  CG1  . VAL   B 1 298 ? 17.847 32.024  51.705 1.00 16.07 ? 298  VAL   B CG1  1 
ATOM   14002 C  CG2  . VAL   B 1 298 ? 20.121 33.030  52.012 1.00 13.88 ? 298  VAL   B CG2  1 
ATOM   14003 H  H    . VAL   B 1 298 ? 20.638 31.057  50.100 1.00 15.28 ? 298  VAL   B H    1 
ATOM   14004 H  HA   . VAL   B 1 298 ? 18.481 32.439  49.131 1.00 19.54 ? 298  VAL   B HA   1 
ATOM   14005 H  HB   . VAL   B 1 298 ? 18.532 33.822  51.025 1.00 17.53 ? 298  VAL   B HB   1 
ATOM   14006 H  HG11 . VAL   B 1 298 ? 17.633 32.328  52.601 1.00 19.28 ? 298  VAL   B HG11 1 
ATOM   14007 H  HG12 . VAL   B 1 298 ? 17.048 32.050  51.156 1.00 19.28 ? 298  VAL   B HG12 1 
ATOM   14008 H  HG13 . VAL   B 1 298 ? 18.182 31.115  51.744 1.00 19.28 ? 298  VAL   B HG13 1 
ATOM   14009 H  HG21 . VAL   B 1 298 ? 19.839 33.310  52.897 1.00 16.66 ? 298  VAL   B HG21 1 
ATOM   14010 H  HG22 . VAL   B 1 298 ? 20.554 32.164  52.070 1.00 16.66 ? 298  VAL   B HG22 1 
ATOM   14011 H  HG23 . VAL   B 1 298 ? 20.745 33.680  51.651 1.00 16.66 ? 298  VAL   B HG23 1 
ATOM   14012 N  N    . ARG   B 1 299 ? 19.606 34.668  48.661 1.00 17.91 ? 299  ARG   B N    1 
ATOM   14013 C  CA   . ARG   B 1 299 ? 20.379 35.758  48.015 1.00 14.65 ? 299  ARG   B CA   1 
ATOM   14014 C  C    . ARG   B 1 299 ? 20.646 36.863  49.036 1.00 17.48 ? 299  ARG   B C    1 
ATOM   14015 O  O    . ARG   B 1 299 ? 19.671 37.386  49.606 1.00 17.84 ? 299  ARG   B O    1 
ATOM   14016 C  CB   . ARG   B 1 299 ? 19.597 36.315  46.822 1.00 18.82 ? 299  ARG   B CB   1 
ATOM   14017 C  CG   . ARG   B 1 299 ? 20.375 37.288  45.949 1.00 18.58 ? 299  ARG   B CG   1 
ATOM   14018 C  CD   . ARG   B 1 299 ? 19.536 37.724  44.762 1.00 21.36 ? 299  ARG   B CD   1 
ATOM   14019 N  NE   . ARG   B 1 299 ? 19.168 36.610  43.899 1.00 20.28 ? 299  ARG   B NE   1 
ATOM   14020 C  CZ   . ARG   B 1 299 ? 17.934 36.140  43.753 1.00 20.94 ? 299  ARG   B CZ   1 
ATOM   14021 N  NH1  . ARG   B 1 299 ? 16.959 36.586  44.523 1.00 22.26 ? 299  ARG   B NH1  1 
ATOM   14022 N  NH2  . ARG   B 1 299 ? 17.681 35.219  42.839 1.00 20.98 ? 299  ARG   B NH2  1 
ATOM   14023 H  H    . ARG   B 1 299 ? 18.773 34.841  48.784 1.00 21.50 ? 299  ARG   B H    1 
ATOM   14024 H  HA   . ARG   B 1 299 ? 21.226 35.410  47.694 1.00 17.59 ? 299  ARG   B HA   1 
ATOM   14025 H  HB2  . ARG   B 1 299 ? 19.299 35.574  46.272 1.00 22.59 ? 299  ARG   B HB2  1 
ATOM   14026 H  HB3  . ARG   B 1 299 ? 18.802 36.761  47.152 1.00 22.59 ? 299  ARG   B HB3  1 
ATOM   14027 H  HG2  . ARG   B 1 299 ? 20.634 38.063  46.471 1.00 22.30 ? 299  ARG   B HG2  1 
ATOM   14028 H  HG3  . ARG   B 1 299 ? 21.193 36.869  45.638 1.00 22.30 ? 299  ARG   B HG3  1 
ATOM   14029 H  HD2  . ARG   B 1 299 ? 18.731 38.161  45.082 1.00 25.63 ? 299  ARG   B HD2  1 
ATOM   14030 H  HD3  . ARG   B 1 299 ? 20.029 38.380  44.245 1.00 25.63 ? 299  ARG   B HD3  1 
ATOM   14031 H  HE   . ARG   B 1 299 ? 19.795 36.229  43.451 1.00 24.34 ? 299  ARG   B HE   1 
ATOM   14032 H  HH11 . ARG   B 1 299 ? 17.122 37.182  45.121 1.00 26.71 ? 299  ARG   B HH11 1 
ATOM   14033 H  HH12 . ARG   B 1 299 ? 16.161 36.280  44.427 1.00 26.71 ? 299  ARG   B HH12 1 
ATOM   14034 H  HH21 . ARG   B 1 299 ? 18.315 34.924  42.339 1.00 25.18 ? 299  ARG   B HH21 1 
ATOM   14035 H  HH22 . ARG   B 1 299 ? 16.882 34.915  42.745 1.00 25.18 ? 299  ARG   B HH22 1 
ATOM   14036 N  N    . LEU   B 1 300 ? 21.914 37.184  49.266 1.00 16.88 ? 300  LEU   B N    1 
ATOM   14037 C  CA   . LEU   B 1 300 ? 22.257 38.316  50.160 1.00 17.33 ? 300  LEU   B CA   1 
ATOM   14038 C  C    . LEU   B 1 300 ? 21.949 39.619  49.414 1.00 20.11 ? 300  LEU   B C    1 
ATOM   14039 O  O    . LEU   B 1 300 ? 21.672 39.558  48.207 1.00 22.60 ? 300  LEU   B O    1 
ATOM   14040 C  CB   . LEU   B 1 300 ? 23.733 38.210  50.546 1.00 16.69 ? 300  LEU   B CB   1 
ATOM   14041 C  CG   . LEU   B 1 300 ? 24.102 36.940  51.309 1.00 19.35 ? 300  LEU   B CG   1 
ATOM   14042 C  CD1  . LEU   B 1 300 ? 25.602 36.853  51.536 1.00 23.12 ? 300  LEU   B CD1  1 
ATOM   14043 C  CD2  . LEU   B 1 300 ? 23.354 36.874  52.632 1.00 22.56 ? 300  LEU   B CD2  1 
ATOM   14044 H  H    . LEU   B 1 300 ? 22.589 36.774  48.926 1.00 20.26 ? 300  LEU   B H    1 
ATOM   14045 H  HA   . LEU   B 1 300 ? 21.736 38.299  50.978 1.00 20.80 ? 300  LEU   B HA   1 
ATOM   14046 H  HB2  . LEU   B 1 300 ? 24.270 38.256  49.739 1.00 20.03 ? 300  LEU   B HB2  1 
ATOM   14047 H  HB3  . LEU   B 1 300 ? 23.969 38.979  51.088 1.00 20.03 ? 300  LEU   B HB3  1 
ATOM   14048 H  HG   . LEU   B 1 300 ? 23.838 36.179  50.769 1.00 23.23 ? 300  LEU   B HG   1 
ATOM   14049 H  HD11 . LEU   B 1 300 ? 25.809 36.039  52.021 1.00 27.74 ? 300  LEU   B HD11 1 
ATOM   14050 H  HD12 . LEU   B 1 300 ? 26.059 36.844  50.680 1.00 27.74 ? 300  LEU   B HD12 1 
ATOM   14051 H  HD13 . LEU   B 1 300 ? 25.897 37.620  52.051 1.00 27.74 ? 300  LEU   B HD13 1 
ATOM   14052 H  HD21 . LEU   B 1 300 ? 23.600 36.062  53.103 1.00 27.07 ? 300  LEU   B HD21 1 
ATOM   14053 H  HD22 . LEU   B 1 300 ? 23.586 37.644  53.174 1.00 27.07 ? 300  LEU   B HD22 1 
ATOM   14054 H  HD23 . LEU   B 1 300 ? 22.399 36.873  52.464 1.00 27.07 ? 300  LEU   B HD23 1 
ATOM   14055 N  N    . LYS   B 1 301 ? 22.015 40.752  50.107 1.00 23.45 ? 301  LYS   B N    1 
ATOM   14056 C  CA   . LYS   B 1 301 ? 21.620 42.046  49.486 1.00 24.60 ? 301  LYS   B CA   1 
ATOM   14057 C  C    . LYS   B 1 301 ? 22.495 42.366  48.269 1.00 21.69 ? 301  LYS   B C    1 
ATOM   14058 O  O    . LYS   B 1 301 ? 21.989 43.053  47.362 1.00 24.85 ? 301  LYS   B O    1 
ATOM   14059 C  CB   . LYS   B 1 301 ? 21.705 43.159  50.533 1.00 30.74 ? 301  LYS   B CB   1 
ATOM   14060 C  CG   . LYS   B 1 301 ? 20.773 42.990  51.724 1.00 32.68 ? 301  LYS   B CG   1 
ATOM   14061 C  CD   . LYS   B 1 301 ? 20.987 44.029  52.801 1.00 41.89 ? 301  LYS   B CD   1 
ATOM   14062 C  CE   . LYS   B 1 301 ? 22.450 44.312  53.069 1.00 38.48 ? 301  LYS   B CE   1 
ATOM   14063 N  NZ   . LYS   B 1 301 ? 22.963 43.516  54.208 1.00 38.29 ? 301  LYS   B NZ   1 
ATOM   14064 H  H    . LYS   B 1 301 ? 22.279 40.808  50.924 1.00 28.14 ? 301  LYS   B H    1 
ATOM   14065 H  HA   . LYS   B 1 301 ? 20.705 41.977  49.171 1.00 29.52 ? 301  LYS   B HA   1 
ATOM   14066 H  HB2  . LYS   B 1 301 ? 22.618 43.211  50.858 1.00 36.89 ? 301  LYS   B HB2  1 
ATOM   14067 H  HB3  . LYS   B 1 301 ? 21.509 44.006  50.103 1.00 36.89 ? 301  LYS   B HB3  1 
ATOM   14068 H  HG2  . LYS   B 1 301 ? 19.854 43.036  51.417 1.00 39.21 ? 301  LYS   B HG2  1 
ATOM   14069 H  HG3  . LYS   B 1 301 ? 20.901 42.107  52.105 1.00 39.21 ? 301  LYS   B HG3  1 
ATOM   14070 H  HD2  . LYS   B 1 301 ? 20.546 44.853  52.541 1.00 50.27 ? 301  LYS   B HD2  1 
ATOM   14071 H  HD3  . LYS   B 1 301 ? 20.565 43.729  53.621 1.00 50.27 ? 301  LYS   B HD3  1 
ATOM   14072 H  HE2  . LYS   B 1 301 ? 22.969 44.112  52.274 1.00 46.17 ? 301  LYS   B HE2  1 
ATOM   14073 H  HE3  . LYS   B 1 301 ? 22.568 45.257  53.255 1.00 46.17 ? 301  LYS   B HE3  1 
ATOM   14074 H  HZ1  . LYS   B 1 301 ? 23.687 43.910  54.544 1.00 45.96 ? 301  LYS   B HZ1  1 
ATOM   14075 H  HZ2  . LYS   B 1 301 ? 22.337 43.461  54.838 1.00 45.96 ? 301  LYS   B HZ2  1 
ATOM   14076 H  HZ3  . LYS   B 1 301 ? 23.174 42.698  53.928 1.00 45.96 ? 301  LYS   B HZ3  1 
ATOM   14077 N  N    . ASP   B 1 302 ? 23.738 41.882  48.240 1.00 20.21 ? 302  ASP   B N    1 
ATOM   14078 C  CA   . ASP   B 1 302 ? 24.663 42.254  47.132 1.00 25.00 ? 302  ASP   B CA   1 
ATOM   14079 C  C    . ASP   B 1 302 ? 24.455 41.351  45.906 1.00 18.99 ? 302  ASP   B C    1 
ATOM   14080 O  O    . ASP   B 1 302 ? 25.149 41.561  44.903 1.00 19.60 ? 302  ASP   B O    1 
ATOM   14081 C  CB   . ASP   B 1 302 ? 26.117 42.253  47.609 1.00 24.37 ? 302  ASP   B CB   1 
ATOM   14082 C  CG   . ASP   B 1 302 ? 26.644 40.869  47.934 1.00 23.82 ? 302  ASP   B CG   1 
ATOM   14083 O  OD1  . ASP   B 1 302 ? 25.830 39.931  47.989 1.00 21.11 ? 302  ASP   B OD1  1 
ATOM   14084 O  OD2  . ASP   B 1 302 ? 27.864 40.748  48.132 1.00 26.90 ? 302  ASP   B OD2  1 
ATOM   14085 H  H    . ASP   B 1 302 ? 24.070 41.351  48.829 1.00 24.26 ? 302  ASP   B H    1 
ATOM   14086 H  HA   . ASP   B 1 302 ? 24.453 43.159  46.854 1.00 30.00 ? 302  ASP   B HA   1 
ATOM   14087 H  HB2  . ASP   B 1 302 ? 26.675 42.651  46.923 1.00 29.25 ? 302  ASP   B HB2  1 
ATOM   14088 H  HB3  . ASP   B 1 302 ? 26.192 42.814  48.397 1.00 29.25 ? 302  ASP   B HB3  1 
ATOM   14089 N  N    . GLY   B 1 303 ? 23.536 40.387  45.987 1.00 19.16 ? 303  GLY   B N    1 
ATOM   14090 C  CA   . GLY   B 1 303 ? 23.266 39.488  44.851 1.00 20.30 ? 303  GLY   B CA   1 
ATOM   14091 C  C    . GLY   B 1 303 ? 24.040 38.186  44.957 1.00 19.93 ? 303  GLY   B C    1 
ATOM   14092 O  O    . GLY   B 1 303 ? 23.722 37.260  44.197 1.00 18.39 ? 303  GLY   B O    1 
ATOM   14093 H  H    . GLY   B 1 303 ? 23.058 40.234  46.685 1.00 23.00 ? 303  GLY   B H    1 
ATOM   14094 H  HA2  . GLY   B 1 303 ? 22.316 39.296  44.811 1.00 24.37 ? 303  GLY   B HA2  1 
ATOM   14095 H  HA3  . GLY   B 1 303 ? 23.500 39.936  44.023 1.00 24.37 ? 303  GLY   B HA3  1 
ATOM   14096 N  N    . THR   B 1 304 ? 25.015 38.125  45.865 1.00 18.94 ? 304  THR   B N    1 
ATOM   14097 C  CA   . THR   B 1 304 ? 25.745 36.852  46.101 1.00 18.50 ? 304  THR   B CA   1 
ATOM   14098 C  C    . THR   B 1 304 ? 24.806 35.867  46.803 1.00 17.20 ? 304  THR   B C    1 
ATOM   14099 O  O    . THR   B 1 304 ? 23.786 36.321  47.351 1.00 18.44 ? 304  THR   B O    1 
ATOM   14100 C  CB   . THR   B 1 304 ? 27.033 37.065  46.909 1.00 19.47 ? 304  THR   B CB   1 
ATOM   14101 O  OG1  . THR   B 1 304 ? 26.713 37.604  48.191 1.00 21.26 ? 304  THR   B OG1  1 
ATOM   14102 C  CG2  . THR   B 1 304 ? 28.021 37.960  46.193 1.00 25.58 ? 304  THR   B CG2  1 
ATOM   14103 H  H    . THR   B 1 304 ? 25.272 38.787  46.350 1.00 22.73 ? 304  THR   B H    1 
ATOM   14104 H  HA   . THR   B 1 304 ? 26.020 36.487  45.245 1.00 22.21 ? 304  THR   B HA   1 
ATOM   14105 H  HB   . THR   B 1 304 ? 27.460 36.200  47.014 1.00 23.37 ? 304  THR   B HB   1 
ATOM   14106 H  HG1  . THR   B 1 304 ? 26.082 38.153  48.115 1.00 25.51 ? 304  THR   B HG1  1 
ATOM   14107 H  HG21 . THR   B 1 304 ? 28.816 38.066  46.738 1.00 30.70 ? 304  THR   B HG21 1 
ATOM   14108 H  HG22 . THR   B 1 304 ? 28.263 37.560  45.343 1.00 30.70 ? 304  THR   B HG22 1 
ATOM   14109 H  HG23 . THR   B 1 304 ? 27.618 38.828  46.038 1.00 30.70 ? 304  THR   B HG23 1 
ATOM   14110 N  N    . GLU   B 1 305 ? 25.158 34.582  46.805 1.00 14.88 ? 305  GLU   B N    1 
ATOM   14111 C  CA   . GLU   B 1 305 ? 24.245 33.553  47.366 1.00 16.51 ? 305  GLU   B CA   1 
ATOM   14112 C  C    . GLU   B 1 305 ? 24.977 32.709  48.415 1.00 16.46 ? 305  GLU   B C    1 
ATOM   14113 O  O    . GLU   B 1 305 ? 26.208 32.621  48.350 1.00 15.46 ? 305  GLU   B O    1 
ATOM   14114 C  CB   . GLU   B 1 305 ? 23.705 32.692  46.223 1.00 13.17 ? 305  GLU   B CB   1 
ATOM   14115 C  CG   . GLU   B 1 305 ? 23.064 33.519  45.123 1.00 16.21 ? 305  GLU   B CG   1 
ATOM   14116 C  CD   . GLU   B 1 305 ? 22.642 32.761  43.876 1.00 15.61 ? 305  GLU   B CD   1 
ATOM   14117 O  OE1  . GLU   B 1 305 ? 22.918 31.552  43.801 1.00 18.20 ? 305  GLU   B OE1  1 
ATOM   14118 O  OE2  . GLU   B 1 305 ? 22.038 33.387  42.985 1.00 18.62 ? 305  GLU   B OE2  1 
ATOM   14119 H  H    . GLU   B 1 305 ? 25.901 34.279  46.496 1.00 17.86 ? 305  GLU   B H    1 
ATOM   14120 H  HA   . GLU   B 1 305 ? 23.497 33.979  47.812 1.00 19.82 ? 305  GLU   B HA   1 
ATOM   14121 H  HB2  . GLU   B 1 305 ? 24.429 32.167  45.848 1.00 15.81 ? 305  GLU   B HB2  1 
ATOM   14122 H  HB3  . GLU   B 1 305 ? 23.053 32.066  46.574 1.00 15.81 ? 305  GLU   B HB3  1 
ATOM   14123 H  HG2  . GLU   B 1 305 ? 22.283 33.962  45.490 1.00 19.45 ? 305  GLU   B HG2  1 
ATOM   14124 H  HG3  . GLU   B 1 305 ? 23.688 34.214  44.861 1.00 19.45 ? 305  GLU   B HG3  1 
ATOM   14125 N  N    . CYS   B 1 306 ? 24.213 32.112  49.334 1.00 12.05 ? 306  CYS   B N    1 
ATOM   14126 C  CA   . CYS   B 1 306 ? 24.816 31.246  50.379 1.00 15.85 ? 306  CYS   B CA   1 
ATOM   14127 C  C    . CYS   B 1 306 ? 23.725 30.410  51.060 1.00 16.15 ? 306  CYS   B C    1 
ATOM   14128 O  O    . CYS   B 1 306 ? 22.539 30.582  50.725 1.00 13.97 ? 306  CYS   B O    1 
ATOM   14129 C  CB   . CYS   B 1 306 ? 25.555 32.091  51.407 1.00 13.09 ? 306  CYS   B CB   1 
ATOM   14130 S  SG   . CYS   B 1 306 ? 24.457 33.207  52.319 1.00 16.97 ? 306  CYS   B SG   1 
ATOM   14131 H  H    . CYS   B 1 306 ? 23.357 32.188  49.378 1.00 14.46 ? 306  CYS   B H    1 
ATOM   14132 H  HA   . CYS   B 1 306 ? 25.454 30.647  49.960 1.00 19.02 ? 306  CYS   B HA   1 
ATOM   14133 H  HB2  . CYS   B 1 306 ? 26.009 31.506  52.034 1.00 15.72 ? 306  CYS   B HB2  1 
ATOM   14134 H  HB3  . CYS   B 1 306 ? 26.240 32.612  50.959 1.00 15.72 ? 306  CYS   B HB3  1 
ATOM   14135 H  HG   . CYS   B 1 306 ? 25.098 33.840  53.111 1.00 20.37 ? 306  CYS   B HG   1 
ATOM   14136 N  N    . GLY   B 1 307 ? 24.130 29.510  51.959 1.00 11.02 ? 307  GLY   B N    1 
ATOM   14137 C  CA   . GLY   B 1 307 ? 23.145 28.708  52.702 1.00 11.95 ? 307  GLY   B CA   1 
ATOM   14138 C  C    . GLY   B 1 307 ? 22.200 29.604  53.483 1.00 13.36 ? 307  GLY   B C    1 
ATOM   14139 O  O    . GLY   B 1 307 ? 22.688 30.531  54.145 1.00 12.50 ? 307  GLY   B O    1 
ATOM   14140 H  H    . GLY   B 1 307 ? 24.952 29.348  52.153 1.00 13.22 ? 307  GLY   B H    1 
ATOM   14141 H  HA2  . GLY   B 1 307 ? 22.639 28.157  52.085 1.00 14.35 ? 307  GLY   B HA2  1 
ATOM   14142 H  HA3  . GLY   B 1 307 ? 23.603 28.106  53.309 1.00 14.35 ? 307  GLY   B HA3  1 
ATOM   14143 N  N    . GLY   B 1 308 ? 20.904 29.294  53.434 1.00 12.34 ? 308  GLY   B N    1 
ATOM   14144 C  CA   . GLY   B 1 308 ? 19.896 30.130  54.109 1.00 13.55 ? 308  GLY   B CA   1 
ATOM   14145 C  C    . GLY   B 1 308 ? 19.604 29.680  55.526 1.00 14.77 ? 308  GLY   B C    1 
ATOM   14146 O  O    . GLY   B 1 308 ? 20.116 28.631  55.939 1.00 12.93 ? 308  GLY   B O    1 
ATOM   14147 H  H    . GLY   B 1 308 ? 20.585 28.611  53.020 1.00 14.81 ? 308  GLY   B H    1 
ATOM   14148 H  HA2  . GLY   B 1 308 ? 20.204 31.050  54.124 1.00 16.27 ? 308  GLY   B HA2  1 
ATOM   14149 H  HA3  . GLY   B 1 308 ? 19.074 30.115  53.595 1.00 16.27 ? 308  GLY   B HA3  1 
ATOM   14150 N  N    . PRO   B 1 309 ? 18.779 30.434  56.283 1.00 13.67 ? 309  PRO   B N    1 
ATOM   14151 C  CA   . PRO   B 1 309 ? 18.539 30.126  57.689 1.00 14.65 ? 309  PRO   B CA   1 
ATOM   14152 C  C    . PRO   B 1 309 ? 17.427 29.115  57.979 1.00 14.33 ? 309  PRO   B C    1 
ATOM   14153 O  O    . PRO   B 1 309 ? 16.450 29.078  57.265 1.00 12.11 ? 309  PRO   B O    1 
ATOM   14154 C  CB   . PRO   B 1 309 ? 18.114 31.494  58.246 1.00 15.13 ? 309  PRO   B CB   1 
ATOM   14155 C  CG   . PRO   B 1 309 ? 17.391 32.148  57.090 1.00 14.20 ? 309  PRO   B CG   1 
ATOM   14156 C  CD   . PRO   B 1 309 ? 18.090 31.648  55.842 1.00 13.01 ? 309  PRO   B CD   1 
ATOM   14157 H  HA   . PRO   B 1 309 ? 19.327 29.712  58.076 1.00 17.59 ? 309  PRO   B HA   1 
ATOM   14158 H  HB2  . PRO   B 1 309 ? 17.536 31.399  59.019 1.00 18.16 ? 309  PRO   B HB2  1 
ATOM   14159 H  HB3  . PRO   B 1 309 ? 18.881 32.017  58.528 1.00 18.16 ? 309  PRO   B HB3  1 
ATOM   14160 H  HG2  . PRO   B 1 309 ? 16.451 31.907  57.084 1.00 17.04 ? 309  PRO   B HG2  1 
ATOM   14161 H  HG3  . PRO   B 1 309 ? 17.436 33.115  57.152 1.00 17.04 ? 309  PRO   B HG3  1 
ATOM   14162 H  HD2  . PRO   B 1 309 ? 17.457 31.459  55.132 1.00 15.62 ? 309  PRO   B HD2  1 
ATOM   14163 H  HD3  . PRO   B 1 309 ? 18.714 32.305  55.497 1.00 15.62 ? 309  PRO   B HD3  1 
ATOM   14164 N  N    . GLU   B 1 310 ? 17.640 28.310  59.019 1.00 14.08 ? 310  GLU   B N    1 
ATOM   14165 C  CA   . GLU   B 1 310 ? 16.590 27.361  59.460 1.00 12.46 ? 310  GLU   B CA   1 
ATOM   14166 C  C    . GLU   B 1 310 ? 15.662 28.097  60.431 1.00 10.05 ? 310  GLU   B C    1 
ATOM   14167 O  O    . GLU   B 1 310 ? 16.021 29.198  60.875 1.00 12.71 ? 310  GLU   B O    1 
ATOM   14168 C  CB   . GLU   B 1 310 ? 17.215 26.173  60.188 1.00 13.33 ? 310  GLU   B CB   1 
ATOM   14169 C  CG   . GLU   B 1 310 ? 18.347 25.526  59.415 1.00 10.17 ? 310  GLU   B CG   1 
ATOM   14170 C  CD   . GLU   B 1 310 ? 17.889 24.686  58.236 1.00 11.98 ? 310  GLU   B CD   1 
ATOM   14171 O  OE1  . GLU   B 1 310 ? 16.668 24.547  58.052 1.00 11.51 ? 310  GLU   B OE1  1 
ATOM   14172 O  OE2  . GLU   B 1 310 ? 18.757 24.169  57.510 1.00 14.94 ? 310  GLU   B OE2  1 
ATOM   14173 H  H    . GLU   B 1 310 ? 18.366 28.289  59.480 1.00 16.90 ? 310  GLU   B H    1 
ATOM   14174 H  HA   . GLU   B 1 310 ? 16.103 27.035  58.687 1.00 14.96 ? 310  GLU   B HA   1 
ATOM   14175 H  HB2  . GLU   B 1 310 ? 17.547 26.468  61.050 1.00 16.00 ? 310  GLU   B HB2  1 
ATOM   14176 H  HB3  . GLU   B 1 310 ? 16.529 25.510  60.361 1.00 16.00 ? 310  GLU   B HB3  1 
ATOM   14177 H  HG2  . GLU   B 1 310 ? 18.944 26.219  59.094 1.00 12.20 ? 310  GLU   B HG2  1 
ATOM   14178 H  HG3  . GLU   B 1 310 ? 18.860 24.967  60.019 1.00 12.20 ? 310  GLU   B HG3  1 
ATOM   14179 N  N    . TYR   B 1 311 ? 14.534 27.474  60.760 1.00 11.29 ? 311  TYR   B N    1 
ATOM   14180 C  CA   . TYR   B 1 311 ? 13.561 28.078  61.708 1.00 12.01 ? 311  TYR   B CA   1 
ATOM   14181 C  C    . TYR   B 1 311 ? 14.234 28.553  63.002 1.00 11.41 ? 311  TYR   B C    1 
ATOM   14182 O  O    . TYR   B 1 311 ? 14.022 29.704  63.400 1.00 12.18 ? 311  TYR   B O    1 
ATOM   14183 C  CB   . TYR   B 1 311 ? 12.463 27.066  62.037 1.00 11.41 ? 311  TYR   B CB   1 
ATOM   14184 C  CG   . TYR   B 1 311 ? 11.579 27.489  63.182 1.00 12.07 ? 311  TYR   B CG   1 
ATOM   14185 C  CD1  . TYR   B 1 311 ? 10.899 28.694  63.144 1.00 12.98 ? 311  TYR   B CD1  1 
ATOM   14186 C  CD2  . TYR   B 1 311 ? 11.444 26.704  64.314 1.00 12.54 ? 311  TYR   B CD2  1 
ATOM   14187 C  CE1  . TYR   B 1 311 ? 10.096 29.103  64.195 1.00 12.16 ? 311  TYR   B CE1  1 
ATOM   14188 C  CE2  . TYR   B 1 311 ? 10.644 27.097  65.373 1.00 12.84 ? 311  TYR   B CE2  1 
ATOM   14189 C  CZ   . TYR   B 1 311 ? 9.970  28.303  65.314 1.00 13.00 ? 311  TYR   B CZ   1 
ATOM   14190 O  OH   . TYR   B 1 311 ? 9.179  28.709  66.359 1.00 12.63 ? 311  TYR   B OH   1 
ATOM   14191 H  H    . TYR   B 1 311 ? 14.303 26.704  60.454 1.00 13.55 ? 311  TYR   B H    1 
ATOM   14192 H  HA   . TYR   B 1 311 ? 13.176 28.856  61.276 1.00 14.42 ? 311  TYR   B HA   1 
ATOM   14193 H  HB2  . TYR   B 1 311 ? 11.915 26.927  61.249 1.00 13.70 ? 311  TYR   B HB2  1 
ATOM   14194 H  HB3  . TYR   B 1 311 ? 12.873 26.213  62.252 1.00 13.70 ? 311  TYR   B HB3  1 
ATOM   14195 H  HD1  . TYR   B 1 311 ? 10.983 29.241  62.396 1.00 15.57 ? 311  TYR   B HD1  1 
ATOM   14196 H  HD2  . TYR   B 1 311 ? 11.901 25.895  64.364 1.00 15.05 ? 311  TYR   B HD2  1 
ATOM   14197 H  HE1  . TYR   B 1 311 ? 9.643  29.914  64.148 1.00 14.60 ? 311  TYR   B HE1  1 
ATOM   14198 H  HE2  . TYR   B 1 311 ? 10.560 26.552  66.122 1.00 15.41 ? 311  TYR   B HE2  1 
ATOM   14199 H  HH   . TYR   B 1 311 ? 9.467  28.376  67.075 1.00 15.16 ? 311  TYR   B HH   1 
ATOM   14200 N  N    . GLU   B 1 312 ? 15.008 27.688  63.661 1.00 12.66 ? 312  GLU   B N    1 
ATOM   14201 C  CA   . GLU   B 1 312 ? 15.577 28.088  64.979 1.00 12.76 ? 312  GLU   B CA   1 
ATOM   14202 C  C    . GLU   B 1 312 ? 16.478 29.316  64.811 1.00 11.84 ? 312  GLU   B C    1 
ATOM   14203 O  O    . GLU   B 1 312 ? 16.580 30.096  65.767 1.00 11.53 ? 312  GLU   B O    1 
ATOM   14204 C  CB   . GLU   B 1 312 ? 16.345 26.945  65.648 1.00 11.91 ? 312  GLU   B CB   1 
ATOM   14205 C  CG   . GLU   B 1 312 ? 15.711 25.579  65.444 1.00 12.23 ? 312  GLU   B CG   1 
ATOM   14206 C  CD   . GLU   B 1 312 ? 14.365 25.356  66.112 1.00 15.29 ? 312  GLU   B CD   1 
ATOM   14207 O  OE1  . GLU   B 1 312 ? 14.112 25.985  67.151 1.00 14.98 ? 312  GLU   B OE1  1 
ATOM   14208 O  OE2  . GLU   B 1 312 ? 13.578 24.547  65.590 1.00 15.09 ? 312  GLU   B OE2  1 
ATOM   14209 H  H    . GLU   B 1 312 ? 15.215 26.899  63.389 1.00 15.20 ? 312  GLU   B H    1 
ATOM   14210 H  HA   . GLU   B 1 312 ? 14.835 28.312  65.563 1.00 15.32 ? 312  GLU   B HA   1 
ATOM   14211 H  HB2  . GLU   B 1 312 ? 17.250 26.927  65.300 1.00 14.30 ? 312  GLU   B HB2  1 
ATOM   14212 H  HB3  . GLU   B 1 312 ? 16.410 27.123  66.599 1.00 14.30 ? 312  GLU   B HB3  1 
ATOM   14213 H  HG2  . GLU   B 1 312 ? 15.606 25.431  64.491 1.00 14.68 ? 312  GLU   B HG2  1 
ATOM   14214 H  HG3  . GLU   B 1 312 ? 16.328 24.905  65.770 1.00 14.68 ? 312  GLU   B HG3  1 
ATOM   14215 N  N    . THR   B 1 313 ? 17.101 29.457  63.639 1.00 10.96 ? 313  THR   B N    1 
ATOM   14216 C  CA   . THR   B 1 313 ? 18.012 30.604  63.379 1.00 14.75 ? 313  THR   B CA   1 
ATOM   14217 C  C    . THR   B 1 313 ? 17.177 31.868  63.140 1.00 13.51 ? 313  THR   B C    1 
ATOM   14218 O  O    . THR   B 1 313 ? 17.543 32.928  63.669 1.00 14.08 ? 313  THR   B O    1 
ATOM   14219 C  CB   . THR   B 1 313 ? 18.950 30.294  62.207 1.00 14.10 ? 313  THR   B CB   1 
ATOM   14220 O  OG1  . THR   B 1 313 ? 19.674 29.106  62.532 1.00 13.25 ? 313  THR   B OG1  1 
ATOM   14221 C  CG2  . THR   B 1 313 ? 19.910 31.422  61.903 1.00 12.74 ? 313  THR   B CG2  1 
ATOM   14222 H  H    . THR   B 1 313 ? 17.018 28.911  62.980 1.00 13.16 ? 313  THR   B H    1 
ATOM   14223 H  HA   . THR   B 1 313 ? 18.577 30.759  64.152 1.00 17.70 ? 313  THR   B HA   1 
ATOM   14224 H  HB   . THR   B 1 313 ? 18.414 30.176  61.407 1.00 16.93 ? 313  THR   B HB   1 
ATOM   14225 H  HG1  . THR   B 1 313 ? 19.926 28.729  61.825 1.00 15.91 ? 313  THR   B HG1  1 
ATOM   14226 H  HG21 . THR   B 1 313 ? 20.477 31.172  61.156 1.00 15.29 ? 313  THR   B HG21 1 
ATOM   14227 H  HG22 . THR   B 1 313 ? 19.409 32.221  61.675 1.00 15.29 ? 313  THR   B HG22 1 
ATOM   14228 H  HG23 . THR   B 1 313 ? 20.461 31.597  62.682 1.00 15.29 ? 313  THR   B HG23 1 
ATOM   14229 N  N    . LEU   B 1 314 ? 16.095 31.745  62.376 1.00 11.09 ? 314  LEU   B N    1 
ATOM   14230 C  CA   . LEU   B 1 314 ? 15.183 32.898  62.180 1.00 13.25 ? 314  LEU   B CA   1 
ATOM   14231 C  C    . LEU   B 1 314 ? 14.687 33.359  63.553 1.00 12.15 ? 314  LEU   B C    1 
ATOM   14232 O  O    . LEU   B 1 314 ? 14.537 34.572  63.758 1.00 17.06 ? 314  LEU   B O    1 
ATOM   14233 C  CB   . LEU   B 1 314 ? 14.027 32.444  61.292 1.00 12.80 ? 314  LEU   B CB   1 
ATOM   14234 C  CG   . LEU   B 1 314 ? 14.414 32.177  59.841 1.00 12.59 ? 314  LEU   B CG   1 
ATOM   14235 C  CD1  . LEU   B 1 314 ? 13.433 31.222  59.190 1.00 13.72 ? 314  LEU   B CD1  1 
ATOM   14236 C  CD2  . LEU   B 1 314 ? 14.489 33.478  59.062 1.00 14.85 ? 314  LEU   B CD2  1 
ATOM   14237 H  H    . LEU   B 1 314 ? 15.865 31.025  61.966 1.00 13.32 ? 314  LEU   B H    1 
ATOM   14238 H  HA   . LEU   B 1 314 ? 15.632 33.642  61.749 1.00 15.91 ? 314  LEU   B HA   1 
ATOM   14239 H  HB2  . LEU   B 1 314 ? 13.644 31.636  61.667 1.00 15.37 ? 314  LEU   B HB2  1 
ATOM   14240 H  HB3  . LEU   B 1 314 ? 13.334 33.122  61.311 1.00 15.37 ? 314  LEU   B HB3  1 
ATOM   14241 H  HG   . LEU   B 1 314 ? 15.291 31.763  59.832 1.00 15.11 ? 314  LEU   B HG   1 
ATOM   14242 H  HD11 . LEU   B 1 314 ? 13.696 31.065  58.270 1.00 16.47 ? 314  LEU   B HD11 1 
ATOM   14243 H  HD12 . LEU   B 1 314 ? 13.431 30.381  59.673 1.00 16.47 ? 314  LEU   B HD12 1 
ATOM   14244 H  HD13 . LEU   B 1 314 ? 12.543 31.608  59.210 1.00 16.47 ? 314  LEU   B HD13 1 
ATOM   14245 H  HD21 . LEU   B 1 314 ? 14.736 33.291  58.143 1.00 17.82 ? 314  LEU   B HD21 1 
ATOM   14246 H  HD22 . LEU   B 1 314 ? 13.624 33.917  59.081 1.00 17.82 ? 314  LEU   B HD22 1 
ATOM   14247 H  HD23 . LEU   B 1 314 ? 15.155 34.058  59.464 1.00 17.82 ? 314  LEU   B HD23 1 
ATOM   14248 N  N    . TRP   B 1 315 ? 14.466 32.414  64.463 1.00 13.31 ? 315  TRP   B N    1 
ATOM   14249 C  CA   . TRP   B 1 315 ? 13.945 32.773  65.807 1.00 14.52 ? 315  TRP   B CA   1 
ATOM   14250 C  C    . TRP   B 1 315 ? 15.019 33.439  66.667 1.00 12.85 ? 315  TRP   B C    1 
ATOM   14251 O  O    . TRP   B 1 315 ? 14.744 34.511  67.220 1.00 11.89 ? 315  TRP   B O    1 
ATOM   14252 C  CB   . TRP   B 1 315 ? 13.413 31.531  66.534 1.00 13.49 ? 315  TRP   B CB   1 
ATOM   14253 C  CG   . TRP   B 1 315 ? 13.250 31.752  68.007 1.00 12.66 ? 315  TRP   B CG   1 
ATOM   14254 C  CD1  . TRP   B 1 315 ? 12.259 32.460  68.621 1.00 11.83 ? 315  TRP   B CD1  1 
ATOM   14255 C  CD2  . TRP   B 1 315 ? 14.112 31.278  69.057 1.00 11.55 ? 315  TRP   B CD2  1 
ATOM   14256 N  NE1  . TRP   B 1 315 ? 12.441 32.455  69.976 1.00 13.05 ? 315  TRP   B NE1  1 
ATOM   14257 C  CE2  . TRP   B 1 315 ? 13.567 31.737  70.275 1.00 12.69 ? 315  TRP   B CE2  1 
ATOM   14258 C  CE3  . TRP   B 1 315 ? 15.278 30.507  69.094 1.00 14.22 ? 315  TRP   B CE3  1 
ATOM   14259 C  CZ2  . TRP   B 1 315 ? 14.149 31.449  71.508 1.00 10.94 ? 315  TRP   B CZ2  1 
ATOM   14260 C  CZ3  . TRP   B 1 315 ? 15.854 30.226  70.312 1.00 12.28 ? 315  TRP   B CZ3  1 
ATOM   14261 C  CH2  . TRP   B 1 315 ? 15.297 30.691  71.503 1.00 11.42 ? 315  TRP   B CH2  1 
ATOM   14262 H  H    . TRP   B 1 315 ? 14.604 31.574  64.339 1.00 15.98 ? 315  TRP   B H    1 
ATOM   14263 H  HA   . TRP   B 1 315 ? 13.221 33.404  65.672 1.00 17.43 ? 315  TRP   B HA   1 
ATOM   14264 H  HB2  . TRP   B 1 315 ? 12.558 31.278  66.152 1.00 16.20 ? 315  TRP   B HB2  1 
ATOM   14265 H  HB3  . TRP   B 1 315 ? 14.020 30.789  66.387 1.00 16.20 ? 315  TRP   B HB3  1 
ATOM   14266 H  HD1  . TRP   B 1 315 ? 11.559 32.886  68.181 1.00 14.20 ? 315  TRP   B HD1  1 
ATOM   14267 H  HE1  . TRP   B 1 315 ? 11.929 32.841  70.549 1.00 15.66 ? 315  TRP   B HE1  1 
ATOM   14268 H  HE3  . TRP   B 1 315 ? 15.659 30.189  68.307 1.00 17.07 ? 315  TRP   B HE3  1 
ATOM   14269 H  HZ2  . TRP   B 1 315 ? 13.776 31.757  72.302 1.00 13.13 ? 315  TRP   B HZ2  1 
ATOM   14270 H  HZ3  . TRP   B 1 315 ? 16.631 29.715  70.341 1.00 14.74 ? 315  TRP   B HZ3  1 
ATOM   14271 H  HH2  . TRP   B 1 315 ? 15.710 30.484  72.310 1.00 13.71 ? 315  TRP   B HH2  1 
ATOM   14272 N  N    . CYS   B 1 316 ? 16.198 32.824  66.770 1.00 13.67 ? 316  CYS   B N    1 
ATOM   14273 C  CA   . CYS   B 1 316 ? 17.218 33.323  67.732 1.00 12.41 ? 316  CYS   B CA   1 
ATOM   14274 C  C    . CYS   B 1 316 ? 17.828 34.663  67.301 1.00 14.43 ? 316  CYS   B C    1 
ATOM   14275 O  O    . CYS   B 1 316 ? 18.297 35.388  68.183 1.00 15.73 ? 316  CYS   B O    1 
ATOM   14276 C  CB   . CYS   B 1 316 ? 18.299 32.273  67.965 1.00 14.36 ? 316  CYS   B CB   1 
ATOM   14277 S  SG   . CYS   B 1 316 ? 19.380 31.992  66.538 1.00 14.55 ? 316  CYS   B SG   1 
ATOM   14278 H  H    . CYS   B 1 316 ? 16.434 32.135  66.312 1.00 16.41 ? 316  CYS   B H    1 
ATOM   14279 H  HA   . CYS   B 1 316 ? 16.761 33.486  68.572 1.00 14.90 ? 316  CYS   B HA   1 
ATOM   14280 H  HB2  . CYS   B 1 316 ? 18.842 32.545  68.721 1.00 17.24 ? 316  CYS   B HB2  1 
ATOM   14281 H  HB3  . CYS   B 1 316 ? 17.875 31.435  68.207 1.00 17.24 ? 316  CYS   B HB3  1 
ATOM   14282 H  HG   . CYS   B 1 316 ? 20.499 31.783  66.918 1.00 17.46 ? 316  CYS   B HG   1 
ATOM   14283 N  N    . PHE   B 1 317 ? 17.837 34.954  66.000 1.00 12.52 ? 317  PHE   B N    1 
ATOM   14284 C  CA   . PHE   B 1 317 ? 18.326 36.278  65.535 1.00 13.31 ? 317  PHE   B CA   1 
ATOM   14285 C  C    . PHE   B 1 317 ? 17.121 37.125  65.114 1.00 13.59 ? 317  PHE   B C    1 
ATOM   14286 O  O    . PHE   B 1 317 ? 17.301 38.148  64.438 1.00 15.15 ? 317  PHE   B O    1 
ATOM   14287 C  CB   . PHE   B 1 317 ? 19.345 36.114  64.407 1.00 15.95 ? 317  PHE   B CB   1 
ATOM   14288 C  CG   . PHE   B 1 317 ? 20.685 35.596  64.861 1.00 13.18 ? 317  PHE   B CG   1 
ATOM   14289 C  CD1  . PHE   B 1 317 ? 21.457 36.318  65.755 1.00 14.55 ? 317  PHE   B CD1  1 
ATOM   14290 C  CD2  . PHE   B 1 317 ? 21.170 34.382  64.403 1.00 14.91 ? 317  PHE   B CD2  1 
ATOM   14291 C  CE1  . PHE   B 1 317 ? 22.687 35.841  66.177 1.00 12.98 ? 317  PHE   B CE1  1 
ATOM   14292 C  CE2  . PHE   B 1 317 ? 22.399 33.905  64.827 1.00 15.24 ? 317  PHE   B CE2  1 
ATOM   14293 C  CZ   . PHE   B 1 317 ? 23.155 34.635  65.712 1.00 15.70 ? 317  PHE   B CZ   1 
ATOM   14294 H  H    . PHE   B 1 317 ? 17.574 34.422  65.377 1.00 15.02 ? 317  PHE   B H    1 
ATOM   14295 H  HA   . PHE   B 1 317 ? 18.788 36.736  66.255 1.00 15.97 ? 317  PHE   B HA   1 
ATOM   14296 H  HB2  . PHE   B 1 317 ? 18.983 35.508  63.742 1.00 19.14 ? 317  PHE   B HB2  1 
ATOM   14297 H  HB3  . PHE   B 1 317 ? 19.471 36.971  63.971 1.00 19.14 ? 317  PHE   B HB3  1 
ATOM   14298 H  HD1  . PHE   B 1 317 ? 21.146 37.133  66.076 1.00 17.46 ? 317  PHE   B HD1  1 
ATOM   14299 H  HD2  . PHE   B 1 317 ? 20.664 33.882  63.804 1.00 17.90 ? 317  PHE   B HD2  1 
ATOM   14300 H  HE1  . PHE   B 1 317 ? 23.197 36.337  66.776 1.00 15.57 ? 317  PHE   B HE1  1 
ATOM   14301 H  HE2  . PHE   B 1 317 ? 22.713 33.088  64.512 1.00 18.29 ? 317  PHE   B HE2  1 
ATOM   14302 H  HZ   . PHE   B 1 317 ? 23.981 34.314  65.996 1.00 18.84 ? 317  PHE   B HZ   1 
ATOM   14303 N  N    . GLY   B 1 318 ? 15.926 36.687  65.502 1.00 13.61 ? 318  GLY   B N    1 
ATOM   14304 C  CA   . GLY   B 1 318 ? 14.708 37.454  65.194 1.00 13.98 ? 318  GLY   B CA   1 
ATOM   14305 C  C    . GLY   B 1 318 ? 13.896 37.717  66.448 1.00 12.89 ? 318  GLY   B C    1 
ATOM   14306 O  O    . GLY   B 1 318 ? 14.339 38.515  67.277 1.00 15.28 ? 318  GLY   B O    1 
ATOM   14307 H  H    . GLY   B 1 318 ? 15.794 35.958  65.939 1.00 16.33 ? 318  GLY   B H    1 
ATOM   14308 H  HA2  . GLY   B 1 318 ? 14.949 38.297  64.779 1.00 16.78 ? 318  GLY   B HA2  1 
ATOM   14309 H  HA3  . GLY   B 1 318 ? 14.169 36.966  64.552 1.00 16.78 ? 318  GLY   B HA3  1 
ATOM   14310 N  N    . SER   B 1 319 ? 12.769 37.023  66.588 1.00 13.17 ? 319  SER   B N    1 
ATOM   14311 C  CA   . SER   B 1 319 ? 11.848 37.275  67.727 1.00 13.91 ? 319  SER   B CA   1 
ATOM   14312 C  C    . SER   B 1 319 ? 12.565 37.228  69.084 1.00 13.34 ? 319  SER   B C    1 
ATOM   14313 O  O    . SER   B 1 319 ? 12.195 38.010  69.967 1.00 16.39 ? 319  SER   B O    1 
ATOM   14314 C  CB   . SER   B 1 319 ? 10.693 36.308  67.667 1.00 16.04 ? 319  SER   B CB   1 
ATOM   14315 O  OG   . SER   B 1 319 ? 10.236 36.144  66.335 1.00 16.52 ? 319  SER   B OG   1 
ATOM   14316 H  H    . SER   B 1 319 ? 12.511 36.406  66.047 1.00 15.81 ? 319  SER   B H    1 
ATOM   14317 H  HA   . SER   B 1 319 ? 11.504 38.178  67.644 1.00 16.70 ? 319  SER   B HA   1 
ATOM   14318 H  HB2  . SER   B 1 319 ? 10.967 35.450  68.027 1.00 19.25 ? 319  SER   B HB2  1 
ATOM   14319 H  HB3  . SER   B 1 319 ? 9.967  36.631  68.224 1.00 19.25 ? 319  SER   B HB3  1 
ATOM   14320 H  HG   . SER   B 1 319 ? 9.915  35.374  66.242 1.00 19.83 ? 319  SER   B HG   1 
ATOM   14321 N  N    . ASP   B 1 320 ? 13.537 36.333  69.252 1.00 13.16 ? 320  ASP   B N    1 
ATOM   14322 C  CA   . ASP   B 1 320 ? 14.197 36.191  70.576 1.00 15.01 ? 320  ASP   B CA   1 
ATOM   14323 C  C    . ASP   B 1 320 ? 14.903 37.499  70.949 1.00 15.38 ? 320  ASP   B C    1 
ATOM   14324 O  O    . ASP   B 1 320 ? 15.017 37.782  72.145 1.00 13.71 ? 320  ASP   B O    1 
ATOM   14325 C  CB   . ASP   B 1 320 ? 15.170 35.009  70.608 1.00 12.76 ? 320  ASP   B CB   1 
ATOM   14326 C  CG   . ASP   B 1 320 ? 15.372 34.444  72.002 1.00 14.59 ? 320  ASP   B CG   1 
ATOM   14327 O  OD1  . ASP   B 1 320 ? 14.451 34.584  72.825 1.00 14.66 ? 320  ASP   B OD1  1 
ATOM   14328 O  OD2  . ASP   B 1 320 ? 16.446 33.867  72.251 1.00 12.45 ? 320  ASP   B OD2  1 
ATOM   14329 H  H    . ASP   B 1 320 ? 13.831 35.807  68.638 1.00 15.80 ? 320  ASP   B H    1 
ATOM   14330 H  HA   . ASP   B 1 320 ? 13.511 36.004  71.236 1.00 18.02 ? 320  ASP   B HA   1 
ATOM   14331 H  HB2  . ASP   B 1 320 ? 14.838 34.308  70.025 1.00 15.32 ? 320  ASP   B HB2  1 
ATOM   14332 H  HB3  . ASP   B 1 320 ? 16.027 35.292  70.252 1.00 15.32 ? 320  ASP   B HB3  1 
ATOM   14333 N  N    . CYS   B 1 321 ? 15.366 38.246  69.945 1.00 14.23 ? 321  CYS   B N    1 
ATOM   14334 C  CA   . CYS   B 1 321 ? 16.082 39.523  70.212 1.00 15.05 ? 321  CYS   B CA   1 
ATOM   14335 C  C    . CYS   B 1 321 ? 15.197 40.724  69.847 1.00 15.61 ? 321  CYS   B C    1 
ATOM   14336 O  O    . CYS   B 1 321 ? 15.733 41.839  69.762 1.00 15.26 ? 321  CYS   B O    1 
ATOM   14337 C  CB   . CYS   B 1 321 ? 17.371 39.590  69.404 1.00 13.98 ? 321  CYS   B CB   1 
ATOM   14338 S  SG   . CYS   B 1 321 ? 18.623 38.417  69.989 1.00 14.58 ? 321  CYS   B SG   1 
ATOM   14339 H  H    . CYS   B 1 321 ? 15.284 38.046  69.113 1.00 17.07 ? 321  CYS   B H    1 
ATOM   14340 H  HA   . CYS   B 1 321 ? 16.293 39.555  71.158 1.00 18.06 ? 321  CYS   B HA   1 
ATOM   14341 H  HB2  . CYS   B 1 321 ? 17.174 39.409  68.472 1.00 16.78 ? 321  CYS   B HB2  1 
ATOM   14342 H  HB3  . CYS   B 1 321 ? 17.730 40.490  69.449 1.00 16.78 ? 321  CYS   B HB3  1 
ATOM   14343 H  HG   . CYS   B 1 321 ? 18.519 37.386  69.384 1.00 17.50 ? 321  CYS   B HG   1 
ATOM   14344 N  N    . GLY   B 1 322 ? 13.897 40.495  69.649 1.00 14.44 ? 322  GLY   B N    1 
ATOM   14345 C  CA   . GLY   B 1 322 ? 12.962 41.582  69.292 1.00 15.38 ? 322  GLY   B CA   1 
ATOM   14346 C  C    . GLY   B 1 322 ? 13.258 42.178  67.928 1.00 16.18 ? 322  GLY   B C    1 
ATOM   14347 O  O    . GLY   B 1 322 ? 12.918 43.350  67.720 1.00 16.75 ? 322  GLY   B O    1 
ATOM   14348 H  H    . GLY   B 1 322 ? 13.531 39.720  69.715 1.00 17.33 ? 322  GLY   B H    1 
ATOM   14349 H  HA2  . GLY   B 1 322 ? 12.054 41.240  69.302 1.00 18.46 ? 322  GLY   B HA2  1 
ATOM   14350 H  HA3  . GLY   B 1 322 ? 13.010 42.280  69.964 1.00 18.46 ? 322  GLY   B HA3  1 
ATOM   14351 N  N    . SER   B 1 323 ? 13.858 41.391  67.030 1.00 13.43 ? 323  SER   B N    1 
ATOM   14352 C  CA   . SER   B 1 323 ? 14.240 41.882  65.679 1.00 15.91 ? 323  SER   B CA   1 
ATOM   14353 C  C    . SER   B 1 323 ? 13.447 41.131  64.603 1.00 16.72 ? 323  SER   B C    1 
ATOM   14354 O  O    . SER   B 1 323 ? 13.206 39.939  64.785 1.00 16.17 ? 323  SER   B O    1 
ATOM   14355 C  CB   . SER   B 1 323 ? 15.729 41.741  65.459 1.00 16.17 ? 323  SER   B CB   1 
ATOM   14356 O  OG   . SER   B 1 323 ? 16.108 42.257  64.194 1.00 14.28 ? 323  SER   B OG   1 
ATOM   14357 H  H    . SER   B 1 323 ? 14.057 40.567  67.175 1.00 16.12 ? 323  SER   B H    1 
ATOM   14358 H  HA   . SER   B 1 323 ? 14.022 42.825  65.616 1.00 19.09 ? 323  SER   B HA   1 
ATOM   14359 H  HB2  . SER   B 1 323 ? 16.209 42.210  66.160 1.00 19.40 ? 323  SER   B HB2  1 
ATOM   14360 H  HB3  . SER   B 1 323 ? 15.981 40.806  65.519 1.00 19.40 ? 323  SER   B HB3  1 
ATOM   14361 H  HG   . SER   B 1 323 ? 16.194 41.625  63.648 1.00 17.14 ? 323  SER   B HG   1 
ATOM   14362 N  N    . TYR   B 1 324 ? 13.067 41.816  63.523 1.00 17.00 ? 324  TYR   B N    1 
ATOM   14363 C  CA   . TYR   B 1 324 ? 12.239 41.174  62.468 1.00 17.47 ? 324  TYR   B CA   1 
ATOM   14364 C  C    . TYR   B 1 324 ? 12.783 41.569  61.089 1.00 18.38 ? 324  TYR   B C    1 
ATOM   14365 O  O    . TYR   B 1 324 ? 11.988 41.743  60.159 1.00 19.17 ? 324  TYR   B O    1 
ATOM   14366 C  CB   . TYR   B 1 324 ? 10.758 41.470  62.724 1.00 15.34 ? 324  TYR   B CB   1 
ATOM   14367 C  CG   . TYR   B 1 324 ? 10.323 41.048  64.104 1.00 15.52 ? 324  TYR   B CG   1 
ATOM   14368 C  CD1  . TYR   B 1 324 ? 9.953  39.740  64.364 1.00 15.37 ? 324  TYR   B CD1  1 
ATOM   14369 C  CD2  . TYR   B 1 324 ? 10.341 41.938  65.164 1.00 16.40 ? 324  TYR   B CD2  1 
ATOM   14370 C  CE1  . TYR   B 1 324 ? 9.579  39.334  65.634 1.00 14.73 ? 324  TYR   B CE1  1 
ATOM   14371 C  CE2  . TYR   B 1 324 ? 9.976  41.548  66.442 1.00 14.60 ? 324  TYR   B CE2  1 
ATOM   14372 C  CZ   . TYR   B 1 324 ? 9.591  40.241  66.677 1.00 15.03 ? 324  TYR   B CZ   1 
ATOM   14373 O  OH   . TYR   B 1 324 ? 9.223  39.843  67.938 1.00 16.34 ? 324  TYR   B OH   1 
ATOM   14374 H  H    . TYR   B 1 324 ? 13.268 42.639  63.374 1.00 20.41 ? 324  TYR   B H    1 
ATOM   14375 H  HA   . TYR   B 1 324 ? 12.300 40.206  62.492 1.00 20.97 ? 324  TYR   B HA   1 
ATOM   14376 H  HB2  . TYR   B 1 324 ? 10.596 42.420  62.612 1.00 18.41 ? 324  TYR   B HB2  1 
ATOM   14377 H  HB3  . TYR   B 1 324 ? 10.219 41.010  62.062 1.00 18.41 ? 324  TYR   B HB3  1 
ATOM   14378 H  HD1  . TYR   B 1 324 ? 9.956  39.120  63.671 1.00 18.45 ? 324  TYR   B HD1  1 
ATOM   14379 H  HD2  . TYR   B 1 324 ? 10.604 42.817  65.015 1.00 19.69 ? 324  TYR   B HD2  1 
ATOM   14380 H  HE1  . TYR   B 1 324 ? 9.320  38.453  65.785 1.00 17.68 ? 324  TYR   B HE1  1 
ATOM   14381 H  HE2  . TYR   B 1 324 ? 9.990  42.163  67.139 1.00 17.52 ? 324  TYR   B HE2  1 
ATOM   14382 H  HH   . TYR   B 1 324 ? 9.410  39.031  68.041 1.00 19.62 ? 324  TYR   B HH   1 
ATOM   14383 N  N    . ASP   B 1 325 ? 14.112 41.668  60.982 1.00 16.51 ? 325  ASP   B N    1 
ATOM   14384 C  CA   . ASP   B 1 325 ? 14.788 41.994  59.700 1.00 17.61 ? 325  ASP   B CA   1 
ATOM   14385 C  C    . ASP   B 1 325 ? 15.280 40.681  59.082 1.00 17.65 ? 325  ASP   B C    1 
ATOM   14386 O  O    . ASP   B 1 325 ? 16.245 40.124  59.616 1.00 17.52 ? 325  ASP   B O    1 
ATOM   14387 C  CB   . ASP   B 1 325 ? 15.921 42.978  59.974 1.00 18.17 ? 325  ASP   B CB   1 
ATOM   14388 C  CG   . ASP   B 1 325 ? 16.641 43.477  58.734 1.00 17.18 ? 325  ASP   B CG   1 
ATOM   14389 O  OD1  . ASP   B 1 325 ? 16.666 42.745  57.729 1.00 16.61 ? 325  ASP   B OD1  1 
ATOM   14390 O  OD2  . ASP   B 1 325 ? 17.174 44.597  58.792 1.00 20.49 ? 325  ASP   B OD2  1 
ATOM   14391 H  H    . ASP   B 1 325 ? 14.651 41.550  61.642 1.00 19.81 ? 325  ASP   B H    1 
ATOM   14392 H  HA   . ASP   B 1 325 ? 14.187 42.420  59.069 1.00 21.13 ? 325  ASP   B HA   1 
ATOM   14393 H  HB2  . ASP   B 1 325 ? 15.562 43.741  60.454 1.00 21.81 ? 325  ASP   B HB2  1 
ATOM   14394 H  HB3  . ASP   B 1 325 ? 16.567 42.553  60.560 1.00 21.81 ? 325  ASP   B HB3  1 
ATOM   14395 N  N    . LEU   B 1 326 ? 14.638 40.219  58.007 1.00 18.49 ? 326  LEU   B N    1 
ATOM   14396 C  CA   . LEU   B 1 326 ? 14.973 38.895  57.412 1.00 15.32 ? 326  LEU   B CA   1 
ATOM   14397 C  C    . LEU   B 1 326 ? 16.343 38.937  56.725 1.00 16.00 ? 326  LEU   B C    1 
ATOM   14398 O  O    . LEU   B 1 326 ? 17.084 37.958  56.850 1.00 15.85 ? 326  LEU   B O    1 
ATOM   14399 C  CB   . LEU   B 1 326 ? 13.868 38.518  56.424 1.00 17.79 ? 326  LEU   B CB   1 
ATOM   14400 C  CG   . LEU   B 1 326 ? 13.977 37.132  55.794 1.00 14.39 ? 326  LEU   B CG   1 
ATOM   14401 C  CD1  . LEU   B 1 326 ? 14.170 36.073  56.865 1.00 17.47 ? 326  LEU   B CD1  1 
ATOM   14402 C  CD2  . LEU   B 1 326 ? 12.744 36.823  54.960 1.00 17.32 ? 326  LEU   B CD2  1 
ATOM   14403 H  H    . LEU   B 1 326 ? 14.009 40.644  57.602 1.00 22.19 ? 326  LEU   B H    1 
ATOM   14404 H  HA   . LEU   B 1 326 ? 15.027 38.223  58.109 1.00 18.38 ? 326  LEU   B HA   1 
ATOM   14405 H  HB2  . LEU   B 1 326 ? 13.015 38.579  56.882 1.00 21.35 ? 326  LEU   B HB2  1 
ATOM   14406 H  HB3  . LEU   B 1 326 ? 13.856 39.177  55.712 1.00 21.35 ? 326  LEU   B HB3  1 
ATOM   14407 H  HG   . LEU   B 1 326 ? 14.752 37.124  55.210 1.00 17.27 ? 326  LEU   B HG   1 
ATOM   14408 H  HD11 . LEU   B 1 326 ? 14.237 35.200  56.448 1.00 20.96 ? 326  LEU   B HD11 1 
ATOM   14409 H  HD12 . LEU   B 1 326 ? 14.983 36.258  57.360 1.00 20.96 ? 326  LEU   B HD12 1 
ATOM   14410 H  HD13 . LEU   B 1 326 ? 13.413 36.084  57.471 1.00 20.96 ? 326  LEU   B HD13 1 
ATOM   14411 H  HD21 . LEU   B 1 326 ? 12.831 35.940  54.568 1.00 20.79 ? 326  LEU   B HD21 1 
ATOM   14412 H  HD22 . LEU   B 1 326 ? 11.956 36.849  55.525 1.00 20.79 ? 326  LEU   B HD22 1 
ATOM   14413 H  HD23 . LEU   B 1 326 ? 12.657 37.482  54.254 1.00 20.79 ? 326  LEU   B HD23 1 
ATOM   14414 N  N    . ASP   B 1 327 ? 16.652 40.031  56.027 1.00 17.95 ? 327  ASP   B N    1 
ATOM   14415 C  CA   . ASP   B 1 327 ? 18.001 40.162  55.417 1.00 18.60 ? 327  ASP   B CA   1 
ATOM   14416 C  C    . ASP   B 1 327 ? 19.070 39.989  56.501 1.00 16.85 ? 327  ASP   B C    1 
ATOM   14417 O  O    . ASP   B 1 327 ? 20.075 39.316  56.230 1.00 17.45 ? 327  ASP   B O    1 
ATOM   14418 C  CB   . ASP   B 1 327 ? 18.172 41.482  54.659 1.00 19.96 ? 327  ASP   B CB   1 
ATOM   14419 C  CG   . ASP   B 1 327 ? 17.456 41.515  53.320 1.00 22.59 ? 327  ASP   B CG   1 
ATOM   14420 O  OD1  . ASP   B 1 327 ? 17.365 40.456  52.675 1.00 21.52 ? 327  ASP   B OD1  1 
ATOM   14421 O  OD2  . ASP   B 1 327 ? 16.996 42.604  52.934 1.00 27.38 ? 327  ASP   B OD2  1 
ATOM   14422 H  H    . ASP   B 1 327 ? 16.122 40.694  55.892 1.00 21.55 ? 327  ASP   B H    1 
ATOM   14423 H  HA   . ASP   B 1 327 ? 18.105 39.460  54.755 1.00 22.32 ? 327  ASP   B HA   1 
ATOM   14424 H  HB2  . ASP   B 1 327 ? 17.842 42.208  55.211 1.00 23.95 ? 327  ASP   B HB2  1 
ATOM   14425 H  HB3  . ASP   B 1 327 ? 19.118 41.643  54.515 1.00 23.95 ? 327  ASP   B HB3  1 
ATOM   14426 N  N    . ALA   B 1 328 ? 18.874 40.595  57.673 1.00 17.52 ? 328  ALA   B N    1 
ATOM   14427 C  CA   . ALA   B 1 328 ? 19.911 40.532  58.728 1.00 18.40 ? 328  ALA   B CA   1 
ATOM   14428 C  C    . ALA   B 1 328 ? 20.047 39.095  59.245 1.00 14.25 ? 328  ALA   B C    1 
ATOM   14429 O  O    . ALA   B 1 328 ? 21.143 38.710  59.646 1.00 15.24 ? 328  ALA   B O    1 
ATOM   14430 C  CB   . ALA   B 1 328 ? 19.573 41.474  59.856 1.00 17.53 ? 328  ALA   B CB   1 
ATOM   14431 H  H    . ALA   B 1 328 ? 18.168 41.040  57.882 1.00 21.03 ? 328  ALA   B H    1 
ATOM   14432 H  HA   . ALA   B 1 328 ? 20.761 40.807  58.349 1.00 22.09 ? 328  ALA   B HA   1 
ATOM   14433 H  HB1  . ALA   B 1 328 ? 20.260 41.422  60.538 1.00 21.04 ? 328  ALA   B HB1  1 
ATOM   14434 H  HB2  . ALA   B 1 328 ? 19.524 42.381  59.516 1.00 21.04 ? 328  ALA   B HB2  1 
ATOM   14435 H  HB3  . ALA   B 1 328 ? 18.717 41.226  60.240 1.00 21.04 ? 328  ALA   B HB3  1 
ATOM   14436 N  N    . ILE   B 1 329 ? 18.939 38.358  59.270 1.00 16.21 ? 329  ILE   B N    1 
ATOM   14437 C  CA   . ILE   B 1 329 ? 19.004 36.938  59.722 1.00 14.57 ? 329  ILE   B CA   1 
ATOM   14438 C  C    . ILE   B 1 329 ? 19.806 36.156  58.677 1.00 14.66 ? 329  ILE   B C    1 
ATOM   14439 O  O    . ILE   B 1 329 ? 20.665 35.357  59.068 1.00 13.51 ? 329  ILE   B O    1 
ATOM   14440 C  CB   . ILE   B 1 329 ? 17.593 36.361  59.946 1.00 14.92 ? 329  ILE   B CB   1 
ATOM   14441 C  CG1  . ILE   B 1 329 ? 16.901 37.040  61.130 1.00 17.04 ? 329  ILE   B CG1  1 
ATOM   14442 C  CG2  . ILE   B 1 329 ? 17.654 34.851  60.120 1.00 16.77 ? 329  ILE   B CG2  1 
ATOM   14443 C  CD1  . ILE   B 1 329 ? 15.458 36.637  61.313 1.00 17.53 ? 329  ILE   B CD1  1 
ATOM   14444 H  H    . ILE   B 1 329 ? 18.158 38.635  59.041 1.00 19.46 ? 329  ILE   B H    1 
ATOM   14445 H  HA   . ILE   B 1 329 ? 19.450 36.869  60.581 1.00 17.49 ? 329  ILE   B HA   1 
ATOM   14446 H  HB   . ILE   B 1 329 ? 17.059 36.546  59.158 1.00 17.91 ? 329  ILE   B HB   1 
ATOM   14447 H  HG12 . ILE   B 1 329 ? 17.390 36.832  61.941 1.00 20.46 ? 329  ILE   B HG12 1 
ATOM   14448 H  HG13 . ILE   B 1 329 ? 16.946 38.002  61.011 1.00 20.46 ? 329  ILE   B HG13 1 
ATOM   14449 H  HG21 . ILE   B 1 329 ? 16.759 34.505  60.260 1.00 20.13 ? 329  ILE   B HG21 1 
ATOM   14450 H  HG22 . ILE   B 1 329 ? 18.035 34.448  59.324 1.00 20.13 ? 329  ILE   B HG22 1 
ATOM   14451 H  HG23 . ILE   B 1 329 ? 18.207 34.636  60.887 1.00 20.13 ? 329  ILE   B HG23 1 
ATOM   14452 H  HD11 . ILE   B 1 329 ? 15.086 37.104  62.078 1.00 21.04 ? 329  ILE   B HD11 1 
ATOM   14453 H  HD12 . ILE   B 1 329 ? 14.954 36.868  60.517 1.00 21.04 ? 329  ILE   B HD12 1 
ATOM   14454 H  HD13 . ILE   B 1 329 ? 15.406 35.680  61.462 1.00 21.04 ? 329  ILE   B HD13 1 
ATOM   14455 N  N    . ASN   B 1 330 ? 19.504 36.380  57.398 1.00 15.40 ? 330  ASN   B N    1 
ATOM   14456 C  CA   . ASN   B 1 330 ? 20.284 35.722  56.320 1.00 13.76 ? 330  ASN   B CA   1 
ATOM   14457 C  C    . ASN   B 1 330 ? 21.767 36.014  56.559 1.00 14.65 ? 330  ASN   B C    1 
ATOM   14458 O  O    . ASN   B 1 330 ? 22.597 35.112  56.349 1.00 15.21 ? 330  ASN   B O    1 
ATOM   14459 C  CB   . ASN   B 1 330 ? 19.820 36.194  54.940 1.00 14.81 ? 330  ASN   B CB   1 
ATOM   14460 C  CG   . ASN   B 1 330 ? 18.449 35.674  54.571 1.00 18.08 ? 330  ASN   B CG   1 
ATOM   14461 O  OD1  . ASN   B 1 330 ? 17.952 34.739  55.192 1.00 14.95 ? 330  ASN   B OD1  1 
ATOM   14462 N  ND2  . ASN   B 1 330 ? 17.835 36.269  53.562 1.00 17.91 ? 330  ASN   B ND2  1 
ATOM   14463 H  H    . ASN   B 1 330 ? 18.870 36.894  57.128 1.00 18.48 ? 330  ASN   B H    1 
ATOM   14464 H  HA   . ASN   B 1 330 ? 20.141 34.763  56.340 1.00 16.51 ? 330  ASN   B HA   1 
ATOM   14465 H  HB2  . ASN   B 1 330 ? 19.809 37.164  54.922 1.00 17.78 ? 330  ASN   B HB2  1 
ATOM   14466 H  HB3  . ASN   B 1 330 ? 20.461 35.905  54.272 1.00 17.78 ? 330  ASN   B HB3  1 
ATOM   14467 H  HD21 . ASN   B 1 330 ? 17.055 36.003  53.317 1.00 21.49 ? 330  ASN   B HD21 1 
ATOM   14468 H  HD22 . ASN   B 1 330 ? 18.216 36.921  53.151 1.00 21.49 ? 330  ASN   B HD22 1 
ATOM   14469 N  N    A GLU   B 1 331 ? 22.079 37.235  56.988 0.27 16.92 ? 331  GLU   B N    1 
ATOM   14470 N  N    B GLU   B 1 331 ? 22.083 37.240  56.982 0.73 16.92 ? 331  GLU   B N    1 
ATOM   14471 C  CA   A GLU   B 1 331 ? 23.487 37.639  57.224 0.27 13.67 ? 331  GLU   B CA   1 
ATOM   14472 C  CA   B GLU   B 1 331 ? 23.497 37.634  57.221 0.73 13.67 ? 331  GLU   B CA   1 
ATOM   14473 C  C    A GLU   B 1 331 ? 24.021 36.965  58.491 0.27 13.61 ? 331  GLU   B C    1 
ATOM   14474 C  C    B GLU   B 1 331 ? 24.011 36.939  58.484 0.73 13.61 ? 331  GLU   B C    1 
ATOM   14475 O  O    A GLU   B 1 331 ? 25.122 36.402  58.445 0.27 13.26 ? 331  GLU   B O    1 
ATOM   14476 O  O    B GLU   B 1 331 ? 25.137 36.416  58.451 0.73 13.26 ? 331  GLU   B O    1 
ATOM   14477 C  CB   A GLU   B 1 331 ? 23.533 39.160  57.355 0.27 21.23 ? 331  GLU   B CB   1 
ATOM   14478 C  CB   B GLU   B 1 331 ? 23.606 39.154  57.352 0.73 21.23 ? 331  GLU   B CB   1 
ATOM   14479 C  CG   A GLU   B 1 331 ? 24.808 39.663  57.971 0.27 25.02 ? 331  GLU   B CG   1 
ATOM   14480 C  CG   B GLU   B 1 331 ? 24.791 39.604  58.183 0.73 25.02 ? 331  GLU   B CG   1 
ATOM   14481 C  CD   A GLU   B 1 331 ? 25.857 39.926  56.913 0.27 37.43 ? 331  GLU   B CD   1 
ATOM   14482 C  CD   B GLU   B 1 331 ? 25.672 40.630  57.492 0.73 37.43 ? 331  GLU   B CD   1 
ATOM   14483 O  OE1  A GLU   B 1 331 ? 25.565 39.739  55.716 0.27 43.87 ? 331  GLU   B OE1  1 
ATOM   14484 O  OE1  B GLU   B 1 331 ? 26.502 40.224  56.655 0.73 43.87 ? 331  GLU   B OE1  1 
ATOM   14485 O  OE2  A GLU   B 1 331 ? 26.953 40.315  57.291 0.27 45.72 ? 331  GLU   B OE2  1 
ATOM   14486 O  OE2  B GLU   B 1 331 ? 25.521 41.831  57.788 0.73 45.72 ? 331  GLU   B OE2  1 
ATOM   14487 H  H    A GLU   B 1 331 ? 21.500 37.850  57.151 0.27 20.31 ? 331  GLU   B H    1 
ATOM   14488 H  H    B GLU   B 1 331 ? 21.508 37.860  57.138 0.73 20.31 ? 331  GLU   B H    1 
ATOM   14489 H  HA   A GLU   B 1 331 ? 24.047 37.360  56.483 0.27 16.41 ? 331  GLU   B HA   1 
ATOM   14490 H  HA   B GLU   B 1 331 ? 24.043 37.358  56.468 0.73 16.41 ? 331  GLU   B HA   1 
ATOM   14491 H  HB2  A GLU   B 1 331 ? 23.426 39.558  56.477 0.27 25.48 ? 331  GLU   B HB2  1 
ATOM   14492 H  HB2  B GLU   B 1 331 ? 23.674 39.544  56.466 0.73 25.48 ? 331  GLU   B HB2  1 
ATOM   14493 H  HB3  A GLU   B 1 331 ? 22.782 39.455  57.893 0.27 25.48 ? 331  GLU   B HB3  1 
ATOM   14494 H  HB3  B GLU   B 1 331 ? 22.791 39.497  57.751 0.73 25.48 ? 331  GLU   B HB3  1 
ATOM   14495 H  HG2  A GLU   B 1 331 ? 24.632 40.478  58.466 0.27 30.03 ? 331  GLU   B HG2  1 
ATOM   14496 H  HG2  B GLU   B 1 331 ? 24.467 39.978  59.017 0.73 30.03 ? 331  GLU   B HG2  1 
ATOM   14497 H  HG3  A GLU   B 1 331 ? 25.142 39.012  58.607 0.27 30.03 ? 331  GLU   B HG3  1 
ATOM   14498 H  HG3  B GLU   B 1 331 ? 25.329 38.829  58.410 0.73 30.03 ? 331  GLU   B HG3  1 
ATOM   14499 N  N    . ALA   B 1 332 ? 23.259 37.041  59.583 1.00 15.03 ? 332  ALA   B N    1 
ATOM   14500 C  CA   . ALA   B 1 332 ? 23.687 36.435  60.865 1.00 15.18 ? 332  ALA   B CA   1 
ATOM   14501 C  C    . ALA   B 1 332 ? 23.977 34.945  60.672 1.00 13.03 ? 332  ALA   B C    1 
ATOM   14502 O  O    . ALA   B 1 332 ? 24.983 34.465  61.210 1.00 12.95 ? 332  ALA   B O    1 
ATOM   14503 C  CB   . ALA   B 1 332 ? 22.595 36.631  61.880 1.00 15.72 ? 332  ALA   B CB   1 
ATOM   14504 H  H    A ALA   B 1 332 ? 22.495 37.434  59.611 0.27 18.04 ? 332  ALA   B H    1 
ATOM   14505 H  H    B ALA   B 1 332 ? 22.504 37.451  59.615 0.73 18.04 ? 332  ALA   B H    1 
ATOM   14506 H  HA   . ALA   B 1 332 ? 24.500 36.863  61.177 1.00 18.22 ? 332  ALA   B HA   1 
ATOM   14507 H  HB1  . ALA   B 1 332 ? 22.864 36.238  62.725 1.00 18.87 ? 332  ALA   B HB1  1 
ATOM   14508 H  HB2  . ALA   B 1 332 ? 22.433 37.580  62.002 1.00 18.87 ? 332  ALA   B HB2  1 
ATOM   14509 H  HB3  . ALA   B 1 332 ? 21.783 36.202  61.568 1.00 18.87 ? 332  ALA   B HB3  1 
ATOM   14510 N  N    . ASN   B 1 333 ? 23.090 34.256  59.958 1.00 14.06 ? 333  ASN   B N    1 
ATOM   14511 C  CA   . ASN   B 1 333 ? 23.263 32.802  59.715 1.00 12.96 ? 333  ASN   B CA   1 
ATOM   14512 C  C    . ASN   B 1 333 ? 24.601 32.583  59.006 1.00 12.20 ? 333  ASN   B C    1 
ATOM   14513 O  O    . ASN   B 1 333 ? 25.402 31.754  59.461 1.00 13.86 ? 333  ASN   B O    1 
ATOM   14514 C  CB   . ASN   B 1 333 ? 22.100 32.257  58.887 1.00 13.37 ? 333  ASN   B CB   1 
ATOM   14515 C  CG   . ASN   B 1 333 ? 22.168 30.761  58.671 1.00 13.15 ? 333  ASN   B CG   1 
ATOM   14516 O  OD1  . ASN   B 1 333 ? 22.206 29.996  59.630 1.00 15.87 ? 333  ASN   B OD1  1 
ATOM   14517 N  ND2  . ASN   B 1 333 ? 22.177 30.342  57.417 1.00 17.54 ? 333  ASN   B ND2  1 
ATOM   14518 H  H    . ASN   B 1 333 ? 22.384 34.597  59.604 1.00 16.88 ? 333  ASN   B H    1 
ATOM   14519 H  HA   . ASN   B 1 333 ? 23.266 32.322  60.558 1.00 15.56 ? 333  ASN   B HA   1 
ATOM   14520 H  HB2  . ASN   B 1 333 ? 21.265 32.476  59.330 1.00 16.04 ? 333  ASN   B HB2  1 
ATOM   14521 H  HB3  . ASN   B 1 333 ? 22.089 32.702  58.025 1.00 16.04 ? 333  ASN   B HB3  1 
ATOM   14522 H  HD21 . ASN   B 1 333 ? 22.211 29.500  57.245 1.00 21.05 ? 333  ASN   B HD21 1 
ATOM   14523 H  HD22 . ASN   B 1 333 ? 22.149 30.911  56.773 1.00 21.05 ? 333  ASN   B HD22 1 
ATOM   14524 N  N    . MET   B 1 334 ? 24.816 33.325  57.923 1.00 13.10 ? 334  MET   B N    1 
ATOM   14525 C  CA   . MET   B 1 334 ? 26.091 33.198  57.171 1.00 13.11 ? 334  MET   B CA   1 
ATOM   14526 C  C    . MET   B 1 334 ? 27.278 33.434  58.112 1.00 12.72 ? 334  MET   B C    1 
ATOM   14527 O  O    . MET   B 1 334 ? 28.255 32.675  58.026 1.00 13.29 ? 334  MET   B O    1 
ATOM   14528 C  CB   . MET   B 1 334 ? 26.134 34.216  56.026 1.00 13.14 ? 334  MET   B CB   1 
ATOM   14529 C  CG   . MET   B 1 334 ? 27.390 34.129  55.190 1.00 17.82 ? 334  MET   B CG   1 
ATOM   14530 S  SD   . MET   B 1 334 ? 28.612 35.343  55.736 1.00 17.66 ? 334  MET   B SD   1 
ATOM   14531 C  CE   . MET   B 1 334 ? 27.626 36.840  55.702 1.00 26.02 ? 334  MET   B CE   1 
ATOM   14532 H  H    . MET   B 1 334 ? 24.260 33.898  57.604 1.00 15.73 ? 334  MET   B H    1 
ATOM   14533 H  HA   . MET   B 1 334 ? 26.146 32.303  56.802 1.00 15.74 ? 334  MET   B HA   1 
ATOM   14534 H  HB2  . MET   B 1 334 ? 25.363 34.081  55.453 1.00 15.77 ? 334  MET   B HB2  1 
ATOM   14535 H  HB3  . MET   B 1 334 ? 26.061 35.110  56.395 1.00 15.77 ? 334  MET   B HB3  1 
ATOM   14536 H  HG2  . MET   B 1 334 ? 27.764 33.236  55.254 1.00 21.39 ? 334  MET   B HG2  1 
ATOM   14537 H  HG3  . MET   B 1 334 ? 27.173 34.280  54.257 1.00 21.39 ? 334  MET   B HG3  1 
ATOM   14538 H  HE1  . MET   B 1 334 ? 28.171 37.593  55.980 1.00 31.23 ? 334  MET   B HE1  1 
ATOM   14539 H  HE2  . MET   B 1 334 ? 27.300 36.993  54.801 1.00 31.23 ? 334  MET   B HE2  1 
ATOM   14540 H  HE3  . MET   B 1 334 ? 26.873 36.746  56.306 1.00 31.23 ? 334  MET   B HE3  1 
ATOM   14541 N  N    . LEU   B 1 335 ? 27.187 34.439  58.983 1.00 13.91 ? 335  LEU   B N    1 
ATOM   14542 C  CA   . LEU   B 1 335 ? 28.341 34.779  59.857 1.00 11.82 ? 335  LEU   B CA   1 
ATOM   14543 C  C    . LEU   B 1 335 ? 28.612 33.628  60.835 1.00 13.43 ? 335  LEU   B C    1 
ATOM   14544 O  O    . LEU   B 1 335 ? 29.785 33.325  61.078 1.00 15.09 ? 335  LEU   B O    1 
ATOM   14545 C  CB   . LEU   B 1 335 ? 28.038 36.077  60.610 1.00 15.33 ? 335  LEU   B CB   1 
ATOM   14546 C  CG   . LEU   B 1 335 ? 28.050 37.347  59.763 1.00 15.98 ? 335  LEU   B CG   1 
ATOM   14547 C  CD1  . LEU   B 1 335 ? 27.623 38.552  60.592 1.00 18.20 ? 335  LEU   B CD1  1 
ATOM   14548 C  CD2  . LEU   B 1 335 ? 29.427 37.575  59.162 1.00 16.07 ? 335  LEU   B CD2  1 
ATOM   14549 H  H    . LEU   B 1 335 ? 26.490 34.931  59.091 1.00 16.70 ? 335  LEU   B H    1 
ATOM   14550 H  HA   . LEU   B 1 335 ? 29.136 34.909  59.317 1.00 14.19 ? 335  LEU   B HA   1 
ATOM   14551 H  HB2  . LEU   B 1 335 ? 27.167 35.994  61.028 1.00 18.39 ? 335  LEU   B HB2  1 
ATOM   14552 H  HB3  . LEU   B 1 335 ? 28.687 36.177  61.324 1.00 18.39 ? 335  LEU   B HB3  1 
ATOM   14553 H  HG   . LEU   B 1 335 ? 27.414 37.235  59.039 1.00 19.18 ? 335  LEU   B HG   1 
ATOM   14554 H  HD11 . LEU   B 1 335 ? 27.637 39.348  60.038 1.00 21.85 ? 335  LEU   B HD11 1 
ATOM   14555 H  HD12 . LEU   B 1 335 ? 26.725 38.410  60.931 1.00 21.85 ? 335  LEU   B HD12 1 
ATOM   14556 H  HD13 . LEU   B 1 335 ? 28.235 38.666  61.336 1.00 21.85 ? 335  LEU   B HD13 1 
ATOM   14557 H  HD21 . LEU   B 1 335 ? 29.417 38.385  58.628 1.00 19.29 ? 335  LEU   B HD21 1 
ATOM   14558 H  HD22 . LEU   B 1 335 ? 30.080 37.666  59.874 1.00 19.29 ? 335  LEU   B HD22 1 
ATOM   14559 H  HD23 . LEU   B 1 335 ? 29.664 36.820  58.600 1.00 19.29 ? 335  LEU   B HD23 1 
ATOM   14560 N  N    . CYS   B 1 336 ? 27.552 33.032  61.381 1.00 13.90 ? 336  CYS   B N    1 
ATOM   14561 C  CA   . CYS   B 1 336 ? 27.721 31.911  62.343 1.00 13.10 ? 336  CYS   B CA   1 
ATOM   14562 C  C    . CYS   B 1 336 ? 28.324 30.701  61.619 1.00 13.50 ? 336  CYS   B C    1 
ATOM   14563 O  O    . CYS   B 1 336 ? 29.140 30.001  62.226 1.00 11.33 ? 336  CYS   B O    1 
ATOM   14564 C  CB   . CYS   B 1 336 ? 26.388 31.517  62.966 1.00 10.99 ? 336  CYS   B CB   1 
ATOM   14565 S  SG   . CYS   B 1 336 ? 25.806 32.690  64.222 1.00 14.87 ? 336  CYS   B SG   1 
ATOM   14566 H  H    . CYS   B 1 336 ? 26.736 33.249  61.219 1.00 16.69 ? 336  CYS   B H    1 
ATOM   14567 H  HA   . CYS   B 1 336 ? 28.315 32.204  63.051 1.00 15.73 ? 336  CYS   B HA   1 
ATOM   14568 H  HB2  . CYS   B 1 336 ? 25.720 31.445  62.266 1.00 13.19 ? 336  CYS   B HB2  1 
ATOM   14569 H  HB3  . CYS   B 1 336 ? 26.474 30.638  63.368 1.00 13.19 ? 336  CYS   B HB3  1 
ATOM   14570 H  HG   . CYS   B 1 336 ? 24.637 32.904  64.059 1.00 17.85 ? 336  CYS   B HG   1 
ATOM   14571 N  N    . ASN   B 1 337 ? 27.906 30.478  60.373 1.00 14.01 ? 337  ASN   B N    1 
ATOM   14572 C  CA   . ASN   B 1 337 ? 28.459 29.354  59.574 1.00 12.57 ? 337  ASN   B CA   1 
ATOM   14573 C  C    . ASN   B 1 337 ? 29.936 29.626  59.267 1.00 13.09 ? 337  ASN   B C    1 
ATOM   14574 O  O    . ASN   B 1 337 ? 30.712 28.661  59.233 1.00 12.78 ? 337  ASN   B O    1 
ATOM   14575 C  CB   . ASN   B 1 337 ? 27.673 29.163  58.279 1.00 14.87 ? 337  ASN   B CB   1 
ATOM   14576 C  CG   . ASN   B 1 337 ? 26.319 28.527  58.499 1.00 12.22 ? 337  ASN   B CG   1 
ATOM   14577 O  OD1  . ASN   B 1 337 ? 26.096 27.857  59.503 1.00 12.82 ? 337  ASN   B OD1  1 
ATOM   14578 N  ND2  . ASN   B 1 337 ? 25.413 28.727  57.556 1.00 13.50 ? 337  ASN   B ND2  1 
ATOM   14579 H  H    . ASN   B 1 337 ? 27.313 30.951  59.968 1.00 16.82 ? 337  ASN   B H    1 
ATOM   14580 H  HA   . ASN   B 1 337 ? 28.382 28.536  60.090 1.00 15.08 ? 337  ASN   B HA   1 
ATOM   14581 H  HB2  . ASN   B 1 337 ? 27.554 30.024  57.848 1.00 17.85 ? 337  ASN   B HB2  1 
ATOM   14582 H  HB3  . ASN   B 1 337 ? 28.189 28.611  57.671 1.00 17.85 ? 337  ASN   B HB3  1 
ATOM   14583 H  HD21 . ASN   B 1 337 ? 24.629 28.381  57.632 1.00 16.20 ? 337  ASN   B HD21 1 
ATOM   14584 H  HD22 . ASN   B 1 337 ? 25.608 29.203  56.867 1.00 16.20 ? 337  ASN   B HD22 1 
ATOM   14585 N  N    . GLU   B 1 338 ? 30.303 30.893  59.052 1.00 12.80 ? 338  GLU   B N    1 
ATOM   14586 C  CA   . GLU   B 1 338 ? 31.699 31.240  58.660 1.00 14.20 ? 338  GLU   B CA   1 
ATOM   14587 C  C    . GLU   B 1 338 ? 32.635 31.204  59.873 1.00 13.40 ? 338  GLU   B C    1 
ATOM   14588 O  O    . GLU   B 1 338 ? 33.757 30.696  59.726 1.00 12.15 ? 338  GLU   B O    1 
ATOM   14589 C  CB   . GLU   B 1 338 ? 31.718 32.615  57.992 1.00 13.41 ? 338  GLU   B CB   1 
ATOM   14590 C  CG   . GLU   B 1 338 ? 31.076 32.609  56.621 1.00 14.20 ? 338  GLU   B CG   1 
ATOM   14591 C  CD   . GLU   B 1 338 ? 31.957 32.018  55.536 1.00 16.06 ? 338  GLU   B CD   1 
ATOM   14592 O  OE1  . GLU   B 1 338 ? 32.277 30.819  55.622 1.00 13.34 ? 338  GLU   B OE1  1 
ATOM   14593 O  OE2  . GLU   B 1 338 ? 32.325 32.764  54.615 1.00 19.96 ? 338  GLU   B OE2  1 
ATOM   14594 H  H    . GLU   B 1 338 ? 29.774 31.567  59.124 1.00 15.37 ? 338  GLU   B H    1 
ATOM   14595 H  HA   . GLU   B 1 338 ? 32.020 30.580  58.026 1.00 17.04 ? 338  GLU   B HA   1 
ATOM   14596 H  HB2  . GLU   B 1 338 ? 31.255 33.252  58.559 1.00 16.10 ? 338  GLU   B HB2  1 
ATOM   14597 H  HB3  . GLU   B 1 338 ? 32.636 32.919  57.914 1.00 16.10 ? 338  GLU   B HB3  1 
ATOM   14598 H  HG2  . GLU   B 1 338 ? 30.248 32.106  56.663 1.00 17.05 ? 338  GLU   B HG2  1 
ATOM   14599 H  HG3  . GLU   B 1 338 ? 30.844 33.519  56.378 1.00 17.05 ? 338  GLU   B HG3  1 
ATOM   14600 N  N    . TYR   B 1 339 ? 32.191 31.739  61.015 1.00 15.27 ? 339  TYR   B N    1 
ATOM   14601 C  CA   . TYR   B 1 339 ? 33.017 31.733  62.250 1.00 13.46 ? 339  TYR   B CA   1 
ATOM   14602 C  C    . TYR   B 1 339 ? 32.937 30.351  62.892 1.00 12.80 ? 339  TYR   B C    1 
ATOM   14603 O  O    . TYR   B 1 339 ? 33.844 29.992  63.640 1.00 13.61 ? 339  TYR   B O    1 
ATOM   14604 C  CB   . TYR   B 1 339 ? 32.527 32.774  63.256 1.00 14.07 ? 339  TYR   B CB   1 
ATOM   14605 C  CG   . TYR   B 1 339 ? 32.674 34.207  62.809 1.00 14.45 ? 339  TYR   B CG   1 
ATOM   14606 C  CD1  . TYR   B 1 339 ? 33.840 34.659  62.213 1.00 19.82 ? 339  TYR   B CD1  1 
ATOM   14607 C  CD2  . TYR   B 1 339 ? 31.639 35.110  62.981 1.00 15.04 ? 339  TYR   B CD2  1 
ATOM   14608 C  CE1  . TYR   B 1 339 ? 33.970 35.973  61.799 1.00 19.85 ? 339  TYR   B CE1  1 
ATOM   14609 C  CE2  . TYR   B 1 339 ? 31.751 36.426  62.574 1.00 20.41 ? 339  TYR   B CE2  1 
ATOM   14610 C  CZ   . TYR   B 1 339 ? 32.923 36.857  61.983 1.00 20.19 ? 339  TYR   B CZ   1 
ATOM   14611 O  OH   . TYR   B 1 339 ? 33.041 38.157  61.575 1.00 24.98 ? 339  TYR   B OH   1 
ATOM   14612 H  H    . TYR   B 1 339 ? 31.420 32.110  61.104 1.00 18.32 ? 339  TYR   B H    1 
ATOM   14613 H  HA   . TYR   B 1 339 ? 33.931 31.950  62.006 1.00 16.16 ? 339  TYR   B HA   1 
ATOM   14614 H  HB2  . TYR   B 1 339 ? 31.592 32.603  63.449 1.00 16.89 ? 339  TYR   B HB2  1 
ATOM   14615 H  HB3  . TYR   B 1 339 ? 33.014 32.656  64.087 1.00 16.89 ? 339  TYR   B HB3  1 
ATOM   14616 H  HD1  . TYR   B 1 339 ? 34.548 34.069  62.089 1.00 23.78 ? 339  TYR   B HD1  1 
ATOM   14617 H  HD2  . TYR   B 1 339 ? 30.849 34.824  63.380 1.00 18.05 ? 339  TYR   B HD2  1 
ATOM   14618 H  HE1  . TYR   B 1 339 ? 34.759 36.260  61.399 1.00 23.83 ? 339  TYR   B HE1  1 
ATOM   14619 H  HE2  . TYR   B 1 339 ? 31.043 37.017  62.697 1.00 24.49 ? 339  TYR   B HE2  1 
ATOM   14620 H  HH   . TYR   B 1 339 ? 33.759 38.253  61.150 1.00 29.98 ? 339  TYR   B HH   1 
ATOM   14621 N  N    . GLY   B 1 340 ? 31.856 29.629  62.611 1.00 13.55 ? 340  GLY   B N    1 
ATOM   14622 C  CA   . GLY   B 1 340 ? 31.717 28.264  63.145 1.00 13.50 ? 340  GLY   B CA   1 
ATOM   14623 C  C    . GLY   B 1 340 ? 31.167 28.224  64.558 1.00 12.65 ? 340  GLY   B C    1 
ATOM   14624 O  O    . GLY   B 1 340 ? 31.859 27.651  65.430 1.00 13.27 ? 340  GLY   B O    1 
ATOM   14625 H  H    . GLY   B 1 340 ? 31.201 29.898  62.124 1.00 16.26 ? 340  GLY   B H    1 
ATOM   14626 H  HA2  . GLY   B 1 340 ? 31.132 27.754  62.563 1.00 16.21 ? 340  GLY   B HA2  1 
ATOM   14627 H  HA3  . GLY   B 1 340 ? 32.583 27.828  63.130 1.00 16.21 ? 340  GLY   B HA3  1 
ATOM   14628 N  N    . ILE   B 1 341 ? 29.988 28.813  64.748 1.00 13.48 ? 341  ILE   B N    1 
ATOM   14629 C  CA   . ILE   B 1 341 ? 29.327 28.727  66.076 1.00 11.76 ? 341  ILE   B CA   1 
ATOM   14630 C  C    . ILE   B 1 341 ? 27.892 28.260  65.852 1.00 13.06 ? 341  ILE   B C    1 
ATOM   14631 O  O    . ILE   B 1 341 ? 27.380 28.419  64.736 1.00 11.80 ? 341  ILE   B O    1 
ATOM   14632 C  CB   . ILE   B 1 341 ? 29.341 30.084  66.805 1.00 12.92 ? 341  ILE   B CB   1 
ATOM   14633 C  CG1  . ILE   B 1 341 ? 28.723 31.188  65.945 1.00 12.21 ? 341  ILE   B CG1  1 
ATOM   14634 C  CG2  . ILE   B 1 341 ? 30.740 30.445  67.268 1.00 13.18 ? 341  ILE   B CG2  1 
ATOM   14635 C  CD1  . ILE   B 1 341 ? 28.817 32.563  66.561 1.00 13.24 ? 341  ILE   B CD1  1 
ATOM   14636 H  H    . ILE   B 1 341 ? 29.557 29.256  64.150 1.00 16.17 ? 341  ILE   B H    1 
ATOM   14637 H  HA   . ILE   B 1 341 ? 29.809 28.100  66.638 1.00 14.12 ? 341  ILE   B HA   1 
ATOM   14638 H  HB   . ILE   B 1 341 ? 28.788 29.999  67.598 1.00 15.51 ? 341  ILE   B HB   1 
ATOM   14639 H  HG12 . ILE   B 1 341 ? 29.164 31.199  65.081 1.00 14.66 ? 341  ILE   B HG12 1 
ATOM   14640 H  HG13 . ILE   B 1 341 ? 27.790 30.978  65.785 1.00 14.66 ? 341  ILE   B HG13 1 
ATOM   14641 H  HG21 . ILE   B 1 341 ? 30.720 31.302  67.723 1.00 15.82 ? 341  ILE   B HG21 1 
ATOM   14642 H  HG22 . ILE   B 1 341 ? 31.065 29.764  67.877 1.00 15.82 ? 341  ILE   B HG22 1 
ATOM   14643 H  HG23 . ILE   B 1 341 ? 31.331 30.501  66.501 1.00 15.82 ? 341  ILE   B HG23 1 
ATOM   14644 H  HD11 . ILE   B 1 341 ? 28.409 33.212  65.967 1.00 15.89 ? 341  ILE   B HD11 1 
ATOM   14645 H  HD12 . ILE   B 1 341 ? 28.354 32.568  67.413 1.00 15.89 ? 341  ILE   B HD12 1 
ATOM   14646 H  HD13 . ILE   B 1 341 ? 29.749 32.793  66.699 1.00 15.89 ? 341  ILE   B HD13 1 
ATOM   14647 N  N    . ASP   B 1 342 ? 27.282 27.710  66.892 1.00 14.09 ? 342  ASP   B N    1 
ATOM   14648 C  CA   . ASP   B 1 342 ? 25.861 27.308  66.817 1.00 13.01 ? 342  ASP   B CA   1 
ATOM   14649 C  C    . ASP   B 1 342 ? 25.016 28.586  66.827 1.00 14.60 ? 342  ASP   B C    1 
ATOM   14650 O  O    . ASP   B 1 342 ? 25.177 29.384  67.755 1.00 12.93 ? 342  ASP   B O    1 
ATOM   14651 C  CB   . ASP   B 1 342 ? 25.559 26.380  67.992 1.00 13.03 ? 342  ASP   B CB   1 
ATOM   14652 C  CG   . ASP   B 1 342 ? 24.084 26.223  68.309 1.00 13.75 ? 342  ASP   B CG   1 
ATOM   14653 O  OD1  . ASP   B 1 342 ? 23.281 26.197  67.363 1.00 13.78 ? 342  ASP   B OD1  1 
ATOM   14654 O  OD2  . ASP   B 1 342 ? 23.760 26.111  69.504 1.00 13.90 ? 342  ASP   B OD2  1 
ATOM   14655 H  H    . ASP   B 1 342 ? 27.659 27.557  67.650 1.00 16.91 ? 342  ASP   B H    1 
ATOM   14656 H  HA   . ASP   B 1 342 ? 25.653 26.819  66.006 1.00 15.61 ? 342  ASP   B HA   1 
ATOM   14657 H  HB2  . ASP   B 1 342 ? 25.932 25.505  67.802 1.00 15.64 ? 342  ASP   B HB2  1 
ATOM   14658 H  HB3  . ASP   B 1 342 ? 26.013 26.717  68.780 1.00 15.64 ? 342  ASP   B HB3  1 
ATOM   14659 N  N    . THR   B 1 343 ? 24.163 28.760  65.818 1.00 11.60 ? 343  THR   B N    1 
ATOM   14660 C  CA   . THR   B 1 343 ? 23.303 29.965  65.752 1.00 14.13 ? 343  THR   B CA   1 
ATOM   14661 C  C    . THR   B 1 343 ? 22.427 30.031  67.000 1.00 15.26 ? 343  THR   B C    1 
ATOM   14662 O  O    . THR   B 1 343 ? 22.243 31.137  67.533 1.00 14.91 ? 343  THR   B O    1 
ATOM   14663 C  CB   . THR   B 1 343 ? 22.387 29.925  64.526 1.00 11.62 ? 343  THR   B CB   1 
ATOM   14664 O  OG1  . THR   B 1 343 ? 21.694 28.677  64.515 1.00 11.95 ? 343  THR   B OG1  1 
ATOM   14665 C  CG2  . THR   B 1 343 ? 23.134 30.102  63.222 1.00 11.48 ? 343  THR   B CG2  1 
ATOM   14666 H  H    . THR   B 1 343 ? 24.061 28.207  65.167 1.00 13.93 ? 343  THR   B H    1 
ATOM   14667 H  HA   . THR   B 1 343 ? 23.881 30.742  65.692 1.00 16.96 ? 343  THR   B HA   1 
ATOM   14668 H  HB   . THR   B 1 343 ? 21.769 30.670  64.596 1.00 13.95 ? 343  THR   B HB   1 
ATOM   14669 H  HG1  . THR   B 1 343 ? 21.070 28.708  63.953 1.00 14.35 ? 343  THR   B HG1  1 
ATOM   14670 H  HG21 . THR   B 1 343 ? 22.507 30.068  62.483 1.00 13.78 ? 343  THR   B HG21 1 
ATOM   14671 H  HG22 . THR   B 1 343 ? 23.587 30.960  63.222 1.00 13.78 ? 343  THR   B HG22 1 
ATOM   14672 H  HG23 . THR   B 1 343 ? 23.787 29.392  63.124 1.00 13.78 ? 343  THR   B HG23 1 
ATOM   14673 N  N    . ILE   B 1 344 ? 21.907 28.887  67.430 1.00 12.48 ? 344  ILE   B N    1 
ATOM   14674 C  CA   . ILE   B 1 344 ? 20.929 28.899  68.555 1.00 13.43 ? 344  ILE   B CA   1 
ATOM   14675 C  C    . ILE   B 1 344 ? 21.576 29.478  69.820 1.00 12.65 ? 344  ILE   B C    1 
ATOM   14676 O  O    . ILE   B 1 344 ? 21.029 30.453  70.361 1.00 11.12 ? 344  ILE   B O    1 
ATOM   14677 C  CB   . ILE   B 1 344 ? 20.332 27.495  68.785 1.00 13.14 ? 344  ILE   B CB   1 
ATOM   14678 C  CG1  . ILE   B 1 344 ? 19.674 26.947  67.517 1.00 11.59 ? 344  ILE   B CG1  1 
ATOM   14679 C  CG2  . ILE   B 1 344 ? 19.360 27.509  69.956 1.00 13.97 ? 344  ILE   B CG2  1 
ATOM   14680 C  CD1  . ILE   B 1 344 ? 19.063 25.576  67.685 1.00 11.69 ? 344  ILE   B CD1  1 
ATOM   14681 H  H    . ILE   B 1 344 ? 22.089 28.111  67.108 1.00 14.97 ? 344  ILE   B H    1 
ATOM   14682 H  HA   . ILE   B 1 344 ? 20.188 29.479  68.320 1.00 16.12 ? 344  ILE   B HA   1 
ATOM   14683 H  HB   . ILE   B 1 344 ? 21.061 26.895  69.008 1.00 15.78 ? 344  ILE   B HB   1 
ATOM   14684 H  HG12 . ILE   B 1 344 ? 18.984 27.565  67.229 1.00 13.91 ? 344  ILE   B HG12 1 
ATOM   14685 H  HG13 . ILE   B 1 344 ? 20.337 26.911  66.810 1.00 13.91 ? 344  ILE   B HG13 1 
ATOM   14686 H  HG21 . ILE   B 1 344 ? 18.996 26.619  70.085 1.00 16.77 ? 344  ILE   B HG21 1 
ATOM   14687 H  HG22 . ILE   B 1 344 ? 19.826 27.787  70.760 1.00 16.77 ? 344  ILE   B HG22 1 
ATOM   14688 H  HG23 . ILE   B 1 344 ? 18.638 28.130  69.770 1.00 16.77 ? 344  ILE   B HG23 1 
ATOM   14689 H  HD11 . ILE   B 1 344 ? 18.666 25.293  66.846 1.00 14.03 ? 344  ILE   B HD11 1 
ATOM   14690 H  HD12 . ILE   B 1 344 ? 19.752 24.944  67.946 1.00 14.03 ? 344  ILE   B HD12 1 
ATOM   14691 H  HD13 . ILE   B 1 344 ? 18.378 25.609  68.371 1.00 14.03 ? 344  ILE   B HD13 1 
ATOM   14692 N  N    . THR   B 1 345 ? 22.665 28.884  70.280 1.00 12.82 ? 345  THR   B N    1 
ATOM   14693 C  CA   . THR   B 1 345 ? 23.287 29.375  71.530 1.00 14.41 ? 345  THR   B CA   1 
ATOM   14694 C  C    . THR   B 1 345 ? 23.736 30.833  71.328 1.00 14.87 ? 345  THR   B C    1 
ATOM   14695 O  O    . THR   B 1 345 ? 23.714 31.598  72.303 1.00 12.25 ? 345  THR   B O    1 
ATOM   14696 C  CB   . THR   B 1 345 ? 24.408 28.428  71.975 1.00 11.74 ? 345  THR   B CB   1 
ATOM   14697 O  OG1  . THR   B 1 345 ? 23.806 27.263  72.538 1.00 12.93 ? 345  THR   B OG1  1 
ATOM   14698 C  CG2  . THR   B 1 345 ? 25.351 29.061  72.976 1.00 11.79 ? 345  THR   B CG2  1 
ATOM   14699 H  H    . THR   B 1 345 ? 23.059 28.216  69.908 1.00 15.38 ? 345  THR   B H    1 
ATOM   14700 H  HA   . THR   B 1 345 ? 22.647 29.377  72.259 1.00 17.30 ? 345  THR   B HA   1 
ATOM   14701 H  HB   . THR   B 1 345 ? 24.945 28.206  71.199 1.00 14.09 ? 345  THR   B HB   1 
ATOM   14702 H  HG1  . THR   B 1 345 ? 23.544 27.432  73.318 1.00 15.52 ? 345  THR   B HG1  1 
ATOM   14703 H  HG21 . THR   B 1 345 ? 26.038 28.422  73.223 1.00 14.15 ? 345  THR   B HG21 1 
ATOM   14704 H  HG22 . THR   B 1 345 ? 25.765 29.844  72.580 1.00 14.15 ? 345  THR   B HG22 1 
ATOM   14705 H  HG23 . THR   B 1 345 ? 24.855 29.323  73.767 1.00 14.15 ? 345  THR   B HG23 1 
ATOM   14706 N  N    . CYS   B 1 346 ? 24.130 31.189  70.105 1.00 12.45 ? 346  CYS   B N    1 
ATOM   14707 C  CA   . CYS   B 1 346 ? 24.632 32.566  69.852 1.00 14.10 ? 346  CYS   B CA   1 
ATOM   14708 C  C    . CYS   B 1 346 ? 23.489 33.575  70.028 1.00 13.10 ? 346  CYS   B C    1 
ATOM   14709 O  O    . CYS   B 1 346 ? 23.628 34.479  70.866 1.00 14.27 ? 346  CYS   B O    1 
ATOM   14710 C  CB   . CYS   B 1 346 ? 25.216 32.679  68.449 1.00 14.35 ? 346  CYS   B CB   1 
ATOM   14711 S  SG   . CYS   B 1 346 ? 25.840 34.338  68.071 1.00 14.83 ? 346  CYS   B SG   1 
ATOM   14712 H  H    . CYS   B 1 346 ? 24.120 30.672  69.418 1.00 14.94 ? 346  CYS   B H    1 
ATOM   14713 H  HA   . CYS   B 1 346 ? 25.335 32.761  70.491 1.00 16.92 ? 346  CYS   B HA   1 
ATOM   14714 H  HB2  . CYS   B 1 346 ? 25.938 32.038  68.352 1.00 17.23 ? 346  CYS   B HB2  1 
ATOM   14715 H  HB3  . CYS   B 1 346 ? 24.535 32.440  67.801 1.00 17.23 ? 346  CYS   B HB3  1 
ATOM   14716 H  HG   . CYS   B 1 346 ? 26.285 34.354  66.956 1.00 17.80 ? 346  CYS   B HG   1 
ATOM   14717 N  N    . GLY   B 1 347 ? 22.400 33.401  69.276 1.00 14.89 ? 347  GLY   B N    1 
ATOM   14718 C  CA   . GLY   B 1 347 ? 21.283 34.364  69.330 1.00 15.48 ? 347  GLY   B CA   1 
ATOM   14719 C  C    . GLY   B 1 347 ? 20.640 34.407  70.704 1.00 15.68 ? 347  GLY   B C    1 
ATOM   14720 O  O    . GLY   B 1 347 ? 20.268 35.502  71.144 1.00 13.15 ? 347  GLY   B O    1 
ATOM   14721 H  H    . GLY   B 1 347 ? 22.284 32.744  68.734 1.00 17.87 ? 347  GLY   B H    1 
ATOM   14722 H  HA2  . GLY   B 1 347 ? 21.607 35.248  69.097 1.00 18.58 ? 347  GLY   B HA2  1 
ATOM   14723 H  HA3  . GLY   B 1 347 ? 20.616 34.123  68.668 1.00 18.58 ? 347  GLY   B HA3  1 
ATOM   14724 N  N    . ALA   B 1 348 ? 20.531 33.249  71.361 1.00 14.54 ? 348  ALA   B N    1 
ATOM   14725 C  CA   . ALA   B 1 348 ? 19.855 33.199  72.678 1.00 14.52 ? 348  ALA   B CA   1 
ATOM   14726 C  C    . ALA   B 1 348 ? 20.753 33.785  73.774 1.00 14.11 ? 348  ALA   B C    1 
ATOM   14727 O  O    . ALA   B 1 348 ? 20.214 34.229  74.799 1.00 13.77 ? 348  ALA   B O    1 
ATOM   14728 C  CB   . ALA   B 1 348 ? 19.429 31.786  72.996 1.00 14.87 ? 348  ALA   B CB   1 
ATOM   14729 H  H    . ALA   B 1 348 ? 20.831 32.495  71.076 1.00 17.45 ? 348  ALA   B H    1 
ATOM   14730 H  HA   . ALA   B 1 348 ? 19.055 33.746  72.640 1.00 17.43 ? 348  ALA   B HA   1 
ATOM   14731 H  HB1  . ALA   B 1 348 ? 18.988 31.767  73.860 1.00 17.84 ? 348  ALA   B HB1  1 
ATOM   14732 H  HB2  . ALA   B 1 348 ? 18.816 31.471  72.314 1.00 17.84 ? 348  ALA   B HB2  1 
ATOM   14733 H  HB3  . ALA   B 1 348 ? 20.209 31.210  73.019 1.00 17.84 ? 348  ALA   B HB3  1 
ATOM   14734 N  N    . THR   B 1 349 ? 22.072 33.782  73.566 1.00 13.45 ? 349  THR   B N    1 
ATOM   14735 C  CA   . THR   B 1 349 ? 22.990 34.417  74.548 1.00 13.60 ? 349  THR   B CA   1 
ATOM   14736 C  C    . THR   B 1 349 ? 22.875 35.942  74.394 1.00 14.46 ? 349  THR   B C    1 
ATOM   14737 O  O    . THR   B 1 349 ? 22.909 36.645  75.414 1.00 12.83 ? 349  THR   B O    1 
ATOM   14738 C  CB   . THR   B 1 349 ? 24.421 33.879  74.395 1.00 13.45 ? 349  THR   B CB   1 
ATOM   14739 O  OG1  . THR   B 1 349 ? 24.400 32.478  74.666 1.00 14.07 ? 349  THR   B OG1  1 
ATOM   14740 C  CG2  . THR   B 1 349 ? 25.404 34.570  75.313 1.00 14.95 ? 349  THR   B CG2  1 
ATOM   14741 H  H    . THR   B 1 349 ? 22.458 33.429  72.883 1.00 16.14 ? 349  THR   B H    1 
ATOM   14742 H  HA   . THR   B 1 349 ? 22.737 34.190  75.457 1.00 16.32 ? 349  THR   B HA   1 
ATOM   14743 H  HB   . THR   B 1 349 ? 24.720 34.055  73.489 1.00 16.14 ? 349  THR   B HB   1 
ATOM   14744 H  HG1  . THR   B 1 349 ? 24.267 32.056  73.952 1.00 16.89 ? 349  THR   B HG1  1 
ATOM   14745 H  HG21 . THR   B 1 349 ? 26.289 34.197  75.179 1.00 17.95 ? 349  THR   B HG21 1 
ATOM   14746 H  HG22 . THR   B 1 349 ? 25.420 35.519  75.114 1.00 17.95 ? 349  THR   B HG22 1 
ATOM   14747 H  HG23 . THR   B 1 349 ? 25.134 34.438  76.235 1.00 17.95 ? 349  THR   B HG23 1 
ATOM   14748 N  N    . ILE   B 1 350 ? 22.733 36.419  73.157 1.00 13.18 ? 350  ILE   B N    1 
ATOM   14749 C  CA   . ILE   B 1 350 ? 22.530 37.880  72.934 1.00 14.09 ? 350  ILE   B CA   1 
ATOM   14750 C  C    . ILE   B 1 350 ? 21.193 38.269  73.579 1.00 14.64 ? 350  ILE   B C    1 
ATOM   14751 O  O    . ILE   B 1 350 ? 21.129 39.328  74.216 1.00 14.27 ? 350  ILE   B O    1 
ATOM   14752 C  CB   . ILE   B 1 350 ? 22.576 38.220  71.431 1.00 13.97 ? 350  ILE   B CB   1 
ATOM   14753 C  CG1  . ILE   B 1 350 ? 23.963 37.969  70.833 1.00 15.05 ? 350  ILE   B CG1  1 
ATOM   14754 C  CG2  . ILE   B 1 350 ? 22.107 39.647  71.184 1.00 16.35 ? 350  ILE   B CG2  1 
ATOM   14755 C  CD1  . ILE   B 1 350 ? 23.990 37.995  69.324 1.00 14.81 ? 350  ILE   B CD1  1 
ATOM   14756 H  H    . ILE   B 1 350 ? 22.748 35.940  72.443 1.00 15.82 ? 350  ILE   B H    1 
ATOM   14757 H  HA   . ILE   B 1 350 ? 23.244 38.392  73.344 1.00 16.91 ? 350  ILE   B HA   1 
ATOM   14758 H  HB   . ILE   B 1 350 ? 21.963 37.623  70.975 1.00 16.77 ? 350  ILE   B HB   1 
ATOM   14759 H  HG12 . ILE   B 1 350 ? 24.578 38.639  71.171 1.00 18.06 ? 350  ILE   B HG12 1 
ATOM   14760 H  HG13 . ILE   B 1 350 ? 24.287 37.107  71.139 1.00 18.06 ? 350  ILE   B HG13 1 
ATOM   14761 H  HG21 . ILE   B 1 350 ? 22.144 39.840  70.234 1.00 19.62 ? 350  ILE   B HG21 1 
ATOM   14762 H  HG22 . ILE   B 1 350 ? 21.195 39.747  71.499 1.00 19.62 ? 350  ILE   B HG22 1 
ATOM   14763 H  HG23 . ILE   B 1 350 ? 22.683 40.264  71.661 1.00 19.62 ? 350  ILE   B HG23 1 
ATOM   14764 H  HD11 . ILE   B 1 350 ? 24.894 37.830  69.013 1.00 17.77 ? 350  ILE   B HD11 1 
ATOM   14765 H  HD12 . ILE   B 1 350 ? 23.399 37.308  68.978 1.00 17.77 ? 350  ILE   B HD12 1 
ATOM   14766 H  HD13 . ILE   B 1 350 ? 23.694 38.864  69.010 1.00 17.77 ? 350  ILE   B HD13 1 
ATOM   14767 N  N    . ALA   B 1 351 ? 20.177 37.417  73.418 1.00 15.58 ? 351  ALA   B N    1 
ATOM   14768 C  CA   . ALA   B 1 351 ? 18.860 37.702  74.031 1.00 15.49 ? 351  ALA   B CA   1 
ATOM   14769 C  C    . ALA   B 1 351 ? 19.015 37.814  75.552 1.00 14.62 ? 351  ALA   B C    1 
ATOM   14770 O  O    . ALA   B 1 351 ? 18.447 38.743  76.143 1.00 14.72 ? 351  ALA   B O    1 
ATOM   14771 C  CB   . ALA   B 1 351 ? 17.868 36.629  73.669 1.00 14.27 ? 351  ALA   B CB   1 
ATOM   14772 H  H    . ALA   B 1 351 ? 20.220 36.684  72.970 1.00 18.70 ? 351  ALA   B H    1 
ATOM   14773 H  HA   . ALA   B 1 351 ? 18.524 38.545  73.689 1.00 18.59 ? 351  ALA   B HA   1 
ATOM   14774 H  HB1  . ALA   B 1 351 ? 17.011 36.829  74.077 1.00 17.13 ? 351  ALA   B HB1  1 
ATOM   14775 H  HB2  . ALA   B 1 351 ? 17.766 36.594  72.705 1.00 17.13 ? 351  ALA   B HB2  1 
ATOM   14776 H  HB3  . ALA   B 1 351 ? 18.187 35.771  73.991 1.00 17.13 ? 351  ALA   B HB3  1 
ATOM   14777 N  N    . ALA   B 1 352 ? 19.739 36.876  76.156 1.00 13.33 ? 352  ALA   B N    1 
ATOM   14778 C  CA   . ALA   B 1 352 ? 19.917 36.903  77.625 1.00 14.50 ? 352  ALA   B CA   1 
ATOM   14779 C  C    . ALA   B 1 352 ? 20.605 38.211  78.035 1.00 13.47 ? 352  ALA   B C    1 
ATOM   14780 O  O    . ALA   B 1 352 ? 20.195 38.812  79.036 1.00 14.73 ? 352  ALA   B O    1 
ATOM   14781 C  CB   . ALA   B 1 352 ? 20.707 35.705  78.078 1.00 15.36 ? 352  ALA   B CB   1 
ATOM   14782 H  H    . ALA   B 1 352 ? 20.131 36.225  75.753 1.00 16.00 ? 352  ALA   B H    1 
ATOM   14783 H  HA   . ALA   B 1 352 ? 19.049 36.864  78.056 1.00 17.40 ? 352  ALA   B HA   1 
ATOM   14784 H  HB1  . ALA   B 1 352 ? 20.816 35.735  79.041 1.00 18.43 ? 352  ALA   B HB1  1 
ATOM   14785 H  HB2  . ALA   B 1 352 ? 20.235 34.894  77.831 1.00 18.43 ? 352  ALA   B HB2  1 
ATOM   14786 H  HB3  . ALA   B 1 352 ? 21.579 35.713  77.654 1.00 18.43 ? 352  ALA   B HB3  1 
ATOM   14787 N  N    . ALA   B 1 353 ? 21.625 38.619  77.277 1.00 14.29 ? 353  ALA   B N    1 
ATOM   14788 C  CA   . ALA   B 1 353 ? 22.337 39.880  77.588 1.00 14.87 ? 353  ALA   B CA   1 
ATOM   14789 C  C    . ALA   B 1 353 ? 21.385 41.072  77.433 1.00 14.46 ? 353  ALA   B C    1 
ATOM   14790 O  O    . ALA   B 1 353 ? 21.499 42.019  78.217 1.00 15.37 ? 353  ALA   B O    1 
ATOM   14791 C  CB   . ALA   B 1 353 ? 23.540 40.026  76.689 1.00 20.90 ? 353  ALA   B CB   1 
ATOM   14792 H  H    . ALA   B 1 353 ? 21.922 38.195  76.590 1.00 17.15 ? 353  ALA   B H    1 
ATOM   14793 H  HA   . ALA   B 1 353 ? 22.645 39.857  78.507 1.00 17.85 ? 353  ALA   B HA   1 
ATOM   14794 H  HB1  . ALA   B 1 353 ? 24.002 40.853  76.898 1.00 25.09 ? 353  ALA   B HB1  1 
ATOM   14795 H  HB2  . ALA   B 1 353 ? 24.141 39.277  76.828 1.00 25.09 ? 353  ALA   B HB2  1 
ATOM   14796 H  HB3  . ALA   B 1 353 ? 23.252 40.042  75.763 1.00 25.09 ? 353  ALA   B HB3  1 
ATOM   14797 N  N    . MET   B 1 354 ? 20.504 41.022  76.434 1.00 15.86 ? 354  MET   B N    1 
ATOM   14798 C  CA   . MET   B 1 354 ? 19.527 42.121  76.213 1.00 14.38 ? 354  MET   B CA   1 
ATOM   14799 C  C    . MET   B 1 354 ? 18.573 42.196  77.412 1.00 16.88 ? 354  MET   B C    1 
ATOM   14800 O  O    . MET   B 1 354 ? 18.209 43.313  77.800 1.00 15.98 ? 354  MET   B O    1 
ATOM   14801 C  CB   . MET   B 1 354 ? 18.740 41.897  74.920 1.00 16.40 ? 354  MET   B CB   1 
ATOM   14802 C  CG   . MET   B 1 354 ? 19.567 42.165  73.676 1.00 14.76 ? 354  MET   B CG   1 
ATOM   14803 S  SD   . MET   B 1 354 ? 18.608 42.079  72.146 1.00 15.47 ? 354  MET   B SD   1 
ATOM   14804 C  CE   . MET   B 1 354 ? 19.707 42.942  71.023 1.00 19.12 ? 354  MET   B CE   1 
ATOM   14805 H  H    . MET   B 1 354 ? 20.446 40.373  75.873 1.00 19.04 ? 354  MET   B H    1 
ATOM   14806 H  HA   . MET   B 1 354 ? 20.007 42.959  76.128 1.00 17.26 ? 354  MET   B HA   1 
ATOM   14807 H  HB2  . MET   B 1 354 ? 18.416 40.983  74.897 1.00 19.68 ? 354  MET   B HB2  1 
ATOM   14808 H  HB3  . MET   B 1 354 ? 17.961 42.474  74.916 1.00 19.68 ? 354  MET   B HB3  1 
ATOM   14809 H  HG2  . MET   B 1 354 ? 19.972 43.044  73.748 1.00 17.72 ? 354  MET   B HG2  1 
ATOM   14810 H  HG3  . MET   B 1 354 ? 20.292 41.522  73.632 1.00 17.72 ? 354  MET   B HG3  1 
ATOM   14811 H  HE1  . MET   B 1 354 ? 19.308 42.972  70.139 1.00 22.95 ? 354  MET   B HE1  1 
ATOM   14812 H  HE2  . MET   B 1 354 ? 19.852 43.846  71.343 1.00 22.95 ? 354  MET   B HE2  1 
ATOM   14813 H  HE3  . MET   B 1 354 ? 20.556 42.475  70.978 1.00 22.95 ? 354  MET   B HE3  1 
ATOM   14814 N  N    . GLU   B 1 355 ? 18.208 41.040  77.979 1.00 18.05 ? 355  GLU   B N    1 
ATOM   14815 C  CA   . GLU   B 1 355 ? 17.334 41.043  79.185 1.00 16.32 ? 355  GLU   B CA   1 
ATOM   14816 C  C    . GLU   B 1 355 ? 18.127 41.533  80.406 1.00 14.96 ? 355  GLU   B C    1 
ATOM   14817 O  O    . GLU   B 1 355 ? 17.569 42.317  81.186 1.00 15.40 ? 355  GLU   B O    1 
ATOM   14818 C  CB   . GLU   B 1 355 ? 16.714 39.667  79.447 1.00 17.04 ? 355  GLU   B CB   1 
ATOM   14819 C  CG   . GLU   B 1 355 ? 15.863 39.642  80.706 1.00 16.05 ? 355  GLU   B CG   1 
ATOM   14820 C  CD   . GLU   B 1 355 ? 14.729 38.632  80.728 1.00 17.26 ? 355  GLU   B CD   1 
ATOM   14821 O  OE1  . GLU   B 1 355 ? 14.836 37.610  80.027 1.00 14.46 ? 355  GLU   B OE1  1 
ATOM   14822 O  OE2  . GLU   B 1 355 ? 13.746 38.869  81.457 1.00 16.18 ? 355  GLU   B OE2  1 
ATOM   14823 H  H    . GLU   B 1 355 ? 18.442 40.261  77.699 1.00 21.67 ? 355  GLU   B H    1 
ATOM   14824 H  HA   . GLU   B 1 355 ? 16.599 41.655  79.021 1.00 19.59 ? 355  GLU   B HA   1 
ATOM   14825 H  HB2  . GLU   B 1 355 ? 16.169 39.411  78.687 1.00 20.46 ? 355  GLU   B HB2  1 
ATOM   14826 H  HB3  . GLU   B 1 355 ? 17.420 39.007  79.525 1.00 20.46 ? 355  GLU   B HB3  1 
ATOM   14827 H  HG2  . GLU   B 1 355 ? 16.443 39.466  81.463 1.00 19.27 ? 355  GLU   B HG2  1 
ATOM   14828 H  HG3  . GLU   B 1 355 ? 15.486 40.526  80.837 1.00 19.27 ? 355  GLU   B HG3  1 
ATOM   14829 N  N    . LEU   B 1 356 ? 19.372 41.083  80.564 1.00 15.55 ? 356  LEU   B N    1 
ATOM   14830 C  CA   . LEU   B 1 356 ? 20.219 41.581  81.682 1.00 15.95 ? 356  LEU   B CA   1 
ATOM   14831 C  C    . LEU   B 1 356 ? 20.332 43.110  81.580 1.00 17.80 ? 356  LEU   B C    1 
ATOM   14832 O  O    . LEU   B 1 356 ? 20.252 43.784  82.620 1.00 19.39 ? 356  LEU   B O    1 
ATOM   14833 C  CB   . LEU   B 1 356 ? 21.600 40.920  81.615 1.00 16.67 ? 356  LEU   B CB   1 
ATOM   14834 C  CG   . LEU   B 1 356 ? 21.657 39.452  82.029 1.00 17.35 ? 356  LEU   B CG   1 
ATOM   14835 C  CD1  . LEU   B 1 356 ? 23.062 38.900  81.850 1.00 18.00 ? 356  LEU   B CD1  1 
ATOM   14836 C  CD2  . LEU   B 1 356 ? 21.193 39.278  83.466 1.00 19.25 ? 356  LEU   B CD2  1 
ATOM   14837 H  H    . LEU   B 1 356 ? 19.749 40.503  80.054 1.00 18.67 ? 356  LEU   B H    1 
ATOM   14838 H  HA   . LEU   B 1 356 ? 19.817 41.354  82.535 1.00 19.14 ? 356  LEU   B HA   1 
ATOM   14839 H  HB2  . LEU   B 1 356 ? 21.932 40.995  80.707 1.00 20.00 ? 356  LEU   B HB2  1 
ATOM   14840 H  HB3  . LEU   B 1 356 ? 22.207 41.422  82.181 1.00 20.00 ? 356  LEU   B HB3  1 
ATOM   14841 H  HG   . LEU   B 1 356 ? 21.056 38.952  81.454 1.00 20.83 ? 356  LEU   B HG   1 
ATOM   14842 H  HD11 . LEU   B 1 356 ? 23.080 37.968  82.117 1.00 21.60 ? 356  LEU   B HD11 1 
ATOM   14843 H  HD12 . LEU   B 1 356 ? 23.323 38.974  80.919 1.00 21.60 ? 356  LEU   B HD12 1 
ATOM   14844 H  HD13 . LEU   B 1 356 ? 23.681 39.406  82.400 1.00 21.60 ? 356  LEU   B HD13 1 
ATOM   14845 H  HD21 . LEU   B 1 356 ? 21.237 38.340  83.709 1.00 23.10 ? 356  LEU   B HD21 1 
ATOM   14846 H  HD22 . LEU   B 1 356 ? 21.767 39.791  84.056 1.00 23.10 ? 356  LEU   B HD22 1 
ATOM   14847 H  HD23 . LEU   B 1 356 ? 20.279 39.591  83.551 1.00 23.10 ? 356  LEU   B HD23 1 
ATOM   14848 N  N    . TYR   B 1 357 ? 20.508 43.632  80.366 1.00 16.51 ? 357  TYR   B N    1 
ATOM   14849 C  CA   . TYR   B 1 357 ? 20.574 45.105  80.179 1.00 18.82 ? 357  TYR   B CA   1 
ATOM   14850 C  C    . TYR   B 1 357 ? 19.219 45.732  80.520 1.00 18.11 ? 357  TYR   B C    1 
ATOM   14851 O  O    . TYR   B 1 357 ? 19.178 46.721  81.268 1.00 19.96 ? 357  TYR   B O    1 
ATOM   14852 C  CB   . TYR   B 1 357 ? 20.939 45.474  78.742 1.00 21.83 ? 357  TYR   B CB   1 
ATOM   14853 C  CG   . TYR   B 1 357 ? 20.954 46.962  78.515 1.00 20.38 ? 357  TYR   B CG   1 
ATOM   14854 C  CD1  . TYR   B 1 357 ? 22.016 47.733  78.951 1.00 21.46 ? 357  TYR   B CD1  1 
ATOM   14855 C  CD2  . TYR   B 1 357 ? 19.888 47.604  77.909 1.00 19.76 ? 357  TYR   B CD2  1 
ATOM   14856 C  CE1  . TYR   B 1 357 ? 22.032 49.104  78.770 1.00 24.10 ? 357  TYR   B CE1  1 
ATOM   14857 C  CE2  . TYR   B 1 357 ? 19.886 48.975  77.721 1.00 22.44 ? 357  TYR   B CE2  1 
ATOM   14858 C  CZ   . TYR   B 1 357 ? 20.963 49.727  78.153 1.00 22.45 ? 357  TYR   B CZ   1 
ATOM   14859 O  OH   . TYR   B 1 357 ? 20.976 51.086  77.971 1.00 28.75 ? 357  TYR   B OH   1 
ATOM   14860 H  H    . TYR   B 1 357 ? 20.591 43.171  79.645 1.00 19.81 ? 357  TYR   B H    1 
ATOM   14861 H  HA   . TYR   B 1 357 ? 21.264 45.445  80.770 1.00 22.59 ? 357  TYR   B HA   1 
ATOM   14862 H  HB2  . TYR   B 1 357 ? 21.812 45.109  78.529 1.00 26.20 ? 357  TYR   B HB2  1 
ATOM   14863 H  HB3  . TYR   B 1 357 ? 20.304 45.064  78.135 1.00 26.20 ? 357  TYR   B HB3  1 
ATOM   14864 H  HD1  . TYR   B 1 357 ? 22.734 47.321  79.375 1.00 25.76 ? 357  TYR   B HD1  1 
ATOM   14865 H  HD2  . TYR   B 1 357 ? 19.158 47.104  77.622 1.00 23.71 ? 357  TYR   B HD2  1 
ATOM   14866 H  HE1  . TYR   B 1 357 ? 22.759 49.605  79.062 1.00 28.92 ? 357  TYR   B HE1  1 
ATOM   14867 H  HE2  . TYR   B 1 357 ? 19.164 49.389  77.306 1.00 26.93 ? 357  TYR   B HE2  1 
ATOM   14868 H  HH   . TYR   B 1 357 ? 21.689 51.404  78.281 1.00 34.50 ? 357  TYR   B HH   1 
ATOM   14869 N  N    . GLN   B 1 358 ? 18.149 45.172  79.957 1.00 16.50 ? 358  GLN   B N    1 
ATOM   14870 C  CA   . GLN   B 1 358 ? 16.785 45.684  80.234 1.00 18.58 ? 358  GLN   B CA   1 
ATOM   14871 C  C    . GLN   B 1 358 ? 16.578 45.794  81.746 1.00 18.45 ? 358  GLN   B C    1 
ATOM   14872 O  O    . GLN   B 1 358 ? 15.962 46.791  82.174 1.00 17.78 ? 358  GLN   B O    1 
ATOM   14873 C  CB   . GLN   B 1 358 ? 15.752 44.735  79.624 1.00 17.59 ? 358  GLN   B CB   1 
ATOM   14874 C  CG   . GLN   B 1 358 ? 14.343 44.904  80.171 1.00 17.74 ? 358  GLN   B CG   1 
ATOM   14875 C  CD   . GLN   B 1 358 ? 13.504 43.667  79.966 1.00 18.72 ? 358  GLN   B CD   1 
ATOM   14876 O  OE1  . GLN   B 1 358 ? 13.418 43.124  78.867 1.00 16.68 ? 358  GLN   B OE1  1 
ATOM   14877 N  NE2  . GLN   B 1 358 ? 12.873 43.210  81.035 1.00 18.56 ? 358  GLN   B NE2  1 
ATOM   14878 H  H    . GLN   B 1 358 ? 18.180 44.503  79.417 1.00 19.81 ? 358  GLN   B H    1 
ATOM   14879 H  HA   . GLN   B 1 358 ? 16.678 46.563  79.838 1.00 22.30 ? 358  GLN   B HA   1 
ATOM   14880 H  HB2  . GLN   B 1 358 ? 15.733 44.870  78.664 1.00 21.12 ? 358  GLN   B HB2  1 
ATOM   14881 H  HB3  . GLN   B 1 358 ? 16.039 43.821  79.776 1.00 21.12 ? 358  GLN   B HB3  1 
ATOM   14882 H  HG2  . GLN   B 1 358 ? 14.387 45.110  81.118 1.00 21.29 ? 358  GLN   B HG2  1 
ATOM   14883 H  HG3  . GLN   B 1 358 ? 13.916 45.659  79.736 1.00 21.29 ? 358  GLN   B HG3  1 
ATOM   14884 H  HE21 . GLN   B 1 358 ? 12.956 43.615  81.789 1.00 22.27 ? 358  GLN   B HE21 1 
ATOM   14885 H  HE22 . GLN   B 1 358 ? 12.380 42.508  80.976 1.00 22.27 ? 358  GLN   B HE22 1 
ATOM   14886 N  N    . ARG   B 1 359 ? 17.097 44.839  82.519 1.00 17.06 ? 359  ARG   B N    1 
ATOM   14887 C  CA   . ARG   B 1 359 ? 16.817 44.809  83.982 1.00 17.55 ? 359  ARG   B CA   1 
ATOM   14888 C  C    . ARG   B 1 359 ? 17.919 45.512  84.782 1.00 18.41 ? 359  ARG   B C    1 
ATOM   14889 O  O    . ARG   B 1 359 ? 17.891 45.401  86.017 1.00 18.95 ? 359  ARG   B O    1 
ATOM   14890 C  CB   . ARG   B 1 359 ? 16.566 43.364  84.425 1.00 17.28 ? 359  ARG   B CB   1 
ATOM   14891 C  CG   . ARG   B 1 359 ? 15.387 42.715  83.713 1.00 16.73 ? 359  ARG   B CG   1 
ATOM   14892 C  CD   . ARG   B 1 359 ? 15.137 41.285  84.148 1.00 19.35 ? 359  ARG   B CD   1 
ATOM   14893 N  NE   . ARG   B 1 359 ? 13.941 40.709  83.549 1.00 17.42 ? 359  ARG   B NE   1 
ATOM   14894 C  CZ   . ARG   B 1 359 ? 12.708 40.882  84.009 1.00 22.11 ? 359  ARG   B CZ   1 
ATOM   14895 N  NH1  . ARG   B 1 359 ? 12.514 41.463  85.178 1.00 19.42 ? 359  ARG   B NH1  1 
ATOM   14896 N  NH2  . ARG   B 1 359 ? 11.671 40.475  83.297 1.00 21.16 ? 359  ARG   B NH2  1 
ATOM   14897 H  H    . ARG   B 1 359 ? 17.605 44.206  82.235 1.00 20.47 ? 359  ARG   B H    1 
ATOM   14898 H  HA   . ARG   B 1 359 ? 16.010 45.313  84.168 1.00 21.07 ? 359  ARG   B HA   1 
ATOM   14899 H  HB2  . ARG   B 1 359 ? 17.365 42.838  84.261 1.00 20.74 ? 359  ARG   B HB2  1 
ATOM   14900 H  HB3  . ARG   B 1 359 ? 16.407 43.348  85.382 1.00 20.74 ? 359  ARG   B HB3  1 
ATOM   14901 H  HG2  . ARG   B 1 359 ? 14.589 43.241  83.878 1.00 20.08 ? 359  ARG   B HG2  1 
ATOM   14902 H  HG3  . ARG   B 1 359 ? 15.546 42.732  82.756 1.00 20.08 ? 359  ARG   B HG3  1 
ATOM   14903 H  HD2  . ARG   B 1 359 ? 15.905 40.741  83.912 1.00 23.23 ? 359  ARG   B HD2  1 
ATOM   14904 H  HD3  . ARG   B 1 359 ? 15.055 41.256  85.114 1.00 23.23 ? 359  ARG   B HD3  1 
ATOM   14905 H  HE   . ARG   B 1 359 ? 14.041 40.222  82.847 1.00 20.91 ? 359  ARG   B HE   1 
ATOM   14906 H  HH11 . ARG   B 1 359 ? 13.187 41.730  85.642 1.00 23.31 ? 359  ARG   B HH11 1 
ATOM   14907 H  HH12 . ARG   B 1 359 ? 11.715 41.575  85.475 1.00 23.31 ? 359  ARG   B HH12 1 
ATOM   14908 H  HH21 . ARG   B 1 359 ? 11.795 40.097  82.534 1.00 25.39 ? 359  ARG   B HH21 1 
ATOM   14909 H  HH22 . ARG   B 1 359 ? 10.873 40.588  83.597 1.00 25.39 ? 359  ARG   B HH22 1 
ATOM   14910 N  N    . GLY   B 1 360 ? 18.864 46.172  84.108 1.00 18.61 ? 360  GLY   B N    1 
ATOM   14911 C  CA   . GLY   B 1 360 ? 19.864 46.990  84.825 1.00 19.57 ? 360  GLY   B CA   1 
ATOM   14912 C  C    . GLY   B 1 360 ? 21.063 46.246  85.388 1.00 20.71 ? 360  GLY   B C    1 
ATOM   14913 O  O    . GLY   B 1 360 ? 21.820 46.867  86.144 1.00 21.39 ? 360  GLY   B O    1 
ATOM   14914 H  H    . GLY   B 1 360 ? 18.948 46.164  83.252 1.00 22.34 ? 360  GLY   B H    1 
ATOM   14915 H  HA2  . GLY   B 1 360 ? 20.188 47.675  84.219 1.00 23.48 ? 360  GLY   B HA2  1 
ATOM   14916 H  HA3  . GLY   B 1 360 ? 19.417 47.445  85.556 1.00 23.48 ? 360  GLY   B HA3  1 
ATOM   14917 N  N    . TYR   B 1 361 ? 21.250 44.976  85.024 1.00 20.03 ? 361  TYR   B N    1 
ATOM   14918 C  CA   . TYR   B 1 361 ? 22.425 44.197  85.499 1.00 21.36 ? 361  TYR   B CA   1 
ATOM   14919 C  C    . TYR   B 1 361 ? 23.671 44.622  84.716 1.00 21.08 ? 361  TYR   B C    1 
ATOM   14920 O  O    . TYR   B 1 361 ? 24.768 44.614  85.289 1.00 22.41 ? 361  TYR   B O    1 
ATOM   14921 C  CB   . TYR   B 1 361 ? 22.180 42.696  85.331 1.00 19.52 ? 361  TYR   B CB   1 
ATOM   14922 C  CG   . TYR   B 1 361 ? 21.120 42.149  86.251 1.00 21.95 ? 361  TYR   B CG   1 
ATOM   14923 C  CD1  . TYR   B 1 361 ? 19.777 42.251  85.935 1.00 20.44 ? 361  TYR   B CD1  1 
ATOM   14924 C  CD2  . TYR   B 1 361 ? 21.461 41.550  87.451 1.00 20.80 ? 361  TYR   B CD2  1 
ATOM   14925 C  CE1  . TYR   B 1 361 ? 18.798 41.761  86.782 1.00 19.99 ? 361  TYR   B CE1  1 
ATOM   14926 C  CE2  . TYR   B 1 361 ? 20.495 41.053  88.310 1.00 23.77 ? 361  TYR   B CE2  1 
ATOM   14927 C  CZ   . TYR   B 1 361 ? 19.158 41.160  87.974 1.00 22.14 ? 361  TYR   B CZ   1 
ATOM   14928 O  OH   . TYR   B 1 361 ? 18.200 40.669  88.825 1.00 25.99 ? 361  TYR   B OH   1 
ATOM   14929 H  H    . TYR   B 1 361 ? 20.719 44.540  84.507 1.00 24.04 ? 361  TYR   B H    1 
ATOM   14930 H  HA   . TYR   B 1 361 ? 22.562 44.377  86.442 1.00 25.64 ? 361  TYR   B HA   1 
ATOM   14931 H  HB2  . TYR   B 1 361 ? 21.923 42.519  84.413 1.00 23.43 ? 361  TYR   B HB2  1 
ATOM   14932 H  HB3  . TYR   B 1 361 ? 23.011 42.221  85.489 1.00 23.43 ? 361  TYR   B HB3  1 
ATOM   14933 H  HD1  . TYR   B 1 361 ? 19.527 42.657  85.137 1.00 24.53 ? 361  TYR   B HD1  1 
ATOM   14934 H  HD2  . TYR   B 1 361 ? 22.358 41.480  87.686 1.00 24.96 ? 361  TYR   B HD2  1 
ATOM   14935 H  HE1  . TYR   B 1 361 ? 17.901 41.836  86.550 1.00 23.99 ? 361  TYR   B HE1  1 
ATOM   14936 H  HE2  . TYR   B 1 361 ? 20.745 40.649  89.110 1.00 28.53 ? 361  TYR   B HE2  1 
ATOM   14937 H  HH   . TYR   B 1 361 ? 17.532 40.420  88.381 1.00 31.20 ? 361  TYR   B HH   1 
ATOM   14938 N  N    . ILE   B 1 362 ? 23.487 44.957  83.440 1.00 23.41 ? 362  ILE   B N    1 
ATOM   14939 C  CA   . ILE   B 1 362 ? 24.618 45.428  82.588 1.00 25.63 ? 362  ILE   B CA   1 
ATOM   14940 C  C    . ILE   B 1 362 ? 24.485 46.942  82.407 1.00 28.86 ? 362  ILE   B C    1 
ATOM   14941 O  O    . ILE   B 1 362 ? 23.427 47.387  81.935 1.00 28.07 ? 362  ILE   B O    1 
ATOM   14942 C  CB   . ILE   B 1 362 ? 24.627 44.693  81.233 1.00 23.11 ? 362  ILE   B CB   1 
ATOM   14943 C  CG1  . ILE   B 1 362 ? 24.730 43.177  81.412 1.00 20.57 ? 362  ILE   B CG1  1 
ATOM   14944 C  CG2  . ILE   B 1 362 ? 25.733 45.234  80.340 1.00 20.97 ? 362  ILE   B CG2  1 
ATOM   14945 C  CD1  . ILE   B 1 362 ? 24.520 42.399  80.136 1.00 20.31 ? 362  ILE   B CD1  1 
ATOM   14946 H  H    . ILE   B 1 362 ? 22.727 44.924  83.038 1.00 28.09 ? 362  ILE   B H    1 
ATOM   14947 H  HA   . ILE   B 1 362 ? 25.464 45.229  83.018 1.00 30.76 ? 362  ILE   B HA   1 
ATOM   14948 H  HB   . ILE   B 1 362 ? 23.779 44.863  80.793 1.00 27.74 ? 362  ILE   B HB   1 
ATOM   14949 H  HG12 . ILE   B 1 362 ? 25.604 42.961  81.773 1.00 24.68 ? 362  ILE   B HG12 1 
ATOM   14950 H  HG13 . ILE   B 1 362 ? 24.074 42.892  82.067 1.00 24.68 ? 362  ILE   B HG13 1 
ATOM   14951 H  HG21 . ILE   B 1 362 ? 25.725 44.762  79.493 1.00 25.17 ? 362  ILE   B HG21 1 
ATOM   14952 H  HG22 . ILE   B 1 362 ? 25.589 46.180  80.184 1.00 25.17 ? 362  ILE   B HG22 1 
ATOM   14953 H  HG23 . ILE   B 1 362 ? 26.591 45.105  80.773 1.00 25.17 ? 362  ILE   B HG23 1 
ATOM   14954 H  HD11 . ILE   B 1 362 ? 24.598 41.450  80.319 1.00 24.37 ? 362  ILE   B HD11 1 
ATOM   14955 H  HD12 . ILE   B 1 362 ? 23.636 42.588  79.783 1.00 24.37 ? 362  ILE   B HD12 1 
ATOM   14956 H  HD13 . ILE   B 1 362 ? 25.190 42.658  79.485 1.00 24.37 ? 362  ILE   B HD13 1 
ATOM   14957 N  N    . LYS   B 1 363 ? 25.534 47.691  82.743 1.00 25.29 ? 363  LYS   B N    1 
ATOM   14958 C  CA   . LYS   B 1 363 ? 25.465 49.172  82.677 1.00 27.41 ? 363  LYS   B CA   1 
ATOM   14959 C  C    . LYS   B 1 363 ? 25.969 49.671  81.321 1.00 26.75 ? 363  LYS   B C    1 
ATOM   14960 O  O    . LYS   B 1 363 ? 26.736 48.950  80.670 1.00 25.29 ? 363  LYS   B O    1 
ATOM   14961 C  CB   . LYS   B 1 363 ? 26.294 49.776  83.813 1.00 30.36 ? 363  LYS   B CB   1 
ATOM   14962 C  CG   . LYS   B 1 363 ? 25.756 49.524  85.215 1.00 33.99 ? 363  LYS   B CG   1 
ATOM   14963 C  CD   . LYS   B 1 363 ? 26.621 50.120  86.307 1.00 48.63 ? 363  LYS   B CD   1 
ATOM   14964 C  CE   . LYS   B 1 363 ? 26.076 49.891  87.702 1.00 52.69 ? 363  LYS   B CE   1 
ATOM   14965 N  NZ   . LYS   B 1 363 ? 26.959 50.466  88.743 1.00 58.49 ? 363  LYS   B NZ   1 
ATOM   14966 H  H    . LYS   B 1 363 ? 26.289 47.377  83.009 1.00 30.35 ? 363  LYS   B H    1 
ATOM   14967 H  HA   . LYS   B 1 363 ? 24.541 49.451  82.777 1.00 32.90 ? 363  LYS   B HA   1 
ATOM   14968 H  HB2  . LYS   B 1 363 ? 27.195 49.422  83.760 1.00 36.43 ? 363  LYS   B HB2  1 
ATOM   14969 H  HB3  . LYS   B 1 363 ? 26.357 50.734  83.674 1.00 36.43 ? 363  LYS   B HB3  1 
ATOM   14970 H  HG2  . LYS   B 1 363 ? 24.862 49.893  85.282 1.00 40.79 ? 363  LYS   B HG2  1 
ATOM   14971 H  HG3  . LYS   B 1 363 ? 25.680 48.568  85.358 1.00 40.79 ? 363  LYS   B HG3  1 
ATOM   14972 H  HD2  . LYS   B 1 363 ? 27.511 49.739  86.249 1.00 58.36 ? 363  LYS   B HD2  1 
ATOM   14973 H  HD3  . LYS   B 1 363 ? 26.710 51.074  86.155 1.00 58.36 ? 363  LYS   B HD3  1 
ATOM   14974 H  HE2  . LYS   B 1 363 ? 25.193 50.287  87.773 1.00 63.23 ? 363  LYS   B HE2  1 
ATOM   14975 H  HE3  . LYS   B 1 363 ? 25.973 48.939  87.856 1.00 63.23 ? 363  LYS   B HE3  1 
ATOM   14976 H  HZ1  . LYS   B 1 363 ? 26.609 50.313  89.547 1.00 70.20 ? 363  LYS   B HZ1  1 
ATOM   14977 H  HZ2  . LYS   B 1 363 ? 27.763 50.087  88.693 1.00 70.20 ? 363  LYS   B HZ2  1 
ATOM   14978 H  HZ3  . LYS   B 1 363 ? 27.036 51.343  88.615 1.00 70.20 ? 363  LYS   B HZ3  1 
ATOM   14979 N  N    . ASP   B 1 364 ? 25.541 50.870  80.931 1.00 29.74 ? 364  ASP   B N    1 
ATOM   14980 C  CA   . ASP   B 1 364 ? 25.980 51.471  79.646 1.00 32.46 ? 364  ASP   B CA   1 
ATOM   14981 C  C    . ASP   B 1 364 ? 27.511 51.524  79.580 1.00 28.39 ? 364  ASP   B C    1 
ATOM   14982 O  O    . ASP   B 1 364 ? 28.050 51.397  78.476 1.00 24.98 ? 364  ASP   B O    1 
ATOM   14983 C  CB   . ASP   B 1 364 ? 25.379 52.868  79.489 1.00 32.84 ? 364  ASP   B CB   1 
ATOM   14984 C  CG   . ASP   B 1 364 ? 23.870 52.874  79.339 1.00 31.06 ? 364  ASP   B CG   1 
ATOM   14985 O  OD1  . ASP   B 1 364 ? 23.340 51.924  78.739 1.00 29.45 ? 364  ASP   B OD1  1 
ATOM   14986 O  OD2  . ASP   B 1 364 ? 23.242 53.838  79.814 1.00 33.03 ? 364  ASP   B OD2  1 
ATOM   14987 H  H    . ASP   B 1 364 ? 24.999 51.358  81.386 1.00 35.69 ? 364  ASP   B H    1 
ATOM   14988 H  HA   . ASP   B 1 364 ? 25.665 50.918  78.914 1.00 38.95 ? 364  ASP   B HA   1 
ATOM   14989 H  HB2  . ASP   B 1 364 ? 25.621 53.403  80.261 1.00 39.42 ? 364  ASP   B HB2  1 
ATOM   14990 H  HB3  . ASP   B 1 364 ? 25.774 53.295  78.713 1.00 39.42 ? 364  ASP   B HB3  1 
ATOM   14991 N  N    . GLU   B 1 365 ? 28.173 51.702  80.721 1.00 32.51 ? 365  GLU   B N    1 
ATOM   14992 C  CA   . GLU   B 1 365 ? 29.652 51.868  80.735 1.00 36.78 ? 365  GLU   B CA   1 
ATOM   14993 C  C    . GLU   B 1 365 ? 30.359 50.581  80.302 1.00 31.67 ? 365  GLU   B C    1 
ATOM   14994 O  O    . GLU   B 1 365 ? 31.474 50.680  79.774 1.00 28.90 ? 365  GLU   B O    1 
ATOM   14995 C  CB   . GLU   B 1 365 ? 30.111 52.251  82.139 1.00 37.90 ? 365  GLU   B CB   1 
ATOM   14996 C  CG   . GLU   B 1 365 ? 29.597 51.317  83.213 1.00 47.01 ? 365  GLU   B CG   1 
ATOM   14997 C  CD   . GLU   B 1 365 ? 30.342 51.437  84.529 1.00 57.42 ? 365  GLU   B CD   1 
ATOM   14998 O  OE1  . GLU   B 1 365 ? 31.564 51.189  84.536 1.00 64.04 ? 365  GLU   B OE1  1 
ATOM   14999 O  OE2  . GLU   B 1 365 ? 29.702 51.782  85.540 1.00 48.52 ? 365  GLU   B OE2  1 
ATOM   15000 H  H    . GLU   B 1 365 ? 27.801 51.731  81.496 1.00 39.02 ? 365  GLU   B H    1 
ATOM   15001 H  HA   . GLU   B 1 365 ? 29.883 52.570  80.107 1.00 44.14 ? 365  GLU   B HA   1 
ATOM   15002 H  HB2  . GLU   B 1 365 ? 31.081 52.260  82.164 1.00 45.48 ? 365  GLU   B HB2  1 
ATOM   15003 H  HB3  . GLU   B 1 365 ? 29.814 53.153  82.335 1.00 45.48 ? 365  GLU   B HB3  1 
ATOM   15004 H  HG2  . GLU   B 1 365 ? 28.656 51.498  83.365 1.00 56.42 ? 365  GLU   B HG2  1 
ATOM   15005 H  HG3  . GLU   B 1 365 ? 29.663 50.403  82.895 1.00 56.42 ? 365  GLU   B HG3  1 
ATOM   15006 N  N    . GLU   B 1 366 ? 29.740 49.424  80.529 1.00 26.98 ? 366  GLU   B N    1 
ATOM   15007 C  CA   . GLU   B 1 366 ? 30.425 48.140  80.224 1.00 26.43 ? 366  GLU   B CA   1 
ATOM   15008 C  C    . GLU   B 1 366 ? 30.412 47.880  78.714 1.00 28.43 ? 366  GLU   B C    1 
ATOM   15009 O  O    . GLU   B 1 366 ? 31.270 47.115  78.257 1.00 26.84 ? 366  GLU   B O    1 
ATOM   15010 C  CB   . GLU   B 1 366 ? 29.767 46.985  80.985 1.00 31.58 ? 366  GLU   B CB   1 
ATOM   15011 C  CG   . GLU   B 1 366 ? 29.425 47.313  82.425 1.00 32.41 ? 366  GLU   B CG   1 
ATOM   15012 C  CD   . GLU   B 1 366 ? 28.730 46.185  83.170 1.00 34.96 ? 366  GLU   B CD   1 
ATOM   15013 O  OE1  . GLU   B 1 366 ? 29.166 45.027  83.023 1.00 31.31 ? 366  GLU   B OE1  1 
ATOM   15014 O  OE2  . GLU   B 1 366 ? 27.757 46.468  83.892 1.00 26.42 ? 366  GLU   B OE2  1 
ATOM   15015 H  H    . GLU   B 1 366 ? 28.946 49.347  80.850 1.00 32.39 ? 366  GLU   B H    1 
ATOM   15016 H  HA   . GLU   B 1 366 ? 31.348 48.202  80.515 1.00 31.73 ? 366  GLU   B HA   1 
ATOM   15017 H  HB2  . GLU   B 1 366 ? 28.956 46.724  80.521 1.00 37.90 ? 366  GLU   B HB2  1 
ATOM   15018 H  HB3  . GLU   B 1 366 ? 30.362 46.219  80.970 1.00 37.90 ? 366  GLU   B HB3  1 
ATOM   15019 H  HG2  . GLU   B 1 366 ? 30.241 47.545  82.896 1.00 38.90 ? 366  GLU   B HG2  1 
ATOM   15020 H  HG3  . GLU   B 1 366 ? 28.855 48.098  82.441 1.00 38.90 ? 366  GLU   B HG3  1 
ATOM   15021 N  N    . ILE   B 1 367 ? 29.485 48.490  77.973 1.00 25.40 ? 367  ILE   B N    1 
ATOM   15022 C  CA   . ILE   B 1 367 ? 29.364 48.186  76.514 1.00 23.81 ? 367  ILE   B CA   1 
ATOM   15023 C  C    . ILE   B 1 367 ? 29.630 49.449  75.681 1.00 23.60 ? 367  ILE   B C    1 
ATOM   15024 O  O    . ILE   B 1 367 ? 29.507 49.380  74.450 1.00 25.90 ? 367  ILE   B O    1 
ATOM   15025 C  CB   . ILE   B 1 367 ? 27.984 47.573  76.204 1.00 21.76 ? 367  ILE   B CB   1 
ATOM   15026 C  CG1  . ILE   B 1 367 ? 26.842 48.510  76.606 1.00 24.10 ? 367  ILE   B CG1  1 
ATOM   15027 C  CG2  . ILE   B 1 367 ? 27.845 46.204  76.851 1.00 21.02 ? 367  ILE   B CG2  1 
ATOM   15028 C  CD1  . ILE   B 1 367 ? 25.520 48.173  75.957 1.00 24.57 ? 367  ILE   B CD1  1 
ATOM   15029 H  H    . ILE   B 1 367 ? 28.924 49.069  78.272 1.00 30.48 ? 367  ILE   B H    1 
ATOM   15030 H  HA   . ILE   B 1 367 ? 30.035 47.529  76.271 1.00 28.58 ? 367  ILE   B HA   1 
ATOM   15031 H  HB   . ILE   B 1 367 ? 27.921 47.455  75.243 1.00 26.11 ? 367  ILE   B HB   1 
ATOM   15032 H  HG12 . ILE   B 1 367 ? 26.736 48.482  77.570 1.00 28.93 ? 367  ILE   B HG12 1 
ATOM   15033 H  HG13 . ILE   B 1 367 ? 27.084 49.420  76.373 1.00 28.93 ? 367  ILE   B HG13 1 
ATOM   15034 H  HG21 . ILE   B 1 367 ? 26.972 45.836  76.645 1.00 25.23 ? 367  ILE   B HG21 1 
ATOM   15035 H  HG22 . ILE   B 1 367 ? 28.534 45.613  76.509 1.00 25.23 ? 367  ILE   B HG22 1 
ATOM   15036 H  HG23 . ILE   B 1 367 ? 27.941 46.289  77.813 1.00 25.23 ? 367  ILE   B HG23 1 
ATOM   15037 H  HD11 . ILE   B 1 367 ? 24.844 48.802  76.254 1.00 29.49 ? 367  ILE   B HD11 1 
ATOM   15038 H  HD12 . ILE   B 1 367 ? 25.610 48.226  74.993 1.00 29.49 ? 367  ILE   B HD12 1 
ATOM   15039 H  HD13 . ILE   B 1 367 ? 25.256 47.274  76.208 1.00 29.49 ? 367  ILE   B HD13 1 
ATOM   15040 N  N    . ALA   B 1 368 ? 29.985 50.552  76.338 1.00 24.59 ? 368  ALA   B N    1 
ATOM   15041 C  CA   . ALA   B 1 368 ? 30.252 51.825  75.626 1.00 25.23 ? 368  ALA   B CA   1 
ATOM   15042 C  C    . ALA   B 1 368 ? 31.413 51.647  74.638 1.00 26.68 ? 368  ALA   B C    1 
ATOM   15043 O  O    . ALA   B 1 368 ? 31.273 52.060  73.478 1.00 25.20 ? 368  ALA   B O    1 
ATOM   15044 C  CB   . ALA   B 1 368 ? 30.553 52.899  76.642 1.00 27.30 ? 368  ALA   B CB   1 
ATOM   15045 H  H    . ALA   B 1 368 ? 30.079 50.594  77.192 1.00 29.52 ? 368  ALA   B H    1 
ATOM   15046 H  HA   . ALA   B 1 368 ? 29.472 52.089  75.113 1.00 30.28 ? 368  ALA   B HA   1 
ATOM   15047 H  HB1  . ALA   B 1 368 ? 30.729 53.736  76.185 1.00 32.76 ? 368  ALA   B HB1  1 
ATOM   15048 H  HB2  . ALA   B 1 368 ? 29.792 53.008  77.233 1.00 32.76 ? 368  ALA   B HB2  1 
ATOM   15049 H  HB3  . ALA   B 1 368 ? 31.332 52.644  77.161 1.00 32.76 ? 368  ALA   B HB3  1 
ATOM   15050 N  N    . GLY   B 1 369 ? 32.508 51.046  75.096 1.00 27.96 ? 369  GLY   B N    1 
ATOM   15051 C  CA   . GLY   B 1 369 ? 33.691 50.859  74.234 1.00 25.73 ? 369  GLY   B CA   1 
ATOM   15052 C  C    . GLY   B 1 369 ? 33.413 49.996  73.014 1.00 25.28 ? 369  GLY   B C    1 
ATOM   15053 O  O    . GLY   B 1 369 ? 34.166 50.114  72.036 1.00 27.74 ? 369  GLY   B O    1 
ATOM   15054 H  H    . GLY   B 1 369 ? 32.593 50.739  75.895 1.00 33.56 ? 369  GLY   B H    1 
ATOM   15055 H  HA2  . GLY   B 1 369 ? 34.012 51.727  73.943 1.00 30.88 ? 369  GLY   B HA2  1 
ATOM   15056 H  HA3  . GLY   B 1 369 ? 34.402 50.454  74.754 1.00 30.88 ? 369  GLY   B HA3  1 
ATOM   15057 N  N    . ASP   B 1 370 ? 32.380 49.151  73.069 1.00 22.36 ? 370  ASP   B N    1 
ATOM   15058 C  CA   . ASP   B 1 370 ? 32.051 48.238  71.944 1.00 25.67 ? 370  ASP   B CA   1 
ATOM   15059 C  C    . ASP   B 1 370 ? 31.310 49.001  70.841 1.00 24.06 ? 370  ASP   B C    1 
ATOM   15060 O  O    . ASP   B 1 370 ? 31.212 48.472  69.724 1.00 26.45 ? 370  ASP   B O    1 
ATOM   15061 C  CB   . ASP   B 1 370 ? 31.223 47.049  72.437 1.00 23.80 ? 370  ASP   B CB   1 
ATOM   15062 C  CG   . ASP   B 1 370 ? 31.941 46.189  73.462 1.00 24.89 ? 370  ASP   B CG   1 
ATOM   15063 O  OD1  . ASP   B 1 370 ? 32.675 45.275  73.047 1.00 31.11 ? 370  ASP   B OD1  1 
ATOM   15064 O  OD2  . ASP   B 1 370 ? 31.753 46.434  74.663 1.00 27.08 ? 370  ASP   B OD2  1 
ATOM   15065 H  H    . ASP   B 1 370 ? 31.852 49.084  73.745 1.00 26.84 ? 370  ASP   B H    1 
ATOM   15066 H  HA   . ASP   B 1 370 ? 32.878 47.892  71.574 1.00 30.81 ? 370  ASP   B HA   1 
ATOM   15067 H  HB2  . ASP   B 1 370 ? 30.397 47.379  72.825 1.00 28.56 ? 370  ASP   B HB2  1 
ATOM   15068 H  HB3  . ASP   B 1 370 ? 30.979 46.497  71.677 1.00 28.56 ? 370  ASP   B HB3  1 
ATOM   15069 N  N    . ASN   B 1 371 ? 30.764 50.174  71.167 1.00 22.88 ? 371  ASN   B N    1 
ATOM   15070 C  CA   . ASN   B 1 371 ? 29.993 50.963  70.173 1.00 26.44 ? 371  ASN   B CA   1 
ATOM   15071 C  C    . ASN   B 1 371 ? 28.786 50.147  69.702 1.00 27.90 ? 371  ASN   B C    1 
ATOM   15072 O  O    . ASN   B 1 371 ? 28.382 50.318  68.542 1.00 26.86 ? 371  ASN   B O    1 
ATOM   15073 C  CB   . ASN   B 1 371 ? 30.881 51.436  69.021 1.00 32.52 ? 371  ASN   B CB   1 
ATOM   15074 C  CG   . ASN   B 1 371 ? 32.011 52.318  69.502 1.00 37.45 ? 371  ASN   B CG   1 
ATOM   15075 O  OD1  . ASN   B 1 371 ? 31.796 53.483  69.827 1.00 39.21 ? 371  ASN   B OD1  1 
ATOM   15076 N  ND2  . ASN   B 1 371 ? 33.212 51.768  69.568 1.00 38.18 ? 371  ASN   B ND2  1 
ATOM   15077 H  H    . ASN   B 1 371 ? 30.822 50.535  71.945 1.00 27.46 ? 371  ASN   B H    1 
ATOM   15078 H  HA   . ASN   B 1 371 ? 29.659 51.772  70.592 1.00 31.74 ? 371  ASN   B HA   1 
ATOM   15079 H  HB2  . ASN   B 1 371 ? 31.247 50.666  68.559 1.00 39.03 ? 371  ASN   B HB2  1 
ATOM   15080 H  HB3  . ASN   B 1 371 ? 30.343 51.923  68.378 1.00 39.03 ? 371  ASN   B HB3  1 
ATOM   15081 H  HD21 . ASN   B 1 371 ? 33.882 52.230  69.847 1.00 45.82 ? 371  ASN   B HD21 1 
ATOM   15082 H  HD22 . ASN   B 1 371 ? 33.323 50.949  69.331 1.00 45.82 ? 371  ASN   B HD22 1 
ATOM   15083 N  N    . LEU   B 1 372 ? 28.242 49.298  70.583 1.00 22.60 ? 372  LEU   B N    1 
ATOM   15084 C  CA   . LEU   B 1 372 ? 27.016 48.521  70.263 1.00 22.84 ? 372  LEU   B CA   1 
ATOM   15085 C  C    . LEU   B 1 372 ? 26.058 48.642  71.451 1.00 25.20 ? 372  LEU   B C    1 
ATOM   15086 O  O    . LEU   B 1 372 ? 26.540 48.866  72.571 1.00 24.55 ? 372  LEU   B O    1 
ATOM   15087 C  CB   . LEU   B 1 372 ? 27.373 47.050  70.039 1.00 22.57 ? 372  LEU   B CB   1 
ATOM   15088 C  CG   . LEU   B 1 372 ? 28.349 46.756  68.902 1.00 23.13 ? 372  LEU   B CG   1 
ATOM   15089 C  CD1  . LEU   B 1 372 ? 28.637 45.264  68.827 1.00 21.44 ? 372  LEU   B CD1  1 
ATOM   15090 C  CD2  . LEU   B 1 372 ? 27.803 47.256  67.575 1.00 24.90 ? 372  LEU   B CD2  1 
ATOM   15091 H  H    . LEU   B 1 372 ? 28.560 49.153  71.369 1.00 27.12 ? 372  LEU   B H    1 
ATOM   15092 H  HA   . LEU   B 1 372 ? 26.603 48.865  69.455 1.00 27.41 ? 372  LEU   B HA   1 
ATOM   15093 H  HB2  . LEU   B 1 372 ? 27.749 46.699  70.861 1.00 27.08 ? 372  LEU   B HB2  1 
ATOM   15094 H  HB3  . LEU   B 1 372 ? 26.553 46.560  69.871 1.00 27.08 ? 372  LEU   B HB3  1 
ATOM   15095 H  HG   . LEU   B 1 372 ? 29.178 47.226  69.084 1.00 27.76 ? 372  LEU   B HG   1 
ATOM   15096 H  HD11 . LEU   B 1 372 ? 29.257 45.090  68.102 1.00 25.73 ? 372  LEU   B HD11 1 
ATOM   15097 H  HD12 . LEU   B 1 372 ? 29.027 44.967  69.664 1.00 25.73 ? 372  LEU   B HD12 1 
ATOM   15098 H  HD13 . LEU   B 1 372 ? 27.810 44.782  68.667 1.00 25.73 ? 372  LEU   B HD13 1 
ATOM   15099 H  HD21 . LEU   B 1 372 ? 28.438 47.059  66.869 1.00 29.88 ? 372  LEU   B HD21 1 
ATOM   15100 H  HD22 . LEU   B 1 372 ? 26.961 46.814  67.384 1.00 29.88 ? 372  LEU   B HD22 1 
ATOM   15101 H  HD23 . LEU   B 1 372 ? 27.661 48.214  67.624 1.00 29.88 ? 372  LEU   B HD23 1 
ATOM   15102 N  N    . SER   B 1 373 ? 24.762 48.457  71.205 1.00 20.31 ? 373  SER   B N    1 
ATOM   15103 C  CA   . SER   B 1 373 ? 23.777 48.486  72.314 1.00 19.87 ? 373  SER   B CA   1 
ATOM   15104 C  C    . SER   B 1 373 ? 23.330 47.071  72.674 1.00 18.33 ? 373  SER   B C    1 
ATOM   15105 O  O    . SER   B 1 373 ? 23.706 46.131  71.957 1.00 18.90 ? 373  SER   B O    1 
ATOM   15106 C  CB   . SER   B 1 373 ? 22.570 49.293  71.939 1.00 21.47 ? 373  SER   B CB   1 
ATOM   15107 O  OG   . SER   B 1 373 ? 21.562 48.466  71.382 1.00 19.08 ? 373  SER   B OG   1 
ATOM   15108 H  H    . SER   B 1 373 ? 24.428 48.316  70.425 1.00 24.38 ? 373  SER   B H    1 
ATOM   15109 H  HA   . SER   B 1 373 ? 24.212 48.895  73.078 1.00 23.85 ? 373  SER   B HA   1 
ATOM   15110 H  HB2  . SER   B 1 373 ? 22.224 49.748  72.723 1.00 25.76 ? 373  SER   B HB2  1 
ATOM   15111 H  HB3  . SER   B 1 373 ? 22.820 49.979  71.300 1.00 25.76 ? 373  SER   B HB3  1 
ATOM   15112 H  HG   . SER   B 1 373 ? 21.498 48.618  70.558 1.00 22.90 ? 373  SER   B HG   1 
ATOM   15113 N  N    . LEU   B 1 374 ? 22.558 46.953  73.752 1.00 19.23 ? 374  LEU   B N    1 
ATOM   15114 C  CA   . LEU   B 1 374 ? 21.948 45.655  74.132 1.00 17.73 ? 374  LEU   B CA   1 
ATOM   15115 C  C    . LEU   B 1 374 ? 20.438 45.909  74.172 1.00 19.09 ? 374  LEU   B C    1 
ATOM   15116 O  O    . LEU   B 1 374 ? 19.765 45.373  75.066 1.00 15.72 ? 374  LEU   B O    1 
ATOM   15117 C  CB   . LEU   B 1 374 ? 22.500 45.212  75.486 1.00 17.66 ? 374  LEU   B CB   1 
ATOM   15118 C  CG   . LEU   B 1 374 ? 23.830 44.462  75.424 1.00 18.58 ? 374  LEU   B CG   1 
ATOM   15119 C  CD1  . LEU   B 1 374 ? 24.275 44.021  76.808 1.00 22.74 ? 374  LEU   B CD1  1 
ATOM   15120 C  CD2  . LEU   B 1 374 ? 23.734 43.269  74.485 1.00 20.27 ? 374  LEU   B CD2  1 
ATOM   15121 H  H    . LEU   B 1 374 ? 22.369 47.604  74.282 1.00 23.08 ? 374  LEU   B H    1 
ATOM   15122 H  HA   . LEU   B 1 374 ? 22.151 44.941  73.508 1.00 21.28 ? 374  LEU   B HA   1 
ATOM   15123 H  HB2  . LEU   B 1 374 ? 22.611 45.995  76.047 1.00 21.20 ? 374  LEU   B HB2  1 
ATOM   15124 H  HB3  . LEU   B 1 374 ? 21.843 44.644  75.918 1.00 21.20 ? 374  LEU   B HB3  1 
ATOM   15125 H  HG   . LEU   B 1 374 ? 24.499 45.072  75.075 1.00 22.30 ? 374  LEU   B HG   1 
ATOM   15126 H  HD11 . LEU   B 1 374 ? 25.119 43.548  76.741 1.00 27.29 ? 374  LEU   B HD11 1 
ATOM   15127 H  HD12 . LEU   B 1 374 ? 24.385 44.799  77.376 1.00 27.29 ? 374  LEU   B HD12 1 
ATOM   15128 H  HD13 . LEU   B 1 374 ? 23.605 43.433  77.191 1.00 27.29 ? 374  LEU   B HD13 1 
ATOM   15129 H  HD21 . LEU   B 1 374 ? 24.587 42.807  74.460 1.00 24.33 ? 374  LEU   B HD21 1 
ATOM   15130 H  HD22 . LEU   B 1 374 ? 23.047 42.662  74.802 1.00 24.33 ? 374  LEU   B HD22 1 
ATOM   15131 H  HD23 . LEU   B 1 374 ? 23.507 43.576  73.593 1.00 24.33 ? 374  LEU   B HD23 1 
ATOM   15132 N  N    . LYS   B 1 375 ? 19.948 46.707  73.224 1.00 16.87 ? 375  LYS   B N    1 
ATOM   15133 C  CA   . LYS   B 1 375 ? 18.511 47.076  73.202 1.00 16.29 ? 375  LYS   B CA   1 
ATOM   15134 C  C    . LYS   B 1 375 ? 17.736 46.170  72.242 1.00 17.26 ? 375  LYS   B C    1 
ATOM   15135 O  O    . LYS   B 1 375 ? 18.188 45.980  71.106 1.00 16.34 ? 375  LYS   B O    1 
ATOM   15136 C  CB   . LYS   B 1 375 ? 18.352 48.542  72.789 1.00 18.05 ? 375  LYS   B CB   1 
ATOM   15137 C  CG   . LYS   B 1 375 ? 18.923 49.545  73.781 1.00 22.43 ? 375  LYS   B CG   1 
ATOM   15138 C  CD   . LYS   B 1 375 ? 18.927 50.964  73.260 1.00 27.24 ? 375  LYS   B CD   1 
ATOM   15139 C  CE   . LYS   B 1 375 ? 19.435 51.968  74.273 1.00 35.91 ? 375  LYS   B CE   1 
ATOM   15140 N  NZ   . LYS   B 1 375 ? 20.465 51.383  75.161 1.00 41.09 ? 375  LYS   B NZ   1 
ATOM   15141 H  H    . LYS   B 1 375 ? 20.416 47.047  72.588 1.00 20.25 ? 375  LYS   B H    1 
ATOM   15142 H  HA   . LYS   B 1 375 ? 18.149 46.958  74.094 1.00 19.55 ? 375  LYS   B HA   1 
ATOM   15143 H  HB2  . LYS   B 1 375 ? 18.784 48.673  71.930 1.00 21.67 ? 375  LYS   B HB2  1 
ATOM   15144 H  HB3  . LYS   B 1 375 ? 17.409 48.730  72.664 1.00 21.67 ? 375  LYS   B HB3  1 
ATOM   15145 H  HG2  . LYS   B 1 375 ? 18.406 49.510  74.601 1.00 26.93 ? 375  LYS   B HG2  1 
ATOM   15146 H  HG3  . LYS   B 1 375 ? 19.831 49.287  74.006 1.00 26.93 ? 375  LYS   B HG3  1 
ATOM   15147 H  HD2  . LYS   B 1 375 ? 19.479 51.009  72.464 1.00 32.69 ? 375  LYS   B HD2  1 
ATOM   15148 H  HD3  . LYS   B 1 375 ? 18.026 51.208  72.995 1.00 32.69 ? 375  LYS   B HD3  1 
ATOM   15149 H  HE2  . LYS   B 1 375 ? 19.806 52.735  73.810 1.00 43.10 ? 375  LYS   B HE2  1 
ATOM   15150 H  HE3  . LYS   B 1 375 ? 18.693 52.291  74.808 1.00 43.10 ? 375  LYS   B HE3  1 
ATOM   15151 H  HZ1  . LYS   B 1 375 ? 20.978 52.032  75.489 1.00 49.31 ? 375  LYS   B HZ1  1 
ATOM   15152 H  HZ2  . LYS   B 1 375 ? 20.069 50.951  75.831 1.00 49.31 ? 375  LYS   B HZ2  1 
ATOM   15153 H  HZ3  . LYS   B 1 375 ? 20.968 50.813  74.698 1.00 49.31 ? 375  LYS   B HZ3  1 
ATOM   15154 N  N    . TRP   B 1 376 ? 16.596 45.653  72.700 1.00 18.28 ? 376  TRP   B N    1 
ATOM   15155 C  CA   . TRP   B 1 376 ? 15.738 44.818  71.827 1.00 19.03 ? 376  TRP   B CA   1 
ATOM   15156 C  C    . TRP   B 1 376 ? 15.498 45.543  70.500 1.00 18.64 ? 376  TRP   B C    1 
ATOM   15157 O  O    . TRP   B 1 376 ? 15.272 46.765  70.534 1.00 17.62 ? 376  TRP   B O    1 
ATOM   15158 C  CB   . TRP   B 1 376 ? 14.406 44.517  72.525 1.00 17.86 ? 376  TRP   B CB   1 
ATOM   15159 C  CG   . TRP   B 1 376 ? 14.499 43.921  73.897 1.00 18.04 ? 376  TRP   B CG   1 
ATOM   15160 C  CD1  . TRP   B 1 376 ? 14.175 44.528  75.076 1.00 20.85 ? 376  TRP   B CD1  1 
ATOM   15161 C  CD2  . TRP   B 1 376 ? 14.897 42.580  74.238 1.00 17.03 ? 376  TRP   B CD2  1 
ATOM   15162 N  NE1  . TRP   B 1 376 ? 14.363 43.669  76.125 1.00 17.17 ? 376  TRP   B NE1  1 
ATOM   15163 C  CE2  . TRP   B 1 376 ? 14.806 42.466  75.642 1.00 16.63 ? 376  TRP   B CE2  1 
ATOM   15164 C  CE3  . TRP   B 1 376 ? 15.329 41.472  73.502 1.00 16.03 ? 376  TRP   B CE3  1 
ATOM   15165 C  CZ2  . TRP   B 1 376 ? 15.130 41.291  76.316 1.00 16.80 ? 376  TRP   B CZ2  1 
ATOM   15166 C  CZ3  . TRP   B 1 376 ? 15.652 40.312  74.171 1.00 15.18 ? 376  TRP   B CZ3  1 
ATOM   15167 C  CH2  . TRP   B 1 376 ? 15.552 40.224  75.558 1.00 15.51 ? 376  TRP   B CH2  1 
ATOM   15168 H  H    . TRP   B 1 376 ? 16.297 45.766  73.499 1.00 21.94 ? 376  TRP   B H    1 
ATOM   15169 H  HA   . TRP   B 1 376 ? 16.185 43.976  71.649 1.00 22.84 ? 376  TRP   B HA   1 
ATOM   15170 H  HB2  . TRP   B 1 376 ? 13.899 45.342  72.585 1.00 21.43 ? 376  TRP   B HB2  1 
ATOM   15171 H  HB3  . TRP   B 1 376 ? 13.897 43.912  71.963 1.00 21.43 ? 376  TRP   B HB3  1 
ATOM   15172 H  HD1  . TRP   B 1 376 ? 13.869 45.403  75.155 1.00 25.02 ? 376  TRP   B HD1  1 
ATOM   15173 H  HE1  . TRP   B 1 376 ? 14.225 43.855  76.953 1.00 20.60 ? 376  TRP   B HE1  1 
ATOM   15174 H  HE3  . TRP   B 1 376 ? 15.397 41.518  72.576 1.00 19.24 ? 376  TRP   B HE3  1 
ATOM   15175 H  HZ2  . TRP   B 1 376 ? 15.064 41.230  77.242 1.00 20.17 ? 376  TRP   B HZ2  1 
ATOM   15176 H  HZ3  . TRP   B 1 376 ? 15.943 39.573  73.687 1.00 18.22 ? 376  TRP   B HZ3  1 
ATOM   15177 H  HH2  . TRP   B 1 376 ? 15.776 39.426  75.980 1.00 18.62 ? 376  TRP   B HH2  1 
ATOM   15178 N  N    . GLY   B 1 377 ? 15.548 44.820  69.382 1.00 15.93 ? 377  GLY   B N    1 
ATOM   15179 C  CA   . GLY   B 1 377 ? 15.247 45.426  68.071 1.00 20.38 ? 377  GLY   B CA   1 
ATOM   15180 C  C    . GLY   B 1 377 ? 16.427 46.158  67.448 1.00 18.02 ? 377  GLY   B C    1 
ATOM   15181 O  O    . GLY   B 1 377 ? 16.288 46.586  66.295 1.00 16.65 ? 377  GLY   B O    1 
ATOM   15182 H  H    . GLY   B 1 377 ? 15.751 43.985  69.354 1.00 19.12 ? 377  GLY   B H    1 
ATOM   15183 H  HA2  . GLY   B 1 377 ? 14.951 44.731  67.463 1.00 24.46 ? 377  GLY   B HA2  1 
ATOM   15184 H  HA3  . GLY   B 1 377 ? 14.509 46.047  68.173 1.00 24.46 ? 377  GLY   B HA3  1 
ATOM   15185 N  N    . ASP   B 1 378 ? 17.533 46.305  68.183 1.00 16.06 ? 378  ASP   B N    1 
ATOM   15186 C  CA   . ASP   B 1 378 ? 18.747 46.934  67.592 1.00 18.00 ? 378  ASP   B CA   1 
ATOM   15187 C  C    . ASP   B 1 378 ? 19.442 45.902  66.695 1.00 17.30 ? 378  ASP   B C    1 
ATOM   15188 O  O    . ASP   B 1 378 ? 20.495 45.389  67.097 1.00 16.20 ? 378  ASP   B O    1 
ATOM   15189 C  CB   . ASP   B 1 378 ? 19.663 47.534  68.661 1.00 18.66 ? 378  ASP   B CB   1 
ATOM   15190 C  CG   . ASP   B 1 378 ? 20.788 48.370  68.072 1.00 20.57 ? 378  ASP   B CG   1 
ATOM   15191 O  OD1  . ASP   B 1 378 ? 20.930 48.371  66.835 1.00 21.24 ? 378  ASP   B OD1  1 
ATOM   15192 O  OD2  . ASP   B 1 378 ? 21.510 49.009  68.852 1.00 20.28 ? 378  ASP   B OD2  1 
ATOM   15193 H  H    . ASP   B 1 378 ? 17.612 46.059  69.003 1.00 19.28 ? 378  ASP   B H    1 
ATOM   15194 H  HA   . ASP   B 1 378 ? 18.492 47.691  67.042 1.00 21.61 ? 378  ASP   B HA   1 
ATOM   15195 H  HB2  . ASP   B 1 378 ? 19.136 48.085  69.260 1.00 22.39 ? 378  ASP   B HB2  1 
ATOM   15196 H  HB3  . ASP   B 1 378 ? 20.043 46.818  69.194 1.00 22.39 ? 378  ASP   B HB3  1 
ATOM   15197 N  N    . THR   B 1 379 ? 18.865 45.642  65.523 1.00 18.16 ? 379  THR   B N    1 
ATOM   15198 C  CA   . THR   B 1 379 ? 19.404 44.621  64.588 1.00 15.82 ? 379  THR   B CA   1 
ATOM   15199 C  C    . THR   B 1 379 ? 20.900 44.841  64.344 1.00 18.02 ? 379  THR   B C    1 
ATOM   15200 O  O    . THR   B 1 379 ? 21.657 43.864  64.431 1.00 17.53 ? 379  THR   B O    1 
ATOM   15201 C  CB   . THR   B 1 379 ? 18.596 44.649  63.285 1.00 21.12 ? 379  THR   B CB   1 
ATOM   15202 O  OG1  . THR   B 1 379 ? 17.210 44.539  63.612 1.00 20.10 ? 379  THR   B OG1  1 
ATOM   15203 C  CG2  . THR   B 1 379 ? 18.980 43.541  62.331 1.00 20.44 ? 379  THR   B CG2  1 
ATOM   15204 H  H    . THR   B 1 379 ? 18.158 46.041  65.240 1.00 21.79 ? 379  THR   B H    1 
ATOM   15205 H  HA   . THR   B 1 379 ? 19.314 43.739  64.982 1.00 18.99 ? 379  THR   B HA   1 
ATOM   15206 H  HB   . THR   B 1 379 ? 18.787 45.486  62.833 1.00 25.34 ? 379  THR   B HB   1 
ATOM   15207 H  HG1  . THR   B 1 379 ? 17.069 43.802  63.990 1.00 24.13 ? 379  THR   B HG1  1 
ATOM   15208 H  HG21 . THR   B 1 379 ? 18.441 43.605  61.527 1.00 24.53 ? 379  THR   B HG21 1 
ATOM   15209 H  HG22 . THR   B 1 379 ? 19.918 43.624  62.099 1.00 24.53 ? 379  THR   B HG22 1 
ATOM   15210 H  HG23 . THR   B 1 379 ? 18.828 42.682  62.755 1.00 24.53 ? 379  THR   B HG23 1 
ATOM   15211 N  N    . GLU   B 1 380 ? 21.299 46.080  64.058 1.00 18.86 ? 380  GLU   B N    1 
ATOM   15212 C  CA   . GLU   B 1 380 ? 22.721 46.376  63.736 1.00 19.17 ? 380  GLU   B CA   1 
ATOM   15213 C  C    . GLU   B 1 380 ? 23.633 45.921  64.882 1.00 18.74 ? 380  GLU   B C    1 
ATOM   15214 O  O    . GLU   B 1 380 ? 24.676 45.315  64.596 1.00 20.06 ? 380  GLU   B O    1 
ATOM   15215 C  CB   . GLU   B 1 380 ? 22.886 47.867  63.440 1.00 25.51 ? 380  GLU   B CB   1 
ATOM   15216 C  CG   . GLU   B 1 380 ? 24.295 48.268  63.052 1.00 31.51 ? 380  GLU   B CG   1 
ATOM   15217 C  CD   . GLU   B 1 380 ? 24.405 49.712  62.590 1.00 37.88 ? 380  GLU   B CD   1 
ATOM   15218 O  OE1  . GLU   B 1 380 ? 23.396 50.249  62.097 1.00 32.86 ? 380  GLU   B OE1  1 
ATOM   15219 O  OE2  . GLU   B 1 380 ? 25.496 50.295  62.727 1.00 38.23 ? 380  GLU   B OE2  1 
ATOM   15220 H  H    . GLU   B 1 380 ? 20.778 46.764  64.042 1.00 22.64 ? 380  GLU   B H    1 
ATOM   15221 H  HA   . GLU   B 1 380 ? 22.982 45.882  62.943 1.00 23.01 ? 380  GLU   B HA   1 
ATOM   15222 H  HB2  . GLU   B 1 380 ? 22.281 48.114  62.723 1.00 30.62 ? 380  GLU   B HB2  1 
ATOM   15223 H  HB3  . GLU   B 1 380 ? 22.620 48.374  64.223 1.00 30.62 ? 380  GLU   B HB3  1 
ATOM   15224 H  HG2  . GLU   B 1 380 ? 24.883 48.132  63.811 1.00 37.82 ? 380  GLU   B HG2  1 
ATOM   15225 H  HG3  . GLU   B 1 380 ? 24.607 47.684  62.343 1.00 37.82 ? 380  GLU   B HG3  1 
ATOM   15226 N  N    . SER   B 1 381 ? 23.251 46.207  66.128 1.00 16.90 ? 381  SER   B N    1 
ATOM   15227 C  CA   . SER   B 1 381 ? 24.081 45.825  67.298 1.00 21.04 ? 381  SER   B CA   1 
ATOM   15228 C  C    . SER   B 1 381 ? 24.085 44.299  67.458 1.00 18.54 ? 381  SER   B C    1 
ATOM   15229 O  O    . SER   B 1 381 ? 25.158 43.737  67.713 1.00 16.71 ? 381  SER   B O    1 
ATOM   15230 C  CB   . SER   B 1 381 ? 23.601 46.516  68.549 1.00 19.97 ? 381  SER   B CB   1 
ATOM   15231 O  OG   . SER   B 1 381 ? 23.883 47.905  68.495 1.00 20.47 ? 381  SER   B OG   1 
ATOM   15232 H  H    . SER   B 1 381 ? 22.522 46.618  66.326 1.00 20.29 ? 381  SER   B H    1 
ATOM   15233 H  HA   . SER   B 1 381 ? 24.994 46.116  67.146 1.00 25.25 ? 381  SER   B HA   1 
ATOM   15234 H  HB2  . SER   B 1 381 ? 22.646 46.379  68.654 1.00 23.97 ? 381  SER   B HB2  1 
ATOM   15235 H  HB3  . SER   B 1 381 ? 24.031 46.124  69.325 1.00 23.97 ? 381  SER   B HB3  1 
ATOM   15236 H  HG   . SER   B 1 381 ? 23.224 48.337  68.786 1.00 24.57 ? 381  SER   B HG   1 
ATOM   15237 N  N    . MET   B 1 382 ? 22.916 43.668  67.318 1.00 17.28 ? 382  MET   B N    1 
ATOM   15238 C  CA   . MET   B 1 382 ? 22.813 42.186  67.415 1.00 18.36 ? 382  MET   B CA   1 
ATOM   15239 C  C    . MET   B 1 382 ? 23.833 41.554  66.461 1.00 15.50 ? 382  MET   B C    1 
ATOM   15240 O  O    . MET   B 1 382 ? 24.611 40.686  66.898 1.00 20.08 ? 382  MET   B O    1 
ATOM   15241 C  CB   . MET   B 1 382 ? 21.402 41.732  67.024 1.00 16.10 ? 382  MET   B CB   1 
ATOM   15242 C  CG   . MET   B 1 382 ? 21.187 40.232  67.024 1.00 15.22 ? 382  MET   B CG   1 
ATOM   15243 S  SD   . MET   B 1 382 ? 19.573 39.807  66.306 1.00 16.46 ? 382  MET   B SD   1 
ATOM   15244 C  CE   . MET   B 1 382 ? 19.841 40.254  64.592 1.00 17.20 ? 382  MET   B CE   1 
ATOM   15245 H  H    . MET   B 1 382 ? 22.169 44.067  67.167 1.00 20.74 ? 382  MET   B H    1 
ATOM   15246 H  HA   . MET   B 1 382 ? 22.993 41.908  68.327 1.00 22.03 ? 382  MET   B HA   1 
ATOM   15247 H  HB2  . MET   B 1 382 ? 20.766 42.136  67.635 1.00 19.32 ? 382  MET   B HB2  1 
ATOM   15248 H  HB3  . MET   B 1 382 ? 21.201 42.074  66.139 1.00 19.32 ? 382  MET   B HB3  1 
ATOM   15249 H  HG2  . MET   B 1 382 ? 21.894 39.800  66.519 1.00 18.27 ? 382  MET   B HG2  1 
ATOM   15250 H  HG3  . MET   B 1 382 ? 21.240 39.894  67.932 1.00 18.27 ? 382  MET   B HG3  1 
ATOM   15251 H  HE1  . MET   B 1 382 ? 19.037 40.074  64.081 1.00 20.64 ? 382  MET   B HE1  1 
ATOM   15252 H  HE2  . MET   B 1 382 ? 20.056 41.198  64.533 1.00 20.64 ? 382  MET   B HE2  1 
ATOM   15253 H  HE3  . MET   B 1 382 ? 20.576 39.733  64.232 1.00 20.64 ? 382  MET   B HE3  1 
ATOM   15254 N  N    . ILE   B 1 383 ? 23.827 41.998  65.205 1.00 19.33 ? 383  ILE   B N    1 
ATOM   15255 C  CA   . ILE   B 1 383 ? 24.771 41.434  64.196 1.00 17.72 ? 383  ILE   B CA   1 
ATOM   15256 C  C    . ILE   B 1 383 ? 26.206 41.710  64.655 1.00 18.96 ? 383  ILE   B C    1 
ATOM   15257 O  O    . ILE   B 1 383 ? 27.037 40.795  64.560 1.00 17.72 ? 383  ILE   B O    1 
ATOM   15258 C  CB   . ILE   B 1 383 ? 24.498 42.020  62.797 1.00 19.80 ? 383  ILE   B CB   1 
ATOM   15259 C  CG1  . ILE   B 1 383 ? 23.122 41.612  62.268 1.00 21.47 ? 383  ILE   B CG1  1 
ATOM   15260 C  CG2  . ILE   B 1 383 ? 25.610 41.646  61.828 1.00 24.15 ? 383  ILE   B CG2  1 
ATOM   15261 C  CD1  . ILE   B 1 383 ? 23.050 40.179  61.802 1.00 27.64 ? 383  ILE   B CD1  1 
ATOM   15262 H  H    . ILE   B 1 383 ? 23.302 42.611  64.907 1.00 23.20 ? 383  ILE   B H    1 
ATOM   15263 H  HA   . ILE   B 1 383 ? 24.641 40.475  64.127 1.00 21.26 ? 383  ILE   B HA   1 
ATOM   15264 H  HB   . ILE   B 1 383 ? 24.489 42.987  62.878 1.00 23.76 ? 383  ILE   B HB   1 
ATOM   15265 H  HG12 . ILE   B 1 383 ? 22.462 41.750  62.966 1.00 25.77 ? 383  ILE   B HG12 1 
ATOM   15266 H  HG13 . ILE   B 1 383 ? 22.882 42.195  61.531 1.00 25.77 ? 383  ILE   B HG13 1 
ATOM   15267 H  HG21 . ILE   B 1 383 ? 25.419 42.024  60.955 1.00 28.98 ? 383  ILE   B HG21 1 
ATOM   15268 H  HG22 . ILE   B 1 383 ? 26.454 41.995  62.154 1.00 28.98 ? 383  ILE   B HG22 1 
ATOM   15269 H  HG23 . ILE   B 1 383 ? 25.666 40.680  61.757 1.00 28.98 ? 383  ILE   B HG23 1 
ATOM   15270 H  HD11 . ILE   B 1 383 ? 22.155 39.988  61.481 1.00 33.17 ? 383  ILE   B HD11 1 
ATOM   15271 H  HD12 . ILE   B 1 383 ? 23.687 40.040  61.084 1.00 33.17 ? 383  ILE   B HD12 1 
ATOM   15272 H  HD13 . ILE   B 1 383 ? 23.261 39.587  62.541 1.00 33.17 ? 383  ILE   B HD13 1 
ATOM   15273 N  N    . GLY   B 1 384 ? 26.476 42.920  65.147 1.00 17.46 ? 384  GLY   B N    1 
ATOM   15274 C  CA   . GLY   B 1 384 ? 27.849 43.294  65.537 1.00 18.12 ? 384  GLY   B CA   1 
ATOM   15275 C  C    . GLY   B 1 384 ? 28.407 42.450  66.669 1.00 16.42 ? 384  GLY   B C    1 
ATOM   15276 O  O    . GLY   B 1 384 ? 29.630 42.276  66.726 1.00 20.28 ? 384  GLY   B O    1 
ATOM   15277 H  H    . GLY   B 1 384 ? 25.889 43.537  65.264 1.00 20.95 ? 384  GLY   B H    1 
ATOM   15278 H  HA2  . GLY   B 1 384 ? 28.431 43.212  64.765 1.00 21.75 ? 384  GLY   B HA2  1 
ATOM   15279 H  HA3  . GLY   B 1 384 ? 27.860 44.227  65.803 1.00 21.75 ? 384  GLY   B HA3  1 
ATOM   15280 N  N    . TRP   B 1 385 ? 27.548 41.947  67.555 1.00 18.47 ? 385  TRP   B N    1 
ATOM   15281 C  CA   . TRP   B 1 385 ? 28.048 41.196  68.735 1.00 16.29 ? 385  TRP   B CA   1 
ATOM   15282 C  C    . TRP   B 1 385 ? 28.628 39.845  68.299 1.00 16.16 ? 385  TRP   B C    1 
ATOM   15283 O  O    . TRP   B 1 385 ? 29.490 39.329  69.012 1.00 18.35 ? 385  TRP   B O    1 
ATOM   15284 C  CB   . TRP   B 1 385 ? 26.922 41.003  69.758 1.00 17.05 ? 385  TRP   B CB   1 
ATOM   15285 C  CG   . TRP   B 1 385 ? 26.634 42.225  70.575 1.00 15.56 ? 385  TRP   B CG   1 
ATOM   15286 C  CD1  . TRP   B 1 385 ? 25.464 42.925  70.620 1.00 18.11 ? 385  TRP   B CD1  1 
ATOM   15287 C  CD2  . TRP   B 1 385 ? 27.537 42.896  71.472 1.00 18.82 ? 385  TRP   B CD2  1 
ATOM   15288 N  NE1  . TRP   B 1 385 ? 25.577 43.983  71.480 1.00 18.71 ? 385  TRP   B NE1  1 
ATOM   15289 C  CE2  . TRP   B 1 385 ? 26.836 43.991  72.019 1.00 20.96 ? 385  TRP   B CE2  1 
ATOM   15290 C  CE3  . TRP   B 1 385 ? 28.862 42.682  71.867 1.00 21.24 ? 385  TRP   B CE3  1 
ATOM   15291 C  CZ2  . TRP   B 1 385 ? 27.418 44.865  72.934 1.00 19.30 ? 385  TRP   B CZ2  1 
ATOM   15292 C  CZ3  . TRP   B 1 385 ? 29.436 43.546  72.773 1.00 21.46 ? 385  TRP   B CZ3  1 
ATOM   15293 C  CH2  . TRP   B 1 385 ? 28.722 44.622  73.297 1.00 21.11 ? 385  TRP   B CH2  1 
ATOM   15294 H  H    . TRP   B 1 385 ? 26.693 42.020  67.504 1.00 22.17 ? 385  TRP   B H    1 
ATOM   15295 H  HA   . TRP   B 1 385 ? 28.756 41.708  69.156 1.00 19.55 ? 385  TRP   B HA   1 
ATOM   15296 H  HB2  . TRP   B 1 385 ? 26.114 40.738  69.291 1.00 20.47 ? 385  TRP   B HB2  1 
ATOM   15297 H  HB3  . TRP   B 1 385 ? 27.158 40.274  70.353 1.00 20.47 ? 385  TRP   B HB3  1 
ATOM   15298 H  HD1  . TRP   B 1 385 ? 24.699 42.713  70.135 1.00 21.74 ? 385  TRP   B HD1  1 
ATOM   15299 H  HE1  . TRP   B 1 385 ? 24.956 44.552  71.654 1.00 22.45 ? 385  TRP   B HE1  1 
ATOM   15300 H  HE3  . TRP   B 1 385 ? 29.348 41.967  71.523 1.00 25.49 ? 385  TRP   B HE3  1 
ATOM   15301 H  HZ2  . TRP   B 1 385 ? 26.944 45.584  73.285 1.00 23.17 ? 385  TRP   B HZ2  1 
ATOM   15302 H  HZ3  . TRP   B 1 385 ? 30.316 43.409  73.040 1.00 25.76 ? 385  TRP   B HZ3  1 
ATOM   15303 H  HH2  . TRP   B 1 385 ? 29.137 45.189  73.906 1.00 25.33 ? 385  TRP   B HH2  1 
ATOM   15304 N  N    . ILE   B 1 386 ? 28.164 39.311  67.167 1.00 17.82 ? 386  ILE   B N    1 
ATOM   15305 C  CA   . ILE   B 1 386 ? 28.605 37.952  66.724 1.00 14.51 ? 386  ILE   B CA   1 
ATOM   15306 C  C    . ILE   B 1 386 ? 30.138 37.902  66.680 1.00 16.34 ? 386  ILE   B C    1 
ATOM   15307 O  O    . ILE   B 1 386 ? 30.727 37.090  67.405 1.00 15.75 ? 386  ILE   B O    1 
ATOM   15308 C  CB   . ILE   B 1 386 ? 27.950 37.589  65.375 1.00 14.60 ? 386  ILE   B CB   1 
ATOM   15309 C  CG1  . ILE   B 1 386 ? 26.423 37.557  65.486 1.00 17.78 ? 386  ILE   B CG1  1 
ATOM   15310 C  CG2  . ILE   B 1 386 ? 28.504 36.281  64.834 1.00 16.74 ? 386  ILE   B CG2  1 
ATOM   15311 C  CD1  . ILE   B 1 386 ? 25.716 37.266  64.184 1.00 17.95 ? 386  ILE   B CD1  1 
ATOM   15312 H  H    . ILE   B 1 386 ? 27.604 39.698  66.641 1.00 21.38 ? 386  ILE   B H    1 
ATOM   15313 H  HA   . ILE   B 1 386 ? 28.312 37.281  67.360 1.00 17.41 ? 386  ILE   B HA   1 
ATOM   15314 H  HB   . ILE   B 1 386 ? 28.174 38.285  64.738 1.00 17.53 ? 386  ILE   B HB   1 
ATOM   15315 H  HG12 . ILE   B 1 386 ? 26.170 36.885  66.138 1.00 21.34 ? 386  ILE   B HG12 1 
ATOM   15316 H  HG13 . ILE   B 1 386 ? 26.115 38.412  65.826 1.00 21.34 ? 386  ILE   B HG13 1 
ATOM   15317 H  HG21 . ILE   B 1 386 ? 28.078 36.074  63.987 1.00 20.09 ? 386  ILE   B HG21 1 
ATOM   15318 H  HG22 . ILE   B 1 386 ? 29.461 36.365  64.702 1.00 20.09 ? 386  ILE   B HG22 1 
ATOM   15319 H  HG23 . ILE   B 1 386 ? 28.327 35.568  65.467 1.00 20.09 ? 386  ILE   B HG23 1 
ATOM   15320 H  HD11 . ILE   B 1 386 ? 24.757 37.261  64.330 1.00 21.55 ? 386  ILE   B HD11 1 
ATOM   15321 H  HD12 . ILE   B 1 386 ? 25.940 37.950  63.534 1.00 21.55 ? 386  ILE   B HD12 1 
ATOM   15322 H  HD13 . ILE   B 1 386 ? 25.996 36.399  63.850 1.00 21.55 ? 386  ILE   B HD13 1 
ATOM   15323 N  N    . LYS   B 1 387 ? 30.748 38.780  65.888 1.00 19.80 ? 387  LYS   B N    1 
ATOM   15324 C  CA   . LYS   B 1 387 ? 32.228 38.761  65.751 1.00 19.86 ? 387  LYS   B CA   1 
ATOM   15325 C  C    . LYS   B 1 387 ? 32.891 39.018  67.108 1.00 18.15 ? 387  LYS   B C    1 
ATOM   15326 O  O    . LYS   B 1 387 ? 33.903 38.370  67.396 1.00 18.22 ? 387  LYS   B O    1 
ATOM   15327 C  CB   . LYS   B 1 387 ? 32.680 39.803  64.725 1.00 25.10 ? 387  LYS   B CB   1 
ATOM   15328 C  CG   . LYS   B 1 387 ? 34.187 39.921  64.550 1.00 25.98 ? 387  LYS   B CG   1 
ATOM   15329 C  CD   . LYS   B 1 387 ? 34.587 41.021  63.596 1.00 29.46 ? 387  LYS   B CD   1 
ATOM   15330 C  CE   . LYS   B 1 387 ? 36.043 41.414  63.731 1.00 39.75 ? 387  LYS   B CE   1 
ATOM   15331 N  NZ   . LYS   B 1 387 ? 36.483 42.274  62.607 1.00 49.43 ? 387  LYS   B NZ   1 
ATOM   15332 H  H    . LYS   B 1 387 ? 30.347 39.385  65.427 1.00 23.76 ? 387  LYS   B H    1 
ATOM   15333 H  HA   . LYS   B 1 387 ? 32.500 37.884  65.438 1.00 23.83 ? 387  LYS   B HA   1 
ATOM   15334 H  HB2  . LYS   B 1 387 ? 32.284 39.585  63.867 1.00 30.12 ? 387  LYS   B HB2  1 
ATOM   15335 H  HB3  . LYS   B 1 387 ? 32.330 40.669  64.987 1.00 30.12 ? 387  LYS   B HB3  1 
ATOM   15336 H  HG2  . LYS   B 1 387 ? 34.596 40.085  65.414 1.00 31.18 ? 387  LYS   B HG2  1 
ATOM   15337 H  HG3  . LYS   B 1 387 ? 34.537 39.076  64.226 1.00 31.18 ? 387  LYS   B HG3  1 
ATOM   15338 H  HD2  . LYS   B 1 387 ? 34.417 40.732  62.686 1.00 35.36 ? 387  LYS   B HD2  1 
ATOM   15339 H  HD3  . LYS   B 1 387 ? 34.030 41.799  63.755 1.00 35.36 ? 387  LYS   B HD3  1 
ATOM   15340 H  HE2  . LYS   B 1 387 ? 36.176 41.883  64.569 1.00 47.70 ? 387  LYS   B HE2  1 
ATOM   15341 H  HE3  . LYS   B 1 387 ? 36.593 40.615  63.763 1.00 47.70 ? 387  LYS   B HE3  1 
ATOM   15342 H  HZ1  . LYS   B 1 387 ? 37.340 42.488  62.714 1.00 59.32 ? 387  LYS   B HZ1  1 
ATOM   15343 H  HZ2  . LYS   B 1 387 ? 36.381 41.835  61.839 1.00 59.32 ? 387  LYS   B HZ2  1 
ATOM   15344 H  HZ3  . LYS   B 1 387 ? 35.992 43.016  62.591 1.00 59.32 ? 387  LYS   B HZ3  1 
ATOM   15345 N  N    . ARG   B 1 388 ? 32.340 39.937  67.905 1.00 20.79 ? 388  ARG   B N    1 
ATOM   15346 C  CA   . ARG   B 1 388 ? 32.971 40.302  69.203 1.00 20.39 ? 388  ARG   B CA   1 
ATOM   15347 C  C    . ARG   B 1 388 ? 32.963 39.099  70.159 1.00 19.47 ? 388  ARG   B C    1 
ATOM   15348 O  O    . ARG   B 1 388 ? 33.929 38.938  70.910 1.00 20.09 ? 388  ARG   B O    1 
ATOM   15349 C  CB   . ARG   B 1 388 ? 32.258 41.522  69.799 1.00 22.02 ? 388  ARG   B CB   1 
ATOM   15350 C  CG   . ARG   B 1 388 ? 32.143 42.697  68.838 1.00 24.94 ? 388  ARG   B CG   1 
ATOM   15351 C  CD   . ARG   B 1 388 ? 31.873 44.015  69.539 1.00 29.79 ? 388  ARG   B CD   1 
ATOM   15352 N  NE   . ARG   B 1 388 ? 32.898 44.358  70.512 1.00 28.90 ? 388  ARG   B NE   1 
ATOM   15353 C  CZ   . ARG   B 1 388 ? 34.010 45.026  70.229 1.00 31.34 ? 388  ARG   B CZ   1 
ATOM   15354 N  NH1  . ARG   B 1 388 ? 34.348 45.250  68.973 1.00 31.16 ? 388  ARG   B NH1  1 
ATOM   15355 N  NH2  . ARG   B 1 388 ? 34.785 45.463  71.207 1.00 32.64 ? 388  ARG   B NH2  1 
ATOM   15356 H  H    . ARG   B 1 388 ? 31.613 40.361  67.726 1.00 24.95 ? 388  ARG   B H    1 
ATOM   15357 H  HA   . ARG   B 1 388 ? 33.899 40.543  69.059 1.00 24.48 ? 388  ARG   B HA   1 
ATOM   15358 H  HB2  . ARG   B 1 388 ? 31.369 41.259  70.083 1.00 26.43 ? 388  ARG   B HB2  1 
ATOM   15359 H  HB3  . ARG   B 1 388 ? 32.736 41.810  70.593 1.00 26.43 ? 388  ARG   B HB3  1 
ATOM   15360 H  HG2  . ARG   B 1 388 ? 32.964 42.771  68.327 1.00 29.94 ? 388  ARG   B HG2  1 
ATOM   15361 H  HG3  . ARG   B 1 388 ? 31.429 42.521  68.205 1.00 29.94 ? 388  ARG   B HG3  1 
ATOM   15362 H  HD2  . ARG   B 1 388 ? 31.812 44.722  68.877 1.00 35.75 ? 388  ARG   B HD2  1 
ATOM   15363 H  HD3  . ARG   B 1 388 ? 31.013 43.969  69.985 1.00 35.75 ? 388  ARG   B HD3  1 
ATOM   15364 H  HE   . ARG   B 1 388 ? 32.775 44.111  71.327 1.00 34.69 ? 388  ARG   B HE   1 
ATOM   15365 H  HH11 . ARG   B 1 388 ? 33.847 44.963  68.335 1.00 37.40 ? 388  ARG   B HH11 1 
ATOM   15366 H  HH12 . ARG   B 1 388 ? 35.069 45.683  68.792 1.00 37.40 ? 388  ARG   B HH12 1 
ATOM   15367 H  HH21 . ARG   B 1 388 ? 34.569 45.315  72.026 1.00 39.18 ? 388  ARG   B HH21 1 
ATOM   15368 H  HH22 . ARG   B 1 388 ? 35.505 45.896  71.024 1.00 39.18 ? 388  ARG   B HH22 1 
ATOM   15369 N  N    . MET   B 1 389 ? 31.895 38.297  70.133 1.00 17.45 ? 389  MET   B N    1 
ATOM   15370 C  CA   . MET   B 1 389 ? 31.858 37.077  70.978 1.00 17.17 ? 389  MET   B CA   1 
ATOM   15371 C  C    . MET   B 1 389 ? 32.902 36.082  70.453 1.00 18.59 ? 389  MET   B C    1 
ATOM   15372 O  O    . MET   B 1 389 ? 33.666 35.547  71.260 1.00 18.06 ? 389  MET   B O    1 
ATOM   15373 C  CB   . MET   B 1 389 ? 30.460 36.442  70.955 1.00 19.66 ? 389  MET   B CB   1 
ATOM   15374 C  CG   . MET   B 1 389 ? 29.353 37.389  71.386 1.00 20.35 ? 389  MET   B CG   1 
ATOM   15375 S  SD   . MET   B 1 389 ? 27.700 36.932  70.777 1.00 23.10 ? 389  MET   B SD   1 
ATOM   15376 C  CE   . MET   B 1 389 ? 27.619 35.219  71.295 1.00 18.98 ? 389  MET   B CE   1 
ATOM   15377 H  H    . MET   B 1 389 ? 31.195 38.428  69.650 1.00 20.94 ? 389  MET   B H    1 
ATOM   15378 H  HA   . MET   B 1 389 ? 32.061 37.315  71.896 1.00 20.61 ? 389  MET   B HA   1 
ATOM   15379 H  HB2  . MET   B 1 389 ? 30.272 36.124  70.058 1.00 23.60 ? 389  MET   B HB2  1 
ATOM   15380 H  HB3  . MET   B 1 389 ? 30.456 35.666  71.537 1.00 23.60 ? 389  MET   B HB3  1 
ATOM   15381 H  HG2  . MET   B 1 389 ? 29.331 37.425  72.355 1.00 24.43 ? 389  MET   B HG2  1 
ATOM   15382 H  HG3  . MET   B 1 389 ? 29.566 38.282  71.074 1.00 24.43 ? 389  MET   B HG3  1 
ATOM   15383 H  HE1  . MET   B 1 389 ? 26.767 34.840  71.028 1.00 22.78 ? 389  MET   B HE1  1 
ATOM   15384 H  HE2  . MET   B 1 389 ? 28.339 34.720  70.879 1.00 22.78 ? 389  MET   B HE2  1 
ATOM   15385 H  HE3  . MET   B 1 389 ? 27.707 35.168  72.260 1.00 22.78 ? 389  MET   B HE3  1 
ATOM   15386 N  N    . VAL   B 1 390 ? 32.928 35.875  69.137 1.00 18.32 ? 390  VAL   B N    1 
ATOM   15387 C  CA   . VAL   B 1 390 ? 33.858 34.874  68.531 1.00 15.94 ? 390  VAL   B CA   1 
ATOM   15388 C  C    . VAL   B 1 390 ? 35.306 35.241  68.871 1.00 18.86 ? 390  VAL   B C    1 
ATOM   15389 O  O    . VAL   B 1 390 ? 36.068 34.331  69.218 1.00 17.35 ? 390  VAL   B O    1 
ATOM   15390 C  CB   . VAL   B 1 390 ? 33.641 34.796  67.009 1.00 15.63 ? 390  VAL   B CB   1 
ATOM   15391 C  CG1  . VAL   B 1 390 ? 34.767 34.052  66.306 1.00 16.07 ? 390  VAL   B CG1  1 
ATOM   15392 C  CG2  . VAL   B 1 390 ? 32.291 34.196  66.652 1.00 14.84 ? 390  VAL   B CG2  1 
ATOM   15393 H  H    . VAL   B 1 390 ? 32.429 36.289  68.572 1.00 21.99 ? 390  VAL   B H    1 
ATOM   15394 H  HA   . VAL   B 1 390 ? 33.672 33.997  68.900 1.00 19.14 ? 390  VAL   B HA   1 
ATOM   15395 H  HB   . VAL   B 1 390 ? 33.649 35.711  66.688 1.00 18.75 ? 390  VAL   B HB   1 
ATOM   15396 H  HG11 . VAL   B 1 390 ? 34.592 34.026  65.352 1.00 19.29 ? 390  VAL   B HG11 1 
ATOM   15397 H  HG12 . VAL   B 1 390 ? 35.607 34.509  66.468 1.00 19.29 ? 390  VAL   B HG12 1 
ATOM   15398 H  HG13 . VAL   B 1 390 ? 34.821 33.146  66.649 1.00 19.29 ? 390  VAL   B HG13 1 
ATOM   15399 H  HG21 . VAL   B 1 390 ? 32.195 34.165  65.687 1.00 17.82 ? 390  VAL   B HG21 1 
ATOM   15400 H  HG22 . VAL   B 1 390 ? 32.231 33.297  67.011 1.00 17.82 ? 390  VAL   B HG22 1 
ATOM   15401 H  HG23 . VAL   B 1 390 ? 31.584 34.742  67.029 1.00 17.82 ? 390  VAL   B HG23 1 
ATOM   15402 N  N    . TYR   B 1 391 ? 35.643 36.530  68.809 1.00 17.42 ? 391  TYR   B N    1 
ATOM   15403 C  CA   . TYR   B 1 391 ? 37.052 36.953  69.021 1.00 19.70 ? 391  TYR   B CA   1 
ATOM   15404 C  C    . TYR   B 1 391 ? 37.244 37.526  70.429 1.00 20.54 ? 391  TYR   B C    1 
ATOM   15405 O  O    . TYR   B 1 391 ? 38.317 38.090  70.696 1.00 19.74 ? 391  TYR   B O    1 
ATOM   15406 C  CB   . TYR   B 1 391 ? 37.457 37.945  67.928 1.00 19.18 ? 391  TYR   B CB   1 
ATOM   15407 C  CG   . TYR   B 1 391 ? 37.610 37.317  66.566 1.00 20.67 ? 391  TYR   B CG   1 
ATOM   15408 C  CD1  . TYR   B 1 391 ? 38.771 36.647  66.220 1.00 23.05 ? 391  TYR   B CD1  1 
ATOM   15409 C  CD2  . TYR   B 1 391 ? 36.593 37.377  65.630 1.00 20.81 ? 391  TYR   B CD2  1 
ATOM   15410 C  CE1  . TYR   B 1 391 ? 38.922 36.062  64.975 1.00 24.32 ? 391  TYR   B CE1  1 
ATOM   15411 C  CE2  . TYR   B 1 391 ? 36.728 36.798  64.379 1.00 18.82 ? 391  TYR   B CE2  1 
ATOM   15412 C  CZ   . TYR   B 1 391 ? 37.898 36.138  64.050 1.00 20.06 ? 391  TYR   B CZ   1 
ATOM   15413 O  OH   . TYR   B 1 391 ? 38.046 35.561  62.814 1.00 18.86 ? 391  TYR   B OH   1 
ATOM   15414 H  H    . TYR   B 1 391 ? 35.092 37.171  68.650 1.00 20.90 ? 391  TYR   B H    1 
ATOM   15415 H  HA   . TYR   B 1 391 ? 37.636 36.181  68.956 1.00 23.64 ? 391  TYR   B HA   1 
ATOM   15416 H  HB2  . TYR   B 1 391 ? 36.791 38.649  67.878 1.00 23.02 ? 391  TYR   B HB2  1 
ATOM   15417 H  HB3  . TYR   B 1 391 ? 38.295 38.365  68.178 1.00 23.02 ? 391  TYR   B HB3  1 
ATOM   15418 H  HD1  . TYR   B 1 391 ? 39.464 36.589  66.837 1.00 27.66 ? 391  TYR   B HD1  1 
ATOM   15419 H  HD2  . TYR   B 1 391 ? 35.802 37.816  65.845 1.00 24.98 ? 391  TYR   B HD2  1 
ATOM   15420 H  HE1  . TYR   B 1 391 ? 39.711 35.619  64.761 1.00 29.18 ? 391  TYR   B HE1  1 
ATOM   15421 H  HE2  . TYR   B 1 391 ? 36.034 36.853  63.762 1.00 22.59 ? 391  TYR   B HE2  1 
ATOM   15422 H  HH   . TYR   B 1 391 ? 38.827 35.261  62.736 1.00 22.64 ? 391  TYR   B HH   1 
ATOM   15423 N  N    . SER   B 1 392 ? 36.237 37.376  71.294 1.00 19.76 ? 392  SER   B N    1 
ATOM   15424 C  CA   . SER   B 1 392 ? 36.366 37.832  72.704 1.00 21.74 ? 392  SER   B CA   1 
ATOM   15425 C  C    . SER   B 1 392 ? 36.788 39.308  72.754 1.00 25.48 ? 392  SER   B C    1 
ATOM   15426 O  O    . SER   B 1 392 ? 37.726 39.628  73.501 1.00 24.63 ? 392  SER   B O    1 
ATOM   15427 C  CB   . SER   B 1 392 ? 37.307 36.936  73.468 1.00 20.45 ? 392  SER   B CB   1 
ATOM   15428 O  OG   . SER   B 1 392 ? 36.752 35.639  73.616 1.00 24.32 ? 392  SER   B OG   1 
ATOM   15429 H  H    . SER   B 1 392 ? 35.479 37.020  71.099 1.00 23.72 ? 392  SER   B H    1 
ATOM   15430 H  HA   . SER   B 1 392 ? 35.501 37.768  73.139 1.00 26.09 ? 392  SER   B HA   1 
ATOM   15431 H  HB2  . SER   B 1 392 ? 38.156 36.879  73.003 1.00 24.55 ? 392  SER   B HB2  1 
ATOM   15432 H  HB3  . SER   B 1 392 ? 37.487 37.318  74.341 1.00 24.55 ? 392  SER   B HB3  1 
ATOM   15433 H  HG   . SER   B 1 392 ? 36.928 35.179  72.935 1.00 29.19 ? 392  SER   B HG   1 
ATOM   15434 N  N    . GLU   B 1 393 ? 36.102 40.164  71.994 1.00 21.00 ? 393  GLU   B N    1 
ATOM   15435 C  CA   . GLU   B 1 393 ? 36.404 41.617  71.979 1.00 24.27 ? 393  GLU   B CA   1 
ATOM   15436 C  C    . GLU   B 1 393 ? 35.446 42.363  72.914 1.00 25.01 ? 393  GLU   B C    1 
ATOM   15437 O  O    . GLU   B 1 393 ? 34.225 42.232  72.738 1.00 21.86 ? 393  GLU   B O    1 
ATOM   15438 C  CB   . GLU   B 1 393 ? 36.280 42.165  70.560 1.00 24.32 ? 393  GLU   B CB   1 
ATOM   15439 C  CG   . GLU   B 1 393 ? 37.136 41.413  69.559 1.00 22.98 ? 393  GLU   B CG   1 
ATOM   15440 C  CD   . GLU   B 1 393 ? 36.908 41.794  68.107 1.00 32.56 ? 393  GLU   B CD   1 
ATOM   15441 O  OE1  . GLU   B 1 393 ? 35.744 42.036  67.736 1.00 33.33 ? 393  GLU   B OE1  1 
ATOM   15442 O  OE2  . GLU   B 1 393 ? 37.897 41.844  67.351 1.00 31.52 ? 393  GLU   B OE2  1 
ATOM   15443 H  H    . GLU   B 1 393 ? 35.456 39.932  71.476 1.00 25.20 ? 393  GLU   B H    1 
ATOM   15444 H  HA   . GLU   B 1 393 ? 37.314 41.750  72.288 1.00 29.13 ? 393  GLU   B HA   1 
ATOM   15445 H  HB2  . GLU   B 1 393 ? 35.352 42.122  70.282 1.00 29.19 ? 393  GLU   B HB2  1 
ATOM   15446 H  HB3  . GLU   B 1 393 ? 36.534 43.101  70.557 1.00 29.19 ? 393  GLU   B HB3  1 
ATOM   15447 H  HG2  . GLU   B 1 393 ? 38.070 41.562  69.776 1.00 27.58 ? 393  GLU   B HG2  1 
ATOM   15448 H  HG3  . GLU   B 1 393 ? 36.969 40.463  69.660 1.00 27.58 ? 393  GLU   B HG3  1 
ATOM   15449 N  N    . GLY   B 1 394 ? 35.997 43.133  73.852 1.00 23.46 ? 394  GLY   B N    1 
ATOM   15450 C  CA   . GLY   B 1 394 ? 35.170 43.932  74.773 1.00 24.67 ? 394  GLY   B CA   1 
ATOM   15451 C  C    . GLY   B 1 394 ? 34.173 43.087  75.539 1.00 22.11 ? 394  GLY   B C    1 
ATOM   15452 O  O    . GLY   B 1 394 ? 34.561 42.025  76.043 1.00 23.39 ? 394  GLY   B O    1 
ATOM   15453 H  H    . GLY   B 1 394 ? 36.845 43.210  73.975 1.00 28.16 ? 394  GLY   B H    1 
ATOM   15454 H  HA2  . GLY   B 1 394 ? 35.746 44.396  75.401 1.00 29.61 ? 394  GLY   B HA2  1 
ATOM   15455 H  HA3  . GLY   B 1 394 ? 34.694 44.611  74.269 1.00 29.61 ? 394  GLY   B HA3  1 
ATOM   15456 N  N    . PHE   B 1 395 ? 32.936 43.567  75.629 1.00 24.71 ? 395  PHE   B N    1 
ATOM   15457 C  CA   . PHE   B 1 395 ? 31.896 42.849  76.404 1.00 20.93 ? 395  PHE   B CA   1 
ATOM   15458 C  C    . PHE   B 1 395 ? 31.642 41.479  75.766 1.00 20.95 ? 395  PHE   B C    1 
ATOM   15459 O  O    . PHE   B 1 395 ? 31.142 40.576  76.450 1.00 19.08 ? 395  PHE   B O    1 
ATOM   15460 C  CB   . PHE   B 1 395 ? 30.617 43.686  76.464 1.00 20.67 ? 395  PHE   B CB   1 
ATOM   15461 C  CG   . PHE   B 1 395 ? 29.442 42.949  77.051 1.00 20.46 ? 395  PHE   B CG   1 
ATOM   15462 C  CD1  . PHE   B 1 395 ? 29.397 42.658  78.404 1.00 25.31 ? 395  PHE   B CD1  1 
ATOM   15463 C  CD2  . PHE   B 1 395 ? 28.398 42.522  76.248 1.00 21.76 ? 395  PHE   B CD2  1 
ATOM   15464 C  CE1  . PHE   B 1 395 ? 28.323 41.968  78.945 1.00 24.03 ? 395  PHE   B CE1  1 
ATOM   15465 C  CE2  . PHE   B 1 395 ? 27.325 41.833  76.790 1.00 21.97 ? 395  PHE   B CE2  1 
ATOM   15466 C  CZ   . PHE   B 1 395 ? 27.292 41.557  78.137 1.00 25.10 ? 395  PHE   B CZ   1 
ATOM   15467 H  H    . PHE   B 1 395 ? 32.670 44.296  75.258 1.00 29.65 ? 395  PHE   B H    1 
ATOM   15468 H  HA   . PHE   B 1 395 ? 32.200 42.710  77.315 1.00 25.12 ? 395  PHE   B HA   1 
ATOM   15469 H  HB2  . PHE   B 1 395 ? 30.785 44.483  76.991 1.00 24.81 ? 395  PHE   B HB2  1 
ATOM   15470 H  HB3  . PHE   B 1 395 ? 30.390 43.981  75.568 1.00 24.81 ? 395  PHE   B HB3  1 
ATOM   15471 H  HD1  . PHE   B 1 395 ? 30.095 42.928  78.956 1.00 30.37 ? 395  PHE   B HD1  1 
ATOM   15472 H  HD2  . PHE   B 1 395 ? 28.417 42.700  75.335 1.00 26.11 ? 395  PHE   B HD2  1 
ATOM   15473 H  HE1  . PHE   B 1 395 ? 28.301 41.783  79.856 1.00 28.84 ? 395  PHE   B HE1  1 
ATOM   15474 H  HE2  . PHE   B 1 395 ? 26.626 41.557  76.242 1.00 26.36 ? 395  PHE   B HE2  1 
ATOM   15475 H  HZ   . PHE   B 1 395 ? 26.572 41.093  78.500 1.00 30.13 ? 395  PHE   B HZ   1 
ATOM   15476 N  N    . GLY   B 1 396 ? 31.923 41.371  74.465 1.00 17.90 ? 396  GLY   B N    1 
ATOM   15477 C  CA   . GLY   B 1 396 ? 31.670 40.109  73.745 1.00 21.29 ? 396  GLY   B CA   1 
ATOM   15478 C  C    . GLY   B 1 396 ? 32.336 38.940  74.445 1.00 19.51 ? 396  GLY   B C    1 
ATOM   15479 O  O    . GLY   B 1 396 ? 31.815 37.818  74.362 1.00 18.95 ? 396  GLY   B O    1 
ATOM   15480 H  H    . GLY   B 1 396 ? 32.255 42.002  73.984 1.00 21.49 ? 396  GLY   B H    1 
ATOM   15481 H  HA2  . GLY   B 1 396 ? 30.715 39.953  73.686 1.00 25.56 ? 396  GLY   B HA2  1 
ATOM   15482 H  HA3  . GLY   B 1 396 ? 32.003 40.179  72.837 1.00 25.56 ? 396  GLY   B HA3  1 
ATOM   15483 N  N    . ALA   B 1 397 ? 33.458 39.202  75.116 1.00 20.43 ? 397  ALA   B N    1 
ATOM   15484 C  CA   . ALA   B 1 397 ? 34.196 38.123  75.809 1.00 22.53 ? 397  ALA   B CA   1 
ATOM   15485 C  C    . ALA   B 1 397 ? 33.299 37.457  76.861 1.00 21.53 ? 397  ALA   B C    1 
ATOM   15486 O  O    . ALA   B 1 397 ? 33.514 36.275  77.150 1.00 20.24 ? 397  ALA   B O    1 
ATOM   15487 C  CB   . ALA   B 1 397 ? 35.455 38.675  76.423 1.00 22.08 ? 397  ALA   B CB   1 
ATOM   15488 H  H    . ALA   B 1 397 ? 33.811 39.983  75.186 1.00 24.52 ? 397  ALA   B H    1 
ATOM   15489 H  HA   . ALA   B 1 397 ? 34.450 37.442  75.166 1.00 27.04 ? 397  ALA   B HA   1 
ATOM   15490 H  HB1  . ALA   B 1 397 ? 35.934 37.963  76.875 1.00 26.50 ? 397  ALA   B HB1  1 
ATOM   15491 H  HB2  . ALA   B 1 397 ? 36.017 39.051  75.727 1.00 26.50 ? 397  ALA   B HB2  1 
ATOM   15492 H  HB3  . ALA   B 1 397 ? 35.227 39.368  77.063 1.00 26.50 ? 397  ALA   B HB3  1 
ATOM   15493 N  N    . LYS   B 1 398 ? 32.356 38.213  77.430 1.00 22.09 ? 398  LYS   B N    1 
ATOM   15494 C  CA   . LYS   B 1 398 ? 31.473 37.662  78.495 1.00 19.87 ? 398  LYS   B CA   1 
ATOM   15495 C  C    . LYS   B 1 398 ? 30.363 36.785  77.877 1.00 22.02 ? 398  LYS   B C    1 
ATOM   15496 O  O    . LYS   B 1 398 ? 29.800 35.989  78.603 1.00 18.57 ? 398  LYS   B O    1 
ATOM   15497 C  CB   . LYS   B 1 398 ? 30.899 38.818  79.322 1.00 19.91 ? 398  LYS   B CB   1 
ATOM   15498 C  CG   . LYS   B 1 398 ? 31.917 39.532  80.195 1.00 23.96 ? 398  LYS   B CG   1 
ATOM   15499 C  CD   . LYS   B 1 398 ? 31.279 40.459  81.198 1.00 25.98 ? 398  LYS   B CD   1 
ATOM   15500 C  CE   . LYS   B 1 398 ? 32.255 40.934  82.250 1.00 30.25 ? 398  LYS   B CE   1 
ATOM   15501 N  NZ   . LYS   B 1 398 ? 31.562 41.574  83.393 1.00 33.23 ? 398  LYS   B NZ   1 
ATOM   15502 H  H    . LYS   B 1 398 ? 32.204 39.034  77.226 1.00 26.51 ? 398  LYS   B H    1 
ATOM   15503 H  HA   . LYS   B 1 398 ? 31.987 37.091  79.087 1.00 23.85 ? 398  LYS   B HA   1 
ATOM   15504 H  HB2  . LYS   B 1 398 ? 30.497 39.463  78.720 1.00 23.89 ? 398  LYS   B HB2  1 
ATOM   15505 H  HB3  . LYS   B 1 398 ? 30.189 38.476  79.887 1.00 23.89 ? 398  LYS   B HB3  1 
ATOM   15506 H  HG2  . LYS   B 1 398 ? 32.453 38.874  80.665 1.00 28.76 ? 398  LYS   B HG2  1 
ATOM   15507 H  HG3  . LYS   B 1 398 ? 32.521 40.039  79.631 1.00 28.76 ? 398  LYS   B HG3  1 
ATOM   15508 H  HD2  . LYS   B 1 398 ? 30.909 41.226  80.735 1.00 31.19 ? 398  LYS   B HD2  1 
ATOM   15509 H  HD3  . LYS   B 1 398 ? 30.539 40.004  81.630 1.00 31.19 ? 398  LYS   B HD3  1 
ATOM   15510 H  HE2  . LYS   B 1 398 ? 32.779 40.182  82.569 1.00 36.30 ? 398  LYS   B HE2  1 
ATOM   15511 H  HE3  . LYS   B 1 398 ? 32.876 41.565  81.854 1.00 36.30 ? 398  LYS   B HE3  1 
ATOM   15512 H  HZ1  . LYS   B 1 398 ? 32.162 41.829  83.999 1.00 39.88 ? 398  LYS   B HZ1  1 
ATOM   15513 H  HZ2  . LYS   B 1 398 ? 31.110 42.285  83.106 1.00 39.88 ? 398  LYS   B HZ2  1 
ATOM   15514 H  HZ3  . LYS   B 1 398 ? 30.997 40.993  83.761 1.00 39.88 ? 398  LYS   B HZ3  1 
ATOM   15515 N  N    . MET   B 1 399 ? 30.163 36.890  76.560 1.00 18.25 ? 399  MET   B N    1 
ATOM   15516 C  CA   . MET   B 1 399 ? 29.076 36.148  75.873 1.00 15.71 ? 399  MET   B CA   1 
ATOM   15517 C  C    . MET   B 1 399 ? 29.660 34.943  75.106 1.00 19.45 ? 399  MET   B C    1 
ATOM   15518 O  O    . MET   B 1 399 ? 28.926 34.096  74.706 1.00 14.72 ? 399  MET   B O    1 
ATOM   15519 C  CB   . MET   B 1 399 ? 28.360 37.091  74.900 1.00 17.96 ? 399  MET   B CB   1 
ATOM   15520 C  CG   . MET   B 1 399 ? 27.420 38.076  75.576 1.00 20.09 ? 399  MET   B CG   1 
ATOM   15521 S  SD   . MET   B 1 399 ? 26.286 38.866  74.396 1.00 22.33 ? 399  MET   B SD   1 
ATOM   15522 C  CE   . MET   B 1 399 ? 27.411 40.036  73.642 1.00 18.54 ? 399  MET   B CE   1 
ATOM   15523 H  H    . MET   B 1 399 ? 30.640 37.382  76.040 1.00 21.90 ? 399  MET   B H    1 
ATOM   15524 H  HA   . MET   B 1 399 ? 28.443 35.819  76.531 1.00 18.86 ? 399  MET   B HA   1 
ATOM   15525 H  HB2  . MET   B 1 399 ? 29.024 37.586  74.395 1.00 21.56 ? 399  MET   B HB2  1 
ATOM   15526 H  HB3  . MET   B 1 399 ? 27.856 36.562  74.263 1.00 21.56 ? 399  MET   B HB3  1 
ATOM   15527 H  HG2  . MET   B 1 399 ? 26.906 37.614  76.256 1.00 24.12 ? 399  MET   B HG2  1 
ATOM   15528 H  HG3  . MET   B 1 399 ? 27.940 38.758  76.028 1.00 24.12 ? 399  MET   B HG3  1 
ATOM   15529 H  HE1  . MET   B 1 399 ? 26.940 40.550  72.968 1.00 22.25 ? 399  MET   B HE1  1 
ATOM   15530 H  HE2  . MET   B 1 399 ? 27.758 40.635  74.321 1.00 22.25 ? 399  MET   B HE2  1 
ATOM   15531 H  HE3  . MET   B 1 399 ? 28.146 39.557  73.227 1.00 22.25 ? 399  MET   B HE3  1 
ATOM   15532 N  N    . THR   B 1 400 ? 30.995 34.922  74.980 1.00 18.93 ? 400  THR   B N    1 
ATOM   15533 C  CA   . THR   B 1 400 ? 31.650 33.874  74.147 1.00 16.95 ? 400  THR   B CA   1 
ATOM   15534 C  C    . THR   B 1 400 ? 31.246 32.451  74.543 1.00 17.93 ? 400  THR   B C    1 
ATOM   15535 O  O    . THR   B 1 400 ? 31.129 31.624  73.636 1.00 15.81 ? 400  THR   B O    1 
ATOM   15536 C  CB   . THR   B 1 400 ? 33.173 34.061  74.217 1.00 17.66 ? 400  THR   B CB   1 
ATOM   15537 O  OG1  . THR   B 1 400 ? 33.498 35.392  73.820 1.00 17.61 ? 400  THR   B OG1  1 
ATOM   15538 C  CG2  . THR   B 1 400 ? 33.923 33.071  73.351 1.00 19.38 ? 400  THR   B CG2  1 
ATOM   15539 H  H    . THR   B 1 400 ? 31.532 35.482  75.352 1.00 22.72 ? 400  THR   B H    1 
ATOM   15540 H  HA   . THR   B 1 400 ? 31.345 33.985  73.233 1.00 20.34 ? 400  THR   B HA   1 
ATOM   15541 H  HB   . THR   B 1 400 ? 33.447 33.900  75.133 1.00 21.19 ? 400  THR   B HB   1 
ATOM   15542 H  HG1  . THR   B 1 400 ? 33.275 35.508  73.018 1.00 21.14 ? 400  THR   B HG1  1 
ATOM   15543 H  HG21 . THR   B 1 400 ? 34.877 33.230  73.429 1.00 23.26 ? 400  THR   B HG21 1 
ATOM   15544 H  HG22 . THR   B 1 400 ? 33.721 32.168  73.642 1.00 23.26 ? 400  THR   B HG22 1 
ATOM   15545 H  HG23 . THR   B 1 400 ? 33.653 33.180  72.426 1.00 23.26 ? 400  THR   B HG23 1 
ATOM   15546 N  N    . ASN   B 1 401 ? 31.039 32.186  75.835 1.00 15.01 ? 401  ASN   B N    1 
ATOM   15547 C  CA   . ASN   B 1 401 ? 30.799 30.782  76.269 1.00 17.07 ? 401  ASN   B CA   1 
ATOM   15548 C  C    . ASN   B 1 401 ? 29.335 30.520  76.640 1.00 14.26 ? 401  ASN   B C    1 
ATOM   15549 O  O    . ASN   B 1 401 ? 29.080 29.519  77.320 1.00 14.46 ? 401  ASN   B O    1 
ATOM   15550 C  CB   . ASN   B 1 401 ? 31.747 30.376  77.394 1.00 15.90 ? 401  ASN   B CB   1 
ATOM   15551 C  CG   . ASN   B 1 401 ? 33.190 30.323  76.942 1.00 16.31 ? 401  ASN   B CG   1 
ATOM   15552 O  OD1  . ASN   B 1 401 ? 33.469 30.089  75.770 1.00 15.83 ? 401  ASN   B OD1  1 
ATOM   15553 N  ND2  . ASN   B 1 401 ? 34.112 30.540  77.864 1.00 25.80 ? 401  ASN   B ND2  1 
ATOM   15554 H  H    . ASN   B 1 401 ? 31.031 32.773  76.464 1.00 18.01 ? 401  ASN   B H    1 
ATOM   15555 H  HA   . ASN   B 1 401 ? 30.991 30.219  75.503 1.00 20.48 ? 401  ASN   B HA   1 
ATOM   15556 H  HB2  . ASN   B 1 401 ? 31.663 31.006  78.127 1.00 19.09 ? 401  ASN   B HB2  1 
ATOM   15557 H  HB3  . ASN   B 1 401 ? 31.486 29.507  77.736 1.00 19.09 ? 401  ASN   B HB3  1 
ATOM   15558 H  HD21 . ASN   B 1 401 ? 34.945 30.520  77.652 1.00 30.96 ? 401  ASN   B HD21 1 
ATOM   15559 H  HD22 . ASN   B 1 401 ? 33.879 30.701  78.676 1.00 30.96 ? 401  ASN   B HD22 1 
ATOM   15560 N  N    . GLY   B 1 402 ? 28.417 31.384  76.213 1.00 16.04 ? 402  GLY   B N    1 
ATOM   15561 C  CA   . GLY   B 1 402 ? 26.993 31.056  76.425 1.00 14.61 ? 402  GLY   B CA   1 
ATOM   15562 C  C    . GLY   B 1 402 ? 26.276 31.844  77.506 1.00 13.51 ? 402  GLY   B C    1 
ATOM   15563 O  O    . GLY   B 1 402 ? 26.952 32.456  78.339 1.00 16.77 ? 402  GLY   B O    1 
ATOM   15564 H  H    . GLY   B 1 402 ? 28.577 32.131  75.817 1.00 19.25 ? 402  GLY   B H    1 
ATOM   15565 H  HA2  . GLY   B 1 402 ? 26.522 31.189  75.588 1.00 17.53 ? 402  GLY   B HA2  1 
ATOM   15566 H  HA3  . GLY   B 1 402 ? 26.927 30.113  76.641 1.00 17.53 ? 402  GLY   B HA3  1 
ATOM   15567 N  N    . SER   B 1 403 ? 24.946 31.765  77.502 1.00 13.48 ? 403  SER   B N    1 
ATOM   15568 C  CA   . SER   B 1 403 ? 24.113 32.537  78.459 1.00 14.98 ? 403  SER   B CA   1 
ATOM   15569 C  C    . SER   B 1 403 ? 24.267 32.013  79.887 1.00 14.31 ? 403  SER   B C    1 
ATOM   15570 O  O    . SER   B 1 403 ? 24.203 32.829  80.819 1.00 13.99 ? 403  SER   B O    1 
ATOM   15571 C  CB   . SER   B 1 403 ? 22.679 32.474  78.032 1.00 12.72 ? 403  SER   B CB   1 
ATOM   15572 O  OG   . SER   B 1 403 ? 22.148 31.176  78.234 1.00 16.58 ? 403  SER   B OG   1 
ATOM   15573 H  H    . SER   B 1 403 ? 24.497 31.273  76.958 1.00 16.18 ? 403  SER   B H    1 
ATOM   15574 H  HA   . SER   B 1 403 ? 24.415 33.459  78.454 1.00 17.98 ? 403  SER   B HA   1 
ATOM   15575 H  HB2  . SER   B 1 403 ? 22.160 33.122  78.534 1.00 15.27 ? 403  SER   B HB2  1 
ATOM   15576 H  HB3  . SER   B 1 403 ? 22.606 32.715  77.095 1.00 15.27 ? 403  SER   B HB3  1 
ATOM   15577 H  HG   . SER   B 1 403 ? 22.448 30.656  77.647 1.00 19.89 ? 403  SER   B HG   1 
ATOM   15578 N  N    . TYR   B 1 404 ? 24.425 30.701  80.055 1.00 13.57 ? 404  TYR   B N    1 
ATOM   15579 C  CA   . TYR   B 1 404 ? 24.470 30.161  81.438 1.00 14.54 ? 404  TYR   B CA   1 
ATOM   15580 C  C    . TYR   B 1 404 ? 25.614 30.832  82.202 1.00 16.29 ? 404  TYR   B C    1 
ATOM   15581 O  O    . TYR   B 1 404 ? 25.395 31.353  83.306 1.00 15.78 ? 404  TYR   B O    1 
ATOM   15582 C  CB   . TYR   B 1 404 ? 24.626 28.638  81.439 1.00 19.14 ? 404  TYR   B CB   1 
ATOM   15583 C  CG   . TYR   B 1 404 ? 24.629 28.031  82.817 1.00 18.90 ? 404  TYR   B CG   1 
ATOM   15584 C  CD1  . TYR   B 1 404 ? 23.445 27.664  83.433 1.00 19.50 ? 404  TYR   B CD1  1 
ATOM   15585 C  CD2  . TYR   B 1 404 ? 25.810 27.843  83.512 1.00 17.33 ? 404  TYR   B CD2  1 
ATOM   15586 C  CE1  . TYR   B 1 404 ? 23.436 27.114  84.703 1.00 20.03 ? 404  TYR   B CE1  1 
ATOM   15587 C  CE2  . TYR   B 1 404 ? 25.819 27.295  84.783 1.00 21.22 ? 404  TYR   B CE2  1 
ATOM   15588 C  CZ   . TYR   B 1 404 ? 24.627 26.929  85.381 1.00 23.62 ? 404  TYR   B CZ   1 
ATOM   15589 O  OH   . TYR   B 1 404 ? 24.622 26.384  86.640 1.00 24.87 ? 404  TYR   B OH   1 
ATOM   15590 H  H    . TYR   B 1 404 ? 24.505 30.123  79.424 1.00 16.29 ? 404  TYR   B H    1 
ATOM   15591 H  HA   . TYR   B 1 404 ? 23.630 30.359  81.880 1.00 17.45 ? 404  TYR   B HA   1 
ATOM   15592 H  HB2  . TYR   B 1 404 ? 23.904 28.247  80.923 1.00 22.97 ? 404  TYR   B HB2  1 
ATOM   15593 H  HB3  . TYR   B 1 404 ? 25.454 28.405  80.990 1.00 22.97 ? 404  TYR   B HB3  1 
ATOM   15594 H  HD1  . TYR   B 1 404 ? 22.640 27.789  82.985 1.00 23.40 ? 404  TYR   B HD1  1 
ATOM   15595 H  HD2  . TYR   B 1 404 ? 26.615 28.090  83.117 1.00 20.80 ? 404  TYR   B HD2  1 
ATOM   15596 H  HE1  . TYR   B 1 404 ? 22.631 26.869  85.099 1.00 24.04 ? 404  TYR   B HE1  1 
ATOM   15597 H  HE2  . TYR   B 1 404 ? 26.624 27.173  85.233 1.00 25.46 ? 404  TYR   B HE2  1 
ATOM   15598 H  HH   . TYR   B 1 404 ? 23.970 25.860  86.716 1.00 29.84 ? 404  TYR   B HH   1 
ATOM   15599 N  N    . ARG   B 1 405 ? 26.800 30.835  81.605 1.00 15.05 ? 405  ARG   B N    1 
ATOM   15600 C  CA   . ARG   B 1 405 ? 27.991 31.387  82.299 1.00 16.25 ? 405  ARG   B CA   1 
ATOM   15601 C  C    . ARG   B 1 405 ? 27.892 32.917  82.368 1.00 18.40 ? 405  ARG   B C    1 
ATOM   15602 O  O    . ARG   B 1 405 ? 28.302 33.485  83.394 1.00 18.22 ? 405  ARG   B O    1 
ATOM   15603 C  CB   . ARG   B 1 405 ? 29.244 30.874  81.582 1.00 17.31 ? 405  ARG   B CB   1 
ATOM   15604 C  CG   . ARG   B 1 405 ? 29.571 29.420  81.893 1.00 16.87 ? 405  ARG   B CG   1 
ATOM   15605 C  CD   . ARG   B 1 405 ? 30.241 28.699  80.738 1.00 16.24 ? 405  ARG   B CD   1 
ATOM   15606 N  NE   . ARG   B 1 405 ? 30.527 27.302  81.032 1.00 18.57 ? 405  ARG   B NE   1 
ATOM   15607 C  CZ   . ARG   B 1 405 ? 29.821 26.275  80.571 1.00 16.64 ? 405  ARG   B CZ   1 
ATOM   15608 N  NH1  . ARG   B 1 405 ? 28.712 26.487  79.888 1.00 14.96 ? 405  ARG   B NH1  1 
ATOM   15609 N  NH2  . ARG   B 1 405 ? 30.233 25.038  80.790 1.00 16.74 ? 405  ARG   B NH2  1 
ATOM   15610 H  H    . ARG   B 1 405 ? 26.949 30.532  80.814 1.00 18.07 ? 405  ARG   B H    1 
ATOM   15611 H  HA   . ARG   B 1 405 ? 28.041 31.087  83.220 1.00 19.51 ? 405  ARG   B HA   1 
ATOM   15612 H  HB2  . ARG   B 1 405 ? 29.123 30.973  80.625 1.00 20.77 ? 405  ARG   B HB2  1 
ATOM   15613 H  HB3  . ARG   B 1 405 ? 30.000 31.428  81.831 1.00 20.77 ? 405  ARG   B HB3  1 
ATOM   15614 H  HG2  . ARG   B 1 405 ? 30.151 29.384  82.670 1.00 20.24 ? 405  ARG   B HG2  1 
ATOM   15615 H  HG3  . ARG   B 1 405 ? 28.754 28.954  82.128 1.00 20.24 ? 405  ARG   B HG3  1 
ATOM   15616 H  HD2  . ARG   B 1 405 ? 29.670 28.750  79.956 1.00 19.49 ? 405  ARG   B HD2  1 
ATOM   15617 H  HD3  . ARG   B 1 405 ? 31.068 29.154  80.515 1.00 19.49 ? 405  ARG   B HD3  1 
ATOM   15618 H  HE   . ARG   B 1 405 ? 31.200 27.130  81.539 1.00 22.28 ? 405  ARG   B HE   1 
ATOM   15619 H  HH11 . ARG   B 1 405 ? 28.445 27.291  79.740 1.00 17.95 ? 405  ARG   B HH11 1 
ATOM   15620 H  HH12 . ARG   B 1 405 ? 28.256 25.821  79.590 1.00 17.95 ? 405  ARG   B HH12 1 
ATOM   15621 H  HH21 . ARG   B 1 405 ? 30.958 24.898  81.231 1.00 20.10 ? 405  ARG   B HH21 1 
ATOM   15622 H  HH22 . ARG   B 1 405 ? 29.776 24.373  80.492 1.00 20.10 ? 405  ARG   B HH22 1 
ATOM   15623 N  N    . LEU   B 1 406 ? 27.357 33.546  81.323 1.00 16.26 ? 406  LEU   B N    1 
ATOM   15624 C  CA   . LEU   B 1 406 ? 27.164 35.018  81.336 1.00 16.34 ? 406  LEU   B CA   1 
ATOM   15625 C  C    . LEU   B 1 406 ? 26.258 35.393  82.514 1.00 17.72 ? 406  LEU   B C    1 
ATOM   15626 O  O    . LEU   B 1 406 ? 26.652 36.263  83.310 1.00 17.02 ? 406  LEU   B O    1 
ATOM   15627 C  CB   . LEU   B 1 406 ? 26.528 35.446  80.013 1.00 16.22 ? 406  LEU   B CB   1 
ATOM   15628 C  CG   . LEU   B 1 406 ? 25.894 36.836  80.017 1.00 16.62 ? 406  LEU   B CG   1 
ATOM   15629 C  CD1  . LEU   B 1 406 ? 26.962 37.914  79.911 1.00 17.42 ? 406  LEU   B CD1  1 
ATOM   15630 C  CD2  . LEU   B 1 406 ? 24.878 36.974  78.896 1.00 14.41 ? 406  LEU   B CD2  1 
ATOM   15631 H  H    . LEU   B 1 406 ? 27.099 33.155  80.602 1.00 19.52 ? 406  LEU   B H    1 
ATOM   15632 H  HA   . LEU   B 1 406 ? 28.015 35.471  81.438 1.00 19.61 ? 406  LEU   B HA   1 
ATOM   15633 H  HB2  . LEU   B 1 406 ? 27.206 35.417  79.320 1.00 19.47 ? 406  LEU   B HB2  1 
ATOM   15634 H  HB3  . LEU   B 1 406 ? 25.849 34.797  79.772 1.00 19.47 ? 406  LEU   B HB3  1 
ATOM   15635 H  HG   . LEU   B 1 406 ? 25.428 36.951  80.860 1.00 19.95 ? 406  LEU   B HG   1 
ATOM   15636 H  HD11 . LEU   B 1 406 ? 26.541 38.788  79.915 1.00 20.90 ? 406  LEU   B HD11 1 
ATOM   15637 H  HD12 . LEU   B 1 406 ? 27.569 37.844  80.665 1.00 20.90 ? 406  LEU   B HD12 1 
ATOM   15638 H  HD13 . LEU   B 1 406 ? 27.458 37.798  79.086 1.00 20.90 ? 406  LEU   B HD13 1 
ATOM   15639 H  HD21 . LEU   B 1 406 ? 24.490 37.863  78.919 1.00 17.30 ? 406  LEU   B HD21 1 
ATOM   15640 H  HD22 . LEU   B 1 406 ? 25.317 36.835  78.042 1.00 17.30 ? 406  LEU   B HD22 1 
ATOM   15641 H  HD23 . LEU   B 1 406 ? 24.178 36.313  79.010 1.00 17.30 ? 406  LEU   B HD23 1 
ATOM   15642 N  N    . CYS   B 1 407 ? 25.106 34.732  82.628 1.00 16.72 ? 407  CYS   B N    1 
ATOM   15643 C  CA   . CYS   B 1 407 ? 24.130 35.118  83.685 1.00 16.79 ? 407  CYS   B CA   1 
ATOM   15644 C  C    . CYS   B 1 407 ? 24.679 34.792  85.083 1.00 18.73 ? 407  CYS   B C    1 
ATOM   15645 O  O    . CYS   B 1 407 ? 24.395 35.560  86.017 1.00 18.87 ? 407  CYS   B O    1 
ATOM   15646 C  CB   . CYS   B 1 407 ? 22.786 34.434  83.455 1.00 16.32 ? 407  CYS   B CB   1 
ATOM   15647 S  SG   . CYS   B 1 407 ? 21.858 35.134  82.065 1.00 17.11 ? 407  CYS   B SG   1 
ATOM   15648 H  H    . CYS   B 1 407 ? 24.864 34.076  82.127 1.00 20.07 ? 407  CYS   B H    1 
ATOM   15649 H  HA   . CYS   B 1 407 ? 23.993 36.077  83.634 1.00 20.15 ? 407  CYS   B HA   1 
ATOM   15650 H  HB2  . CYS   B 1 407 ? 22.934 33.489  83.294 1.00 19.59 ? 407  CYS   B HB2  1 
ATOM   15651 H  HB3  . CYS   B 1 407 ? 22.252 34.504  84.261 1.00 19.59 ? 407  CYS   B HB3  1 
ATOM   15652 H  HG   . CYS   B 1 407 ? 21.178 34.280  81.567 1.00 20.53 ? 407  CYS   B HG   1 
ATOM   15653 N  N    . GLU   B 1 408 ? 25.450 33.712  85.214 1.00 17.73 ? 408  GLU   B N    1 
ATOM   15654 C  CA   . GLU   B 1 408 ? 26.052 33.370  86.529 1.00 18.54 ? 408  GLU   B CA   1 
ATOM   15655 C  C    . GLU   B 1 408 ? 26.969 34.513  86.980 1.00 19.29 ? 408  GLU   B C    1 
ATOM   15656 O  O    . GLU   B 1 408 ? 26.964 34.836  88.176 1.00 19.82 ? 408  GLU   B O    1 
ATOM   15657 C  CB   . GLU   B 1 408 ? 26.821 32.051  86.452 1.00 22.66 ? 408  GLU   B CB   1 
ATOM   15658 C  CG   . GLU   B 1 408 ? 27.625 31.741  87.698 1.00 27.94 ? 408  GLU   B CG   1 
ATOM   15659 C  CD   . GLU   B 1 408 ? 27.933 30.266  87.887 1.00 39.34 ? 408  GLU   B CD   1 
ATOM   15660 O  OE1  . GLU   B 1 408 ? 27.128 29.432  87.433 1.00 37.98 ? 408  GLU   B OE1  1 
ATOM   15661 O  OE2  . GLU   B 1 408 ? 28.982 29.955  88.481 1.00 49.22 ? 408  GLU   B OE2  1 
ATOM   15662 H  H    . GLU   B 1 408 ? 25.640 33.168  84.575 1.00 21.28 ? 408  GLU   B H    1 
ATOM   15663 H  HA   . GLU   B 1 408 ? 25.344 33.255  87.182 1.00 22.26 ? 408  GLU   B HA   1 
ATOM   15664 H  HB2  . GLU   B 1 408 ? 26.193 31.329  86.294 1.00 27.20 ? 408  GLU   B HB2  1 
ATOM   15665 H  HB3  . GLU   B 1 408 ? 27.420 32.079  85.689 1.00 27.20 ? 408  GLU   B HB3  1 
ATOM   15666 H  HG2  . GLU   B 1 408 ? 28.460 32.234  87.663 1.00 33.53 ? 408  GLU   B HG2  1 
ATOM   15667 H  HG3  . GLU   B 1 408 ? 27.138 32.062  88.473 1.00 33.53 ? 408  GLU   B HG3  1 
ATOM   15668 N  N    . GLY   B 1 409 ? 27.713 35.100  86.042 1.00 19.99 ? 409  GLY   B N    1 
ATOM   15669 C  CA   . GLY   B 1 409 ? 28.654 36.178  86.395 1.00 23.95 ? 409  GLY   B CA   1 
ATOM   15670 C  C    . GLY   B 1 409 ? 27.943 37.418  86.907 1.00 21.80 ? 409  GLY   B C    1 
ATOM   15671 O  O    . GLY   B 1 409 ? 28.562 38.173  87.675 1.00 23.83 ? 409  GLY   B O    1 
ATOM   15672 H  H    . GLY   B 1 409 ? 27.693 34.896  85.207 1.00 23.99 ? 409  GLY   B H    1 
ATOM   15673 H  HA2  . GLY   B 1 409 ? 29.270 35.858  87.072 1.00 28.74 ? 409  GLY   B HA2  1 
ATOM   15674 H  HA3  . GLY   B 1 409 ? 29.184 36.410  85.616 1.00 28.74 ? 409  GLY   B HA3  1 
ATOM   15675 N  N    . TYR   B 1 410 ? 26.694 37.624  86.487 1.00 21.73 ? 410  TYR   B N    1 
ATOM   15676 C  CA   . TYR   B 1 410 ? 25.918 38.814  86.926 1.00 22.26 ? 410  TYR   B CA   1 
ATOM   15677 C  C    . TYR   B 1 410 ? 25.009 38.435  88.099 1.00 26.33 ? 410  TYR   B C    1 
ATOM   15678 O  O    . TYR   B 1 410 ? 24.197 39.278  88.512 1.00 24.74 ? 410  TYR   B O    1 
ATOM   15679 C  CB   . TYR   B 1 410 ? 25.147 39.422  85.752 1.00 21.91 ? 410  TYR   B CB   1 
ATOM   15680 C  CG   . TYR   B 1 410 ? 25.998 40.247  84.822 1.00 22.50 ? 410  TYR   B CG   1 
ATOM   15681 C  CD1  . TYR   B 1 410 ? 26.261 41.580  85.090 1.00 23.36 ? 410  TYR   B CD1  1 
ATOM   15682 C  CD2  . TYR   B 1 410 ? 26.558 39.692  83.685 1.00 20.35 ? 410  TYR   B CD2  1 
ATOM   15683 C  CE1  . TYR   B 1 410 ? 27.049 42.343  84.246 1.00 24.99 ? 410  TYR   B CE1  1 
ATOM   15684 C  CE2  . TYR   B 1 410 ? 27.349 40.441  82.830 1.00 22.76 ? 410  TYR   B CE2  1 
ATOM   15685 C  CZ   . TYR   B 1 410 ? 27.597 41.772  83.112 1.00 24.29 ? 410  TYR   B CZ   1 
ATOM   15686 O  OH   . TYR   B 1 410 ? 28.381 42.519  82.269 1.00 25.89 ? 410  TYR   B OH   1 
ATOM   15687 H  H    . TYR   B 1 410 ? 26.272 37.099  85.953 1.00 26.08 ? 410  TYR   B H    1 
ATOM   15688 H  HA   . TYR   B 1 410 ? 26.526 39.502  87.239 1.00 26.72 ? 410  TYR   B HA   1 
ATOM   15689 H  HB2  . TYR   B 1 410 ? 24.730 38.707  85.246 1.00 26.29 ? 410  TYR   B HB2  1 
ATOM   15690 H  HB3  . TYR   B 1 410 ? 24.432 39.978  86.100 1.00 26.29 ? 410  TYR   B HB3  1 
ATOM   15691 H  HD1  . TYR   B 1 410 ? 25.901 41.971  85.853 1.00 28.04 ? 410  TYR   B HD1  1 
ATOM   15692 H  HD2  . TYR   B 1 410 ? 26.400 38.796  83.491 1.00 24.43 ? 410  TYR   B HD2  1 
ATOM   15693 H  HE1  . TYR   B 1 410 ? 27.210 43.238  84.441 1.00 29.99 ? 410  TYR   B HE1  1 
ATOM   15694 H  HE2  . TYR   B 1 410 ? 27.712 40.050  82.068 1.00 27.32 ? 410  TYR   B HE2  1 
ATOM   15695 H  HH   . TYR   B 1 410 ? 28.522 43.273  82.612 1.00 31.07 ? 410  TYR   B HH   1 
ATOM   15696 N  N    . GLY   B 1 411 ? 25.157 37.213  88.619 1.00 23.04 ? 411  GLY   B N    1 
ATOM   15697 C  CA   . GLY   B 1 411 ? 24.324 36.756  89.748 1.00 25.98 ? 411  GLY   B CA   1 
ATOM   15698 C  C    . GLY   B 1 411 ? 22.851 36.719  89.386 1.00 22.83 ? 411  GLY   B C    1 
ATOM   15699 O  O    . GLY   B 1 411 ? 22.022 37.013  90.261 1.00 22.94 ? 411  GLY   B O    1 
ATOM   15700 H  H    . GLY   B 1 411 ? 25.728 36.635  88.338 1.00 27.65 ? 411  GLY   B H    1 
ATOM   15701 H  HA2  . GLY   B 1 411 ? 24.611 35.872  90.024 1.00 31.18 ? 411  GLY   B HA2  1 
ATOM   15702 H  HA3  . GLY   B 1 411 ? 24.456 37.346  90.506 1.00 31.18 ? 411  GLY   B HA3  1 
ATOM   15703 N  N    . ALA   B 1 412 ? 22.535 36.366  88.137 1.00 22.93 ? 412  ALA   B N    1 
ATOM   15704 C  CA   . ALA   B 1 412 ? 21.126 36.352  87.682 1.00 19.26 ? 412  ALA   B CA   1 
ATOM   15705 C  C    . ALA   B 1 412 ? 20.875 35.122  86.801 1.00 18.86 ? 412  ALA   B C    1 
ATOM   15706 O  O    . ALA   B 1 412 ? 20.483 35.296  85.637 1.00 18.54 ? 412  ALA   B O    1 
ATOM   15707 C  CB   . ALA   B 1 412 ? 20.798 37.631  86.961 1.00 19.18 ? 412  ALA   B CB   1 
ATOM   15708 H  H    . ALA   B 1 412 ? 23.108 36.133  87.540 1.00 27.52 ? 412  ALA   B H    1 
ATOM   15709 H  HA   . ALA   B 1 412 ? 20.538 36.293  88.452 1.00 23.12 ? 412  ALA   B HA   1 
ATOM   15710 H  HB1  . ALA   B 1 412 ? 19.873 37.610  86.668 1.00 23.02 ? 412  ALA   B HB1  1 
ATOM   15711 H  HB2  . ALA   B 1 412 ? 20.930 38.383  87.559 1.00 23.02 ? 412  ALA   B HB2  1 
ATOM   15712 H  HB3  . ALA   B 1 412 ? 21.379 37.726  86.190 1.00 23.02 ? 412  ALA   B HB3  1 
ATOM   15713 N  N    . PRO   B 1 413 ? 21.054 33.892  87.324 1.00 18.74 ? 413  PRO   B N    1 
ATOM   15714 C  CA   . PRO   B 1 413 ? 20.902 32.681  86.510 1.00 17.19 ? 413  PRO   B CA   1 
ATOM   15715 C  C    . PRO   B 1 413 ? 19.467 32.510  86.000 1.00 19.53 ? 413  PRO   B C    1 
ATOM   15716 O  O    . PRO   B 1 413 ? 19.270 31.760  85.079 1.00 15.55 ? 413  PRO   B O    1 
ATOM   15717 C  CB   . PRO   B 1 413 ? 21.228 31.549  87.489 1.00 18.89 ? 413  PRO   B CB   1 
ATOM   15718 C  CG   . PRO   B 1 413 ? 20.957 32.144  88.851 1.00 19.13 ? 413  PRO   B CG   1 
ATOM   15719 C  CD   . PRO   B 1 413 ? 21.374 33.592  88.720 1.00 21.55 ? 413  PRO   B CD   1 
ATOM   15720 H  HA   . PRO   B 1 413 ? 21.469 32.704  85.723 1.00 20.63 ? 413  PRO   B HA   1 
ATOM   15721 H  HB2  . PRO   B 1 413 ? 20.674 30.770  87.326 1.00 22.67 ? 413  PRO   B HB2  1 
ATOM   15722 H  HB3  . PRO   B 1 413 ? 22.151 31.263  87.405 1.00 22.67 ? 413  PRO   B HB3  1 
ATOM   15723 H  HG2  . PRO   B 1 413 ? 20.020 32.066  89.091 1.00 22.96 ? 413  PRO   B HG2  1 
ATOM   15724 H  HG3  . PRO   B 1 413 ? 21.465 31.691  89.542 1.00 22.96 ? 413  PRO   B HG3  1 
ATOM   15725 H  HD2  . PRO   B 1 413 ? 20.887 34.165  89.333 1.00 25.86 ? 413  PRO   B HD2  1 
ATOM   15726 H  HD3  . PRO   B 1 413 ? 22.318 33.714  88.908 1.00 25.86 ? 413  PRO   B HD3  1 
ATOM   15727 N  N    . GLU   B 1 414 ? 18.518 33.221  86.609 1.00 19.18 ? 414  GLU   B N    1 
ATOM   15728 C  CA   . GLU   B 1 414 ? 17.090 33.053  86.240 1.00 16.71 ? 414  GLU   B CA   1 
ATOM   15729 C  C    . GLU   B 1 414 ? 16.841 33.560  84.818 1.00 16.62 ? 414  GLU   B C    1 
ATOM   15730 O  O    . GLU   B 1 414 ? 15.743 33.330  84.301 1.00 19.22 ? 414  GLU   B O    1 
ATOM   15731 C  CB   . GLU   B 1 414 ? 16.198 33.811  87.224 1.00 22.34 ? 414  GLU   B CB   1 
ATOM   15732 C  CG   . GLU   B 1 414 ? 16.491 35.297  87.276 1.00 20.74 ? 414  GLU   B CG   1 
ATOM   15733 C  CD   . GLU   B 1 414 ? 17.404 35.706  88.417 1.00 24.33 ? 414  GLU   B CD   1 
ATOM   15734 O  OE1  . GLU   B 1 414 ? 18.345 34.952  88.718 1.00 20.62 ? 414  GLU   B OE1  1 
ATOM   15735 O  OE2  . GLU   B 1 414 ? 17.162 36.774  89.008 1.00 28.16 ? 414  GLU   B OE2  1 
ATOM   15736 H  H    . GLU   B 1 414 ? 18.666 33.799  87.229 1.00 23.02 ? 414  GLU   B H    1 
ATOM   15737 H  HA   . GLU   B 1 414 ? 16.873 32.108  86.277 1.00 20.05 ? 414  GLU   B HA   1 
ATOM   15738 H  HB2  . GLU   B 1 414 ? 15.269 33.679  86.977 1.00 26.81 ? 414  GLU   B HB2  1 
ATOM   15739 H  HB3  . GLU   B 1 414 ? 16.312 33.434  88.110 1.00 26.81 ? 414  GLU   B HB3  1 
ATOM   15740 H  HG2  . GLU   B 1 414 ? 16.896 35.567  86.437 1.00 24.89 ? 414  GLU   B HG2  1 
ATOM   15741 H  HG3  . GLU   B 1 414 ? 15.653 35.780  87.355 1.00 24.89 ? 414  GLU   B HG3  1 
ATOM   15742 N  N    . TYR   B 1 415 ? 17.808 34.263  84.221 1.00 14.50 ? 415  TYR   B N    1 
ATOM   15743 C  CA   . TYR   B 1 415 ? 17.599 34.864  82.873 1.00 14.85 ? 415  TYR   B CA   1 
ATOM   15744 C  C    . TYR   B 1 415 ? 18.320 34.033  81.808 1.00 13.51 ? 415  TYR   B C    1 
ATOM   15745 O  O    . TYR   B 1 415 ? 18.272 34.416  80.632 1.00 14.88 ? 415  TYR   B O    1 
ATOM   15746 C  CB   . TYR   B 1 415 ? 17.985 36.344  82.881 1.00 16.72 ? 415  TYR   B CB   1 
ATOM   15747 C  CG   . TYR   B 1 415 ? 17.160 37.133  83.864 1.00 17.31 ? 415  TYR   B CG   1 
ATOM   15748 C  CD1  . TYR   B 1 415 ? 15.778 37.071  83.829 1.00 19.00 ? 415  TYR   B CD1  1 
ATOM   15749 C  CD2  . TYR   B 1 415 ? 17.753 37.890  84.859 1.00 16.78 ? 415  TYR   B CD2  1 
ATOM   15750 C  CE1  . TYR   B 1 415 ? 15.001 37.765  84.739 1.00 18.82 ? 415  TYR   B CE1  1 
ATOM   15751 C  CE2  . TYR   B 1 415 ? 16.991 38.592  85.777 1.00 17.82 ? 415  TYR   B CE2  1 
ATOM   15752 C  CZ   . TYR   B 1 415 ? 15.611 38.527  85.719 1.00 16.83 ? 415  TYR   B CZ   1 
ATOM   15753 O  OH   . TYR   B 1 415 ? 14.846 39.222  86.622 1.00 16.66 ? 415  TYR   B OH   1 
ATOM   15754 H  H    . TYR   B 1 415 ? 18.583 34.408  84.563 1.00 17.41 ? 415  TYR   B H    1 
ATOM   15755 H  HA   . TYR   B 1 415 ? 16.658 34.840  82.640 1.00 17.82 ? 415  TYR   B HA   1 
ATOM   15756 H  HB2  . TYR   B 1 415 ? 18.925 36.432  83.104 1.00 20.07 ? 415  TYR   B HB2  1 
ATOM   15757 H  HB3  . TYR   B 1 415 ? 17.869 36.713  81.992 1.00 20.07 ? 415  TYR   B HB3  1 
ATOM   15758 H  HD1  . TYR   B 1 415 ? 15.362 36.551  83.179 1.00 22.80 ? 415  TYR   B HD1  1 
ATOM   15759 H  HD2  . TYR   B 1 415 ? 18.681 37.928  84.912 1.00 20.13 ? 415  TYR   B HD2  1 
ATOM   15760 H  HE1  . TYR   B 1 415 ? 14.073 37.719  84.692 1.00 22.59 ? 415  TYR   B HE1  1 
ATOM   15761 H  HE2  . TYR   B 1 415 ? 17.406 39.106  86.431 1.00 21.39 ? 415  TYR   B HE2  1 
ATOM   15762 H  HH   . TYR   B 1 415 ? 15.347 39.636  87.154 1.00 20.00 ? 415  TYR   B HH   1 
ATOM   15763 N  N    . SER   B 1 416 ? 18.948 32.932  82.220 1.00 14.95 ? 416  SER   B N    1 
ATOM   15764 C  CA   . SER   B 1 416 ? 19.549 32.003  81.228 1.00 14.85 ? 416  SER   B CA   1 
ATOM   15765 C  C    . SER   B 1 416 ? 18.497 30.947  80.868 1.00 16.07 ? 416  SER   B C    1 
ATOM   15766 O  O    . SER   B 1 416 ? 18.192 30.110  81.721 1.00 13.70 ? 416  SER   B O    1 
ATOM   15767 C  CB   . SER   B 1 416 ? 20.803 31.359  81.753 1.00 14.60 ? 416  SER   B CB   1 
ATOM   15768 O  OG   . SER   B 1 416 ? 21.296 30.399  80.835 1.00 13.71 ? 416  SER   B OG   1 
ATOM   15769 H  H    . SER   B 1 416 ? 19.042 32.699  83.043 1.00 17.94 ? 416  SER   B H    1 
ATOM   15770 H  HA   . SER   B 1 416 ? 19.809 32.500  80.437 1.00 17.83 ? 416  SER   B HA   1 
ATOM   15771 H  HB2  . SER   B 1 416 ? 21.478 32.037  81.912 1.00 17.53 ? 416  SER   B HB2  1 
ATOM   15772 H  HB3  . SER   B 1 416 ? 20.621 30.934  82.606 1.00 17.53 ? 416  SER   B HB3  1 
ATOM   15773 H  HG   . SER   B 1 416 ? 21.504 30.780  80.116 1.00 16.45 ? 416  SER   B HG   1 
ATOM   15774 N  N    . MET   B 1 417 ? 17.946 31.020  79.656 1.00 14.20 ? 417  MET   B N    1 
ATOM   15775 C  CA   . MET   B 1 417 ? 16.891 30.060  79.251 1.00 14.35 ? 417  MET   B CA   1 
ATOM   15776 C  C    . MET   B 1 417 ? 17.603 28.791  78.781 1.00 13.69 ? 417  MET   B C    1 
ATOM   15777 O  O    . MET   B 1 417 ? 17.639 28.535  77.566 1.00 14.46 ? 417  MET   B O    1 
ATOM   15778 C  CB   . MET   B 1 417 ? 15.989 30.657  78.171 1.00 14.70 ? 417  MET   B CB   1 
ATOM   15779 C  CG   . MET   B 1 417 ? 15.167 31.831  78.683 1.00 14.64 ? 417  MET   B CG   1 
ATOM   15780 S  SD   . MET   B 1 417 ? 14.040 31.376  80.040 1.00 14.90 ? 417  MET   B SD   1 
ATOM   15781 C  CE   . MET   B 1 417 ? 14.859 32.142  81.439 1.00 16.70 ? 417  MET   B CE   1 
ATOM   15782 H  H    . MET   B 1 417 ? 18.157 31.601  79.058 1.00 17.05 ? 417  MET   B H    1 
ATOM   15783 H  HA   . MET   B 1 417 ? 16.303 29.851  79.993 1.00 17.22 ? 417  MET   B HA   1 
ATOM   15784 H  HB2  . MET   B 1 417 ? 16.534 30.949  77.423 1.00 17.65 ? 417  MET   B HB2  1 
ATOM   15785 H  HB3  . MET   B 1 417 ? 15.392 29.970  77.836 1.00 17.65 ? 417  MET   B HB3  1 
ATOM   15786 H  HG2  . MET   B 1 417 ? 15.766 32.530  78.988 1.00 17.57 ? 417  MET   B HG2  1 
ATOM   15787 H  HG3  . MET   B 1 417 ? 14.650 32.201  77.950 1.00 17.57 ? 417  MET   B HG3  1 
ATOM   15788 H  HE1  . MET   B 1 417 ? 14.349 31.971  82.246 1.00 20.05 ? 417  MET   B HE1  1 
ATOM   15789 H  HE2  . MET   B 1 417 ? 15.750 31.771  81.536 1.00 20.05 ? 417  MET   B HE2  1 
ATOM   15790 H  HE3  . MET   B 1 417 ? 14.922 33.099  81.293 1.00 20.05 ? 417  MET   B HE3  1 
ATOM   15791 N  N    . THR   B 1 418 ? 18.154 28.048  79.738 1.00 12.38 ? 418  THR   B N    1 
ATOM   15792 C  CA   . THR   B 1 418 ? 18.971 26.874  79.365 1.00 10.80 ? 418  THR   B CA   1 
ATOM   15793 C  C    . THR   B 1 418 ? 18.604 25.635  80.175 1.00 10.40 ? 418  THR   B C    1 
ATOM   15794 O  O    . THR   B 1 418 ? 17.967 25.783  81.226 1.00 13.25 ? 418  THR   B O    1 
ATOM   15795 C  CB   . THR   B 1 418 ? 20.449 27.154  79.656 1.00 13.42 ? 418  THR   B CB   1 
ATOM   15796 O  OG1  . THR   B 1 418 ? 20.548 27.700  80.972 1.00 14.51 ? 418  THR   B OG1  1 
ATOM   15797 C  CG2  . THR   B 1 418 ? 21.079 28.103  78.661 1.00 14.31 ? 418  THR   B CG2  1 
ATOM   15798 H  H    . THR   B 1 418 ? 18.077 28.192  80.582 1.00 14.85 ? 418  THR   B H    1 
ATOM   15799 H  HA   . THR   B 1 418 ? 18.805 26.715  78.423 1.00 12.96 ? 418  THR   B HA   1 
ATOM   15800 H  HB   . THR   B 1 418 ? 20.934 26.317  79.581 1.00 16.11 ? 418  THR   B HB   1 
ATOM   15801 H  HG1  . THR   B 1 418 ? 20.787 28.504  80.925 1.00 17.41 ? 418  THR   B HG1  1 
ATOM   15802 H  HG21 . THR   B 1 418 ? 22.010 28.244  78.893 1.00 17.17 ? 418  THR   B HG21 1 
ATOM   15803 H  HG22 . THR   B 1 418 ? 21.022 27.723  77.770 1.00 17.17 ? 418  THR   B HG22 1 
ATOM   15804 H  HG23 . THR   B 1 418 ? 20.610 28.952  78.681 1.00 17.17 ? 418  THR   B HG23 1 
ATOM   15805 N  N    . VAL   B 1 419 ? 18.978 24.462  79.669 1.00 11.14 ? 419  VAL   B N    1 
ATOM   15806 C  CA   . VAL   B 1 419 ? 18.829 23.203  80.449 1.00 13.49 ? 419  VAL   B CA   1 
ATOM   15807 C  C    . VAL   B 1 419 ? 20.190 22.517  80.319 1.00 13.04 ? 419  VAL   B C    1 
ATOM   15808 O  O    . VAL   B 1 419 ? 20.661 22.378  79.184 1.00 12.48 ? 419  VAL   B O    1 
ATOM   15809 C  CB   . VAL   B 1 419 ? 17.681 22.304  79.960 1.00 11.08 ? 419  VAL   B CB   1 
ATOM   15810 C  CG1  . VAL   B 1 419 ? 17.594 21.025  80.781 1.00 12.91 ? 419  VAL   B CG1  1 
ATOM   15811 C  CG2  . VAL   B 1 419 ? 16.345 23.030  79.956 1.00 14.44 ? 419  VAL   B CG2  1 
ATOM   15812 H  H    . VAL   B 1 419 ? 19.318 24.360  78.886 1.00 13.37 ? 419  VAL   B H    1 
ATOM   15813 H  HA   . VAL   B 1 419 ? 18.587 23.389  81.370 1.00 16.20 ? 419  VAL   B HA   1 
ATOM   15814 H  HB   . VAL   B 1 419 ? 17.884 22.066  79.042 1.00 13.29 ? 419  VAL   B HB   1 
ATOM   15815 H  HG11 . VAL   B 1 419 ? 16.864 20.478  80.452 1.00 15.49 ? 419  VAL   B HG11 1 
ATOM   15816 H  HG12 . VAL   B 1 419 ? 18.426 20.533  80.703 1.00 15.49 ? 419  VAL   B HG12 1 
ATOM   15817 H  HG13 . VAL   B 1 419 ? 17.437 21.248  81.712 1.00 15.49 ? 419  VAL   B HG13 1 
ATOM   15818 H  HG21 . VAL   B 1 419 ? 15.651 22.429  79.642 1.00 17.33 ? 419  VAL   B HG21 1 
ATOM   15819 H  HG22 . VAL   B 1 419 ? 16.134 23.325  80.856 1.00 17.33 ? 419  VAL   B HG22 1 
ATOM   15820 H  HG23 . VAL   B 1 419 ? 16.396 23.799  79.368 1.00 17.33 ? 419  VAL   B HG23 1 
ATOM   15821 N  N    . LYS   B 1 420 ? 20.808 22.153  81.439 1.00 13.29 ? 420  LYS   B N    1 
ATOM   15822 C  CA   . LYS   B 1 420 ? 22.183 21.586  81.403 1.00 12.00 ? 420  LYS   B CA   1 
ATOM   15823 C  C    . LYS   B 1 420 ? 23.097 22.588  80.686 1.00 10.66 ? 420  LYS   B C    1 
ATOM   15824 O  O    . LYS   B 1 420 ? 24.005 22.131  79.975 1.00 12.71 ? 420  LYS   B O    1 
ATOM   15825 C  CB   . LYS   B 1 420 ? 22.180 20.180  80.796 1.00 11.94 ? 420  LYS   B CB   1 
ATOM   15826 C  CG   . LYS   B 1 420 ? 21.434 19.139  81.622 1.00 13.45 ? 420  LYS   B CG   1 
ATOM   15827 C  CD   . LYS   B 1 420 ? 21.223 17.820  80.909 1.00 14.32 ? 420  LYS   B CD   1 
ATOM   15828 C  CE   . LYS   B 1 420 ? 20.388 16.845  81.712 1.00 15.48 ? 420  LYS   B CE   1 
ATOM   15829 N  NZ   . LYS   B 1 420 ? 18.974 17.280  81.811 1.00 14.23 ? 420  LYS   B NZ   1 
ATOM   15830 H  H    . LYS   B 1 420 ? 20.466 22.219  82.225 1.00 15.95 ? 420  LYS   B H    1 
ATOM   15831 H  HA   . LYS   B 1 420 ? 22.535 21.462  82.298 1.00 14.41 ? 420  LYS   B HA   1 
ATOM   15832 H  HB2  . LYS   B 1 420 ? 21.782 20.222  79.913 1.00 14.34 ? 420  LYS   B HB2  1 
ATOM   15833 H  HB3  . LYS   B 1 420 ? 23.098 19.888  80.680 1.00 14.34 ? 420  LYS   B HB3  1 
ATOM   15834 H  HG2  . LYS   B 1 420 ? 21.926 18.977  82.442 1.00 16.14 ? 420  LYS   B HG2  1 
ATOM   15835 H  HG3  . LYS   B 1 420 ? 20.570 19.500  81.876 1.00 16.14 ? 420  LYS   B HG3  1 
ATOM   15836 H  HD2  . LYS   B 1 420 ? 20.790 17.984  80.056 1.00 17.19 ? 420  LYS   B HD2  1 
ATOM   15837 H  HD3  . LYS   B 1 420 ? 22.085 17.419  80.717 1.00 17.19 ? 420  LYS   B HD3  1 
ATOM   15838 H  HE2  . LYS   B 1 420 ? 20.428 15.968  81.299 1.00 18.58 ? 420  LYS   B HE2  1 
ATOM   15839 H  HE3  . LYS   B 1 420 ? 20.762 16.756  82.603 1.00 18.58 ? 420  LYS   B HE3  1 
ATOM   15840 H  HZ1  . LYS   B 1 420 ? 18.477 16.608  82.118 1.00 17.08 ? 420  LYS   B HZ1  1 
ATOM   15841 H  HZ2  . LYS   B 1 420 ? 18.914 17.972  82.368 1.00 17.08 ? 420  LYS   B HZ2  1 
ATOM   15842 H  HZ3  . LYS   B 1 420 ? 18.680 17.521  81.006 1.00 17.08 ? 420  LYS   B HZ3  1 
ATOM   15843 N  N    . LYS   B 1 421 ? 22.829 23.888  80.842 1.00 11.73 ? 421  LYS   B N    1 
ATOM   15844 C  CA   . LYS   B 1 421 ? 23.703 24.963  80.288 1.00 13.16 ? 421  LYS   B CA   1 
ATOM   15845 C  C    . LYS   B 1 421 ? 23.578 25.104  78.762 1.00 13.66 ? 421  LYS   B C    1 
ATOM   15846 O  O    . LYS   B 1 421 ? 24.359 25.878  78.196 1.00 14.79 ? 421  LYS   B O    1 
ATOM   15847 C  CB   . LYS   B 1 421 ? 25.160 24.726  80.703 1.00 14.37 ? 421  LYS   B CB   1 
ATOM   15848 C  CG   . LYS   B 1 421 ? 25.406 24.548  82.194 1.00 18.10 ? 421  LYS   B CG   1 
ATOM   15849 C  CD   . LYS   B 1 421 ? 26.877 24.427  82.530 1.00 19.85 ? 421  LYS   B CD   1 
ATOM   15850 C  CE   . LYS   B 1 421 ? 27.130 23.867  83.913 1.00 22.95 ? 421  LYS   B CE   1 
ATOM   15851 N  NZ   . LYS   B 1 421 ? 28.571 23.894  84.258 1.00 29.70 ? 421  LYS   B NZ   1 
ATOM   15852 H  H    . LYS   B 1 421 ? 22.142 24.182  81.268 1.00 14.07 ? 421  LYS   B H    1 
ATOM   15853 H  HA   . LYS   B 1 421 ? 23.399 25.804  80.664 1.00 15.80 ? 421  LYS   B HA   1 
ATOM   15854 H  HB2  . LYS   B 1 421 ? 25.485 23.936  80.243 1.00 17.24 ? 421  LYS   B HB2  1 
ATOM   15855 H  HB3  . LYS   B 1 421 ? 25.693 25.475  80.392 1.00 17.24 ? 421  LYS   B HB3  1 
ATOM   15856 H  HG2  . LYS   B 1 421 ? 25.029 25.303  82.673 1.00 21.73 ? 421  LYS   B HG2  1 
ATOM   15857 H  HG3  . LYS   B 1 421 ? 24.941 23.755  82.503 1.00 21.73 ? 421  LYS   B HG3  1 
ATOM   15858 H  HD2  . LYS   B 1 421 ? 27.307 23.857  81.873 1.00 23.82 ? 421  LYS   B HD2  1 
ATOM   15859 H  HD3  . LYS   B 1 421 ? 27.291 25.301  82.461 1.00 23.82 ? 421  LYS   B HD3  1 
ATOM   15860 H  HE2  . LYS   B 1 421 ? 26.630 24.380  84.567 1.00 27.55 ? 421  LYS   B HE2  1 
ATOM   15861 H  HE3  . LYS   B 1 421 ? 26.803 22.955  83.958 1.00 27.55 ? 421  LYS   B HE3  1 
ATOM   15862 H  HZ1  . LYS   B 1 421 ? 28.680 23.628  85.100 1.00 35.65 ? 421  LYS   B HZ1  1 
ATOM   15863 H  HZ2  . LYS   B 1 421 ? 29.017 23.348  83.715 1.00 35.65 ? 421  LYS   B HZ2  1 
ATOM   15864 H  HZ3  . LYS   B 1 421 ? 28.883 24.723  84.167 1.00 35.65 ? 421  LYS   B HZ3  1 
ATOM   15865 N  N    . GLN   B 1 422 ? 22.608 24.435  78.139 1.00 12.62 ? 422  GLN   B N    1 
ATOM   15866 C  CA   . GLN   B 1 422 ? 22.410 24.613  76.676 1.00 12.31 ? 422  GLN   B CA   1 
ATOM   15867 C  C    . GLN   B 1 422 ? 21.104 25.368  76.415 1.00 12.37 ? 422  GLN   B C    1 
ATOM   15868 O  O    . GLN   B 1 422 ? 20.086 25.007  77.022 1.00 12.61 ? 422  GLN   B O    1 
ATOM   15869 C  CB   . GLN   B 1 422 ? 22.446 23.280  75.928 1.00 12.39 ? 422  GLN   B CB   1 
ATOM   15870 C  CG   . GLN   B 1 422 ? 22.368 23.441  74.418 1.00 13.69 ? 422  GLN   B CG   1 
ATOM   15871 C  CD   . GLN   B 1 422 ? 22.923 22.246  73.683 1.00 10.67 ? 422  GLN   B CD   1 
ATOM   15872 O  OE1  . GLN   B 1 422 ? 24.131 22.104  73.517 1.00 11.84 ? 422  GLN   B OE1  1 
ATOM   15873 N  NE2  . GLN   B 1 422 ? 22.035 21.373  73.239 1.00 13.43 ? 422  GLN   B NE2  1 
ATOM   15874 H  H    . GLN   B 1 422 ? 22.064 23.888  78.520 1.00 15.14 ? 422  GLN   B H    1 
ATOM   15875 H  HA   . GLN   B 1 422 ? 23.148 25.141  76.333 1.00 14.78 ? 422  GLN   B HA   1 
ATOM   15876 H  HB2  . GLN   B 1 422 ? 23.263 22.809  76.156 1.00 14.87 ? 422  GLN   B HB2  1 
ATOM   15877 H  HB3  . GLN   B 1 422 ? 21.707 22.727  76.227 1.00 14.87 ? 422  GLN   B HB3  1 
ATOM   15878 H  HG2  . GLN   B 1 422 ? 21.444 23.577  74.157 1.00 16.43 ? 422  GLN   B HG2  1 
ATOM   15879 H  HG3  . GLN   B 1 422 ? 22.858 24.236  74.154 1.00 16.43 ? 422  GLN   B HG3  1 
ATOM   15880 H  HE21 . GLN   B 1 422 ? 21.196 21.506  73.374 1.00 16.12 ? 422  GLN   B HE21 1 
ATOM   15881 H  HE22 . GLN   B 1 422 ? 22.296 20.672  72.815 1.00 16.12 ? 422  GLN   B HE22 1 
ATOM   15882 N  N    . GLU   B 1 423 ? 21.137 26.328  75.494 1.00 10.13 ? 423  GLU   B N    1 
ATOM   15883 C  CA   . GLU   B 1 423 ? 19.959 27.204  75.258 1.00 11.11 ? 423  GLU   B CA   1 
ATOM   15884 C  C    . GLU   B 1 423 ? 18.766 26.447  74.667 1.00 11.40 ? 423  GLU   B C    1 
ATOM   15885 O  O    . GLU   B 1 423 ? 18.951 25.710  73.689 1.00 13.21 ? 423  GLU   B O    1 
ATOM   15886 C  CB   . GLU   B 1 423 ? 20.361 28.387  74.375 1.00 11.96 ? 423  GLU   B CB   1 
ATOM   15887 C  CG   . GLU   B 1 423 ? 21.151 29.449  75.119 1.00 11.44 ? 423  GLU   B CG   1 
ATOM   15888 C  CD   . GLU   B 1 423 ? 22.568 29.058  75.498 1.00 12.90 ? 423  GLU   B CD   1 
ATOM   15889 O  OE1  . GLU   B 1 423 ? 23.050 28.025  75.000 1.00 13.36 ? 423  GLU   B OE1  1 
ATOM   15890 O  OE2  . GLU   B 1 423 ? 23.183 29.786  76.294 1.00 12.31 ? 423  GLU   B OE2  1 
ATOM   15891 H  H    . GLU   B 1 423 ? 21.817 26.497  74.995 1.00 12.16 ? 423  GLU   B H    1 
ATOM   15892 H  HA   . GLU   B 1 423 ? 19.663 27.536  76.120 1.00 13.34 ? 423  GLU   B HA   1 
ATOM   15893 H  HB2  . GLU   B 1 423 ? 20.890 28.062  73.630 1.00 14.36 ? 423  GLU   B HB2  1 
ATOM   15894 H  HB3  . GLU   B 1 423 ? 19.562 28.790  74.001 1.00 14.36 ? 423  GLU   B HB3  1 
ATOM   15895 H  HG2  . GLU   B 1 423 ? 21.188 30.248  74.570 1.00 13.73 ? 423  GLU   B HG2  1 
ATOM   15896 H  HG3  . GLU   B 1 423 ? 20.669 29.683  75.927 1.00 13.73 ? 423  GLU   B HG3  1 
ATOM   15897 N  N    . ILE   B 1 424 ? 17.584 26.668  75.246 1.00 10.23 ? 424  ILE   B N    1 
ATOM   15898 C  CA   . ILE   B 1 424 ? 16.324 26.060  74.735 1.00 10.72 ? 424  ILE   B CA   1 
ATOM   15899 C  C    . ILE   B 1 424 ? 15.961 26.723  73.402 1.00 14.50 ? 424  ILE   B C    1 
ATOM   15900 O  O    . ILE   B 1 424 ? 16.124 27.946  73.294 1.00 15.97 ? 424  ILE   B O    1 
ATOM   15901 C  CB   . ILE   B 1 424 ? 15.211 26.262  75.785 1.00 13.84 ? 424  ILE   B CB   1 
ATOM   15902 C  CG1  . ILE   B 1 424 ? 15.494 25.477  77.068 1.00 15.80 ? 424  ILE   B CG1  1 
ATOM   15903 C  CG2  . ILE   B 1 424 ? 13.844 25.934  75.207 1.00 12.28 ? 424  ILE   B CG2  1 
ATOM   15904 C  CD1  . ILE   B 1 424 ? 14.829 26.060  78.291 1.00 20.57 ? 424  ILE   B CD1  1 
ATOM   15905 H  H    . ILE   B 1 424 ? 17.478 27.167  75.939 1.00 12.27 ? 424  ILE   B H    1 
ATOM   15906 H  HA   . ILE   B 1 424 ? 16.434 25.108  74.585 1.00 12.86 ? 424  ILE   B HA   1 
ATOM   15907 H  HB   . ILE   B 1 424 ? 15.204 27.201  76.028 1.00 16.62 ? 424  ILE   B HB   1 
ATOM   15908 H  HG12 . ILE   B 1 424 ? 15.194 24.562  76.951 1.00 18.97 ? 424  ILE   B HG12 1 
ATOM   15909 H  HG13 . ILE   B 1 424 ? 16.452 25.445  77.214 1.00 18.97 ? 424  ILE   B HG13 1 
ATOM   15910 H  HG21 . ILE   B 1 424 ? 13.165 26.069  75.886 1.00 14.74 ? 424  ILE   B HG21 1 
ATOM   15911 H  HG22 . ILE   B 1 424 ? 13.665 26.514  74.451 1.00 14.74 ? 424  ILE   B HG22 1 
ATOM   15912 H  HG23 . ILE   B 1 424 ? 13.829 25.009  74.915 1.00 14.74 ? 424  ILE   B HG23 1 
ATOM   15913 H  HD11 . ILE   B 1 424 ? 15.046 25.519  79.066 1.00 24.69 ? 424  ILE   B HD11 1 
ATOM   15914 H  HD12 . ILE   B 1 424 ? 15.145 26.966  78.430 1.00 24.69 ? 424  ILE   B HD12 1 
ATOM   15915 H  HD13 . ILE   B 1 424 ? 13.867 26.069  78.163 1.00 24.69 ? 424  ILE   B HD13 1 
ATOM   15916 N  N    . PRO   B 1 425 ? 15.499 25.965  72.385 1.00 12.62 ? 425  PRO   B N    1 
ATOM   15917 C  CA   . PRO   B 1 425 ? 15.199 26.543  71.073 1.00 11.91 ? 425  PRO   B CA   1 
ATOM   15918 C  C    . PRO   B 1 425 ? 13.843 27.259  70.930 1.00 14.81 ? 425  PRO   B C    1 
ATOM   15919 O  O    . PRO   B 1 425 ? 13.291 27.628  71.943 1.00 13.53 ? 425  PRO   B O    1 
ATOM   15920 C  CB   . PRO   B 1 425 ? 15.336 25.330  70.133 1.00 13.51 ? 425  PRO   B CB   1 
ATOM   15921 C  CG   . PRO   B 1 425 ? 14.912 24.161  70.992 1.00 14.69 ? 425  PRO   B CG   1 
ATOM   15922 C  CD   . PRO   B 1 425 ? 15.340 24.510  72.403 1.00 15.14 ? 425  PRO   B CD   1 
ATOM   15923 H  HA   . PRO   B 1 425 ? 15.800 27.278  70.875 1.00 14.30 ? 425  PRO   B HA   1 
ATOM   15924 H  HB2  . PRO   B 1 425 ? 14.771 25.420  69.350 1.00 16.22 ? 425  PRO   B HB2  1 
ATOM   15925 H  HB3  . PRO   B 1 425 ? 16.247 25.227  69.815 1.00 16.22 ? 425  PRO   B HB3  1 
ATOM   15926 H  HG2  . PRO   B 1 425 ? 13.953 24.023  70.943 1.00 17.63 ? 425  PRO   B HG2  1 
ATOM   15927 H  HG3  . PRO   B 1 425 ? 15.333 23.339  70.694 1.00 17.63 ? 425  PRO   B HG3  1 
ATOM   15928 H  HD2  . PRO   B 1 425 ? 14.674 24.235  73.053 1.00 18.17 ? 425  PRO   B HD2  1 
ATOM   15929 H  HD3  . PRO   B 1 425 ? 16.169 24.066  72.641 1.00 18.17 ? 425  PRO   B HD3  1 
ATOM   15930 N  N    . ALA   B 1 426 ? 13.319 27.379  69.708 1.00 14.11 ? 426  ALA   B N    1 
ATOM   15931 C  CA   . ALA   B 1 426 ? 12.139 28.246  69.433 1.00 11.39 ? 426  ALA   B CA   1 
ATOM   15932 C  C    . ALA   B 1 426 ? 10.767 27.633  69.733 1.00 12.54 ? 426  ALA   B C    1 
ATOM   15933 O  O    . ALA   B 1 426 ? 9.890  27.731  68.865 1.00 13.10 ? 426  ALA   B O    1 
ATOM   15934 C  CB   . ALA   B 1 426 ? 12.202 28.650  67.983 1.00 13.37 ? 426  ALA   B CB   1 
ATOM   15935 H  H    . ALA   B 1 426 ? 13.625 26.970  69.016 1.00 16.93 ? 426  ALA   B H    1 
ATOM   15936 H  HA   . ALA   B 1 426 ? 12.204 28.996  70.045 1.00 13.67 ? 426  ALA   B HA   1 
ATOM   15937 H  HB1  . ALA   B 1 426 ? 11.444 29.217  67.772 1.00 16.05 ? 426  ALA   B HB1  1 
ATOM   15938 H  HB2  . ALA   B 1 426 ? 13.025 29.136  67.818 1.00 16.05 ? 426  ALA   B HB2  1 
ATOM   15939 H  HB3  . ALA   B 1 426 ? 12.177 27.857  67.425 1.00 16.05 ? 426  ALA   B HB3  1 
ATOM   15940 N  N    . TYR   B 1 427 ? 10.578 27.071  70.920 1.00 12.46 ? 427  TYR   B N    1 
ATOM   15941 C  CA   . TYR   B 1 427 ? 9.231  26.570  71.282 1.00 13.46 ? 427  TYR   B CA   1 
ATOM   15942 C  C    . TYR   B 1 427 ? 9.041  26.765  72.787 1.00 12.22 ? 427  TYR   B C    1 
ATOM   15943 O  O    . TYR   B 1 427 ? 9.842  26.231  73.558 1.00 14.23 ? 427  TYR   B O    1 
ATOM   15944 C  CB   . TYR   B 1 427 ? 9.026  25.106  70.884 1.00 12.03 ? 427  TYR   B CB   1 
ATOM   15945 C  CG   . TYR   B 1 427 ? 9.588  24.714  69.540 1.00 11.98 ? 427  TYR   B CG   1 
ATOM   15946 C  CD1  . TYR   B 1 427 ? 10.918 24.357  69.400 1.00 13.11 ? 427  TYR   B CD1  1 
ATOM   15947 C  CD2  . TYR   B 1 427 ? 8.790  24.696  68.409 1.00 13.98 ? 427  TYR   B CD2  1 
ATOM   15948 C  CE1  . TYR   B 1 427 ? 11.442 24.000  68.170 1.00 14.81 ? 427  TYR   B CE1  1 
ATOM   15949 C  CE2  . TYR   B 1 427 ? 9.297  24.335  67.172 1.00 14.79 ? 427  TYR   B CE2  1 
ATOM   15950 C  CZ   . TYR   B 1 427 ? 10.629 23.986  67.052 1.00 13.75 ? 427  TYR   B CZ   1 
ATOM   15951 O  OH   . TYR   B 1 427 ? 11.142 23.628  65.830 1.00 13.09 ? 427  TYR   B OH   1 
ATOM   15952 H  H    . TYR   B 1 427 ? 11.185 26.967  71.520 1.00 14.95 ? 427  TYR   B H    1 
ATOM   15953 H  HA   . TYR   B 1 427 ? 8.564  27.073  70.790 1.00 16.16 ? 427  TYR   B HA   1 
ATOM   15954 H  HB2  . TYR   B 1 427 ? 9.430  24.543  71.563 1.00 14.43 ? 427  TYR   B HB2  1 
ATOM   15955 H  HB3  . TYR   B 1 427 ? 8.075  24.916  70.887 1.00 14.43 ? 427  TYR   B HB3  1 
ATOM   15956 H  HD1  . TYR   B 1 427 ? 11.471 24.357  70.148 1.00 15.74 ? 427  TYR   B HD1  1 
ATOM   15957 H  HD2  . TYR   B 1 427 ? 7.893  24.932  68.482 1.00 16.78 ? 427  TYR   B HD2  1 
ATOM   15958 H  HE1  . TYR   B 1 427 ? 12.340 23.770  68.096 1.00 17.77 ? 427  TYR   B HE1  1 
ATOM   15959 H  HE2  . TYR   B 1 427 ? 8.743  24.327  66.425 1.00 17.75 ? 427  TYR   B HE2  1 
ATOM   15960 H  HH   . TYR   B 1 427 ? 11.924 23.925  65.756 1.00 15.72 ? 427  TYR   B HH   1 
ATOM   15961 N  N    . ASP   B 1 428 ? 8.017  27.529  73.166 1.00 13.46 ? 428  ASP   B N    1 
ATOM   15962 C  CA   . ASP   B 1 428 ? 7.721  27.775  74.599 1.00 14.45 ? 428  ASP   B CA   1 
ATOM   15963 C  C    . ASP   B 1 428 ? 7.009  26.553  75.184 1.00 15.26 ? 428  ASP   B C    1 
ATOM   15964 O  O    . ASP   B 1 428 ? 5.855  26.318  74.813 1.00 14.08 ? 428  ASP   B O    1 
ATOM   15965 C  CB   . ASP   B 1 428 ? 6.879  29.039  74.766 1.00 14.03 ? 428  ASP   B CB   1 
ATOM   15966 C  CG   . ASP   B 1 428 ? 6.790  29.526  76.203 1.00 15.90 ? 428  ASP   B CG   1 
ATOM   15967 O  OD1  . ASP   B 1 428 ? 6.970  28.701  77.116 1.00 14.23 ? 428  ASP   B OD1  1 
ATOM   15968 O  OD2  . ASP   B 1 428 ? 6.541  30.728  76.393 1.00 16.88 ? 428  ASP   B OD2  1 
ATOM   15969 H  H    . ASP   B 1 428 ? 7.478  27.917  72.619 1.00 16.16 ? 428  ASP   B H    1 
ATOM   15970 H  HA   . ASP   B 1 428 ? 8.551  27.914  75.081 1.00 17.35 ? 428  ASP   B HA   1 
ATOM   15971 H  HB2  . ASP   B 1 428 ? 7.255  29.744  74.216 1.00 16.84 ? 428  ASP   B HB2  1 
ATOM   15972 H  HB3  . ASP   B 1 428 ? 5.984  28.868  74.434 1.00 16.84 ? 428  ASP   B HB3  1 
ATOM   15973 N  N    . PRO   B 1 429 ? 7.645  25.796  76.102 1.00 13.45 ? 429  PRO   B N    1 
ATOM   15974 C  CA   . PRO   B 1 429 ? 7.047  24.562  76.611 1.00 15.79 ? 429  PRO   B CA   1 
ATOM   15975 C  C    . PRO   B 1 429 ? 5.873  24.816  77.569 1.00 15.85 ? 429  PRO   B C    1 
ATOM   15976 O  O    . PRO   B 1 429 ? 5.150  23.893  77.852 1.00 14.50 ? 429  PRO   B O    1 
ATOM   15977 C  CB   . PRO   B 1 429 ? 8.210  23.914  77.368 1.00 13.76 ? 429  PRO   B CB   1 
ATOM   15978 C  CG   . PRO   B 1 429 ? 9.061  25.080  77.818 1.00 11.96 ? 429  PRO   B CG   1 
ATOM   15979 C  CD   . PRO   B 1 429 ? 8.947  26.094  76.700 1.00 13.63 ? 429  PRO   B CD   1 
ATOM   15980 H  HA   . PRO   B 1 429 ? 6.673  24.020  75.899 1.00 18.95 ? 429  PRO   B HA   1 
ATOM   15981 H  HB2  . PRO   B 1 429 ? 7.894  23.394  78.124 1.00 16.52 ? 429  PRO   B HB2  1 
ATOM   15982 H  HB3  . PRO   B 1 429 ? 8.711  23.310  76.797 1.00 16.52 ? 429  PRO   B HB3  1 
ATOM   15983 H  HG2  . PRO   B 1 429 ? 8.742  25.445  78.658 1.00 14.36 ? 429  PRO   B HG2  1 
ATOM   15984 H  HG3  . PRO   B 1 429 ? 9.982  24.811  77.957 1.00 14.36 ? 429  PRO   B HG3  1 
ATOM   15985 H  HD2  . PRO   B 1 429 ? 8.986  27.003  77.036 1.00 16.36 ? 429  PRO   B HD2  1 
ATOM   15986 H  HD3  . PRO   B 1 429 ? 9.666  25.999  76.056 1.00 16.36 ? 429  PRO   B HD3  1 
ATOM   15987 N  N    . ARG   B 1 430 ? 5.710  26.065  78.008 1.00 14.11 ? 430  ARG   B N    1 
ATOM   15988 C  CA   . ARG   B 1 430 ? 4.559  26.401  78.889 1.00 15.49 ? 430  ARG   B CA   1 
ATOM   15989 C  C    . ARG   B 1 430 ? 3.252  26.040  78.169 1.00 15.74 ? 430  ARG   B C    1 
ATOM   15990 O  O    . ARG   B 1 430 ? 2.277  25.745  78.868 1.00 17.53 ? 430  ARG   B O    1 
ATOM   15991 C  CB   . ARG   B 1 430 ? 4.639  27.873  79.305 1.00 14.73 ? 430  ARG   B CB   1 
ATOM   15992 C  CG   . ARG   B 1 430 ? 5.759  28.182  80.286 1.00 16.02 ? 430  ARG   B CG   1 
ATOM   15993 C  CD   . ARG   B 1 430 ? 5.823  29.652  80.651 1.00 18.05 ? 430  ARG   B CD   1 
ATOM   15994 N  NE   . ARG   B 1 430 ? 6.170  30.496  79.518 1.00 16.95 ? 430  ARG   B NE   1 
ATOM   15995 C  CZ   . ARG   B 1 430 ? 6.665  31.724  79.619 1.00 19.62 ? 430  ARG   B CZ   1 
ATOM   15996 N  NH1  . ARG   B 1 430 ? 6.616  32.365  80.772 1.00 16.03 ? 430  ARG   B NH1  1 
ATOM   15997 N  NH2  . ARG   B 1 430 ? 7.211  32.305  78.565 1.00 20.35 ? 430  ARG   B NH2  1 
ATOM   15998 H  H    . ARG   B 1 430 ? 6.231  26.723  77.821 1.00 16.94 ? 430  ARG   B H    1 
ATOM   15999 H  HA   . ARG   B 1 430 ? 4.585  25.882  79.708 1.00 18.59 ? 430  ARG   B HA   1 
ATOM   16000 H  HB2  . ARG   B 1 430 ? 4.758  28.417  78.511 1.00 17.67 ? 430  ARG   B HB2  1 
ATOM   16001 H  HB3  . ARG   B 1 430 ? 3.793  28.133  79.703 1.00 17.67 ? 430  ARG   B HB3  1 
ATOM   16002 H  HG2  . ARG   B 1 430 ? 5.633  27.657  81.092 1.00 19.22 ? 430  ARG   B HG2  1 
ATOM   16003 H  HG3  . ARG   B 1 430 ? 6.607  27.910  79.900 1.00 19.22 ? 430  ARG   B HG3  1 
ATOM   16004 H  HD2  . ARG   B 1 430 ? 4.965  29.931  81.007 1.00 21.67 ? 430  ARG   B HD2  1 
ATOM   16005 H  HD3  . ARG   B 1 430 ? 6.477  29.778  81.356 1.00 21.67 ? 430  ARG   B HD3  1 
ATOM   16006 H  HE   . ARG   B 1 430 ? 6.046  30.178  78.729 1.00 20.35 ? 430  ARG   B HE   1 
ATOM   16007 H  HH11 . ARG   B 1 430 ? 6.263  31.987  81.459 1.00 19.23 ? 430  ARG   B HH11 1 
ATOM   16008 H  HH12 . ARG   B 1 430 ? 6.937  33.160  80.836 1.00 19.23 ? 430  ARG   B HH12 1 
ATOM   16009 H  HH21 . ARG   B 1 430 ? 7.246  31.888  77.814 1.00 24.43 ? 430  ARG   B HH21 1 
ATOM   16010 H  HH22 . ARG   B 1 430 ? 7.532  33.100  78.630 1.00 24.43 ? 430  ARG   B HH22 1 
ATOM   16011 N  N    . GLY   B 1 431 ? 3.238  26.042  76.835 1.00 15.02 ? 431  GLY   B N    1 
ATOM   16012 C  CA   . GLY   B 1 431 ? 2.053  25.674  76.031 1.00 15.85 ? 431  GLY   B CA   1 
ATOM   16013 C  C    . GLY   B 1 431 ? 2.190  24.362  75.261 1.00 16.84 ? 431  GLY   B C    1 
ATOM   16014 O  O    . GLY   B 1 431 ? 1.376  24.122  74.388 1.00 16.79 ? 431  GLY   B O    1 
ATOM   16015 H  H    . GLY   B 1 431 ? 3.921  26.259  76.360 1.00 18.03 ? 431  GLY   B H    1 
ATOM   16016 H  HA2  . GLY   B 1 431 ? 1.284  25.611  76.619 1.00 19.02 ? 431  GLY   B HA2  1 
ATOM   16017 H  HA3  . GLY   B 1 431 ? 1.870  26.388  75.400 1.00 19.02 ? 431  GLY   B HA3  1 
ATOM   16018 N  N    . ILE   B 1 432 ? 3.223  23.591  75.574 1.00 15.98 ? 432  ILE   B N    1 
ATOM   16019 C  CA   . ILE   B 1 432 ? 3.516  22.313  74.868 1.00 13.38 ? 432  ILE   B CA   1 
ATOM   16020 C  C    . ILE   B 1 432 ? 4.085  21.367  75.939 1.00 14.16 ? 432  ILE   B C    1 
ATOM   16021 O  O    . ILE   B 1 432 ? 5.264  21.330  76.127 1.00 14.57 ? 432  ILE   B O    1 
ATOM   16022 C  CB   . ILE   B 1 432 ? 4.490  22.537  73.698 1.00 14.22 ? 432  ILE   B CB   1 
ATOM   16023 C  CG1  . ILE   B 1 432 ? 4.433  23.952  73.128 1.00 16.10 ? 432  ILE   B CG1  1 
ATOM   16024 C  CG2  . ILE   B 1 432 ? 4.249  21.487  72.628 1.00 14.38 ? 432  ILE   B CG2  1 
ATOM   16025 C  CD1  . ILE   B 1 432 ? 5.512  24.235  72.112 1.00 14.70 ? 432  ILE   B CD1  1 
ATOM   16026 H  H    . ILE   B 1 432 ? 3.783  23.780  76.199 1.00 19.17 ? 432  ILE   B H    1 
ATOM   16027 H  HA   . ILE   B 1 432 ? 2.722  21.930  74.464 1.00 16.06 ? 432  ILE   B HA   1 
ATOM   16028 H  HB   . ILE   B 1 432 ? 5.391  22.439  74.043 1.00 17.07 ? 432  ILE   B HB   1 
ATOM   16029 H  HG12 . ILE   B 1 432 ? 3.566  24.093  72.716 1.00 19.33 ? 432  ILE   B HG12 1 
ATOM   16030 H  HG13 . ILE   B 1 432 ? 4.508  24.589  73.855 1.00 19.33 ? 432  ILE   B HG13 1 
ATOM   16031 H  HG21 . ILE   B 1 432 ? 4.863  21.629  71.891 1.00 17.25 ? 432  ILE   B HG21 1 
ATOM   16032 H  HG22 . ILE   B 1 432 ? 4.393  20.604  73.003 1.00 17.25 ? 432  ILE   B HG22 1 
ATOM   16033 H  HG23 . ILE   B 1 432 ? 3.337  21.556  72.306 1.00 17.25 ? 432  ILE   B HG23 1 
ATOM   16034 H  HD11 . ILE   B 1 432 ? 5.422  25.145  71.789 1.00 17.65 ? 432  ILE   B HD11 1 
ATOM   16035 H  HD12 . ILE   B 1 432 ? 6.383  24.123  72.525 1.00 17.65 ? 432  ILE   B HD12 1 
ATOM   16036 H  HD13 . ILE   B 1 432 ? 5.426  23.619  71.368 1.00 17.65 ? 432  ILE   B HD13 1 
ATOM   16037 N  N    . GLN   B 1 433 ? 3.207  20.617  76.597 1.00 14.68 ? 433  GLN   B N    1 
ATOM   16038 C  CA   . GLN   B 1 433 ? 3.634  19.863  77.804 1.00 14.73 ? 433  GLN   B CA   1 
ATOM   16039 C  C    . GLN   B 1 433 ? 4.611  18.709  77.518 1.00 14.68 ? 433  GLN   B C    1 
ATOM   16040 O  O    . GLN   B 1 433 ? 5.542  18.544  78.255 1.00 15.19 ? 433  GLN   B O    1 
ATOM   16041 C  CB   . GLN   B 1 433 ? 2.386  19.356  78.538 1.00 17.02 ? 433  GLN   B CB   1 
ATOM   16042 C  CG   . GLN   B 1 433 ? 1.502  20.470  79.083 1.00 16.87 ? 433  GLN   B CG   1 
ATOM   16043 C  CD   . GLN   B 1 433 ? 2.119  21.234  80.231 1.00 16.71 ? 433  GLN   B CD   1 
ATOM   16044 O  OE1  . GLN   B 1 433 ? 3.019  20.762  80.910 1.00 16.73 ? 433  GLN   B OE1  1 
ATOM   16045 N  NE2  . GLN   B 1 433 ? 1.623  22.435  80.465 1.00 19.96 ? 433  GLN   B NE2  1 
ATOM   16046 H  H    . GLN   B 1 433 ? 2.380  20.524  76.380 1.00 17.61 ? 433  GLN   B H    1 
ATOM   16047 H  HA   . GLN   B 1 433 ? 4.135  20.478  78.362 1.00 17.68 ? 433  GLN   B HA   1 
ATOM   16048 H  HB2  . GLN   B 1 433 ? 1.864  18.807  77.932 1.00 20.43 ? 433  GLN   B HB2  1 
ATOM   16049 H  HB3  . GLN   B 1 433 ? 2.662  18.784  79.272 1.00 20.43 ? 433  GLN   B HB3  1 
ATOM   16050 H  HG2  . GLN   B 1 433 ? 1.299  21.090  78.365 1.00 20.25 ? 433  GLN   B HG2  1 
ATOM   16051 H  HG3  . GLN   B 1 433 ? 0.659  20.089  79.375 1.00 20.25 ? 433  GLN   B HG3  1 
ATOM   16052 H  HE21 . GLN   B 1 433 ? 0.990  22.742  79.971 1.00 23.96 ? 433  GLN   B HE21 1 
ATOM   16053 H  HE22 . GLN   B 1 433 ? 1.933  22.910  81.111 1.00 23.96 ? 433  GLN   B HE22 1 
ATOM   16054 N  N    . GLY   B 1 434 ? 4.291  17.907  76.511 1.00 14.64 ? 434  GLY   B N    1 
ATOM   16055 C  CA   . GLY   B 1 434 ? 5.182  16.785  76.178 1.00 13.29 ? 434  GLY   B CA   1 
ATOM   16056 C  C    . GLY   B 1 434 ? 6.543  17.306  75.757 1.00 12.87 ? 434  GLY   B C    1 
ATOM   16057 O  O    . GLY   B 1 434 ? 7.559  16.743  76.184 1.00 12.41 ? 434  GLY   B O    1 
ATOM   16058 H  H    . GLY   B 1 434 ? 3.590  17.984  76.019 1.00 17.57 ? 434  GLY   B H    1 
ATOM   16059 H  HA2  . GLY   B 1 434 ? 5.276  16.199  76.945 1.00 15.96 ? 434  GLY   B HA2  1 
ATOM   16060 H  HA3  . GLY   B 1 434 ? 4.795  16.257  75.463 1.00 15.96 ? 434  GLY   B HA3  1 
ATOM   16061 N  N    . HIS   B 1 435 ? 6.553  18.367  74.953 1.00 13.36 ? 435  HIS   B N    1 
ATOM   16062 C  CA   . HIS   B 1 435 ? 7.845  18.893  74.429 1.00 12.39 ? 435  HIS   B CA   1 
ATOM   16063 C  C    . HIS   B 1 435 ? 8.720  19.404  75.579 1.00 12.41 ? 435  HIS   B C    1 
ATOM   16064 O  O    . HIS   B 1 435 ? 9.954  19.305  75.489 1.00 14.60 ? 435  HIS   B O    1 
ATOM   16065 C  CB   . HIS   B 1 435 ? 7.598  19.972  73.370 1.00 12.05 ? 435  HIS   B CB   1 
ATOM   16066 C  CG   . HIS   B 1 435 ? 8.786  20.261  72.517 1.00 12.94 ? 435  HIS   B CG   1 
ATOM   16067 N  ND1  . HIS   B 1 435 ? 9.371  19.314  71.706 1.00 13.72 ? 435  HIS   B ND1  1 
ATOM   16068 C  CD2  . HIS   B 1 435 ? 9.495  21.383  72.350 1.00 17.69 ? 435  HIS   B CD2  1 
ATOM   16069 C  CE1  . HIS   B 1 435 ? 10.399 19.859  71.075 1.00 17.45 ? 435  HIS   B CE1  1 
ATOM   16070 N  NE2  . HIS   B 1 435 ? 10.493 21.115  71.452 1.00 15.37 ? 435  HIS   B NE2  1 
ATOM   16071 H  H    . HIS   B 1 435 ? 5.853  18.795  74.697 1.00 16.04 ? 435  HIS   B H    1 
ATOM   16072 H  HA   . HIS   B 1 435 ? 8.327  18.171  73.996 1.00 14.87 ? 435  HIS   B HA   1 
ATOM   16073 H  HB2  . HIS   B 1 435 ? 6.863  19.694  72.802 1.00 14.46 ? 435  HIS   B HB2  1 
ATOM   16074 H  HB3  . HIS   B 1 435 ? 7.321  20.790  73.812 1.00 14.46 ? 435  HIS   B HB3  1 
ATOM   16075 H  HD2  . HIS   B 1 435 ? 9.338  22.198  72.769 1.00 21.24 ? 435  HIS   B HD2  1 
ATOM   16076 H  HE1  . HIS   B 1 435 ? 10.958 19.428  70.470 1.00 20.94 ? 435  HIS   B HE1  1 
ATOM   16077 H  HE2  . HIS   B 1 435 ? 11.085 21.676  71.179 1.00 18.45 ? 435  HIS   B HE2  1 
ATOM   16078 N  N    . GLY   B 1 436 ? 8.097  19.968  76.617 1.00 11.59 ? 436  GLY   B N    1 
ATOM   16079 C  CA   . GLY   B 1 436 ? 8.868  20.436  77.784 1.00 11.65 ? 436  GLY   B CA   1 
ATOM   16080 C  C    . GLY   B 1 436 ? 9.598  19.290  78.462 1.00 12.48 ? 436  GLY   B C    1 
ATOM   16081 O  O    . GLY   B 1 436 ? 10.671 19.526  79.026 1.00 12.04 ? 436  GLY   B O    1 
ATOM   16082 H  H    . GLY   B 1 436 ? 7.247  20.089  76.670 1.00 13.91 ? 436  GLY   B H    1 
ATOM   16083 H  HA2  . GLY   B 1 436 ? 9.508  21.108  77.502 1.00 13.99 ? 436  GLY   B HA2  1 
ATOM   16084 H  HA3  . GLY   B 1 436 ? 8.271  20.862  78.419 1.00 13.99 ? 436  GLY   B HA3  1 
ATOM   16085 N  N    . ILE   B 1 437 ? 9.013  18.092  78.426 1.00 13.91 ? 437  ILE   B N    1 
ATOM   16086 C  CA   . ILE   B 1 437 ? 9.713  16.899  78.981 1.00 14.85 ? 437  ILE   B CA   1 
ATOM   16087 C  C    . ILE   B 1 437 ? 11.014 16.713  78.195 1.00 12.19 ? 437  ILE   B C    1 
ATOM   16088 O  O    . ILE   B 1 437 ? 12.063 16.513  78.818 1.00 12.87 ? 437  ILE   B O    1 
ATOM   16089 C  CB   . ILE   B 1 437 ? 8.819  15.644  78.894 1.00 14.62 ? 437  ILE   B CB   1 
ATOM   16090 C  CG1  . ILE   B 1 437 ? 7.448  15.880  79.533 1.00 12.73 ? 437  ILE   B CG1  1 
ATOM   16091 C  CG2  . ILE   B 1 437 ? 9.523  14.434  79.487 1.00 13.02 ? 437  ILE   B CG2  1 
ATOM   16092 C  CD1  . ILE   B 1 437 ? 6.514  14.694  79.442 1.00 13.39 ? 437  ILE   B CD1  1 
ATOM   16093 H  H    . ILE   B 1 437 ? 8.234  17.937  78.097 1.00 16.70 ? 437  ILE   B H    1 
ATOM   16094 H  HA   . ILE   B 1 437 ? 9.912  17.033  79.921 1.00 17.82 ? 437  ILE   B HA   1 
ATOM   16095 H  HB   . ILE   B 1 437 ? 8.660  15.458  77.956 1.00 17.55 ? 437  ILE   B HB   1 
ATOM   16096 H  HG12 . ILE   B 1 437 ? 7.572  16.111  80.467 1.00 15.28 ? 437  ILE   B HG12 1 
ATOM   16097 H  HG13 . ILE   B 1 437 ? 7.029  16.643  79.105 1.00 15.28 ? 437  ILE   B HG13 1 
ATOM   16098 H  HG21 . ILE   B 1 437 ? 8.944  13.658  79.422 1.00 15.63 ? 437  ILE   B HG21 1 
ATOM   16099 H  HG22 . ILE   B 1 437 ? 10.344 14.266  78.999 1.00 15.63 ? 437  ILE   B HG22 1 
ATOM   16100 H  HG23 . ILE   B 1 437 ? 9.730  14.605  80.419 1.00 15.63 ? 437  ILE   B HG23 1 
ATOM   16101 H  HD11 . ILE   B 1 437 ? 5.669  14.914  79.865 1.00 16.07 ? 437  ILE   B HD11 1 
ATOM   16102 H  HD12 . ILE   B 1 437 ? 6.361  14.473  78.510 1.00 16.07 ? 437  ILE   B HD12 1 
ATOM   16103 H  HD13 . ILE   B 1 437 ? 6.912  13.933  79.893 1.00 16.07 ? 437  ILE   B HD13 1 
ATOM   16104 N  N    . THR   B 1 438 ? 10.918 16.760  76.865 1.00 14.69 ? 438  THR   B N    1 
ATOM   16105 C  CA   . THR   B 1 438 ? 12.123 16.567  76.017 1.00 11.36 ? 438  THR   B CA   1 
ATOM   16106 C  C    . THR   B 1 438 ? 13.227 17.528  76.479 1.00 11.57 ? 438  THR   B C    1 
ATOM   16107 O  O    . THR   B 1 438 ? 14.352 17.078  76.696 1.00 12.25 ? 438  THR   B O    1 
ATOM   16108 C  CB   . THR   B 1 438 ? 11.792 16.749  74.531 1.00 13.93 ? 438  THR   B CB   1 
ATOM   16109 O  OG1  . THR   B 1 438 ? 10.928 15.692  74.113 1.00 13.56 ? 438  THR   B OG1  1 
ATOM   16110 C  CG2  . THR   B 1 438 ? 13.031 16.788  73.663 1.00 14.04 ? 438  THR   B CG2  1 
ATOM   16111 H  H    . THR   B 1 438 ? 10.188 16.898  76.433 1.00 17.63 ? 438  THR   B H    1 
ATOM   16112 H  HA   . THR   B 1 438 ? 12.443 15.657  76.118 1.00 13.64 ? 438  THR   B HA   1 
ATOM   16113 H  HB   . THR   B 1 438 ? 11.350 17.606  74.425 1.00 16.72 ? 438  THR   B HB   1 
ATOM   16114 H  HG1  . THR   B 1 438 ? 10.831 15.722  73.279 1.00 16.28 ? 438  THR   B HG1  1 
ATOM   16115 H  HG21 . THR   B 1 438 ? 12.773 16.904  72.735 1.00 16.86 ? 438  THR   B HG21 1 
ATOM   16116 H  HG22 . THR   B 1 438 ? 13.595 17.529  73.936 1.00 16.86 ? 438  THR   B HG22 1 
ATOM   16117 H  HG23 . THR   B 1 438 ? 13.521 15.956  73.760 1.00 16.86 ? 438  THR   B HG23 1 
ATOM   16118 N  N    . TYR   B 1 439 ? 12.896 18.811  76.627 1.00 12.26 ? 439  TYR   B N    1 
ATOM   16119 C  CA   . TYR   B 1 439 ? 13.904 19.812  77.059 1.00 13.28 ? 439  TYR   B CA   1 
ATOM   16120 C  C    . TYR   B 1 439 ? 14.547 19.389  78.386 1.00 13.12 ? 439  TYR   B C    1 
ATOM   16121 O  O    . TYR   B 1 439 ? 15.774 19.457  78.511 1.00 14.09 ? 439  TYR   B O    1 
ATOM   16122 C  CB   . TYR   B 1 439 ? 13.265 21.187  77.269 1.00 11.25 ? 439  TYR   B CB   1 
ATOM   16123 C  CG   . TYR   B 1 439 ? 12.797 21.923  76.040 1.00 11.42 ? 439  TYR   B CG   1 
ATOM   16124 C  CD1  . TYR   B 1 439 ? 13.353 21.687  74.795 1.00 10.53 ? 439  TYR   B CD1  1 
ATOM   16125 C  CD2  . TYR   B 1 439 ? 11.806 22.885  76.134 1.00 13.54 ? 439  TYR   B CD2  1 
ATOM   16126 C  CE1  . TYR   B 1 439 ? 12.926 22.378  73.673 1.00 11.18 ? 439  TYR   B CE1  1 
ATOM   16127 C  CE2  . TYR   B 1 439 ? 11.366 23.584  75.023 1.00 14.60 ? 439  TYR   B CE2  1 
ATOM   16128 C  CZ   . TYR   B 1 439 ? 11.931 23.332  73.788 1.00 12.81 ? 439  TYR   B CZ   1 
ATOM   16129 O  OH   . TYR   B 1 439 ? 11.494 24.033  72.692 1.00 12.67 ? 439  TYR   B OH   1 
ATOM   16130 H  H    . TYR   B 1 439 ? 12.109 19.129  76.487 1.00 14.72 ? 439  TYR   B H    1 
ATOM   16131 H  HA   . TYR   B 1 439 ? 14.572 19.863  76.357 1.00 15.94 ? 439  TYR   B HA   1 
ATOM   16132 H  HB2  . TYR   B 1 439 ? 12.505 21.078  77.862 1.00 13.51 ? 439  TYR   B HB2  1 
ATOM   16133 H  HB3  . TYR   B 1 439 ? 13.907 21.750  77.730 1.00 13.51 ? 439  TYR   B HB3  1 
ATOM   16134 H  HD1  . TYR   B 1 439 ? 14.027 21.052  74.710 1.00 12.63 ? 439  TYR   B HD1  1 
ATOM   16135 H  HD2  . TYR   B 1 439 ? 11.427 23.066  76.964 1.00 16.26 ? 439  TYR   B HD2  1 
ATOM   16136 H  HE1  . TYR   B 1 439 ? 13.308 22.201  72.844 1.00 13.41 ? 439  TYR   B HE1  1 
ATOM   16137 H  HE2  . TYR   B 1 439 ? 10.693 24.220  75.108 1.00 17.53 ? 439  TYR   B HE2  1 
ATOM   16138 H  HH   . TYR   B 1 439 ? 11.109 24.736  72.944 1.00 15.21 ? 439  TYR   B HH   1 
ATOM   16139 N  N    . ALA   B 1 440 ? 13.729 18.961  79.347 1.00 12.23 ? 440  ALA   B N    1 
ATOM   16140 C  CA   . ALA   B 1 440 ? 14.252 18.652  80.696 1.00 10.96 ? 440  ALA   B CA   1 
ATOM   16141 C  C    . ALA   B 1 440 ? 15.105 17.380  80.716 1.00 12.87 ? 440  ALA   B C    1 
ATOM   16142 O  O    . ALA   B 1 440 ? 16.107 17.381  81.433 1.00 13.06 ? 440  ALA   B O    1 
ATOM   16143 C  CB   . ALA   B 1 440 ? 13.089 18.517  81.654 1.00 13.01 ? 440  ALA   B CB   1 
ATOM   16144 H  H    . ALA   B 1 440 ? 12.883 18.842  79.250 1.00 14.68 ? 440  ALA   B H    1 
ATOM   16145 H  HA   . ALA   B 1 440 ? 14.832 19.381  80.968 1.00 13.16 ? 440  ALA   B HA   1 
ATOM   16146 H  HB1  . ALA   B 1 440 ? 13.423 18.314  82.542 1.00 15.62 ? 440  ALA   B HB1  1 
ATOM   16147 H  HB2  . ALA   B 1 440 ? 12.591 19.349  81.678 1.00 15.62 ? 440  ALA   B HB2  1 
ATOM   16148 H  HB3  . ALA   B 1 440 ? 12.506 17.801  81.357 1.00 15.62 ? 440  ALA   B HB3  1 
ATOM   16149 N  N    . VAL   B 1 441 ? 14.727 16.354  79.946 1.00 12.64 ? 441  VAL   B N    1 
ATOM   16150 C  CA   . VAL   B 1 441 ? 15.438 15.040  80.053 1.00 13.63 ? 441  VAL   B CA   1 
ATOM   16151 C  C    . VAL   B 1 441 ? 16.432 14.810  78.905 1.00 11.67 ? 441  VAL   B C    1 
ATOM   16152 O  O    . VAL   B 1 441 ? 17.165 13.817  78.972 1.00 12.75 ? 441  VAL   B O    1 
ATOM   16153 C  CB   . VAL   B 1 441 ? 14.429 13.882  80.138 1.00 11.83 ? 441  VAL   B CB   1 
ATOM   16154 C  CG1  . VAL   B 1 441 ? 13.460 14.078  81.291 1.00 15.42 ? 441  VAL   B CG1  1 
ATOM   16155 C  CG2  . VAL   B 1 441 ? 13.675 13.698  78.832 1.00 12.31 ? 441  VAL   B CG2  1 
ATOM   16156 H  H    . VAL   B 1 441 ? 14.087 16.380  79.372 1.00 15.17 ? 441  VAL   B H    1 
ATOM   16157 H  HA   . VAL   B 1 441 ? 15.957 15.067  80.872 1.00 16.36 ? 441  VAL   B HA   1 
ATOM   16158 H  HB   . VAL   B 1 441 ? 14.938 13.073  80.304 1.00 14.20 ? 441  VAL   B HB   1 
ATOM   16159 H  HG11 . VAL   B 1 441 ? 12.837 13.335  81.320 1.00 18.50 ? 441  VAL   B HG11 1 
ATOM   16160 H  HG12 . VAL   B 1 441 ? 13.953 14.119  82.125 1.00 18.50 ? 441  VAL   B HG12 1 
ATOM   16161 H  HG13 . VAL   B 1 441 ? 12.970 14.905  81.165 1.00 18.50 ? 441  VAL   B HG13 1 
ATOM   16162 H  HG21 . VAL   B 1 441 ? 13.049 12.962  78.920 1.00 14.78 ? 441  VAL   B HG21 1 
ATOM   16163 H  HG22 . VAL   B 1 441 ? 13.190 14.511  78.621 1.00 14.78 ? 441  VAL   B HG22 1 
ATOM   16164 H  HG23 . VAL   B 1 441 ? 14.304 13.503  78.120 1.00 14.78 ? 441  VAL   B HG23 1 
ATOM   16165 N  N    . ASN   B 1 442 ? 16.450 15.688  77.904 1.00 11.98 ? 442  ASN   B N    1 
ATOM   16166 C  CA   . ASN   B 1 442 ? 17.350 15.485  76.739 1.00 13.48 ? 442  ASN   B CA   1 
ATOM   16167 C  C    . ASN   B 1 442 ? 18.766 15.180  77.239 1.00 12.79 ? 442  ASN   B C    1 
ATOM   16168 O  O    . ASN   B 1 442 ? 19.309 15.991  77.999 1.00 12.53 ? 442  ASN   B O    1 
ATOM   16169 C  CB   . ASN   B 1 442 ? 17.323 16.694  75.805 1.00 10.45 ? 442  ASN   B CB   1 
ATOM   16170 C  CG   . ASN   B 1 442 ? 17.881 16.409  74.427 1.00 12.51 ? 442  ASN   B CG   1 
ATOM   16171 O  OD1  . ASN   B 1 442 ? 18.869 15.694  74.283 1.00 12.23 ? 442  ASN   B OD1  1 
ATOM   16172 N  ND2  . ASN   B 1 442 ? 17.256 16.976  73.409 1.00 12.70 ? 442  ASN   B ND2  1 
ATOM   16173 H  H    . ASN   B 1 442 ? 15.964 16.397  77.868 1.00 14.38 ? 442  ASN   B H    1 
ATOM   16174 H  HA   . ASN   B 1 442 ? 17.037 14.727  76.220 1.00 16.18 ? 442  ASN   B HA   1 
ATOM   16175 H  HB2  . ASN   B 1 442 ? 16.408 17.005  75.717 1.00 12.55 ? 442  ASN   B HB2  1 
ATOM   16176 H  HB3  . ASN   B 1 442 ? 17.830 17.416  76.208 1.00 12.55 ? 442  ASN   B HB3  1 
ATOM   16177 H  HD21 . ASN   B 1 442 ? 17.539 16.850  72.607 1.00 15.25 ? 442  ASN   B HD21 1 
ATOM   16178 H  HD22 . ASN   B 1 442 ? 16.567 17.471  73.549 1.00 15.25 ? 442  ASN   B HD22 1 
ATOM   16179 N  N    . ASN   B 1 443 ? 19.345 14.062  76.790 1.00 13.33 ? 443  ASN   B N    1 
ATOM   16180 C  CA   . ASN   B 1 443 ? 20.694 13.646  77.262 1.00 13.07 ? 443  ASN   B CA   1 
ATOM   16181 C  C    . ASN   B 1 443 ? 21.769 14.655  76.836 1.00 11.26 ? 443  ASN   B C    1 
ATOM   16182 O  O    . ASN   B 1 443 ? 22.844 14.646  77.441 1.00 13.29 ? 443  ASN   B O    1 
ATOM   16183 C  CB   . ASN   B 1 443 ? 21.048 12.238  76.772 1.00 13.32 ? 443  ASN   B CB   1 
ATOM   16184 C  CG   . ASN   B 1 443 ? 20.153 11.163  77.353 1.00 14.37 ? 443  ASN   B CG   1 
ATOM   16185 O  OD1  . ASN   B 1 443 ? 19.847 11.180  78.542 1.00 14.04 ? 443  ASN   B OD1  1 
ATOM   16186 N  ND2  . ASN   B 1 443 ? 19.728 10.225  76.522 1.00 12.79 ? 443  ASN   B ND2  1 
ATOM   16187 H  H    . ASN   B 1 443 ? 18.986 13.529  76.218 1.00 16.00 ? 443  ASN   B H    1 
ATOM   16188 H  HA   . ASN   B 1 443 ? 20.667 13.627  78.231 1.00 15.68 ? 443  ASN   B HA   1 
ATOM   16189 H  HB2  . ASN   B 1 443 ? 20.987 12.214  75.804 1.00 15.99 ? 443  ASN   B HB2  1 
ATOM   16190 H  HB3  . ASN   B 1 443 ? 21.970 12.043  77.003 1.00 15.99 ? 443  ASN   B HB3  1 
ATOM   16191 H  HD21 . ASN   B 1 443 ? 19.217 9.596   76.809 1.00 15.35 ? 443  ASN   B HD21 1 
ATOM   16192 H  HD22 . ASN   B 1 443 ? 19.963 10.245  75.695 1.00 15.35 ? 443  ASN   B HD22 1 
ATOM   16193 N  N    . ARG   B 1 444 ? 21.491 15.484  75.829 1.00 11.07 ? 444  ARG   B N    1 
ATOM   16194 C  CA   . ARG   B 1 444 ? 22.543 16.411  75.334 1.00 12.87 ? 444  ARG   B CA   1 
ATOM   16195 C  C    . ARG   B 1 444 ? 22.266 17.834  75.837 1.00 13.32 ? 444  ARG   B C    1 
ATOM   16196 O  O    . ARG   B 1 444 ? 22.999 18.757  75.447 1.00 10.91 ? 444  ARG   B O    1 
ATOM   16197 C  CB   . ARG   B 1 444 ? 22.670 16.331  73.805 1.00 11.72 ? 444  ARG   B CB   1 
ATOM   16198 C  CG   . ARG   B 1 444 ? 21.700 17.189  73.005 1.00 11.29 ? 444  ARG   B CG   1 
ATOM   16199 C  CD   . ARG   B 1 444 ? 22.090 17.114  71.537 1.00 11.50 ? 444  ARG   B CD   1 
ATOM   16200 N  NE   . ARG   B 1 444 ? 21.371 18.033  70.666 1.00 10.69 ? 444  ARG   B NE   1 
ATOM   16201 C  CZ   . ARG   B 1 444 ? 21.894 18.624  69.597 1.00 10.69 ? 444  ARG   B CZ   1 
ATOM   16202 N  NH1  . ARG   B 1 444 ? 23.156 18.409  69.271 1.00 10.65 ? 444  ARG   B NH1  1 
ATOM   16203 N  NH2  . ARG   B 1 444 ? 21.151 19.429  68.857 1.00 9.75  ? 444  ARG   B NH2  1 
ATOM   16204 H  H    . ARG   B 1 444 ? 20.734 15.534  75.425 1.00 13.29 ? 444  ARG   B H    1 
ATOM   16205 H  HA   . ARG   B 1 444 ? 23.404 16.142  75.691 1.00 15.44 ? 444  ARG   B HA   1 
ATOM   16206 H  HB2  . ARG   B 1 444 ? 23.574 16.584  73.560 1.00 14.07 ? 444  ARG   B HB2  1 
ATOM   16207 H  HB3  . ARG   B 1 444 ? 22.552 15.406  73.537 1.00 14.07 ? 444  ARG   B HB3  1 
ATOM   16208 H  HG2  . ARG   B 1 444 ? 20.791 16.875  73.129 1.00 13.55 ? 444  ARG   B HG2  1 
ATOM   16209 H  HG3  . ARG   B 1 444 ? 21.728 18.108  73.315 1.00 13.55 ? 444  ARG   B HG3  1 
ATOM   16210 H  HD2  . ARG   B 1 444 ? 23.041 17.291  71.459 1.00 13.81 ? 444  ARG   B HD2  1 
ATOM   16211 H  HD3  . ARG   B 1 444 ? 21.943 16.208  71.222 1.00 13.81 ? 444  ARG   B HD3  1 
ATOM   16212 H  HE   . ARG   B 1 444 ? 20.550 18.205  70.857 1.00 12.84 ? 444  ARG   B HE   1 
ATOM   16213 H  HH11 . ARG   B 1 444 ? 23.641 17.886  69.751 1.00 12.79 ? 444  ARG   B HH11 1 
ATOM   16214 H  HH12 . ARG   B 1 444 ? 23.493 18.792  68.579 1.00 12.79 ? 444  ARG   B HH12 1 
ATOM   16215 H  HH21 . ARG   B 1 444 ? 20.329 19.570  69.068 1.00 11.70 ? 444  ARG   B HH21 1 
ATOM   16216 H  HH22 . ARG   B 1 444 ? 21.489 19.812  68.165 1.00 11.70 ? 444  ARG   B HH22 1 
ATOM   16217 N  N    . GLY   B 1 445 ? 21.270 17.979  76.710 1.00 11.62 ? 445  GLY   B N    1 
ATOM   16218 C  CA   . GLY   B 1 445 ? 20.950 19.306  77.259 1.00 9.71  ? 445  GLY   B CA   1 
ATOM   16219 C  C    . GLY   B 1 445 ? 19.780 19.949  76.540 1.00 12.68 ? 445  GLY   B C    1 
ATOM   16220 O  O    . GLY   B 1 445 ? 19.126 19.262  75.746 1.00 15.59 ? 445  GLY   B O    1 
ATOM   16221 H  H    . GLY   B 1 445 ? 20.773 17.338  76.996 1.00 13.94 ? 445  GLY   B H    1 
ATOM   16222 H  HA2  . GLY   B 1 445 ? 20.743 19.224  78.203 1.00 11.66 ? 445  GLY   B HA2  1 
ATOM   16223 H  HA3  . GLY   B 1 445 ? 21.728 19.881  77.188 1.00 11.66 ? 445  GLY   B HA3  1 
ATOM   16224 N  N    . GLY   B 1 446 ? 19.536 21.231  76.817 1.00 10.98 ? 446  GLY   B N    1 
ATOM   16225 C  CA   . GLY   B 1 446 ? 18.409 21.948  76.194 1.00 12.40 ? 446  GLY   B CA   1 
ATOM   16226 C  C    . GLY   B 1 446 ? 18.379 21.770  74.689 1.00 11.18 ? 446  GLY   B C    1 
ATOM   16227 O  O    . GLY   B 1 446 ? 19.206 22.389  74.013 1.00 11.53 ? 446  GLY   B O    1 
ATOM   16228 H  H    . GLY   B 1 446 ? 20.006 21.705  77.359 1.00 13.18 ? 446  GLY   B H    1 
ATOM   16229 H  HA2  . GLY   B 1 446 ? 17.575 21.628  76.573 1.00 14.89 ? 446  GLY   B HA2  1 
ATOM   16230 H  HA3  . GLY   B 1 446 ? 18.472 22.893  76.405 1.00 14.89 ? 446  GLY   B HA3  1 
ATOM   16231 N  N    . CYS   B 1 447 ? 17.415 21.001  74.188 1.00 11.27 ? 447  CYS   B N    1 
ATOM   16232 C  CA   . CYS   B 1 447 ? 17.326 20.689  72.743 1.00 13.64 ? 447  CYS   B CA   1 
ATOM   16233 C  C    . CYS   B 1 447 ? 15.950 20.112  72.406 1.00 9.81  ? 447  CYS   B C    1 
ATOM   16234 O  O    . CYS   B 1 447 ? 15.421 19.348  73.197 1.00 12.57 ? 447  CYS   B O    1 
ATOM   16235 C  CB   . CYS   B 1 447 ? 18.465 19.757  72.329 1.00 13.38 ? 447  CYS   B CB   1 
ATOM   16236 S  SG   . CYS   B 1 447 ? 18.187 18.909  70.743 1.00 12.21 ? 447  CYS   B SG   1 
ATOM   16237 H  H    . CYS   B 1 447 ? 16.794 20.644  74.664 1.00 13.53 ? 447  CYS   B H    1 
ATOM   16238 H  HA   . CYS   B 1 447 ? 17.426 21.507  72.232 1.00 16.37 ? 447  CYS   B HA   1 
ATOM   16239 H  HB2  . CYS   B 1 447 ? 19.286 20.270  72.271 1.00 16.05 ? 447  CYS   B HB2  1 
ATOM   16240 H  HB3  . CYS   B 1 447 ? 18.595 19.092  73.023 1.00 16.05 ? 447  CYS   B HB3  1 
ATOM   16241 H  HG   . CYS   B 1 447 ? 17.736 19.686  69.947 1.00 14.66 ? 447  CYS   B HG   1 
ATOM   16242 N  N    . HIS   B 1 448 ? 15.446 20.460  71.224 1.00 11.48 ? 448  HIS   B N    1 
ATOM   16243 C  CA   . HIS   B 1 448 ? 14.118 20.000  70.789 1.00 12.54 ? 448  HIS   B CA   1 
ATOM   16244 C  C    . HIS   B 1 448 ? 14.134 18.779  69.873 1.00 12.40 ? 448  HIS   B C    1 
ATOM   16245 O  O    . HIS   B 1 448 ? 13.219 17.994  69.921 1.00 13.86 ? 448  HIS   B O    1 
ATOM   16246 C  CB   . HIS   B 1 448 ? 13.506 21.112  69.916 1.00 12.25 ? 448  HIS   B CB   1 
ATOM   16247 C  CG   . HIS   B 1 448 ? 14.323 21.433  68.713 1.00 14.84 ? 448  HIS   B CG   1 
ATOM   16248 N  ND1  . HIS   B 1 448 ? 15.650 21.787  68.785 1.00 11.48 ? 448  HIS   B ND1  1 
ATOM   16249 C  CD2  . HIS   B 1 448 ? 14.007 21.430  67.421 1.00 12.76 ? 448  HIS   B CD2  1 
ATOM   16250 C  CE1  . HIS   B 1 448 ? 16.109 22.002  67.565 1.00 11.69 ? 448  HIS   B CE1  1 
ATOM   16251 N  NE2  . HIS   B 1 448 ? 15.133 21.778  66.721 1.00 12.71 ? 448  HIS   B NE2  1 
ATOM   16252 H  H    . HIS   B 1 448 ? 15.853 20.961  70.656 1.00 13.78 ? 448  HIS   B H    1 
ATOM   16253 H  HA   . HIS   B 1 448 ? 13.636 19.781  71.602 1.00 15.05 ? 448  HIS   B HA   1 
ATOM   16254 H  HB2  . HIS   B 1 448 ? 12.618 20.841  69.634 1.00 14.70 ? 448  HIS   B HB2  1 
ATOM   16255 H  HB3  . HIS   B 1 448 ? 13.401 21.914  70.451 1.00 14.70 ? 448  HIS   B HB3  1 
ATOM   16256 H  HD2  . HIS   B 1 448 ? 13.174 21.229  67.059 1.00 15.32 ? 448  HIS   B HD2  1 
ATOM   16257 H  HE1  . HIS   B 1 448 ? 16.973 22.266  67.344 1.00 14.03 ? 448  HIS   B HE1  1 
ATOM   16258 H  HE2  . HIS   B 1 448 ? 15.189 21.839  65.865 1.00 15.26 ? 448  HIS   B HE2  1 
ATOM   16259 N  N    . ILE   B 1 449 ? 15.195 18.647  69.083 1.00 11.90 ? 449  ILE   B N    1 
ATOM   16260 C  CA   . ILE   B 1 449 ? 15.149 17.680  67.957 1.00 12.45 ? 449  ILE   B CA   1 
ATOM   16261 C  C    . ILE   B 1 449 ? 15.494 16.234  68.364 1.00 13.28 ? 449  ILE   B C    1 
ATOM   16262 O  O    . ILE   B 1 449 ? 15.243 15.355  67.569 1.00 12.70 ? 449  ILE   B O    1 
ATOM   16263 C  CB   . ILE   B 1 449 ? 15.990 18.261  66.782 1.00 10.91 ? 449  ILE   B CB   1 
ATOM   16264 C  CG1  . ILE   B 1 449 ? 15.615 17.624  65.442 1.00 12.46 ? 449  ILE   B CG1  1 
ATOM   16265 C  CG2  . ILE   B 1 449 ? 17.483 18.205  67.065 1.00 11.75 ? 449  ILE   B CG2  1 
ATOM   16266 C  CD1  . ILE   B 1 449 ? 14.178 17.866  65.049 1.00 13.58 ? 449  ILE   B CD1  1 
ATOM   16267 H  H    . ILE   B 1 449 ? 15.931 19.084  69.166 1.00 14.28 ? 449  ILE   B H    1 
ATOM   16268 H  HA   . ILE   B 1 449 ? 14.235 17.581  67.649 1.00 14.94 ? 449  ILE   B HA   1 
ATOM   16269 H  HB   . ILE   B 1 449 ? 15.766 19.202  66.708 1.00 13.10 ? 449  ILE   B HB   1 
ATOM   16270 H  HG12 . ILE   B 1 449 ? 16.197 17.975  64.750 1.00 14.96 ? 449  ILE   B HG12 1 
ATOM   16271 H  HG13 . ILE   B 1 449 ? 15.775 16.668  65.489 1.00 14.96 ? 449  ILE   B HG13 1 
ATOM   16272 H  HG21 . ILE   B 1 449 ? 17.969 18.575  66.312 1.00 14.11 ? 449  ILE   B HG21 1 
ATOM   16273 H  HG22 . ILE   B 1 449 ? 17.681 18.721  67.862 1.00 14.11 ? 449  ILE   B HG22 1 
ATOM   16274 H  HG23 . ILE   B 1 449 ? 17.752 17.283  67.202 1.00 14.11 ? 449  ILE   B HG23 1 
ATOM   16275 H  HD11 . ILE   B 1 449 ? 14.000 17.441  64.196 1.00 16.29 ? 449  ILE   B HD11 1 
ATOM   16276 H  HD12 . ILE   B 1 449 ? 13.590 17.493  65.725 1.00 16.29 ? 449  ILE   B HD12 1 
ATOM   16277 H  HD13 . ILE   B 1 449 ? 14.019 18.820  64.974 1.00 16.29 ? 449  ILE   B HD13 1 
ATOM   16278 N  N    . LYS   B 1 450 ? 16.015 16.031  69.566 1.00 10.96 ? 450  LYS   B N    1 
ATOM   16279 C  CA   . LYS   B 1 450 ? 16.230 14.621  69.997 1.00 11.72 ? 450  LYS   B CA   1 
ATOM   16280 C  C    . LYS   B 1 450 ? 14.893 14.060  70.509 1.00 12.58 ? 450  LYS   B C    1 
ATOM   16281 O  O    . LYS   B 1 450 ? 14.856 12.877  70.871 1.00 12.73 ? 450  LYS   B O    1 
ATOM   16282 C  CB   . LYS   B 1 450 ? 17.337 14.513  71.051 1.00 11.49 ? 450  LYS   B CB   1 
ATOM   16283 C  CG   . LYS   B 1 450 ? 18.713 14.999  70.615 1.00 11.93 ? 450  LYS   B CG   1 
ATOM   16284 C  CD   . LYS   B 1 450 ? 19.257 14.273  69.401 1.00 12.16 ? 450  LYS   B CD   1 
ATOM   16285 C  CE   . LYS   B 1 450 ? 19.005 15.012  68.104 1.00 13.25 ? 450  LYS   B CE   1 
ATOM   16286 N  NZ   . LYS   B 1 450 ? 19.774 14.434  66.979 1.00 11.23 ? 450  LYS   B NZ   1 
ATOM   16287 H  H    . LYS   B 1 450 ? 16.244 16.641  70.128 1.00 13.16 ? 450  LYS   B H    1 
ATOM   16288 H  HA   . LYS   B 1 450 ? 16.531 14.093  69.241 1.00 14.07 ? 450  LYS   B HA   1 
ATOM   16289 H  HB2  . LYS   B 1 450 ? 17.066 15.018  71.833 1.00 13.79 ? 450  LYS   B HB2  1 
ATOM   16290 H  HB3  . LYS   B 1 450 ? 17.411 13.585  71.324 1.00 13.79 ? 450  LYS   B HB3  1 
ATOM   16291 H  HG2  . LYS   B 1 450 ? 18.666 15.948  70.420 1.00 14.32 ? 450  LYS   B HG2  1 
ATOM   16292 H  HG3  . LYS   B 1 450 ? 19.334 14.891  71.352 1.00 14.32 ? 450  LYS   B HG3  1 
ATOM   16293 H  HD2  . LYS   B 1 450 ? 20.212 14.141  69.511 1.00 14.60 ? 450  LYS   B HD2  1 
ATOM   16294 H  HD3  . LYS   B 1 450 ? 18.853 13.393  69.349 1.00 14.60 ? 450  LYS   B HD3  1 
ATOM   16295 H  HE2  . LYS   B 1 450 ? 18.058 14.984  67.896 1.00 15.91 ? 450  LYS   B HE2  1 
ATOM   16296 H  HE3  . LYS   B 1 450 ? 19.244 15.946  68.213 1.00 15.91 ? 450  LYS   B HE3  1 
ATOM   16297 H  HZ1  . LYS   B 1 450 ? 19.412 14.692  66.208 1.00 13.48 ? 450  LYS   B HZ1  1 
ATOM   16298 H  HZ2  . LYS   B 1 450 ? 20.617 14.716  67.020 1.00 13.48 ? 450  LYS   B HZ2  1 
ATOM   16299 H  HZ3  . LYS   B 1 450 ? 19.756 13.546  67.032 1.00 13.48 ? 450  LYS   B HZ3  1 
ATOM   16300 N  N    . GLY   B 1 451 ? 13.835 14.880  70.517 1.00 13.45 ? 451  GLY   B N    1 
ATOM   16301 C  CA   . GLY   B 1 451 ? 12.497 14.443  70.969 1.00 13.74 ? 451  GLY   B CA   1 
ATOM   16302 C  C    . GLY   B 1 451 ? 11.439 15.424  70.503 1.00 14.49 ? 451  GLY   B C    1 
ATOM   16303 O  O    . GLY   B 1 451 ? 10.822 16.067  71.365 1.00 15.99 ? 451  GLY   B O    1 
ATOM   16304 H  H    . GLY   B 1 451 ? 13.868 15.701  70.263 1.00 16.14 ? 451  GLY   B H    1 
ATOM   16305 H  HA2  . GLY   B 1 451 ? 12.304 13.559  70.620 1.00 16.50 ? 451  GLY   B HA2  1 
ATOM   16306 H  HA3  . GLY   B 1 451 ? 12.481 14.376  71.937 1.00 16.50 ? 451  GLY   B HA3  1 
ATOM   16307 N  N    . TYR   B 1 452 ? 11.200 15.494  69.196 1.00 14.95 ? 452  TYR   B N    1 
ATOM   16308 C  CA   . TYR   B 1 452 ? 10.302 16.526  68.613 1.00 14.30 ? 452  TYR   B CA   1 
ATOM   16309 C  C    . TYR   B 1 452 ? 8.817  16.254  68.868 1.00 16.76 ? 452  TYR   B C    1 
ATOM   16310 O  O    . TYR   B 1 452 ? 8.109  15.847  67.937 1.00 13.93 ? 452  TYR   B O    1 
ATOM   16311 C  CB   . TYR   B 1 452 ? 10.590 16.631  67.115 1.00 15.59 ? 452  TYR   B CB   1 
ATOM   16312 C  CG   . TYR   B 1 452 ? 10.316 17.987  66.520 1.00 15.11 ? 452  TYR   B CG   1 
ATOM   16313 C  CD1  . TYR   B 1 452 ? 10.832 19.137  67.094 1.00 13.45 ? 452  TYR   B CD1  1 
ATOM   16314 C  CD2  . TYR   B 1 452 ? 9.542  18.117  65.382 1.00 14.01 ? 452  TYR   B CD2  1 
ATOM   16315 C  CE1  . TYR   B 1 452 ? 10.585 20.385  66.548 1.00 11.80 ? 452  TYR   B CE1  1 
ATOM   16316 C  CE2  . TYR   B 1 452 ? 9.284  19.357  64.824 1.00 14.56 ? 452  TYR   B CE2  1 
ATOM   16317 C  CZ   . TYR   B 1 452 ? 9.808  20.495  65.409 1.00 14.31 ? 452  TYR   B CZ   1 
ATOM   16318 O  OH   . TYR   B 1 452 ? 9.552  21.723  64.855 1.00 15.94 ? 452  TYR   B OH   1 
ATOM   16319 H  H    . TYR   B 1 452 ? 11.543 14.957  68.618 1.00 17.94 ? 452  TYR   B H    1 
ATOM   16320 H  HA   . TYR   B 1 452 ? 10.489 17.369  69.055 1.00 17.16 ? 452  TYR   B HA   1 
ATOM   16321 H  HB2  . TYR   B 1 452 ? 11.520 16.404  66.959 1.00 18.72 ? 452  TYR   B HB2  1 
ATOM   16322 H  HB3  . TYR   B 1 452 ? 10.055 15.971  66.647 1.00 18.72 ? 452  TYR   B HB3  1 
ATOM   16323 H  HD1  . TYR   B 1 452 ? 11.354 19.070  67.861 1.00 16.14 ? 452  TYR   B HD1  1 
ATOM   16324 H  HD2  . TYR   B 1 452 ? 9.187  17.355  64.983 1.00 16.82 ? 452  TYR   B HD2  1 
ATOM   16325 H  HE1  . TYR   B 1 452 ? 10.940 21.147  66.946 1.00 14.17 ? 452  TYR   B HE1  1 
ATOM   16326 H  HE2  . TYR   B 1 452 ? 8.760  19.425  64.059 1.00 17.47 ? 452  TYR   B HE2  1 
ATOM   16327 H  HH   . TYR   B 1 452 ? 9.951  22.318  65.295 1.00 19.14 ? 452  TYR   B HH   1 
ATOM   16328 N  N    . MET   B 1 453 ? 8.364  16.538  70.087 1.00 18.26 ? 453  MET   B N    1 
ATOM   16329 C  CA   . MET   B 1 453 ? 6.929  16.360  70.427 1.00 16.28 ? 453  MET   B CA   1 
ATOM   16330 C  C    . MET   B 1 453 ? 6.098  17.427  69.702 1.00 15.85 ? 453  MET   B C    1 
ATOM   16331 O  O    . MET   B 1 453 ? 4.867  17.379  69.803 1.00 14.49 ? 453  MET   B O    1 
ATOM   16332 C  CB   . MET   B 1 453 ? 6.728  16.450  71.941 1.00 14.48 ? 453  MET   B CB   1 
ATOM   16333 C  CG   . MET   B 1 453 ? 7.144  15.191  72.669 1.00 15.48 ? 453  MET   B CG   1 
ATOM   16334 S  SD   . MET   B 1 453 ? 6.084  13.792  72.224 1.00 17.12 ? 453  MET   B SD   1 
ATOM   16335 C  CE   . MET   B 1 453 ? 4.567  14.254  73.059 1.00 15.66 ? 453  MET   B CE   1 
ATOM   16336 H  H    . MET   B 1 453 ? 8.853  16.831  70.731 1.00 21.92 ? 453  MET   B H    1 
ATOM   16337 H  HA   . MET   B 1 453 ? 6.635  15.482  70.138 1.00 19.54 ? 453  MET   B HA   1 
ATOM   16338 H  HB2  . MET   B 1 453 ? 7.237  17.200  72.286 1.00 17.37 ? 453  MET   B HB2  1 
ATOM   16339 H  HB3  . MET   B 1 453 ? 5.794  16.632  72.128 1.00 17.37 ? 453  MET   B HB3  1 
ATOM   16340 H  HG2  . MET   B 1 453 ? 8.067  14.981  72.455 1.00 18.58 ? 453  MET   B HG2  1 
ATOM   16341 H  HG3  . MET   B 1 453 ? 7.102  15.340  73.627 1.00 18.58 ? 453  MET   B HG3  1 
ATOM   16342 H  HE1  . MET   B 1 453 ? 3.892  13.575  72.903 1.00 18.80 ? 453  MET   B HE1  1 
ATOM   16343 H  HE2  . MET   B 1 453 ? 4.732  14.331  74.012 1.00 18.80 ? 453  MET   B HE2  1 
ATOM   16344 H  HE3  . MET   B 1 453 ? 4.255  15.106  72.715 1.00 18.80 ? 453  MET   B HE3  1 
ATOM   16345 N  N    . ILE   B 1 454 ? 6.756  18.352  69.001 1.00 13.11 ? 454  ILE   B N    1 
ATOM   16346 C  CA   . ILE   B 1 454 ? 6.020  19.352  68.172 1.00 15.99 ? 454  ILE   B CA   1 
ATOM   16347 C  C    . ILE   B 1 454 ? 5.230  18.597  67.097 1.00 14.81 ? 454  ILE   B C    1 
ATOM   16348 O  O    . ILE   B 1 454 ? 4.134  19.040  66.731 1.00 17.53 ? 454  ILE   B O    1 
ATOM   16349 C  CB   . ILE   B 1 454 ? 7.021  20.344  67.551 1.00 14.65 ? 454  ILE   B CB   1 
ATOM   16350 C  CG1  . ILE   B 1 454 ? 7.804  21.106  68.623 1.00 16.34 ? 454  ILE   B CG1  1 
ATOM   16351 C  CG2  . ILE   B 1 454 ? 6.329  21.286  66.577 1.00 16.27 ? 454  ILE   B CG2  1 
ATOM   16352 C  CD1  . ILE   B 1 454 ? 6.928  21.798  69.638 1.00 16.79 ? 454  ILE   B CD1  1 
ATOM   16353 H  H    . ILE   B 1 454 ? 7.612  18.429  68.982 1.00 15.74 ? 454  ILE   B H    1 
ATOM   16354 H  HA   . ILE   B 1 454 ? 5.400  19.864  68.715 1.00 19.20 ? 454  ILE   B HA   1 
ATOM   16355 H  HB   . ILE   B 1 454 ? 7.668  19.828  67.045 1.00 17.58 ? 454  ILE   B HB   1 
ATOM   16356 H  HG12 . ILE   B 1 454 ? 8.392  20.487  69.084 1.00 19.61 ? 454  ILE   B HG12 1 
ATOM   16357 H  HG13 . ILE   B 1 454 ? 8.369  21.766  68.192 1.00 19.61 ? 454  ILE   B HG13 1 
ATOM   16358 H  HG21 . ILE   B 1 454 ? 6.980  21.899  66.201 1.00 19.52 ? 454  ILE   B HG21 1 
ATOM   16359 H  HG22 . ILE   B 1 454 ? 5.921  20.771  65.863 1.00 19.52 ? 454  ILE   B HG22 1 
ATOM   16360 H  HG23 . ILE   B 1 454 ? 5.644  21.789  67.045 1.00 19.52 ? 454  ILE   B HG23 1 
ATOM   16361 H  HD11 . ILE   B 1 454 ? 7.484  22.259  70.285 1.00 20.15 ? 454  ILE   B HD11 1 
ATOM   16362 H  HD12 . ILE   B 1 454 ? 6.356  22.439  69.188 1.00 20.15 ? 454  ILE   B HD12 1 
ATOM   16363 H  HD13 . ILE   B 1 454 ? 6.380  21.141  70.094 1.00 20.15 ? 454  ILE   B HD13 1 
ATOM   16364 N  N    . ASN   B 1 455 ? 5.778  17.476  66.623 1.00 17.53 ? 455  ASN   B N    1 
ATOM   16365 C  CA   . ASN   B 1 455 ? 5.087  16.662  65.586 1.00 17.81 ? 455  ASN   B CA   1 
ATOM   16366 C  C    . ASN   B 1 455 ? 3.662  16.322  66.050 1.00 16.61 ? 455  ASN   B C    1 
ATOM   16367 O  O    . ASN   B 1 455 ? 2.717  16.721  65.362 1.00 18.10 ? 455  ASN   B O    1 
ATOM   16368 C  CB   . ASN   B 1 455 ? 5.901  15.420  65.201 1.00 19.77 ? 455  ASN   B CB   1 
ATOM   16369 C  CG   . ASN   B 1 455 ? 6.801  15.645  64.005 1.00 20.30 ? 455  ASN   B CG   1 
ATOM   16370 O  OD1  . ASN   B 1 455 ? 7.140  16.779  63.682 1.00 20.31 ? 455  ASN   B OD1  1 
ATOM   16371 N  ND2  . ASN   B 1 455 ? 7.193  14.568  63.344 1.00 21.88 ? 455  ASN   B ND2  1 
ATOM   16372 H  H    . ASN   B 1 455 ? 6.538  17.164  66.877 1.00 21.04 ? 455  ASN   B H    1 
ATOM   16373 H  HA   . ASN   B 1 455 ? 5.014  17.188  64.774 1.00 21.38 ? 455  ASN   B HA   1 
ATOM   16374 H  HB2  . ASN   B 1 455 ? 6.442  15.147  65.959 1.00 23.72 ? 455  ASN   B HB2  1 
ATOM   16375 H  HB3  . ASN   B 1 455 ? 5.293  14.689  65.008 1.00 23.72 ? 455  ASN   B HB3  1 
ATOM   16376 H  HD21 . ASN   B 1 455 ? 7.706  14.647  62.658 1.00 26.26 ? 455  ASN   B HD21 1 
ATOM   16377 H  HD22 . ASN   B 1 455 ? 6.935  13.789  63.600 1.00 26.26 ? 455  ASN   B HD22 1 
ATOM   16378 N  N    . PRO   B 1 456 ? 3.458  15.586  67.164 1.00 16.44 ? 456  PRO   B N    1 
ATOM   16379 C  CA   . PRO   B 1 456 ? 2.108  15.210  67.585 1.00 20.91 ? 456  PRO   B CA   1 
ATOM   16380 C  C    . PRO   B 1 456 ? 1.321  16.346  68.254 1.00 18.36 ? 456  PRO   B C    1 
ATOM   16381 O  O    . PRO   B 1 456 ? 0.137  16.431  68.026 1.00 19.19 ? 456  PRO   B O    1 
ATOM   16382 C  CB   . PRO   B 1 456 ? 2.346  14.103  68.624 1.00 20.66 ? 456  PRO   B CB   1 
ATOM   16383 C  CG   . PRO   B 1 456 ? 3.723  14.384  69.175 1.00 18.51 ? 456  PRO   B CG   1 
ATOM   16384 C  CD   . PRO   B 1 456 ? 4.490  15.003  68.026 1.00 17.59 ? 456  PRO   B CD   1 
ATOM   16385 H  HA   . PRO   B 1 456 ? 1.579  14.951  66.814 1.00 25.10 ? 456  PRO   B HA   1 
ATOM   16386 H  HB2  . PRO   B 1 456 ? 1.675  14.126  69.324 1.00 24.80 ? 456  PRO   B HB2  1 
ATOM   16387 H  HB3  . PRO   B 1 456 ? 2.302  13.223  68.218 1.00 24.80 ? 456  PRO   B HB3  1 
ATOM   16388 H  HG2  . PRO   B 1 456 ? 3.681  14.987  69.934 1.00 22.22 ? 456  PRO   B HG2  1 
ATOM   16389 H  HG3  . PRO   B 1 456 ? 4.150  13.570  69.483 1.00 22.22 ? 456  PRO   B HG3  1 
ATOM   16390 H  HD2  . PRO   B 1 456 ? 5.111  15.679  68.340 1.00 21.11 ? 456  PRO   B HD2  1 
ATOM   16391 H  HD3  . PRO   B 1 456 ? 5.012  14.337  67.551 1.00 21.11 ? 456  PRO   B HD3  1 
ATOM   16392 N  N    . GLU   B 1 457 ? 1.999  17.193  69.017 1.00 18.34 ? 457  GLU   B N    1 
ATOM   16393 C  CA   . GLU   B 1 457 ? 1.273  18.226  69.805 1.00 16.75 ? 457  GLU   B CA   1 
ATOM   16394 C  C    . GLU   B 1 457 ? 0.897  19.447  68.951 1.00 20.12 ? 457  GLU   B C    1 
ATOM   16395 O  O    . GLU   B 1 457 ? -0.047 20.130  69.318 1.00 19.39 ? 457  GLU   B O    1 
ATOM   16396 C  CB   . GLU   B 1 457 ? 2.094  18.629  71.023 1.00 18.82 ? 457  GLU   B CB   1 
ATOM   16397 C  CG   . GLU   B 1 457 ? 2.207  17.551  72.087 1.00 16.91 ? 457  GLU   B CG   1 
ATOM   16398 C  CD   . GLU   B 1 457 ? 2.983  17.964  73.327 1.00 19.43 ? 457  GLU   B CD   1 
ATOM   16399 O  OE1  . GLU   B 1 457 ? 4.209  18.093  73.236 1.00 16.82 ? 457  GLU   B OE1  1 
ATOM   16400 O  OE2  . GLU   B 1 457 ? 2.358  18.152  74.378 1.00 15.93 ? 457  GLU   B OE2  1 
ATOM   16401 H  H    . GLU   B 1 457 ? 2.855  17.201  69.102 1.00 22.01 ? 457  GLU   B H    1 
ATOM   16402 H  HA   . GLU   B 1 457 ? 0.439  17.837  70.110 1.00 20.10 ? 457  GLU   B HA   1 
ATOM   16403 H  HB2  . GLU   B 1 457 ? 2.986  18.875  70.731 1.00 22.59 ? 457  GLU   B HB2  1 
ATOM   16404 H  HB3  . GLU   B 1 457 ? 1.697  19.420  71.420 1.00 22.59 ? 457  GLU   B HB3  1 
ATOM   16405 H  HG2  . GLU   B 1 457 ? 1.314  17.282  72.354 1.00 20.30 ? 457  GLU   B HG2  1 
ATOM   16406 H  HG3  . GLU   B 1 457 ? 2.634  16.772  71.697 1.00 20.30 ? 457  GLU   B HG3  1 
ATOM   16407 N  N    . ILE   B 1 458 ? 1.621  19.699  67.876 1.00 15.22 ? 458  ILE   B N    1 
ATOM   16408 C  CA   . ILE   B 1 458 ? 1.331  20.862  66.981 1.00 18.24 ? 458  ILE   B CA   1 
ATOM   16409 C  C    . ILE   B 1 458 ? 0.981  20.455  65.539 1.00 17.72 ? 458  ILE   B C    1 
ATOM   16410 O  O    . ILE   B 1 458 ? 0.032  20.979  64.998 1.00 15.65 ? 458  ILE   B O    1 
ATOM   16411 C  CB   . ILE   B 1 458 ? 2.554  21.808  66.968 1.00 17.97 ? 458  ILE   B CB   1 
ATOM   16412 C  CG1  . ILE   B 1 458 ? 3.005  22.198  68.376 1.00 18.97 ? 458  ILE   B CG1  1 
ATOM   16413 C  CG2  . ILE   B 1 458 ? 2.282  23.024  66.098 1.00 21.32 ? 458  ILE   B CG2  1 
ATOM   16414 C  CD1  . ILE   B 1 458 ? 2.289  23.397  68.940 1.00 19.85 ? 458  ILE   B CD1  1 
ATOM   16415 H  H    . ILE   B 1 458 ? 2.291  19.220  67.628 1.00 18.27 ? 458  ILE   B H    1 
ATOM   16416 H  HA   . ILE   B 1 458 ? 0.548  21.307  67.340 1.00 21.90 ? 458  ILE   B HA   1 
ATOM   16417 H  HB   . ILE   B 1 458 ? 3.296  21.321  66.576 1.00 21.57 ? 458  ILE   B HB   1 
ATOM   16418 H  HG12 . ILE   B 1 458 ? 2.869  21.443  68.970 1.00 22.77 ? 458  ILE   B HG12 1 
ATOM   16419 H  HG13 . ILE   B 1 458 ? 3.958  22.379  68.362 1.00 22.77 ? 458  ILE   B HG13 1 
ATOM   16420 H  HG21 . ILE   B 1 458 ? 3.059  23.605  66.102 1.00 25.58 ? 458  ILE   B HG21 1 
ATOM   16421 H  HG22 . ILE   B 1 458 ? 2.097  22.738  65.190 1.00 25.58 ? 458  ILE   B HG22 1 
ATOM   16422 H  HG23 . ILE   B 1 458 ? 1.516  23.507  66.446 1.00 25.58 ? 458  ILE   B HG23 1 
ATOM   16423 H  HD11 . ILE   B 1 458 ? 2.624  23.585  69.830 1.00 23.83 ? 458  ILE   B HD11 1 
ATOM   16424 H  HD12 . ILE   B 1 458 ? 2.443  24.165  68.368 1.00 23.83 ? 458  ILE   B HD12 1 
ATOM   16425 H  HD13 . ILE   B 1 458 ? 1.337  23.214  68.985 1.00 23.83 ? 458  ILE   B HD13 1 
ATOM   16426 N  N    . LEU   B 1 459 ? 1.732  19.531  64.950 1.00 18.35 ? 459  LEU   B N    1 
ATOM   16427 C  CA   . LEU   B 1 459 ? 1.571  19.248  63.503 1.00 20.12 ? 459  LEU   B CA   1 
ATOM   16428 C  C    . LEU   B 1 459 ? 0.637  18.074  63.185 1.00 18.59 ? 459  LEU   B C    1 
ATOM   16429 O  O    . LEU   B 1 459 ? 0.275  17.942  62.029 1.00 20.32 ? 459  LEU   B O    1 
ATOM   16430 C  CB   . LEU   B 1 459 ? 2.968  18.958  62.960 1.00 18.68 ? 459  LEU   B CB   1 
ATOM   16431 C  CG   . LEU   B 1 459 ? 4.001  20.059  63.208 1.00 20.79 ? 459  LEU   B CG   1 
ATOM   16432 C  CD1  . LEU   B 1 459 ? 5.365  19.674  62.664 1.00 17.95 ? 459  LEU   B CD1  1 
ATOM   16433 C  CD2  . LEU   B 1 459 ? 3.554  21.374  62.596 1.00 19.20 ? 459  LEU   B CD2  1 
ATOM   16434 H  H    . LEU   B 1 459 ? 2.331  19.060  65.349 1.00 22.02 ? 459  LEU   B H    1 
ATOM   16435 H  HA   . LEU   B 1 459 ? 1.153  20.018  63.087 1.00 24.15 ? 459  LEU   B HA   1 
ATOM   16436 H  HB2  . LEU   B 1 459 ? 3.291  18.135  63.359 1.00 22.42 ? 459  LEU   B HB2  1 
ATOM   16437 H  HB3  . LEU   B 1 459 ? 2.903  18.804  62.005 1.00 22.42 ? 459  LEU   B HB3  1 
ATOM   16438 H  HG   . LEU   B 1 459 ? 4.075  20.170  64.169 1.00 24.95 ? 459  LEU   B HG   1 
ATOM   16439 H  HD11 . LEU   B 1 459 ? 5.996  20.390  62.836 1.00 21.55 ? 459  LEU   B HD11 1 
ATOM   16440 H  HD12 . LEU   B 1 459 ? 5.670  18.863  63.100 1.00 21.55 ? 459  LEU   B HD12 1 
ATOM   16441 H  HD13 . LEU   B 1 459 ? 5.301  19.523  61.708 1.00 21.55 ? 459  LEU   B HD13 1 
ATOM   16442 H  HD21 . LEU   B 1 459 ? 4.224  22.055  62.766 1.00 23.04 ? 459  LEU   B HD21 1 
ATOM   16443 H  HD22 . LEU   B 1 459 ? 3.441  21.264  61.639 1.00 23.04 ? 459  LEU   B HD22 1 
ATOM   16444 H  HD23 . LEU   B 1 459 ? 2.711  21.645  62.991 1.00 23.04 ? 459  LEU   B HD23 1 
ATOM   16445 N  N    . GLY   B 1 460 ? 0.348  17.248  64.173 1.00 17.60 ? 460  GLY   B N    1 
ATOM   16446 C  CA   . GLY   B 1 460 ? -0.567 16.111  63.968 1.00 18.54 ? 460  GLY   B CA   1 
ATOM   16447 C  C    . GLY   B 1 460 ? 0.113  14.850  63.457 1.00 21.52 ? 460  GLY   B C    1 
ATOM   16448 O  O    . GLY   B 1 460 ? -0.572 13.991  62.911 1.00 21.28 ? 460  GLY   B O    1 
ATOM   16449 H  H    . GLY   B 1 460 ? 0.663  17.317  64.970 1.00 21.13 ? 460  GLY   B H    1 
ATOM   16450 H  HA2  . GLY   B 1 460 ? -1.011 15.910  64.807 1.00 22.25 ? 460  GLY   B HA2  1 
ATOM   16451 H  HA3  . GLY   B 1 460 ? -1.257 16.373  63.338 1.00 22.25 ? 460  GLY   B HA3  1 
ATOM   16452 N  N    . TYR   B 1 461 ? 1.426  14.740  63.659 1.00 21.66 ? 461  TYR   B N    1 
ATOM   16453 C  CA   . TYR   B 1 461 ? 2.166  13.536  63.203 1.00 20.65 ? 461  TYR   B CA   1 
ATOM   16454 C  C    . TYR   B 1 461 ? 2.623  12.729  64.421 1.00 21.12 ? 461  TYR   B C    1 
ATOM   16455 O  O    . TYR   B 1 461 ? 3.277  13.310  65.296 1.00 20.38 ? 461  TYR   B O    1 
ATOM   16456 C  CB   . TYR   B 1 461 ? 3.370  13.952  62.357 1.00 18.61 ? 461  TYR   B CB   1 
ATOM   16457 C  CG   . TYR   B 1 461 ? 3.042  14.407  60.958 1.00 19.21 ? 461  TYR   B CG   1 
ATOM   16458 C  CD1  . TYR   B 1 461 ? 2.504  15.661  60.721 1.00 17.50 ? 461  TYR   B CD1  1 
ATOM   16459 C  CD2  . TYR   B 1 461 ? 3.279  13.587  59.868 1.00 21.18 ? 461  TYR   B CD2  1 
ATOM   16460 C  CE1  . TYR   B 1 461 ? 2.204  16.086  59.438 1.00 21.45 ? 461  TYR   B CE1  1 
ATOM   16461 C  CE2  . TYR   B 1 461 ? 2.985  13.997  58.579 1.00 22.83 ? 461  TYR   B CE2  1 
ATOM   16462 C  CZ   . TYR   B 1 461 ? 2.445  15.251  58.362 1.00 22.27 ? 461  TYR   B CZ   1 
ATOM   16463 O  OH   . TYR   B 1 461 ? 2.150  15.663  57.087 1.00 24.73 ? 461  TYR   B OH   1 
ATOM   16464 H  H    . TYR   B 1 461 ? 1.909  15.334  64.050 1.00 25.99 ? 461  TYR   B H    1 
ATOM   16465 H  HA   . TYR   B 1 461 ? 1.583  12.985  62.658 1.00 24.79 ? 461  TYR   B HA   1 
ATOM   16466 H  HB2  . TYR   B 1 461 ? 3.837  14.669  62.814 1.00 22.33 ? 461  TYR   B HB2  1 
ATOM   16467 H  HB3  . TYR   B 1 461 ? 3.984  13.203  62.303 1.00 22.33 ? 461  TYR   B HB3  1 
ATOM   16468 H  HD1  . TYR   B 1 461 ? 2.341  16.229  61.439 1.00 21.00 ? 461  TYR   B HD1  1 
ATOM   16469 H  HD2  . TYR   B 1 461 ? 3.644  12.742  60.005 1.00 25.42 ? 461  TYR   B HD2  1 
ATOM   16470 H  HE1  . TYR   B 1 461 ? 1.841  16.931  59.300 1.00 25.74 ? 461  TYR   B HE1  1 
ATOM   16471 H  HE2  . TYR   B 1 461 ? 3.150  13.430  57.861 1.00 27.40 ? 461  TYR   B HE2  1 
ATOM   16472 H  HH   . TYR   B 1 461 ? 2.119  14.996  56.577 1.00 29.68 ? 461  TYR   B HH   1 
ATOM   16473 N  N    . PRO   B 1 462 ? 2.316  11.416  64.529 1.00 23.70 ? 462  PRO   B N    1 
ATOM   16474 C  CA   . PRO   B 1 462 ? 1.433  10.698  63.591 1.00 23.56 ? 462  PRO   B CA   1 
ATOM   16475 C  C    . PRO   B 1 462 ? -0.049 10.948  63.878 1.00 26.85 ? 462  PRO   B C    1 
ATOM   16476 O  O    . PRO   B 1 462 ? -0.866 10.532  63.085 1.00 27.38 ? 462  PRO   B O    1 
ATOM   16477 C  CB   . PRO   B 1 462 ? 1.745  9.232   63.905 1.00 26.17 ? 462  PRO   B CB   1 
ATOM   16478 C  CG   . PRO   B 1 462 ? 2.066  9.240   65.376 1.00 23.11 ? 462  PRO   B CG   1 
ATOM   16479 C  CD   . PRO   B 1 462 ? 2.820  10.534  65.585 1.00 24.67 ? 462  PRO   B CD   1 
ATOM   16480 H  HA   . PRO   B 1 462 ? 1.581  10.972  62.672 1.00 28.28 ? 462  PRO   B HA   1 
ATOM   16481 H  HB2  . PRO   B 1 462 ? 0.989  8.657   63.709 1.00 31.41 ? 462  PRO   B HB2  1 
ATOM   16482 H  HB3  . PRO   B 1 462 ? 2.492  8.907   63.379 1.00 31.41 ? 462  PRO   B HB3  1 
ATOM   16483 H  HG2  . PRO   B 1 462 ? 1.260  9.209   65.915 1.00 27.74 ? 462  PRO   B HG2  1 
ATOM   16484 H  HG3  . PRO   B 1 462 ? 2.604  8.472   65.625 1.00 27.74 ? 462  PRO   B HG3  1 
ATOM   16485 H  HD2  . PRO   B 1 462 ? 2.653  10.904  66.466 1.00 29.60 ? 462  PRO   B HD2  1 
ATOM   16486 H  HD3  . PRO   B 1 462 ? 3.778  10.402  65.510 1.00 29.60 ? 462  PRO   B HD3  1 
ATOM   16487 N  N    . GLU   B 1 463 ? -0.352 11.571  65.013 1.00 26.58 ? 463  GLU   B N    1 
ATOM   16488 C  CA   . GLU   B 1 463 ? -1.741 11.955  65.359 1.00 23.39 ? 463  GLU   B CA   1 
ATOM   16489 C  C    . GLU   B 1 463 ? -1.656 13.327  66.031 1.00 24.85 ? 463  GLU   B C    1 
ATOM   16490 O  O    . GLU   B 1 463 ? -0.545 13.719  66.420 1.00 23.48 ? 463  GLU   B O    1 
ATOM   16491 C  CB   . GLU   B 1 463 ? -2.374 10.930  66.299 1.00 27.16 ? 463  GLU   B CB   1 
ATOM   16492 C  CG   . GLU   B 1 463 ? -1.699 10.847  67.655 1.00 28.38 ? 463  GLU   B CG   1 
ATOM   16493 C  CD   . GLU   B 1 463 ? -2.339 9.852   68.610 1.00 38.81 ? 463  GLU   B CD   1 
ATOM   16494 O  OE1  . GLU   B 1 463 ? -3.580 9.851   68.714 1.00 38.30 ? 463  GLU   B OE1  1 
ATOM   16495 O  OE2  . GLU   B 1 463 ? -1.596 9.078   69.242 1.00 36.95 ? 463  GLU   B OE2  1 
ATOM   16496 H  H    . GLU   B 1 463 ? 0.230  11.787  65.608 1.00 31.90 ? 463  GLU   B H    1 
ATOM   16497 H  HA   . GLU   B 1 463 ? -2.299 11.987  64.567 1.00 28.07 ? 463  GLU   B HA   1 
ATOM   16498 H  HB2  . GLU   B 1 463 ? -3.309 11.153  66.425 1.00 32.60 ? 463  GLU   B HB2  1 
ATOM   16499 H  HB3  . GLU   B 1 463 ? -2.345 10.056  65.878 1.00 32.60 ? 463  GLU   B HB3  1 
ATOM   16500 H  HG2  . GLU   B 1 463 ? -0.768 10.605  67.528 1.00 34.06 ? 463  GLU   B HG2  1 
ATOM   16501 H  HG3  . GLU   B 1 463 ? -1.710 11.726  68.065 1.00 34.06 ? 463  GLU   B HG3  1 
ATOM   16502 N  N    . LYS   B 1 464 ? -2.785 14.017  66.177 1.00 24.48 ? 464  LYS   B N    1 
ATOM   16503 C  CA   . LYS   B 1 464 ? -2.776 15.321  66.887 1.00 24.11 ? 464  LYS   B CA   1 
ATOM   16504 C  C    . LYS   B 1 464 ? -3.121 15.106  68.359 1.00 23.03 ? 464  LYS   B C    1 
ATOM   16505 O  O    . LYS   B 1 464 ? -4.139 14.457  68.634 1.00 23.38 ? 464  LYS   B O    1 
ATOM   16506 C  CB   . LYS   B 1 464 ? -3.768 16.303  66.260 1.00 26.99 ? 464  LYS   B CB   1 
ATOM   16507 C  CG   . LYS   B 1 464 ? -3.824 17.673  66.922 1.00 23.63 ? 464  LYS   B CG   1 
ATOM   16508 C  CD   . LYS   B 1 464 ? -2.568 18.490  66.714 1.00 23.52 ? 464  LYS   B CD   1 
ATOM   16509 C  CE   . LYS   B 1 464 ? -2.725 19.930  67.155 1.00 26.91 ? 464  LYS   B CE   1 
ATOM   16510 N  NZ   . LYS   B 1 464 ? -2.795 20.047  68.631 1.00 23.81 ? 464  LYS   B NZ   1 
ATOM   16511 H  H    . LYS   B 1 464 ? -3.554 13.766  65.885 1.00 29.39 ? 464  LYS   B H    1 
ATOM   16512 H  HA   . LYS   B 1 464 ? -1.887 15.702  66.810 1.00 28.93 ? 464  LYS   B HA   1 
ATOM   16513 H  HB2  . LYS   B 1 464 ? -3.539 16.420  65.325 1.00 32.39 ? 464  LYS   B HB2  1 
ATOM   16514 H  HB3  . LYS   B 1 464 ? -4.654 15.909  66.288 1.00 32.39 ? 464  LYS   B HB3  1 
ATOM   16515 H  HG2  . LYS   B 1 464 ? -4.583 18.164  66.571 1.00 28.36 ? 464  LYS   B HG2  1 
ATOM   16516 H  HG3  . LYS   B 1 464 ? -3.975 17.560  67.873 1.00 28.36 ? 464  LYS   B HG3  1 
ATOM   16517 H  HD2  . LYS   B 1 464 ? -1.837 18.083  67.206 1.00 28.23 ? 464  LYS   B HD2  1 
ATOM   16518 H  HD3  . LYS   B 1 464 ? -2.325 18.468  65.775 1.00 28.23 ? 464  LYS   B HD3  1 
ATOM   16519 H  HE2  . LYS   B 1 464 ? -1.978 20.453  66.824 1.00 32.30 ? 464  LYS   B HE2  1 
ATOM   16520 H  HE3  . LYS   B 1 464 ? -3.530 20.303  66.762 1.00 32.30 ? 464  LYS   B HE3  1 
ATOM   16521 H  HZ1  . LYS   B 1 464 ? -3.593 20.363  68.866 1.00 28.58 ? 464  LYS   B HZ1  1 
ATOM   16522 H  HZ2  . LYS   B 1 464 ? -2.673 19.246  68.999 1.00 28.58 ? 464  LYS   B HZ2  1 
ATOM   16523 H  HZ3  . LYS   B 1 464 ? -2.161 20.603  68.915 1.00 28.58 ? 464  LYS   B HZ3  1 
ATOM   16524 N  N    . LEU   B 1 465 ? -2.289 15.622  69.259 1.00 22.00 ? 465  LEU   B N    1 
ATOM   16525 C  CA   . LEU   B 1 465 ? -2.599 15.546  70.706 1.00 24.57 ? 465  LEU   B CA   1 
ATOM   16526 C  C    . LEU   B 1 465 ? -2.997 16.938  71.204 1.00 24.95 ? 465  LEU   B C    1 
ATOM   16527 O  O    . LEU   B 1 465 ? -2.674 17.924  70.518 1.00 22.24 ? 465  LEU   B O    1 
ATOM   16528 C  CB   . LEU   B 1 465 ? -1.361 15.048  71.462 1.00 21.46 ? 465  LEU   B CB   1 
ATOM   16529 C  CG   . LEU   B 1 465 ? -0.773 13.721  70.986 1.00 23.95 ? 465  LEU   B CG   1 
ATOM   16530 C  CD1  . LEU   B 1 465 ? 0.529  13.424  71.714 1.00 22.28 ? 465  LEU   B CD1  1 
ATOM   16531 C  CD2  . LEU   B 1 465 ? -1.766 12.589  71.192 1.00 24.60 ? 465  LEU   B CD2  1 
ATOM   16532 H  H    . LEU   B 1 465 ? -1.549 16.016  69.068 1.00 26.41 ? 465  LEU   B H    1 
ATOM   16533 H  HA   . LEU   B 1 465 ? -3.332 14.930  70.859 1.00 29.48 ? 465  LEU   B HA   1 
ATOM   16534 H  HB2  . LEU   B 1 465 ? -0.671 15.727  71.400 1.00 25.76 ? 465  LEU   B HB2  1 
ATOM   16535 H  HB3  . LEU   B 1 465 ? -1.590 14.961  72.400 1.00 25.76 ? 465  LEU   B HB3  1 
ATOM   16536 H  HG   . LEU   B 1 465 ? -0.586 13.794  70.037 1.00 28.74 ? 465  LEU   B HG   1 
ATOM   16537 H  HD11 . LEU   B 1 465 ? 0.889  12.579  71.401 1.00 26.75 ? 465  LEU   B HD11 1 
ATOM   16538 H  HD12 . LEU   B 1 465 ? 1.167  14.133  71.538 1.00 26.75 ? 465  LEU   B HD12 1 
ATOM   16539 H  HD13 . LEU   B 1 465 ? 0.362  13.370  72.668 1.00 26.75 ? 465  LEU   B HD13 1 
ATOM   16540 H  HD21 . LEU   B 1 465 ? -1.376 11.756  70.884 1.00 29.52 ? 465  LEU   B HD21 1 
ATOM   16541 H  HD22 . LEU   B 1 465 ? -1.982 12.516  72.135 1.00 29.52 ? 465  LEU   B HD22 1 
ATOM   16542 H  HD23 . LEU   B 1 465 ? -2.575 12.772  70.688 1.00 29.52 ? 465  LEU   B HD23 1 
ATOM   16543 N  N    . ASP   B 1 466 ? -3.679 17.007  72.345 1.00 22.17 ? 466  ASP   B N    1 
ATOM   16544 C  CA   . ASP   B 1 466 ? -3.991 18.322  72.962 1.00 22.98 ? 466  ASP   B CA   1 
ATOM   16545 C  C    . ASP   B 1 466 ? -2.698 18.786  73.632 1.00 20.81 ? 466  ASP   B C    1 
ATOM   16546 O  O    . ASP   B 1 466 ? -2.297 18.158  74.622 1.00 19.68 ? 466  ASP   B O    1 
ATOM   16547 C  CB   . ASP   B 1 466 ? -5.173 18.202  73.925 1.00 22.19 ? 466  ASP   B CB   1 
ATOM   16548 C  CG   . ASP   B 1 466 ? -5.374 19.402  74.836 1.00 28.17 ? 466  ASP   B CG   1 
ATOM   16549 O  OD1  . ASP   B 1 466 ? -4.735 20.445  74.599 1.00 27.43 ? 466  ASP   B OD1  1 
ATOM   16550 O  OD2  . ASP   B 1 466 ? -6.181 19.281  75.776 1.00 30.93 ? 466  ASP   B OD2  1 
ATOM   16551 H  H    . ASP   B 1 466 ? -3.970 16.325  72.780 1.00 26.60 ? 466  ASP   B H    1 
ATOM   16552 H  HA   . ASP   B 1 466 ? -4.274 18.982  72.310 1.00 27.58 ? 466  ASP   B HA   1 
ATOM   16553 H  HB2  . ASP   B 1 466 ? -5.982 18.064  73.409 1.00 26.63 ? 466  ASP   B HB2  1 
ATOM   16554 H  HB3  . ASP   B 1 466 ? -5.049 17.412  74.474 1.00 26.63 ? 466  ASP   B HB3  1 
ATOM   16555 N  N    . ARG   B 1 467 ? -2.087 19.854  73.121 1.00 20.87 ? 467  ARG   B N    1 
ATOM   16556 C  CA   . ARG   B 1 467 ? -0.773 20.243  73.627 1.00 18.74 ? 467  ARG   B CA   1 
ATOM   16557 C  C    . ARG   B 1 467 ? -0.813 20.721  75.072 1.00 20.83 ? 467  ARG   B C    1 
ATOM   16558 O  O    . ARG   B 1 467 ? 0.235  20.747  75.729 1.00 18.27 ? 467  ARG   B O    1 
ATOM   16559 C  CB   . ARG   B 1 467 ? -0.158 21.331  72.741 1.00 16.67 ? 467  ARG   B CB   1 
ATOM   16560 C  CG   . ARG   B 1 467 ? -1.015 22.571  72.563 1.00 19.33 ? 467  ARG   B CG   1 
ATOM   16561 C  CD   . ARG   B 1 467 ? -0.543 23.383  71.366 1.00 21.85 ? 467  ARG   B CD   1 
ATOM   16562 N  NE   . ARG   B 1 467 ? -1.406 24.533  71.108 1.00 28.67 ? 467  ARG   B NE   1 
ATOM   16563 C  CZ   . ARG   B 1 467 ? -1.266 25.716  71.684 1.00 22.13 ? 467  ARG   B CZ   1 
ATOM   16564 N  NH1  . ARG   B 1 467 ? -0.292 25.948  72.550 1.00 21.35 ? 467  ARG   B NH1  1 
ATOM   16565 N  NH2  . ARG   B 1 467 ? -2.118 26.691  71.381 1.00 24.83 ? 467  ARG   B NH2  1 
ATOM   16566 H  H    . ARG   B 1 467 ? -2.406 20.354  72.498 1.00 25.04 ? 467  ARG   B H    1 
ATOM   16567 H  HA   . ARG   B 1 467 ? -0.221 19.446  73.601 1.00 22.49 ? 467  ARG   B HA   1 
ATOM   16568 H  HB2  . ARG   B 1 467 ? 0.695  21.595  73.121 1.00 20.01 ? 467  ARG   B HB2  1 
ATOM   16569 H  HB3  . ARG   B 1 467 ? 0.026  20.952  71.867 1.00 20.01 ? 467  ARG   B HB3  1 
ATOM   16570 H  HG2  . ARG   B 1 467 ? -1.942 22.314  72.440 1.00 23.20 ? 467  ARG   B HG2  1 
ATOM   16571 H  HG3  . ARG   B 1 467 ? -0.975 23.115  73.365 1.00 23.20 ? 467  ARG   B HG3  1 
ATOM   16572 H  HD2  . ARG   B 1 467 ? 0.364  23.689  71.522 1.00 26.23 ? 467  ARG   B HD2  1 
ATOM   16573 H  HD3  . ARG   B 1 467 ? -0.520 22.815  70.580 1.00 26.23 ? 467  ARG   B HD3  1 
ATOM   16574 H  HE   . ARG   B 1 467 ? -2.048 24.435  70.544 1.00 34.41 ? 467  ARG   B HE   1 
ATOM   16575 H  HH11 . ARG   B 1 467 ? 0.265  25.324  72.748 1.00 25.63 ? 467  ARG   B HH11 1 
ATOM   16576 H  HH12 . ARG   B 1 467 ? -0.216 26.723  72.915 1.00 25.63 ? 467  ARG   B HH12 1 
ATOM   16577 H  HH21 . ARG   B 1 467 ? -2.751 26.549  70.816 1.00 29.80 ? 467  ARG   B HH21 1 
ATOM   16578 H  HH22 . ARG   B 1 467 ? -2.036 27.464  71.750 1.00 29.80 ? 467  ARG   B HH22 1 
ATOM   16579 N  N    . PHE   B 1 468 ? -1.985 21.099  75.583 1.00 17.57 ? 468  PHE   B N    1 
ATOM   16580 C  CA   . PHE   B 1 468 ? -2.090 21.538  76.968 1.00 22.11 ? 468  PHE   B CA   1 
ATOM   16581 C  C    . PHE   B 1 468 ? -2.290 20.389  77.943 1.00 20.73 ? 468  PHE   B C    1 
ATOM   16582 O  O    . PHE   B 1 468 ? -2.111 20.583  79.151 1.00 20.07 ? 468  PHE   B O    1 
ATOM   16583 C  CB   . PHE   B 1 468 ? -3.249 22.525  77.140 1.00 21.19 ? 468  PHE   B CB   1 
ATOM   16584 C  CG   . PHE   B 1 468 ? -3.149 23.743  76.264 1.00 23.36 ? 468  PHE   B CG   1 
ATOM   16585 C  CD1  . PHE   B 1 468 ? -2.108 24.643  76.421 1.00 22.41 ? 468  PHE   B CD1  1 
ATOM   16586 C  CD2  . PHE   B 1 468 ? -4.113 24.002  75.304 1.00 28.32 ? 468  PHE   B CD2  1 
ATOM   16587 C  CE1  . PHE   B 1 468 ? -2.015 25.767  75.625 1.00 22.87 ? 468  PHE   B CE1  1 
ATOM   16588 C  CE2  . PHE   B 1 468 ? -4.030 25.127  74.503 1.00 31.17 ? 468  PHE   B CE2  1 
ATOM   16589 C  CZ   . PHE   B 1 468 ? -2.978 26.013  74.665 1.00 23.65 ? 468  PHE   B CZ   1 
ATOM   16590 H  H    . PHE   B 1 468 ? -2.725 21.108  75.145 1.00 21.09 ? 468  PHE   B H    1 
ATOM   16591 H  HA   . PHE   B 1 468 ? -1.244 21.966  77.172 1.00 26.54 ? 468  PHE   B HA   1 
ATOM   16592 H  HB2  . PHE   B 1 468 ? -4.083 22.068  76.948 1.00 25.43 ? 468  PHE   B HB2  1 
ATOM   16593 H  HB3  . PHE   B 1 468 ? -3.287 22.807  78.067 1.00 25.43 ? 468  PHE   B HB3  1 
ATOM   16594 H  HD1  . PHE   B 1 468 ? -1.462 24.488  77.072 1.00 26.89 ? 468  PHE   B HD1  1 
ATOM   16595 H  HD2  . PHE   B 1 468 ? -4.824 23.413  75.197 1.00 33.99 ? 468  PHE   B HD2  1 
ATOM   16596 H  HE1  . PHE   B 1 468 ? -1.305 26.358  75.735 1.00 27.45 ? 468  PHE   B HE1  1 
ATOM   16597 H  HE2  . PHE   B 1 468 ? -4.679 25.288  73.857 1.00 37.41 ? 468  PHE   B HE2  1 
ATOM   16598 H  HZ   . PHE   B 1 468 ? -2.920 26.771  74.129 1.00 28.38 ? 468  PHE   B HZ   1 
ATOM   16599 N  N    . ALA   B 1 469 ? -2.654 19.220  77.417 1.00 18.72 ? 469  ALA   B N    1 
ATOM   16600 C  CA   . ALA   B 1 469 ? -2.971 18.068  78.295 1.00 19.00 ? 469  ALA   B CA   1 
ATOM   16601 C  C    . ALA   B 1 469 ? -1.707 17.437  78.886 1.00 15.20 ? 469  ALA   B C    1 
ATOM   16602 O  O    . ALA   B 1 469 ? -0.615 17.645  78.341 1.00 16.44 ? 469  ALA   B O    1 
ATOM   16603 C  CB   . ALA   B 1 469 ? -3.778 17.055  77.526 1.00 22.64 ? 469  ALA   B CB   1 
ATOM   16604 H  H    . ALA   B 1 469 ? -2.725 19.065  76.574 1.00 22.47 ? 469  ALA   B H    1 
ATOM   16605 H  HA   . ALA   B 1 469 ? -3.497 18.389  79.044 1.00 22.80 ? 469  ALA   B HA   1 
ATOM   16606 H  HB1  . ALA   B 1 469 ? -3.985 16.302  78.101 1.00 27.17 ? 469  ALA   B HB1  1 
ATOM   16607 H  HB2  . ALA   B 1 469 ? -4.603 17.463  77.219 1.00 27.17 ? 469  ALA   B HB2  1 
ATOM   16608 H  HB3  . ALA   B 1 469 ? -3.267 16.747  76.762 1.00 27.17 ? 469  ALA   B HB3  1 
ATOM   16609 N  N    . LEU   B 1 470 ? -1.892 16.666  79.943 1.00 19.15 ? 470  LEU   B N    1 
ATOM   16610 C  CA   . LEU   B 1 470 ? -0.749 16.018  80.616 1.00 18.23 ? 470  LEU   B CA   1 
ATOM   16611 C  C    . LEU   B 1 470 ? -0.794 14.497  80.395 1.00 19.45 ? 470  LEU   B C    1 
ATOM   16612 O  O    . LEU   B 1 470 ? 0.235  13.863  80.304 1.00 17.20 ? 470  LEU   B O    1 
ATOM   16613 C  CB   . LEU   B 1 470 ? -0.869 16.360  82.098 1.00 19.09 ? 470  LEU   B CB   1 
ATOM   16614 C  CG   . LEU   B 1 470 ? -0.800 17.844  82.455 1.00 18.71 ? 470  LEU   B CG   1 
ATOM   16615 C  CD1  . LEU   B 1 470 ? -0.694 18.029  83.958 1.00 26.05 ? 470  LEU   B CD1  1 
ATOM   16616 C  CD2  . LEU   B 1 470 ? 0.377  18.511  81.764 1.00 19.51 ? 470  LEU   B CD2  1 
ATOM   16617 H  H    . LEU   B 1 470 ? -2.659 16.498  80.293 1.00 22.98 ? 470  LEU   B H    1 
ATOM   16618 H  HA   . LEU   B 1 470 ? 0.097  16.331  80.259 1.00 21.88 ? 470  LEU   B HA   1 
ATOM   16619 H  HB2  . LEU   B 1 470 ? -1.711 16.006  82.425 1.00 22.91 ? 470  LEU   B HB2  1 
ATOM   16620 H  HB3  . LEU   B 1 470 ? -0.162 15.898  82.576 1.00 22.91 ? 470  LEU   B HB3  1 
ATOM   16621 H  HG   . LEU   B 1 470 ? -1.618 18.264  82.146 1.00 22.46 ? 470  LEU   B HG   1 
ATOM   16622 H  HD11 . LEU   B 1 470 ? -0.651 18.976  84.166 1.00 31.27 ? 470  LEU   B HD11 1 
ATOM   16623 H  HD12 . LEU   B 1 470 ? -1.471 17.639  84.388 1.00 31.27 ? 470  LEU   B HD12 1 
ATOM   16624 H  HD13 . LEU   B 1 470 ? 0.108  17.591  84.282 1.00 31.27 ? 470  LEU   B HD13 1 
ATOM   16625 H  HD21 . LEU   B 1 470 ? 0.403  19.451  82.003 1.00 23.42 ? 470  LEU   B HD21 1 
ATOM   16626 H  HD22 . LEU   B 1 470 ? 1.202  18.084  82.044 1.00 23.42 ? 470  LEU   B HD22 1 
ATOM   16627 H  HD23 . LEU   B 1 470 ? 0.279  18.425  80.803 1.00 23.42 ? 470  LEU   B HD23 1 
ATOM   16628 N  N    . ASP   B 1 471 ? -1.994 13.962  80.391 1.00 18.84 ? 471  ASP   B N    1 
ATOM   16629 C  CA   . ASP   B 1 471 ? -2.129 12.495  80.272 1.00 22.20 ? 471  ASP   B CA   1 
ATOM   16630 C  C    . ASP   B 1 471 ? -1.508 11.983  78.968 1.00 21.79 ? 471  ASP   B C    1 
ATOM   16631 O  O    . ASP   B 1 471 ? -1.799 12.548  77.945 1.00 20.40 ? 471  ASP   B O    1 
ATOM   16632 C  CB   . ASP   B 1 471 ? -3.598 12.088  80.391 1.00 26.37 ? 471  ASP   B CB   1 
ATOM   16633 C  CG   . ASP   B 1 471 ? -4.129 12.222  81.805 1.00 37.82 ? 471  ASP   B CG   1 
ATOM   16634 O  OD1  . ASP   B 1 471 ? -3.389 11.876  82.736 1.00 39.76 ? 471  ASP   B OD1  1 
ATOM   16635 O  OD2  . ASP   B 1 471 ? -5.273 12.686  81.962 1.00 42.96 ? 471  ASP   B OD2  1 
ATOM   16636 H  H    . ASP   B 1 471 ? -2.732 14.399  80.453 1.00 22.62 ? 471  ASP   B H    1 
ATOM   16637 H  HA   . ASP   B 1 471 ? -1.640 12.082  81.001 1.00 26.64 ? 471  ASP   B HA   1 
ATOM   16638 H  HB2  . ASP   B 1 471 ? -4.131 12.638  79.796 1.00 31.64 ? 471  ASP   B HB2  1 
ATOM   16639 H  HB3  . ASP   B 1 471 ? -3.700 11.169  80.097 1.00 31.64 ? 471  ASP   B HB3  1 
ATOM   16640 N  N    . GLY   B 1 472 ? -0.677 10.939  79.078 1.00 20.18 ? 472  GLY   B N    1 
ATOM   16641 C  CA   . GLY   B 1 472 ? -0.081 10.293  77.897 1.00 21.77 ? 472  GLY   B CA   1 
ATOM   16642 C  C    . GLY   B 1 472 ? 1.171  10.969  77.370 1.00 19.79 ? 472  GLY   B C    1 
ATOM   16643 O  O    . GLY   B 1 472 ? 1.790  10.398  76.494 1.00 17.23 ? 472  GLY   B O    1 
ATOM   16644 H  H    . GLY   B 1 472 ? -0.445 10.589  79.828 1.00 24.22 ? 472  GLY   B H    1 
ATOM   16645 H  HA2  . GLY   B 1 472 ? 0.132  9.373   78.119 1.00 26.12 ? 472  GLY   B HA2  1 
ATOM   16646 H  HA3  . GLY   B 1 472 ? -0.743 10.268  77.188 1.00 26.12 ? 472  GLY   B HA3  1 
ATOM   16647 N  N    . LYS   B 1 473 ? 1.499  12.141  77.928 1.00 16.94 ? 473  LYS   B N    1 
ATOM   16648 C  CA   . LYS   B 1 473 ? 2.638  12.933  77.389 1.00 18.19 ? 473  LYS   B CA   1 
ATOM   16649 C  C    . LYS   B 1 473 ? 3.967  12.234  77.696 1.00 13.27 ? 473  LYS   B C    1 
ATOM   16650 O  O    . LYS   B 1 473 ? 4.824  12.190  76.802 1.00 17.13 ? 473  LYS   B O    1 
ATOM   16651 C  CB   . LYS   B 1 473 ? 2.589  14.368  77.925 1.00 16.06 ? 473  LYS   B CB   1 
ATOM   16652 C  CG   . LYS   B 1 473 ? 1.463  15.225  77.361 1.00 16.45 ? 473  LYS   B CG   1 
ATOM   16653 C  CD   . LYS   B 1 473 ? 1.277  15.067  75.866 1.00 16.92 ? 473  LYS   B CD   1 
ATOM   16654 C  CE   . LYS   B 1 473 ? 0.048  15.773  75.334 1.00 19.13 ? 473  LYS   B CE   1 
ATOM   16655 N  NZ   . LYS   B 1 473 ? 0.050  17.216  75.671 1.00 20.79 ? 473  LYS   B NZ   1 
ATOM   16656 H  H    . LYS   B 1 473 ? 1.094  12.494  78.599 1.00 20.33 ? 473  LYS   B H    1 
ATOM   16657 H  HA   . LYS   B 1 473 ? 2.564  12.988  76.423 1.00 21.84 ? 473  LYS   B HA   1 
ATOM   16658 H  HB2  . LYS   B 1 473 ? 2.501  14.336  78.890 1.00 19.28 ? 473  LYS   B HB2  1 
ATOM   16659 H  HB3  . LYS   B 1 473 ? 3.435  14.801  77.732 1.00 19.28 ? 473  LYS   B HB3  1 
ATOM   16660 H  HG2  . LYS   B 1 473 ? 0.634  14.994  77.809 1.00 19.74 ? 473  LYS   B HG2  1 
ATOM   16661 H  HG3  . LYS   B 1 473 ? 1.644  16.157  77.561 1.00 19.74 ? 473  LYS   B HG3  1 
ATOM   16662 H  HD2  . LYS   B 1 473 ? 2.062  15.411  75.411 1.00 20.31 ? 473  LYS   B HD2  1 
ATOM   16663 H  HD3  . LYS   B 1 473 ? 1.217  14.123  75.652 1.00 20.31 ? 473  LYS   B HD3  1 
ATOM   16664 H  HE2  . LYS   B 1 473 ? 0.006  15.666  74.371 1.00 22.96 ? 473  LYS   B HE2  1 
ATOM   16665 H  HE3  . LYS   B 1 473 ? -0.748 15.357  75.701 1.00 22.96 ? 473  LYS   B HE3  1 
ATOM   16666 H  HZ1  . LYS   B 1 473 ? -0.646 17.613  75.283 1.00 24.95 ? 473  LYS   B HZ1  1 
ATOM   16667 H  HZ2  . LYS   B 1 473 ? -0.006 17.315  76.554 1.00 24.95 ? 473  LYS   B HZ2  1 
ATOM   16668 H  HZ3  . LYS   B 1 473 ? 0.804  17.588  75.379 1.00 24.95 ? 473  LYS   B HZ3  1 
ATOM   16669 N  N    . ALA   B 1 474 ? 4.121  11.706  78.910 1.00 15.58 ? 474  ALA   B N    1 
ATOM   16670 C  CA   . ALA   B 1 474 ? 5.393  11.054  79.291 1.00 17.63 ? 474  ALA   B CA   1 
ATOM   16671 C  C    . ALA   B 1 474 ? 5.644  9.843   78.387 1.00 15.84 ? 474  ALA   B C    1 
ATOM   16672 O  O    . ALA   B 1 474 ? 6.779  9.675   77.913 1.00 15.14 ? 474  ALA   B O    1 
ATOM   16673 C  CB   . ALA   B 1 474 ? 5.367  10.667  80.749 1.00 20.45 ? 474  ALA   B CB   1 
ATOM   16674 H  H    . ALA   B 1 474 ? 3.518  11.710  79.523 1.00 18.70 ? 474  ALA   B H    1 
ATOM   16675 H  HA   . ALA   B 1 474 ? 6.126  11.677  79.169 1.00 21.16 ? 474  ALA   B HA   1 
ATOM   16676 H  HB1  . ALA   B 1 474 ? 6.206  10.241  80.986 1.00 24.54 ? 474  ALA   B HB1  1 
ATOM   16677 H  HB2  . ALA   B 1 474 ? 5.243  11.461  81.293 1.00 24.54 ? 474  ALA   B HB2  1 
ATOM   16678 H  HB3  . ALA   B 1 474 ? 4.635  10.050  80.907 1.00 24.54 ? 474  ALA   B HB3  1 
ATOM   16679 N  N    . ALA   B 1 475 ? 4.609  9.032   78.176 1.00 16.01 ? 475  ALA   B N    1 
ATOM   16680 C  CA   . ALA   B 1 475 ? 4.761  7.822   77.340 1.00 19.57 ? 475  ALA   B CA   1 
ATOM   16681 C  C    . ALA   B 1 475 ? 5.083  8.225   75.899 1.00 17.56 ? 475  ALA   B C    1 
ATOM   16682 O  O    . ALA   B 1 475 ? 5.916  7.554   75.274 1.00 18.68 ? 475  ALA   B O    1 
ATOM   16683 C  CB   . ALA   B 1 475 ? 3.496  7.003   77.411 1.00 20.13 ? 475  ALA   B CB   1 
ATOM   16684 H  H    . ALA   B 1 475 ? 3.821  9.154   78.498 1.00 19.22 ? 475  ALA   B H    1 
ATOM   16685 H  HA   . ALA   B 1 475 ? 5.495  7.281   77.670 1.00 23.48 ? 475  ALA   B HA   1 
ATOM   16686 H  HB1  . ALA   B 1 475 ? 3.593  6.209   76.863 1.00 24.16 ? 475  ALA   B HB1  1 
ATOM   16687 H  HB2  . ALA   B 1 475 ? 3.330  6.743   78.331 1.00 24.16 ? 475  ALA   B HB2  1 
ATOM   16688 H  HB3  . ALA   B 1 475 ? 2.750  7.530   77.085 1.00 24.16 ? 475  ALA   B HB3  1 
ATOM   16689 N  N    . TYR   B 1 476 ? 4.435  9.279   75.403 1.00 15.71 ? 476  TYR   B N    1 
ATOM   16690 C  CA   . TYR   B 1 476 ? 4.640  9.702   73.994 1.00 16.43 ? 476  TYR   B CA   1 
ATOM   16691 C  C    . TYR   B 1 476 ? 6.058  10.252  73.821 1.00 19.65 ? 476  TYR   B C    1 
ATOM   16692 O  O    . TYR   B 1 476 ? 6.690  10.001  72.785 1.00 15.44 ? 476  TYR   B O    1 
ATOM   16693 C  CB   . TYR   B 1 476 ? 3.588  10.730  73.576 1.00 23.46 ? 476  TYR   B CB   1 
ATOM   16694 C  CG   . TYR   B 1 476 ? 2.972  10.444  72.232 1.00 24.48 ? 476  TYR   B CG   1 
ATOM   16695 C  CD1  . TYR   B 1 476 ? 3.707  10.599  71.070 1.00 26.05 ? 476  TYR   B CD1  1 
ATOM   16696 C  CD2  . TYR   B 1 476 ? 1.667  9.997   72.122 1.00 25.04 ? 476  TYR   B CD2  1 
ATOM   16697 C  CE1  . TYR   B 1 476 ? 3.157  10.331  69.829 1.00 28.05 ? 476  TYR   B CE1  1 
ATOM   16698 C  CE2  . TYR   B 1 476 ? 1.101  9.725   70.889 1.00 28.21 ? 476  TYR   B CE2  1 
ATOM   16699 C  CZ   . TYR   B 1 476 ? 1.850  9.892   69.738 1.00 27.51 ? 476  TYR   B CZ   1 
ATOM   16700 O  OH   . TYR   B 1 476 ? 1.306  9.626   68.508 1.00 35.65 ? 476  TYR   B OH   1 
ATOM   16701 H  H    . TYR   B 1 476 ? 3.880  9.762   75.848 1.00 18.85 ? 476  TYR   B H    1 
ATOM   16702 H  HA   . TYR   B 1 476 ? 4.536  8.931   73.414 1.00 19.72 ? 476  TYR   B HA   1 
ATOM   16703 H  HB2  . TYR   B 1 476 ? 2.887  10.756  74.246 1.00 28.16 ? 476  TYR   B HB2  1 
ATOM   16704 H  HB3  . TYR   B 1 476 ? 3.995  11.610  73.557 1.00 28.16 ? 476  TYR   B HB3  1 
ATOM   16705 H  HD1  . TYR   B 1 476 ? 4.589  10.889  71.124 1.00 31.27 ? 476  TYR   B HD1  1 
ATOM   16706 H  HD2  . TYR   B 1 476 ? 1.160  9.877   72.892 1.00 30.05 ? 476  TYR   B HD2  1 
ATOM   16707 H  HE1  . TYR   B 1 476 ? 3.665  10.446  69.059 1.00 33.66 ? 476  TYR   B HE1  1 
ATOM   16708 H  HE2  . TYR   B 1 476 ? 0.220  9.431   70.834 1.00 33.86 ? 476  TYR   B HE2  1 
ATOM   16709 H  HH   . TYR   B 1 476 ? 0.559  9.254   68.606 1.00 42.78 ? 476  TYR   B HH   1 
ATOM   16710 N  N    . ALA   B 1 477 ? 6.537  10.978  74.827 1.00 14.14 ? 477  ALA   B N    1 
ATOM   16711 C  CA   . ALA   B 1 477 ? 7.905  11.531  74.760 1.00 15.20 ? 477  ALA   B CA   1 
ATOM   16712 C  C    . ALA   B 1 477 ? 8.917  10.380  74.693 1.00 15.12 ? 477  ALA   B C    1 
ATOM   16713 O  O    . ALA   B 1 477 ? 9.857  10.462  73.897 1.00 16.35 ? 477  ALA   B O    1 
ATOM   16714 C  CB   . ALA   B 1 477 ? 8.149  12.424  75.949 1.00 16.68 ? 477  ALA   B CB   1 
ATOM   16715 H  H    . ALA   B 1 477 ? 6.104  11.164  75.546 1.00 16.97 ? 477  ALA   B H    1 
ATOM   16716 H  HA   . ALA   B 1 477 ? 8.011  12.069  73.960 1.00 18.25 ? 477  ALA   B HA   1 
ATOM   16717 H  HB1  . ALA   B 1 477 ? 9.048  12.786  75.903 1.00 20.02 ? 477  ALA   B HB1  1 
ATOM   16718 H  HB2  . ALA   B 1 477 ? 7.507  13.151  75.945 1.00 20.02 ? 477  ALA   B HB2  1 
ATOM   16719 H  HB3  . ALA   B 1 477 ? 8.049  11.910  76.766 1.00 20.02 ? 477  ALA   B HB3  1 
ATOM   16720 N  N    . LYS   B 1 478 ? 8.718  9.353   75.523 1.00 16.41 ? 478  LYS   B N    1 
ATOM   16721 C  CA   . LYS   B 1 478 ? 9.646  8.193   75.516 1.00 17.11 ? 478  LYS   B CA   1 
ATOM   16722 C  C    . LYS   B 1 478 ? 9.686  7.610   74.100 1.00 16.25 ? 478  LYS   B C    1 
ATOM   16723 O  O    . LYS   B 1 478 ? 10.786 7.355   73.596 1.00 16.90 ? 478  LYS   B O    1 
ATOM   16724 C  CB   . LYS   B 1 478 ? 9.218  7.109   76.508 1.00 17.67 ? 478  LYS   B CB   1 
ATOM   16725 C  CG   . LYS   B 1 478 ? 10.084 5.857   76.480 1.00 17.33 ? 478  LYS   B CG   1 
ATOM   16726 C  CD   . LYS   B 1 478 ? 9.700  4.819   77.507 1.00 19.45 ? 478  LYS   B CD   1 
ATOM   16727 C  CE   . LYS   B 1 478 ? 10.677 3.663   77.551 1.00 19.94 ? 478  LYS   B CE   1 
ATOM   16728 N  NZ   . LYS   B 1 478 ? 10.797 2.997   76.233 1.00 21.31 ? 478  LYS   B NZ   1 
ATOM   16729 H  H    . LYS   B 1 478 ? 8.072  9.299   76.088 1.00 19.70 ? 478  LYS   B H    1 
ATOM   16730 H  HA   . LYS   B 1 478 ? 10.525 8.501   75.788 1.00 20.54 ? 478  LYS   B HA   1 
ATOM   16731 H  HB2  . LYS   B 1 478 ? 9.234  7.481   77.404 1.00 21.20 ? 478  LYS   B HB2  1 
ATOM   16732 H  HB3  . LYS   B 1 478 ? 8.300  6.859   76.321 1.00 21.20 ? 478  LYS   B HB3  1 
ATOM   16733 H  HG2  . LYS   B 1 478 ? 10.032 5.459   75.597 1.00 20.80 ? 478  LYS   B HG2  1 
ATOM   16734 H  HG3  . LYS   B 1 478 ? 11.009 6.112   76.622 1.00 20.80 ? 478  LYS   B HG3  1 
ATOM   16735 H  HD2  . LYS   B 1 478 ? 9.655  5.235   78.382 1.00 23.34 ? 478  LYS   B HD2  1 
ATOM   16736 H  HD3  . LYS   B 1 478 ? 8.813  4.482   77.307 1.00 23.34 ? 478  LYS   B HD3  1 
ATOM   16737 H  HE2  . LYS   B 1 478 ? 11.548 3.985   77.831 1.00 23.93 ? 478  LYS   B HE2  1 
ATOM   16738 H  HE3  . LYS   B 1 478 ? 10.386 3.018   78.215 1.00 23.93 ? 478  LYS   B HE3  1 
ATOM   16739 H  HZ1  . LYS   B 1 478 ? 11.296 2.265   76.315 1.00 25.57 ? 478  LYS   B HZ1  1 
ATOM   16740 H  HZ2  . LYS   B 1 478 ? 9.988  2.773   75.939 1.00 25.57 ? 478  LYS   B HZ2  1 
ATOM   16741 H  HZ3  . LYS   B 1 478 ? 11.179 3.553   75.653 1.00 25.57 ? 478  LYS   B HZ3  1 
ATOM   16742 N  N    . LEU   B 1 479 ? 8.512  7.429   73.492 1.00 18.42 ? 479  LEU   B N    1 
ATOM   16743 C  CA   . LEU   B 1 479 ? 8.464  6.830   72.133 1.00 20.74 ? 479  LEU   B CA   1 
ATOM   16744 C  C    . LEU   B 1 479 ? 9.282  7.703   71.178 1.00 19.08 ? 479  LEU   B C    1 
ATOM   16745 O  O    . LEU   B 1 479 ? 10.082 7.155   70.409 1.00 18.68 ? 479  LEU   B O    1 
ATOM   16746 C  CB   . LEU   B 1 479 ? 7.011  6.737   71.667 1.00 21.74 ? 479  LEU   B CB   1 
ATOM   16747 C  CG   . LEU   B 1 479 ? 6.820  6.694   70.152 1.00 29.66 ? 479  LEU   B CG   1 
ATOM   16748 C  CD1  . LEU   B 1 479 ? 7.353  5.389   69.580 1.00 33.30 ? 479  LEU   B CD1  1 
ATOM   16749 C  CD2  . LEU   B 1 479 ? 5.358  6.885   69.782 1.00 33.52 ? 479  LEU   B CD2  1 
ATOM   16750 H  H    . LEU   B 1 479 ? 7.748  7.636   73.828 1.00 22.11 ? 479  LEU   B H    1 
ATOM   16751 H  HA   . LEU   B 1 479 ? 8.840  5.936   72.147 1.00 24.89 ? 479  LEU   B HA   1 
ATOM   16752 H  HB2  . LEU   B 1 479 ? 6.612  5.941   72.052 1.00 26.09 ? 479  LEU   B HB2  1 
ATOM   16753 H  HB3  . LEU   B 1 479 ? 6.523  7.498   72.019 1.00 26.09 ? 479  LEU   B HB3  1 
ATOM   16754 H  HG   . LEU   B 1 479 ? 7.326  7.426   69.765 1.00 35.60 ? 479  LEU   B HG   1 
ATOM   16755 H  HD11 . LEU   B 1 479 ? 7.223  5.380   68.619 1.00 39.96 ? 479  LEU   B HD11 1 
ATOM   16756 H  HD12 . LEU   B 1 479 ? 8.299  5.311   69.779 1.00 39.96 ? 479  LEU   B HD12 1 
ATOM   16757 H  HD13 . LEU   B 1 479 ? 6.877  4.643   69.977 1.00 39.96 ? 479  LEU   B HD13 1 
ATOM   16758 H  HD21 . LEU   B 1 479 ? 5.261  6.854   68.817 1.00 40.22 ? 479  LEU   B HD21 1 
ATOM   16759 H  HD22 . LEU   B 1 479 ? 4.828  6.178   70.182 1.00 40.22 ? 479  LEU   B HD22 1 
ATOM   16760 H  HD23 . LEU   B 1 479 ? 5.051  7.745   70.110 1.00 40.22 ? 479  LEU   B HD23 1 
ATOM   16761 N  N    . PHE   B 1 480 ? 9.075  9.018   71.239 1.00 20.31 ? 480  PHE   B N    1 
ATOM   16762 C  CA   . PHE   B 1 480 ? 9.779  9.923   70.295 1.00 16.64 ? 480  PHE   B CA   1 
ATOM   16763 C  C    . PHE   B 1 480 ? 11.283 9.863   70.567 1.00 16.48 ? 480  PHE   B C    1 
ATOM   16764 O  O    . PHE   B 1 480 ? 12.070 9.885   69.617 1.00 17.52 ? 480  PHE   B O    1 
ATOM   16765 C  CB   . PHE   B 1 480 ? 9.211  11.341  70.389 1.00 21.06 ? 480  PHE   B CB   1 
ATOM   16766 C  CG   . PHE   B 1 480 ? 8.366  11.721  69.202 1.00 21.31 ? 480  PHE   B CG   1 
ATOM   16767 C  CD1  . PHE   B 1 480 ? 8.941  12.285  68.076 1.00 21.98 ? 480  PHE   B CD1  1 
ATOM   16768 C  CD2  . PHE   B 1 480 ? 7.002  11.483  69.199 1.00 26.61 ? 480  PHE   B CD2  1 
ATOM   16769 C  CE1  . PHE   B 1 480 ? 8.165  12.621  66.979 1.00 23.82 ? 480  PHE   B CE1  1 
ATOM   16770 C  CE2  . PHE   B 1 480 ? 6.228  11.820  68.101 1.00 27.15 ? 480  PHE   B CE2  1 
ATOM   16771 C  CZ   . PHE   B 1 480 ? 6.811  12.388  66.994 1.00 25.78 ? 480  PHE   B CZ   1 
ATOM   16772 H  H    . PHE   B 1 480 ? 8.550  9.407   71.798 1.00 24.38 ? 480  PHE   B H    1 
ATOM   16773 H  HA   . PHE   B 1 480 ? 9.635  9.633   69.381 1.00 19.97 ? 480  PHE   B HA   1 
ATOM   16774 H  HB2  . PHE   B 1 480 ? 8.678  11.417  71.196 1.00 25.28 ? 480  PHE   B HB2  1 
ATOM   16775 H  HB3  . PHE   B 1 480 ? 9.943  11.972  70.473 1.00 25.28 ? 480  PHE   B HB3  1 
ATOM   16776 H  HD1  . PHE   B 1 480 ? 9.858  12.440  68.056 1.00 26.39 ? 480  PHE   B HD1  1 
ATOM   16777 H  HD2  . PHE   B 1 480 ? 6.601  11.093  69.942 1.00 31.93 ? 480  PHE   B HD2  1 
ATOM   16778 H  HE1  . PHE   B 1 480 ? 8.561  13.005  66.231 1.00 28.59 ? 480  PHE   B HE1  1 
ATOM   16779 H  HE2  . PHE   B 1 480 ? 5.312  11.661  68.113 1.00 32.58 ? 480  PHE   B HE2  1 
ATOM   16780 H  HZ   . PHE   B 1 480 ? 6.291  12.614  66.257 1.00 30.94 ? 480  PHE   B HZ   1 
ATOM   16781 N  N    . HIS   B 1 481 ? 11.655 9.802   71.845 1.00 15.88 ? 481  HIS   B N    1 
ATOM   16782 C  CA   . HIS   B 1 481 ? 13.091 9.738   72.209 1.00 14.57 ? 481  HIS   B CA   1 
ATOM   16783 C  C    . HIS   B 1 481 ? 13.702 8.466   71.615 1.00 15.67 ? 481  HIS   B C    1 
ATOM   16784 O  O    . HIS   B 1 481 ? 14.808 8.519   71.054 1.00 15.34 ? 481  HIS   B O    1 
ATOM   16785 C  CB   . HIS   B 1 481 ? 13.246 9.810   73.731 1.00 14.84 ? 481  HIS   B CB   1 
ATOM   16786 C  CG   . HIS   B 1 481 ? 12.754 11.093  74.311 1.00 14.29 ? 481  HIS   B CG   1 
ATOM   16787 N  ND1  . HIS   B 1 481 ? 12.443 11.250  75.644 1.00 14.31 ? 481  HIS   B ND1  1 
ATOM   16788 C  CD2  . HIS   B 1 481 ? 12.513 12.275  73.734 1.00 15.11 ? 481  HIS   B CD2  1 
ATOM   16789 C  CE1  . HIS   B 1 481 ? 12.031 12.491  75.854 1.00 15.83 ? 481  HIS   B CE1  1 
ATOM   16790 N  NE2  . HIS   B 1 481 ? 12.066 13.131  74.706 1.00 14.32 ? 481  HIS   B NE2  1 
ATOM   16791 H  H    . HIS   B 1 481 ? 11.111 9.796   72.511 1.00 19.05 ? 481  HIS   B H    1 
ATOM   16792 H  HA   . HIS   B 1 481 ? 13.570 10.496  71.840 1.00 17.48 ? 481  HIS   B HA   1 
ATOM   16793 H  HB2  . HIS   B 1 481 ? 12.762 9.073   74.135 1.00 17.82 ? 481  HIS   B HB2  1 
ATOM   16794 H  HB3  . HIS   B 1 481 ? 14.181 9.695   73.961 1.00 17.82 ? 481  HIS   B HB3  1 
ATOM   16795 H  HD2  . HIS   B 1 481 ? 12.628 12.479  72.834 1.00 18.14 ? 481  HIS   B HD2  1 
ATOM   16796 H  HE1  . HIS   B 1 481 ? 11.764 12.847  76.670 1.00 19.00 ? 481  HIS   B HE1  1 
ATOM   16797 H  HE2  . HIS   B 1 481 ? 11.844 13.953  74.585 1.00 17.18 ? 481  HIS   B HE2  1 
ATOM   16798 N  N    . ASP   B 1 482 ? 12.988 7.348   71.747 1.00 16.93 ? 482  ASP   B N    1 
ATOM   16799 C  CA   . ASP   B 1 482 ? 13.554 6.054   71.285 1.00 15.78 ? 482  ASP   B CA   1 
ATOM   16800 C  C    . ASP   B 1 482 ? 13.584 6.006   69.754 1.00 15.90 ? 482  ASP   B C    1 
ATOM   16801 O  O    . ASP   B 1 482 ? 14.574 5.517   69.199 1.00 16.54 ? 482  ASP   B O    1 
ATOM   16802 C  CB   . ASP   B 1 482 ? 12.774 4.878   71.879 1.00 16.16 ? 482  ASP   B CB   1 
ATOM   16803 C  CG   . ASP   B 1 482 ? 12.876 4.790   73.391 1.00 17.56 ? 482  ASP   B CG   1 
ATOM   16804 O  OD1  . ASP   B 1 482 ? 13.732 5.488   73.958 1.00 17.70 ? 482  ASP   B OD1  1 
ATOM   16805 O  OD2  . ASP   B 1 482 ? 12.097 4.024   73.983 1.00 17.55 ? 482  ASP   B OD2  1 
ATOM   16806 H  H    . ASP   B 1 482 ? 12.200 7.304   72.088 1.00 20.31 ? 482  ASP   B H    1 
ATOM   16807 H  HA   . ASP   B 1 482 ? 14.468 5.979   71.600 1.00 18.94 ? 482  ASP   B HA   1 
ATOM   16808 H  HB2  . ASP   B 1 482 ? 11.840 4.958   71.629 1.00 19.39 ? 482  ASP   B HB2  1 
ATOM   16809 H  HB3  . ASP   B 1 482 ? 13.102 4.052   71.491 1.00 19.39 ? 482  ASP   B HB3  1 
ATOM   16810 N  N    . LEU   B 1 483 ? 12.528 6.503   69.108 1.00 16.82 ? 483  LEU   B N    1 
ATOM   16811 C  CA   . LEU   B 1 483 ? 12.463 6.471   67.620 1.00 18.71 ? 483  LEU   B CA   1 
ATOM   16812 C  C    . LEU   B 1 483 ? 13.528 7.400   67.024 1.00 15.56 ? 483  LEU   B C    1 
ATOM   16813 O  O    . LEU   B 1 483 ? 14.143 7.026   66.022 1.00 14.35 ? 483  LEU   B O    1 
ATOM   16814 C  CB   . LEU   B 1 483 ? 11.063 6.878   67.156 1.00 17.59 ? 483  LEU   B CB   1 
ATOM   16815 C  CG   . LEU   B 1 483 ? 10.866 6.905   65.641 1.00 19.75 ? 483  LEU   B CG   1 
ATOM   16816 C  CD1  . LEU   B 1 483 ? 11.004 5.510   65.052 1.00 19.54 ? 483  LEU   B CD1  1 
ATOM   16817 C  CD2  . LEU   B 1 483 ? 9.518  7.506   65.280 1.00 20.03 ? 483  LEU   B CD2  1 
ATOM   16818 H  H    . LEU   B 1 483 ? 11.846 6.859   69.492 1.00 20.19 ? 483  LEU   B H    1 
ATOM   16819 H  HA   . LEU   B 1 483 ? 12.642 5.569   67.310 1.00 22.46 ? 483  LEU   B HA   1 
ATOM   16820 H  HB2  . LEU   B 1 483 ? 10.418 6.264   67.541 1.00 21.11 ? 483  LEU   B HB2  1 
ATOM   16821 H  HB3  . LEU   B 1 483 ? 10.863 7.759   67.510 1.00 21.11 ? 483  LEU   B HB3  1 
ATOM   16822 H  HG   . LEU   B 1 483 ? 11.560 7.466   65.260 1.00 23.70 ? 483  LEU   B HG   1 
ATOM   16823 H  HD11 . LEU   B 1 483 ? 10.876 5.550   64.091 1.00 23.46 ? 483  LEU   B HD11 1 
ATOM   16824 H  HD12 . LEU   B 1 483 ? 11.889 5.163   65.245 1.00 23.46 ? 483  LEU   B HD12 1 
ATOM   16825 H  HD13 . LEU   B 1 483 ? 10.336 4.926   65.443 1.00 23.46 ? 483  LEU   B HD13 1 
ATOM   16826 H  HD21 . LEU   B 1 483 ? 9.415  7.513   64.316 1.00 24.04 ? 483  LEU   B HD21 1 
ATOM   16827 H  HD22 . LEU   B 1 483 ? 8.810  6.975   65.677 1.00 24.04 ? 483  LEU   B HD22 1 
ATOM   16828 H  HD23 . LEU   B 1 483 ? 9.468  8.414   65.617 1.00 24.04 ? 483  LEU   B HD23 1 
ATOM   16829 N  N    . THR   B 1 484 ? 13.719 8.573   67.632 1.00 14.13 ? 484  THR   B N    1 
ATOM   16830 C  CA   . THR   B 1 484 ? 14.753 9.517   67.136 1.00 15.24 ? 484  THR   B CA   1 
ATOM   16831 C  C    . THR   B 1 484 ? 16.135 8.869   67.294 1.00 14.90 ? 484  THR   B C    1 
ATOM   16832 O  O    . THR   B 1 484 ? 16.975 9.054   66.404 1.00 13.99 ? 484  THR   B O    1 
ATOM   16833 C  CB   . THR   B 1 484 ? 14.626 10.883  67.827 1.00 14.74 ? 484  THR   B CB   1 
ATOM   16834 O  OG1  . THR   B 1 484 ? 13.298 11.355  67.607 1.00 12.89 ? 484  THR   B OG1  1 
ATOM   16835 C  CG2  . THR   B 1 484 ? 15.630 11.892  67.316 1.00 13.04 ? 484  THR   B CG2  1 
ATOM   16836 H  H    . THR   B 1 484 ? 13.277 8.845   68.318 1.00 16.96 ? 484  THR   B H    1 
ATOM   16837 H  HA   . THR   B 1 484 ? 14.623 9.696   66.192 1.00 18.29 ? 484  THR   B HA   1 
ATOM   16838 H  HB   . THR   B 1 484 ? 14.811 10.774  68.773 1.00 17.69 ? 484  THR   B HB   1 
ATOM   16839 H  HG1  . THR   B 1 484 ? 12.774 10.981  68.147 1.00 15.47 ? 484  THR   B HG1  1 
ATOM   16840 H  HG21 . THR   B 1 484 ? 15.509 12.734  67.782 1.00 15.65 ? 484  THR   B HG21 1 
ATOM   16841 H  HG22 . THR   B 1 484 ? 16.529 11.563  67.473 1.00 15.65 ? 484  THR   B HG22 1 
ATOM   16842 H  HG23 . THR   B 1 484 ? 15.497 12.027  66.365 1.00 15.65 ? 484  THR   B HG23 1 
ATOM   16843 N  N    . ALA   B 1 485 ? 16.352 8.139   68.393 1.00 14.30 ? 485  ALA   B N    1 
ATOM   16844 C  CA   . ALA   B 1 485 ? 17.645 7.437   68.570 1.00 14.00 ? 485  ALA   B CA   1 
ATOM   16845 C  C    . ALA   B 1 485 ? 17.840 6.434   67.427 1.00 15.17 ? 485  ALA   B C    1 
ATOM   16846 O  O    . ALA   B 1 485 ? 18.973 6.291   66.948 1.00 14.35 ? 485  ALA   B O    1 
ATOM   16847 C  CB   . ALA   B 1 485 ? 17.704 6.769   69.921 1.00 18.17 ? 485  ALA   B CB   1 
ATOM   16848 H  H    . ALA   B 1 485 ? 15.787 8.035   69.033 1.00 17.17 ? 485  ALA   B H    1 
ATOM   16849 H  HA   . ALA   B 1 485 ? 18.372 8.079   68.538 1.00 16.80 ? 485  ALA   B HA   1 
ATOM   16850 H  HB1  . ALA   B 1 485 ? 18.555 6.315   70.021 1.00 21.81 ? 485  ALA   B HB1  1 
ATOM   16851 H  HB2  . ALA   B 1 485 ? 17.611 7.438   70.617 1.00 21.81 ? 485  ALA   B HB2  1 
ATOM   16852 H  HB3  . ALA   B 1 485 ? 16.983 6.124   69.995 1.00 21.81 ? 485  ALA   B HB3  1 
ATOM   16853 N  N    . VAL   B 1 486 ? 16.756 5.784   67.011 1.00 14.59 ? 486  VAL   B N    1 
ATOM   16854 C  CA   . VAL   B 1 486 ? 16.843 4.822   65.873 1.00 16.12 ? 486  VAL   B CA   1 
ATOM   16855 C  C    . VAL   B 1 486 ? 17.234 5.584   64.602 1.00 14.68 ? 486  VAL   B C    1 
ATOM   16856 O  O    . VAL   B 1 486 ? 18.242 5.220   63.986 1.00 16.32 ? 486  VAL   B O    1 
ATOM   16857 C  CB   . VAL   B 1 486 ? 15.519 4.058   65.683 1.00 15.19 ? 486  VAL   B CB   1 
ATOM   16858 C  CG1  . VAL   B 1 486 ? 15.465 3.340   64.344 1.00 20.88 ? 486  VAL   B CG1  1 
ATOM   16859 C  CG2  . VAL   B 1 486 ? 15.248 3.093   66.826 1.00 16.35 ? 486  VAL   B CG2  1 
ATOM   16860 H  H    . VAL   B 1 486 ? 15.972 5.872   67.354 1.00 17.51 ? 486  VAL   B H    1 
ATOM   16861 H  HA   . VAL   B 1 486 ? 17.524 4.159   66.068 1.00 19.34 ? 486  VAL   B HA   1 
ATOM   16862 H  HB   . VAL   B 1 486 ? 14.814 4.725   65.689 1.00 18.23 ? 486  VAL   B HB   1 
ATOM   16863 H  HG11 . VAL   B 1 486 ? 14.619 2.872   64.261 1.00 25.06 ? 486  VAL   B HG11 1 
ATOM   16864 H  HG12 . VAL   B 1 486 ? 15.547 3.987   63.626 1.00 25.06 ? 486  VAL   B HG12 1 
ATOM   16865 H  HG13 . VAL   B 1 486 ? 16.194 2.702   64.289 1.00 25.06 ? 486  VAL   B HG13 1 
ATOM   16866 H  HG21 . VAL   B 1 486 ? 14.408 2.633   66.669 1.00 19.63 ? 486  VAL   B HG21 1 
ATOM   16867 H  HG22 . VAL   B 1 486 ? 15.967 2.444   66.879 1.00 19.63 ? 486  VAL   B HG22 1 
ATOM   16868 H  HG23 . VAL   B 1 486 ? 15.196 3.585   67.660 1.00 19.63 ? 486  VAL   B HG23 1 
ATOM   16869 N  N    . ILE   B 1 487 ? 16.468 6.613   64.238 1.00 14.35 ? 487  ILE   B N    1 
ATOM   16870 C  CA   . ILE   B 1 487 ? 16.720 7.331   62.951 1.00 15.45 ? 487  ILE   B CA   1 
ATOM   16871 C  C    . ILE   B 1 487 ? 18.126 7.937   62.962 1.00 14.49 ? 487  ILE   B C    1 
ATOM   16872 O  O    . ILE   B 1 487 ? 18.844 7.785   61.961 1.00 14.67 ? 487  ILE   B O    1 
ATOM   16873 C  CB   . ILE   B 1 487 ? 15.622 8.385   62.708 1.00 15.87 ? 487  ILE   B CB   1 
ATOM   16874 C  CG1  . ILE   B 1 487 ? 14.242 7.726   62.623 1.00 15.54 ? 487  ILE   B CG1  1 
ATOM   16875 C  CG2  . ILE   B 1 487 ? 15.931 9.219   61.475 1.00 16.05 ? 487  ILE   B CG2  1 
ATOM   16876 C  CD1  . ILE   B 1 487 ? 13.089 8.661   62.890 1.00 16.52 ? 487  ILE   B CD1  1 
ATOM   16877 H  H    . ILE   B 1 487 ? 15.809 6.917   64.699 1.00 17.22 ? 487  ILE   B H    1 
ATOM   16878 H  HA   . ILE   B 1 487 ? 16.681 6.706   62.210 1.00 18.55 ? 487  ILE   B HA   1 
ATOM   16879 H  HB   . ILE   B 1 487 ? 15.606 8.990   63.466 1.00 19.05 ? 487  ILE   B HB   1 
ATOM   16880 H  HG12 . ILE   B 1 487 ? 14.134 7.340   61.740 1.00 18.65 ? 487  ILE   B HG12 1 
ATOM   16881 H  HG13 . ILE   B 1 487 ? 14.205 6.994   63.259 1.00 18.65 ? 487  ILE   B HG13 1 
ATOM   16882 H  HG21 . ILE   B 1 487 ? 15.228 9.874   61.343 1.00 19.26 ? 487  ILE   B HG21 1 
ATOM   16883 H  HG22 . ILE   B 1 487 ? 16.778 9.675   61.597 1.00 19.26 ? 487  ILE   B HG22 1 
ATOM   16884 H  HG23 . ILE   B 1 487 ? 15.984 8.641   60.698 1.00 19.26 ? 487  ILE   B HG23 1 
ATOM   16885 H  HD11 . ILE   B 1 487 ? 12.253 8.173   62.818 1.00 19.83 ? 487  ILE   B HD11 1 
ATOM   16886 H  HD12 . ILE   B 1 487 ? 13.172 9.030   63.783 1.00 19.83 ? 487  ILE   B HD12 1 
ATOM   16887 H  HD13 . ILE   B 1 487 ? 13.099 9.381   62.240 1.00 19.83 ? 487  ILE   B HD13 1 
ATOM   16888 N  N    . ASP   B 1 488 ? 18.491 8.607   64.054 1.00 14.91 ? 488  ASP   B N    1 
ATOM   16889 C  CA   . ASP   B 1 488 ? 19.858 9.160   64.177 1.00 12.76 ? 488  ASP   B CA   1 
ATOM   16890 C  C    . ASP   B 1 488 ? 20.879 8.048   63.932 1.00 14.95 ? 488  ASP   B C    1 
ATOM   16891 O  O    . ASP   B 1 488 ? 21.846 8.291   63.202 1.00 14.63 ? 488  ASP   B O    1 
ATOM   16892 C  CB   . ASP   B 1 488 ? 20.094 9.727   65.577 1.00 12.45 ? 488  ASP   B CB   1 
ATOM   16893 C  CG   . ASP   B 1 488 ? 19.711 11.189  65.733 1.00 13.59 ? 488  ASP   B CG   1 
ATOM   16894 O  OD1  . ASP   B 1 488 ? 19.486 11.849  64.704 1.00 13.49 ? 488  ASP   B OD1  1 
ATOM   16895 O  OD2  . ASP   B 1 488 ? 19.648 11.654  66.885 1.00 13.93 ? 488  ASP   B OD2  1 
ATOM   16896 H  H    . ASP   B 1 488 ? 17.978 8.755   64.728 1.00 17.90 ? 488  ASP   B H    1 
ATOM   16897 H  HA   . ASP   B 1 488 ? 19.957 9.870   63.523 1.00 15.32 ? 488  ASP   B HA   1 
ATOM   16898 H  HB2  . ASP   B 1 488 ? 19.589 9.201   66.217 1.00 14.94 ? 488  ASP   B HB2  1 
ATOM   16899 H  HB3  . ASP   B 1 488 ? 21.032 9.623   65.802 1.00 14.94 ? 488  ASP   B HB3  1 
ATOM   16900 N  N    . SER   B 1 489 ? 20.644 6.871   64.518 1.00 15.35 ? 489  SER   B N    1 
ATOM   16901 C  CA   . SER   B 1 489 ? 21.655 5.783   64.444 1.00 13.66 ? 489  SER   B CA   1 
ATOM   16902 C  C    . SER   B 1 489 ? 21.692 5.128   63.056 1.00 13.76 ? 489  SER   B C    1 
ATOM   16903 O  O    . SER   B 1 489 ? 22.723 4.538   62.722 1.00 15.04 ? 489  SER   B O    1 
ATOM   16904 C  CB   . SER   B 1 489 ? 21.416 4.775   65.545 1.00 16.38 ? 489  SER   B CB   1 
ATOM   16905 O  OG   . SER   B 1 489 ? 21.510 5.389   66.820 1.00 14.73 ? 489  SER   B OG   1 
ATOM   16906 H  H    . SER   B 1 489 ? 19.929 6.675   64.954 1.00 18.42 ? 489  SER   B H    1 
ATOM   16907 H  HA   . SER   B 1 489 ? 22.533 6.173   64.580 1.00 16.40 ? 489  SER   B HA   1 
ATOM   16908 H  HB2  . SER   B 1 489 ? 20.539 4.375   65.438 1.00 19.66 ? 489  SER   B HB2  1 
ATOM   16909 H  HB3  . SER   B 1 489 ? 22.065 4.057   65.478 1.00 19.66 ? 489  SER   B HB3  1 
ATOM   16910 H  HG   . SER   B 1 489 ? 20.771 5.735   67.020 1.00 17.67 ? 489  SER   B HG   1 
ATOM   16911 N  N    . LEU   B 1 490 ? 20.617 5.256   62.279 1.00 13.78 ? 490  LEU   B N    1 
ATOM   16912 C  CA   . LEU   B 1 490 ? 20.559 4.645   60.924 1.00 17.70 ? 490  LEU   B CA   1 
ATOM   16913 C  C    . LEU   B 1 490 ? 21.386 5.467   59.933 1.00 15.58 ? 490  LEU   B C    1 
ATOM   16914 O  O    . LEU   B 1 490 ? 21.941 4.873   59.003 1.00 14.55 ? 490  LEU   B O    1 
ATOM   16915 C  CB   . LEU   B 1 490 ? 19.104 4.618   60.454 1.00 16.56 ? 490  LEU   B CB   1 
ATOM   16916 C  CG   . LEU   B 1 490 ? 18.199 3.577   61.107 1.00 16.82 ? 490  LEU   B CG   1 
ATOM   16917 C  CD1  . LEU   B 1 490 ? 16.756 3.785   60.675 1.00 18.04 ? 490  LEU   B CD1  1 
ATOM   16918 C  CD2  . LEU   B 1 490 ? 18.659 2.171   60.761 1.00 16.28 ? 490  LEU   B CD2  1 
ATOM   16919 H  H    . LEU   B 1 490 ? 19.909 5.688   62.505 1.00 16.54 ? 490  LEU   B H    1 
ATOM   16920 H  HA   . LEU   B 1 490 ? 20.919 3.745   60.967 1.00 21.25 ? 490  LEU   B HA   1 
ATOM   16921 H  HB2  . LEU   B 1 490 ? 18.719 5.495   60.607 1.00 19.88 ? 490  LEU   B HB2  1 
ATOM   16922 H  HB3  . LEU   B 1 490 ? 19.097 4.469   59.496 1.00 19.88 ? 490  LEU   B HB3  1 
ATOM   16923 H  HG   . LEU   B 1 490 ? 18.253 3.686   62.069 1.00 20.19 ? 490  LEU   B HG   1 
ATOM   16924 H  HD11 . LEU   B 1 490 ? 16.192 3.118   61.097 1.00 21.66 ? 490  LEU   B HD11 1 
ATOM   16925 H  HD12 . LEU   B 1 490 ? 16.463 4.670   60.941 1.00 21.66 ? 490  LEU   B HD12 1 
ATOM   16926 H  HD13 . LEU   B 1 490 ? 16.691 3.700   59.711 1.00 21.66 ? 490  LEU   B HD13 1 
ATOM   16927 H  HD21 . LEU   B 1 490 ? 18.072 1.525   61.185 1.00 19.54 ? 490  LEU   B HD21 1 
ATOM   16928 H  HD22 . LEU   B 1 490 ? 18.633 2.049   59.799 1.00 19.54 ? 490  LEU   B HD22 1 
ATOM   16929 H  HD23 . LEU   B 1 490 ? 19.566 2.040   61.078 1.00 19.54 ? 490  LEU   B HD23 1 
ATOM   16930 N  N    . GLY   B 1 491 ? 21.439 6.785   60.117 1.00 16.34 ? 491  GLY   B N    1 
ATOM   16931 C  CA   . GLY   B 1 491 ? 22.122 7.650   59.136 1.00 16.57 ? 491  GLY   B CA   1 
ATOM   16932 C  C    . GLY   B 1 491 ? 21.106 8.325   58.228 1.00 15.66 ? 491  GLY   B C    1 
ATOM   16933 O  O    . GLY   B 1 491 ? 21.481 8.718   57.115 1.00 16.43 ? 491  GLY   B O    1 
ATOM   16934 H  H    . GLY   B 1 491 ? 21.095 7.198   60.788 1.00 19.61 ? 491  GLY   B H    1 
ATOM   16935 H  HA2  . GLY   B 1 491 ? 22.648 8.321   59.598 1.00 19.88 ? 491  GLY   B HA2  1 
ATOM   16936 H  HA3  . GLY   B 1 491 ? 22.739 7.123   58.605 1.00 19.88 ? 491  GLY   B HA3  1 
ATOM   16937 N  N    . LEU   B 1 492 ? 19.859 8.441   58.696 1.00 15.18 ? 492  LEU   B N    1 
ATOM   16938 C  CA   . LEU   B 1 492 ? 18.788 9.088   57.895 1.00 13.82 ? 492  LEU   B CA   1 
ATOM   16939 C  C    . LEU   B 1 492 ? 18.339 10.398  58.550 1.00 14.08 ? 492  LEU   B C    1 
ATOM   16940 O  O    . LEU   B 1 492 ? 18.809 10.702  59.657 1.00 14.67 ? 492  LEU   B O    1 
ATOM   16941 C  CB   . LEU   B 1 492 ? 17.601 8.131   57.779 1.00 14.88 ? 492  LEU   B CB   1 
ATOM   16942 C  CG   . LEU   B 1 492 ? 17.878 6.824   57.040 1.00 18.96 ? 492  LEU   B CG   1 
ATOM   16943 C  CD1  . LEU   B 1 492 ? 16.591 6.040   56.845 1.00 19.07 ? 492  LEU   B CD1  1 
ATOM   16944 C  CD2  . LEU   B 1 492 ? 18.548 7.091   55.701 1.00 17.84 ? 492  LEU   B CD2  1 
ATOM   16945 H  H    . LEU   B 1 492 ? 19.606 8.157   59.467 1.00 18.21 ? 492  LEU   B H    1 
ATOM   16946 H  HA   . LEU   B 1 492 ? 19.133 9.292   57.012 1.00 16.59 ? 492  LEU   B HA   1 
ATOM   16947 H  HB2  . LEU   B 1 492 ? 17.289 7.919   58.672 1.00 17.86 ? 492  LEU   B HB2  1 
ATOM   16948 H  HB3  . LEU   B 1 492 ? 16.877 8.592   57.327 1.00 17.86 ? 492  LEU   B HB3  1 
ATOM   16949 H  HG   . LEU   B 1 492 ? 18.484 6.293   57.580 1.00 22.75 ? 492  LEU   B HG   1 
ATOM   16950 H  HD11 . LEU   B 1 492 ? 16.783 5.214   56.375 1.00 22.89 ? 492  LEU   B HD11 1 
ATOM   16951 H  HD12 . LEU   B 1 492 ? 16.202 5.836   57.710 1.00 22.89 ? 492  LEU   B HD12 1 
ATOM   16952 H  HD13 . LEU   B 1 492 ? 15.965 6.569   56.326 1.00 22.89 ? 492  LEU   B HD13 1 
ATOM   16953 H  HD21 . LEU   B 1 492 ? 18.715 6.249   55.249 1.00 21.42 ? 492  LEU   B HD21 1 
ATOM   16954 H  HD22 . LEU   B 1 492 ? 17.968 7.643   55.153 1.00 21.42 ? 492  LEU   B HD22 1 
ATOM   16955 H  HD23 . LEU   B 1 492 ? 19.389 7.552   55.846 1.00 21.42 ? 492  LEU   B HD23 1 
ATOM   16956 N  N    . CYS   B 1 493 ? 17.434 11.114  57.880 1.00 13.52 ? 493  CYS   B N    1 
ATOM   16957 C  CA   . CYS   B 1 493 ? 16.975 12.432  58.387 1.00 15.51 ? 493  CYS   B CA   1 
ATOM   16958 C  C    . CYS   B 1 493 ? 15.694 12.278  59.210 1.00 12.34 ? 493  CYS   B C    1 
ATOM   16959 O  O    . CYS   B 1 493 ? 14.816 11.520  58.789 1.00 14.97 ? 493  CYS   B O    1 
ATOM   16960 C  CB   . CYS   B 1 493 ? 16.706 13.380  57.231 1.00 15.24 ? 493  CYS   B CB   1 
ATOM   16961 S  SG   . CYS   B 1 493 ? 16.275 15.050  57.784 1.00 13.81 ? 493  CYS   B SG   1 
ATOM   16962 H  H    . CYS   B 1 493 ? 17.072 10.867  57.140 1.00 16.23 ? 493  CYS   B H    1 
ATOM   16963 H  HA   . CYS   B 1 493 ? 17.677 12.795  58.949 1.00 18.62 ? 493  CYS   B HA   1 
ATOM   16964 H  HB2  . CYS   B 1 493 ? 17.492 13.424  56.664 1.00 18.30 ? 493  CYS   B HB2  1 
ATOM   16965 H  HB3  . CYS   B 1 493 ? 15.984 13.026  56.689 1.00 18.30 ? 493  CYS   B HB3  1 
ATOM   16966 N  N    . ILE   B 1 494 ? 15.604 13.006  60.324 1.00 13.76 ? 494  ILE   B N    1 
ATOM   16967 C  CA   . ILE   B 1 494 ? 14.414 12.948  61.220 1.00 14.50 ? 494  ILE   B CA   1 
ATOM   16968 C  C    . ILE   B 1 494 ? 13.169 13.428  60.466 1.00 16.25 ? 494  ILE   B C    1 
ATOM   16969 O  O    . ILE   B 1 494 ? 12.070 13.017  60.840 1.00 15.60 ? 494  ILE   B O    1 
ATOM   16970 C  CB   . ILE   B 1 494 ? 14.678 13.793  62.482 1.00 14.31 ? 494  ILE   B CB   1 
ATOM   16971 C  CG1  . ILE   B 1 494 ? 13.622 13.543  63.562 1.00 12.05 ? 494  ILE   B CG1  1 
ATOM   16972 C  CG2  . ILE   B 1 494 ? 14.796 15.269  62.135 1.00 14.50 ? 494  ILE   B CG2  1 
ATOM   16973 C  CD1  . ILE   B 1 494 ? 13.545 12.104  64.012 1.00 15.43 ? 494  ILE   B CD1  1 
ATOM   16974 H  H    . ILE   B 1 494 ? 16.218 13.546  60.590 1.00 16.52 ? 494  ILE   B H    1 
ATOM   16975 H  HA   . ILE   B 1 494 ? 14.254 12.033  61.499 1.00 17.40 ? 494  ILE   B HA   1 
ATOM   16976 H  HB   . ILE   B 1 494 ? 15.529 13.512  62.853 1.00 17.17 ? 494  ILE   B HB   1 
ATOM   16977 H  HG12 . ILE   B 1 494 ? 13.816 14.104  64.329 1.00 14.47 ? 494  ILE   B HG12 1 
ATOM   16978 H  HG13 . ILE   B 1 494 ? 12.754 13.815  63.224 1.00 14.47 ? 494  ILE   B HG13 1 
ATOM   16979 H  HG21 . ILE   B 1 494 ? 14.962 15.779  62.943 1.00 17.40 ? 494  ILE   B HG21 1 
ATOM   16980 H  HG22 . ILE   B 1 494 ? 15.531 15.398  61.515 1.00 17.40 ? 494  ILE   B HG22 1 
ATOM   16981 H  HG23 . ILE   B 1 494 ? 13.971 15.572  61.725 1.00 17.40 ? 494  ILE   B HG23 1 
ATOM   16982 H  HD11 . ILE   B 1 494 ? 12.860 12.014  64.693 1.00 18.52 ? 494  ILE   B HD11 1 
ATOM   16983 H  HD12 . ILE   B 1 494 ? 13.323 11.539  63.255 1.00 18.52 ? 494  ILE   B HD12 1 
ATOM   16984 H  HD13 . ILE   B 1 494 ? 14.402 11.833  64.377 1.00 18.52 ? 494  ILE   B HD13 1 
ATOM   16985 N  N    . PHE   B 1 495 ? 13.352 14.254  59.434 1.00 16.54 ? 495  PHE   B N    1 
ATOM   16986 C  CA   . PHE   B 1 495 ? 12.193 14.825  58.698 1.00 15.11 ? 495  PHE   B CA   1 
ATOM   16987 C  C    . PHE   B 1 495 ? 11.473 13.736  57.892 1.00 15.05 ? 495  PHE   B C    1 
ATOM   16988 O  O    . PHE   B 1 495 ? 10.402 14.021  57.348 1.00 15.15 ? 495  PHE   B O    1 
ATOM   16989 C  CB   . PHE   B 1 495 ? 12.629 16.018  57.842 1.00 15.31 ? 495  PHE   B CB   1 
ATOM   16990 C  CG   . PHE   B 1 495 ? 13.061 17.221  58.641 1.00 14.74 ? 495  PHE   B CG   1 
ATOM   16991 C  CD1  . PHE   B 1 495 ? 12.496 17.490  59.876 1.00 18.17 ? 495  PHE   B CD1  1 
ATOM   16992 C  CD2  . PHE   B 1 495 ? 14.036 18.080  58.162 1.00 16.07 ? 495  PHE   B CD2  1 
ATOM   16993 C  CE1  . PHE   B 1 495 ? 12.894 18.594  60.613 1.00 15.87 ? 495  PHE   B CE1  1 
ATOM   16994 C  CE2  . PHE   B 1 495 ? 14.434 19.183  58.900 1.00 13.18 ? 495  PHE   B CE2  1 
ATOM   16995 C  CZ   . PHE   B 1 495 ? 13.861 19.438  60.122 1.00 15.44 ? 495  PHE   B CZ   1 
ATOM   16996 H  H    . PHE   B 1 495 ? 14.122 14.500  59.140 1.00 19.85 ? 495  PHE   B H    1 
ATOM   16997 H  HA   . PHE   B 1 495 ? 11.548 15.166  59.337 1.00 18.14 ? 495  PHE   B HA   1 
ATOM   16998 H  HB2  . PHE   B 1 495 ? 13.361 15.742  57.269 1.00 18.37 ? 495  PHE   B HB2  1 
ATOM   16999 H  HB3  . PHE   B 1 495 ? 11.895 16.273  57.262 1.00 18.37 ? 495  PHE   B HB3  1 
ATOM   17000 H  HD1  . PHE   B 1 495 ? 11.841 16.923  60.215 1.00 21.80 ? 495  PHE   B HD1  1 
ATOM   17001 H  HD2  . PHE   B 1 495 ? 14.428 17.915  57.335 1.00 19.29 ? 495  PHE   B HD2  1 
ATOM   17002 H  HE1  . PHE   B 1 495 ? 12.506 18.764  61.441 1.00 19.05 ? 495  PHE   B HE1  1 
ATOM   17003 H  HE2  . PHE   B 1 495 ? 15.090 19.752  58.567 1.00 15.82 ? 495  PHE   B HE2  1 
ATOM   17004 H  HZ   . PHE   B 1 495 ? 14.127 20.180  60.616 1.00 18.53 ? 495  PHE   B HZ   1 
ATOM   17005 N  N    . THR   B 1 496 ? 12.037 12.525  57.832 1.00 17.94 ? 496  THR   B N    1 
ATOM   17006 C  CA   . THR   B 1 496 ? 11.321 11.398  57.173 1.00 17.05 ? 496  THR   B CA   1 
ATOM   17007 C  C    . THR   B 1 496 ? 10.118 10.994  58.031 1.00 18.12 ? 496  THR   B C    1 
ATOM   17008 O  O    . THR   B 1 496 ? 9.269  10.247  57.531 1.00 18.82 ? 496  THR   B O    1 
ATOM   17009 C  CB   . THR   B 1 496 ? 12.243 10.194  56.944 1.00 17.88 ? 496  THR   B CB   1 
ATOM   17010 O  OG1  . THR   B 1 496 ? 12.860 9.843   58.183 1.00 16.75 ? 496  THR   B OG1  1 
ATOM   17011 C  CG2  . THR   B 1 496 ? 13.304 10.463  55.900 1.00 16.72 ? 496  THR   B CG2  1 
ATOM   17012 H  H    . THR   B 1 496 ? 12.810 12.328  58.153 1.00 21.54 ? 496  THR   B H    1 
ATOM   17013 H  HA   . THR   B 1 496 ? 11.018 11.696  56.301 1.00 20.47 ? 496  THR   B HA   1 
ATOM   17014 H  HB   . THR   B 1 496 ? 11.700 9.463   56.611 1.00 21.46 ? 496  THR   B HB   1 
ATOM   17015 H  HG1  . THR   B 1 496 ? 13.586 10.258  58.262 1.00 20.11 ? 496  THR   B HG1  1 
ATOM   17016 H  HG21 . THR   B 1 496 ? 13.859 9.675   55.792 1.00 20.06 ? 496  THR   B HG21 1 
ATOM   17017 H  HG22 . THR   B 1 496 ? 12.879 10.677  55.055 1.00 20.06 ? 496  THR   B HG22 1 
ATOM   17018 H  HG23 . THR   B 1 496 ? 13.855 11.210  56.183 1.00 20.06 ? 496  THR   B HG23 1 
ATOM   17019 N  N    . THR   B 1 497 ? 10.055 11.482  59.274 1.00 18.17 ? 497  THR   B N    1 
ATOM   17020 C  CA   . THR   B 1 497 ? 8.894  11.185  60.157 1.00 19.06 ? 497  THR   B CA   1 
ATOM   17021 C  C    . THR   B 1 497 ? 7.630  11.814  59.567 1.00 18.25 ? 497  THR   B C    1 
ATOM   17022 O  O    . THR   B 1 497 ? 6.535  11.453  60.014 1.00 19.47 ? 497  THR   B O    1 
ATOM   17023 C  CB   . THR   B 1 497 ? 9.124  11.679  61.589 1.00 19.88 ? 497  THR   B CB   1 
ATOM   17024 O  OG1  . THR   B 1 497 ? 9.551  13.039  61.538 1.00 19.26 ? 497  THR   B OG1  1 
ATOM   17025 C  CG2  . THR   B 1 497 ? 10.145 10.844  62.330 1.00 20.36 ? 497  THR   B CG2  1 
ATOM   17026 H  H    . THR   B 1 497 ? 10.659 11.980  59.630 1.00 21.81 ? 497  THR   B H    1 
ATOM   17027 H  HA   . THR   B 1 497 ? 8.787  10.222  60.203 1.00 22.87 ? 497  THR   B HA   1 
ATOM   17028 H  HB   . THR   B 1 497 ? 8.289  11.599  62.076 1.00 23.86 ? 497  THR   B HB   1 
ATOM   17029 H  HG1  . THR   B 1 497 ? 10.390 13.069  61.507 1.00 23.12 ? 497  THR   B HG1  1 
ATOM   17030 H  HG21 . THR   B 1 497 ? 10.258 11.192  63.228 1.00 24.43 ? 497  THR   B HG21 1 
ATOM   17031 H  HG22 . THR   B 1 497 ? 9.839  9.925   62.376 1.00 24.43 ? 497  THR   B HG22 1 
ATOM   17032 H  HG23 . THR   B 1 497 ? 10.994 10.879  61.861 1.00 24.43 ? 497  THR   B HG23 1 
ATOM   17033 N  N    . PHE   B 1 498 ? 7.790  12.721  58.610 1.00 20.28 ? 498  PHE   B N    1 
ATOM   17034 C  CA   . PHE   B 1 498 ? 6.602  13.291  57.926 1.00 19.35 ? 498  PHE   B CA   1 
ATOM   17035 C  C    . PHE   B 1 498 ? 6.139  12.289  56.865 1.00 19.41 ? 498  PHE   B C    1 
ATOM   17036 O  O    . PHE   B 1 498 ? 6.226  12.590  55.666 1.00 19.44 ? 498  PHE   B O    1 
ATOM   17037 C  CB   . PHE   B 1 498 ? 6.919  14.683  57.378 1.00 20.49 ? 498  PHE   B CB   1 
ATOM   17038 C  CG   . PHE   B 1 498 ? 7.177  15.699  58.459 1.00 16.39 ? 498  PHE   B CG   1 
ATOM   17039 C  CD1  . PHE   B 1 498 ? 6.201  15.989  59.397 1.00 17.62 ? 498  PHE   B CD1  1 
ATOM   17040 C  CD2  . PHE   B 1 498 ? 8.399  16.341  58.557 1.00 19.10 ? 498  PHE   B CD2  1 
ATOM   17041 C  CE1  . PHE   B 1 498 ? 6.435  16.915  60.400 1.00 19.53 ? 498  PHE   B CE1  1 
ATOM   17042 C  CE2  . PHE   B 1 498 ? 8.633  17.266  59.562 1.00 19.81 ? 498  PHE   B CE2  1 
ATOM   17043 C  CZ   . PHE   B 1 498 ? 7.651  17.552  60.480 1.00 19.45 ? 498  PHE   B CZ   1 
ATOM   17044 H  H    . PHE   B 1 498 ? 8.549  13.021  58.339 1.00 24.34 ? 498  PHE   B H    1 
ATOM   17045 H  HA   . PHE   B 1 498 ? 5.866  13.425  58.543 1.00 23.23 ? 498  PHE   B HA   1 
ATOM   17046 H  HB2  . PHE   B 1 498 ? 7.697  14.628  56.801 1.00 24.60 ? 498  PHE   B HB2  1 
ATOM   17047 H  HB3  . PHE   B 1 498 ? 6.179  14.985  56.828 1.00 24.60 ? 498  PHE   B HB3  1 
ATOM   17048 H  HD1  . PHE   B 1 498 ? 5.379  15.557  59.353 1.00 21.14 ? 498  PHE   B HD1  1 
ATOM   17049 H  HD2  . PHE   B 1 498 ? 9.070  16.150  57.942 1.00 22.92 ? 498  PHE   B HD2  1 
ATOM   17050 H  HE1  . PHE   B 1 498 ? 5.769  17.106  61.020 1.00 23.44 ? 498  PHE   B HE1  1 
ATOM   17051 H  HE2  . PHE   B 1 498 ? 9.457  17.694  59.615 1.00 23.78 ? 498  PHE   B HE2  1 
ATOM   17052 H  HZ   . PHE   B 1 498 ? 7.808  18.174  61.153 1.00 23.34 ? 498  PHE   B HZ   1 
ATOM   17053 N  N    . GLY   B 1 499 ? 5.679  11.121  57.320 1.00 21.92 ? 499  GLY   B N    1 
ATOM   17054 C  CA   . GLY   B 1 499 ? 5.200  10.085  56.389 1.00 20.87 ? 499  GLY   B CA   1 
ATOM   17055 C  C    . GLY   B 1 499 ? 5.674  8.694   56.772 1.00 22.75 ? 499  GLY   B C    1 
ATOM   17056 O  O    . GLY   B 1 499 ? 4.935  7.733   56.488 1.00 23.72 ? 499  GLY   B O    1 
ATOM   17057 H  H    . GLY   B 1 499 ? 5.635  10.907  58.152 1.00 26.31 ? 499  GLY   B H    1 
ATOM   17058 H  HA2  . GLY   B 1 499 ? 4.230  10.098  56.366 1.00 25.05 ? 499  GLY   B HA2  1 
ATOM   17059 H  HA3  . GLY   B 1 499 ? 5.507  10.293  55.493 1.00 25.05 ? 499  GLY   B HA3  1 
ATOM   17060 N  N    . LEU   B 1 500 ? 6.851  8.574   57.391 1.00 18.74 ? 500  LEU   B N    1 
ATOM   17061 C  CA   . LEU   B 1 500 ? 7.404  7.219   57.665 1.00 19.51 ? 500  LEU   B CA   1 
ATOM   17062 C  C    . LEU   B 1 500 ? 7.292  6.856   59.148 1.00 20.26 ? 500  LEU   B C    1 
ATOM   17063 O  O    . LEU   B 1 500 ? 7.318  7.772   59.988 1.00 21.18 ? 500  LEU   B O    1 
ATOM   17064 C  CB   . LEU   B 1 500 ? 8.865  7.163   57.210 1.00 21.06 ? 500  LEU   B CB   1 
ATOM   17065 C  CG   . LEU   B 1 500 ? 9.108  7.404   55.722 1.00 18.49 ? 500  LEU   B CG   1 
ATOM   17066 C  CD1  . LEU   B 1 500 ? 10.530 7.020   55.344 1.00 19.58 ? 500  LEU   B CD1  1 
ATOM   17067 C  CD2  . LEU   B 1 500 ? 8.106  6.638   54.872 1.00 17.14 ? 500  LEU   B CD2  1 
ATOM   17068 H  H    . LEU   B 1 500 ? 7.338  9.231   57.656 1.00 22.49 ? 500  LEU   B H    1 
ATOM   17069 H  HA   . LEU   B 1 500 ? 6.884  6.569   57.167 1.00 23.41 ? 500  LEU   B HA   1 
ATOM   17070 H  HB2  . LEU   B 1 500 ? 9.368  7.822   57.713 1.00 25.28 ? 500  LEU   B HB2  1 
ATOM   17071 H  HB3  . LEU   B 1 500 ? 9.225  6.293   57.442 1.00 25.28 ? 500  LEU   B HB3  1 
ATOM   17072 H  HG   . LEU   B 1 500 ? 8.987  8.351   55.549 1.00 22.19 ? 500  LEU   B HG   1 
ATOM   17073 H  HD11 . LEU   B 1 500 ? 10.667 7.179   54.397 1.00 23.50 ? 500  LEU   B HD11 1 
ATOM   17074 H  HD12 . LEU   B 1 500 ? 11.157 7.555   55.856 1.00 23.50 ? 500  LEU   B HD12 1 
ATOM   17075 H  HD13 . LEU   B 1 500 ? 10.674 6.081   55.538 1.00 23.50 ? 500  LEU   B HD13 1 
ATOM   17076 H  HD21 . LEU   B 1 500 ? 8.281  6.808   53.933 1.00 20.57 ? 500  LEU   B HD21 1 
ATOM   17077 H  HD22 . LEU   B 1 500 ? 8.190  5.688   55.050 1.00 20.57 ? 500  LEU   B HD22 1 
ATOM   17078 H  HD23 . LEU   B 1 500 ? 7.207  6.929   55.090 1.00 20.57 ? 500  LEU   B HD23 1 
ATOM   17079 N  N    . GLY   B 1 501 ? 7.188  5.559   59.438 1.00 25.27 ? 501  GLY   B N    1 
ATOM   17080 C  CA   . GLY   B 1 501 ? 7.133  5.075   60.829 1.00 23.22 ? 501  GLY   B CA   1 
ATOM   17081 C  C    . GLY   B 1 501 ? 8.125  3.948   61.056 1.00 23.08 ? 501  GLY   B C    1 
ATOM   17082 O  O    . GLY   B 1 501 ? 8.838  3.602   60.103 1.00 22.29 ? 501  GLY   B O    1 
ATOM   17083 H  H    . GLY   B 1 501 ? 7.147  4.937   58.845 1.00 30.33 ? 501  GLY   B H    1 
ATOM   17084 H  HA2  . GLY   B 1 501 ? 7.325  5.806   61.437 1.00 27.87 ? 501  GLY   B HA2  1 
ATOM   17085 H  HA3  . GLY   B 1 501 ? 6.236  4.766   61.032 1.00 27.87 ? 501  GLY   B HA3  1 
ATOM   17086 N  N    . ILE   B 1 502 ? 8.146  3.379   62.259 1.00 19.86 ? 502  ILE   B N    1 
ATOM   17087 C  CA   . ILE   B 1 502 ? 9.153  2.339   62.626 1.00 21.62 ? 502  ILE   B CA   1 
ATOM   17088 C  C    . ILE   B 1 502 ? 9.243  1.236   61.560 1.00 22.24 ? 502  ILE   B C    1 
ATOM   17089 O  O    . ILE   B 1 502 ? 10.373 0.836   61.242 1.00 24.75 ? 502  ILE   B O    1 
ATOM   17090 C  CB   . ILE   B 1 502 ? 8.834  1.774   64.024 1.00 21.08 ? 502  ILE   B CB   1 
ATOM   17091 C  CG1  . ILE   B 1 502 ? 9.901  0.781   64.492 1.00 25.63 ? 502  ILE   B CG1  1 
ATOM   17092 C  CG2  . ILE   B 1 502 ? 7.438  1.171   64.061 1.00 22.49 ? 502  ILE   B CG2  1 
ATOM   17093 C  CD1  . ILE   B 1 502 ? 11.282 1.379   64.621 1.00 23.14 ? 502  ILE   B CD1  1 
ATOM   17094 H  H    . ILE   B 1 502 ? 7.592  3.571   62.888 1.00 23.84 ? 502  ILE   B H    1 
ATOM   17095 H  HA   . ILE   B 1 502 ? 10.030 2.753   62.661 1.00 25.95 ? 502  ILE   B HA   1 
ATOM   17096 H  HB   . ILE   B 1 502 ? 8.849  2.513   64.652 1.00 25.31 ? 502  ILE   B HB   1 
ATOM   17097 H  HG12 . ILE   B 1 502 ? 9.635  0.416   65.350 1.00 30.76 ? 502  ILE   B HG12 1 
ATOM   17098 H  HG13 . ILE   B 1 502 ? 9.936  0.040   63.867 1.00 30.76 ? 502  ILE   B HG13 1 
ATOM   17099 H  HG21 . ILE   B 1 502 ? 7.259  0.822   64.948 1.00 27.00 ? 502  ILE   B HG21 1 
ATOM   17100 H  HG22 . ILE   B 1 502 ? 6.784  1.854   63.845 1.00 27.00 ? 502  ILE   B HG22 1 
ATOM   17101 H  HG23 . ILE   B 1 502 ? 7.379  0.451   63.413 1.00 27.00 ? 502  ILE   B HG23 1 
ATOM   17102 H  HD11 . ILE   B 1 502 ? 11.904 0.697   64.920 1.00 27.77 ? 502  ILE   B HD11 1 
ATOM   17103 H  HD12 . ILE   B 1 502 ? 11.568 1.722   63.760 1.00 27.77 ? 502  ILE   B HD12 1 
ATOM   17104 H  HD13 . ILE   B 1 502 ? 11.262 2.103   65.266 1.00 27.77 ? 502  ILE   B HD13 1 
ATOM   17105 N  N    . GLN   B 1 503 ? 8.113  0.759   61.037 1.00 22.39 ? 503  GLN   B N    1 
ATOM   17106 C  CA   . GLN   B 1 503 ? 8.180  -0.388  60.088 1.00 22.35 ? 503  GLN   B CA   1 
ATOM   17107 C  C    . GLN   B 1 503 ? 8.935  0.033   58.822 1.00 21.98 ? 503  GLN   B C    1 
ATOM   17108 O  O    . GLN   B 1 503 ? 9.684  -0.790  58.283 1.00 22.98 ? 503  GLN   B O    1 
ATOM   17109 C  CB   . GLN   B 1 503 ? 6.782  -0.907  59.751 1.00 22.66 ? 503  GLN   B CB   1 
ATOM   17110 C  CG   . GLN   B 1 503 ? 6.796  -2.124  58.838 1.00 23.33 ? 503  GLN   B CG   1 
ATOM   17111 C  CD   . GLN   B 1 503 ? 7.599  -3.257  59.427 1.00 27.96 ? 503  GLN   B CD   1 
ATOM   17112 O  OE1  . GLN   B 1 503 ? 7.383  -3.668  60.564 1.00 29.83 ? 503  GLN   B OE1  1 
ATOM   17113 N  NE2  . GLN   B 1 503 ? 8.539  -3.771  58.652 1.00 26.46 ? 503  GLN   B NE2  1 
ATOM   17114 H  H    . GLN   B 1 503 ? 7.324  1.060   61.201 1.00 26.87 ? 503  GLN   B H    1 
ATOM   17115 H  HA   . GLN   B 1 503 ? 8.662  -1.116  60.511 1.00 26.82 ? 503  GLN   B HA   1 
ATOM   17116 H  HB2  . GLN   B 1 503 ? 6.321  -1.133  60.574 1.00 27.20 ? 503  GLN   B HB2  1 
ATOM   17117 H  HB3  . GLN   B 1 503 ? 6.274  -0.198  59.327 1.00 27.20 ? 503  GLN   B HB3  1 
ATOM   17118 H  HG2  . GLN   B 1 503 ? 5.886  -2.420  58.680 1.00 28.00 ? 503  GLN   B HG2  1 
ATOM   17119 H  HG3  . GLN   B 1 503 ? 7.168  -1.878  57.976 1.00 28.00 ? 503  GLN   B HG3  1 
ATOM   17120 H  HE21 . GLN   B 1 503 ? 8.662  -3.458  57.861 1.00 31.75 ? 503  GLN   B HE21 1 
ATOM   17121 H  HE22 . GLN   B 1 503 ? 9.027  -4.418  58.939 1.00 31.75 ? 503  GLN   B HE22 1 
ATOM   17122 N  N    . ASP   B 1 504 ? 8.745  1.276   58.387 1.00 22.62 ? 504  ASP   B N    1 
ATOM   17123 C  CA   . ASP   B 1 504 ? 9.436  1.786   57.176 1.00 23.76 ? 504  ASP   B CA   1 
ATOM   17124 C  C    . ASP   B 1 504 ? 10.950 1.720   57.402 1.00 21.94 ? 504  ASP   B C    1 
ATOM   17125 O  O    . ASP   B 1 504 ? 11.680 1.364   56.465 1.00 22.89 ? 504  ASP   B O    1 
ATOM   17126 C  CB   . ASP   B 1 504 ? 8.949  3.199   56.854 1.00 21.93 ? 504  ASP   B CB   1 
ATOM   17127 C  CG   . ASP   B 1 504 ? 7.454  3.252   56.603 1.00 22.83 ? 504  ASP   B CG   1 
ATOM   17128 O  OD1  . ASP   B 1 504 ? 7.013  2.672   55.595 1.00 24.26 ? 504  ASP   B OD1  1 
ATOM   17129 O  OD2  . ASP   B 1 504 ? 6.745  3.860   57.423 1.00 22.02 ? 504  ASP   B OD2  1 
ATOM   17130 H  H    . ASP   B 1 504 ? 8.226  1.846   58.768 1.00 27.15 ? 504  ASP   B H    1 
ATOM   17131 H  HA   . ASP   B 1 504 ? 9.227  1.235   56.405 1.00 28.51 ? 504  ASP   B HA   1 
ATOM   17132 H  HB2  . ASP   B 1 504 ? 9.172  3.791   57.589 1.00 26.32 ? 504  ASP   B HB2  1 
ATOM   17133 H  HB3  . ASP   B 1 504 ? 9.418  3.530   56.072 1.00 26.32 ? 504  ASP   B HB3  1 
ATOM   17134 N  N    . TYR   B 1 505 ? 11.393 2.073   58.606 1.00 22.47 ? 505  TYR   B N    1 
ATOM   17135 C  CA   . TYR   B 1 505 ? 12.843 2.064   58.921 1.00 19.34 ? 505  TYR   B CA   1 
ATOM   17136 C  C    . TYR   B 1 505 ? 13.333 0.612   58.951 1.00 20.14 ? 505  TYR   B C    1 
ATOM   17137 O  O    . TYR   B 1 505 ? 14.460 0.342   58.515 1.00 19.97 ? 505  TYR   B O    1 
ATOM   17138 C  CB   . TYR   B 1 505 ? 13.079 2.845   60.217 1.00 18.41 ? 505  TYR   B CB   1 
ATOM   17139 C  CG   . TYR   B 1 505 ? 12.632 4.283   60.127 1.00 17.10 ? 505  TYR   B CG   1 
ATOM   17140 C  CD1  . TYR   B 1 505 ? 13.242 5.164   59.250 1.00 18.29 ? 505  TYR   B CD1  1 
ATOM   17141 C  CD2  . TYR   B 1 505 ? 11.583 4.758   60.894 1.00 18.42 ? 505  TYR   B CD2  1 
ATOM   17142 C  CE1  . TYR   B 1 505 ? 12.831 6.482   59.145 1.00 14.84 ? 505  TYR   B CE1  1 
ATOM   17143 C  CE2  . TYR   B 1 505 ? 11.157 6.073   60.801 1.00 19.74 ? 505  TYR   B CE2  1 
ATOM   17144 C  CZ   . TYR   B 1 505 ? 11.785 6.939   59.924 1.00 17.66 ? 505  TYR   B CZ   1 
ATOM   17145 O  OH   . TYR   B 1 505 ? 11.374 8.246   59.825 1.00 19.44 ? 505  TYR   B OH   1 
ATOM   17146 H  H    . TYR   B 1 505 ? 10.886 2.320   59.255 1.00 26.97 ? 505  TYR   B H    1 
ATOM   17147 H  HA   . TYR   B 1 505 ? 13.368 2.513   58.240 1.00 23.21 ? 505  TYR   B HA   1 
ATOM   17148 H  HB2  . TYR   B 1 505 ? 12.605 2.409   60.943 1.00 22.09 ? 505  TYR   B HB2  1 
ATOM   17149 H  HB3  . TYR   B 1 505 ? 14.023 2.818   60.438 1.00 22.09 ? 505  TYR   B HB3  1 
ATOM   17150 H  HD1  . TYR   B 1 505 ? 13.944 4.863   58.719 1.00 21.95 ? 505  TYR   B HD1  1 
ATOM   17151 H  HD2  . TYR   B 1 505 ? 11.154 4.182   61.485 1.00 22.11 ? 505  TYR   B HD2  1 
ATOM   17152 H  HE1  . TYR   B 1 505 ? 13.257 7.058   58.552 1.00 17.82 ? 505  TYR   B HE1  1 
ATOM   17153 H  HE2  . TYR   B 1 505 ? 10.451 6.373   61.327 1.00 23.69 ? 505  TYR   B HE2  1 
ATOM   17154 H  HH   . TYR   B 1 505 ? 11.889 8.663   59.309 1.00 23.34 ? 505  TYR   B HH   1 
ATOM   17155 N  N    . VAL   B 1 506 ? 12.491 -0.284  59.465 1.00 23.16 ? 506  VAL   B N    1 
ATOM   17156 C  CA   . VAL   B 1 506 ? 12.845 -1.731  59.481 1.00 20.47 ? 506  VAL   B CA   1 
ATOM   17157 C  C    . VAL   B 1 506 ? 13.005 -2.192  58.030 1.00 23.49 ? 506  VAL   B C    1 
ATOM   17158 O  O    . VAL   B 1 506 ? 14.002 -2.869  57.731 1.00 25.10 ? 506  VAL   B O    1 
ATOM   17159 C  CB   . VAL   B 1 506 ? 11.758 -2.542  60.208 1.00 25.22 ? 506  VAL   B CB   1 
ATOM   17160 C  CG1  . VAL   B 1 506 ? 11.977 -4.040  60.055 1.00 22.60 ? 506  VAL   B CG1  1 
ATOM   17161 C  CG2  . VAL   B 1 506 ? 11.662 -2.164  61.677 1.00 22.98 ? 506  VAL   B CG2  1 
ATOM   17162 H  H    . VAL   B 1 506 ? 11.724 -0.094  59.805 1.00 27.80 ? 506  VAL   B H    1 
ATOM   17163 H  HA   . VAL   B 1 506 ? 13.675 -1.873  59.962 1.00 24.56 ? 506  VAL   B HA   1 
ATOM   17164 H  HB   . VAL   B 1 506 ? 10.914 -2.318  59.786 1.00 30.27 ? 506  VAL   B HB   1 
ATOM   17165 H  HG11 . VAL   B 1 506 ? 11.276 -4.519  60.524 1.00 27.12 ? 506  VAL   B HG11 1 
ATOM   17166 H  HG12 . VAL   B 1 506 ? 11.956 -4.276  59.114 1.00 27.12 ? 506  VAL   B HG12 1 
ATOM   17167 H  HG13 . VAL   B 1 506 ? 12.839 -4.281  60.429 1.00 27.12 ? 506  VAL   B HG13 1 
ATOM   17168 H  HG21 . VAL   B 1 506 ? 10.969 -2.693  62.103 1.00 27.58 ? 506  VAL   B HG21 1 
ATOM   17169 H  HG22 . VAL   B 1 506 ? 12.512 -2.335  62.112 1.00 27.58 ? 506  VAL   B HG22 1 
ATOM   17170 H  HG23 . VAL   B 1 506 ? 11.443 -1.222  61.755 1.00 27.58 ? 506  VAL   B HG23 1 
ATOM   17171 N  N    . ASP   B 1 507 ? 12.053 -1.824  57.174 1.00 23.18 ? 507  ASP   B N    1 
ATOM   17172 C  CA   . ASP   B 1 507 ? 12.107 -2.230  55.745 1.00 23.61 ? 507  ASP   B CA   1 
ATOM   17173 C  C    . ASP   B 1 507 ? 13.457 -1.825  55.143 1.00 22.84 ? 507  ASP   B C    1 
ATOM   17174 O  O    . ASP   B 1 507 ? 14.126 -2.690  54.551 1.00 22.28 ? 507  ASP   B O    1 
ATOM   17175 C  CB   . ASP   B 1 507 ? 10.926 -1.644  54.968 1.00 25.28 ? 507  ASP   B CB   1 
ATOM   17176 C  CG   . ASP   B 1 507 ? 9.577  -2.126  55.466 1.00 26.21 ? 507  ASP   B CG   1 
ATOM   17177 O  OD1  . ASP   B 1 507 ? 9.538  -3.201  56.091 1.00 27.43 ? 507  ASP   B OD1  1 
ATOM   17178 O  OD2  . ASP   B 1 507 ? 8.579  -1.421  55.226 1.00 25.03 ? 507  ASP   B OD2  1 
ATOM   17179 H  H    . ASP   B 1 507 ? 11.371 -1.345  57.386 1.00 27.82 ? 507  ASP   B H    1 
ATOM   17180 H  HA   . ASP   B 1 507 ? 12.031 -3.195  55.681 1.00 28.33 ? 507  ASP   B HA   1 
ATOM   17181 H  HB2  . ASP   B 1 507 ? 10.958 -0.676  55.026 1.00 30.34 ? 507  ASP   B HB2  1 
ATOM   17182 H  HB3  . ASP   B 1 507 ? 11.018 -1.875  54.030 1.00 30.34 ? 507  ASP   B HB3  1 
ATOM   17183 N  N    . MET   B 1 508 ? 13.850 -0.560  55.313 1.00 21.78 ? 508  MET   B N    1 
ATOM   17184 C  CA   . MET   B 1 508 ? 15.110 -0.063  54.701 1.00 20.68 ? 508  MET   B CA   1 
ATOM   17185 C  C    . MET   B 1 508 ? 16.334 -0.748  55.334 1.00 18.52 ? 508  MET   B C    1 
ATOM   17186 O  O    . MET   B 1 508 ? 17.215 -1.195  54.586 1.00 22.83 ? 508  MET   B O    1 
ATOM   17187 C  CB   . MET   B 1 508 ? 15.202 1.460   54.845 1.00 21.59 ? 508  MET   B CB   1 
ATOM   17188 C  CG   . MET   B 1 508 ? 14.128 2.187   54.057 1.00 21.71 ? 508  MET   B CG   1 
ATOM   17189 S  SD   . MET   B 1 508 ? 14.245 3.992   54.159 1.00 21.66 ? 508  MET   B SD   1 
ATOM   17190 C  CE   . MET   B 1 508 ? 13.432 4.283   55.730 1.00 16.92 ? 508  MET   B CE   1 
ATOM   17191 H  H    . MET   B 1 508 ? 13.416 0.025   55.770 1.00 26.15 ? 508  MET   B H    1 
ATOM   17192 H  HA   . MET   B 1 508 ? 15.102 -0.284  53.756 1.00 24.82 ? 508  MET   B HA   1 
ATOM   17193 H  HB2  . MET   B 1 508 ? 15.127 1.698   55.782 1.00 25.91 ? 508  MET   B HB2  1 
ATOM   17194 H  HB3  . MET   B 1 508 ? 16.075 1.758   54.546 1.00 25.91 ? 508  MET   B HB3  1 
ATOM   17195 H  HG2  . MET   B 1 508 ? 14.184 1.919   53.126 1.00 26.06 ? 508  MET   B HG2  1 
ATOM   17196 H  HG3  . MET   B 1 508 ? 13.257 1.909   54.380 1.00 26.06 ? 508  MET   B HG3  1 
ATOM   17197 H  HE1  . MET   B 1 508 ? 13.422 5.235   55.918 1.00 20.31 ? 508  MET   B HE1  1 
ATOM   17198 H  HE2  . MET   B 1 508 ? 12.521 3.952   55.689 1.00 20.31 ? 508  MET   B HE2  1 
ATOM   17199 H  HE3  . MET   B 1 508 ? 13.913 3.820   56.434 1.00 20.31 ? 508  MET   B HE3  1 
ATOM   17200 N  N    . TYR   B 1 509 ? 16.390 -0.816  56.665 1.00 20.19 ? 509  TYR   B N    1 
ATOM   17201 C  CA   . TYR   B 1 509 ? 17.565 -1.416  57.347 1.00 21.63 ? 509  TYR   B CA   1 
ATOM   17202 C  C    . TYR   B 1 509 ? 17.759 -2.863  56.878 1.00 21.25 ? 509  TYR   B C    1 
ATOM   17203 O  O    . TYR   B 1 509 ? 18.884 -3.219  56.498 1.00 23.26 ? 509  TYR   B O    1 
ATOM   17204 C  CB   . TYR   B 1 509 ? 17.388 -1.404  58.867 1.00 21.46 ? 509  TYR   B CB   1 
ATOM   17205 C  CG   . TYR   B 1 509 ? 18.544 -1.997  59.629 1.00 21.53 ? 509  TYR   B CG   1 
ATOM   17206 C  CD1  . TYR   B 1 509 ? 18.587 -3.347  59.931 1.00 21.62 ? 509  TYR   B CD1  1 
ATOM   17207 C  CD2  . TYR   B 1 509 ? 19.605 -1.208  60.040 1.00 22.52 ? 509  TYR   B CD2  1 
ATOM   17208 C  CE1  . TYR   B 1 509 ? 19.651 -3.898  60.623 1.00 21.02 ? 509  TYR   B CE1  1 
ATOM   17209 C  CE2  . TYR   B 1 509 ? 20.675 -1.742  60.737 1.00 23.23 ? 509  TYR   B CE2  1 
ATOM   17210 C  CZ   . TYR   B 1 509 ? 20.699 -3.093  61.030 1.00 20.15 ? 509  TYR   B CZ   1 
ATOM   17211 O  OH   . TYR   B 1 509 ? 21.759 -3.624  61.720 1.00 20.94 ? 509  TYR   B OH   1 
ATOM   17212 H  H    . TYR   B 1 509 ? 15.774 -0.529  57.192 1.00 24.23 ? 509  TYR   B H    1 
ATOM   17213 H  HA   . TYR   B 1 509 ? 18.344 -0.885  57.119 1.00 25.96 ? 509  TYR   B HA   1 
ATOM   17214 H  HB2  . TYR   B 1 509 ? 17.257 -0.489  59.160 1.00 25.76 ? 509  TYR   B HB2  1 
ATOM   17215 H  HB3  . TYR   B 1 509 ? 16.581 -1.893  59.092 1.00 25.76 ? 509  TYR   B HB3  1 
ATOM   17216 H  HD1  . TYR   B 1 509 ? 17.886 -3.896  59.663 1.00 25.95 ? 509  TYR   B HD1  1 
ATOM   17217 H  HD2  . TYR   B 1 509 ? 19.599 -0.299  59.843 1.00 27.03 ? 509  TYR   B HD2  1 
ATOM   17218 H  HE1  . TYR   B 1 509 ? 19.661 -4.808  60.814 1.00 25.23 ? 509  TYR   B HE1  1 
ATOM   17219 H  HE2  . TYR   B 1 509 ? 21.376 -1.194  61.007 1.00 27.88 ? 509  TYR   B HE2  1 
ATOM   17220 H  HH   . TYR   B 1 509 ? 22.358 -3.042  61.805 1.00 25.13 ? 509  TYR   B HH   1 
ATOM   17221 N  N    . ASN   B 1 510 ? 16.691 -3.659  56.904 1.00 23.59 ? 510  ASN   B N    1 
ATOM   17222 C  CA   . ASN   B 1 510 ? 16.813 -5.108  56.574 1.00 23.12 ? 510  ASN   B CA   1 
ATOM   17223 C  C    . ASN   B 1 510 ? 17.188 -5.300  55.098 1.00 25.09 ? 510  ASN   B C    1 
ATOM   17224 O  O    . ASN   B 1 510 ? 18.001 -6.194  54.809 1.00 25.20 ? 510  ASN   B O    1 
ATOM   17225 C  CB   . ASN   B 1 510 ? 15.543 -5.870  56.959 1.00 22.90 ? 510  ASN   B CB   1 
ATOM   17226 C  CG   . ASN   B 1 510 ? 15.456 -6.153  58.444 1.00 26.15 ? 510  ASN   B CG   1 
ATOM   17227 O  OD1  . ASN   B 1 510 ? 16.424 -5.962  59.177 1.00 24.27 ? 510  ASN   B OD1  1 
ATOM   17228 N  ND2  . ASN   B 1 510 ? 14.301 -6.609  58.897 1.00 25.70 ? 510  ASN   B ND2  1 
ATOM   17229 H  H    . ASN   B 1 510 ? 15.896 -3.400  57.104 1.00 28.31 ? 510  ASN   B H    1 
ATOM   17230 H  HA   . ASN   B 1 510 ? 17.534 -5.485  57.102 1.00 27.75 ? 510  ASN   B HA   1 
ATOM   17231 H  HB2  . ASN   B 1 510 ? 14.767 -5.356  56.686 1.00 27.48 ? 510  ASN   B HB2  1 
ATOM   17232 H  HB3  . ASN   B 1 510 ? 15.514 -6.708  56.472 1.00 27.48 ? 510  ASN   B HB3  1 
ATOM   17233 H  HD21 . ASN   B 1 510 ? 14.206 -6.784  59.734 1.00 30.84 ? 510  ASN   B HD21 1 
ATOM   17234 H  HD22 . ASN   B 1 510 ? 13.644 -6.731  58.355 1.00 30.84 ? 510  ASN   B HD22 1 
ATOM   17235 N  N    . ALA   B 1 511 ? 16.619 -4.490  54.208 1.00 22.87 ? 511  ALA   B N    1 
ATOM   17236 C  CA   . ALA   B 1 511 ? 16.957 -4.602  52.771 1.00 24.75 ? 511  ALA   B CA   1 
ATOM   17237 C  C    . ALA   B 1 511 ? 18.454 -4.356  52.574 1.00 25.55 ? 511  ALA   B C    1 
ATOM   17238 O  O    . ALA   B 1 511 ? 19.062 -5.070  51.761 1.00 25.38 ? 511  ALA   B O    1 
ATOM   17239 C  CB   . ALA   B 1 511 ? 16.141 -3.634  51.961 1.00 25.92 ? 511  ALA   B CB   1 
ATOM   17240 H  H    . ALA   B 1 511 ? 16.046 -3.878  54.400 1.00 27.44 ? 511  ALA   B H    1 
ATOM   17241 H  HA   . ALA   B 1 511 ? 16.746 -5.497  52.463 1.00 29.71 ? 511  ALA   B HA   1 
ATOM   17242 H  HB1  . ALA   B 1 511 ? 16.374 -3.720  51.023 1.00 31.11 ? 511  ALA   B HB1  1 
ATOM   17243 H  HB2  . ALA   B 1 511 ? 15.198 -3.828  52.079 1.00 31.11 ? 511  ALA   B HB2  1 
ATOM   17244 H  HB3  . ALA   B 1 511 ? 16.324 -2.729  52.258 1.00 31.11 ? 511  ALA   B HB3  1 
ATOM   17245 N  N    . VAL   B 1 512 ? 19.022 -3.383  53.291 1.00 22.64 ? 512  VAL   B N    1 
ATOM   17246 C  CA   . VAL   B 1 512 ? 20.453 -3.012  53.076 1.00 25.76 ? 512  VAL   B CA   1 
ATOM   17247 C  C    . VAL   B 1 512 ? 21.378 -3.921  53.891 1.00 24.27 ? 512  VAL   B C    1 
ATOM   17248 O  O    . VAL   B 1 512 ? 22.405 -4.344  53.344 1.00 24.01 ? 512  VAL   B O    1 
ATOM   17249 C  CB   . VAL   B 1 512 ? 20.682 -1.534  53.456 1.00 22.45 ? 512  VAL   B CB   1 
ATOM   17250 C  CG1  . VAL   B 1 512 ? 22.157 -1.167  53.469 1.00 24.64 ? 512  VAL   B CG1  1 
ATOM   17251 C  CG2  . VAL   B 1 512 ? 19.897 -0.592  52.558 1.00 25.66 ? 512  VAL   B CG2  1 
ATOM   17252 H  H    . VAL   B 1 512 ? 18.618 -2.926  53.897 1.00 27.17 ? 512  VAL   B H    1 
ATOM   17253 H  HA   . VAL   B 1 512 ? 20.663 -3.130  52.136 1.00 30.92 ? 512  VAL   B HA   1 
ATOM   17254 H  HB   . VAL   B 1 512 ? 20.348 -1.429  54.361 1.00 26.94 ? 512  VAL   B HB   1 
ATOM   17255 H  HG11 . VAL   B 1 512 ? 22.256 -0.233  53.712 1.00 29.57 ? 512  VAL   B HG11 1 
ATOM   17256 H  HG12 . VAL   B 1 512 ? 22.623 -1.720  54.116 1.00 29.57 ? 512  VAL   B HG12 1 
ATOM   17257 H  HG13 . VAL   B 1 512 ? 22.535 -1.313  52.588 1.00 29.57 ? 512  VAL   B HG13 1 
ATOM   17258 H  HG21 . VAL   B 1 512 ? 20.065 0.325   52.825 1.00 30.79 ? 512  VAL   B HG21 1 
ATOM   17259 H  HG22 . VAL   B 1 512 ? 20.175 -0.716  51.637 1.00 30.79 ? 512  VAL   B HG22 1 
ATOM   17260 H  HG23 . VAL   B 1 512 ? 18.949 -0.783  52.638 1.00 30.79 ? 512  VAL   B HG23 1 
ATOM   17261 N  N    . VAL   B 1 513 ? 21.024 -4.214  55.143 1.00 24.27 ? 513  VAL   B N    1 
ATOM   17262 C  CA   . VAL   B 1 513 ? 21.958 -4.964  56.036 1.00 24.25 ? 513  VAL   B CA   1 
ATOM   17263 C  C    . VAL   B 1 513 ? 21.729 -6.477  55.949 1.00 25.75 ? 513  VAL   B C    1 
ATOM   17264 O  O    . VAL   B 1 513 ? 22.725 -7.215  55.977 1.00 23.44 ? 513  VAL   B O    1 
ATOM   17265 C  CB   . VAL   B 1 513 ? 21.813 -4.466  57.487 1.00 20.62 ? 513  VAL   B CB   1 
ATOM   17266 C  CG1  . VAL   B 1 513 ? 22.606 -5.314  58.467 1.00 27.32 ? 513  VAL   B CG1  1 
ATOM   17267 C  CG2  . VAL   B 1 513 ? 22.195 -2.999  57.611 1.00 21.53 ? 513  VAL   B CG2  1 
ATOM   17268 H  H    . VAL   B 1 513 ? 20.272 -4.001  55.501 1.00 29.13 ? 513  VAL   B H    1 
ATOM   17269 H  HA   . VAL   B 1 513 ? 22.865 -4.795  55.736 1.00 29.10 ? 513  VAL   B HA   1 
ATOM   17270 H  HB   . VAL   B 1 513 ? 20.876 -4.556  57.720 1.00 24.75 ? 513  VAL   B HB   1 
ATOM   17271 H  HG11 . VAL   B 1 513 ? 22.487 -4.967  59.365 1.00 32.79 ? 513  VAL   B HG11 1 
ATOM   17272 H  HG12 . VAL   B 1 513 ? 22.291 -6.231  58.431 1.00 32.79 ? 513  VAL   B HG12 1 
ATOM   17273 H  HG13 . VAL   B 1 513 ? 23.547 -5.286  58.232 1.00 32.79 ? 513  VAL   B HG13 1 
ATOM   17274 H  HG21 . VAL   B 1 513 ? 22.094 -2.715  58.533 1.00 25.85 ? 513  VAL   B HG21 1 
ATOM   17275 H  HG22 . VAL   B 1 513 ? 23.118 -2.880  57.336 1.00 25.85 ? 513  VAL   B HG22 1 
ATOM   17276 H  HG23 . VAL   B 1 513 ? 21.617 -2.465  57.043 1.00 25.85 ? 513  VAL   B HG23 1 
ATOM   17277 N  N    . GLY   B 1 514 ? 20.475 -6.911  55.857 1.00 24.51 ? 514  GLY   B N    1 
ATOM   17278 C  CA   . GLY   B 1 514 ? 20.197 -8.358  55.889 1.00 26.92 ? 514  GLY   B CA   1 
ATOM   17279 C  C    . GLY   B 1 514 ? 18.769 -8.654  56.299 1.00 25.66 ? 514  GLY   B C    1 
ATOM   17280 O  O    . GLY   B 1 514 ? 18.293 -8.043  57.270 1.00 24.82 ? 514  GLY   B O    1 
ATOM   17281 H  H    . GLY   B 1 514 ? 19.784 -6.406  55.777 1.00 29.41 ? 514  GLY   B H    1 
ATOM   17282 H  HA2  . GLY   B 1 514 ? 20.366 -8.738  55.013 1.00 32.31 ? 514  GLY   B HA2  1 
ATOM   17283 H  HA3  . GLY   B 1 514 ? 20.806 -8.790  56.508 1.00 32.31 ? 514  GLY   B HA3  1 
ATOM   17284 N  N    . GLU   B 1 515 ? 18.127 -9.597  55.610 1.00 29.03 ? 515  GLU   B N    1 
ATOM   17285 C  CA   . GLU   B 1 515 ? 16.697 -9.899  55.867 1.00 29.90 ? 515  GLU   B CA   1 
ATOM   17286 C  C    . GLU   B 1 515 ? 16.459 -10.277 57.332 1.00 30.80 ? 515  GLU   B C    1 
ATOM   17287 O  O    . GLU   B 1 515 ? 17.296 -11.002 57.892 1.00 31.06 ? 515  GLU   B O    1 
ATOM   17288 C  CB   . GLU   B 1 515 ? 16.243 -11.020 54.931 1.00 37.44 ? 515  GLU   B CB   1 
ATOM   17289 C  CG   . GLU   B 1 515 ? 14.777 -11.374 55.078 1.00 45.20 ? 515  GLU   B CG   1 
ATOM   17290 C  CD   . GLU   B 1 515 ? 14.362 -12.636 54.342 1.00 49.72 ? 515  GLU   B CD   1 
ATOM   17291 O  OE1  . GLU   B 1 515 ? 15.257 -13.400 53.933 1.00 44.82 ? 515  GLU   B OE1  1 
ATOM   17292 O  OE2  . GLU   B 1 515 ? 13.146 -12.848 54.177 1.00 54.41 ? 515  GLU   B OE2  1 
ATOM   17293 H  H    . GLU   B 1 515 ? 18.489 -10.075 54.993 1.00 34.84 ? 515  GLU   B H    1 
ATOM   17294 H  HA   . GLU   B 1 515 ? 16.172 -9.102  55.691 1.00 35.88 ? 515  GLU   B HA   1 
ATOM   17295 H  HB2  . GLU   B 1 515 ? 16.414 -10.755 54.014 1.00 44.94 ? 515  GLU   B HB2  1 
ATOM   17296 H  HB3  . GLU   B 1 515 ? 16.778 -11.811 55.102 1.00 44.94 ? 515  GLU   B HB3  1 
ATOM   17297 H  HG2  . GLU   B 1 515 ? 14.574 -11.480 56.020 1.00 54.24 ? 515  GLU   B HG2  1 
ATOM   17298 H  HG3  . GLU   B 1 515 ? 14.242 -10.633 54.754 1.00 54.24 ? 515  GLU   B HG3  1 
ATOM   17299 N  N    . SER   B 1 516 ? 15.375 -9.769  57.925 1.00 31.25 ? 516  SER   B N    1 
ATOM   17300 C  CA   . SER   B 1 516 ? 14.982 -10.153 59.310 1.00 32.88 ? 516  SER   B CA   1 
ATOM   17301 C  C    . SER   B 1 516 ? 16.067 -9.844  60.349 1.00 30.68 ? 516  SER   B C    1 
ATOM   17302 O  O    . SER   B 1 516 ? 16.010 -10.444 61.432 1.00 32.34 ? 516  SER   B O    1 
ATOM   17303 C  CB   . SER   B 1 516 ? 14.573 -11.608 59.360 1.00 31.44 ? 516  SER   B CB   1 
ATOM   17304 O  OG   . SER   B 1 516 ? 13.844 -11.965 58.197 1.00 39.25 ? 516  SER   B OG   1 
ATOM   17305 H  H    . SER   B 1 516 ? 14.848 -9.201  57.552 1.00 37.50 ? 516  SER   B H    1 
ATOM   17306 H  HA   . SER   B 1 516 ? 14.218 -9.605  59.549 1.00 39.46 ? 516  SER   B HA   1 
ATOM   17307 H  HB2  . SER   B 1 516 ? 15.361 -12.168 59.437 1.00 37.73 ? 516  SER   B HB2  1 
ATOM   17308 H  HB3  . SER   B 1 516 ? 14.032 -11.770 60.149 1.00 37.73 ? 516  SER   B HB3  1 
ATOM   17309 H  HG   . SER   B 1 516 ? 13.626 -12.775 58.240 1.00 47.10 ? 516  SER   B HG   1 
ATOM   17310 N  N    . THR   B 1 517 ? 16.992 -8.926  60.059 1.00 28.82 ? 517  THR   B N    1 
ATOM   17311 C  CA   . THR   B 1 517 ? 17.988 -8.555  61.100 1.00 26.93 ? 517  THR   B CA   1 
ATOM   17312 C  C    . THR   B 1 517 ? 17.245 -7.939  62.291 1.00 29.75 ? 517  THR   B C    1 
ATOM   17313 O  O    . THR   B 1 517 ? 17.546 -8.321  63.435 1.00 27.13 ? 517  THR   B O    1 
ATOM   17314 C  CB   . THR   B 1 517 ? 19.084 -7.633  60.547 1.00 27.58 ? 517  THR   B CB   1 
ATOM   17315 O  OG1  . THR   B 1 517 ? 19.711 -8.288  59.444 1.00 30.53 ? 517  THR   B OG1  1 
ATOM   17316 C  CG2  . THR   B 1 517 ? 20.122 -7.275  61.586 1.00 30.01 ? 517  THR   B CG2  1 
ATOM   17317 H  H    . THR   B 1 517 ? 17.069 -8.517  59.306 1.00 34.59 ? 517  THR   B H    1 
ATOM   17318 H  HA   . THR   B 1 517 ? 18.454 -9.351  61.399 1.00 32.33 ? 517  THR   B HA   1 
ATOM   17319 H  HB   . THR   B 1 517 ? 18.668 -6.802  60.269 1.00 33.10 ? 517  THR   B HB   1 
ATOM   17320 H  HG1  . THR   B 1 517 ? 19.205 -8.256  58.774 1.00 36.64 ? 517  THR   B HG1  1 
ATOM   17321 H  HG21 . THR   B 1 517 ? 20.790 -6.694  61.190 1.00 36.02 ? 517  THR   B HG21 1 
ATOM   17322 H  HG22 . THR   B 1 517 ? 19.694 -6.818  62.327 1.00 36.02 ? 517  THR   B HG22 1 
ATOM   17323 H  HG23 . THR   B 1 517 ? 20.549 -8.084  61.909 1.00 36.02 ? 517  THR   B HG23 1 
ATOM   17324 N  N    . TYR   B 1 518 ? 16.296 -7.043  62.015 1.00 30.37 ? 518  TYR   B N    1 
ATOM   17325 C  CA   . TYR   B 1 518 ? 15.529 -6.376  63.099 1.00 28.61 ? 518  TYR   B CA   1 
ATOM   17326 C  C    . TYR   B 1 518 ? 14.031 -6.442  62.815 1.00 29.33 ? 518  TYR   B C    1 
ATOM   17327 O  O    . TYR   B 1 518 ? 13.657 -6.709  61.660 1.00 27.68 ? 518  TYR   B O    1 
ATOM   17328 C  CB   . TYR   B 1 518 ? 15.901 -4.892  63.201 1.00 27.17 ? 518  TYR   B CB   1 
ATOM   17329 C  CG   . TYR   B 1 518 ? 16.923 -4.549  64.255 1.00 24.27 ? 518  TYR   B CG   1 
ATOM   17330 C  CD1  . TYR   B 1 518 ? 16.609 -4.603  65.602 1.00 23.38 ? 518  TYR   B CD1  1 
ATOM   17331 C  CD2  . TYR   B 1 518 ? 18.202 -4.152  63.904 1.00 25.16 ? 518  TYR   B CD2  1 
ATOM   17332 C  CE1  . TYR   B 1 518 ? 17.541 -4.280  66.574 1.00 23.13 ? 518  TYR   B CE1  1 
ATOM   17333 C  CE2  . TYR   B 1 518 ? 19.147 -3.826  64.862 1.00 24.28 ? 518  TYR   B CE2  1 
ATOM   17334 C  CZ   . TYR   B 1 518 ? 18.815 -3.889  66.203 1.00 23.27 ? 518  TYR   B CZ   1 
ATOM   17335 O  OH   . TYR   B 1 518 ? 19.750 -3.569  67.155 1.00 23.55 ? 518  TYR   B OH   1 
ATOM   17336 H  H    . TYR   B 1 518 ? 16.075 -6.803  61.219 1.00 36.44 ? 518  TYR   B H    1 
ATOM   17337 H  HA   . TYR   B 1 518 ? 15.745 -6.838  63.924 1.00 34.34 ? 518  TYR   B HA   1 
ATOM   17338 H  HB2  . TYR   B 1 518 ? 16.237 -4.599  62.340 1.00 32.61 ? 518  TYR   B HB2  1 
ATOM   17339 H  HB3  . TYR   B 1 518 ? 15.094 -4.384  63.378 1.00 32.61 ? 518  TYR   B HB3  1 
ATOM   17340 H  HD1  . TYR   B 1 518 ? 15.754 -4.862  65.860 1.00 28.06 ? 518  TYR   B HD1  1 
ATOM   17341 H  HD2  . TYR   B 1 518 ? 18.432 -4.103  63.004 1.00 30.19 ? 518  TYR   B HD2  1 
ATOM   17342 H  HE1  . TYR   B 1 518 ? 17.311 -4.326  67.474 1.00 27.76 ? 518  TYR   B HE1  1 
ATOM   17343 H  HE2  . TYR   B 1 518 ? 20.002 -3.566  64.605 1.00 29.14 ? 518  TYR   B HE2  1 
ATOM   17344 H  HH   . TYR   B 1 518 ? 20.513 -3.554  66.804 1.00 28.27 ? 518  TYR   B HH   1 
ATOM   17345 N  N    . ASP   B 1 519 ? 13.208 -6.228  63.843 1.00 29.94 ? 519  ASP   B N    1 
ATOM   17346 C  CA   . ASP   B 1 519 ? 11.742 -6.102  63.629 1.00 27.30 ? 519  ASP   B CA   1 
ATOM   17347 C  C    . ASP   B 1 519 ? 11.313 -4.795  64.314 1.00 27.33 ? 519  ASP   B C    1 
ATOM   17348 O  O    . ASP   B 1 519 ? 12.153 -4.200  65.005 1.00 25.39 ? 519  ASP   B O    1 
ATOM   17349 C  CB   . ASP   B 1 519 ? 10.967 -7.355  64.056 1.00 30.20 ? 519  ASP   B CB   1 
ATOM   17350 C  CG   . ASP   B 1 519 ? 10.916 -7.614  65.552 1.00 33.22 ? 519  ASP   B CG   1 
ATOM   17351 O  OD1  . ASP   B 1 519 ? 11.336 -6.737  66.321 1.00 29.86 ? 519  ASP   B OD1  1 
ATOM   17352 O  OD2  . ASP   B 1 519 ? 10.443 -8.703  65.932 1.00 35.03 ? 519  ASP   B OD2  1 
ATOM   17353 H  H    . ASP   B 1 519 ? 13.462 -6.152  64.661 1.00 35.93 ? 519  ASP   B H    1 
ATOM   17354 H  HA   . ASP   B 1 519 ? 11.523 -6.046  62.686 1.00 32.76 ? 519  ASP   B HA   1 
ATOM   17355 H  HB2  . ASP   B 1 519 ? 10.058 -7.283  63.725 1.00 36.25 ? 519  ASP   B HB2  1 
ATOM   17356 H  HB3  . ASP   B 1 519 ? 11.366 -8.126  63.623 1.00 36.25 ? 519  ASP   B HB3  1 
ATOM   17357 N  N    . ALA   B 1 520 ? 10.076 -4.355  64.101 1.00 25.57 ? 520  ALA   B N    1 
ATOM   17358 C  CA   . ALA   B 1 520 ? 9.634  -3.060  64.666 1.00 26.70 ? 520  ALA   B CA   1 
ATOM   17359 C  C    . ALA   B 1 520 ? 9.930  -3.029  66.169 1.00 24.73 ? 520  ALA   B C    1 
ATOM   17360 O  O    . ALA   B 1 520 ? 10.468 -2.020  66.653 1.00 26.61 ? 520  ALA   B O    1 
ATOM   17361 C  CB   . ALA   B 1 520 ? 8.166  -2.866  64.389 1.00 22.65 ? 520  ALA   B CB   1 
ATOM   17362 H  H    . ALA   B 1 520 ? 9.481  -4.774  63.643 1.00 30.69 ? 520  ALA   B H    1 
ATOM   17363 H  HA   . ALA   B 1 520 ? 10.119 -2.331  64.249 1.00 32.04 ? 520  ALA   B HA   1 
ATOM   17364 H  HB1  . ALA   B 1 520 ? 7.876  -2.018  64.759 1.00 27.18 ? 520  ALA   B HB1  1 
ATOM   17365 H  HB2  . ALA   B 1 520 ? 8.014  -2.869  63.431 1.00 27.18 ? 520  ALA   B HB2  1 
ATOM   17366 H  HB3  . ALA   B 1 520 ? 7.661  -3.586  64.798 1.00 27.18 ? 520  ALA   B HB3  1 
ATOM   17367 N  N    . ASP   B 1 521 ? 9.614  -4.115  66.872 1.00 24.33 ? 521  ASP   B N    1 
ATOM   17368 C  CA   . ASP   B 1 521 ? 9.777  -4.132  68.349 1.00 26.48 ? 521  ASP   B CA   1 
ATOM   17369 C  C    . ASP   B 1 521 ? 11.257 -4.079  68.727 1.00 26.19 ? 521  ASP   B C    1 
ATOM   17370 O  O    . ASP   B 1 521 ? 11.615 -3.257  69.582 1.00 23.39 ? 521  ASP   B O    1 
ATOM   17371 C  CB   . ASP   B 1 521 ? 9.115  -5.371  68.949 1.00 31.39 ? 521  ASP   B CB   1 
ATOM   17372 C  CG   . ASP   B 1 521 ? 7.658  -5.148  69.305 1.00 37.46 ? 521  ASP   B CG   1 
ATOM   17373 O  OD1  . ASP   B 1 521 ? 7.007  -4.343  68.614 1.00 38.68 ? 521  ASP   B OD1  1 
ATOM   17374 O  OD2  . ASP   B 1 521 ? 7.192  -5.779  70.270 1.00 40.34 ? 521  ASP   B OD2  1 
ATOM   17375 H  H    . ASP   B 1 521 ? 9.309  -4.844  66.532 1.00 29.20 ? 521  ASP   B H    1 
ATOM   17376 H  HA   . ASP   B 1 521 ? 9.340  -3.346  68.713 1.00 31.78 ? 521  ASP   B HA   1 
ATOM   17377 H  HB2  . ASP   B 1 521 ? 9.180  -6.105  68.318 1.00 37.67 ? 521  ASP   B HB2  1 
ATOM   17378 H  HB3  . ASP   B 1 521 ? 9.600  -5.638  69.745 1.00 37.67 ? 521  ASP   B HB3  1 
ATOM   17379 N  N    . SER   B 1 522 ? 12.073 -4.942  68.118 1.00 23.13 ? 522  SER   B N    1 
ATOM   17380 C  CA   . SER   B 1 522 ? 13.506 -5.020  68.490 1.00 26.66 ? 522  SER   B CA   1 
ATOM   17381 C  C    . SER   B 1 522 ? 14.220 -3.706  68.145 1.00 22.43 ? 522  SER   B C    1 
ATOM   17382 O  O    . SER   B 1 522 ? 15.120 -3.313  68.900 1.00 22.21 ? 522  SER   B O    1 
ATOM   17383 C  CB   . SER   B 1 522 ? 14.157 -6.216  67.826 1.00 23.64 ? 522  SER   B CB   1 
ATOM   17384 O  OG   . SER   B 1 522 ? 13.874 -6.247  66.438 1.00 24.76 ? 522  SER   B OG   1 
ATOM   17385 H  H    . SER   B 1 522 ? 11.831 -5.485  67.497 1.00 27.76 ? 522  SER   B H    1 
ATOM   17386 H  HA   . SER   B 1 522 ? 13.581 -5.145  69.449 1.00 31.99 ? 522  SER   B HA   1 
ATOM   17387 H  HB2  . SER   B 1 522 ? 15.117 -6.183  67.963 1.00 28.37 ? 522  SER   B HB2  1 
ATOM   17388 H  HB3  . SER   B 1 522 ? 13.840 -7.033  68.242 1.00 28.37 ? 522  SER   B HB3  1 
ATOM   17389 H  HG   . SER   B 1 522 ? 13.090 -6.524  66.318 1.00 29.72 ? 522  SER   B HG   1 
ATOM   17390 N  N    . LEU   B 1 523 ? 13.833 -3.069  67.037 1.00 21.24 ? 523  LEU   B N    1 
ATOM   17391 C  CA   . LEU   B 1 523 ? 14.524 -1.823  66.605 1.00 21.32 ? 523  LEU   B CA   1 
ATOM   17392 C  C    . LEU   B 1 523 ? 14.176 -0.695  67.584 1.00 21.07 ? 523  LEU   B C    1 
ATOM   17393 O  O    . LEU   B 1 523 ? 15.090 0.019   68.016 1.00 19.99 ? 523  LEU   B O    1 
ATOM   17394 C  CB   . LEU   B 1 523 ? 14.100 -1.465  65.176 1.00 19.41 ? 523  LEU   B CB   1 
ATOM   17395 C  CG   . LEU   B 1 523 ? 14.950 -0.395  64.496 1.00 19.88 ? 523  LEU   B CG   1 
ATOM   17396 C  CD1  . LEU   B 1 523 ? 16.421 -0.779  64.526 1.00 20.35 ? 523  LEU   B CD1  1 
ATOM   17397 C  CD2  . LEU   B 1 523 ? 14.483 -0.159  63.068 1.00 21.50 ? 523  LEU   B CD2  1 
ATOM   17398 H  H    . LEU   B 1 523 ? 13.191 -3.325  66.526 1.00 25.49 ? 523  LEU   B H    1 
ATOM   17399 H  HA   . LEU   B 1 523 ? 15.485 -1.954  66.609 1.00 25.59 ? 523  LEU   B HA   1 
ATOM   17400 H  HB2  . LEU   B 1 523 ? 14.125 -2.270  64.635 1.00 23.29 ? 523  LEU   B HB2  1 
ATOM   17401 H  HB3  . LEU   B 1 523 ? 13.178 -1.163  65.193 1.00 23.29 ? 523  LEU   B HB3  1 
ATOM   17402 H  HG   . LEU   B 1 523 ? 14.843 0.434   64.988 1.00 23.86 ? 523  LEU   B HG   1 
ATOM   17403 H  HD11 . LEU   B 1 523 ? 16.945 -0.089  64.090 1.00 24.42 ? 523  LEU   B HD11 1 
ATOM   17404 H  HD12 . LEU   B 1 523 ? 16.712 -0.873  65.446 1.00 24.42 ? 523  LEU   B HD12 1 
ATOM   17405 H  HD13 . LEU   B 1 523 ? 16.545 -1.621  64.061 1.00 24.42 ? 523  LEU   B HD13 1 
ATOM   17406 H  HD21 . LEU   B 1 523 ? 15.035 0.523   62.655 1.00 25.81 ? 523  LEU   B HD21 1 
ATOM   17407 H  HD22 . LEU   B 1 523 ? 14.557 -0.984  62.563 1.00 25.81 ? 523  LEU   B HD22 1 
ATOM   17408 H  HD23 . LEU   B 1 523 ? 13.558 0.134   63.074 1.00 25.81 ? 523  LEU   B HD23 1 
ATOM   17409 N  N    . LEU   B 1 524 ? 12.894 -0.563  67.917 1.00 20.01 ? 524  LEU   B N    1 
ATOM   17410 C  CA   . LEU   B 1 524 ? 12.469 0.491   68.871 1.00 23.36 ? 524  LEU   B CA   1 
ATOM   17411 C  C    . LEU   B 1 524 ? 13.098 0.191   70.233 1.00 19.33 ? 524  LEU   B C    1 
ATOM   17412 O  O    . LEU   B 1 524 ? 13.486 1.141   70.928 1.00 20.59 ? 524  LEU   B O    1 
ATOM   17413 C  CB   . LEU   B 1 524 ? 10.941 0.528   68.933 1.00 26.00 ? 524  LEU   B CB   1 
ATOM   17414 C  CG   . LEU   B 1 524 ? 10.291 1.642   68.116 1.00 29.94 ? 524  LEU   B CG   1 
ATOM   17415 C  CD1  . LEU   B 1 524 ? 8.776  1.579   68.223 1.00 34.01 ? 524  LEU   B CD1  1 
ATOM   17416 C  CD2  . LEU   B 1 524 ? 10.805 3.005   68.556 1.00 27.20 ? 524  LEU   B CD2  1 
ATOM   17417 H  H    . LEU   B 1 524 ? 12.258 -1.057  67.615 1.00 24.01 ? 524  LEU   B H    1 
ATOM   17418 H  HA   . LEU   B 1 524 ? 12.769 1.368   68.585 1.00 28.04 ? 524  LEU   B HA   1 
ATOM   17419 H  HB2  . LEU   B 1 524 ? 10.597 -0.325  68.624 1.00 31.21 ? 524  LEU   B HB2  1 
ATOM   17420 H  HB3  . LEU   B 1 524 ? 10.670 0.624   69.859 1.00 31.21 ? 524  LEU   B HB3  1 
ATOM   17421 H  HG   . LEU   B 1 524 ? 10.533 1.512   67.186 1.00 35.93 ? 524  LEU   B HG   1 
ATOM   17422 H  HD11 . LEU   B 1 524 ? 8.384  2.294   67.698 1.00 40.81 ? 524  LEU   B HD11 1 
ATOM   17423 H  HD12 . LEU   B 1 524 ? 8.463  0.724   67.889 1.00 40.81 ? 524  LEU   B HD12 1 
ATOM   17424 H  HD13 . LEU   B 1 524 ? 8.513  1.679   69.151 1.00 40.81 ? 524  LEU   B HD13 1 
ATOM   17425 H  HD21 . LEU   B 1 524 ? 10.381 3.698   68.026 1.00 32.64 ? 524  LEU   B HD21 1 
ATOM   17426 H  HD22 . LEU   B 1 524 ? 10.597 3.143   69.493 1.00 32.64 ? 524  LEU   B HD22 1 
ATOM   17427 H  HD23 . LEU   B 1 524 ? 11.766 3.045   68.430 1.00 32.64 ? 524  LEU   B HD23 1 
ATOM   17428 N  N    . GLU   B 1 525 ? 13.256 -1.084  70.589 1.00 23.01 ? 525  GLU   B N    1 
ATOM   17429 C  CA   . GLU   B 1 525 ? 13.922 -1.425  71.873 1.00 21.12 ? 525  GLU   B CA   1 
ATOM   17430 C  C    . GLU   B 1 525 ? 15.393 -0.992  71.823 1.00 20.56 ? 525  GLU   B C    1 
ATOM   17431 O  O    . GLU   B 1 525 ? 15.926 -0.588  72.864 1.00 18.97 ? 525  GLU   B O    1 
ATOM   17432 C  CB   . GLU   B 1 525 ? 13.790 -2.922  72.167 1.00 23.87 ? 525  GLU   B CB   1 
ATOM   17433 C  CG   . GLU   B 1 525 ? 14.569 -3.372  73.388 1.00 27.95 ? 525  GLU   B CG   1 
ATOM   17434 C  CD   . GLU   B 1 525 ? 14.302 -4.809  73.800 1.00 31.72 ? 525  GLU   B CD   1 
ATOM   17435 O  OE1  . GLU   B 1 525 ? 14.945 -5.711  73.233 1.00 30.65 ? 525  GLU   B OE1  1 
ATOM   17436 O  OE2  . GLU   B 1 525 ? 13.450 -5.020  74.683 1.00 33.30 ? 525  GLU   B OE2  1 
ATOM   17437 H  H    . GLU   B 1 525 ? 12.996 -1.758  70.123 1.00 27.62 ? 525  GLU   B H    1 
ATOM   17438 H  HA   . GLU   B 1 525 ? 13.486 -0.947  72.596 1.00 25.34 ? 525  GLU   B HA   1 
ATOM   17439 H  HB2  . GLU   B 1 525 ? 12.853 -3.138  72.293 1.00 28.64 ? 525  GLU   B HB2  1 
ATOM   17440 H  HB3  . GLU   B 1 525 ? 14.095 -3.424  71.395 1.00 28.64 ? 525  GLU   B HB3  1 
ATOM   17441 H  HG2  . GLU   B 1 525 ? 15.517 -3.267  73.211 1.00 33.54 ? 525  GLU   B HG2  1 
ATOM   17442 H  HG3  . GLU   B 1 525 ? 14.353 -2.787  74.131 1.00 33.54 ? 525  GLU   B HG3  1 
ATOM   17443 N  N    . ALA   B 1 526 ? 16.014 -1.076  70.642 1.00 18.32 ? 526  ALA   B N    1 
ATOM   17444 C  CA   . ALA   B 1 526 ? 17.426 -0.661  70.501 1.00 17.80 ? 526  ALA   B CA   1 
ATOM   17445 C  C    . ALA   B 1 526 ? 17.521 0.851   70.725 1.00 16.00 ? 526  ALA   B C    1 
ATOM   17446 O  O    . ALA   B 1 526 ? 18.504 1.296   71.321 1.00 17.39 ? 526  ALA   B O    1 
ATOM   17447 C  CB   . ALA   B 1 526 ? 17.959 -1.055  69.150 1.00 19.95 ? 526  ALA   B CB   1 
ATOM   17448 H  H    . ALA   B 1 526 ? 15.648 -1.364  69.919 1.00 21.99 ? 526  ALA   B H    1 
ATOM   17449 H  HA   . ALA   B 1 526 ? 17.971 -1.111  71.165 1.00 21.36 ? 526  ALA   B HA   1 
ATOM   17450 H  HB1  . ALA   B 1 526 ? 18.885 -0.776  69.073 1.00 23.94 ? 526  ALA   B HB1  1 
ATOM   17451 H  HB2  . ALA   B 1 526 ? 17.902 -2.018  69.048 1.00 23.94 ? 526  ALA   B HB2  1 
ATOM   17452 H  HB3  . ALA   B 1 526 ? 17.434 -0.625  68.457 1.00 23.94 ? 526  ALA   B HB3  1 
ATOM   17453 N  N    . GLY   B 1 527 ? 16.525 1.599   70.249 1.00 16.94 ? 527  GLY   B N    1 
ATOM   17454 C  CA   . GLY   B 1 527 ? 16.512 3.050   70.513 1.00 14.98 ? 527  GLY   B CA   1 
ATOM   17455 C  C    . GLY   B 1 527 ? 16.473 3.308   72.008 1.00 16.28 ? 527  GLY   B C    1 
ATOM   17456 O  O    . GLY   B 1 527 ? 17.177 4.213   72.470 1.00 15.49 ? 527  GLY   B O    1 
ATOM   17457 H  H    . GLY   B 1 527 ? 15.864 1.303   69.785 1.00 20.34 ? 527  GLY   B H    1 
ATOM   17458 H  HA2  . GLY   B 1 527 ? 17.300 3.463   70.127 1.00 17.98 ? 527  GLY   B HA2  1 
ATOM   17459 H  HA3  . GLY   B 1 527 ? 15.741 3.456   70.087 1.00 17.98 ? 527  GLY   B HA3  1 
ATOM   17460 N  N    . ASP   B 1 528 ? 15.681 2.515   72.734 1.00 14.79 ? 528  ASP   B N    1 
ATOM   17461 C  CA   . ASP   B 1 528 ? 15.607 2.626   74.212 1.00 17.95 ? 528  ASP   B CA   1 
ATOM   17462 C  C    . ASP   B 1 528 ? 16.988 2.330   74.795 1.00 18.27 ? 528  ASP   B C    1 
ATOM   17463 O  O    . ASP   B 1 528 ? 17.441 3.080   75.667 1.00 17.34 ? 528  ASP   B O    1 
ATOM   17464 C  CB   . ASP   B 1 528 ? 14.537 1.668   74.737 1.00 19.41 ? 528  ASP   B CB   1 
ATOM   17465 C  CG   . ASP   B 1 528 ? 14.192 1.831   76.209 1.00 20.16 ? 528  ASP   B CG   1 
ATOM   17466 O  OD1  . ASP   B 1 528 ? 14.974 2.471   76.933 1.00 17.55 ? 528  ASP   B OD1  1 
ATOM   17467 O  OD2  . ASP   B 1 528 ? 13.141 1.305   76.615 1.00 20.90 ? 528  ASP   B OD2  1 
ATOM   17468 H  H    . ASP   B 1 528 ? 15.176 1.905   72.399 1.00 17.76 ? 528  ASP   B H    1 
ATOM   17469 H  HA   . ASP   B 1 528 ? 15.353 3.522   74.483 1.00 21.55 ? 528  ASP   B HA   1 
ATOM   17470 H  HB2  . ASP   B 1 528 ? 13.729 1.790   74.214 1.00 23.29 ? 528  ASP   B HB2  1 
ATOM   17471 H  HB3  . ASP   B 1 528 ? 14.837 0.758   74.588 1.00 23.29 ? 528  ASP   B HB3  1 
ATOM   17472 N  N    A ARG   B 1 529 ? 17.620 1.256   74.316 0.70 16.35 ? 529  ARG   B N    1 
ATOM   17473 N  N    B ARG   B 1 529 ? 17.633 1.270   74.298 0.30 16.35 ? 529  ARG   B N    1 
ATOM   17474 C  CA   A ARG   B 1 529 ? 18.991 0.910   74.771 0.70 18.94 ? 529  ARG   B CA   1 
ATOM   17475 C  CA   B ARG   B 1 529 ? 18.994 0.903   74.771 0.30 18.94 ? 529  ARG   B CA   1 
ATOM   17476 C  C    A ARG   B 1 529 ? 19.926 2.096   74.521 0.70 17.81 ? 529  ARG   B C    1 
ATOM   17477 C  C    B ARG   B 1 529 ? 19.955 2.067   74.504 0.30 17.81 ? 529  ARG   B C    1 
ATOM   17478 O  O    A ARG   B 1 529 ? 20.730 2.416   75.405 0.70 17.21 ? 529  ARG   B O    1 
ATOM   17479 O  O    B ARG   B 1 529 ? 20.636 2.485   75.459 0.30 17.20 ? 529  ARG   B O    1 
ATOM   17480 C  CB   A ARG   B 1 529 ? 19.494 -0.324  74.016 0.70 21.00 ? 529  ARG   B CB   1 
ATOM   17481 C  CB   B ARG   B 1 529 ? 19.478 -0.368  74.066 0.30 21.00 ? 529  ARG   B CB   1 
ATOM   17482 C  CG   A ARG   B 1 529 ? 21.001 -0.530  74.074 0.70 21.15 ? 529  ARG   B CG   1 
ATOM   17483 C  CG   B ARG   B 1 529 ? 20.990 -0.544  74.068 0.30 21.15 ? 529  ARG   B CG   1 
ATOM   17484 C  CD   A ARG   B 1 529 ? 21.413 -1.912  73.602 0.70 21.59 ? 529  ARG   B CD   1 
ATOM   17485 C  CD   B ARG   B 1 529 ? 21.455 -1.554  73.037 0.30 21.59 ? 529  ARG   B CD   1 
ATOM   17486 N  NE   A ARG   B 1 529 ? 20.940 -2.221  72.262 0.70 27.42 ? 529  ARG   B NE   1 
ATOM   17487 N  NE   B ARG   B 1 529 ? 20.807 -2.847  73.195 0.30 27.42 ? 529  ARG   B NE   1 
ATOM   17488 C  CZ   A ARG   B 1 529 ? 19.982 -3.097  71.982 0.70 20.94 ? 529  ARG   B CZ   1 
ATOM   17489 C  CZ   B ARG   B 1 529 ? 19.872 -3.326  72.383 0.30 20.94 ? 529  ARG   B CZ   1 
ATOM   17490 N  NH1  A ARG   B 1 529 ? 19.259 -3.623  72.955 0.70 24.47 ? 529  ARG   B NH1  1 
ATOM   17491 N  NH1  B ARG   B 1 529 ? 19.991 -3.180  71.076 0.30 24.47 ? 529  ARG   B NH1  1 
ATOM   17492 N  NH2  A ARG   B 1 529 ? 19.747 -3.444  70.730 0.70 20.19 ? 529  ARG   B NH2  1 
ATOM   17493 N  NH2  B ARG   B 1 529 ? 18.820 -3.952  72.882 0.30 20.19 ? 529  ARG   B NH2  1 
ATOM   17494 H  H    A ARG   B 1 529 ? 17.287 0.716   73.735 0.70 19.63 ? 529  ARG   B H    1 
ATOM   17495 H  H    B ARG   B 1 529 ? 17.312 0.750   73.693 0.30 19.63 ? 529  ARG   B H    1 
ATOM   17496 H  HA   A ARG   B 1 529 ? 18.975 0.711   75.720 0.70 22.73 ? 529  ARG   B HA   1 
ATOM   17497 H  HA   B ARG   B 1 529 ? 18.966 0.726   75.724 0.30 22.73 ? 529  ARG   B HA   1 
ATOM   17498 H  HB2  A ARG   B 1 529 ? 19.057 -1.111  74.378 0.70 25.20 ? 529  ARG   B HB2  1 
ATOM   17499 H  HB2  B ARG   B 1 529 ? 19.072 -1.138  74.494 0.30 25.20 ? 529  ARG   B HB2  1 
ATOM   17500 H  HB3  A ARG   B 1 529 ? 19.224 -0.253  73.087 0.70 25.20 ? 529  ARG   B HB3  1 
ATOM   17501 H  HB3  B ARG   B 1 529 ? 19.165 -0.356  73.148 0.30 25.20 ? 529  ARG   B HB3  1 
ATOM   17502 H  HG2  A ARG   B 1 529 ? 21.438 0.140   73.526 0.70 25.38 ? 529  ARG   B HG2  1 
ATOM   17503 H  HG2  B ARG   B 1 529 ? 21.413 0.311   73.893 0.30 25.38 ? 529  ARG   B HG2  1 
ATOM   17504 H  HG3  A ARG   B 1 529 ? 21.309 -0.397  74.984 0.70 25.38 ? 529  ARG   B HG3  1 
ATOM   17505 H  HG3  B ARG   B 1 529 ? 21.279 -0.828  74.949 0.30 25.38 ? 529  ARG   B HG3  1 
ATOM   17506 H  HD2  A ARG   B 1 529 ? 22.380 -1.979  73.621 0.70 25.91 ? 529  ARG   B HD2  1 
ATOM   17507 H  HD2  B ARG   B 1 529 ? 21.274 -1.211  72.148 0.30 25.91 ? 529  ARG   B HD2  1 
ATOM   17508 H  HD3  A ARG   B 1 529 ? 21.070 -2.575  74.221 0.70 25.91 ? 529  ARG   B HD3  1 
ATOM   17509 H  HD3  B ARG   B 1 529 ? 22.416 -1.666  73.108 0.30 25.91 ? 529  ARG   B HD3  1 
ATOM   17510 H  HE   A ARG   B 1 529 ? 21.307 -1.807  71.604 0.70 32.91 ? 529  ARG   B HE   1 
ATOM   17511 H  HE   B ARG   B 1 529 ? 21.046 -3.335  73.861 0.30 32.91 ? 529  ARG   B HE   1 
ATOM   17512 H  HH11 A ARG   B 1 529 ? 19.408 -3.398  73.772 0.70 29.37 ? 529  ARG   B HH11 1 
ATOM   17513 H  HH11 B ARG   B 1 529 ? 20.675 -2.774  70.749 0.30 29.36 ? 529  ARG   B HH11 1 
ATOM   17514 H  HH12 A ARG   B 1 529 ? 18.639 -4.190  72.772 0.70 29.37 ? 529  ARG   B HH12 1 
ATOM   17515 H  HH12 B ARG   B 1 529 ? 19.384 -3.491  70.552 0.30 29.36 ? 529  ARG   B HH12 1 
ATOM   17516 H  HH21 A ARG   B 1 529 ? 20.215 -3.103  70.094 0.70 24.23 ? 529  ARG   B HH21 1 
ATOM   17517 H  HH21 B ARG   B 1 529 ? 18.741 -4.049  73.733 0.30 24.23 ? 529  ARG   B HH21 1 
ATOM   17518 H  HH22 A ARG   B 1 529 ? 19.126 -4.011  70.550 0.70 24.23 ? 529  ARG   B HH22 1 
ATOM   17519 H  HH22 B ARG   B 1 529 ? 18.215 -4.262  72.356 0.30 24.23 ? 529  ARG   B HH22 1 
ATOM   17520 N  N    . ILE   B 1 530 ? 19.797 2.729   73.353 1.00 15.59 ? 530  ILE   B N    1 
ATOM   17521 C  CA   . ILE   B 1 530 ? 20.718 3.847   72.997 1.00 13.60 ? 530  ILE   B CA   1 
ATOM   17522 C  C    . ILE   B 1 530 ? 20.474 5.038   73.935 1.00 14.07 ? 530  ILE   B C    1 
ATOM   17523 O  O    . ILE   B 1 530 ? 21.453 5.585   74.455 1.00 15.90 ? 530  ILE   B O    1 
ATOM   17524 C  CB   . ILE   B 1 530 ? 20.559 4.224   71.511 1.00 15.52 ? 530  ILE   B CB   1 
ATOM   17525 C  CG1  . ILE   B 1 530 ? 21.116 3.126   70.601 1.00 16.48 ? 530  ILE   B CG1  1 
ATOM   17526 C  CG2  . ILE   B 1 530 ? 21.201 5.570   71.222 1.00 17.43 ? 530  ILE   B CG2  1 
ATOM   17527 C  CD1  . ILE   B 1 530 ? 20.516 3.107   69.217 1.00 18.17 ? 530  ILE   B CD1  1 
ATOM   17528 H  H    A ILE   B 1 530 ? 19.204 2.543   72.759 0.70 18.71 ? 530  ILE   B H    1 
ATOM   17529 H  H    B ILE   B 1 530 ? 19.185 2.562   72.772 0.30 18.71 ? 530  ILE   B H    1 
ATOM   17530 H  HA   . ILE   B 1 530 ? 21.638 3.564   73.117 1.00 16.33 ? 530  ILE   B HA   1 
ATOM   17531 H  HB   . ILE   B 1 530 ? 19.611 4.305   71.320 1.00 18.63 ? 530  ILE   B HB   1 
ATOM   17532 H  HG12 . ILE   B 1 530 ? 22.076 3.239   70.525 1.00 19.77 ? 530  ILE   B HG12 1 
ATOM   17533 H  HG13 . ILE   B 1 530 ? 20.964 2.265   71.020 1.00 19.77 ? 530  ILE   B HG13 1 
ATOM   17534 H  HG21 . ILE   B 1 530 ? 21.089 5.787   70.283 1.00 20.92 ? 530  ILE   B HG21 1 
ATOM   17535 H  HG22 . ILE   B 1 530 ? 20.777 6.254   71.764 1.00 20.92 ? 530  ILE   B HG22 1 
ATOM   17536 H  HG23 . ILE   B 1 530 ? 22.147 5.530   71.434 1.00 20.92 ? 530  ILE   B HG23 1 
ATOM   17537 H  HD11 . ILE   B 1 530 ? 20.915 2.389   68.701 1.00 21.81 ? 530  ILE   B HD11 1 
ATOM   17538 H  HD12 . ILE   B 1 530 ? 19.559 2.965   69.281 1.00 21.81 ? 530  ILE   B HD12 1 
ATOM   17539 H  HD13 . ILE   B 1 530 ? 20.688 3.955   68.778 1.00 21.81 ? 530  ILE   B HD13 1 
ATOM   17540 N  N    . TRP   B 1 531 ? 19.209 5.418   74.125 1.00 15.95 ? 531  TRP   B N    1 
ATOM   17541 C  CA   . TRP   B 1 531 ? 18.887 6.550   75.033 1.00 14.45 ? 531  TRP   B CA   1 
ATOM   17542 C  C    . TRP   B 1 531 ? 19.397 6.227   76.439 1.00 14.40 ? 531  TRP   B C    1 
ATOM   17543 O  O    . TRP   B 1 531 ? 19.964 7.117   77.087 1.00 14.19 ? 531  TRP   B O    1 
ATOM   17544 C  CB   . TRP   B 1 531 ? 17.380 6.822   75.032 1.00 15.28 ? 531  TRP   B CB   1 
ATOM   17545 C  CG   . TRP   B 1 531 ? 16.980 7.991   75.876 1.00 15.15 ? 531  TRP   B CG   1 
ATOM   17546 C  CD1  . TRP   B 1 531 ? 16.768 8.003   77.223 1.00 16.81 ? 531  TRP   B CD1  1 
ATOM   17547 C  CD2  . TRP   B 1 531 ? 16.747 9.336   75.423 1.00 13.84 ? 531  TRP   B CD2  1 
ATOM   17548 N  NE1  . TRP   B 1 531 ? 16.418 9.258   77.640 1.00 16.73 ? 531  TRP   B NE1  1 
ATOM   17549 C  CE2  . TRP   B 1 531 ? 16.397 10.098  76.557 1.00 16.46 ? 531  TRP   B CE2  1 
ATOM   17550 C  CE3  . TRP   B 1 531 ? 16.801 9.968   74.177 1.00 14.01 ? 531  TRP   B CE3  1 
ATOM   17551 C  CZ2  . TRP   B 1 531 ? 16.101 11.457  76.477 1.00 15.14 ? 531  TRP   B CZ2  1 
ATOM   17552 C  CZ3  . TRP   B 1 531 ? 16.507 11.310  74.099 1.00 14.30 ? 531  TRP   B CZ3  1 
ATOM   17553 C  CH2  . TRP   B 1 531 ? 16.163 12.043  75.234 1.00 14.20 ? 531  TRP   B CH2  1 
ATOM   17554 H  H    . TRP   B 1 531 ? 18.528 5.049   73.751 1.00 19.15 ? 531  TRP   B H    1 
ATOM   17555 H  HA   . TRP   B 1 531 ? 19.327 7.356   74.721 1.00 17.34 ? 531  TRP   B HA   1 
ATOM   17556 H  HB2  . TRP   B 1 531 ? 17.088 6.976   74.120 1.00 18.33 ? 531  TRP   B HB2  1 
ATOM   17557 H  HB3  . TRP   B 1 531 ? 16.916 6.031   75.348 1.00 18.33 ? 531  TRP   B HB3  1 
ATOM   17558 H  HD1  . TRP   B 1 531 ? 16.850 7.262   77.780 1.00 20.17 ? 531  TRP   B HD1  1 
ATOM   17559 H  HE1  . TRP   B 1 531 ? 16.240 9.483   78.451 1.00 20.07 ? 531  TRP   B HE1  1 
ATOM   17560 H  HE3  . TRP   B 1 531 ? 17.032 9.489   73.414 1.00 16.82 ? 531  TRP   B HE3  1 
ATOM   17561 H  HZ2  . TRP   B 1 531 ? 15.871 11.948  77.233 1.00 18.17 ? 531  TRP   B HZ2  1 
ATOM   17562 H  HZ3  . TRP   B 1 531 ? 16.538 11.736  73.273 1.00 17.16 ? 531  TRP   B HZ3  1 
ATOM   17563 H  HH2  . TRP   B 1 531 ? 15.971 12.949  75.149 1.00 17.04 ? 531  TRP   B HH2  1 
ATOM   17564 N  N    . THR   B 1 532 ? 19.193 4.985   76.872 1.00 14.05 ? 532  THR   B N    1 
ATOM   17565 C  CA   . THR   B 1 532 ? 19.599 4.584   78.244 1.00 15.70 ? 532  THR   B CA   1 
ATOM   17566 C  C    . THR   B 1 532 ? 21.128 4.589   78.342 1.00 15.46 ? 532  THR   B C    1 
ATOM   17567 O  O    . THR   B 1 532 ? 21.646 4.994   79.394 1.00 13.20 ? 532  THR   B O    1 
ATOM   17568 C  CB   . THR   B 1 532 ? 18.943 3.249   78.627 1.00 18.66 ? 532  THR   B CB   1 
ATOM   17569 O  OG1  . THR   B 1 532 ? 17.532 3.368   78.448 1.00 17.86 ? 532  THR   B OG1  1 
ATOM   17570 C  CG2  . THR   B 1 532 ? 19.250 2.833   80.049 1.00 16.23 ? 532  THR   B CG2  1 
ATOM   17571 H  H    . THR   B 1 532 ? 18.829 4.361   76.406 1.00 16.86 ? 532  THR   B H    1 
ATOM   17572 H  HA   . THR   B 1 532 ? 19.279 5.224   78.899 1.00 18.85 ? 532  THR   B HA   1 
ATOM   17573 H  HB   . THR   B 1 532 ? 19.308 2.559   78.051 1.00 22.40 ? 532  THR   B HB   1 
ATOM   17574 H  HG1  . THR   B 1 532 ? 17.346 3.300   77.632 1.00 21.44 ? 532  THR   B HG1  1 
ATOM   17575 H  HG21 . THR   B 1 532 ? 18.814 1.988   80.240 1.00 19.48 ? 532  THR   B HG21 1 
ATOM   17576 H  HG22 . THR   B 1 532 ? 20.209 2.734   80.158 1.00 19.48 ? 532  THR   B HG22 1 
ATOM   17577 H  HG23 . THR   B 1 532 ? 18.924 3.510   80.662 1.00 19.48 ? 532  THR   B HG23 1 
ATOM   17578 N  N    . LEU   B 1 533 ? 21.825 4.199   77.277 1.00 15.74 ? 533  LEU   B N    1 
ATOM   17579 C  CA   . LEU   B 1 533 ? 23.311 4.231   77.299 1.00 15.54 ? 533  LEU   B CA   1 
ATOM   17580 C  C    . LEU   B 1 533 ? 23.789 5.672   77.523 1.00 16.35 ? 533  LEU   B C    1 
ATOM   17581 O  O    . LEU   B 1 533 ? 24.709 5.875   78.325 1.00 15.68 ? 533  LEU   B O    1 
ATOM   17582 C  CB   . LEU   B 1 533 ? 23.837 3.666   75.976 1.00 15.52 ? 533  LEU   B CB   1 
ATOM   17583 C  CG   . LEU   B 1 533 ? 25.358 3.631   75.841 1.00 16.53 ? 533  LEU   B CG   1 
ATOM   17584 C  CD1  . LEU   B 1 533 ? 25.954 2.586   76.769 1.00 19.29 ? 533  LEU   B CD1  1 
ATOM   17585 C  CD2  . LEU   B 1 533 ? 25.766 3.358   74.403 1.00 17.59 ? 533  LEU   B CD2  1 
ATOM   17586 H  H    . LEU   B 1 533 ? 21.478 3.917   76.542 1.00 18.89 ? 533  LEU   B H    1 
ATOM   17587 H  HA   . LEU   B 1 533 ? 23.653 3.687   78.026 1.00 18.66 ? 533  LEU   B HA   1 
ATOM   17588 H  HB2  . LEU   B 1 533 ? 23.497 2.764   75.868 1.00 18.63 ? 533  LEU   B HB2  1 
ATOM   17589 H  HB3  . LEU   B 1 533 ? 23.474 4.195   75.248 1.00 18.63 ? 533  LEU   B HB3  1 
ATOM   17590 H  HG   . LEU   B 1 533 ? 25.703 4.501   76.096 1.00 19.84 ? 533  LEU   B HG   1 
ATOM   17591 H  HD11 . LEU   B 1 533 ? 26.919 2.578   76.670 1.00 23.15 ? 533  LEU   B HD11 1 
ATOM   17592 H  HD12 . LEU   B 1 533 ? 25.725 2.800   77.687 1.00 23.15 ? 533  LEU   B HD12 1 
ATOM   17593 H  HD13 . LEU   B 1 533 ? 25.599 1.712   76.543 1.00 23.15 ? 533  LEU   B HD13 1 
ATOM   17594 H  HD21 . LEU   B 1 533 ? 26.734 3.340   74.339 1.00 21.11 ? 533  LEU   B HD21 1 
ATOM   17595 H  HD22 . LEU   B 1 533 ? 25.408 2.502   74.122 1.00 21.11 ? 533  LEU   B HD22 1 
ATOM   17596 H  HD23 . LEU   B 1 533 ? 25.417 4.058   73.829 1.00 21.11 ? 533  LEU   B HD23 1 
ATOM   17597 N  N    . GLU   B 1 534 ? 23.171 6.629   76.825 1.00 14.11 ? 534  GLU   B N    1 
ATOM   17598 C  CA   . GLU   B 1 534 ? 23.554 8.056   76.971 1.00 15.70 ? 534  GLU   B CA   1 
ATOM   17599 C  C    . GLU   B 1 534 ? 23.289 8.503   78.415 1.00 14.78 ? 534  GLU   B C    1 
ATOM   17600 O  O    . GLU   B 1 534 ? 24.123 9.229   78.975 1.00 15.20 ? 534  GLU   B O    1 
ATOM   17601 C  CB   . GLU   B 1 534 ? 22.770 8.910   75.972 1.00 15.91 ? 534  GLU   B CB   1 
ATOM   17602 C  CG   . GLU   B 1 534 ? 23.073 8.572   74.525 1.00 16.33 ? 534  GLU   B CG   1 
ATOM   17603 C  CD   . GLU   B 1 534 ? 22.142 9.213   73.511 1.00 12.49 ? 534  GLU   B CD   1 
ATOM   17604 O  OE1  . GLU   B 1 534 ? 21.081 9.716   73.919 1.00 15.74 ? 534  GLU   B OE1  1 
ATOM   17605 O  OE2  . GLU   B 1 534 ? 22.484 9.205   72.316 1.00 14.34 ? 534  GLU   B OE2  1 
ATOM   17606 H  H    . GLU   B 1 534 ? 22.534 6.484   76.266 1.00 16.94 ? 534  GLU   B H    1 
ATOM   17607 H  HA   . GLU   B 1 534 ? 24.499 8.168   76.781 1.00 18.85 ? 534  GLU   B HA   1 
ATOM   17608 H  HB2  . GLU   B 1 534 ? 21.820 8.794   76.132 1.00 19.10 ? 534  GLU   B HB2  1 
ATOM   17609 H  HB3  . GLU   B 1 534 ? 22.972 9.846   76.128 1.00 19.10 ? 534  GLU   B HB3  1 
ATOM   17610 H  HG2  . GLU   B 1 534 ? 23.983 8.844   74.327 1.00 19.60 ? 534  GLU   B HG2  1 
ATOM   17611 H  HG3  . GLU   B 1 534 ? 23.035 7.609   74.416 1.00 19.60 ? 534  GLU   B HG3  1 
ATOM   17612 N  N    . LYS   B 1 535 ? 22.154 8.082   78.973 1.00 15.14 ? 535  LYS   B N    1 
ATOM   17613 C  CA   . LYS   B 1 535 ? 21.815 8.453   80.371 1.00 14.49 ? 535  LYS   B CA   1 
ATOM   17614 C  C    . LYS   B 1 535 ? 22.921 7.946   81.303 1.00 17.45 ? 535  LYS   B C    1 
ATOM   17615 O  O    . LYS   B 1 535 ? 23.354 8.707   82.178 1.00 13.33 ? 535  LYS   B O    1 
ATOM   17616 C  CB   . LYS   B 1 535 ? 20.463 7.849   80.755 1.00 16.30 ? 535  LYS   B CB   1 
ATOM   17617 C  CG   . LYS   B 1 535 ? 20.102 7.951   82.230 1.00 17.45 ? 535  LYS   B CG   1 
ATOM   17618 C  CD   . LYS   B 1 535 ? 19.845 9.370   82.680 1.00 14.27 ? 535  LYS   B CD   1 
ATOM   17619 C  CE   . LYS   B 1 535 ? 19.507 9.461   84.152 1.00 16.32 ? 535  LYS   B CE   1 
ATOM   17620 N  NZ   . LYS   B 1 535 ? 19.303 10.860  84.592 1.00 18.84 ? 535  LYS   B NZ   1 
ATOM   17621 H  H    . LYS   B 1 535 ? 21.570 7.590   78.577 1.00 18.17 ? 535  LYS   B H    1 
ATOM   17622 H  HA   . LYS   B 1 535 ? 21.750 9.417   80.452 1.00 17.39 ? 535  LYS   B HA   1 
ATOM   17623 H  HB2  . LYS   B 1 535 ? 19.770 8.287   80.236 1.00 19.57 ? 535  LYS   B HB2  1 
ATOM   17624 H  HB3  . LYS   B 1 535 ? 20.459 6.913   80.500 1.00 19.57 ? 535  LYS   B HB3  1 
ATOM   17625 H  HG2  . LYS   B 1 535 ? 19.312 7.415   82.402 1.00 20.95 ? 535  LYS   B HG2  1 
ATOM   17626 H  HG3  . LYS   B 1 535 ? 20.822 7.574   82.760 1.00 20.95 ? 535  LYS   B HG3  1 
ATOM   17627 H  HD2  . LYS   B 1 535 ? 20.629 9.911   82.498 1.00 17.13 ? 535  LYS   B HD2  1 
ATOM   17628 H  HD3  . LYS   B 1 535 ? 19.116 9.744   82.160 1.00 17.13 ? 535  LYS   B HD3  1 
ATOM   17629 H  HE2  . LYS   B 1 535 ? 18.704 8.947   84.330 1.00 19.59 ? 535  LYS   B HE2  1 
ATOM   17630 H  HE3  . LYS   B 1 535 ? 20.221 9.061   84.672 1.00 19.59 ? 535  LYS   B HE3  1 
ATOM   17631 H  HZ1  . LYS   B 1 535 ? 19.078 10.871  85.453 1.00 22.61 ? 535  LYS   B HZ1  1 
ATOM   17632 H  HZ2  . LYS   B 1 535 ? 20.056 11.321  84.476 1.00 22.61 ? 535  LYS   B HZ2  1 
ATOM   17633 H  HZ3  . LYS   B 1 535 ? 18.652 11.231  84.111 1.00 22.61 ? 535  LYS   B HZ3  1 
ATOM   17634 N  N    . LEU   B 1 536 ? 23.352 6.701   81.096 1.00 18.27 ? 536  LEU   B N    1 
ATOM   17635 C  CA   . LEU   B 1 536 ? 24.407 6.111   81.958 1.00 16.07 ? 536  LEU   B CA   1 
ATOM   17636 C  C    . LEU   B 1 536 ? 25.708 6.901   81.774 1.00 17.28 ? 536  LEU   B C    1 
ATOM   17637 O  O    . LEU   B 1 536 ? 26.394 7.160   82.771 1.00 18.81 ? 536  LEU   B O    1 
ATOM   17638 C  CB   . LEU   B 1 536 ? 24.590 4.638   81.578 1.00 17.78 ? 536  LEU   B CB   1 
ATOM   17639 C  CG   . LEU   B 1 536 ? 23.381 3.740   81.833 1.00 18.51 ? 536  LEU   B CG   1 
ATOM   17640 C  CD1  . LEU   B 1 536 ? 23.590 2.361   81.227 1.00 22.07 ? 536  LEU   B CD1  1 
ATOM   17641 C  CD2  . LEU   B 1 536 ? 23.095 3.629   83.323 1.00 22.05 ? 536  LEU   B CD2  1 
ATOM   17642 H  H    . LEU   B 1 536 ? 23.059 6.182   80.476 1.00 21.93 ? 536  LEU   B H    1 
ATOM   17643 H  HA   . LEU   B 1 536 ? 24.153 6.159   82.893 1.00 19.29 ? 536  LEU   B HA   1 
ATOM   17644 H  HB2  . LEU   B 1 536 ? 24.817 4.589   80.636 1.00 21.34 ? 536  LEU   B HB2  1 
ATOM   17645 H  HB3  . LEU   B 1 536 ? 25.346 4.284   82.071 1.00 21.34 ? 536  LEU   B HB3  1 
ATOM   17646 H  HG   . LEU   B 1 536 ? 22.612 4.147   81.403 1.00 22.21 ? 536  LEU   B HG   1 
ATOM   17647 H  HD11 . LEU   B 1 536 ? 22.811 1.809   81.401 1.00 26.49 ? 536  LEU   B HD11 1 
ATOM   17648 H  HD12 . LEU   B 1 536 ? 23.719 2.444   80.269 1.00 26.49 ? 536  LEU   B HD12 1 
ATOM   17649 H  HD13 . LEU   B 1 536 ? 24.373 1.948   81.624 1.00 26.49 ? 536  LEU   B HD13 1 
ATOM   17650 H  HD21 . LEU   B 1 536 ? 22.325 3.056   83.463 1.00 26.47 ? 536  LEU   B HD21 1 
ATOM   17651 H  HD22 . LEU   B 1 536 ? 23.866 3.250   83.773 1.00 26.47 ? 536  LEU   B HD22 1 
ATOM   17652 H  HD23 . LEU   B 1 536 ? 22.911 4.510   83.684 1.00 26.47 ? 536  LEU   B HD23 1 
ATOM   17653 N  N    . PHE   B 1 537 ? 26.034 7.258   80.531 1.00 15.52 ? 537  PHE   B N    1 
ATOM   17654 C  CA   . PHE   B 1 537 ? 27.236 8.101   80.322 1.00 15.59 ? 537  PHE   B CA   1 
ATOM   17655 C  C    . PHE   B 1 537 ? 27.105 9.384   81.154 1.00 14.70 ? 537  PHE   B C    1 
ATOM   17656 O  O    . PHE   B 1 537 ? 28.067 9.758   81.834 1.00 16.06 ? 537  PHE   B O    1 
ATOM   17657 C  CB   . PHE   B 1 537 ? 27.416 8.416   78.833 1.00 18.55 ? 537  PHE   B CB   1 
ATOM   17658 C  CG   . PHE   B 1 537 ? 28.565 9.341   78.524 1.00 13.50 ? 537  PHE   B CG   1 
ATOM   17659 C  CD1  . PHE   B 1 537 ? 28.437 10.712  78.672 1.00 13.64 ? 537  PHE   B CD1  1 
ATOM   17660 C  CD2  . PHE   B 1 537 ? 29.777 8.838   78.082 1.00 16.30 ? 537  PHE   B CD2  1 
ATOM   17661 C  CE1  . PHE   B 1 537 ? 29.497 11.559  78.393 1.00 16.19 ? 537  PHE   B CE1  1 
ATOM   17662 C  CE2  . PHE   B 1 537 ? 30.836 9.686   77.799 1.00 18.58 ? 537  PHE   B CE2  1 
ATOM   17663 C  CZ   . PHE   B 1 537 ? 30.694 11.044  77.955 1.00 16.19 ? 537  PHE   B CZ   1 
ATOM   17664 H  H    . PHE   B 1 537 ? 25.602 7.040   79.820 1.00 18.63 ? 537  PHE   B H    1 
ATOM   17665 H  HA   . PHE   B 1 537 ? 28.026 7.621   80.615 1.00 18.71 ? 537  PHE   B HA   1 
ATOM   17666 H  HB2  . PHE   B 1 537 ? 27.547 7.584   78.352 1.00 22.26 ? 537  PHE   B HB2  1 
ATOM   17667 H  HB3  . PHE   B 1 537 ? 26.597 8.812   78.497 1.00 22.26 ? 537  PHE   B HB3  1 
ATOM   17668 H  HD1  . PHE   B 1 537 ? 27.629 11.069  78.963 1.00 16.37 ? 537  PHE   B HD1  1 
ATOM   17669 H  HD2  . PHE   B 1 537 ? 29.882 7.920   77.974 1.00 19.56 ? 537  PHE   B HD2  1 
ATOM   17670 H  HE1  . PHE   B 1 537 ? 29.399 12.477  78.502 1.00 19.43 ? 537  PHE   B HE1  1 
ATOM   17671 H  HE2  . PHE   B 1 537 ? 31.645 9.335   77.503 1.00 22.30 ? 537  PHE   B HE2  1 
ATOM   17672 H  HZ   . PHE   B 1 537 ? 31.405 11.612  77.765 1.00 19.43 ? 537  PHE   B HZ   1 
ATOM   17673 N  N    . ASN   B 1 538 ? 25.947 10.043  81.075 1.00 14.37 ? 538  ASN   B N    1 
ATOM   17674 C  CA   . ASN   B 1 538 ? 25.756 11.333  81.790 1.00 16.48 ? 538  ASN   B CA   1 
ATOM   17675 C  C    . ASN   B 1 538 ? 25.891 11.125  83.305 1.00 15.57 ? 538  ASN   B C    1 
ATOM   17676 O  O    . ASN   B 1 538 ? 26.545 11.947  83.960 1.00 16.01 ? 538  ASN   B O    1 
ATOM   17677 C  CB   . ASN   B 1 538 ? 24.409 11.969  81.434 1.00 16.37 ? 538  ASN   B CB   1 
ATOM   17678 C  CG   . ASN   B 1 538 ? 24.443 12.737  80.130 1.00 13.31 ? 538  ASN   B CG   1 
ATOM   17679 O  OD1  . ASN   B 1 538 ? 25.465 12.772  79.450 1.00 13.00 ? 538  ASN   B OD1  1 
ATOM   17680 N  ND2  . ASN   B 1 538 ? 23.330 13.356  79.776 1.00 14.60 ? 538  ASN   B ND2  1 
ATOM   17681 H  H    . ASN   B 1 538 ? 25.265 9.775   80.624 1.00 17.25 ? 538  ASN   B H    1 
ATOM   17682 H  HA   . ASN   B 1 538 ? 26.450 11.948  81.504 1.00 19.78 ? 538  ASN   B HA   1 
ATOM   17683 H  HB2  . ASN   B 1 538 ? 23.734 11.274  81.377 1.00 19.64 ? 538  ASN   B HB2  1 
ATOM   17684 H  HB3  . ASN   B 1 538 ? 24.141 12.567  82.149 1.00 19.64 ? 538  ASN   B HB3  1 
ATOM   17685 H  HD21 . ASN   B 1 538 ? 23.302 13.806  79.044 1.00 17.52 ? 538  ASN   B HD21 1 
ATOM   17686 H  HD22 . ASN   B 1 538 ? 22.633 13.309  80.278 1.00 17.52 ? 538  ASN   B HD22 1 
ATOM   17687 N  N    . LEU   B 1 539 ? 25.270 10.070  83.827 1.00 14.36 ? 539  LEU   B N    1 
ATOM   17688 C  CA   . LEU   B 1 539 ? 25.410 9.770   85.276 1.00 16.33 ? 539  LEU   B CA   1 
ATOM   17689 C  C    . LEU   B 1 539 ? 26.895 9.576   85.601 1.00 17.23 ? 539  LEU   B C    1 
ATOM   17690 O  O    . LEU   B 1 539 ? 27.363 10.138  86.600 1.00 17.68 ? 539  LEU   B O    1 
ATOM   17691 C  CB   . LEU   B 1 539 ? 24.595 8.515   85.599 1.00 18.64 ? 539  LEU   B CB   1 
ATOM   17692 C  CG   . LEU   B 1 539 ? 23.079 8.675   85.498 1.00 19.36 ? 539  LEU   B CG   1 
ATOM   17693 C  CD1  . LEU   B 1 539 ? 22.382 7.324   85.573 1.00 21.52 ? 539  LEU   B CD1  1 
ATOM   17694 C  CD2  . LEU   B 1 539 ? 22.560 9.606   86.583 1.00 19.64 ? 539  LEU   B CD2  1 
ATOM   17695 H  H    . LEU   B 1 539 ? 24.775 9.523   83.385 1.00 17.24 ? 539  LEU   B H    1 
ATOM   17696 H  HA   . LEU   B 1 539 ? 25.074 10.501  85.818 1.00 19.60 ? 539  LEU   B HA   1 
ATOM   17697 H  HB2  . LEU   B 1 539 ? 24.871 7.805   84.998 1.00 22.37 ? 539  LEU   B HB2  1 
ATOM   17698 H  HB3  . LEU   B 1 539 ? 24.816 8.227   86.499 1.00 22.37 ? 539  LEU   B HB3  1 
ATOM   17699 H  HG   . LEU   B 1 539 ? 22.878 9.071   84.636 1.00 23.24 ? 539  LEU   B HG   1 
ATOM   17700 H  HD11 . LEU   B 1 539 ? 21.423 7.451   85.507 1.00 25.83 ? 539  LEU   B HD11 1 
ATOM   17701 H  HD12 . LEU   B 1 539 ? 22.685 6.762   84.842 1.00 25.83 ? 539  LEU   B HD12 1 
ATOM   17702 H  HD13 . LEU   B 1 539 ? 22.594 6.897   86.418 1.00 25.83 ? 539  LEU   B HD13 1 
ATOM   17703 H  HD21 . LEU   B 1 539 ? 21.597 9.694   86.501 1.00 23.57 ? 539  LEU   B HD21 1 
ATOM   17704 H  HD22 . LEU   B 1 539 ? 22.778 9.241   87.455 1.00 23.57 ? 539  LEU   B HD22 1 
ATOM   17705 H  HD23 . LEU   B 1 539 ? 22.973 10.478  86.486 1.00 23.57 ? 539  LEU   B HD23 1 
ATOM   17706 N  N    . ALA   B 1 540 ? 27.599 8.818   84.763 1.00 17.95 ? 540  ALA   B N    1 
ATOM   17707 C  CA   . ALA   B 1 540 ? 29.041 8.573   84.981 1.00 17.32 ? 540  ALA   B CA   1 
ATOM   17708 C  C    . ALA   B 1 540 ? 29.817 9.892   84.923 1.00 18.98 ? 540  ALA   B C    1 
ATOM   17709 O  O    . ALA   B 1 540 ? 30.868 9.983   85.570 1.00 21.96 ? 540  ALA   B O    1 
ATOM   17710 C  CB   . ALA   B 1 540 ? 29.544 7.591   83.953 1.00 17.89 ? 540  ALA   B CB   1 
ATOM   17711 H  H    . ALA   B 1 540 ? 27.272 8.436   84.066 1.00 21.54 ? 540  ALA   B H    1 
ATOM   17712 H  HA   . ALA   B 1 540 ? 29.178 8.191   85.862 1.00 20.79 ? 540  ALA   B HA   1 
ATOM   17713 H  HB1  . ALA   B 1 540 ? 30.490 7.430   84.095 1.00 21.47 ? 540  ALA   B HB1  1 
ATOM   17714 H  HB2  . ALA   B 1 540 ? 29.058 6.756   84.038 1.00 21.47 ? 540  ALA   B HB2  1 
ATOM   17715 H  HB3  . ALA   B 1 540 ? 29.409 7.955   83.064 1.00 21.47 ? 540  ALA   B HB3  1 
ATOM   17716 N  N    . ALA   B 1 541 ? 29.309 10.875  84.175 1.00 18.41 ? 541  ALA   B N    1 
ATOM   17717 C  CA   . ALA   B 1 541 ? 30.041 12.153  84.008 1.00 16.38 ? 541  ALA   B CA   1 
ATOM   17718 C  C    . ALA   B 1 541 ? 29.700 13.136  85.134 1.00 20.27 ? 541  ALA   B C    1 
ATOM   17719 O  O    . ALA   B 1 541 ? 30.274 14.233  85.149 1.00 18.28 ? 541  ALA   B O    1 
ATOM   17720 C  CB   . ALA   B 1 541 ? 29.736 12.753  82.657 1.00 16.22 ? 541  ALA   B CB   1 
ATOM   17721 H  H    . ALA   B 1 541 ? 28.557 10.832  83.760 1.00 22.09 ? 541  ALA   B H    1 
ATOM   17722 H  HA   . ALA   B 1 541 ? 30.992 11.970  84.058 1.00 19.66 ? 541  ALA   B HA   1 
ATOM   17723 H  HB1  . ALA   B 1 541 ? 30.219 13.588  82.557 1.00 19.47 ? 541  ALA   B HB1  1 
ATOM   17724 H  HB2  . ALA   B 1 541 ? 30.009 12.137  81.960 1.00 19.47 ? 541  ALA   B HB2  1 
ATOM   17725 H  HB3  . ALA   B 1 541 ? 28.783 12.920  82.585 1.00 19.47 ? 541  ALA   B HB3  1 
ATOM   17726 N  N    . GLY   B 1 542 ? 28.772 12.756  86.014 1.00 16.99 ? 542  GLY   B N    1 
ATOM   17727 C  CA   . GLY   B 1 542 ? 28.392 13.646  87.129 1.00 17.38 ? 542  GLY   B CA   1 
ATOM   17728 C  C    . GLY   B 1 542 ? 27.159 14.473  86.814 1.00 18.89 ? 542  GLY   B C    1 
ATOM   17729 O  O    . GLY   B 1 542 ? 26.909 15.449  87.532 1.00 19.09 ? 542  GLY   B O    1 
ATOM   17730 H  H    . GLY   B 1 542 ? 28.355 12.004  85.990 1.00 20.40 ? 542  GLY   B H    1 
ATOM   17731 H  HA2  . GLY   B 1 542 ? 28.227 13.114  87.923 1.00 20.86 ? 542  GLY   B HA2  1 
ATOM   17732 H  HA3  . GLY   B 1 542 ? 29.132 14.238  87.333 1.00 20.86 ? 542  GLY   B HA3  1 
ATOM   17733 N  N    . ILE   B 1 543 ? 26.434 14.111  85.755 1.00 15.56 ? 543  ILE   B N    1 
ATOM   17734 C  CA   . ILE   B 1 543 ? 25.153 14.807  85.449 1.00 20.22 ? 543  ILE   B CA   1 
ATOM   17735 C  C    . ILE   B 1 543 ? 24.034 14.089  86.209 1.00 24.33 ? 543  ILE   B C    1 
ATOM   17736 O  O    . ILE   B 1 543 ? 23.576 13.038  85.732 1.00 26.48 ? 543  ILE   B O    1 
ATOM   17737 C  CB   . ILE   B 1 543 ? 24.896 14.862  83.932 1.00 17.58 ? 543  ILE   B CB   1 
ATOM   17738 C  CG1  . ILE   B 1 543 ? 26.097 15.444  83.183 1.00 16.92 ? 543  ILE   B CG1  1 
ATOM   17739 C  CG2  . ILE   B 1 543 ? 23.618 15.631  83.633 1.00 18.72 ? 543  ILE   B CG2  1 
ATOM   17740 C  CD1  . ILE   B 1 543 ? 26.386 16.885  83.527 1.00 17.55 ? 543  ILE   B CD1  1 
ATOM   17741 H  H    . ILE   B 1 543 ? 26.648 13.484  85.207 1.00 18.68 ? 543  ILE   B H    1 
ATOM   17742 H  HA   . ILE   B 1 543 ? 25.192 15.731  85.740 1.00 24.27 ? 543  ILE   B HA   1 
ATOM   17743 H  HB   . ILE   B 1 543 ? 24.777 13.954  83.612 1.00 21.10 ? 543  ILE   B HB   1 
ATOM   17744 H  HG12 . ILE   B 1 543 ? 26.882 14.909  83.381 1.00 20.31 ? 543  ILE   B HG12 1 
ATOM   17745 H  HG13 . ILE   B 1 543 ? 25.938 15.373  82.229 1.00 20.31 ? 543  ILE   B HG13 1 
ATOM   17746 H  HG21 . ILE   B 1 543 ? 23.472 15.656  82.674 1.00 22.47 ? 543  ILE   B HG21 1 
ATOM   17747 H  HG22 . ILE   B 1 543 ? 22.868 15.192  84.063 1.00 22.47 ? 543  ILE   B HG22 1 
ATOM   17748 H  HG23 . ILE   B 1 543 ? 23.699 16.537  83.971 1.00 22.47 ? 543  ILE   B HG23 1 
ATOM   17749 H  HD11 . ILE   B 1 543 ? 27.155 17.191  83.021 1.00 21.07 ? 543  ILE   B HD11 1 
ATOM   17750 H  HD12 . ILE   B 1 543 ? 25.616 17.431  83.306 1.00 21.07 ? 543  ILE   B HD12 1 
ATOM   17751 H  HD13 . ILE   B 1 543 ? 26.574 16.960  84.476 1.00 21.07 ? 543  ILE   B HD13 1 
ATOM   17752 N  N    . ASP   B 1 544 ? 23.618 14.656  87.343 1.00 26.92 ? 544  ASP   B N    1 
ATOM   17753 C  CA   . ASP   B 1 544 ? 22.575 14.032  88.199 1.00 30.32 ? 544  ASP   B CA   1 
ATOM   17754 C  C    . ASP   B 1 544 ? 21.189 14.244  87.588 1.00 27.23 ? 544  ASP   B C    1 
ATOM   17755 O  O    . ASP   B 1 544 ? 21.022 15.193  86.810 1.00 21.25 ? 544  ASP   B O    1 
ATOM   17756 C  CB   . ASP   B 1 544 ? 22.626 14.626  89.609 1.00 30.28 ? 544  ASP   B CB   1 
ATOM   17757 C  CG   . ASP   B 1 544 ? 21.678 13.972  90.598 1.00 42.78 ? 544  ASP   B CG   1 
ATOM   17758 O  OD1  . ASP   B 1 544 ? 20.497 14.361  90.620 1.00 42.92 ? 544  ASP   B OD1  1 
ATOM   17759 O  OD2  . ASP   B 1 544 ? 22.132 13.084  91.342 1.00 46.05 ? 544  ASP   B OD2  1 
ATOM   17760 H  H    . ASP   B 1 544 ? 23.921 15.403  87.643 1.00 32.31 ? 544  ASP   B H    1 
ATOM   17761 H  HA   . ASP   B 1 544 ? 22.747 13.079  88.254 1.00 36.39 ? 544  ASP   B HA   1 
ATOM   17762 H  HB2  . ASP   B 1 544 ? 23.532 14.551  89.948 1.00 36.34 ? 544  ASP   B HB2  1 
ATOM   17763 H  HB3  . ASP   B 1 544 ? 22.420 15.572  89.557 1.00 36.34 ? 544  ASP   B HB3  1 
ATOM   17764 N  N    . SER   B 1 545 ? 20.229 13.394  87.957 1.00 25.12 ? 545  SER   B N    1 
ATOM   17765 C  CA   . SER   B 1 545 ? 18.837 13.556  87.471 1.00 23.80 ? 545  SER   B CA   1 
ATOM   17766 C  C    . SER   B 1 545 ? 18.284 14.922  87.904 1.00 20.53 ? 545  SER   B C    1 
ATOM   17767 O  O    . SER   B 1 545 ? 17.324 15.388  87.287 1.00 20.01 ? 545  SER   B O    1 
ATOM   17768 C  CB   . SER   B 1 545 ? 17.985 12.415  87.956 1.00 23.65 ? 545  SER   B CB   1 
ATOM   17769 O  OG   . SER   B 1 545 ? 18.502 11.173  87.503 1.00 22.05 ? 545  SER   B OG   1 
ATOM   17770 H  H    . SER   B 1 545 ? 20.351 12.723  88.481 1.00 30.15 ? 545  SER   B H    1 
ATOM   17771 H  HA   . SER   B 1 545 ? 18.824 13.533  86.501 1.00 28.56 ? 545  SER   B HA   1 
ATOM   17772 H  HB2  . SER   B 1 545 ? 17.950 12.421  88.925 1.00 28.38 ? 545  SER   B HB2  1 
ATOM   17773 H  HB3  . SER   B 1 545 ? 17.075 12.527  87.638 1.00 28.38 ? 545  SER   B HB3  1 
ATOM   17774 H  HG   . SER   B 1 545 ? 18.224 10.556  88.000 1.00 26.46 ? 545  SER   B HG   1 
ATOM   17775 N  N    . SER   B 1 546 ? 18.898 15.539  88.916 1.00 17.66 ? 546  SER   B N    1 
ATOM   17776 C  CA   . SER   B 1 546 ? 18.448 16.872  89.395 1.00 22.73 ? 546  SER   B CA   1 
ATOM   17777 C  C    . SER   B 1 546 ? 18.616 17.921  88.290 1.00 19.73 ? 546  SER   B C    1 
ATOM   17778 O  O    . SER   B 1 546 ? 17.986 18.983  88.384 1.00 17.33 ? 546  SER   B O    1 
ATOM   17779 C  CB   . SER   B 1 546 ? 19.189 17.279  90.645 1.00 23.83 ? 546  SER   B CB   1 
ATOM   17780 O  OG   . SER   B 1 546 ? 20.565 17.492  90.379 1.00 27.52 ? 546  SER   B OG   1 
ATOM   17781 H  H    . SER   B 1 546 ? 19.571 15.215  89.341 1.00 21.20 ? 546  SER   B H    1 
ATOM   17782 H  HA   . SER   B 1 546 ? 17.506 16.812  89.619 1.00 27.28 ? 546  SER   B HA   1 
ATOM   17783 H  HB2  . SER   B 1 546 ? 18.798 18.090  91.007 1.00 28.60 ? 546  SER   B HB2  1 
ATOM   17784 H  HB3  . SER   B 1 546 ? 19.090 16.590  91.321 1.00 28.60 ? 546  SER   B HB3  1 
ATOM   17785 H  HG   . SER   B 1 546 ? 20.956 17.718  91.087 1.00 33.03 ? 546  SER   B HG   1 
ATOM   17786 N  N    . GLN   B 1 547 ? 19.444 17.620  87.288 1.00 19.54 ? 547  GLN   B N    1 
ATOM   17787 C  CA   . GLN   B 1 547 ? 19.657 18.558  86.152 1.00 17.30 ? 547  GLN   B CA   1 
ATOM   17788 C  C    . GLN   B 1 547 ? 18.496 18.418  85.164 1.00 17.22 ? 547  GLN   B C    1 
ATOM   17789 O  O    . GLN   B 1 547 ? 18.483 19.161  84.171 1.00 13.11 ? 547  GLN   B O    1 
ATOM   17790 C  CB   . GLN   B 1 547 ? 21.008 18.289  85.489 1.00 19.28 ? 547  GLN   B CB   1 
ATOM   17791 C  CG   . GLN   B 1 547 ? 22.186 18.384  86.448 1.00 21.51 ? 547  GLN   B CG   1 
ATOM   17792 C  CD   . GLN   B 1 547 ? 23.442 18.870  85.766 1.00 20.49 ? 547  GLN   B CD   1 
ATOM   17793 O  OE1  . GLN   B 1 547 ? 23.393 19.514  84.722 1.00 22.60 ? 547  GLN   B OE1  1 
ATOM   17794 N  NE2  . GLN   B 1 547 ? 24.584 18.565  86.359 1.00 20.76 ? 547  GLN   B NE2  1 
ATOM   17795 H  H    . GLN   B 1 547 ? 19.893 16.888  87.236 1.00 23.45 ? 547  GLN   B H    1 
ATOM   17796 H  HA   . GLN   B 1 547 ? 19.675 19.473  86.474 1.00 20.77 ? 547  GLN   B HA   1 
ATOM   17797 H  HB2  . GLN   B 1 547 ? 20.994 17.404  85.092 1.00 23.14 ? 547  GLN   B HB2  1 
ATOM   17798 H  HB3  . GLN   B 1 547 ? 21.137 18.923  84.766 1.00 23.14 ? 547  GLN   B HB3  1 
ATOM   17799 H  HG2  . GLN   B 1 547 ? 21.961 18.986  87.174 1.00 25.81 ? 547  GLN   B HG2  1 
ATOM   17800 H  HG3  . GLN   B 1 547 ? 22.351 17.513  86.842 1.00 25.81 ? 547  GLN   B HG3  1 
ATOM   17801 H  HE21 . GLN   B 1 547 ? 24.581 18.112  87.090 1.00 24.92 ? 547  GLN   B HE21 1 
ATOM   17802 H  HE22 . GLN   B 1 547 ? 25.329 18.820  86.014 1.00 24.92 ? 547  GLN   B HE22 1 
ATOM   17803 N  N    . ASP   B 1 548 ? 17.574 17.488  85.430 1.00 16.45 ? 548  ASP   B N    1 
ATOM   17804 C  CA   . ASP   B 1 548 ? 16.355 17.372  84.597 1.00 15.29 ? 548  ASP   B CA   1 
ATOM   17805 C  C    . ASP   B 1 548 ? 15.356 18.418  85.097 1.00 17.32 ? 548  ASP   B C    1 
ATOM   17806 O  O    . ASP   B 1 548 ? 14.568 18.097  85.988 1.00 18.87 ? 548  ASP   B O    1 
ATOM   17807 C  CB   . ASP   B 1 548 ? 15.742 15.974  84.661 1.00 16.05 ? 548  ASP   B CB   1 
ATOM   17808 C  CG   . ASP   B 1 548 ? 16.572 14.918  83.956 1.00 15.69 ? 548  ASP   B CG   1 
ATOM   17809 O  OD1  . ASP   B 1 548 ? 17.574 15.291  83.319 1.00 15.80 ? 548  ASP   B OD1  1 
ATOM   17810 O  OD2  . ASP   B 1 548 ? 16.205 13.734  84.051 1.00 18.30 ? 548  ASP   B OD2  1 
ATOM   17811 H  H    . ASP   B 1 548 ? 17.627 16.921  86.075 1.00 19.75 ? 548  ASP   B H    1 
ATOM   17812 H  HA   . ASP   B 1 548 ? 16.586 17.525  83.667 1.00 18.35 ? 548  ASP   B HA   1 
ATOM   17813 H  HB2  . ASP   B 1 548 ? 15.630 15.720  85.590 1.00 19.26 ? 548  ASP   B HB2  1 
ATOM   17814 H  HB3  . ASP   B 1 548 ? 14.857 15.998  84.264 1.00 19.26 ? 548  ASP   B HB3  1 
ATOM   17815 N  N    . THR   B 1 549 ? 15.418 19.623  84.543 1.00 16.17 ? 549  THR   B N    1 
ATOM   17816 C  CA   . THR   B 1 549 ? 14.525 20.698  85.029 1.00 17.84 ? 549  THR   B CA   1 
ATOM   17817 C  C    . THR   B 1 549 ? 14.328 21.740  83.933 1.00 15.28 ? 549  THR   B C    1 
ATOM   17818 O  O    . THR   B 1 549 ? 14.826 21.527  82.817 1.00 13.69 ? 549  THR   B O    1 
ATOM   17819 C  CB   . THR   B 1 549 ? 15.086 21.332  86.307 1.00 20.63 ? 549  THR   B CB   1 
ATOM   17820 O  OG1  . THR   B 1 549 ? 14.090 22.198  86.853 1.00 24.28 ? 549  THR   B OG1  1 
ATOM   17821 C  CG2  . THR   B 1 549 ? 16.366 22.102  86.065 1.00 21.23 ? 549  THR   B CG2  1 
ATOM   17822 H  H    . THR   B 1 549 ? 15.949 19.845  83.904 1.00 19.40 ? 549  THR   B H    1 
ATOM   17823 H  HA   . THR   B 1 549 ? 13.660 20.317  85.249 1.00 21.42 ? 549  THR   B HA   1 
ATOM   17824 H  HB   . THR   B 1 549 ? 15.307 20.620  86.928 1.00 24.76 ? 549  THR   B HB   1 
ATOM   17825 H  HG1  . THR   B 1 549 ? 14.425 22.955  86.997 1.00 29.14 ? 549  THR   B HG1  1 
ATOM   17826 H  HG21 . THR   B 1 549 ? 16.678 22.482  86.901 1.00 25.48 ? 549  THR   B HG21 1 
ATOM   17827 H  HG22 . THR   B 1 549 ? 17.042 21.504  85.710 1.00 25.48 ? 549  THR   B HG22 1 
ATOM   17828 H  HG23 . THR   B 1 549 ? 16.200 22.815  85.429 1.00 25.48 ? 549  THR   B HG23 1 
ATOM   17829 N  N    . LEU   B 1 550 ? 13.584 22.793  84.248 1.00 17.06 ? 550  LEU   B N    1 
ATOM   17830 C  CA   . LEU   B 1 550 ? 13.394 23.904  83.289 1.00 14.05 ? 550  LEU   B CA   1 
ATOM   17831 C  C    . LEU   B 1 550 ? 13.678 25.198  84.046 1.00 15.13 ? 550  LEU   B C    1 
ATOM   17832 O  O    . LEU   B 1 550 ? 13.630 25.176  85.281 1.00 18.21 ? 550  LEU   B O    1 
ATOM   17833 C  CB   . LEU   B 1 550 ? 11.956 23.886  82.767 1.00 17.28 ? 550  LEU   B CB   1 
ATOM   17834 C  CG   . LEU   B 1 550 ? 11.610 22.762  81.793 1.00 16.20 ? 550  LEU   B CG   1 
ATOM   17835 C  CD1  . LEU   B 1 550 ? 10.156 22.860  81.361 1.00 16.11 ? 550  LEU   B CD1  1 
ATOM   17836 C  CD2  . LEU   B 1 550 ? 12.525 22.794  80.580 1.00 16.06 ? 550  LEU   B CD2  1 
ATOM   17837 H  H    . LEU   B 1 550 ? 13.180 22.894  85.000 1.00 20.48 ? 550  LEU   B H    1 
ATOM   17838 H  HA   . LEU   B 1 550 ? 13.988 23.823  82.526 1.00 16.86 ? 550  LEU   B HA   1 
ATOM   17839 H  HB2  . LEU   B 1 550 ? 11.356 23.827  83.527 1.00 20.74 ? 550  LEU   B HB2  1 
ATOM   17840 H  HB3  . LEU   B 1 550 ? 11.779 24.734  82.330 1.00 20.74 ? 550  LEU   B HB3  1 
ATOM   17841 H  HG   . LEU   B 1 550 ? 11.742 21.917  82.250 1.00 19.44 ? 550  LEU   B HG   1 
ATOM   17842 H  HD11 . LEU   B 1 550 ? 9.952  22.140  80.743 1.00 19.34 ? 550  LEU   B HD11 1 
ATOM   17843 H  HD12 . LEU   B 1 550 ? 9.582  22.790  82.139 1.00 19.34 ? 550  LEU   B HD12 1 
ATOM   17844 H  HD13 . LEU   B 1 550 ? 10.005 23.713  80.924 1.00 19.34 ? 550  LEU   B HD13 1 
ATOM   17845 H  HD21 . LEU   B 1 550 ? 12.288 22.073  79.976 1.00 19.28 ? 550  LEU   B HD21 1 
ATOM   17846 H  HD22 . LEU   B 1 550 ? 12.427 23.644  80.123 1.00 19.28 ? 550  LEU   B HD22 1 
ATOM   17847 H  HD23 . LEU   B 1 550 ? 13.446 22.686  80.866 1.00 19.28 ? 550  LEU   B HD23 1 
ATOM   17848 N  N    . PRO   B 1 551 ? 14.019 26.307  83.365 1.00 17.80 ? 551  PRO   B N    1 
ATOM   17849 C  CA   . PRO   B 1 551 ? 14.183 27.579  84.055 1.00 15.65 ? 551  PRO   B CA   1 
ATOM   17850 C  C    . PRO   B 1 551 ? 12.915 27.886  84.867 1.00 15.97 ? 551  PRO   B C    1 
ATOM   17851 O  O    . PRO   B 1 551 ? 11.843 27.517  84.442 1.00 16.88 ? 551  PRO   B O    1 
ATOM   17852 C  CB   . PRO   B 1 551 ? 14.352 28.570  82.900 1.00 16.14 ? 551  PRO   B CB   1 
ATOM   17853 C  CG   . PRO   B 1 551 ? 14.956 27.742  81.788 1.00 14.05 ? 551  PRO   B CG   1 
ATOM   17854 C  CD   . PRO   B 1 551 ? 14.310 26.380  81.933 1.00 14.79 ? 551  PRO   B CD   1 
ATOM   17855 H  HA   . PRO   B 1 551 ? 14.923 27.603  84.681 1.00 18.78 ? 551  PRO   B HA   1 
ATOM   17856 H  HB2  . PRO   B 1 551 ? 13.502 28.954  82.635 1.00 19.37 ? 551  PRO   B HB2  1 
ATOM   17857 H  HB3  . PRO   B 1 551 ? 14.931 29.308  83.148 1.00 19.37 ? 551  PRO   B HB3  1 
ATOM   17858 H  HG2  . PRO   B 1 551 ? 14.770 28.130  80.918 1.00 16.86 ? 551  PRO   B HG2  1 
ATOM   17859 H  HG3  . PRO   B 1 551 ? 15.921 27.686  81.874 1.00 16.86 ? 551  PRO   B HG3  1 
ATOM   17860 H  HD2  . PRO   B 1 551 ? 13.504 26.306  81.398 1.00 17.75 ? 551  PRO   B HD2  1 
ATOM   17861 H  HD3  . PRO   B 1 551 ? 14.905 25.668  81.650 1.00 17.75 ? 551  PRO   B HD3  1 
ATOM   17862 N  N    . LYS   B 1 552 ? 13.077 28.575  85.995 1.00 17.98 ? 552  LYS   B N    1 
ATOM   17863 C  CA   . LYS   B 1 552 ? 11.919 28.904  86.869 1.00 18.08 ? 552  LYS   B CA   1 
ATOM   17864 C  C    . LYS   B 1 552 ? 10.825 29.616  86.068 1.00 19.51 ? 552  LYS   B C    1 
ATOM   17865 O  O    . LYS   B 1 552 ? 9.647  29.307  86.282 1.00 17.80 ? 552  LYS   B O    1 
ATOM   17866 C  CB   . LYS   B 1 552 ? 12.397 29.776  88.031 1.00 25.35 ? 552  LYS   B CB   1 
ATOM   17867 C  CG   . LYS   B 1 552 ? 13.404 29.119  88.963 1.00 29.32 ? 552  LYS   B CG   1 
ATOM   17868 C  CD   . LYS   B 1 552 ? 13.514 29.819  90.299 1.00 43.42 ? 552  LYS   B CD   1 
ATOM   17869 C  CE   . LYS   B 1 552 ? 14.924 29.834  90.849 1.00 50.26 ? 552  LYS   B CE   1 
ATOM   17870 N  NZ   . LYS   B 1 552 ? 15.583 31.145  90.640 1.00 52.52 ? 552  LYS   B NZ   1 
ATOM   17871 H  H    . LYS   B 1 552 ? 13.835 28.864  86.280 1.00 21.58 ? 552  LYS   B H    1 
ATOM   17872 H  HA   . LYS   B 1 552 ? 11.540 28.084  87.222 1.00 21.70 ? 552  LYS   B HA   1 
ATOM   17873 H  HB2  . LYS   B 1 552 ? 12.793 30.584  87.669 1.00 30.42 ? 552  LYS   B HB2  1 
ATOM   17874 H  HB3  . LYS   B 1 552 ? 11.625 30.047  88.552 1.00 30.42 ? 552  LYS   B HB3  1 
ATOM   17875 H  HG2  . LYS   B 1 552 ? 13.149 28.194  89.108 1.00 35.19 ? 552  LYS   B HG2  1 
ATOM   17876 H  HG3  . LYS   B 1 552 ? 14.275 29.109  88.536 1.00 35.19 ? 552  LYS   B HG3  1 
ATOM   17877 H  HD2  . LYS   B 1 552 ? 13.199 30.732  90.206 1.00 52.11 ? 552  LYS   B HD2  1 
ATOM   17878 H  HD3  . LYS   B 1 552 ? 12.929 29.381  90.937 1.00 52.11 ? 552  LYS   B HD3  1 
ATOM   17879 H  HE2  . LYS   B 1 552 ? 14.903 29.630  91.797 1.00 60.32 ? 552  LYS   B HE2  1 
ATOM   17880 H  HE3  . LYS   B 1 552 ? 15.446 29.138  90.420 1.00 60.32 ? 552  LYS   B HE3  1 
ATOM   17881 H  HZ1  . LYS   B 1 552 ? 16.186 31.074  89.990 1.00 63.03 ? 552  LYS   B HZ1  1 
ATOM   17882 H  HZ2  . LYS   B 1 552 ? 14.973 31.751  90.413 1.00 63.03 ? 552  LYS   B HZ2  1 
ATOM   17883 H  HZ3  . LYS   B 1 552 ? 15.986 31.398  91.392 1.00 63.03 ? 552  LYS   B HZ3  1 
ATOM   17884 N  N    . ARG   B 1 553 ? 11.213 30.535  85.181 1.00 18.39 ? 553  ARG   B N    1 
ATOM   17885 C  CA   . ARG   B 1 553 ? 10.221 31.295  84.378 1.00 16.25 ? 553  ARG   B CA   1 
ATOM   17886 C  C    . ARG   B 1 553 ? 9.220  30.330  83.739 1.00 15.44 ? 553  ARG   B C    1 
ATOM   17887 O  O    . ARG   B 1 553 ? 8.021  30.630  83.760 1.00 17.55 ? 553  ARG   B O    1 
ATOM   17888 C  CB   . ARG   B 1 553 ? 10.931 32.091  83.275 1.00 17.18 ? 553  ARG   B CB   1 
ATOM   17889 C  CG   . ARG   B 1 553 ? 10.023 32.599  82.165 1.00 17.19 ? 553  ARG   B CG   1 
ATOM   17890 C  CD   . ARG   B 1 553 ? 10.743 33.611  81.291 1.00 17.28 ? 553  ARG   B CD   1 
ATOM   17891 N  NE   . ARG   B 1 553 ? 11.010 34.853  82.004 1.00 17.84 ? 553  ARG   B NE   1 
ATOM   17892 C  CZ   . ARG   B 1 553 ? 11.985 35.704  81.705 1.00 20.67 ? 553  ARG   B CZ   1 
ATOM   17893 N  NH1  . ARG   B 1 553 ? 12.698 35.536  80.606 1.00 18.11 ? 553  ARG   B NH1  1 
ATOM   17894 N  NH2  . ARG   B 1 553 ? 12.246 36.721  82.510 1.00 20.30 ? 553  ARG   B NH2  1 
ATOM   17895 H  H    . ARG   B 1 553 ? 12.034 30.739  85.023 1.00 22.07 ? 553  ARG   B H    1 
ATOM   17896 H  HA   . ARG   B 1 553 ? 9.752  31.909  84.965 1.00 19.50 ? 553  ARG   B HA   1 
ATOM   17897 H  HB2  . ARG   B 1 553 ? 11.380 32.849  83.680 1.00 20.62 ? 553  ARG   B HB2  1 
ATOM   17898 H  HB3  . ARG   B 1 553 ? 11.618 31.531  82.882 1.00 20.62 ? 553  ARG   B HB3  1 
ATOM   17899 H  HG2  . ARG   B 1 553 ? 9.723  31.853  81.622 1.00 20.63 ? 553  ARG   B HG2  1 
ATOM   17900 H  HG3  . ARG   B 1 553 ? 9.231  33.006  82.551 1.00 20.63 ? 553  ARG   B HG3  1 
ATOM   17901 H  HD2  . ARG   B 1 553 ? 11.579 33.231  80.979 1.00 20.74 ? 553  ARG   B HD2  1 
ATOM   17902 H  HD3  . ARG   B 1 553 ? 10.206 33.799  80.505 1.00 20.74 ? 553  ARG   B HD3  1 
ATOM   17903 H  HE   . ARG   B 1 553 ? 10.499 35.050  82.667 1.00 21.41 ? 553  ARG   B HE   1 
ATOM   17904 H  HH11 . ARG   B 1 553 ? 12.531 34.875  80.082 1.00 21.74 ? 553  ARG   B HH11 1 
ATOM   17905 H  HH12 . ARG   B 1 553 ? 13.329 36.088  80.414 1.00 21.74 ? 553  ARG   B HH12 1 
ATOM   17906 H  HH21 . ARG   B 1 553 ? 11.784 36.831  83.227 1.00 24.36 ? 553  ARG   B HH21 1 
ATOM   17907 H  HH22 . ARG   B 1 553 ? 12.877 37.272  82.316 1.00 24.36 ? 553  ARG   B HH22 1 
ATOM   17908 N  N    . LEU   B 1 554 ? 9.701  29.210  83.199 1.00 17.86 ? 554  LEU   B N    1 
ATOM   17909 C  CA   . LEU   B 1 554 ? 8.806  28.299  82.432 1.00 17.99 ? 554  LEU   B CA   1 
ATOM   17910 C  C    . LEU   B 1 554 ? 7.996  27.392  83.368 1.00 17.50 ? 554  LEU   B C    1 
ATOM   17911 O  O    . LEU   B 1 554 ? 7.022  26.785  82.899 1.00 19.22 ? 554  LEU   B O    1 
ATOM   17912 C  CB   . LEU   B 1 554 ? 9.669  27.486  81.459 1.00 15.00 ? 554  LEU   B CB   1 
ATOM   17913 C  CG   . LEU   B 1 554 ? 10.519 28.330  80.509 1.00 15.39 ? 554  LEU   B CG   1 
ATOM   17914 C  CD1  . LEU   B 1 554 ? 11.326 27.451  79.567 1.00 15.80 ? 554  LEU   B CD1  1 
ATOM   17915 C  CD2  . LEU   B 1 554 ? 9.649  29.295  79.720 1.00 17.45 ? 554  LEU   B CD2  1 
ATOM   17916 H  H    . LEU   B 1 554 ? 10.520 28.953  83.256 1.00 21.44 ? 554  LEU   B H    1 
ATOM   17917 H  HA   . LEU   B 1 554 ? 8.158  28.819  81.932 1.00 21.59 ? 554  LEU   B HA   1 
ATOM   17918 H  HB2  . LEU   B 1 554 ? 10.255 26.906  81.971 1.00 18.01 ? 554  LEU   B HB2  1 
ATOM   17919 H  HB3  . LEU   B 1 554 ? 9.090  26.912  80.933 1.00 18.01 ? 554  LEU   B HB3  1 
ATOM   17920 H  HG   . LEU   B 1 554 ? 11.140 28.845  81.047 1.00 18.47 ? 554  LEU   B HG   1 
ATOM   17921 H  HD11 . LEU   B 1 554 ? 11.855 28.010  78.976 1.00 18.97 ? 554  LEU   B HD11 1 
ATOM   17922 H  HD12 . LEU   B 1 554 ? 11.915 26.878  80.083 1.00 18.97 ? 554  LEU   B HD12 1 
ATOM   17923 H  HD13 . LEU   B 1 554 ? 10.724 26.903  79.040 1.00 18.97 ? 554  LEU   B HD13 1 
ATOM   17924 H  HD21 . LEU   B 1 554 ? 10.206 29.820  79.124 1.00 20.95 ? 554  LEU   B HD21 1 
ATOM   17925 H  HD22 . LEU   B 1 554 ? 9.001  28.795  79.199 1.00 20.95 ? 554  LEU   B HD22 1 
ATOM   17926 H  HD23 . LEU   B 1 554 ? 9.184  29.886  80.332 1.00 20.95 ? 554  LEU   B HD23 1 
ATOM   17927 N  N    . LEU   B 1 555 ? 8.380  27.335  84.639 1.00 17.26 ? 555  LEU   B N    1 
ATOM   17928 C  CA   . LEU   B 1 555 ? 7.625  26.509  85.615 1.00 19.26 ? 555  LEU   B CA   1 
ATOM   17929 C  C    . LEU   B 1 555 ? 6.712  27.388  86.473 1.00 19.12 ? 555  LEU   B C    1 
ATOM   17930 O  O    . LEU   B 1 555 ? 5.722  26.846  86.989 1.00 19.64 ? 555  LEU   B O    1 
ATOM   17931 C  CB   . LEU   B 1 555 ? 8.621  25.778  86.515 1.00 17.37 ? 555  LEU   B CB   1 
ATOM   17932 C  CG   . LEU   B 1 555 ? 9.566  24.810  85.807 1.00 16.93 ? 555  LEU   B CG   1 
ATOM   17933 C  CD1  . LEU   B 1 555 ? 10.585 24.245  86.783 1.00 18.50 ? 555  LEU   B CD1  1 
ATOM   17934 C  CD2  . LEU   B 1 555 ? 8.789  23.687  85.139 1.00 18.49 ? 555  LEU   B CD2  1 
ATOM   17935 H  H    . LEU   B 1 555 ? 9.058  27.753  84.964 1.00 20.72 ? 555  LEU   B H    1 
ATOM   17936 H  HA   . LEU   B 1 555 ? 7.074  25.872  85.134 1.00 23.11 ? 555  LEU   B HA   1 
ATOM   17937 H  HB2  . LEU   B 1 555 ? 9.154  26.439  86.984 1.00 20.85 ? 555  LEU   B HB2  1 
ATOM   17938 H  HB3  . LEU   B 1 555 ? 8.124  25.286  87.187 1.00 20.85 ? 555  LEU   B HB3  1 
ATOM   17939 H  HG   . LEU   B 1 555 ? 10.041 25.302  85.119 1.00 20.32 ? 555  LEU   B HG   1 
ATOM   17940 H  HD11 . LEU   B 1 555 ? 11.176 23.633  86.316 1.00 22.21 ? 555  LEU   B HD11 1 
ATOM   17941 H  HD12 . LEU   B 1 555 ? 11.106 24.970  87.163 1.00 22.21 ? 555  LEU   B HD12 1 
ATOM   17942 H  HD13 . LEU   B 1 555 ? 10.125 23.771  87.493 1.00 22.21 ? 555  LEU   B HD13 1 
ATOM   17943 H  HD21 . LEU   B 1 555 ? 9.407  23.085  84.696 1.00 22.19 ? 555  LEU   B HD21 1 
ATOM   17944 H  HD22 . LEU   B 1 555 ? 8.286  23.198  85.809 1.00 22.19 ? 555  LEU   B HD22 1 
ATOM   17945 H  HD23 . LEU   B 1 555 ? 8.178  24.061  84.485 1.00 22.19 ? 555  LEU   B HD23 1 
ATOM   17946 N  N    . GLU   B 1 556 ? 7.001  28.687  86.578 1.00 18.07 ? 556  GLU   B N    1 
ATOM   17947 C  CA   . GLU   B 1 556 ? 6.238  29.533  87.538 1.00 20.25 ? 556  GLU   B CA   1 
ATOM   17948 C  C    . GLU   B 1 556 ? 5.574  30.755  86.889 1.00 23.58 ? 556  GLU   B C    1 
ATOM   17949 O  O    . GLU   B 1 556 ? 4.625  31.279  87.495 1.00 20.09 ? 556  GLU   B O    1 
ATOM   17950 C  CB   . GLU   B 1 556 ? 7.175  30.000  88.653 1.00 20.91 ? 556  GLU   B CB   1 
ATOM   17951 C  CG   . GLU   B 1 556 ? 7.989  28.891  89.288 1.00 24.99 ? 556  GLU   B CG   1 
ATOM   17952 C  CD   . GLU   B 1 556 ? 8.976  29.393  90.328 1.00 36.04 ? 556  GLU   B CD   1 
ATOM   17953 O  OE1  . GLU   B 1 556 ? 9.144  30.622  90.431 1.00 38.74 ? 556  GLU   B OE1  1 
ATOM   17954 O  OE2  . GLU   B 1 556 ? 9.572  28.557  91.031 1.00 36.50 ? 556  GLU   B OE2  1 
ATOM   17955 H  H    . GLU   B 1 556 ? 7.608  29.096  86.127 1.00 21.69 ? 556  GLU   B H    1 
ATOM   17956 H  HA   . GLU   B 1 556 ? 5.522  28.981  87.888 1.00 24.31 ? 556  GLU   B HA   1 
ATOM   17957 H  HB2  . GLU   B 1 556 ? 7.781  30.667  88.294 1.00 25.10 ? 556  GLU   B HB2  1 
ATOM   17958 H  HB3  . GLU   B 1 556 ? 6.649  30.436  89.342 1.00 25.10 ? 556  GLU   B HB3  1 
ATOM   17959 H  HG2  . GLU   B 1 556 ? 7.387  28.253  89.703 1.00 30.00 ? 556  GLU   B HG2  1 
ATOM   17960 H  HG3  . GLU   B 1 556 ? 8.473  28.415  88.595 1.00 30.00 ? 556  GLU   B HG3  1 
ATOM   17961 N  N    . GLU   B 1 557 ? 6.061  31.226  85.741 1.00 21.34 ? 557  GLU   B N    1 
ATOM   17962 C  CA   . GLU   B 1 557 ? 5.482  32.466  85.164 1.00 18.63 ? 557  GLU   B CA   1 
ATOM   17963 C  C    . GLU   B 1 557 ? 4.533  32.109  84.019 1.00 20.12 ? 557  GLU   B C    1 
ATOM   17964 O  O    . GLU   B 1 557 ? 4.989  31.580  82.999 1.00 18.25 ? 557  GLU   B O    1 
ATOM   17965 C  CB   . GLU   B 1 557 ? 6.580  33.423  84.698 1.00 23.20 ? 557  GLU   B CB   1 
ATOM   17966 C  CG   . GLU   B 1 557 ? 7.661  33.665  85.730 1.00 29.47 ? 557  GLU   B CG   1 
ATOM   17967 C  CD   . GLU   B 1 557 ? 8.765  34.599  85.265 1.00 36.78 ? 557  GLU   B CD   1 
ATOM   17968 O  OE1  . GLU   B 1 557 ? 8.638  35.165  84.161 1.00 30.81 ? 557  GLU   B OE1  1 
ATOM   17969 O  OE2  . GLU   B 1 557 ? 9.749  34.758  86.009 1.00 40.17 ? 557  GLU   B OE2  1 
ATOM   17970 H  H    . GLU   B 1 557 ? 6.699  30.868  85.289 1.00 25.62 ? 557  GLU   B H    1 
ATOM   17971 H  HA   . GLU   B 1 557 ? 4.977  32.925  85.853 1.00 22.36 ? 557  GLU   B HA   1 
ATOM   17972 H  HB2  . GLU   B 1 557 ? 6.987  33.066  83.893 1.00 27.84 ? 557  GLU   B HB2  1 
ATOM   17973 H  HB3  . GLU   B 1 557 ? 6.177  34.272  84.459 1.00 27.84 ? 557  GLU   B HB3  1 
ATOM   17974 H  HG2  . GLU   B 1 557 ? 7.254  34.034  86.530 1.00 35.37 ? 557  GLU   B HG2  1 
ATOM   17975 H  HG3  . GLU   B 1 557 ? 8.054  32.814  85.978 1.00 35.37 ? 557  GLU   B HG3  1 
ATOM   17976 N  N    . PRO   B 1 558 ? 3.222  32.380  84.157 1.00 20.43 ? 558  PRO   B N    1 
ATOM   17977 C  CA   . PRO   B 1 558 ? 2.262  32.054  83.116 1.00 21.32 ? 558  PRO   B CA   1 
ATOM   17978 C  C    . PRO   B 1 558 ? 2.534  32.853  81.835 1.00 17.98 ? 558  PRO   B C    1 
ATOM   17979 O  O    . PRO   B 1 558 ? 3.001  33.962  81.930 1.00 19.88 ? 558  PRO   B O    1 
ATOM   17980 C  CB   . PRO   B 1 558 ? 0.905  32.473  83.710 1.00 26.01 ? 558  PRO   B CB   1 
ATOM   17981 C  CG   . PRO   B 1 558 ? 1.155  32.563  85.197 1.00 28.00 ? 558  PRO   B CG   1 
ATOM   17982 C  CD   . PRO   B 1 558 ? 2.600  32.996  85.327 1.00 21.06 ? 558  PRO   B CD   1 
ATOM   17983 H  HA   . PRO   B 1 558 ? 2.302  31.117  82.870 1.00 25.59 ? 558  PRO   B HA   1 
ATOM   17984 H  HB2  . PRO   B 1 558 ? 0.609  33.323  83.349 1.00 31.22 ? 558  PRO   B HB2  1 
ATOM   17985 H  HB3  . PRO   B 1 558 ? 0.214  31.823  83.507 1.00 31.22 ? 558  PRO   B HB3  1 
ATOM   17986 H  HG2  . PRO   B 1 558 ? 0.558  33.203  85.615 1.00 33.60 ? 558  PRO   B HG2  1 
ATOM   17987 H  HG3  . PRO   B 1 558 ? 1.004  31.709  85.631 1.00 33.60 ? 558  PRO   B HG3  1 
ATOM   17988 H  HD2  . PRO   B 1 558 ? 2.690  33.962  85.317 1.00 25.28 ? 558  PRO   B HD2  1 
ATOM   17989 H  HD3  . PRO   B 1 558 ? 2.998  32.683  86.154 1.00 25.28 ? 558  PRO   B HD3  1 
ATOM   17990 N  N    . ILE   B 1 559 ? 2.257  32.252  80.683 1.00 17.64 ? 559  ILE   B N    1 
ATOM   17991 C  CA   . ILE   B 1 559 ? 2.389  33.013  79.409 1.00 17.23 ? 559  ILE   B CA   1 
ATOM   17992 C  C    . ILE   B 1 559 ? 1.555  34.286  79.564 1.00 18.22 ? 559  ILE   B C    1 
ATOM   17993 O  O    . ILE   B 1 559 ? 0.355  34.171  79.859 1.00 19.34 ? 559  ILE   B O    1 
ATOM   17994 C  CB   . ILE   B 1 559 ? 1.952  32.156  78.209 1.00 16.44 ? 559  ILE   B CB   1 
ATOM   17995 C  CG1  . ILE   B 1 559 ? 2.998  31.081  77.899 1.00 17.63 ? 559  ILE   B CG1  1 
ATOM   17996 C  CG2  . ILE   B 1 559 ? 1.653  33.025  76.997 1.00 17.94 ? 559  ILE   B CG2  1 
ATOM   17997 C  CD1  . ILE   B 1 559 ? 2.572  30.087  76.848 1.00 18.62 ? 559  ILE   B CD1  1 
ATOM   17998 H  H    . ILE   B 1 559 ? 1.999  31.436  80.601 1.00 21.18 ? 559  ILE   B H    1 
ATOM   17999 H  HA   . ILE   B 1 559 ? 3.313  33.250  79.232 1.00 20.68 ? 559  ILE   B HA   1 
ATOM   18000 H  HB   . ILE   B 1 559 ? 1.128  31.700  78.443 1.00 19.73 ? 559  ILE   B HB   1 
ATOM   18001 H  HG12 . ILE   B 1 559 ? 3.815  31.514  77.607 1.00 21.16 ? 559  ILE   B HG12 1 
ATOM   18002 H  HG13 . ILE   B 1 559 ? 3.207  30.602  78.716 1.00 21.16 ? 559  ILE   B HG13 1 
ATOM   18003 H  HG21 . ILE   B 1 559 ? 1.380  32.463  76.255 1.00 21.53 ? 559  ILE   B HG21 1 
ATOM   18004 H  HG22 . ILE   B 1 559 ? 0.939  33.645  77.212 1.00 21.53 ? 559  ILE   B HG22 1 
ATOM   18005 H  HG23 . ILE   B 1 559 ? 2.449  33.522  76.750 1.00 21.53 ? 559  ILE   B HG23 1 
ATOM   18006 H  HD11 . ILE   B 1 559 ? 3.282  29.441  76.706 1.00 22.34 ? 559  ILE   B HD11 1 
ATOM   18007 H  HD12 . ILE   B 1 559 ? 1.771  29.627  77.143 1.00 22.34 ? 559  ILE   B HD12 1 
ATOM   18008 H  HD13 . ILE   B 1 559 ? 2.389  30.553  76.017 1.00 22.34 ? 559  ILE   B HD13 1 
ATOM   18009 N  N    . PRO   B 1 560 ? 2.145  35.486  79.397 1.00 19.16 ? 560  PRO   B N    1 
ATOM   18010 C  CA   . PRO   B 1 560 ? 1.414  36.736  79.656 1.00 21.39 ? 560  PRO   B CA   1 
ATOM   18011 C  C    . PRO   B 1 560 ? 0.263  37.034  78.687 1.00 24.08 ? 560  PRO   B C    1 
ATOM   18012 O  O    . PRO   B 1 560 ? -0.730 37.563  79.135 1.00 24.81 ? 560  PRO   B O    1 
ATOM   18013 C  CB   . PRO   B 1 560 ? 2.504  37.805  79.501 1.00 23.59 ? 560  PRO   B CB   1 
ATOM   18014 C  CG   . PRO   B 1 560 ? 3.514  37.172  78.568 1.00 21.30 ? 560  PRO   B CG   1 
ATOM   18015 C  CD   . PRO   B 1 560 ? 3.520  35.708  78.951 1.00 19.69 ? 560  PRO   B CD   1 
ATOM   18016 H  HA   . PRO   B 1 560 ? 0.979  36.697  80.522 1.00 25.67 ? 560  PRO   B HA   1 
ATOM   18017 H  HB2  . PRO   B 1 560 ? 2.145  38.626  79.130 1.00 28.31 ? 560  PRO   B HB2  1 
ATOM   18018 H  HB3  . PRO   B 1 560 ? 2.904  38.030  80.356 1.00 28.31 ? 560  PRO   B HB3  1 
ATOM   18019 H  HG2  . PRO   B 1 560 ? 3.261  37.293  77.639 1.00 25.56 ? 560  PRO   B HG2  1 
ATOM   18020 H  HG3  . PRO   B 1 560 ? 4.392  37.569  78.677 1.00 25.56 ? 560  PRO   B HG3  1 
ATOM   18021 H  HD2  . PRO   B 1 560 ? 3.751  35.140  78.199 1.00 23.63 ? 560  PRO   B HD2  1 
ATOM   18022 H  HD3  . PRO   B 1 560 ? 4.161  35.522  79.655 1.00 23.63 ? 560  PRO   B HD3  1 
ATOM   18023 N  N    . ASP   B 1 561 ? 0.417  36.705  77.405 1.00 22.77 ? 561  ASP   B N    1 
ATOM   18024 C  CA   . ASP   B 1 561 ? -0.634 37.075  76.427 1.00 26.60 ? 561  ASP   B CA   1 
ATOM   18025 C  C    . ASP   B 1 561 ? -0.638 36.125  75.232 1.00 24.32 ? 561  ASP   B C    1 
ATOM   18026 O  O    . ASP   B 1 561 ? 0.386  35.467  74.995 1.00 21.55 ? 561  ASP   B O    1 
ATOM   18027 C  CB   . ASP   B 1 561 ? -0.427 38.503  75.925 1.00 25.20 ? 561  ASP   B CB   1 
ATOM   18028 C  CG   . ASP   B 1 561 ? -1.064 39.548  76.822 1.00 39.09 ? 561  ASP   B CG   1 
ATOM   18029 O  OD1  . ASP   B 1 561 ? -2.304 39.663  76.791 1.00 43.80 ? 561  ASP   B OD1  1 
ATOM   18030 O  OD2  . ASP   B 1 561 ? -0.315 40.224  77.549 1.00 42.04 ? 561  ASP   B OD2  1 
ATOM   18031 H  H    . ASP   B 1 561 ? 1.093  36.283  77.080 1.00 27.33 ? 561  ASP   B H    1 
ATOM   18032 H  HA   . ASP   B 1 561 ? -1.487 37.011  76.885 1.00 31.92 ? 561  ASP   B HA   1 
ATOM   18033 H  HB2  . ASP   B 1 561 ? 0.524  38.681  75.855 1.00 30.24 ? 561  ASP   B HB2  1 
ATOM   18034 H  HB3  . ASP   B 1 561 ? -0.797 38.583  75.032 1.00 30.24 ? 561  ASP   B HB3  1 
ATOM   18035 N  N    . GLY   B 1 562 ? -1.757 36.070  74.516 1.00 25.67 ? 562  GLY   B N    1 
ATOM   18036 C  CA   . GLY   B 1 562 ? -1.797 35.272  73.280 1.00 26.32 ? 562  GLY   B CA   1 
ATOM   18037 C  C    . GLY   B 1 562 ? -2.609 33.999  73.382 1.00 21.59 ? 562  GLY   B C    1 
ATOM   18038 O  O    . GLY   B 1 562 ? -3.227 33.757  74.429 1.00 23.03 ? 562  GLY   B O    1 
ATOM   18039 H  H    . GLY   B 1 562 ? -2.489 36.474  74.716 1.00 30.80 ? 562  GLY   B H    1 
ATOM   18040 H  HA2  . GLY   B 1 562 ? -2.162 35.819  72.567 1.00 31.59 ? 562  GLY   B HA2  1 
ATOM   18041 H  HA3  . GLY   B 1 562 ? -0.889 35.044  73.026 1.00 31.59 ? 562  GLY   B HA3  1 
ATOM   18042 N  N    . PRO   B 1 563 ? -2.613 33.171  72.320 1.00 21.44 ? 563  PRO   B N    1 
ATOM   18043 C  CA   . PRO   B 1 563 ? -3.409 31.937  72.293 1.00 23.22 ? 563  PRO   B CA   1 
ATOM   18044 C  C    . PRO   B 1 563 ? -3.147 30.967  73.456 1.00 26.60 ? 563  PRO   B C    1 
ATOM   18045 O  O    . PRO   B 1 563 ? -4.007 30.156  73.722 1.00 24.88 ? 563  PRO   B O    1 
ATOM   18046 C  CB   . PRO   B 1 563 ? -2.979 31.300  70.959 1.00 25.07 ? 563  PRO   B CB   1 
ATOM   18047 C  CG   . PRO   B 1 563 ? -2.557 32.470  70.106 1.00 29.22 ? 563  PRO   B CG   1 
ATOM   18048 C  CD   . PRO   B 1 563 ? -1.868 33.398  71.081 1.00 25.58 ? 563  PRO   B CD   1 
ATOM   18049 H  HA   . PRO   B 1 563 ? -4.355 32.132  72.380 1.00 27.86 ? 563  PRO   B HA   1 
ATOM   18050 H  HB2  . PRO   B 1 563 ? -2.250 30.673  71.085 1.00 30.09 ? 563  PRO   B HB2  1 
ATOM   18051 H  HB3  . PRO   B 1 563 ? -3.708 30.809  70.550 1.00 30.09 ? 563  PRO   B HB3  1 
ATOM   18052 H  HG2  . PRO   B 1 563 ? -1.959 32.194  69.394 1.00 35.07 ? 563  PRO   B HG2  1 
ATOM   18053 H  HG3  . PRO   B 1 563 ? -3.320 32.898  69.686 1.00 35.07 ? 563  PRO   B HG3  1 
ATOM   18054 H  HD2  . PRO   B 1 563 ? -0.928 33.182  71.181 1.00 30.71 ? 563  PRO   B HD2  1 
ATOM   18055 H  HD3  . PRO   B 1 563 ? -1.918 34.323  70.795 1.00 30.71 ? 563  PRO   B HD3  1 
ATOM   18056 N  N    . SER   B 1 564 ? -1.977 31.060  74.093 1.00 23.51 ? 564  SER   B N    1 
ATOM   18057 C  CA   . SER   B 1 564 ? -1.621 30.126  75.193 1.00 20.88 ? 564  SER   B CA   1 
ATOM   18058 C  C    . SER   B 1 564 ? -1.483 30.896  76.512 1.00 18.79 ? 564  SER   B C    1 
ATOM   18059 O  O    . SER   B 1 564 ? -0.807 30.401  77.422 1.00 19.97 ? 564  SER   B O    1 
ATOM   18060 C  CB   . SER   B 1 564 ? -0.366 29.346  74.845 1.00 18.23 ? 564  SER   B CB   1 
ATOM   18061 O  OG   . SER   B 1 564 ? -0.538 28.627  73.636 1.00 18.86 ? 564  SER   B OG   1 
ATOM   18062 H  H    . SER   B 1 564 ? -1.375 31.647  73.913 1.00 28.21 ? 564  SER   B H    1 
ATOM   18063 H  HA   . SER   B 1 564 ? -2.333 29.477  75.308 1.00 25.06 ? 564  SER   B HA   1 
ATOM   18064 H  HB2  . SER   B 1 564 ? 0.385  29.954  74.760 1.00 21.88 ? 564  SER   B HB2  1 
ATOM   18065 H  HB3  . SER   B 1 564 ? -0.153 28.731  75.564 1.00 21.88 ? 564  SER   B HB3  1 
ATOM   18066 H  HG   . SER   B 1 564 ? -0.241 29.081  72.995 1.00 22.63 ? 564  SER   B HG   1 
ATOM   18067 N  N    . LYS   B 1 565 ? -2.132 32.056  76.610 1.00 21.06 ? 565  LYS   B N    1 
ATOM   18068 C  CA   . LYS   B 1 565 ? -2.025 32.904  77.828 1.00 21.27 ? 565  LYS   B CA   1 
ATOM   18069 C  C    . LYS   B 1 565 ? -2.396 32.122  79.091 1.00 21.13 ? 565  LYS   B C    1 
ATOM   18070 O  O    . LYS   B 1 565 ? -3.371 31.361  79.041 1.00 19.59 ? 565  LYS   B O    1 
ATOM   18071 C  CB   . LYS   B 1 565 ? -2.950 34.118  77.685 1.00 23.23 ? 565  LYS   B CB   1 
ATOM   18072 C  CG   . LYS   B 1 565 ? -2.993 35.069  78.872 1.00 21.17 ? 565  LYS   B CG   1 
ATOM   18073 C  CD   . LYS   B 1 565 ? -3.994 36.186  78.668 1.00 27.68 ? 565  LYS   B CD   1 
ATOM   18074 C  CE   . LYS   B 1 565 ? -4.333 36.922  79.946 1.00 24.57 ? 565  LYS   B CE   1 
ATOM   18075 N  NZ   . LYS   B 1 565 ? -3.140 37.586  80.520 1.00 31.75 ? 565  LYS   B NZ   1 
ATOM   18076 H  H    . LYS   B 1 565 ? -2.638 32.378  75.994 1.00 25.27 ? 565  LYS   B H    1 
ATOM   18077 H  HA   . LYS   B 1 565 ? -1.103 33.194  77.915 1.00 25.53 ? 565  LYS   B HA   1 
ATOM   18078 H  HB2  . LYS   B 1 565 ? -2.676 34.620  76.901 1.00 27.88 ? 565  LYS   B HB2  1 
ATOM   18079 H  HB3  . LYS   B 1 565 ? -3.850 33.798  77.517 1.00 27.88 ? 565  LYS   B HB3  1 
ATOM   18080 H  HG2  . LYS   B 1 565 ? -3.221 34.574  79.674 1.00 25.41 ? 565  LYS   B HG2  1 
ATOM   18081 H  HG3  . LYS   B 1 565 ? -2.111 35.448  79.014 1.00 25.41 ? 565  LYS   B HG3  1 
ATOM   18082 H  HD2  . LYS   B 1 565 ? -3.639 36.817  78.023 1.00 33.22 ? 565  LYS   B HD2  1 
ATOM   18083 H  HD3  . LYS   B 1 565 ? -4.807 35.819  78.288 1.00 33.22 ? 565  LYS   B HD3  1 
ATOM   18084 H  HE2  . LYS   B 1 565 ? -5.019 37.584  79.768 1.00 29.49 ? 565  LYS   B HE2  1 
ATOM   18085 H  HE3  . LYS   B 1 565 ? -4.701 36.299  80.592 1.00 29.49 ? 565  LYS   B HE3  1 
ATOM   18086 H  HZ1  . LYS   B 1 565 ? -3.396 38.275  81.022 1.00 38.11 ? 565  LYS   B HZ1  1 
ATOM   18087 H  HZ2  . LYS   B 1 565 ? -2.689 37.005  81.022 1.00 38.11 ? 565  LYS   B HZ2  1 
ATOM   18088 H  HZ3  . LYS   B 1 565 ? -2.617 37.877  79.862 1.00 38.11 ? 565  LYS   B HZ3  1 
ATOM   18089 N  N    . GLY   B 1 566 ? -1.629 32.296  80.168 1.00 21.00 ? 566  GLY   B N    1 
ATOM   18090 C  CA   . GLY   B 1 566 ? -1.981 31.678  81.461 1.00 22.38 ? 566  GLY   B CA   1 
ATOM   18091 C  C    . GLY   B 1 566 ? -1.343 30.323  81.702 1.00 20.74 ? 566  GLY   B C    1 
ATOM   18092 O  O    . GLY   B 1 566 ? -1.466 29.823  82.831 1.00 22.13 ? 566  GLY   B O    1 
ATOM   18093 H  H    . GLY   B 1 566 ? -0.907 32.762  80.178 1.00 25.20 ? 566  GLY   B H    1 
ATOM   18094 H  HA2  . GLY   B 1 566 ? -1.719 32.279  82.176 1.00 26.86 ? 566  GLY   B HA2  1 
ATOM   18095 H  HA3  . GLY   B 1 566 ? -2.945 31.583  81.510 1.00 26.86 ? 566  GLY   B HA3  1 
ATOM   18096 N  N    . GLU   B 1 567 ? -0.645 29.775  80.709 1.00 18.30 ? 567  GLU   B N    1 
ATOM   18097 C  CA   . GLU   B 1 567 ? -0.115 28.392  80.845 1.00 17.73 ? 567  GLU   B CA   1 
ATOM   18098 C  C    . GLU   B 1 567 ? 1.306  28.359  81.410 1.00 16.68 ? 567  GLU   B C    1 
ATOM   18099 O  O    . GLU   B 1 567 ? 2.050  29.323  81.189 1.00 15.76 ? 567  GLU   B O    1 
ATOM   18100 C  CB   . GLU   B 1 567 ? -0.160 27.673  79.495 1.00 20.10 ? 567  GLU   B CB   1 
ATOM   18101 C  CG   . GLU   B 1 567 ? -1.566 27.459  78.972 1.00 21.68 ? 567  GLU   B CG   1 
ATOM   18102 C  CD   . GLU   B 1 567 ? -2.400 26.496  79.800 1.00 22.41 ? 567  GLU   B CD   1 
ATOM   18103 O  OE1  . GLU   B 1 567 ? -1.935 25.368  80.037 1.00 24.41 ? 567  GLU   B OE1  1 
ATOM   18104 O  OE2  . GLU   B 1 567 ? -3.511 26.880  80.205 1.00 26.01 ? 567  GLU   B OE2  1 
ATOM   18105 H  H    . GLU   B 1 567 ? -0.464 30.164  79.964 1.00 21.96 ? 567  GLU   B H    1 
ATOM   18106 H  HA   . GLU   B 1 567 ? -0.686 27.931  81.480 1.00 21.28 ? 567  GLU   B HA   1 
ATOM   18107 H  HB2  . GLU   B 1 567 ? 0.344  28.187  78.845 1.00 24.12 ? 567  GLU   B HB2  1 
ATOM   18108 H  HB3  . GLU   B 1 567 ? 0.281  26.813  79.580 1.00 24.12 ? 567  GLU   B HB3  1 
ATOM   18109 H  HG2  . GLU   B 1 567 ? -2.020 28.315  78.936 1.00 26.02 ? 567  GLU   B HG2  1 
ATOM   18110 H  HG3  . GLU   B 1 567 ? -1.515 27.126  78.062 1.00 26.02 ? 567  GLU   B HG3  1 
ATOM   18111 N  N    . VAL   B 1 568 ? 1.632  27.299  82.153 1.00 19.78 ? 568  VAL   B N    1 
ATOM   18112 C  CA   . VAL   B 1 568 ? 3.014  27.069  82.662 1.00 17.06 ? 568  VAL   B CA   1 
ATOM   18113 C  C    . VAL   B 1 568 ? 3.288  25.577  82.432 1.00 15.56 ? 568  VAL   B C    1 
ATOM   18114 O  O    . VAL   B 1 568 ? 2.322  24.819  82.269 1.00 15.89 ? 568  VAL   B O    1 
ATOM   18115 C  CB   . VAL   B 1 568 ? 3.191  27.427  84.151 1.00 19.43 ? 568  VAL   B CB   1 
ATOM   18116 C  CG1  . VAL   B 1 568 ? 2.870  28.884  84.434 1.00 24.51 ? 568  VAL   B CG1  1 
ATOM   18117 C  CG2  . VAL   B 1 568 ? 2.382  26.509  85.053 1.00 22.77 ? 568  VAL   B CG2  1 
ATOM   18118 H  H    . VAL   B 1 568 ? 1.070  26.689  82.381 1.00 23.74 ? 568  VAL   B H    1 
ATOM   18119 H  HA   . VAL   B 1 568 ? 3.638  27.646  82.195 1.00 20.48 ? 568  VAL   B HA   1 
ATOM   18120 H  HB   . VAL   B 1 568 ? 4.130  27.292  84.355 1.00 23.32 ? 568  VAL   B HB   1 
ATOM   18121 H  HG11 . VAL   B 1 568 ? 2.994  29.065  85.379 1.00 29.41 ? 568  VAL   B HG11 1 
ATOM   18122 H  HG12 . VAL   B 1 568 ? 3.461  29.452  83.916 1.00 29.41 ? 568  VAL   B HG12 1 
ATOM   18123 H  HG13 . VAL   B 1 568 ? 1.950  29.066  84.188 1.00 29.41 ? 568  VAL   B HG13 1 
ATOM   18124 H  HG21 . VAL   B 1 568 ? 2.518  26.763  85.979 1.00 27.33 ? 568  VAL   B HG21 1 
ATOM   18125 H  HG22 . VAL   B 1 568 ? 1.441  26.585  84.832 1.00 27.33 ? 568  VAL   B HG22 1 
ATOM   18126 H  HG23 . VAL   B 1 568 ? 2.671  25.592  84.924 1.00 27.33 ? 568  VAL   B HG23 1 
ATOM   18127 N  N    . HIS   B 1 569 ? 4.560  25.185  82.396 1.00 15.23 ? 569  HIS   B N    1 
ATOM   18128 C  CA   . HIS   B 1 569 ? 4.901  23.761  82.156 1.00 15.61 ? 569  HIS   B CA   1 
ATOM   18129 C  C    . HIS   B 1 569 ? 4.757  22.994  83.468 1.00 17.13 ? 569  HIS   B C    1 
ATOM   18130 O  O    . HIS   B 1 569 ? 5.221  23.495  84.507 1.00 15.98 ? 569  HIS   B O    1 
ATOM   18131 C  CB   . HIS   B 1 569 ? 6.313  23.591  81.595 1.00 16.69 ? 569  HIS   B CB   1 
ATOM   18132 C  CG   . HIS   B 1 569 ? 6.546  22.193  81.142 1.00 13.30 ? 569  HIS   B CG   1 
ATOM   18133 N  ND1  . HIS   B 1 569 ? 7.226  21.264  81.897 1.00 17.39 ? 569  HIS   B ND1  1 
ATOM   18134 C  CD2  . HIS   B 1 569 ? 6.152  21.558  80.035 1.00 16.46 ? 569  HIS   B CD2  1 
ATOM   18135 C  CE1  . HIS   B 1 569 ? 7.252  20.112  81.247 1.00 15.51 ? 569  HIS   B CE1  1 
ATOM   18136 N  NE2  . HIS   B 1 569 ? 6.604  20.269  80.116 1.00 16.44 ? 569  HIS   B NE2  1 
ATOM   18137 H  H    . HIS   B 1 569 ? 5.235  25.707  82.504 1.00 18.28 ? 569  HIS   B H    1 
ATOM   18138 H  HA   . HIS   B 1 569 ? 4.291  23.409  81.490 1.00 18.74 ? 569  HIS   B HA   1 
ATOM   18139 H  HB2  . HIS   B 1 569 ? 6.444  24.201  80.852 1.00 20.03 ? 569  HIS   B HB2  1 
ATOM   18140 H  HB3  . HIS   B 1 569 ? 6.964  23.827  82.274 1.00 20.03 ? 569  HIS   B HB3  1 
ATOM   18141 H  HD2  . HIS   B 1 569 ? 5.660  21.925  79.336 1.00 19.76 ? 569  HIS   B HD2  1 
ATOM   18142 H  HE1  . HIS   B 1 569 ? 7.658  19.328  81.540 1.00 18.62 ? 569  HIS   B HE1  1 
ATOM   18143 H  HE2  . HIS   B 1 569 ? 6.483  19.660  79.521 1.00 19.74 ? 569  HIS   B HE2  1 
ATOM   18144 N  N    . ARG   B 1 570 ? 4.139  21.813  83.414 1.00 14.38 ? 570  ARG   B N    1 
ATOM   18145 C  CA   . ARG   B 1 570 ? 3.881  21.039  84.656 1.00 16.03 ? 570  ARG   B CA   1 
ATOM   18146 C  C    . ARG   B 1 570 ? 4.879  19.882  84.776 1.00 16.27 ? 570  ARG   B C    1 
ATOM   18147 O  O    . ARG   B 1 570 ? 4.434  18.732  84.881 1.00 18.02 ? 570  ARG   B O    1 
ATOM   18148 C  CB   . ARG   B 1 570 ? 2.432  20.547  84.642 1.00 17.70 ? 570  ARG   B CB   1 
ATOM   18149 C  CG   . ARG   B 1 570 ? 1.423  21.627  84.285 1.00 21.63 ? 570  ARG   B CG   1 
ATOM   18150 C  CD   . ARG   B 1 570 ? 1.122  22.521  85.471 1.00 22.48 ? 570  ARG   B CD   1 
ATOM   18151 N  NE   . ARG   B 1 570 ? 0.564  21.767  86.585 1.00 33.87 ? 570  ARG   B NE   1 
ATOM   18152 C  CZ   . ARG   B 1 570 ? -0.668 21.271  86.615 1.00 32.14 ? 570  ARG   B CZ   1 
ATOM   18153 N  NH1  . ARG   B 1 570 ? -1.521 21.549  85.646 1.00 33.78 ? 570  ARG   B NH1  1 
ATOM   18154 N  NH2  . ARG   B 1 570 ? -1.046 20.501  87.619 1.00 31.59 ? 570  ARG   B NH2  1 
ATOM   18155 H  H    . ARG   B 1 570 ? 3.862  21.440  82.690 1.00 17.26 ? 570  ARG   B H    1 
ATOM   18156 H  HA   . ARG   B 1 570 ? 4.005  21.603  85.435 1.00 19.24 ? 570  ARG   B HA   1 
ATOM   18157 H  HB2  . ARG   B 1 570 ? 2.352  19.818  84.007 1.00 21.25 ? 570  ARG   B HB2  1 
ATOM   18158 H  HB3  . ARG   B 1 570 ? 2.213  20.187  85.516 1.00 21.25 ? 570  ARG   B HB3  1 
ATOM   18159 H  HG2  . ARG   B 1 570 ? 1.767  22.163  83.553 1.00 25.96 ? 570  ARG   B HG2  1 
ATOM   18160 H  HG3  . ARG   B 1 570 ? 0.602  21.214  83.973 1.00 25.96 ? 570  ARG   B HG3  1 
ATOM   18161 H  HD2  . ARG   B 1 570 ? 1.935  22.966  85.756 1.00 26.98 ? 570  ARG   B HD2  1 
ATOM   18162 H  HD3  . ARG   B 1 570 ? 0.498  23.214  85.204 1.00 26.98 ? 570  ARG   B HD3  1 
ATOM   18163 H  HE   . ARG   B 1 570 ? 1.066  21.634  87.270 1.00 40.65 ? 570  ARG   B HE   1 
ATOM   18164 H  HH11 . ARG   B 1 570 ? -1.280 22.053  84.992 1.00 40.54 ? 570  ARG   B HH11 1 
ATOM   18165 H  HH12 . ARG   B 1 570 ? -2.318 21.226  85.669 1.00 40.54 ? 570  ARG   B HH12 1 
ATOM   18166 H  HH21 . ARG   B 1 570 ? -0.495 20.320  88.254 1.00 37.92 ? 570  ARG   B HH21 1 
ATOM   18167 H  HH22 . ARG   B 1 570 ? -1.844 20.180  87.638 1.00 37.92 ? 570  ARG   B HH22 1 
ATOM   18168 N  N    . LEU   B 1 571 ? 6.179  20.193  84.782 1.00 14.71 ? 571  LEU   B N    1 
ATOM   18169 C  CA   . LEU   B 1 571 ? 7.225  19.141  84.870 1.00 16.65 ? 571  LEU   B CA   1 
ATOM   18170 C  C    . LEU   B 1 571 ? 7.100  18.375  86.190 1.00 17.10 ? 571  LEU   B C    1 
ATOM   18171 O  O    . LEU   B 1 571 ? 7.427  17.182  86.205 1.00 17.36 ? 571  LEU   B O    1 
ATOM   18172 C  CB   . LEU   B 1 571 ? 8.597  19.813  84.775 1.00 17.17 ? 571  LEU   B CB   1 
ATOM   18173 C  CG   . LEU   B 1 571 ? 9.784  18.861  84.656 1.00 17.03 ? 571  LEU   B CG   1 
ATOM   18174 C  CD1  . LEU   B 1 571 ? 9.732  18.100  83.340 1.00 14.67 ? 571  LEU   B CD1  1 
ATOM   18175 C  CD2  . LEU   B 1 571 ? 11.096 19.619  84.783 1.00 20.26 ? 571  LEU   B CD2  1 
ATOM   18176 H  H    . LEU   B 1 571 ? 6.483  20.996  84.737 1.00 17.66 ? 571  LEU   B H    1 
ATOM   18177 H  HA   . LEU   B 1 571 ? 7.116  18.507  84.144 1.00 19.98 ? 571  LEU   B HA   1 
ATOM   18178 H  HB2  . LEU   B 1 571 ? 8.598  20.405  84.007 1.00 20.61 ? 571  LEU   B HB2  1 
ATOM   18179 H  HB3  . LEU   B 1 571 ? 8.724  20.368  85.561 1.00 20.61 ? 571  LEU   B HB3  1 
ATOM   18180 H  HG   . LEU   B 1 571 ? 9.731  18.220  85.382 1.00 20.44 ? 571  LEU   B HG   1 
ATOM   18181 H  HD11 . LEU   B 1 571 ? 10.493 17.501  83.282 1.00 17.61 ? 571  LEU   B HD11 1 
ATOM   18182 H  HD12 . LEU   B 1 571 ? 8.911  17.585  83.296 1.00 17.61 ? 571  LEU   B HD12 1 
ATOM   18183 H  HD13 . LEU   B 1 571 ? 9.759  18.728  82.601 1.00 17.61 ? 571  LEU   B HD13 1 
ATOM   18184 H  HD21 . LEU   B 1 571 ? 11.837 18.998  84.705 1.00 24.31 ? 571  LEU   B HD21 1 
ATOM   18185 H  HD22 . LEU   B 1 571 ? 11.156 20.283  84.079 1.00 24.31 ? 571  LEU   B HD22 1 
ATOM   18186 H  HD23 . LEU   B 1 571 ? 11.133 20.059  85.646 1.00 24.31 ? 571  LEU   B HD23 1 
ATOM   18187 N  N    . ASP   B 1 572 ? 6.629  19.042  87.246 1.00 19.04 ? 572  ASP   B N    1 
ATOM   18188 C  CA   . ASP   B 1 572 ? 6.575  18.401  88.589 1.00 20.74 ? 572  ASP   B CA   1 
ATOM   18189 C  C    . ASP   B 1 572 ? 5.712  17.139  88.535 1.00 21.47 ? 572  ASP   B C    1 
ATOM   18190 O  O    . ASP   B 1 572 ? 5.950  16.228  89.342 1.00 23.08 ? 572  ASP   B O    1 
ATOM   18191 C  CB   . ASP   B 1 572 ? 6.086  19.388  89.654 1.00 20.23 ? 572  ASP   B CB   1 
ATOM   18192 C  CG   . ASP   B 1 572 ? 4.675  19.902  89.423 1.00 23.12 ? 572  ASP   B CG   1 
ATOM   18193 O  OD1  . ASP   B 1 572 ? 4.268  20.009  88.253 1.00 26.66 ? 572  ASP   B OD1  1 
ATOM   18194 O  OD2  . ASP   B 1 572 ? 3.997  20.196  90.422 1.00 31.30 ? 572  ASP   B OD2  1 
ATOM   18195 H  H    . ASP   B 1 572 ? 6.339  19.851  87.220 1.00 22.86 ? 572  ASP   B H    1 
ATOM   18196 H  HA   . ASP   B 1 572 ? 7.472  18.136  88.845 1.00 24.89 ? 572  ASP   B HA   1 
ATOM   18197 H  HB2  . ASP   B 1 572 ? 6.125  18.957  90.522 1.00 24.28 ? 572  ASP   B HB2  1 
ATOM   18198 H  HB3  . ASP   B 1 572 ? 6.694  20.143  89.685 1.00 24.28 ? 572  ASP   B HB3  1 
ATOM   18199 N  N    . VAL   B 1 573 ? 4.763  17.096  87.606 1.00 19.59 ? 573  VAL   B N    1 
ATOM   18200 C  CA   . VAL   B 1 573 ? 3.850  15.924  87.490 1.00 19.30 ? 573  VAL   B CA   1 
ATOM   18201 C  C    . VAL   B 1 573 ? 4.337  14.992  86.376 1.00 20.34 ? 573  VAL   B C    1 
ATOM   18202 O  O    . VAL   B 1 573 ? 4.218  13.770  86.545 1.00 21.80 ? 573  VAL   B O    1 
ATOM   18203 C  CB   . VAL   B 1 573 ? 2.412  16.403  87.223 1.00 23.32 ? 573  VAL   B CB   1 
ATOM   18204 C  CG1  . VAL   B 1 573 ? 1.521  15.289  86.699 1.00 30.07 ? 573  VAL   B CG1  1 
ATOM   18205 C  CG2  . VAL   B 1 573 ? 1.804  17.057  88.453 1.00 28.02 ? 573  VAL   B CG2  1 
ATOM   18206 H  H    . VAL   B 1 573 ? 4.620  17.720  87.032 1.00 23.51 ? 573  VAL   B H    1 
ATOM   18207 H  HA   . VAL   B 1 573 ? 3.854  15.428  88.324 1.00 23.16 ? 573  VAL   B HA   1 
ATOM   18208 H  HB   . VAL   B 1 573 ? 2.469  17.075  86.525 1.00 27.99 ? 573  VAL   B HB   1 
ATOM   18209 H  HG11 . VAL   B 1 573 ? 0.628  15.634  86.545 1.00 36.09 ? 573  VAL   B HG11 1 
ATOM   18210 H  HG12 . VAL   B 1 573 ? 1.884  14.949  85.866 1.00 36.09 ? 573  VAL   B HG12 1 
ATOM   18211 H  HG13 . VAL   B 1 573 ? 1.482  14.572  87.351 1.00 36.09 ? 573  VAL   B HG13 1 
ATOM   18212 H  HG21 . VAL   B 1 573 ? 0.900  17.347  88.252 1.00 33.63 ? 573  VAL   B HG21 1 
ATOM   18213 H  HG22 . VAL   B 1 573 ? 1.784  16.418  89.183 1.00 33.63 ? 573  VAL   B HG22 1 
ATOM   18214 H  HG23 . VAL   B 1 573 ? 2.340  17.824  88.710 1.00 33.63 ? 573  VAL   B HG23 1 
ATOM   18215 N  N    . LEU   B 1 574 ? 4.921  15.542  85.312 1.00 16.63 ? 574  LEU   B N    1 
ATOM   18216 C  CA   . LEU   B 1 574 ? 5.284  14.704  84.137 1.00 16.54 ? 574  LEU   B CA   1 
ATOM   18217 C  C    . LEU   B 1 574 ? 6.613  13.959  84.335 1.00 15.04 ? 574  LEU   B C    1 
ATOM   18218 O  O    . LEU   B 1 574 ? 6.713  12.819  83.861 1.00 15.95 ? 574  LEU   B O    1 
ATOM   18219 C  CB   . LEU   B 1 574 ? 5.345  15.624  82.912 1.00 16.64 ? 574  LEU   B CB   1 
ATOM   18220 C  CG   . LEU   B 1 574 ? 4.059  16.383  82.592 1.00 14.94 ? 574  LEU   B CG   1 
ATOM   18221 C  CD1  . LEU   B 1 574 ? 4.329  17.515  81.612 1.00 18.70 ? 574  LEU   B CD1  1 
ATOM   18222 C  CD2  . LEU   B 1 574 ? 3.000  15.442  82.040 1.00 18.34 ? 574  LEU   B CD2  1 
ATOM   18223 H  H    . LEU   B 1 574 ? 5.117  16.376  85.239 1.00 19.95 ? 574  LEU   B H    1 
ATOM   18224 H  HA   . LEU   B 1 574 ? 4.612  14.015  84.016 1.00 19.85 ? 574  LEU   B HA   1 
ATOM   18225 H  HB2  . LEU   B 1 574 ? 6.057  16.269  83.047 1.00 19.97 ? 574  LEU   B HB2  1 
ATOM   18226 H  HB3  . LEU   B 1 574 ? 5.588  15.091  82.139 1.00 19.97 ? 574  LEU   B HB3  1 
ATOM   18227 H  HG   . LEU   B 1 574 ? 3.725  16.768  83.417 1.00 17.93 ? 574  LEU   B HG   1 
ATOM   18228 H  HD11 . LEU   B 1 574 ? 3.501  17.983  81.422 1.00 22.44 ? 574  LEU   B HD11 1 
ATOM   18229 H  HD12 . LEU   B 1 574 ? 4.968  18.133  81.999 1.00 22.44 ? 574  LEU   B HD12 1 
ATOM   18230 H  HD13 . LEU   B 1 574 ? 4.690  17.151  80.788 1.00 22.44 ? 574  LEU   B HD13 1 
ATOM   18231 H  HD21 . LEU   B 1 574 ? 2.193  15.943  81.844 1.00 22.01 ? 574  LEU   B HD21 1 
ATOM   18232 H  HD22 . LEU   B 1 574 ? 3.328  15.026  81.227 1.00 22.01 ? 574  LEU   B HD22 1 
ATOM   18233 H  HD23 . LEU   B 1 574 ? 2.803  14.756  82.697 1.00 22.01 ? 574  LEU   B HD23 1 
ATOM   18234 N  N    . LEU   B 1 575 ? 7.594  14.579  84.988 1.00 14.38 ? 575  LEU   B N    1 
ATOM   18235 C  CA   . LEU   B 1 575 ? 8.935  13.942  85.099 1.00 17.07 ? 575  LEU   B CA   1 
ATOM   18236 C  C    . LEU   B 1 575 ? 8.862  12.593  85.836 1.00 17.28 ? 575  LEU   B C    1 
ATOM   18237 O  O    . LEU   B 1 575 ? 9.462  11.627  85.340 1.00 16.63 ? 575  LEU   B O    1 
ATOM   18238 C  CB   . LEU   B 1 575 ? 9.913  14.900  85.788 1.00 17.54 ? 575  LEU   B CB   1 
ATOM   18239 C  CG   . LEU   B 1 575 ? 11.358 14.410  85.855 1.00 17.95 ? 575  LEU   B CG   1 
ATOM   18240 C  CD1  . LEU   B 1 575 ? 11.885 14.096  84.464 1.00 15.50 ? 575  LEU   B CD1  1 
ATOM   18241 C  CD2  . LEU   B 1 575 ? 12.246 15.432  86.543 1.00 20.97 ? 575  LEU   B CD2  1 
ATOM   18242 H  H    . LEU   B 1 575 ? 7.521  15.347  85.368 1.00 17.26 ? 575  LEU   B H    1 
ATOM   18243 H  HA   . LEU   B 1 575 ? 9.260  13.757  84.204 1.00 20.49 ? 575  LEU   B HA   1 
ATOM   18244 H  HB2  . LEU   B 1 575 ? 9.895  15.750  85.321 1.00 21.05 ? 575  LEU   B HB2  1 
ATOM   18245 H  HB3  . LEU   B 1 575 ? 9.600  15.066  86.691 1.00 21.05 ? 575  LEU   B HB3  1 
ATOM   18246 H  HG   . LEU   B 1 575 ? 11.373 13.594  86.379 1.00 21.54 ? 575  LEU   B HG   1 
ATOM   18247 H  HD11 . LEU   B 1 575 ? 12.802 13.787  84.527 1.00 18.60 ? 575  LEU   B HD11 1 
ATOM   18248 H  HD12 . LEU   B 1 575 ? 11.338 13.404  84.059 1.00 18.60 ? 575  LEU   B HD12 1 
ATOM   18249 H  HD13 . LEU   B 1 575 ? 11.851 14.896  83.917 1.00 18.60 ? 575  LEU   B HD13 1 
ATOM   18250 H  HD21 . LEU   B 1 575 ? 13.157 15.101  86.574 1.00 25.17 ? 575  LEU   B HD21 1 
ATOM   18251 H  HD22 . LEU   B 1 575 ? 12.223 16.266  86.049 1.00 25.17 ? 575  LEU   B HD22 1 
ATOM   18252 H  HD23 . LEU   B 1 575 ? 11.926 15.583  87.446 1.00 25.17 ? 575  LEU   B HD23 1 
ATOM   18253 N  N    . PRO   B 1 576 ? 8.191  12.477  87.001 1.00 16.65 ? 576  PRO   B N    1 
ATOM   18254 C  CA   . PRO   B 1 576 ? 8.102  11.190  87.685 1.00 18.67 ? 576  PRO   B CA   1 
ATOM   18255 C  C    . PRO   B 1 576 ? 7.513  10.109  86.769 1.00 18.69 ? 576  PRO   B C    1 
ATOM   18256 O  O    . PRO   B 1 576 ? 8.021  9.011   86.758 1.00 18.69 ? 576  PRO   B O    1 
ATOM   18257 C  CB   . PRO   B 1 576 ? 7.141  11.476  88.848 1.00 22.58 ? 576  PRO   B CB   1 
ATOM   18258 C  CG   . PRO   B 1 576 ? 7.301  12.955  89.106 1.00 25.35 ? 576  PRO   B CG   1 
ATOM   18259 C  CD   . PRO   B 1 576 ? 7.519  13.554  87.734 1.00 17.73 ? 576  PRO   B CD   1 
ATOM   18260 H  HA   . PRO   B 1 576 ? 8.969  10.858  87.966 1.00 22.41 ? 576  PRO   B HA   1 
ATOM   18261 H  HB2  . PRO   B 1 576 ? 6.226  11.254  88.614 1.00 27.10 ? 576  PRO   B HB2  1 
ATOM   18262 H  HB3  . PRO   B 1 576 ? 7.368  10.953  89.632 1.00 27.10 ? 576  PRO   B HB3  1 
ATOM   18263 H  HG2  . PRO   B 1 576 ? 6.513  13.327  89.533 1.00 30.43 ? 576  PRO   B HG2  1 
ATOM   18264 H  HG3  . PRO   B 1 576 ? 8.053  13.132  89.693 1.00 30.43 ? 576  PRO   B HG3  1 
ATOM   18265 H  HD2  . PRO   B 1 576 ? 6.681  13.804  87.315 1.00 21.28 ? 576  PRO   B HD2  1 
ATOM   18266 H  HD3  . PRO   B 1 576 ? 8.065  14.355  87.775 1.00 21.28 ? 576  PRO   B HD3  1 
ATOM   18267 N  N    . GLU   B 1 577 ? 6.464  10.459  86.024 1.00 17.68 ? 577  GLU   B N    1 
ATOM   18268 C  CA   . GLU   B 1 577 ? 5.816  9.481   85.110 1.00 20.94 ? 577  GLU   B CA   1 
ATOM   18269 C  C    . GLU   B 1 577 ? 6.783  9.112   83.977 1.00 16.31 ? 577  GLU   B C    1 
ATOM   18270 O  O    . GLU   B 1 577 ? 6.774  7.956   83.542 1.00 19.92 ? 577  GLU   B O    1 
ATOM   18271 C  CB   . GLU   B 1 577 ? 4.497  10.036  84.573 1.00 21.92 ? 577  GLU   B CB   1 
ATOM   18272 C  CG   . GLU   B 1 577 ? 3.766  9.076   83.651 1.00 26.96 ? 577  GLU   B CG   1 
ATOM   18273 C  CD   . GLU   B 1 577 ? 3.207  7.829   84.316 1.00 37.67 ? 577  GLU   B CD   1 
ATOM   18274 O  OE1  . GLU   B 1 577 ? 3.265  7.744   85.558 1.00 39.63 ? 577  GLU   B OE1  1 
ATOM   18275 O  OE2  . GLU   B 1 577 ? 2.713  6.947   83.590 1.00 33.95 ? 577  GLU   B OE2  1 
ATOM   18276 H  H    . GLU   B 1 577 ? 6.109  11.242  86.024 1.00 21.22 ? 577  GLU   B H    1 
ATOM   18277 H  HA   . GLU   B 1 577 ? 5.606  8.672   85.602 1.00 25.13 ? 577  GLU   B HA   1 
ATOM   18278 H  HB2  . GLU   B 1 577 ? 3.920  10.258  85.320 1.00 26.31 ? 577  GLU   B HB2  1 
ATOM   18279 H  HB3  . GLU   B 1 577 ? 4.673  10.862  84.095 1.00 26.31 ? 577  GLU   B HB3  1 
ATOM   18280 H  HG2  . GLU   B 1 577 ? 3.035  9.553   83.227 1.00 32.36 ? 577  GLU   B HG2  1 
ATOM   18281 H  HG3  . GLU   B 1 577 ? 4.374  8.803   82.946 1.00 32.36 ? 577  GLU   B HG3  1 
ATOM   18282 N  N    . TYR   B 1 578 ? 7.607  10.066  83.541 1.00 15.20 ? 578  TYR   B N    1 
ATOM   18283 C  CA   . TYR   B 1 578 ? 8.604  9.753   82.487 1.00 14.66 ? 578  TYR   B CA   1 
ATOM   18284 C  C    . TYR   B 1 578 ? 9.587  8.691   82.999 1.00 15.30 ? 578  TYR   B C    1 
ATOM   18285 O  O    . TYR   B 1 578 ? 9.820  7.698   82.299 1.00 14.68 ? 578  TYR   B O    1 
ATOM   18286 C  CB   . TYR   B 1 578 ? 9.335  11.021  82.034 1.00 12.96 ? 578  TYR   B CB   1 
ATOM   18287 C  CG   . TYR   B 1 578 ? 10.356 10.769  80.954 1.00 15.63 ? 578  TYR   B CG   1 
ATOM   18288 C  CD1  . TYR   B 1 578 ? 9.971  10.584  79.637 1.00 15.72 ? 578  TYR   B CD1  1 
ATOM   18289 C  CD2  . TYR   B 1 578 ? 11.703 10.680  81.254 1.00 15.32 ? 578  TYR   B CD2  1 
ATOM   18290 C  CE1  . TYR   B 1 578 ? 10.901 10.337  78.641 1.00 16.29 ? 578  TYR   B CE1  1 
ATOM   18291 C  CE2  . TYR   B 1 578 ? 12.646 10.435  80.271 1.00 13.19 ? 578  TYR   B CE2  1 
ATOM   18292 C  CZ   . TYR   B 1 578 ? 12.244 10.262  78.960 1.00 15.54 ? 578  TYR   B CZ   1 
ATOM   18293 O  OH   . TYR   B 1 578 ? 13.182 10.016  77.989 1.00 13.93 ? 578  TYR   B OH   1 
ATOM   18294 H  H    . TYR   B 1 578 ? 7.615  10.878  83.825 1.00 18.25 ? 578  TYR   B H    1 
ATOM   18295 H  HA   . TYR   B 1 578 ? 8.143  9.394   81.713 1.00 17.60 ? 578  TYR   B HA   1 
ATOM   18296 H  HB2  . TYR   B 1 578 ? 8.684  11.664  81.711 1.00 15.56 ? 578  TYR   B HB2  1 
ATOM   18297 H  HB3  . TYR   B 1 578 ? 9.775  11.423  82.799 1.00 15.56 ? 578  TYR   B HB3  1 
ATOM   18298 H  HD1  . TYR   B 1 578 ? 9.069  10.627  79.416 1.00 18.87 ? 578  TYR   B HD1  1 
ATOM   18299 H  HD2  . TYR   B 1 578 ? 11.981 10.787  82.135 1.00 18.39 ? 578  TYR   B HD2  1 
ATOM   18300 H  HE1  . TYR   B 1 578 ? 10.623 10.222  77.761 1.00 19.55 ? 578  TYR   B HE1  1 
ATOM   18301 H  HE2  . TYR   B 1 578 ? 13.548 10.387  80.492 1.00 15.83 ? 578  TYR   B HE2  1 
ATOM   18302 H  HH   . TYR   B 1 578 ? 13.069 10.548  77.349 1.00 16.72 ? 578  TYR   B HH   1 
ATOM   18303 N  N    . TYR   B 1 579 ? 10.154 8.917   84.183 1.00 15.15 ? 579  TYR   B N    1 
ATOM   18304 C  CA   . TYR   B 1 579 ? 11.095 7.930   84.766 1.00 17.52 ? 579  TYR   B CA   1 
ATOM   18305 C  C    . TYR   B 1 579 ? 10.383 6.580   84.869 1.00 17.04 ? 579  TYR   B C    1 
ATOM   18306 O  O    . TYR   B 1 579 ? 10.987 5.545   84.554 1.00 16.91 ? 579  TYR   B O    1 
ATOM   18307 C  CB   . TYR   B 1 579 ? 11.571 8.388   86.144 1.00 15.83 ? 579  TYR   B CB   1 
ATOM   18308 C  CG   . TYR   B 1 579 ? 12.476 9.593   86.172 1.00 17.11 ? 579  TYR   B CG   1 
ATOM   18309 C  CD1  . TYR   B 1 579 ? 13.184 9.994   85.051 1.00 16.25 ? 579  TYR   B CD1  1 
ATOM   18310 C  CD2  . TYR   B 1 579 ? 12.633 10.328  87.333 1.00 18.09 ? 579  TYR   B CD2  1 
ATOM   18311 C  CE1  . TYR   B 1 579 ? 14.021 11.098  85.085 1.00 18.38 ? 579  TYR   B CE1  1 
ATOM   18312 C  CE2  . TYR   B 1 579 ? 13.464 11.434  87.384 1.00 18.17 ? 579  TYR   B CE2  1 
ATOM   18313 C  CZ   . TYR   B 1 579 ? 14.160 11.822  86.255 1.00 16.52 ? 579  TYR   B CZ   1 
ATOM   18314 O  OH   . TYR   B 1 579 ? 14.981 12.921  86.312 1.00 18.59 ? 579  TYR   B OH   1 
ATOM   18315 H  H    . TYR   B 1 579 ? 10.018 9.617   84.664 1.00 18.18 ? 579  TYR   B H    1 
ATOM   18316 H  HA   . TYR   B 1 579 ? 11.875 7.848   84.196 1.00 21.03 ? 579  TYR   B HA   1 
ATOM   18317 H  HB2  . TYR   B 1 579 ? 10.791 8.581   86.687 1.00 19.00 ? 579  TYR   B HB2  1 
ATOM   18318 H  HB3  . TYR   B 1 579 ? 12.035 7.649   86.567 1.00 19.00 ? 579  TYR   B HB3  1 
ATOM   18319 H  HD1  . TYR   B 1 579 ? 13.096 9.513   84.260 1.00 19.51 ? 579  TYR   B HD1  1 
ATOM   18320 H  HD2  . TYR   B 1 579 ? 12.169 10.073  88.098 1.00 21.71 ? 579  TYR   B HD2  1 
ATOM   18321 H  HE1  . TYR   B 1 579 ? 14.489 11.352  84.322 1.00 22.06 ? 579  TYR   B HE1  1 
ATOM   18322 H  HE2  . TYR   B 1 579 ? 13.554 11.914  88.175 1.00 21.81 ? 579  TYR   B HE2  1 
ATOM   18323 H  HH   . TYR   B 1 579 ? 15.312 13.064  85.553 1.00 22.31 ? 579  TYR   B HH   1 
ATOM   18324 N  N    . SER   B 1 580 ? 9.119  6.611   85.290 1.00 16.41 ? 580  SER   B N    1 
ATOM   18325 C  CA   . SER   B 1 580 ? 8.369  5.346   85.492 1.00 18.32 ? 580  SER   B CA   1 
ATOM   18326 C  C    . SER   B 1 580 ? 8.211  4.597   84.168 1.00 17.51 ? 580  SER   B C    1 
ATOM   18327 O  O    . SER   B 1 580 ? 8.520  3.401   84.130 1.00 20.42 ? 580  SER   B O    1 
ATOM   18328 C  CB   . SER   B 1 580 ? 7.026  5.594   86.136 1.00 22.66 ? 580  SER   B CB   1 
ATOM   18329 O  OG   . SER   B 1 580 ? 6.395  4.367   86.467 1.00 22.79 ? 580  SER   B OG   1 
ATOM   18330 H  H    . SER   B 1 580 ? 8.678  7.329   85.463 1.00 19.70 ? 580  SER   B H    1 
ATOM   18331 H  HA   . SER   B 1 580 ? 8.883  4.791   86.099 1.00 21.99 ? 580  SER   B HA   1 
ATOM   18332 H  HB2  . SER   B 1 580 ? 7.140  6.131   86.936 1.00 27.19 ? 580  SER   B HB2  1 
ATOM   18333 H  HB3  . SER   B 1 580 ? 6.461  6.101   85.532 1.00 27.19 ? 580  SER   B HB3  1 
ATOM   18334 H  HG   . SER   B 1 580 ? 5.991  4.069   85.793 1.00 27.36 ? 580  SER   B HG   1 
ATOM   18335 N  N    . VAL   B 1 581 ? 7.725  5.282   83.137 1.00 16.58 ? 581  VAL   B N    1 
ATOM   18336 C  CA   . VAL   B 1 581 ? 7.474  4.594   81.839 1.00 19.26 ? 581  VAL   B CA   1 
ATOM   18337 C  C    . VAL   B 1 581 ? 8.809  4.086   81.276 1.00 18.09 ? 581  VAL   B C    1 
ATOM   18338 O  O    . VAL   B 1 581 ? 8.794  3.103   80.526 1.00 19.56 ? 581  VAL   B O    1 
ATOM   18339 C  CB   . VAL   B 1 581 ? 6.729  5.504   80.845 1.00 22.51 ? 581  VAL   B CB   1 
ATOM   18340 C  CG1  . VAL   B 1 581 ? 5.374  5.932   81.389 1.00 24.92 ? 581  VAL   B CG1  1 
ATOM   18341 C  CG2  . VAL   B 1 581 ? 7.551  6.715   80.436 1.00 18.40 ? 581  VAL   B CG2  1 
ATOM   18342 H  H    . VAL   B 1 581 ? 7.534  6.120   83.150 1.00 19.90 ? 581  VAL   B H    1 
ATOM   18343 H  HA   . VAL   B 1 581 ? 6.890  3.834   81.988 1.00 23.11 ? 581  VAL   B HA   1 
ATOM   18344 H  HB   . VAL   B 1 581 ? 6.583  4.974   80.046 1.00 27.02 ? 581  VAL   B HB   1 
ATOM   18345 H  HG11 . VAL   B 1 581 ? 4.931  6.503   80.742 1.00 29.91 ? 581  VAL   B HG11 1 
ATOM   18346 H  HG12 . VAL   B 1 581 ? 4.829  5.147   81.554 1.00 29.91 ? 581  VAL   B HG12 1 
ATOM   18347 H  HG13 . VAL   B 1 581 ? 5.497  6.420   82.218 1.00 29.91 ? 581  VAL   B HG13 1 
ATOM   18348 H  HG21 . VAL   B 1 581 ? 7.042  7.256   79.812 1.00 22.08 ? 581  VAL   B HG21 1 
ATOM   18349 H  HG22 . VAL   B 1 581 ? 7.764  7.242   81.222 1.00 22.08 ? 581  VAL   B HG22 1 
ATOM   18350 H  HG23 . VAL   B 1 581 ? 8.373  6.421   80.013 1.00 22.08 ? 581  VAL   B HG23 1 
ATOM   18351 N  N    . ARG   B 1 582 ? 9.915  4.727   81.651 1.00 15.72 ? 582  ARG   B N    1 
ATOM   18352 C  CA   . ARG   B 1 582 ? 11.238 4.328   81.106 1.00 15.31 ? 582  ARG   B CA   1 
ATOM   18353 C  C    . ARG   B 1 582 ? 11.762 3.115   81.871 1.00 16.50 ? 582  ARG   B C    1 
ATOM   18354 O  O    . ARG   B 1 582 ? 12.765 2.538   81.431 1.00 18.99 ? 582  ARG   B O    1 
ATOM   18355 C  CB   . ARG   B 1 582 ? 12.237 5.479   81.236 1.00 14.67 ? 582  ARG   B CB   1 
ATOM   18356 C  CG   . ARG   B 1 582 ? 12.069 6.569   80.188 1.00 15.79 ? 582  ARG   B CG   1 
ATOM   18357 C  CD   . ARG   B 1 582 ? 13.401 7.039   79.638 1.00 14.83 ? 582  ARG   B CD   1 
ATOM   18358 N  NE   . ARG   B 1 582 ? 13.988 6.079   78.716 1.00 18.14 ? 582  ARG   B NE   1 
ATOM   18359 C  CZ   . ARG   B 1 582 ? 13.925 6.171   77.394 1.00 16.13 ? 582  ARG   B CZ   1 
ATOM   18360 N  NH1  . ARG   B 1 582 ? 13.427 7.256   76.828 1.00 17.52 ? 582  ARG   B NH1  1 
ATOM   18361 N  NH2  . ARG   B 1 582 ? 14.363 5.176   76.642 1.00 16.41 ? 582  ARG   B NH2  1 
ATOM   18362 H  H    . ARG   B 1 582 ? 9.934  5.383   82.207 1.00 18.86 ? 582  ARG   B H    1 
ATOM   18363 H  HA   . ARG   B 1 582 ? 11.134 4.105   80.168 1.00 18.38 ? 582  ARG   B HA   1 
ATOM   18364 H  HB2  . ARG   B 1 582 ? 12.147 5.874   82.117 1.00 17.61 ? 582  ARG   B HB2  1 
ATOM   18365 H  HB3  . ARG   B 1 582 ? 13.137 5.122   81.176 1.00 17.61 ? 582  ARG   B HB3  1 
ATOM   18366 H  HG2  . ARG   B 1 582 ? 11.520 6.236   79.461 1.00 18.95 ? 582  ARG   B HG2  1 
ATOM   18367 H  HG3  . ARG   B 1 582 ? 11.598 7.322   80.578 1.00 18.95 ? 582  ARG   B HG3  1 
ATOM   18368 H  HD2  . ARG   B 1 582 ? 13.280 7.888   79.184 1.00 17.80 ? 582  ARG   B HD2  1 
ATOM   18369 H  HD3  . ARG   B 1 582 ? 14.015 7.195   80.373 1.00 17.80 ? 582  ARG   B HD3  1 
ATOM   18370 H  HE   . ARG   B 1 582 ? 14.405 5.405   79.051 1.00 21.77 ? 582  ARG   B HE   1 
ATOM   18371 H  HH11 . ARG   B 1 582 ? 13.143 7.904   77.317 1.00 21.03 ? 582  ARG   B HH11 1 
ATOM   18372 H  HH12 . ARG   B 1 582 ? 13.387 7.314   75.971 1.00 21.03 ? 582  ARG   B HH12 1 
ATOM   18373 H  HH21 . ARG   B 1 582 ? 14.688 4.470   77.010 1.00 19.70 ? 582  ARG   B HH21 1 
ATOM   18374 H  HH22 . ARG   B 1 582 ? 14.323 5.235   75.785 1.00 19.70 ? 582  ARG   B HH22 1 
ATOM   18375 N  N    . GLY   B 1 583 ? 11.111 2.744   82.975 1.00 17.22 ? 583  GLY   B N    1 
ATOM   18376 C  CA   . GLY   B 1 583 ? 11.646 1.647   83.802 1.00 18.91 ? 583  GLY   B CA   1 
ATOM   18377 C  C    . GLY   B 1 583 ? 12.834 2.130   84.610 1.00 22.40 ? 583  GLY   B C    1 
ATOM   18378 O  O    . GLY   B 1 583 ? 13.755 1.333   84.843 1.00 19.99 ? 583  GLY   B O    1 
ATOM   18379 H  H    . GLY   B 1 583 ? 10.381 3.098   83.260 1.00 20.67 ? 583  GLY   B H    1 
ATOM   18380 H  HA2  . GLY   B 1 583 ? 10.955 1.315   84.397 1.00 22.70 ? 583  GLY   B HA2  1 
ATOM   18381 H  HA3  . GLY   B 1 583 ? 11.912 0.906   83.235 1.00 22.70 ? 583  GLY   B HA3  1 
ATOM   18382 N  N    . TRP   B 1 584 ? 12.807 3.402   85.008 1.00 17.40 ? 584  TRP   B N    1 
ATOM   18383 C  CA   . TRP   B 1 584 ? 13.898 3.982   85.825 1.00 18.22 ? 584  TRP   B CA   1 
ATOM   18384 C  C    . TRP   B 1 584 ? 13.393 4.209   87.252 1.00 21.18 ? 584  TRP   B C    1 
ATOM   18385 O  O    . TRP   B 1 584 ? 12.168 4.178   87.452 1.00 21.49 ? 584  TRP   B O    1 
ATOM   18386 C  CB   . TRP   B 1 584 ? 14.402 5.293   85.204 1.00 18.00 ? 584  TRP   B CB   1 
ATOM   18387 C  CG   . TRP   B 1 584 ? 15.030 5.154   83.851 1.00 17.36 ? 584  TRP   B CG   1 
ATOM   18388 C  CD1  . TRP   B 1 584 ? 15.201 4.010   83.129 1.00 19.27 ? 584  TRP   B CD1  1 
ATOM   18389 C  CD2  . TRP   B 1 584 ? 15.570 6.218   83.047 1.00 17.52 ? 584  TRP   B CD2  1 
ATOM   18390 N  NE1  . TRP   B 1 584 ? 15.812 4.286   81.935 1.00 17.52 ? 584  TRP   B NE1  1 
ATOM   18391 C  CE2  . TRP   B 1 584 ? 16.049 5.633   81.856 1.00 17.19 ? 584  TRP   B CE2  1 
ATOM   18392 C  CE3  . TRP   B 1 584 ? 15.695 7.600   83.218 1.00 17.67 ? 584  TRP   B CE3  1 
ATOM   18393 C  CZ2  . TRP   B 1 584 ? 16.643 6.386   80.845 1.00 15.23 ? 584  TRP   B CZ2  1 
ATOM   18394 C  CZ3  . TRP   B 1 584 ? 16.280 8.344   82.217 1.00 17.19 ? 584  TRP   B CZ3  1 
ATOM   18395 C  CH2  . TRP   B 1 584 ? 16.746 7.743   81.049 1.00 14.91 ? 584  TRP   B CH2  1 
ATOM   18396 H  H    . TRP   B 1 584 ? 12.172 3.951   84.821 1.00 20.88 ? 584  TRP   B H    1 
ATOM   18397 H  HA   . TRP   B 1 584 ? 14.645 3.364   85.849 1.00 21.87 ? 584  TRP   B HA   1 
ATOM   18398 H  HB2  . TRP   B 1 584 ? 13.657 5.911   85.138 1.00 21.61 ? 584  TRP   B HB2  1 
ATOM   18399 H  HB3  . TRP   B 1 584 ? 15.049 5.692   85.806 1.00 21.61 ? 584  TRP   B HB3  1 
ATOM   18400 H  HD1  . TRP   B 1 584 ? 14.940 3.162   83.408 1.00 23.13 ? 584  TRP   B HD1  1 
ATOM   18401 H  HE1  . TRP   B 1 584 ? 16.014 3.707   81.332 1.00 21.03 ? 584  TRP   B HE1  1 
ATOM   18402 H  HE3  . TRP   B 1 584 ? 15.388 8.010   83.994 1.00 21.21 ? 584  TRP   B HE3  1 
ATOM   18403 H  HZ2  . TRP   B 1 584 ? 16.957 5.988   80.065 1.00 18.27 ? 584  TRP   B HZ2  1 
ATOM   18404 H  HZ3  . TRP   B 1 584 ? 16.366 9.264   82.323 1.00 20.63 ? 584  TRP   B HZ3  1 
ATOM   18405 H  HH2  . TRP   B 1 584 ? 17.136 8.272   80.391 1.00 17.90 ? 584  TRP   B HH2  1 
ATOM   18406 N  N    . SER   B 1 585 ? 14.309 4.445   88.189 1.00 18.82 ? 585  SER   B N    1 
ATOM   18407 C  CA   . SER   B 1 585 ? 13.936 4.698   89.601 1.00 23.57 ? 585  SER   B CA   1 
ATOM   18408 C  C    . SER   B 1 585 ? 13.230 6.046   89.729 1.00 22.07 ? 585  SER   B C    1 
ATOM   18409 O  O    . SER   B 1 585 ? 13.222 6.809   88.749 1.00 22.65 ? 585  SER   B O    1 
ATOM   18410 C  CB   . SER   B 1 585 ? 15.164 4.668   90.470 1.00 20.94 ? 585  SER   B CB   1 
ATOM   18411 O  OG   . SER   B 1 585 ? 15.852 5.905   90.423 1.00 21.02 ? 585  SER   B OG   1 
ATOM   18412 H  H    . SER   B 1 585 ? 15.155 4.465   88.037 1.00 22.58 ? 585  SER   B H    1 
ATOM   18413 H  HA   . SER   B 1 585 ? 13.327 4.002   89.894 1.00 28.29 ? 585  SER   B HA   1 
ATOM   18414 H  HB2  . SER   B 1 585 ? 14.911 4.470   91.385 1.00 25.13 ? 585  SER   B HB2  1 
ATOM   18415 H  HB3  . SER   B 1 585 ? 15.753 3.955   90.178 1.00 25.13 ? 585  SER   B HB3  1 
ATOM   18416 H  HG   . SER   B 1 585 ? 16.458 5.911   91.004 1.00 25.22 ? 585  SER   B HG   1 
ATOM   18417 N  N    . LYS   B 1 586 ? 12.675 6.330   90.908 1.00 24.61 ? 586  LYS   B N    1 
ATOM   18418 C  CA   . LYS   B 1 586 ? 12.060 7.659   91.150 1.00 21.18 ? 586  LYS   B CA   1 
ATOM   18419 C  C    . LYS   B 1 586 ? 13.170 8.715   91.154 1.00 25.63 ? 586  LYS   B C    1 
ATOM   18420 O  O    . LYS   B 1 586 ? 12.842 9.904   91.033 1.00 29.25 ? 586  LYS   B O    1 
ATOM   18421 C  CB   . LYS   B 1 586 ? 11.283 7.649   92.470 1.00 26.87 ? 586  LYS   B CB   1 
ATOM   18422 C  CG   . LYS   B 1 586 ? 9.977  6.867   92.440 1.00 29.88 ? 586  LYS   B CG   1 
ATOM   18423 C  CD   . LYS   B 1 586 ? 9.125  7.064   93.676 1.00 40.94 ? 586  LYS   B CD   1 
ATOM   18424 C  CE   . LYS   B 1 586 ? 7.863  6.228   93.658 1.00 44.62 ? 586  LYS   B CE   1 
ATOM   18425 N  NZ   . LYS   B 1 586 ? 7.070  6.402   94.898 1.00 55.08 ? 586  LYS   B NZ   1 
ATOM   18426 H  H    . LYS   B 1 586 ? 12.639 5.787   91.574 1.00 29.54 ? 586  LYS   B H    1 
ATOM   18427 H  HA   . LYS   B 1 586 ? 11.427 7.872   90.447 1.00 25.42 ? 586  LYS   B HA   1 
ATOM   18428 H  HB2  . LYS   B 1 586 ? 11.852 7.277   93.162 1.00 32.25 ? 586  LYS   B HB2  1 
ATOM   18429 H  HB3  . LYS   B 1 586 ? 11.090 8.565   92.724 1.00 32.25 ? 586  LYS   B HB3  1 
ATOM   18430 H  HG2  . LYS   B 1 586 ? 9.467  7.133   91.659 1.00 35.86 ? 586  LYS   B HG2  1 
ATOM   18431 H  HG3  . LYS   B 1 586 ? 10.176 5.923   92.341 1.00 35.86 ? 586  LYS   B HG3  1 
ATOM   18432 H  HD2  . LYS   B 1 586 ? 9.646  6.838   94.462 1.00 49.14 ? 586  LYS   B HD2  1 
ATOM   18433 H  HD3  . LYS   B 1 586 ? 8.886  8.001   93.753 1.00 49.14 ? 586  LYS   B HD3  1 
ATOM   18434 H  HE2  . LYS   B 1 586 ? 7.323  6.475   92.891 1.00 53.55 ? 586  LYS   B HE2  1 
ATOM   18435 H  HE3  . LYS   B 1 586 ? 8.096  5.292   93.552 1.00 53.55 ? 586  LYS   B HE3  1 
ATOM   18436 H  HZ1  . LYS   B 1 586 ? 6.337  5.899   94.855 1.00 66.10 ? 586  LYS   B HZ1  1 
ATOM   18437 H  HZ2  . LYS   B 1 586 ? 7.558  6.155   95.600 1.00 66.10 ? 586  LYS   B HZ2  1 
ATOM   18438 H  HZ3  . LYS   B 1 586 ? 6.837  7.257   94.984 1.00 66.10 ? 586  LYS   B HZ3  1 
ATOM   18439 N  N    . GLU   B 1 587 ? 14.431 8.286   91.267 1.00 24.58 ? 587  GLU   B N    1 
ATOM   18440 C  CA   . GLU   B 1 587 ? 15.576 9.235   91.200 1.00 23.26 ? 587  GLU   B CA   1 
ATOM   18441 C  C    . GLU   B 1 587 ? 16.141 9.266   89.773 1.00 21.49 ? 587  GLU   B C    1 
ATOM   18442 O  O    . GLU   B 1 587 ? 17.204 9.869   89.586 1.00 21.22 ? 587  GLU   B O    1 
ATOM   18443 C  CB   . GLU   B 1 587 ? 16.661 8.833   92.200 1.00 24.37 ? 587  GLU   B CB   1 
ATOM   18444 C  CG   . GLU   B 1 587 ? 16.202 8.891   93.644 1.00 33.23 ? 587  GLU   B CG   1 
ATOM   18445 C  CD   . GLU   B 1 587 ? 15.304 7.748   94.083 1.00 35.83 ? 587  GLU   B CD   1 
ATOM   18446 O  OE1  . GLU   B 1 587 ? 15.499 6.620   93.591 1.00 38.42 ? 587  GLU   B OE1  1 
ATOM   18447 O  OE2  . GLU   B 1 587 ? 14.409 7.991   94.914 1.00 44.61 ? 587  GLU   B OE2  1 
ATOM   18448 H  H    . GLU   B 1 587 ? 14.653 7.463   91.382 1.00 29.50 ? 587  GLU   B H    1 
ATOM   18449 H  HA   . GLU   B 1 587 ? 15.265 10.124  91.433 1.00 27.92 ? 587  GLU   B HA   1 
ATOM   18450 H  HB2  . GLU   B 1 587 ? 16.959 7.932   91.999 1.00 29.24 ? 587  GLU   B HB2  1 
ATOM   18451 H  HB3  . GLU   B 1 587 ? 17.427 9.417   92.088 1.00 29.24 ? 587  GLU   B HB3  1 
ATOM   18452 H  HG2  . GLU   B 1 587 ? 16.985 8.907   94.217 1.00 39.88 ? 587  GLU   B HG2  1 
ATOM   18453 H  HG3  . GLU   B 1 587 ? 15.730 9.727   93.785 1.00 39.88 ? 587  GLU   B HG3  1 
ATOM   18454 N  N    . GLY   B 1 588 ? 15.464 8.623   88.822 1.00 17.99 ? 588  GLY   B N    1 
ATOM   18455 C  CA   . GLY   B 1 588 ? 15.897 8.674   87.411 1.00 19.66 ? 588  GLY   B CA   1 
ATOM   18456 C  C    . GLY   B 1 588 ? 17.075 7.763   87.113 1.00 22.52 ? 588  GLY   B C    1 
ATOM   18457 O  O    . GLY   B 1 588 ? 17.819 8.059   86.170 1.00 23.27 ? 588  GLY   B O    1 
ATOM   18458 H  H    . GLY   B 1 588 ? 14.757 8.154   88.964 1.00 21.60 ? 588  GLY   B H    1 
ATOM   18459 H  HA2  . GLY   B 1 588 ? 15.152 8.427   86.841 1.00 23.60 ? 588  GLY   B HA2  1 
ATOM   18460 H  HA3  . GLY   B 1 588 ? 16.136 9.586   87.185 1.00 23.60 ? 588  GLY   B HA3  1 
ATOM   18461 N  N    . ILE   B 1 589 ? 17.216 6.675   87.869 1.00 18.58 ? 589  ILE   B N    1 
ATOM   18462 C  CA   . ILE   B 1 589 ? 18.328 5.707   87.639 1.00 18.82 ? 589  ILE   B CA   1 
ATOM   18463 C  C    . ILE   B 1 589 ? 17.761 4.428   87.015 1.00 18.57 ? 589  ILE   B C    1 
ATOM   18464 O  O    . ILE   B 1 589 ? 16.889 3.802   87.627 1.00 18.97 ? 589  ILE   B O    1 
ATOM   18465 C  CB   . ILE   B 1 589 ? 19.084 5.423   88.952 1.00 21.11 ? 589  ILE   B CB   1 
ATOM   18466 C  CG1  . ILE   B 1 589 ? 19.423 6.717   89.694 1.00 23.01 ? 589  ILE   B CG1  1 
ATOM   18467 C  CG2  . ILE   B 1 589 ? 20.320 4.579   88.687 1.00 22.67 ? 589  ILE   B CG2  1 
ATOM   18468 C  CD1  . ILE   B 1 589 ? 20.322 7.646   88.915 1.00 24.03 ? 589  ILE   B CD1  1 
ATOM   18469 H  H    . ILE   B 1 589 ? 16.691 6.468   88.518 1.00 22.30 ? 589  ILE   B H    1 
ATOM   18470 H  HA   . ILE   B 1 589 ? 18.972 6.089   87.022 1.00 22.58 ? 589  ILE   B HA   1 
ATOM   18471 H  HB   . ILE   B 1 589 ? 18.499 4.913   89.533 1.00 25.33 ? 589  ILE   B HB   1 
ATOM   18472 H  HG12 . ILE   B 1 589 ? 18.599 7.182   89.909 1.00 27.62 ? 589  ILE   B HG12 1 
ATOM   18473 H  HG13 . ILE   B 1 589 ? 19.852 6.495   90.535 1.00 27.62 ? 589  ILE   B HG13 1 
ATOM   18474 H  HG21 . ILE   B 1 589 ? 20.782 4.411   89.523 1.00 27.20 ? 589  ILE   B HG21 1 
ATOM   18475 H  HG22 . ILE   B 1 589 ? 20.056 3.735   88.288 1.00 27.20 ? 589  ILE   B HG22 1 
ATOM   18476 H  HG23 . ILE   B 1 589 ? 20.911 5.052   88.081 1.00 27.20 ? 589  ILE   B HG23 1 
ATOM   18477 H  HD11 . ILE   B 1 589 ? 20.497 8.443   89.440 1.00 28.84 ? 589  ILE   B HD11 1 
ATOM   18478 H  HD12 . ILE   B 1 589 ? 21.160 7.198   88.720 1.00 28.84 ? 589  ILE   B HD12 1 
ATOM   18479 H  HD13 . ILE   B 1 589 ? 19.888 7.895   88.084 1.00 28.84 ? 589  ILE   B HD13 1 
ATOM   18480 N  N    . PRO   B 1 590 ? 18.202 4.016   85.802 1.00 18.20 ? 590  PRO   B N    1 
ATOM   18481 C  CA   . PRO   B 1 590 ? 17.728 2.779   85.201 1.00 18.33 ? 590  PRO   B CA   1 
ATOM   18482 C  C    . PRO   B 1 590 ? 17.878 1.608   86.181 1.00 20.93 ? 590  PRO   B C    1 
ATOM   18483 O  O    . PRO   B 1 590 ? 18.920 1.484   86.785 1.00 20.39 ? 590  PRO   B O    1 
ATOM   18484 C  CB   . PRO   B 1 590 ? 18.643 2.571   83.986 1.00 18.71 ? 590  PRO   B CB   1 
ATOM   18485 C  CG   . PRO   B 1 590 ? 19.025 3.975   83.591 1.00 17.63 ? 590  PRO   B CG   1 
ATOM   18486 C  CD   . PRO   B 1 590 ? 19.143 4.715   84.907 1.00 18.66 ? 590  PRO   B CD   1 
ATOM   18487 H  HA   . PRO   B 1 590 ? 16.789 2.823   84.961 1.00 22.00 ? 590  PRO   B HA   1 
ATOM   18488 H  HB2  . PRO   B 1 590 ? 19.422 2.039   84.212 1.00 22.45 ? 590  PRO   B HB2  1 
ATOM   18489 H  HB3  . PRO   B 1 590 ? 18.183 2.110   83.267 1.00 22.45 ? 590  PRO   B HB3  1 
ATOM   18490 H  HG2  . PRO   B 1 590 ? 19.862 3.989   83.101 1.00 21.16 ? 590  PRO   B HG2  1 
ATOM   18491 H  HG3  . PRO   B 1 590 ? 18.353 4.377   83.018 1.00 21.16 ? 590  PRO   B HG3  1 
ATOM   18492 H  HD2  . PRO   B 1 590 ? 20.049 4.683   85.251 1.00 22.39 ? 590  PRO   B HD2  1 
ATOM   18493 H  HD3  . PRO   B 1 590 ? 18.910 5.651   84.809 1.00 22.39 ? 590  PRO   B HD3  1 
ATOM   18494 N  N    . THR   B 1 591 ? 16.831 0.797   86.297 1.00 21.03 ? 591  THR   B N    1 
ATOM   18495 C  CA   . THR   B 1 591 ? 16.854 -0.352  87.236 1.00 21.06 ? 591  THR   B CA   1 
ATOM   18496 C  C    . THR   B 1 591 ? 17.679 -1.501  86.651 1.00 22.11 ? 591  THR   B C    1 
ATOM   18497 O  O    . THR   B 1 591 ? 17.870 -1.529  85.428 1.00 21.07 ? 591  THR   B O    1 
ATOM   18498 C  CB   . THR   B 1 591 ? 15.428 -0.833  87.526 1.00 23.50 ? 591  THR   B CB   1 
ATOM   18499 O  OG1  . THR   B 1 591 ? 14.898 -1.389  86.323 1.00 25.20 ? 591  THR   B OG1  1 
ATOM   18500 C  CG2  . THR   B 1 591 ? 14.530 0.278   88.023 1.00 24.22 ? 591  THR   B CG2  1 
ATOM   18501 H  H    . THR   B 1 591 ? 16.100 0.883   85.852 1.00 25.24 ? 591  THR   B H    1 
ATOM   18502 H  HA   . THR   B 1 591 ? 17.263 -0.060  88.066 1.00 25.27 ? 591  THR   B HA   1 
ATOM   18503 H  HB   . THR   B 1 591 ? 15.463 -1.496  88.234 1.00 28.20 ? 591  THR   B HB   1 
ATOM   18504 H  HG1  . THR   B 1 591 ? 14.082 -1.559  86.428 1.00 30.24 ? 591  THR   B HG1  1 
ATOM   18505 H  HG21 . THR   B 1 591 ? 13.642 -0.074  88.192 1.00 29.06 ? 591  THR   B HG21 1 
ATOM   18506 H  HG22 . THR   B 1 591 ? 14.893 0.645   88.844 1.00 29.06 ? 591  THR   B HG22 1 
ATOM   18507 H  HG23 . THR   B 1 591 ? 14.478 0.977   87.352 1.00 29.06 ? 591  THR   B HG23 1 
ATOM   18508 N  N    . GLU   B 1 592 ? 18.107 -2.431  87.507 1.00 22.89 ? 592  GLU   B N    1 
ATOM   18509 C  CA   . GLU   B 1 592 ? 18.865 -3.618  87.031 1.00 23.81 ? 592  GLU   B CA   1 
ATOM   18510 C  C    . GLU   B 1 592 ? 18.023 -4.372  86.001 1.00 25.86 ? 592  GLU   B C    1 
ATOM   18511 O  O    . GLU   B 1 592 ? 18.578 -4.787  84.976 1.00 26.30 ? 592  GLU   B O    1 
ATOM   18512 C  CB   . GLU   B 1 592 ? 19.202 -4.530  88.210 1.00 25.56 ? 592  GLU   B CB   1 
ATOM   18513 C  CG   . GLU   B 1 592 ? 19.580 -5.937  87.792 1.00 26.28 ? 592  GLU   B CG   1 
ATOM   18514 C  CD   . GLU   B 1 592 ? 19.986 -6.841  88.942 1.00 27.94 ? 592  GLU   B CD   1 
ATOM   18515 O  OE1  . GLU   B 1 592 ? 19.799 -6.434  90.101 1.00 28.41 ? 592  GLU   B OE1  1 
ATOM   18516 O  OE2  . GLU   B 1 592 ? 20.492 -7.944  88.672 1.00 29.18 ? 592  GLU   B OE2  1 
ATOM   18517 H  H    . GLU   B 1 592 ? 17.977 -2.404  88.357 1.00 27.47 ? 592  GLU   B H    1 
ATOM   18518 H  HA   . GLU   B 1 592 ? 19.694 -3.330  86.618 1.00 28.58 ? 592  GLU   B HA   1 
ATOM   18519 H  HB2  . GLU   B 1 592 ? 19.935 -4.141  88.712 1.00 30.67 ? 592  GLU   B HB2  1 
ATOM   18520 H  HB3  . GLU   B 1 592 ? 18.439 -4.571  88.807 1.00 30.67 ? 592  GLU   B HB3  1 
ATOM   18521 H  HG2  . GLU   B 1 592 ? 18.829 -6.338  87.328 1.00 31.54 ? 592  GLU   B HG2  1 
ATOM   18522 H  HG3  . GLU   B 1 592 ? 20.312 -5.889  87.158 1.00 31.54 ? 592  GLU   B HG3  1 
ATOM   18523 N  N    . GLU   B 1 593 ? 16.731 -4.529  86.274 1.00 23.53 ? 593  GLU   B N    1 
ATOM   18524 C  CA   . GLU   B 1 593 ? 15.852 -5.299  85.363 1.00 27.18 ? 593  GLU   B CA   1 
ATOM   18525 C  C    . GLU   B 1 593 ? 15.747 -4.581  84.013 1.00 23.53 ? 593  GLU   B C    1 
ATOM   18526 O  O    . GLU   B 1 593 ? 15.697 -5.266  82.984 1.00 22.75 ? 593  GLU   B O    1 
ATOM   18527 C  CB   . GLU   B 1 593 ? 14.478 -5.477  86.004 1.00 23.98 ? 593  GLU   B CB   1 
ATOM   18528 C  CG   . GLU   B 1 593 ? 14.496 -6.447  87.171 1.00 28.15 ? 593  GLU   B CG   1 
ATOM   18529 C  CD   . GLU   B 1 593 ? 14.976 -7.847  86.830 1.00 35.10 ? 593  GLU   B CD   1 
ATOM   18530 O  OE1  . GLU   B 1 593 ? 14.408 -8.453  85.902 1.00 32.84 ? 593  GLU   B OE1  1 
ATOM   18531 O  OE2  . GLU   B 1 593 ? 15.913 -8.329  87.495 1.00 27.87 ? 593  GLU   B OE2  1 
ATOM   18532 H  H    . GLU   B 1 593 ? 16.338 -4.207  86.968 1.00 28.24 ? 593  GLU   B H    1 
ATOM   18533 H  HA   . GLU   B 1 593 ? 16.231 -6.178  85.208 1.00 32.63 ? 593  GLU   B HA   1 
ATOM   18534 H  HB2  . GLU   B 1 593 ? 14.154 -4.615  86.310 1.00 28.78 ? 593  GLU   B HB2  1 
ATOM   18535 H  HB3  . GLU   B 1 593 ? 13.852 -5.794  85.335 1.00 28.78 ? 593  GLU   B HB3  1 
ATOM   18536 H  HG2  . GLU   B 1 593 ? 15.065 -6.084  87.868 1.00 33.79 ? 593  GLU   B HG2  1 
ATOM   18537 H  HG3  . GLU   B 1 593 ? 13.601 -6.507  87.539 1.00 33.79 ? 593  GLU   B HG3  1 
ATOM   18538 N  N    . THR   B 1 594 ? 15.704 -3.247  84.041 1.00 21.71 ? 594  THR   B N    1 
ATOM   18539 C  CA   . THR   B 1 594 ? 15.643 -2.479  82.770 1.00 20.42 ? 594  THR   B CA   1 
ATOM   18540 C  C    . THR   B 1 594 ? 16.956 -2.694  82.005 1.00 22.16 ? 594  THR   B C    1 
ATOM   18541 O  O    . THR   B 1 594 ? 16.893 -2.987  80.802 1.00 21.30 ? 594  THR   B O    1 
ATOM   18542 C  CB   . THR   B 1 594 ? 15.315 -1.004  83.039 1.00 20.94 ? 594  THR   B CB   1 
ATOM   18543 O  OG1  . THR   B 1 594 ? 13.960 -0.931  83.478 1.00 20.92 ? 594  THR   B OG1  1 
ATOM   18544 C  CG2  . THR   B 1 594 ? 15.506 -0.125  81.821 1.00 20.31 ? 594  THR   B CG2  1 
ATOM   18545 H  H    . THR   B 1 594 ? 15.709 -2.771  84.757 1.00 26.05 ? 594  THR   B H    1 
ATOM   18546 H  HA   . THR   B 1 594 ? 14.921 -2.801  82.208 1.00 24.50 ? 594  THR   B HA   1 
ATOM   18547 H  HB   . THR   B 1 594 ? 15.928 -0.673  83.714 1.00 25.14 ? 594  THR   B HB   1 
ATOM   18548 H  HG1  . THR   B 1 594 ? 13.862 -0.262  83.976 1.00 25.10 ? 594  THR   B HG1  1 
ATOM   18549 H  HG21 . THR   B 1 594 ? 15.286 0.792   82.046 1.00 24.37 ? 594  THR   B HG21 1 
ATOM   18550 H  HG22 . THR   B 1 594 ? 16.430 -0.173  81.529 1.00 24.37 ? 594  THR   B HG22 1 
ATOM   18551 H  HG23 . THR   B 1 594 ? 14.925 -0.431  81.107 1.00 24.37 ? 594  THR   B HG23 1 
ATOM   18552 N  N    . LEU   B 1 595 ? 18.090 -2.576  82.694 1.00 21.10 ? 595  LEU   B N    1 
ATOM   18553 C  CA   . LEU   B 1 595 ? 19.410 -2.794  82.042 1.00 21.80 ? 595  LEU   B CA   1 
ATOM   18554 C  C    . LEU   B 1 595 ? 19.460 -4.208  81.447 1.00 23.86 ? 595  LEU   B C    1 
ATOM   18555 O  O    . LEU   B 1 595 ? 19.964 -4.364  80.326 1.00 25.56 ? 595  LEU   B O    1 
ATOM   18556 C  CB   . LEU   B 1 595 ? 20.525 -2.568  83.066 1.00 22.30 ? 595  LEU   B CB   1 
ATOM   18557 C  CG   . LEU   B 1 595 ? 20.609 -1.154  83.635 1.00 21.71 ? 595  LEU   B CG   1 
ATOM   18558 C  CD1  . LEU   B 1 595 ? 21.722 -1.043  84.666 1.00 26.06 ? 595  LEU   B CD1  1 
ATOM   18559 C  CD2  . LEU   B 1 595 ? 20.808 -0.137  82.522 1.00 22.39 ? 595  LEU   B CD2  1 
ATOM   18560 H  H    . LEU   B 1 595 ? 18.131 -2.374  83.529 1.00 25.33 ? 595  LEU   B H    1 
ATOM   18561 H  HA   . LEU   B 1 595 ? 19.537 -2.162  81.317 1.00 26.16 ? 595  LEU   B HA   1 
ATOM   18562 H  HB2  . LEU   B 1 595 ? 20.401 -3.190  83.800 1.00 26.76 ? 595  LEU   B HB2  1 
ATOM   18563 H  HB3  . LEU   B 1 595 ? 21.374 -2.785  82.651 1.00 26.76 ? 595  LEU   B HB3  1 
ATOM   18564 H  HG   . LEU   B 1 595 ? 19.768 -0.962  84.079 1.00 26.05 ? 595  LEU   B HG   1 
ATOM   18565 H  HD11 . LEU   B 1 595 ? 21.754 -0.137  85.011 1.00 31.28 ? 595  LEU   B HD11 1 
ATOM   18566 H  HD12 . LEU   B 1 595 ? 21.551 -1.660  85.394 1.00 31.28 ? 595  LEU   B HD12 1 
ATOM   18567 H  HD13 . LEU   B 1 595 ? 22.571 -1.261  84.251 1.00 31.28 ? 595  LEU   B HD13 1 
ATOM   18568 H  HD21 . LEU   B 1 595 ? 20.859 0.754   82.903 1.00 26.87 ? 595  LEU   B HD21 1 
ATOM   18569 H  HD22 . LEU   B 1 595 ? 21.631 -0.333  82.048 1.00 26.87 ? 595  LEU   B HD22 1 
ATOM   18570 H  HD23 . LEU   B 1 595 ? 20.061 -0.182  81.905 1.00 26.87 ? 595  LEU   B HD23 1 
ATOM   18571 N  N    . LYS   B 1 596 ? 18.936 -5.197  82.176 1.00 25.60 ? 596  LYS   B N    1 
ATOM   18572 C  CA   . LYS   B 1 596 ? 18.961 -6.597  81.684 1.00 27.49 ? 596  LYS   B CA   1 
ATOM   18573 C  C    . LYS   B 1 596 ? 18.115 -6.706  80.416 1.00 27.66 ? 596  LYS   B C    1 
ATOM   18574 O  O    . LYS   B 1 596 ? 18.585 -7.311  79.442 1.00 27.57 ? 596  LYS   B O    1 
ATOM   18575 C  CB   . LYS   B 1 596 ? 18.418 -7.549  82.752 1.00 29.47 ? 596  LYS   B CB   1 
ATOM   18576 C  CG   . LYS   B 1 596 ? 19.323 -7.753  83.957 1.00 32.95 ? 596  LYS   B CG   1 
ATOM   18577 C  CD   . LYS   B 1 596 ? 19.094 -9.078  84.639 1.00 38.48 ? 596  LYS   B CD   1 
ATOM   18578 C  CE   . LYS   B 1 596 ? 18.746 -8.936  86.104 1.00 35.70 ? 596  LYS   B CE   1 
ATOM   18579 N  NZ   . LYS   B 1 596 ? 17.896 -10.057 86.569 1.00 41.32 ? 596  LYS   B NZ   1 
ATOM   18580 H  H    . LYS   B 1 596 ? 18.566 -5.091  82.945 1.00 30.72 ? 596  LYS   B H    1 
ATOM   18581 H  HA   . LYS   B 1 596 ? 19.878 -6.845  81.486 1.00 32.99 ? 596  LYS   B HA   1 
ATOM   18582 H  HB2  . LYS   B 1 596 ? 17.563 -7.212  83.061 1.00 35.36 ? 596  LYS   B HB2  1 
ATOM   18583 H  HB3  . LYS   B 1 596 ? 18.251 -8.412  82.341 1.00 35.36 ? 596  LYS   B HB3  1 
ATOM   18584 H  HG2  . LYS   B 1 596 ? 20.249 -7.695  83.675 1.00 39.54 ? 596  LYS   B HG2  1 
ATOM   18585 H  HG3  . LYS   B 1 596 ? 19.175 -7.036  84.593 1.00 39.54 ? 596  LYS   B HG3  1 
ATOM   18586 H  HD2  . LYS   B 1 596 ? 18.378 -9.550  84.186 1.00 46.17 ? 596  LYS   B HD2  1 
ATOM   18587 H  HD3  . LYS   B 1 596 ? 19.892 -9.623  84.553 1.00 46.17 ? 596  LYS   B HD3  1 
ATOM   18588 H  HE2  . LYS   B 1 596 ? 19.560 -8.906  86.630 1.00 42.84 ? 596  LYS   B HE2  1 
ATOM   18589 H  HE3  . LYS   B 1 596 ? 18.283 -8.096  86.248 1.00 42.84 ? 596  LYS   B HE3  1 
ATOM   18590 H  HZ1  . LYS   B 1 596 ? 17.152 -9.734  86.935 1.00 49.59 ? 596  LYS   B HZ1  1 
ATOM   18591 H  HZ2  . LYS   B 1 596 ? 17.684 -10.576 85.878 1.00 49.59 ? 596  LYS   B HZ2  1 
ATOM   18592 H  HZ3  . LYS   B 1 596 ? 18.340 -10.536 87.174 1.00 49.59 ? 596  LYS   B HZ3  1 
ATOM   18593 N  N    . LYS   B 1 597 ? 16.905 -6.152  80.444 1.00 24.39 ? 597  LYS   B N    1 
ATOM   18594 C  CA   . LYS   B 1 597 ? 15.996 -6.265  79.277 1.00 27.38 ? 597  LYS   B CA   1 
ATOM   18595 C  C    . LYS   B 1 597 ? 16.631 -5.559  78.076 1.00 25.16 ? 597  LYS   B C    1 
ATOM   18596 O  O    . LYS   B 1 597 ? 16.455 -6.048  76.952 1.00 25.92 ? 597  LYS   B O    1 
ATOM   18597 C  CB   . LYS   B 1 597 ? 14.637 -5.642  79.606 1.00 29.21 ? 597  LYS   B CB   1 
ATOM   18598 C  CG   . LYS   B 1 597 ? 13.734 -5.388  78.409 1.00 30.56 ? 597  LYS   B CG   1 
ATOM   18599 C  CD   . LYS   B 1 597 ? 12.645 -4.384  78.694 1.00 35.42 ? 597  LYS   B CD   1 
ATOM   18600 C  CE   . LYS   B 1 597 ? 13.176 -3.041  79.147 1.00 36.92 ? 597  LYS   B CE   1 
ATOM   18601 N  NZ   . LYS   B 1 597 ? 12.073 -2.136  79.546 1.00 40.36 ? 597  LYS   B NZ   1 
ATOM   18602 H  H    . LYS   B 1 597 ? 16.586 -5.712  81.111 1.00 29.27 ? 597  LYS   B H    1 
ATOM   18603 H  HA   . LYS   B 1 597 ? 15.858 -7.201  79.062 1.00 32.86 ? 597  LYS   B HA   1 
ATOM   18604 H  HB2  . LYS   B 1 597 ? 14.172 -6.225  80.226 1.00 35.05 ? 597  LYS   B HB2  1 
ATOM   18605 H  HB3  . LYS   B 1 597 ? 14.786 -4.801  80.065 1.00 35.05 ? 597  LYS   B HB3  1 
ATOM   18606 H  HG2  . LYS   B 1 597 ? 14.272 -5.072  77.666 1.00 36.68 ? 597  LYS   B HG2  1 
ATOM   18607 H  HG3  . LYS   B 1 597 ? 13.330 -6.225  78.131 1.00 36.68 ? 597  LYS   B HG3  1 
ATOM   18608 H  HD2  . LYS   B 1 597 ? 12.110 -4.261  77.895 1.00 42.51 ? 597  LYS   B HD2  1 
ATOM   18609 H  HD3  . LYS   B 1 597 ? 12.056 -4.740  79.378 1.00 42.51 ? 597  LYS   B HD3  1 
ATOM   18610 H  HE2  . LYS   B 1 597 ? 13.782 -3.165  79.894 1.00 44.30 ? 597  LYS   B HE2  1 
ATOM   18611 H  HE3  . LYS   B 1 597 ? 13.688 -2.634  78.431 1.00 44.30 ? 597  LYS   B HE3  1 
ATOM   18612 H  HZ1  . LYS   B 1 597 ? 12.253 -1.309  79.272 1.00 48.43 ? 597  LYS   B HZ1  1 
ATOM   18613 H  HZ2  . LYS   B 1 597 ? 11.313 -2.412  79.174 1.00 48.43 ? 597  LYS   B HZ2  1 
ATOM   18614 H  HZ3  . LYS   B 1 597 ? 11.989 -2.143  80.432 1.00 48.43 ? 597  LYS   B HZ3  1 
ATOM   18615 N  N    . LEU   B 1 598 ? 17.358 -4.465  78.316 1.00 24.51 ? 598  LEU   B N    1 
ATOM   18616 C  CA   . LEU   B 1 598 ? 17.917 -3.663  77.193 1.00 25.13 ? 598  LEU   B CA   1 
ATOM   18617 C  C    . LEU   B 1 598 ? 19.274 -4.218  76.741 1.00 24.02 ? 598  LEU   B C    1 
ATOM   18618 O  O    . LEU   B 1 598 ? 19.817 -3.703  75.753 1.00 25.16 ? 598  LEU   B O    1 
ATOM   18619 C  CB   . LEU   B 1 598 ? 18.045 -2.206  77.652 1.00 23.45 ? 598  LEU   B CB   1 
ATOM   18620 C  CG   . LEU   B 1 598 ? 16.725 -1.473  77.879 1.00 22.27 ? 598  LEU   B CG   1 
ATOM   18621 C  CD1  . LEU   B 1 598 ? 16.975 -0.009  78.202 1.00 20.07 ? 598  LEU   B CD1  1 
ATOM   18622 C  CD2  . LEU   B 1 598 ? 15.814 -1.606  76.669 1.00 24.87 ? 598  LEU   B CD2  1 
ATOM   18623 H  H    . LEU   B 1 598 ? 17.542 -4.166  79.101 1.00 29.42 ? 598  LEU   B H    1 
ATOM   18624 H  HA   . LEU   B 1 598 ? 17.321 -3.713  76.429 1.00 30.17 ? 598  LEU   B HA   1 
ATOM   18625 H  HB2  . LEU   B 1 598 ? 18.555 -2.186  78.477 1.00 28.14 ? 598  LEU   B HB2  1 
ATOM   18626 H  HB3  . LEU   B 1 598 ? 18.559 -1.718  76.990 1.00 28.14 ? 598  LEU   B HB3  1 
ATOM   18627 H  HG   . LEU   B 1 598 ? 16.280 -1.883  78.637 1.00 26.73 ? 598  LEU   B HG   1 
ATOM   18628 H  HD11 . LEU   B 1 598 ? 16.127 0.441   78.343 1.00 24.09 ? 598  LEU   B HD11 1 
ATOM   18629 H  HD12 . LEU   B 1 598 ? 17.514 0.058   79.006 1.00 24.09 ? 598  LEU   B HD12 1 
ATOM   18630 H  HD13 . LEU   B 1 598 ? 17.444 0.410   77.463 1.00 24.09 ? 598  LEU   B HD13 1 
ATOM   18631 H  HD21 . LEU   B 1 598 ? 14.983 -1.134  76.836 1.00 29.85 ? 598  LEU   B HD21 1 
ATOM   18632 H  HD22 . LEU   B 1 598 ? 16.251 -1.226  75.891 1.00 29.85 ? 598  LEU   B HD22 1 
ATOM   18633 H  HD23 . LEU   B 1 598 ? 15.625 -2.544  76.507 1.00 29.85 ? 598  LEU   B HD23 1 
ATOM   18634 N  N    . GLY   B 1 599 ? 19.795 -5.223  77.443 1.00 24.84 ? 599  GLY   B N    1 
ATOM   18635 C  CA   . GLY   B 1 599 ? 21.102 -5.804  77.090 1.00 26.36 ? 599  GLY   B CA   1 
ATOM   18636 C  C    . GLY   B 1 599 ? 22.246 -4.942  77.585 1.00 27.93 ? 599  GLY   B C    1 
ATOM   18637 O  O    . GLY   B 1 599 ? 23.339 -5.028  77.003 1.00 27.44 ? 599  GLY   B O    1 
ATOM   18638 H  H    . GLY   B 1 599 ? 19.414 -5.585  78.124 1.00 29.81 ? 599  GLY   B H    1 
ATOM   18639 H  HA2  . GLY   B 1 599 ? 21.176 -6.692  77.472 1.00 31.63 ? 599  GLY   B HA2  1 
ATOM   18640 H  HA3  . GLY   B 1 599 ? 21.164 -5.903  76.127 1.00 31.63 ? 599  GLY   B HA3  1 
ATOM   18641 N  N    . LEU   B 1 600 ? 22.005 -4.136  78.622 1.00 25.05 ? 600  LEU   B N    1 
ATOM   18642 C  CA   . LEU   B 1 600 ? 23.062 -3.257  79.195 1.00 27.14 ? 600  LEU   B CA   1 
ATOM   18643 C  C    . LEU   B 1 600 ? 23.560 -3.866  80.510 1.00 26.99 ? 600  LEU   B C    1 
ATOM   18644 O  O    . LEU   B 1 600 ? 23.866 -3.099  81.436 1.00 28.26 ? 600  LEU   B O    1 
ATOM   18645 C  CB   . LEU   B 1 600 ? 22.481 -1.855  79.393 1.00 23.44 ? 600  LEU   B CB   1 
ATOM   18646 C  CG   . LEU   B 1 600 ? 22.094 -1.141  78.098 1.00 26.08 ? 600  LEU   B CG   1 
ATOM   18647 C  CD1  . LEU   B 1 600 ? 21.342 0.149   78.380 1.00 24.24 ? 600  LEU   B CD1  1 
ATOM   18648 C  CD2  . LEU   B 1 600 ? 23.322 -0.869  77.243 1.00 27.90 ? 600  LEU   B CD2  1 
ATOM   18649 H  H    . LEU   B 1 600 ? 21.242 -4.075  79.015 1.00 30.06 ? 600  LEU   B H    1 
ATOM   18650 H  HA   . LEU   B 1 600 ? 23.822 -3.186  78.596 1.00 32.57 ? 600  LEU   B HA   1 
ATOM   18651 H  HB2  . LEU   B 1 600 ? 21.697 -1.919  79.960 1.00 28.13 ? 600  LEU   B HB2  1 
ATOM   18652 H  HB3  . LEU   B 1 600 ? 23.130 -1.312  79.867 1.00 28.13 ? 600  LEU   B HB3  1 
ATOM   18653 H  HG   . LEU   B 1 600 ? 21.501 -1.729  77.605 1.00 31.31 ? 600  LEU   B HG   1 
ATOM   18654 H  HD11 . LEU   B 1 600 ? 21.110 0.579   77.542 1.00 29.09 ? 600  LEU   B HD11 1 
ATOM   18655 H  HD12 . LEU   B 1 600 ? 20.532 -0.050  78.875 1.00 29.09 ? 600  LEU   B HD12 1 
ATOM   18656 H  HD13 . LEU   B 1 600 ? 21.903 0.743   78.903 1.00 29.09 ? 600  LEU   B HD13 1 
ATOM   18657 H  HD21 . LEU   B 1 600 ? 23.055 -0.416  76.428 1.00 33.48 ? 600  LEU   B HD21 1 
ATOM   18658 H  HD22 . LEU   B 1 600 ? 23.942 -0.308  77.736 1.00 33.48 ? 600  LEU   B HD22 1 
ATOM   18659 H  HD23 . LEU   B 1 600 ? 23.754 -1.709  77.020 1.00 33.48 ? 600  LEU   B HD23 1 
ATOM   18660 N  N    . ASP   B 1 601 ? 23.688 -5.193  80.554 1.00 28.27 ? 601  ASP   B N    1 
ATOM   18661 C  CA   . ASP   B 1 601 ? 24.089 -5.916  81.790 1.00 29.16 ? 601  ASP   B CA   1 
ATOM   18662 C  C    . ASP   B 1 601 ? 25.448 -5.443  82.310 1.00 28.68 ? 601  ASP   B C    1 
ATOM   18663 O  O    . ASP   B 1 601 ? 25.643 -5.440  83.530 1.00 28.96 ? 601  ASP   B O    1 
ATOM   18664 C  CB   . ASP   B 1 601 ? 24.084 -7.421  81.522 1.00 34.74 ? 601  ASP   B CB   1 
ATOM   18665 C  CG   . ASP   B 1 601 ? 22.811 -7.891  80.842 1.00 38.15 ? 601  ASP   B CG   1 
ATOM   18666 O  OD1  . ASP   B 1 601 ? 22.713 -7.734  79.611 1.00 33.98 ? 601  ASP   B OD1  1 
ATOM   18667 O  OD2  . ASP   B 1 601 ? 21.926 -8.402  81.553 1.00 34.54 ? 601  ASP   B OD2  1 
ATOM   18668 H  H    . ASP   B 1 601 ? 23.548 -5.706  79.878 1.00 33.92 ? 601  ASP   B H    1 
ATOM   18669 H  HA   . ASP   B 1 601 ? 23.445 -5.718  82.488 1.00 34.99 ? 601  ASP   B HA   1 
ATOM   18670 H  HB2  . ASP   B 1 601 ? 24.846 -7.649  80.967 1.00 41.69 ? 601  ASP   B HB2  1 
ATOM   18671 H  HB3  . ASP   B 1 601 ? 24.192 -7.895  82.361 1.00 41.69 ? 601  ASP   B HB3  1 
ATOM   18672 N  N    . GLU   B 1 602 ? 26.353 -5.054  81.415 1.00 29.40 ? 602  GLU   B N    1 
ATOM   18673 C  CA   . GLU   B 1 602 ? 27.718 -4.671  81.859 1.00 30.95 ? 602  GLU   B CA   1 
ATOM   18674 C  C    . GLU   B 1 602 ? 27.671 -3.419  82.744 1.00 32.07 ? 602  GLU   B C    1 
ATOM   18675 O  O    . GLU   B 1 602 ? 28.690 -3.113  83.367 1.00 32.87 ? 602  GLU   B O    1 
ATOM   18676 C  CB   . GLU   B 1 602 ? 28.625 -4.451  80.650 1.00 38.49 ? 602  GLU   B CB   1 
ATOM   18677 C  CG   . GLU   B 1 602 ? 28.402 -3.122  79.954 1.00 34.42 ? 602  GLU   B CG   1 
ATOM   18678 C  CD   . GLU   B 1 602 ? 29.320 -2.887  78.768 1.00 43.63 ? 602  GLU   B CD   1 
ATOM   18679 O  OE1  . GLU   B 1 602 ? 28.949 -3.284  77.648 1.00 40.56 ? 602  GLU   B OE1  1 
ATOM   18680 O  OE2  . GLU   B 1 602 ? 30.406 -2.313  78.971 1.00 44.21 ? 602  GLU   B OE2  1 
ATOM   18681 H  H    . GLU   B 1 602 ? 26.215 -5.002  80.568 1.00 35.29 ? 602  GLU   B H    1 
ATOM   18682 H  HA   . GLU   B 1 602 ? 28.085 -5.396  82.389 1.00 37.15 ? 602  GLU   B HA   1 
ATOM   18683 H  HB2  . GLU   B 1 602 ? 29.550 -4.506  80.936 1.00 46.20 ? 602  GLU   B HB2  1 
ATOM   18684 H  HB3  . GLU   B 1 602 ? 28.481 -5.169  80.013 1.00 46.20 ? 602  GLU   B HB3  1 
ATOM   18685 H  HG2  . GLU   B 1 602 ? 27.481 -3.075  79.653 1.00 41.30 ? 602  GLU   B HG2  1 
ATOM   18686 H  HG3  . GLU   B 1 602 ? 28.528 -2.406  80.596 1.00 41.30 ? 602  GLU   B HG3  1 
ATOM   18687 N  N    . TYR   B 1 603 ? 26.532 -2.719  82.780 1.00 28.05 ? 603  TYR   B N    1 
ATOM   18688 C  CA   . TYR   B 1 603 ? 26.418 -1.474  83.584 1.00 27.94 ? 603  TYR   B CA   1 
ATOM   18689 C  C    . TYR   B 1 603 ? 25.645 -1.751  84.881 1.00 29.65 ? 603  TYR   B C    1 
ATOM   18690 O  O    . TYR   B 1 603 ? 25.460 -0.828  85.688 1.00 29.35 ? 603  TYR   B O    1 
ATOM   18691 C  CB   . TYR   B 1 603 ? 25.758 -0.379  82.744 1.00 26.15 ? 603  TYR   B CB   1 
ATOM   18692 C  CG   . TYR   B 1 603 ? 26.531 -0.041  81.497 1.00 26.20 ? 603  TYR   B CG   1 
ATOM   18693 C  CD1  . TYR   B 1 603 ? 27.730 0.646   81.571 1.00 27.38 ? 603  TYR   B CD1  1 
ATOM   18694 C  CD2  . TYR   B 1 603 ? 26.078 -0.428  80.248 1.00 27.36 ? 603  TYR   B CD2  1 
ATOM   18695 C  CE1  . TYR   B 1 603 ? 28.455 0.954   80.433 1.00 29.30 ? 603  TYR   B CE1  1 
ATOM   18696 C  CE2  . TYR   B 1 603 ? 26.790 -0.128  79.100 1.00 26.89 ? 603  TYR   B CE2  1 
ATOM   18697 C  CZ   . TYR   B 1 603 ? 27.983 0.564   79.194 1.00 29.36 ? 603  TYR   B CZ   1 
ATOM   18698 O  OH   . TYR   B 1 603 ? 28.694 0.865   78.060 1.00 29.04 ? 603  TYR   B OH   1 
ATOM   18699 H  H    . TYR   B 1 603 ? 25.817 -2.937  82.355 1.00 33.67 ? 603  TYR   B H    1 
ATOM   18700 H  HA   . TYR   B 1 603 ? 27.301 -1.163  83.836 1.00 33.53 ? 603  TYR   B HA   1 
ATOM   18701 H  HB2  . TYR   B 1 603 ? 24.864 -0.664  82.496 1.00 31.38 ? 603  TYR   B HB2  1 
ATOM   18702 H  HB3  . TYR   B 1 603 ? 25.661 0.421   83.284 1.00 31.38 ? 603  TYR   B HB3  1 
ATOM   18703 H  HD1  . TYR   B 1 603 ? 28.055 0.906   82.403 1.00 32.86 ? 603  TYR   B HD1  1 
ATOM   18704 H  HD2  . TYR   B 1 603 ? 25.279 -0.899  80.179 1.00 32.83 ? 603  TYR   B HD2  1 
ATOM   18705 H  HE1  . TYR   B 1 603 ? 29.256 1.421   80.502 1.00 35.16 ? 603  TYR   B HE1  1 
ATOM   18706 H  HE2  . TYR   B 1 603 ? 26.467 -0.391  78.268 1.00 32.27 ? 603  TYR   B HE2  1 
ATOM   18707 H  HH   . TYR   B 1 603 ? 29.479 1.079   78.270 1.00 34.85 ? 603  TYR   B HH   1 
ATOM   18708 N  N    . ILE   B 1 604 ? 25.233 -3.002  85.077 1.00 29.60 ? 604  ILE   B N    1 
ATOM   18709 C  CA   . ILE   B 1 604 ? 24.435 -3.362  86.284 1.00 31.61 ? 604  ILE   B CA   1 
ATOM   18710 C  C    . ILE   B 1 604 ? 25.319 -3.240  87.527 1.00 31.16 ? 604  ILE   B C    1 
ATOM   18711 O  O    . ILE   B 1 604 ? 26.478 -3.680  87.469 1.00 35.34 ? 604  ILE   B O    1 
ATOM   18712 C  CB   . ILE   B 1 604 ? 23.827 -4.771  86.132 1.00 29.55 ? 604  ILE   B CB   1 
ATOM   18713 C  CG1  . ILE   B 1 604 ? 22.696 -4.792  85.103 1.00 29.24 ? 604  ILE   B CG1  1 
ATOM   18714 C  CG2  . ILE   B 1 604 ? 23.372 -5.316  87.477 1.00 29.58 ? 604  ILE   B CG2  1 
ATOM   18715 C  CD1  . ILE   B 1 604 ? 22.171 -6.174  84.812 1.00 33.78 ? 604  ILE   B CD1  1 
ATOM   18716 H  H    . ILE   B 1 604 ? 25.394 -3.656  84.542 1.00 35.53 ? 604  ILE   B H    1 
ATOM   18717 H  HA   . ILE   B 1 604 ? 23.691 -2.748  86.383 1.00 37.93 ? 604  ILE   B HA   1 
ATOM   18718 H  HB   . ILE   B 1 604 ? 24.524 -5.357  85.797 1.00 35.46 ? 604  ILE   B HB   1 
ATOM   18719 H  HG12 . ILE   B 1 604 ? 21.967 -4.238  85.423 1.00 35.09 ? 604  ILE   B HG12 1 
ATOM   18720 H  HG13 . ILE   B 1 604 ? 23.013 -4.394  84.277 1.00 35.09 ? 604  ILE   B HG13 1 
ATOM   18721 H  HG21 . ILE   B 1 604 ? 22.994 -6.201  87.357 1.00 35.50 ? 604  ILE   B HG21 1 
ATOM   18722 H  HG22 . ILE   B 1 604 ? 24.131 -5.368  88.079 1.00 35.50 ? 604  ILE   B HG22 1 
ATOM   18723 H  HG23 . ILE   B 1 604 ? 22.700 -4.727  87.855 1.00 35.50 ? 604  ILE   B HG23 1 
ATOM   18724 H  HD11 . ILE   B 1 604 ? 21.459 -6.118  84.155 1.00 40.54 ? 604  ILE   B HD11 1 
ATOM   18725 H  HD12 . ILE   B 1 604 ? 22.889 -6.726  84.465 1.00 40.54 ? 604  ILE   B HD12 1 
ATOM   18726 H  HD13 . ILE   B 1 604 ? 21.827 -6.568  85.629 1.00 40.54 ? 604  ILE   B HD13 1 
ATOM   18727 N  N    . GLY   B 1 605 ? 24.799 -2.626  88.590 1.00 33.29 ? 605  GLY   B N    1 
ATOM   18728 C  CA   . GLY   B 1 605 ? 25.543 -2.536  89.860 1.00 33.68 ? 605  GLY   B CA   1 
ATOM   18729 C  C    . GLY   B 1 605 ? 26.477 -1.345  89.927 1.00 37.85 ? 605  GLY   B C    1 
ATOM   18730 O  O    . GLY   B 1 605 ? 27.147 -1.191  90.959 1.00 41.38 ? 605  GLY   B O    1 
ATOM   18731 H  H    . GLY   B 1 605 ? 24.023 -2.256  88.602 1.00 39.95 ? 605  GLY   B H    1 
ATOM   18732 H  HA2  . GLY   B 1 605 ? 24.911 -2.485  90.594 1.00 40.42 ? 605  GLY   B HA2  1 
ATOM   18733 H  HA3  . GLY   B 1 605 ? 26.057 -3.349  89.984 1.00 40.42 ? 605  GLY   B HA3  1 
ATOM   18734 N  N    . LYS   B 1 606 ? 26.517 -0.517  88.881 1.00 40.49 ? 606  LYS   B N    1 
ATOM   18735 C  CA   . LYS   B 1 606 ? 27.508 0.594   88.866 1.00 41.34 ? 606  LYS   B CA   1 
ATOM   18736 C  C    . LYS   B 1 606 ? 26.828 1.955   89.077 1.00 38.33 ? 606  LYS   B C    1 
ATOM   18737 O  O    . LYS   B 1 606 ? 27.561 2.933   89.295 1.00 38.38 ? 606  LYS   B O    1 
ATOM   18738 C  CB   . LYS   B 1 606 ? 28.315 0.528   87.565 1.00 41.44 ? 606  LYS   B CB   1 
ATOM   18739 C  CG   . LYS   B 1 606 ? 29.139 -0.740  87.397 1.00 42.14 ? 606  LYS   B CG   1 
ATOM   18740 C  CD   . LYS   B 1 606 ? 29.317 -1.168  85.960 1.00 46.85 ? 606  LYS   B CD   1 
ATOM   18741 C  CE   . LYS   B 1 606 ? 30.297 -2.313  85.816 1.00 50.10 ? 606  LYS   B CE   1 
ATOM   18742 N  NZ   . LYS   B 1 606 ? 30.985 -2.289  84.504 1.00 57.43 ? 606  LYS   B NZ   1 
ATOM   18743 H  H    . LYS   B 1 606 ? 26.006 -0.567  88.191 1.00 48.59 ? 606  LYS   B H    1 
ATOM   18744 H  HA   . LYS   B 1 606 ? 28.124 0.492   89.609 1.00 49.62 ? 606  LYS   B HA   1 
ATOM   18745 H  HB2  . LYS   B 1 606 ? 27.705 0.605   86.815 1.00 49.73 ? 606  LYS   B HB2  1 
ATOM   18746 H  HB3  . LYS   B 1 606 ? 28.909 1.294   87.527 1.00 49.73 ? 606  LYS   B HB3  1 
ATOM   18747 H  HG2  . LYS   B 1 606 ? 30.013 -0.602  87.795 1.00 50.58 ? 606  LYS   B HG2  1 
ATOM   18748 H  HG3  . LYS   B 1 606 ? 28.713 -1.459  87.889 1.00 50.58 ? 606  LYS   B HG3  1 
ATOM   18749 H  HD2  . LYS   B 1 606 ? 28.458 -1.433  85.595 1.00 56.22 ? 606  LYS   B HD2  1 
ATOM   18750 H  HD3  . LYS   B 1 606 ? 29.627 -0.413  85.436 1.00 56.22 ? 606  LYS   B HD3  1 
ATOM   18751 H  HE2  . LYS   B 1 606 ? 30.955 -2.266  86.527 1.00 60.13 ? 606  LYS   B HE2  1 
ATOM   18752 H  HE3  . LYS   B 1 606 ? 29.827 -3.155  85.919 1.00 60.13 ? 606  LYS   B HE3  1 
ATOM   18753 H  HZ1  . LYS   B 1 606 ? 31.677 -2.848  84.521 1.00 68.92 ? 606  LYS   B HZ1  1 
ATOM   18754 H  HZ2  . LYS   B 1 606 ? 30.417 -2.540  83.866 1.00 68.92 ? 606  LYS   B HZ2  1 
ATOM   18755 H  HZ3  . LYS   B 1 606 ? 31.274 -1.464  84.335 1.00 68.92 ? 606  LYS   B HZ3  1 
ATOM   18756 N  N    . PHE   B 1 607 ? 25.487 1.992   89.046 1.00 39.11 ? 607  PHE   B N    1 
ATOM   18757 C  CA   . PHE   B 1 607 ? 24.720 3.255   89.236 1.00 41.69 ? 607  PHE   B CA   1 
ATOM   18758 C  C    . PHE   B 1 607 ? 23.613 3.074   90.292 1.00 43.28 ? 607  PHE   B C    1 
ATOM   18759 O  O    . PHE   B 1 607 ? 23.326 4.065   90.957 1.00 41.37 ? 607  PHE   B O    1 
ATOM   18760 C  CB   . PHE   B 1 607 ? 24.154 3.751   87.899 1.00 42.27 ? 607  PHE   B CB   1 
ATOM   18761 C  CG   . PHE   B 1 607 ? 25.164 3.920   86.791 1.00 40.85 ? 607  PHE   B CG   1 
ATOM   18762 C  CD1  . PHE   B 1 607 ? 25.543 2.844   86.004 1.00 38.98 ? 607  PHE   B CD1  1 
ATOM   18763 C  CD2  . PHE   B 1 607 ? 25.726 5.158   86.525 1.00 35.95 ? 607  PHE   B CD2  1 
ATOM   18764 C  CE1  . PHE   B 1 607 ? 26.465 3.002   84.982 1.00 37.03 ? 607  PHE   B CE1  1 
ATOM   18765 C  CE2  . PHE   B 1 607 ? 26.649 5.315   85.503 1.00 27.31 ? 607  PHE   B CE2  1 
ATOM   18766 C  CZ   . PHE   B 1 607 ? 27.017 4.237   84.733 1.00 34.66 ? 607  PHE   B CZ   1 
ATOM   18767 O  OXT  . PHE   B 1 607 ? 23.058 1.961   90.436 1.00 29.28 ? 607  PHE   B OXT  1 
ATOM   18768 H  H    . PHE   B 1 607 ? 24.995 1.299   88.916 1.00 46.94 ? 607  PHE   B H    1 
ATOM   18769 H  HA   . PHE   B 1 607 ? 25.327 3.935   89.568 1.00 50.03 ? 607  PHE   B HA   1 
ATOM   18770 H  HB2  . PHE   B 1 607 ? 23.473 3.128   87.602 1.00 50.72 ? 607  PHE   B HB2  1 
ATOM   18771 H  HB3  . PHE   B 1 607 ? 23.714 4.603   88.048 1.00 50.72 ? 607  PHE   B HB3  1 
ATOM   18772 H  HD1  . PHE   B 1 607 ? 25.174 2.006   86.164 1.00 46.78 ? 607  PHE   B HD1  1 
ATOM   18773 H  HD2  . PHE   B 1 607 ? 25.481 5.893   87.039 1.00 43.15 ? 607  PHE   B HD2  1 
ATOM   18774 H  HE1  . PHE   B 1 607 ? 26.711 2.271   84.463 1.00 44.44 ? 607  PHE   B HE1  1 
ATOM   18775 H  HE2  . PHE   B 1 607 ? 27.020 6.151   85.338 1.00 32.77 ? 607  PHE   B HE2  1 
ATOM   18776 H  HZ   . PHE   B 1 607 ? 27.636 4.342   84.047 1.00 41.60 ? 607  PHE   B HZ   1 
HETATM 18777 FE FE1  . SF4   C 2 .   ? 16.647 32.834  32.126 1.00 11.73 ? 701  SF4   A FE1  1 
HETATM 18778 FE FE2  . SF4   C 2 .   ? 16.452 30.392  33.117 1.00 12.15 ? 701  SF4   A FE2  1 
HETATM 18779 FE FE3  . SF4   C 2 .   ? 16.537 32.504  34.759 1.00 13.00 ? 701  SF4   A FE3  1 
HETATM 18780 FE FE4  . SF4   C 2 .   ? 18.681 31.734  33.495 1.00 11.78 ? 701  SF4   A FE4  1 
HETATM 18781 S  S1   . SF4   C 2 .   ? 17.623 30.493  35.129 1.00 13.75 ? 701  SF4   A S1   1 
HETATM 18782 S  S2   . SF4   C 2 .   ? 17.994 33.928  33.661 1.00 13.24 ? 701  SF4   A S2   1 
HETATM 18783 S  S3   . SF4   C 2 .   ? 17.889 31.010  31.433 1.00 11.67 ? 701  SF4   A S3   1 
HETATM 18784 S  S4   . SF4   C 2 .   ? 14.830 32.016  33.266 1.00 11.21 ? 701  SF4   A S4   1 
HETATM 18785 C  C1   . A1IJH D 3 .   ? 21.141 29.255  22.680 1.00 9.10  ? 702  A1IJH A C1   1 
HETATM 18786 C  C2   . A1IJH D 3 .   ? 21.024 27.746  22.482 1.00 7.11  ? 702  A1IJH A C2   1 
HETATM 18787 C  C3   . A1IJH D 3 .   ? 19.882 27.190  23.286 1.00 8.25  ? 702  A1IJH A C3   1 
HETATM 18788 S  S3   . A1IJH D 3 .   ? 18.475 28.108  23.444 1.00 9.13  ? 702  A1IJH A S3   1 
HETATM 18789 C  C4   . A1IJH D 3 .   ? 19.947 25.998  23.876 1.00 8.66  ? 702  A1IJH A C4   1 
HETATM 18790 S  S4   . A1IJH D 3 .   ? 18.598 25.369  24.631 1.00 10.04 ? 702  A1IJH A S4   1 
HETATM 18791 C  C5   . A1IJH D 3 .   ? 21.214 25.203  23.880 1.00 9.31  ? 702  A1IJH A C5   1 
HETATM 18792 N  N6   . A1IJH D 3 .   ? 21.888 25.271  25.158 1.00 11.97 ? 702  A1IJH A N6   1 
HETATM 18793 C  C7   . A1IJH D 3 .   ? 23.086 24.679  25.216 1.00 8.44  ? 702  A1IJH A C7   1 
HETATM 18794 C  C8   . A1IJH D 3 .   ? 23.633 24.068  26.442 1.00 7.54  ? 702  A1IJH A C8   1 
HETATM 18795 O  O8   . A1IJH D 3 .   ? 22.987 24.096  27.504 1.00 7.14  ? 702  A1IJH A O8   1 
HETATM 18796 N  N9   . A1IJH D 3 .   ? 24.840 23.497  26.375 1.00 9.03  ? 702  A1IJH A N9   1 
HETATM 18797 C  C10  . A1IJH D 3 .   ? 25.550 23.463  25.234 1.00 5.88  ? 702  A1IJH A C10  1 
HETATM 18798 N  N10  . A1IJH D 3 .   ? 26.764 22.867  25.236 1.00 10.05 ? 702  A1IJH A N10  1 
HETATM 18799 N  N11  . A1IJH D 3 .   ? 25.104 23.998  24.075 1.00 7.87  ? 702  A1IJH A N11  1 
HETATM 18800 C  C12  . A1IJH D 3 .   ? 23.907 24.606  24.000 1.00 8.14  ? 702  A1IJH A C12  1 
HETATM 18801 N  N13  . A1IJH D 3 .   ? 23.454 25.142  22.852 1.00 9.26  ? 702  A1IJH A N13  1 
HETATM 18802 C  C14  . A1IJH D 3 .   ? 22.128 25.722  22.776 1.00 7.80  ? 702  A1IJH A C14  1 
HETATM 18803 O  O2   . A1IJH D 3 .   ? 22.228 27.132  22.909 1.00 8.87  ? 702  A1IJH A O2   1 
HETATM 18804 C  C21  . A1IJH D 3 .   ? 20.098 29.180  28.098 1.00 12.88 ? 702  A1IJH A C21  1 
HETATM 18805 C  C22  . A1IJH D 3 .   ? 18.727 29.840  28.199 1.00 9.69  ? 702  A1IJH A C22  1 
HETATM 18806 C  C23  . A1IJH D 3 .   ? 17.836 29.272  27.130 1.00 10.76 ? 702  A1IJH A C23  1 
HETATM 18807 S  S23  . A1IJH D 3 .   ? 17.669 27.595  27.034 1.00 10.65 ? 702  A1IJH A S23  1 
HETATM 18808 C  C24  . A1IJH D 3 .   ? 17.166 30.047  26.282 1.00 12.01 ? 702  A1IJH A C24  1 
HETATM 18809 S  S24  . A1IJH D 3 .   ? 16.155 29.324  25.136 1.00 10.51 ? 702  A1IJH A S24  1 
HETATM 18810 C  C25  . A1IJH D 3 .   ? 17.253 31.541  26.362 1.00 12.01 ? 702  A1IJH A C25  1 
HETATM 18811 N  N26  . A1IJH D 3 .   ? 18.220 32.174  25.482 1.00 11.91 ? 702  A1IJH A N26  1 
HETATM 18812 C  C27  . A1IJH D 3 .   ? 18.239 33.513  25.603 1.00 10.27 ? 702  A1IJH A C27  1 
HETATM 18813 C  C28  . A1IJH D 3 .   ? 18.485 34.447  24.485 1.00 11.47 ? 702  A1IJH A C28  1 
HETATM 18814 O  O28  . A1IJH D 3 .   ? 18.719 34.020  23.341 1.00 9.54  ? 702  A1IJH A O28  1 
HETATM 18815 N  N29  . A1IJH D 3 .   ? 18.454 35.761  24.743 1.00 10.17 ? 702  A1IJH A N29  1 
HETATM 18816 C  C30  . A1IJH D 3 .   ? 18.199 36.247  25.971 1.00 8.15  ? 702  A1IJH A C30  1 
HETATM 18817 N  N30  . A1IJH D 3 .   ? 18.181 37.587  26.159 1.00 11.12 ? 702  A1IJH A N30  1 
HETATM 18818 N  N31  . A1IJH D 3 .   ? 17.960 35.449  27.036 1.00 11.78 ? 702  A1IJH A N31  1 
HETATM 18819 C  C32  . A1IJH D 3 .   ? 17.960 34.109  26.921 1.00 12.05 ? 702  A1IJH A C32  1 
HETATM 18820 N  N33  . A1IJH D 3 .   ? 17.722 33.312  27.980 1.00 12.77 ? 702  A1IJH A N33  1 
HETATM 18821 C  C34  . A1IJH D 3 .   ? 17.623 31.877  27.795 1.00 12.31 ? 702  A1IJH A C34  1 
HETATM 18822 O  O22  . A1IJH D 3 .   ? 18.870 31.249  28.054 1.00 10.49 ? 702  A1IJH A O22  1 
HETATM 18823 P  P1   . A1IJH D 3 .   ? 23.111 30.927  22.172 1.00 9.15  ? 702  A1IJH A P1   1 
HETATM 18824 O  O1P  . A1IJH D 3 .   ? 23.847 30.442  23.507 1.00 7.47  ? 702  A1IJH A O1P  1 
HETATM 18825 O  O2P  . A1IJH D 3 .   ? 24.141 31.063  21.087 1.00 8.11  ? 702  A1IJH A O2P  1 
HETATM 18826 O  O3P  . A1IJH D 3 .   ? 22.377 32.211  22.451 1.00 8.11  ? 702  A1IJH A O3P  1 
HETATM 18827 O  O4P  . A1IJH D 3 .   ? 22.064 29.789  21.736 1.00 7.63  ? 702  A1IJH A O4P  1 
HETATM 18828 P  P2   . A1IJH D 3 .   ? 22.536 29.857  28.730 1.00 9.86  ? 702  A1IJH A P2   1 
HETATM 18829 O  O5P  . A1IJH D 3 .   ? 22.700 30.834  27.469 1.00 8.93  ? 702  A1IJH A O5P  1 
HETATM 18830 O  O6P  . A1IJH D 3 .   ? 23.239 30.443  29.924 1.00 10.24 ? 702  A1IJH A O6P  1 
HETATM 18831 O  O7P  . A1IJH D 3 .   ? 23.074 28.494  28.371 1.00 11.69 ? 702  A1IJH A O7P  1 
HETATM 18832 O  O8P  . A1IJH D 3 .   ? 20.974 29.743  29.066 1.00 11.22 ? 702  A1IJH A O8P  1 
HETATM 18833 MG MG   . A1IJH D 3 .   ? 23.339 30.608  25.485 1.00 7.57  ? 702  A1IJH A MG   1 
HETATM 18834 W  W    . A1IJH D 3 .   ? 16.771 26.895  24.908 1.00 18.08 ? 702  A1IJH A W    1 
HETATM 18835 H  H12  . A1IJH D 3 .   ? 20.273 29.673  22.570 1.00 10.92 ? 702  A1IJH A H12  1 
HETATM 18836 H  H11  . A1IJH D 3 .   ? 21.438 29.450  23.583 1.00 10.92 ? 702  A1IJH A H11  1 
HETATM 18837 H  H2   . A1IJH D 3 .   ? 20.862 27.566  21.543 1.00 8.54  ? 702  A1IJH A H2   1 
HETATM 18838 H  H5   . A1IJH D 3 .   ? 20.993 24.272  23.721 1.00 11.18 ? 702  A1IJH A H5   1 
HETATM 18839 H  H6   . A1IJH D 3 .   ? 21.540 25.667  25.838 1.00 14.37 ? 702  A1IJH A H6   1 
HETATM 18840 H  H9   . A1IJH D 3 .   ? 25.172 23.141  27.084 1.00 10.84 ? 702  A1IJH A H9   1 
HETATM 18841 H  H102 . A1IJH D 3 .   ? 27.230 22.837  24.514 1.00 12.06 ? 702  A1IJH A H102 1 
HETATM 18842 H  H101 . A1IJH D 3 .   ? 27.070 22.517  25.960 1.00 12.06 ? 702  A1IJH A H101 1 
HETATM 18843 H  H13  . A1IJH D 3 .   ? 23.957 25.140  22.155 1.00 11.12 ? 702  A1IJH A H13  1 
HETATM 18844 H  H14  . A1IJH D 3 .   ? 21.748 25.473  21.919 1.00 9.37  ? 702  A1IJH A H14  1 
HETATM 18845 H  H211 . A1IJH D 3 .   ? 20.462 29.305  27.208 1.00 15.46 ? 702  A1IJH A H211 1 
HETATM 18846 H  H212 . A1IJH D 3 .   ? 20.017 28.224  28.239 1.00 15.46 ? 702  A1IJH A H212 1 
HETATM 18847 H  H22  . A1IJH D 3 .   ? 18.327 29.664  29.065 1.00 11.63 ? 702  A1IJH A H22  1 
HETATM 18848 H  H25  . A1IJH D 3 .   ? 16.393 31.884  26.074 1.00 14.42 ? 702  A1IJH A H25  1 
HETATM 18849 H  H26  . A1IJH D 3 .   ? 18.727 31.738  24.941 1.00 14.30 ? 702  A1IJH A H26  1 
HETATM 18850 H  H29  . A1IJH D 3 .   ? 18.602 36.313  24.101 1.00 12.20 ? 702  A1IJH A H29  1 
HETATM 18851 H  H301 . A1IJH D 3 .   ? 18.331 38.116  25.498 1.00 13.35 ? 702  A1IJH A H301 1 
HETATM 18852 H  H302 . A1IJH D 3 .   ? 18.019 37.910  26.940 1.00 13.35 ? 702  A1IJH A H302 1 
HETATM 18853 H  H33  . A1IJH D 3 .   ? 17.629 33.653  28.764 1.00 15.33 ? 702  A1IJH A H33  1 
HETATM 18854 H  H34  . A1IJH D 3 .   ? 16.942 31.561  28.410 1.00 14.78 ? 702  A1IJH A H34  1 
HETATM 18855 CL CL   . CL    E 4 .   ? 33.656 33.507  7.486  1.00 20.88 ? 703  CL    A CL   1 
HETATM 18856 MG MG   . MG    F 5 .   ? 31.544 23.119  44.076 0.74 28.93 ? 704  MG    A MG   1 
HETATM 18857 FE FE1  . SF4   G 2 .   ? 16.811 16.417  55.933 1.00 13.70 ? 701  SF4   B FE1  1 
HETATM 18858 FE FE2  . SF4   G 2 .   ? 16.339 18.789  54.785 1.00 12.99 ? 701  SF4   B FE2  1 
HETATM 18859 FE FE3  . SF4   G 2 .   ? 16.650 16.633  53.301 1.00 13.76 ? 701  SF4   B FE3  1 
HETATM 18860 FE FE4  . SF4   G 2 .   ? 18.731 17.663  54.537 1.00 13.00 ? 701  SF4   B FE4  1 
HETATM 18861 S  S1   . SF4   G 2 .   ? 17.564 18.712  52.833 1.00 12.52 ? 701  SF4   B S1   1 
HETATM 18862 S  S2   . SF4   G 2 .   ? 18.242 15.401  54.430 1.00 14.28 ? 701  SF4   B S2   1 
HETATM 18863 S  S3   . SF4   G 2 .   ? 17.818 18.402  56.515 1.00 12.47 ? 701  SF4   B S3   1 
HETATM 18864 S  S4   . SF4   G 2 .   ? 14.899 16.988  54.744 1.00 14.04 ? 701  SF4   B S4   1 
HETATM 18865 C  C1   . A1IJH H 3 .   ? 20.821 21.011  65.261 1.00 8.99  ? 702  A1IJH B C1   1 
HETATM 18866 C  C2   . A1IJH H 3 .   ? 20.564 22.513  65.363 1.00 10.49 ? 702  A1IJH B C2   1 
HETATM 18867 C  C3   . A1IJH H 3 .   ? 19.379 22.902  64.524 1.00 9.67  ? 702  A1IJH B C3   1 
HETATM 18868 S  S3   . A1IJH H 3 .   ? 18.070 21.843  64.406 1.00 11.25 ? 702  A1IJH B S3   1 
HETATM 18869 C  C4   . A1IJH H 3 .   ? 19.335 24.063  63.871 1.00 10.39 ? 702  A1IJH B C4   1 
HETATM 18870 S  S4   . A1IJH H 3 .   ? 17.922 24.526  63.109 1.00 11.39 ? 702  A1IJH B S4   1 
HETATM 18871 C  C5   . A1IJH H 3 .   ? 20.538 24.957  63.805 1.00 11.03 ? 702  A1IJH B C5   1 
HETATM 18872 N  N6   . A1IJH H 3 .   ? 21.226 24.859  62.534 1.00 11.55 ? 702  A1IJH B N6   1 
HETATM 18873 C  C7   . A1IJH H 3 .   ? 22.369 25.551  62.434 1.00 9.51  ? 702  A1IJH B C7   1 
HETATM 18874 C  C8   . A1IJH H 3 .   ? 22.869 26.123  61.168 1.00 9.07  ? 702  A1IJH B C8   1 
HETATM 18875 O  O8   . A1IJH H 3 .   ? 22.238 25.972  60.103 1.00 11.33 ? 702  A1IJH B O8   1 
HETATM 18876 N  N9   . A1IJH H 3 .   ? 24.019 26.801  61.201 1.00 9.83  ? 702  A1IJH B N9   1 
HETATM 18877 C  C10  . A1IJH H 3 .   ? 24.716 26.977  62.335 1.00 8.77  ? 702  A1IJH B C10  1 
HETATM 18878 N  N10  . A1IJH H 3 .   ? 25.873 27.675  62.284 1.00 11.64 ? 702  A1IJH B N10  1 
HETATM 18879 N  N11  . A1IJH H 3 .   ? 24.313 26.483  63.528 1.00 9.77  ? 702  A1IJH B N11  1 
HETATM 18880 C  C12  . A1IJH H 3 .   ? 23.174 25.781  63.642 1.00 9.58  ? 702  A1IJH B C12  1 
HETATM 18881 N  N13  . A1IJH H 3 .   ? 22.767 25.287  64.825 1.00 10.27 ? 702  A1IJH B N13  1 
HETATM 18882 C  C14  . A1IJH H 3 .   ? 21.492 24.603  64.942 1.00 12.25 ? 702  A1IJH B C14  1 
HETATM 18883 O  O2   . A1IJH H 3 .   ? 21.719 23.203  64.908 1.00 11.23 ? 702  A1IJH B O2   1 
HETATM 18884 C  C21  . A1IJH H 3 .   ? 19.897 20.656  59.858 1.00 13.51 ? 702  A1IJH B C21  1 
HETATM 18885 C  C22  . A1IJH H 3 .   ? 18.572 19.920  59.738 1.00 12.89 ? 702  A1IJH B C22  1 
HETATM 18886 C  C23  . A1IJH H 3 .   ? 17.614 20.488  60.746 1.00 12.56 ? 702  A1IJH B C23  1 
HETATM 18887 S  S23  . A1IJH H 3 .   ? 17.330 22.155  60.709 1.00 8.87  ? 702  A1IJH B S23  1 
HETATM 18888 C  C24  . A1IJH H 3 .   ? 16.985 19.714  61.628 1.00 14.02 ? 702  A1IJH B C24  1 
HETATM 18889 S  S24  . A1IJH H 3 .   ? 15.912 20.402  62.738 1.00 12.17 ? 702  A1IJH B S24  1 
HETATM 18890 C  C25  . A1IJH H 3 .   ? 17.175 18.227  61.625 1.00 13.44 ? 702  A1IJH B C25  1 
HETATM 18891 N  N26  . A1IJH H 3 .   ? 18.162 17.721  62.563 1.00 13.66 ? 702  A1IJH B N26  1 
HETATM 18892 C  C27  . A1IJH H 3 .   ? 18.330 16.388  62.503 1.00 12.13 ? 702  A1IJH B C27  1 
HETATM 18893 C  C28  . A1IJH H 3 .   ? 18.681 15.542  63.664 1.00 13.41 ? 702  A1IJH B C28  1 
HETATM 18894 O  O28  . A1IJH H 3 .   ? 18.864 16.037  64.792 1.00 11.07 ? 702  A1IJH B O28  1 
HETATM 18895 N  N29  . A1IJH H 3 .   ? 18.800 14.226  63.467 1.00 11.75 ? 702  A1IJH B N29  1 
HETATM 18896 C  C30  . A1IJH H 3 .   ? 18.608 13.656  62.266 1.00 11.46 ? 702  A1IJH B C30  1 
HETATM 18897 N  N30  . A1IJH H 3 .   ? 18.749 12.315  62.151 1.00 12.55 ? 702  A1IJH B N30  1 
HETATM 18898 N  N31  . A1IJH H 3 .   ? 18.281 14.367  61.161 1.00 12.00 ? 702  A1IJH B N31  1 
HETATM 18899 C  C32  . A1IJH H 3 .   ? 18.128 15.702  61.210 1.00 12.02 ? 702  A1IJH B C32  1 
HETATM 18900 N  N33  . A1IJH H 3 .   ? 17.800 16.409  60.113 1.00 13.98 ? 702  A1IJH B N33  1 
HETATM 18901 C  C34  . A1IJH H 3 .   ? 17.591 17.839  60.216 1.00 11.64 ? 702  A1IJH B C34  1 
HETATM 18902 O  O22  . A1IJH H 3 .   ? 18.799 18.528  59.947 1.00 10.10 ? 702  A1IJH B O22  1 
HETATM 18903 P  P1   . A1IJH H 3 .   ? 22.991 19.612  65.789 1.00 11.54 ? 702  A1IJH B P1   1 
HETATM 18904 O  O1P  . A1IJH H 3 .   ? 23.620 20.077  64.390 1.00 12.92 ? 702  A1IJH B O1P  1 
HETATM 18905 O  O2P  . A1IJH H 3 .   ? 24.065 19.657  66.840 1.00 9.64  ? 702  A1IJH B O2P  1 
HETATM 18906 O  O3P  . A1IJH H 3 .   ? 22.396 18.236  65.644 1.00 9.82  ? 702  A1IJH B O3P  1 
HETATM 18907 O  O4P  . A1IJH H 3 .   ? 21.829 20.643  66.197 1.00 10.44 ? 702  A1IJH B O4P  1 
HETATM 18908 P  P2   . A1IJH H 3 .   ? 22.361 20.188  59.161 1.00 11.30 ? 702  A1IJH B P2   1 
HETATM 18909 O  O5P  . A1IJH H 3 .   ? 22.679 19.337  60.481 1.00 8.93  ? 702  A1IJH B O5P  1 
HETATM 18910 O  O6P  . A1IJH H 3 .   ? 23.079 19.595  57.979 1.00 11.15 ? 702  A1IJH B O6P  1 
HETATM 18911 O  O7P  . A1IJH H 3 .   ? 22.761 21.625  59.387 1.00 12.30 ? 702  A1IJH B O7P  1 
HETATM 18912 O  O8P  . A1IJH H 3 .   ? 20.785 20.123  58.890 1.00 11.93 ? 702  A1IJH B O8P  1 
HETATM 18913 MG MG   . A1IJH H 3 .   ? 23.212 19.691  62.386 1.00 8.75  ? 702  A1IJH B MG   1 
HETATM 18914 W  W    . A1IJH H 3 .   ? 16.304 22.812  62.744 1.00 19.55 ? 702  A1IJH B W    1 
HETATM 18915 H  H12  . A1IJH H 3 .   ? 20.004 20.519  65.439 1.00 10.79 ? 702  A1IJH B H12  1 
HETATM 18916 H  H11  . A1IJH H 3 .   ? 21.100 20.780  64.361 1.00 10.79 ? 702  A1IJH B H11  1 
HETATM 18917 H  H2   . A1IJH H 3 .   ? 20.375 22.746  66.286 1.00 12.59 ? 702  A1IJH B H2   1 
HETATM 18918 H  H5   . A1IJH H 3 .   ? 20.233 25.873  63.895 1.00 13.24 ? 702  A1IJH B H5   1 
HETATM 18919 H  H6   . A1IJH H 3 .   ? 20.920 24.386  61.884 1.00 13.86 ? 702  A1IJH B H6   1 
HETATM 18920 H  H9   . A1IJH H 3 .   ? 24.324 27.137  60.470 1.00 11.80 ? 702  A1IJH B H9   1 
HETATM 18921 H  H102 . A1IJH H 3 .   ? 26.333 27.798  63.000 1.00 13.97 ? 702  A1IJH B H102 1 
HETATM 18922 H  H101 . A1IJH H 3 .   ? 26.149 27.996  61.535 1.00 13.97 ? 702  A1IJH B H101 1 
HETATM 18923 H  H13  . A1IJH H 3 .   ? 23.267 25.377  65.519 1.00 12.32 ? 702  A1IJH B H13  1 
HETATM 18924 H  H14  . A1IJH H 3 .   ? 21.086 24.882  65.778 1.00 14.71 ? 702  A1IJH B H14  1 
HETATM 18925 H  H211 . A1IJH H 3 .   ? 20.264 20.550  60.750 1.00 16.22 ? 702  A1IJH B H211 1 
HETATM 18926 H  H212 . A1IJH H 3 .   ? 19.771 21.607  59.715 1.00 16.22 ? 702  A1IJH B H212 1 
HETATM 18927 H  H22  . A1IJH H 3 .   ? 18.185 20.032  58.856 1.00 15.47 ? 702  A1IJH B H22  1 
HETATM 18928 H  H25  . A1IJH H 3 .   ? 16.335 17.833  61.909 1.00 16.14 ? 702  A1IJH B H25  1 
HETATM 18929 H  H26  . A1IJH H 3 .   ? 18.598 18.226  63.106 1.00 16.39 ? 702  A1IJH B H26  1 
HETATM 18930 H  H29  . A1IJH H 3 .   ? 19.007 13.725  64.134 1.00 14.11 ? 702  A1IJH B H29  1 
HETATM 18931 H  H301 . A1IJH H 3 .   ? 18.958 11.844  62.840 1.00 15.06 ? 702  A1IJH B H301 1 
HETATM 18932 H  H302 . A1IJH H 3 .   ? 18.630 11.934  61.389 1.00 15.06 ? 702  A1IJH B H302 1 
HETATM 18933 H  H33  . A1IJH H 3 .   ? 17.715 16.014  59.354 1.00 16.78 ? 702  A1IJH B H33  1 
HETATM 18934 H  H34  . A1IJH H 3 .   ? 16.899 18.074  59.578 1.00 13.97 ? 702  A1IJH B H34  1 
HETATM 18935 C  C1   . EDO   I 6 .   ? 13.497 18.205  88.736 1.00 30.32 ? 703  EDO   B C1   1 
HETATM 18936 O  O1   . EDO   I 6 .   ? 14.422 17.148  88.566 1.00 26.37 ? 703  EDO   B O1   1 
HETATM 18937 C  C2   . EDO   I 6 .   ? 12.212 17.801  89.351 1.00 35.63 ? 703  EDO   B C2   1 
HETATM 18938 O  O2   . EDO   I 6 .   ? 11.085 18.416  88.756 1.00 38.79 ? 703  EDO   B O2   1 
HETATM 18939 H  H11  . EDO   I 6 .   ? 13.317 18.605  87.871 1.00 36.39 ? 703  EDO   B H11  1 
HETATM 18940 H  H12  . EDO   I 6 .   ? 13.905 18.892  89.287 1.00 36.39 ? 703  EDO   B H12  1 
HETATM 18941 H  HO1  . EDO   I 6 .   ? 14.714 17.155  87.779 1.00 31.64 ? 703  EDO   B HO1  1 
HETATM 18942 H  H21  . EDO   I 6 .   ? 12.230 18.020  90.296 1.00 42.76 ? 703  EDO   B H21  1 
HETATM 18943 H  H22  . EDO   I 6 .   ? 12.119 16.838  89.285 1.00 42.76 ? 703  EDO   B H22  1 
HETATM 18944 H  HO2  . EDO   I 6 .   ? 11.252 19.226  88.611 1.00 46.55 ? 703  EDO   B HO2  1 
HETATM 18945 C  C1   . EDO   J 6 .   ? 21.272 -7.034  66.712 1.00 18.94 ? 704  EDO   B C1   1 
HETATM 18946 O  O1   . EDO   J 6 .   ? 21.444 -6.948  68.112 1.00 18.95 ? 704  EDO   B O1   1 
HETATM 18947 C  C2   . EDO   J 6 .   ? 20.546 -8.244  66.263 1.00 18.94 ? 704  EDO   B C2   1 
HETATM 18948 O  O2   . EDO   J 6 .   ? 20.909 -8.643  64.958 1.00 18.95 ? 704  EDO   B O2   1 
HETATM 18949 H  H11  . EDO   J 6 .   ? 22.144 -7.016  66.287 1.00 22.73 ? 704  EDO   B H11  1 
HETATM 18950 H  H12  . EDO   J 6 .   ? 20.791 -6.249  66.406 1.00 22.73 ? 704  EDO   B H12  1 
HETATM 18951 H  HO1  . EDO   J 6 .   ? 22.241 -7.128  68.308 1.00 22.74 ? 704  EDO   B HO1  1 
HETATM 18952 H  H21  . EDO   J 6 .   ? 19.592 -8.073  66.292 1.00 22.73 ? 704  EDO   B H21  1 
HETATM 18953 H  H22  . EDO   J 6 .   ? 20.723 -8.971  66.881 1.00 22.73 ? 704  EDO   B H22  1 
HETATM 18954 H  HO2  . EDO   J 6 .   ? 20.477 -9.331  64.745 1.00 22.75 ? 704  EDO   B HO2  1 
HETATM 18955 CL CL   . CL    K 4 .   ? 15.333 23.519  43.729 1.00 16.70 ? 705  CL    B CL   1 
HETATM 18956 CL CL   . CL    L 4 .   ? 33.552 19.105  80.547 1.00 28.93 ? 706  CL    B CL   1 
HETATM 18957 O  O    . HOH   M 7 .   ? 3.020  52.635  44.954 1.00 25.72 ? 801  HOH   A O    1 
HETATM 18958 O  O    . HOH   M 7 .   ? 35.536 31.325  8.588  1.00 25.66 ? 802  HOH   A O    1 
HETATM 18959 O  O    . HOH   M 7 .   ? 42.722 36.439  39.767 1.00 15.27 ? 803  HOH   A O    1 
HETATM 18960 O  O    . HOH   M 7 .   ? 40.338 30.432  43.315 1.00 15.96 ? 804  HOH   A O    1 
HETATM 18961 O  O    . HOH   M 7 .   ? 5.225  44.250  -7.014 1.00 36.12 ? 805  HOH   A O    1 
HETATM 18962 O  O    . HOH   M 7 .   ? 29.487 9.964   33.138 1.00 35.73 ? 806  HOH   A O    1 
HETATM 18963 O  O    . HOH   M 7 .   ? 54.491 29.043  26.297 1.00 40.70 ? 807  HOH   A O    1 
HETATM 18964 O  O    . HOH   M 7 .   ? 42.835 51.414  23.626 1.00 24.04 ? 808  HOH   A O    1 
HETATM 18965 O  O    . HOH   M 7 .   ? 39.382 31.348  41.092 1.00 23.93 ? 809  HOH   A O    1 
HETATM 18966 O  O    . HOH   M 7 .   ? 4.482  37.871  26.457 1.00 24.36 ? 810  HOH   A O    1 
HETATM 18967 O  O    . HOH   M 7 .   ? 1.897  11.276  22.649 1.00 36.43 ? 811  HOH   A O    1 
HETATM 18968 O  O    . HOH   M 7 .   ? -7.818 36.754  4.804  1.00 23.83 ? 812  HOH   A O    1 
HETATM 18969 O  O    . HOH   M 7 .   ? 40.671 17.365  30.161 1.00 18.78 ? 813  HOH   A O    1 
HETATM 18970 O  O    . HOH   M 7 .   ? -2.551 11.472  11.800 1.00 30.11 ? 814  HOH   A O    1 
HETATM 18971 O  O    . HOH   M 7 .   ? 42.880 47.063  41.209 1.00 34.19 ? 815  HOH   A O    1 
HETATM 18972 O  O    . HOH   M 7 .   ? 17.517 26.303  4.410  1.00 17.90 ? 816  HOH   A O    1 
HETATM 18973 O  O    . HOH   M 7 .   ? 31.033 29.836  38.206 1.00 26.88 ? 817  HOH   A O    1 
HETATM 18974 O  O    . HOH   M 7 .   ? 48.030 21.544  28.384 1.00 27.14 ? 818  HOH   A O    1 
HETATM 18975 O  O    . HOH   M 7 .   ? 21.780 59.102  11.901 1.00 31.60 ? 819  HOH   A O    1 
HETATM 18976 O  O    . HOH   M 7 .   ? 30.633 5.833   2.505  1.00 19.12 ? 820  HOH   A O    1 
HETATM 18977 O  O    A HOH   M 7 .   ? 19.654 56.002  -1.260 0.95 24.48 ? 821  HOH   A O    1 
HETATM 18978 O  O    . HOH   M 7 .   ? 23.823 31.390  38.919 1.00 24.48 ? 822  HOH   A O    1 
HETATM 18979 O  O    . HOH   M 7 .   ? 21.408 21.781  27.377 1.00 13.31 ? 823  HOH   A O    1 
HETATM 18980 O  O    . HOH   M 7 .   ? 15.146 27.205  23.411 1.00 11.64 ? 824  HOH   A O    1 
HETATM 18981 O  O    . HOH   M 7 .   ? 24.966 -0.707  16.953 1.00 34.86 ? 825  HOH   A O    1 
HETATM 18982 O  O    . HOH   M 7 .   ? 15.657 39.455  17.658 1.00 11.69 ? 826  HOH   A O    1 
HETATM 18983 O  O    . HOH   M 7 .   ? 4.031  13.638  31.613 1.00 25.95 ? 827  HOH   A O    1 
HETATM 18984 O  O    . HOH   M 7 .   ? 11.917 50.852  47.228 1.00 37.49 ? 828  HOH   A O    1 
HETATM 18985 O  O    . HOH   M 7 .   ? 29.600 50.432  10.784 1.00 19.56 ? 829  HOH   A O    1 
HETATM 18986 O  O    . HOH   M 7 .   ? 12.811 13.750  1.770  1.00 28.99 ? 830  HOH   A O    1 
HETATM 18987 O  O    . HOH   M 7 .   ? 29.911 0.494   12.394 1.00 28.46 ? 831  HOH   A O    1 
HETATM 18988 O  O    B HOH   M 7 .   ? 45.905 17.890  30.073 0.67 28.94 ? 832  HOH   A O    1 
HETATM 18989 O  O    . HOH   M 7 .   ? 16.882 2.866   21.244 1.00 29.48 ? 833  HOH   A O    1 
HETATM 18990 O  O    . HOH   M 7 .   ? -2.453 28.203  6.193  1.00 31.81 ? 834  HOH   A O    1 
HETATM 18991 O  O    . HOH   M 7 .   ? -6.116 28.616  9.734  1.00 31.92 ? 835  HOH   A O    1 
HETATM 18992 O  O    . HOH   M 7 .   ? 22.307 42.705  41.961 1.00 19.48 ? 836  HOH   A O    1 
HETATM 18993 O  O    . HOH   M 7 .   ? 18.540 9.556   23.995 1.00 11.66 ? 837  HOH   A O    1 
HETATM 18994 O  O    . HOH   M 7 .   ? 46.782 35.164  40.170 1.00 25.60 ? 838  HOH   A O    1 
HETATM 18995 O  O    . HOH   M 7 .   ? 40.039 44.235  43.795 1.00 22.61 ? 839  HOH   A O    1 
HETATM 18996 O  O    . HOH   M 7 .   ? 51.384 29.358  25.643 1.00 31.10 ? 840  HOH   A O    1 
HETATM 18997 O  O    . HOH   M 7 .   ? 1.483  37.179  36.443 1.00 22.98 ? 841  HOH   A O    1 
HETATM 18998 O  O    . HOH   M 7 .   ? 9.885  53.700  13.449 1.00 37.65 ? 842  HOH   A O    1 
HETATM 18999 O  O    . HOH   M 7 .   ? 28.274 22.960  8.336  1.00 11.39 ? 843  HOH   A O    1 
HETATM 19000 O  O    . HOH   M 7 .   ? 9.637  17.455  11.623 1.00 23.89 ? 844  HOH   A O    1 
HETATM 19001 O  O    . HOH   M 7 .   ? 14.901 25.773  -0.164 1.00 25.40 ? 845  HOH   A O    1 
HETATM 19002 O  O    . HOH   M 7 .   ? 3.389  53.547  23.103 1.00 38.87 ? 846  HOH   A O    1 
HETATM 19003 O  O    . HOH   M 7 .   ? 5.762  47.764  9.668  1.00 33.42 ? 847  HOH   A O    1 
HETATM 19004 O  O    . HOH   M 7 .   ? 4.847  10.426  32.945 1.00 34.05 ? 848  HOH   A O    1 
HETATM 19005 O  O    . HOH   M 7 .   ? 29.112 5.142   23.479 1.00 23.76 ? 849  HOH   A O    1 
HETATM 19006 O  O    . HOH   M 7 .   ? 5.966  26.146  0.755  1.00 18.49 ? 850  HOH   A O    1 
HETATM 19007 O  O    . HOH   M 7 .   ? 14.857 10.654  41.969 1.00 28.95 ? 851  HOH   A O    1 
HETATM 19008 O  O    . HOH   M 7 .   ? 0.827  39.752  40.014 1.00 35.78 ? 852  HOH   A O    1 
HETATM 19009 O  O    . HOH   M 7 .   ? 15.750 24.487  31.656 1.00 10.93 ? 853  HOH   A O    1 
HETATM 19010 O  O    . HOH   M 7 .   ? 49.976 36.092  16.448 1.00 35.95 ? 854  HOH   A O    1 
HETATM 19011 O  O    . HOH   M 7 .   ? 43.318 33.704  13.638 1.00 16.86 ? 855  HOH   A O    1 
HETATM 19012 O  O    . HOH   M 7 .   ? 33.499 36.302  3.783  1.00 28.59 ? 856  HOH   A O    1 
HETATM 19013 O  O    . HOH   M 7 .   ? 35.903 51.350  22.989 1.00 29.15 ? 857  HOH   A O    1 
HETATM 19014 O  O    . HOH   M 7 .   ? 25.878 26.135  16.336 1.00 9.69  ? 858  HOH   A O    1 
HETATM 19015 O  O    . HOH   M 7 .   ? 20.614 17.112  -4.122 1.00 26.94 ? 859  HOH   A O    1 
HETATM 19016 O  O    . HOH   M 7 .   ? 17.769 2.177   5.002  1.00 29.29 ? 860  HOH   A O    1 
HETATM 19017 O  O    . HOH   M 7 .   ? -3.180 25.591  6.775  1.00 29.62 ? 861  HOH   A O    1 
HETATM 19018 O  O    . HOH   M 7 .   ? 9.300  47.396  16.112 1.00 25.60 ? 862  HOH   A O    1 
HETATM 19019 O  O    . HOH   M 7 .   ? 34.541 15.436  32.208 1.00 26.03 ? 863  HOH   A O    1 
HETATM 19020 O  O    . HOH   M 7 .   ? 16.904 61.477  33.073 1.00 38.15 ? 864  HOH   A O    1 
HETATM 19021 O  O    . HOH   M 7 .   ? 26.556 35.985  33.721 1.00 9.39  ? 865  HOH   A O    1 
HETATM 19022 O  O    . HOH   M 7 .   ? 35.117 25.517  42.977 1.00 22.54 ? 866  HOH   A O    1 
HETATM 19023 O  O    . HOH   M 7 .   ? 30.962 46.924  46.145 1.00 33.95 ? 867  HOH   A O    1 
HETATM 19024 O  O    . HOH   M 7 .   ? 28.633 37.117  39.551 1.00 15.52 ? 868  HOH   A O    1 
HETATM 19025 O  O    . HOH   M 7 .   ? 0.665  25.281  8.909  1.00 16.14 ? 869  HOH   A O    1 
HETATM 19026 O  O    . HOH   M 7 .   ? 52.673 38.333  19.410 1.00 26.50 ? 870  HOH   A O    1 
HETATM 19027 O  O    . HOH   M 7 .   ? 4.789  10.285  11.942 1.00 28.07 ? 871  HOH   A O    1 
HETATM 19028 O  O    . HOH   M 7 .   ? -4.525 20.159  14.953 1.00 31.96 ? 872  HOH   A O    1 
HETATM 19029 O  O    . HOH   M 7 .   ? 2.521  7.532   24.323 1.00 28.72 ? 873  HOH   A O    1 
HETATM 19030 O  O    . HOH   M 7 .   ? 46.852 33.148  37.316 1.00 20.20 ? 874  HOH   A O    1 
HETATM 19031 O  O    . HOH   M 7 .   ? 33.502 45.943  3.781  1.00 29.81 ? 875  HOH   A O    1 
HETATM 19032 O  O    . HOH   M 7 .   ? -3.473 20.042  6.631  1.00 19.22 ? 876  HOH   A O    1 
HETATM 19033 O  O    . HOH   M 7 .   ? 3.882  27.239  -0.400 1.00 21.98 ? 877  HOH   A O    1 
HETATM 19034 O  O    . HOH   M 7 .   ? 17.295 13.322  42.066 1.00 34.70 ? 878  HOH   A O    1 
HETATM 19035 O  O    . HOH   M 7 .   ? 47.379 38.332  39.652 1.00 36.34 ? 879  HOH   A O    1 
HETATM 19036 O  O    . HOH   M 7 .   ? 32.109 51.594  17.232 1.00 24.81 ? 880  HOH   A O    1 
HETATM 19037 O  O    . HOH   M 7 .   ? 39.262 48.351  13.617 1.00 31.95 ? 881  HOH   A O    1 
HETATM 19038 O  O    . HOH   M 7 .   ? 54.515 30.244  19.010 1.00 39.80 ? 882  HOH   A O    1 
HETATM 19039 O  O    . HOH   M 7 .   ? 44.780 40.320  42.240 1.00 37.33 ? 883  HOH   A O    1 
HETATM 19040 O  O    . HOH   M 7 .   ? 3.267  51.859  27.313 1.00 29.42 ? 884  HOH   A O    1 
HETATM 19041 O  O    . HOH   M 7 .   ? 7.164  15.272  37.353 1.00 21.16 ? 885  HOH   A O    1 
HETATM 19042 O  O    . HOH   M 7 .   ? -1.590 27.679  24.366 1.00 33.26 ? 886  HOH   A O    1 
HETATM 19043 O  O    . HOH   M 7 .   ? 14.482 13.017  -0.410 1.00 30.55 ? 887  HOH   A O    1 
HETATM 19044 O  O    . HOH   M 7 .   ? 34.333 18.491  8.949  1.00 21.63 ? 888  HOH   A O    1 
HETATM 19045 O  O    . HOH   M 7 .   ? 48.395 47.742  21.667 1.00 20.18 ? 889  HOH   A O    1 
HETATM 19046 O  O    . HOH   M 7 .   ? 19.759 33.536  41.387 1.00 12.42 ? 890  HOH   A O    1 
HETATM 19047 O  O    . HOH   M 7 .   ? 19.558 7.678   36.319 1.00 19.07 ? 891  HOH   A O    1 
HETATM 19048 O  O    . HOH   M 7 .   ? 44.308 30.950  44.141 1.00 22.23 ? 892  HOH   A O    1 
HETATM 19049 O  O    . HOH   M 7 .   ? 29.285 -0.352  18.196 1.00 37.06 ? 893  HOH   A O    1 
HETATM 19050 O  O    . HOH   M 7 .   ? 8.382  53.957  34.340 1.00 26.66 ? 894  HOH   A O    1 
HETATM 19051 O  O    . HOH   M 7 .   ? 21.826 5.237   29.191 1.00 26.65 ? 895  HOH   A O    1 
HETATM 19052 O  O    . HOH   M 7 .   ? 24.132 23.280  30.027 1.00 10.96 ? 896  HOH   A O    1 
HETATM 19053 O  O    . HOH   M 7 .   ? 5.037  13.936  3.458  1.00 26.41 ? 897  HOH   A O    1 
HETATM 19054 O  O    . HOH   M 7 .   ? 42.021 17.494  24.469 1.00 14.88 ? 898  HOH   A O    1 
HETATM 19055 O  O    . HOH   M 7 .   ? 4.489  43.796  36.090 1.00 25.89 ? 899  HOH   A O    1 
HETATM 19056 O  O    . HOH   M 7 .   ? 26.250 27.217  36.229 1.00 17.97 ? 900  HOH   A O    1 
HETATM 19057 O  O    . HOH   M 7 .   ? 1.190  36.485  33.766 1.00 26.52 ? 901  HOH   A O    1 
HETATM 19058 O  O    . HOH   M 7 .   ? 33.425 56.817  30.793 1.00 25.13 ? 902  HOH   A O    1 
HETATM 19059 O  O    . HOH   M 7 .   ? 22.670 23.071  32.355 1.00 11.55 ? 903  HOH   A O    1 
HETATM 19060 O  O    . HOH   M 7 .   ? 6.898  50.003  37.384 1.00 36.50 ? 904  HOH   A O    1 
HETATM 19061 O  O    . HOH   M 7 .   ? 41.923 39.262  7.196  1.00 20.26 ? 905  HOH   A O    1 
HETATM 19062 O  O    . HOH   M 7 .   ? 25.495 0.361   20.020 1.00 28.93 ? 906  HOH   A O    1 
HETATM 19063 O  O    . HOH   M 7 .   ? 44.119 20.958  21.919 1.00 31.07 ? 907  HOH   A O    1 
HETATM 19064 O  O    . HOH   M 7 .   ? 10.647 32.321  42.516 1.00 26.91 ? 908  HOH   A O    1 
HETATM 19065 O  O    . HOH   M 7 .   ? 19.881 36.404  3.906  1.00 18.66 ? 909  HOH   A O    1 
HETATM 19066 O  O    . HOH   M 7 .   ? 37.398 12.557  26.014 1.00 29.70 ? 910  HOH   A O    1 
HETATM 19067 O  O    . HOH   M 7 .   ? 14.547 4.416   20.234 1.00 25.81 ? 911  HOH   A O    1 
HETATM 19068 O  O    . HOH   M 7 .   ? 12.920 27.676  45.134 1.00 21.11 ? 912  HOH   A O    1 
HETATM 19069 O  O    . HOH   M 7 .   ? 48.457 38.385  13.362 1.00 28.25 ? 913  HOH   A O    1 
HETATM 19070 O  O    . HOH   M 7 .   ? 25.483 22.236  -0.064 1.00 22.83 ? 914  HOH   A O    1 
HETATM 19071 O  O    . HOH   M 7 .   ? 39.296 14.494  26.045 1.00 29.75 ? 915  HOH   A O    1 
HETATM 19072 O  O    . HOH   M 7 .   ? 17.972 60.038  10.677 1.00 26.31 ? 916  HOH   A O    1 
HETATM 19073 O  O    . HOH   M 7 .   ? 16.740 39.281  5.678  1.00 15.07 ? 917  HOH   A O    1 
HETATM 19074 O  O    . HOH   M 7 .   ? 5.674  40.241  26.142 1.00 27.75 ? 918  HOH   A O    1 
HETATM 19075 O  O    . HOH   M 7 .   ? 37.029 15.291  33.490 1.00 38.11 ? 919  HOH   A O    1 
HETATM 19076 O  O    . HOH   M 7 .   ? 15.328 19.427  2.014  1.00 16.70 ? 920  HOH   A O    1 
HETATM 19077 O  O    . HOH   M 7 .   ? 30.292 35.931  5.018  1.00 14.18 ? 921  HOH   A O    1 
HETATM 19078 O  O    . HOH   M 7 .   ? 34.581 4.165   18.948 1.00 31.36 ? 922  HOH   A O    1 
HETATM 19079 O  O    . HOH   M 7 .   ? 35.174 29.408  38.891 1.00 23.11 ? 923  HOH   A O    1 
HETATM 19080 O  O    . HOH   M 7 .   ? 23.138 25.079  34.374 1.00 13.81 ? 924  HOH   A O    1 
HETATM 19081 O  O    . HOH   M 7 .   ? 8.507  25.089  41.412 1.00 29.67 ? 925  HOH   A O    1 
HETATM 19082 O  O    . HOH   M 7 .   ? 32.033 19.305  2.533  1.00 25.04 ? 926  HOH   A O    1 
HETATM 19083 O  O    . HOH   M 7 .   ? 13.870 14.197  41.085 1.00 29.06 ? 927  HOH   A O    1 
HETATM 19084 O  O    . HOH   M 7 .   ? 12.729 29.627  41.067 1.00 22.25 ? 928  HOH   A O    1 
HETATM 19085 O  O    . HOH   M 7 .   ? 17.997 3.411   23.456 1.00 27.54 ? 929  HOH   A O    1 
HETATM 19086 O  O    . HOH   M 7 .   ? 17.725 17.849  12.496 1.00 10.35 ? 930  HOH   A O    1 
HETATM 19087 O  O    . HOH   M 7 .   ? 27.526 8.074   -1.271 1.00 23.60 ? 931  HOH   A O    1 
HETATM 19088 O  O    . HOH   M 7 .   ? 36.384 17.849  36.244 1.00 27.05 ? 932  HOH   A O    1 
HETATM 19089 O  O    . HOH   M 7 .   ? 24.573 31.755  14.936 1.00 11.00 ? 933  HOH   A O    1 
HETATM 19090 O  O    . HOH   M 7 .   ? 31.046 18.818  8.746  1.00 13.94 ? 934  HOH   A O    1 
HETATM 19091 O  O    . HOH   M 7 .   ? 11.012 53.547  36.029 1.00 26.51 ? 935  HOH   A O    1 
HETATM 19092 O  O    . HOH   M 7 .   ? 9.451  48.525  1.482  1.00 26.30 ? 936  HOH   A O    1 
HETATM 19093 O  O    . HOH   M 7 .   ? 13.837 7.808   39.758 1.00 37.60 ? 937  HOH   A O    1 
HETATM 19094 O  O    . HOH   M 7 .   ? 5.321  44.800  13.128 1.00 23.27 ? 938  HOH   A O    1 
HETATM 19095 O  O    . HOH   M 7 .   ? 21.049 13.774  -3.324 1.00 24.19 ? 939  HOH   A O    1 
HETATM 19096 O  O    . HOH   M 7 .   ? 28.122 24.778  37.547 1.00 24.88 ? 940  HOH   A O    1 
HETATM 19097 O  O    . HOH   M 7 .   ? 33.970 51.286  35.574 1.00 23.80 ? 941  HOH   A O    1 
HETATM 19098 O  O    . HOH   M 7 .   ? 8.036  34.530  -2.941 1.00 20.16 ? 942  HOH   A O    1 
HETATM 19099 O  O    . HOH   M 7 .   ? 21.690 34.403  20.882 1.00 10.54 ? 943  HOH   A O    1 
HETATM 19100 O  O    . HOH   M 7 .   ? 30.007 -0.371  9.804  1.00 19.12 ? 944  HOH   A O    1 
HETATM 19101 O  O    . HOH   M 7 .   ? 19.903 5.531   10.177 1.00 13.33 ? 945  HOH   A O    1 
HETATM 19102 O  O    . HOH   M 7 .   ? 45.176 47.007  23.948 1.00 16.03 ? 946  HOH   A O    1 
HETATM 19103 O  O    . HOH   M 7 .   ? 22.270 13.853  45.735 1.00 27.50 ? 947  HOH   A O    1 
HETATM 19104 O  O    . HOH   M 7 .   ? 38.705 18.459  15.366 1.00 14.43 ? 948  HOH   A O    1 
HETATM 19105 O  O    . HOH   M 7 .   ? 17.041 16.611  45.385 1.00 24.73 ? 949  HOH   A O    1 
HETATM 19106 O  O    . HOH   M 7 .   ? 4.071  13.743  24.599 1.00 24.70 ? 950  HOH   A O    1 
HETATM 19107 O  O    . HOH   M 7 .   ? 16.392 31.772  -2.072 1.00 25.40 ? 951  HOH   A O    1 
HETATM 19108 O  O    . HOH   M 7 .   ? 50.341 23.038  25.613 1.00 28.17 ? 952  HOH   A O    1 
HETATM 19109 O  O    . HOH   M 7 .   ? 17.962 55.968  20.700 1.00 34.67 ? 953  HOH   A O    1 
HETATM 19110 O  O    . HOH   M 7 .   ? 37.694 48.563  36.474 1.00 22.32 ? 954  HOH   A O    1 
HETATM 19111 O  O    . HOH   M 7 .   ? 43.660 27.279  18.103 1.00 27.95 ? 955  HOH   A O    1 
HETATM 19112 O  O    . HOH   M 7 .   ? 42.053 22.961  13.426 1.00 29.78 ? 956  HOH   A O    1 
HETATM 19113 O  O    . HOH   M 7 .   ? 18.573 37.232  7.190  1.00 21.13 ? 957  HOH   A O    1 
HETATM 19114 O  O    . HOH   M 7 .   ? 12.600 35.660  20.790 1.00 11.47 ? 958  HOH   A O    1 
HETATM 19115 O  O    . HOH   M 7 .   ? -5.511 36.384  19.910 1.00 38.95 ? 959  HOH   A O    1 
HETATM 19116 O  O    . HOH   M 7 .   ? 0.017  41.044  13.214 1.00 17.51 ? 960  HOH   A O    1 
HETATM 19117 O  O    . HOH   M 7 .   ? 45.196 37.626  7.931  1.00 22.95 ? 961  HOH   A O    1 
HETATM 19118 O  O    . HOH   M 7 .   ? 11.095 10.457  5.181  1.00 24.00 ? 962  HOH   A O    1 
HETATM 19119 O  O    . HOH   M 7 .   ? 5.282  9.105   25.604 1.00 20.89 ? 963  HOH   A O    1 
HETATM 19120 O  O    . HOH   M 7 .   ? 11.294 49.813  9.723  1.00 19.55 ? 964  HOH   A O    1 
HETATM 19121 O  O    . HOH   M 7 .   ? 21.799 2.001   4.779  1.00 25.50 ? 965  HOH   A O    1 
HETATM 19122 O  O    . HOH   M 7 .   ? 22.271 51.373  1.357  1.00 30.67 ? 966  HOH   A O    1 
HETATM 19123 O  O    . HOH   M 7 .   ? 37.741 25.167  11.078 1.00 21.18 ? 967  HOH   A O    1 
HETATM 19124 O  O    . HOH   M 7 .   ? 3.567  43.011  32.787 1.00 26.19 ? 968  HOH   A O    1 
HETATM 19125 O  O    . HOH   M 7 .   ? -1.464 36.740  12.910 1.00 17.92 ? 969  HOH   A O    1 
HETATM 19126 O  O    . HOH   M 7 .   ? -4.037 18.552  10.187 1.00 27.30 ? 970  HOH   A O    1 
HETATM 19127 O  O    . HOH   M 7 .   ? 51.207 37.239  21.373 1.00 18.18 ? 971  HOH   A O    1 
HETATM 19128 O  O    . HOH   M 7 .   ? 3.733  36.943  42.977 1.00 31.04 ? 972  HOH   A O    1 
HETATM 19129 O  O    . HOH   M 7 .   ? 41.419 18.095  15.356 1.00 28.23 ? 973  HOH   A O    1 
HETATM 19130 O  O    . HOH   M 7 .   ? 31.552 44.612  1.992  1.00 21.25 ? 974  HOH   A O    1 
HETATM 19131 O  O    . HOH   M 7 .   ? 27.886 1.570   19.564 1.00 24.17 ? 975  HOH   A O    1 
HETATM 19132 O  O    . HOH   M 7 .   ? 41.491 14.189  32.660 1.00 44.62 ? 976  HOH   A O    1 
HETATM 19133 O  O    . HOH   M 7 .   ? 38.225 20.927  14.196 1.00 18.80 ? 977  HOH   A O    1 
HETATM 19134 O  O    . HOH   M 7 .   ? 46.465 25.057  37.954 1.00 17.27 ? 978  HOH   A O    1 
HETATM 19135 O  O    . HOH   M 7 .   ? 3.140  20.456  38.618 1.00 35.81 ? 979  HOH   A O    1 
HETATM 19136 O  O    . HOH   M 7 .   ? 21.221 39.446  4.375  1.00 21.43 ? 980  HOH   A O    1 
HETATM 19137 O  O    . HOH   M 7 .   ? 19.907 29.652  3.827  1.00 14.75 ? 981  HOH   A O    1 
HETATM 19138 O  O    . HOH   M 7 .   ? 24.881 45.443  41.452 1.00 21.39 ? 982  HOH   A O    1 
HETATM 19139 O  O    . HOH   M 7 .   ? 32.823 58.648  26.038 1.00 30.76 ? 983  HOH   A O    1 
HETATM 19140 O  O    . HOH   M 7 .   ? 37.321 17.576  10.842 1.00 16.87 ? 984  HOH   A O    1 
HETATM 19141 O  O    . HOH   M 7 .   ? 33.745 7.910   21.206 1.00 21.07 ? 985  HOH   A O    1 
HETATM 19142 O  O    . HOH   M 7 .   ? 3.543  37.868  -0.458 1.00 24.89 ? 986  HOH   A O    1 
HETATM 19143 O  O    . HOH   M 7 .   ? 22.154 30.112  41.552 1.00 19.49 ? 987  HOH   A O    1 
HETATM 19144 O  O    . HOH   M 7 .   ? 46.818 43.935  15.776 1.00 22.36 ? 988  HOH   A O    1 
HETATM 19145 O  O    . HOH   M 7 .   ? 18.550 27.337  32.013 1.00 11.78 ? 989  HOH   A O    1 
HETATM 19146 O  O    . HOH   M 7 .   ? 4.089  49.766  34.071 1.00 33.04 ? 990  HOH   A O    1 
HETATM 19147 O  O    . HOH   M 7 .   ? 20.078 36.218  35.044 1.00 13.31 ? 991  HOH   A O    1 
HETATM 19148 O  O    . HOH   M 7 .   ? -4.416 35.594  11.062 1.00 25.29 ? 992  HOH   A O    1 
HETATM 19149 O  O    . HOH   M 7 .   ? 47.333 28.441  15.868 1.00 30.94 ? 993  HOH   A O    1 
HETATM 19150 O  O    . HOH   M 7 .   ? 15.000 56.316  14.952 1.00 25.60 ? 994  HOH   A O    1 
HETATM 19151 O  O    . HOH   M 7 .   ? 7.093  8.945   15.261 1.00 23.38 ? 995  HOH   A O    1 
HETATM 19152 O  O    . HOH   M 7 .   ? 27.633 -4.247  4.888  1.00 35.55 ? 996  HOH   A O    1 
HETATM 19153 O  O    . HOH   M 7 .   ? 6.392  54.297  27.314 1.00 26.03 ? 997  HOH   A O    1 
HETATM 19154 O  O    . HOH   M 7 .   ? 21.110 10.810  34.274 1.00 12.29 ? 998  HOH   A O    1 
HETATM 19155 O  O    . HOH   M 7 .   ? 34.364 53.563  23.240 1.00 24.94 ? 999  HOH   A O    1 
HETATM 19156 O  O    . HOH   M 7 .   ? 19.903 60.219  40.003 1.00 33.74 ? 1000 HOH   A O    1 
HETATM 19157 O  O    . HOH   M 7 .   ? 38.732 24.646  43.239 1.00 14.70 ? 1001 HOH   A O    1 
HETATM 19158 O  O    . HOH   M 7 .   ? 19.239 51.450  0.546  1.00 24.78 ? 1002 HOH   A O    1 
HETATM 19159 O  O    . HOH   M 7 .   ? 7.258  18.129  28.621 1.00 13.17 ? 1003 HOH   A O    1 
HETATM 19160 O  O    . HOH   M 7 .   ? 28.908 53.632  6.514  1.00 34.75 ? 1004 HOH   A O    1 
HETATM 19161 O  O    . HOH   M 7 .   ? 44.547 48.038  19.785 1.00 19.19 ? 1005 HOH   A O    1 
HETATM 19162 O  O    . HOH   M 7 .   ? 47.849 26.866  19.561 1.00 29.16 ? 1006 HOH   A O    1 
HETATM 19163 O  O    . HOH   M 7 .   ? 11.382 17.869  -0.329 1.00 26.56 ? 1007 HOH   A O    1 
HETATM 19164 O  O    . HOH   M 7 .   ? 22.256 27.233  41.634 1.00 15.38 ? 1008 HOH   A O    1 
HETATM 19165 O  O    . HOH   M 7 .   ? 5.234  52.817  34.006 1.00 35.38 ? 1009 HOH   A O    1 
HETATM 19166 O  O    . HOH   M 7 .   ? 13.348 47.236  9.249  1.00 15.36 ? 1010 HOH   A O    1 
HETATM 19167 O  O    . HOH   M 7 .   ? 33.252 37.298  42.723 1.00 19.02 ? 1011 HOH   A O    1 
HETATM 19168 O  O    . HOH   M 7 .   ? 4.376  29.967  -4.902 1.00 27.60 ? 1012 HOH   A O    1 
HETATM 19169 O  O    . HOH   M 7 .   ? 11.533 57.898  42.740 1.00 39.81 ? 1013 HOH   A O    1 
HETATM 19170 O  O    . HOH   M 7 .   ? 21.895 26.192  29.256 1.00 11.51 ? 1014 HOH   A O    1 
HETATM 19171 O  O    . HOH   M 7 .   ? 18.855 1.240   16.738 1.00 31.89 ? 1015 HOH   A O    1 
HETATM 19172 O  O    . HOH   M 7 .   ? 8.569  42.316  -0.702 1.00 17.86 ? 1016 HOH   A O    1 
HETATM 19173 O  O    . HOH   M 7 .   ? 16.589 46.344  -3.865 1.00 24.40 ? 1017 HOH   A O    1 
HETATM 19174 O  O    . HOH   M 7 .   ? 52.747 44.334  26.084 1.00 30.93 ? 1018 HOH   A O    1 
HETATM 19175 O  O    . HOH   M 7 .   ? 23.262 17.058  31.717 1.00 12.81 ? 1019 HOH   A O    1 
HETATM 19176 O  O    . HOH   M 7 .   ? 18.648 10.056  39.853 1.00 25.17 ? 1020 HOH   A O    1 
HETATM 19177 O  O    . HOH   M 7 .   ? 0.870  28.467  27.931 1.00 29.61 ? 1021 HOH   A O    1 
HETATM 19178 O  O    . HOH   M 7 .   ? 10.401 13.041  4.675  1.00 31.19 ? 1022 HOH   A O    1 
HETATM 19179 O  O    . HOH   M 7 .   ? 25.941 23.021  9.355  1.00 8.82  ? 1023 HOH   A O    1 
HETATM 19180 O  O    . HOH   M 7 .   ? 7.696  30.961  41.728 1.00 35.04 ? 1024 HOH   A O    1 
HETATM 19181 O  O    . HOH   M 7 .   ? 20.565 9.549   38.077 1.00 20.49 ? 1025 HOH   A O    1 
HETATM 19182 O  O    . HOH   M 7 .   ? 31.618 10.677  22.920 1.00 18.79 ? 1026 HOH   A O    1 
HETATM 19183 O  O    . HOH   M 7 .   ? 18.321 32.671  8.861  1.00 11.22 ? 1027 HOH   A O    1 
HETATM 19184 O  O    . HOH   M 7 .   ? 8.490  7.569   17.426 1.00 29.52 ? 1028 HOH   A O    1 
HETATM 19185 O  O    . HOH   M 7 .   ? 21.920 22.134  2.534  1.00 16.02 ? 1029 HOH   A O    1 
HETATM 19186 O  O    . HOH   M 7 .   ? 12.038 56.189  35.897 1.00 29.81 ? 1030 HOH   A O    1 
HETATM 19187 O  O    . HOH   M 7 .   ? 34.749 25.280  22.941 1.00 10.77 ? 1031 HOH   A O    1 
HETATM 19188 O  O    . HOH   M 7 .   ? 36.138 -0.483  6.786  1.00 30.47 ? 1032 HOH   A O    1 
HETATM 19189 O  O    . HOH   M 7 .   ? 6.843  47.306  44.260 1.00 24.99 ? 1033 HOH   A O    1 
HETATM 19190 O  O    . HOH   M 7 .   ? 20.727 59.463  34.582 1.00 32.39 ? 1034 HOH   A O    1 
HETATM 19191 O  O    . HOH   M 7 .   ? 34.996 -4.035  4.100  1.00 35.04 ? 1035 HOH   A O    1 
HETATM 19192 O  O    . HOH   M 7 .   ? 16.304 14.385  -2.944 1.00 30.94 ? 1036 HOH   A O    1 
HETATM 19193 O  O    . HOH   M 7 .   ? 30.750 54.839  15.016 1.00 34.49 ? 1037 HOH   A O    1 
HETATM 19194 O  O    . HOH   M 7 .   ? -0.235 30.733  30.707 1.00 26.46 ? 1038 HOH   A O    1 
HETATM 19195 O  O    . HOH   M 7 .   ? 16.331 49.071  -1.016 1.00 21.45 ? 1039 HOH   A O    1 
HETATM 19196 O  O    . HOH   M 7 .   ? 4.449  20.080  29.518 1.00 17.70 ? 1040 HOH   A O    1 
HETATM 19197 O  O    . HOH   M 7 .   ? 25.774 30.977  4.851  1.00 15.98 ? 1041 HOH   A O    1 
HETATM 19198 O  O    . HOH   M 7 .   ? 47.246 38.969  10.591 1.00 23.77 ? 1042 HOH   A O    1 
HETATM 19199 O  O    . HOH   M 7 .   ? 38.005 3.004   16.609 1.00 34.68 ? 1043 HOH   A O    1 
HETATM 19200 O  O    . HOH   M 7 .   ? 36.345 5.062   10.099 1.00 24.35 ? 1044 HOH   A O    1 
HETATM 19201 O  O    . HOH   M 7 .   ? 40.961 23.518  41.964 1.00 19.46 ? 1045 HOH   A O    1 
HETATM 19202 O  O    . HOH   M 7 .   ? 33.374 28.096  6.100  1.00 26.04 ? 1046 HOH   A O    1 
HETATM 19203 O  O    . HOH   M 7 .   ? 0.305  24.539  4.961  1.00 19.58 ? 1047 HOH   A O    1 
HETATM 19204 O  O    . HOH   M 7 .   ? 51.545 38.468  32.620 1.00 31.75 ? 1048 HOH   A O    1 
HETATM 19205 O  O    . HOH   M 7 .   ? 1.642  37.627  7.038  1.00 14.26 ? 1049 HOH   A O    1 
HETATM 19206 O  O    . HOH   M 7 .   ? 14.745 33.937  -0.499 1.00 21.49 ? 1050 HOH   A O    1 
HETATM 19207 O  O    . HOH   M 7 .   ? 27.069 -0.008  10.199 1.00 24.70 ? 1051 HOH   A O    1 
HETATM 19208 O  O    . HOH   M 7 .   ? 25.244 58.135  34.173 1.00 28.96 ? 1052 HOH   A O    1 
HETATM 19209 O  O    . HOH   M 7 .   ? 13.042 19.304  34.940 1.00 13.30 ? 1053 HOH   A O    1 
HETATM 19210 O  O    . HOH   M 7 .   ? 28.199 38.900  41.766 1.00 22.15 ? 1054 HOH   A O    1 
HETATM 19211 O  O    . HOH   M 7 .   ? -4.789 38.082  3.163  1.00 33.34 ? 1055 HOH   A O    1 
HETATM 19212 O  O    . HOH   M 7 .   ? 1.774  16.362  13.385 1.00 16.38 ? 1056 HOH   A O    1 
HETATM 19213 O  O    . HOH   M 7 .   ? 46.879 22.817  34.321 1.00 28.15 ? 1057 HOH   A O    1 
HETATM 19214 O  O    . HOH   M 7 .   ? 30.993 21.147  31.745 1.00 12.26 ? 1058 HOH   A O    1 
HETATM 19215 O  O    . HOH   M 7 .   ? -7.399 31.767  11.768 1.00 29.63 ? 1059 HOH   A O    1 
HETATM 19216 O  O    . HOH   M 7 .   ? 40.321 35.615  15.107 1.00 12.30 ? 1060 HOH   A O    1 
HETATM 19217 O  O    . HOH   M 7 .   ? 35.931 9.016   6.240  1.00 26.90 ? 1061 HOH   A O    1 
HETATM 19218 O  O    . HOH   M 7 .   ? 14.909 54.950  19.020 1.00 19.52 ? 1062 HOH   A O    1 
HETATM 19219 O  O    . HOH   M 7 .   ? 47.236 50.556  21.660 1.00 25.66 ? 1063 HOH   A O    1 
HETATM 19220 O  O    . HOH   M 7 .   ? 32.080 57.809  28.679 1.00 30.43 ? 1064 HOH   A O    1 
HETATM 19221 O  O    . HOH   M 7 .   ? 20.613 24.173  3.984  1.00 21.25 ? 1065 HOH   A O    1 
HETATM 19222 O  O    . HOH   M 7 .   ? 10.476 52.278  2.150  1.00 24.73 ? 1066 HOH   A O    1 
HETATM 19223 O  O    . HOH   M 7 .   ? 26.616 47.708  30.421 1.00 13.40 ? 1067 HOH   A O    1 
HETATM 19224 O  O    . HOH   M 7 .   ? 2.486  30.939  40.397 1.00 36.87 ? 1068 HOH   A O    1 
HETATM 19225 O  O    . HOH   M 7 .   ? 49.259 43.123  28.917 1.00 28.98 ? 1069 HOH   A O    1 
HETATM 19226 O  O    . HOH   M 7 .   ? 12.847 8.074   30.628 1.00 15.03 ? 1070 HOH   A O    1 
HETATM 19227 O  O    . HOH   M 7 .   ? -4.076 8.329   7.074  1.00 35.38 ? 1071 HOH   A O    1 
HETATM 19228 O  O    . HOH   M 7 .   ? 9.588  5.935   12.774 1.00 33.99 ? 1072 HOH   A O    1 
HETATM 19229 O  O    . HOH   M 7 .   ? 14.636 7.044   29.098 1.00 17.75 ? 1073 HOH   A O    1 
HETATM 19230 O  O    . HOH   M 7 .   ? 18.441 21.866  3.142  1.00 19.90 ? 1074 HOH   A O    1 
HETATM 19231 O  O    . HOH   M 7 .   ? 39.575 44.148  11.720 1.00 20.78 ? 1075 HOH   A O    1 
HETATM 19232 O  O    . HOH   M 7 .   ? 28.617 26.637  17.490 1.00 11.23 ? 1076 HOH   A O    1 
HETATM 19233 O  O    . HOH   M 7 .   ? 23.335 47.663  41.905 1.00 20.90 ? 1077 HOH   A O    1 
HETATM 19234 O  O    . HOH   M 7 .   ? -2.461 15.912  20.391 1.00 33.00 ? 1078 HOH   A O    1 
HETATM 19235 O  O    . HOH   M 7 .   ? 42.776 48.618  33.493 1.00 27.43 ? 1079 HOH   A O    1 
HETATM 19236 O  O    . HOH   M 7 .   ? 24.584 21.167  2.184  1.00 17.05 ? 1080 HOH   A O    1 
HETATM 19237 O  O    . HOH   M 7 .   ? 33.241 29.843  36.829 1.00 19.58 ? 1081 HOH   A O    1 
HETATM 19238 O  O    . HOH   M 7 .   ? 10.438 39.557  -1.918 1.00 25.35 ? 1082 HOH   A O    1 
HETATM 19239 O  O    . HOH   M 7 .   ? 36.249 2.603   8.468  1.00 25.93 ? 1083 HOH   A O    1 
HETATM 19240 O  O    . HOH   M 7 .   ? 24.905 35.182  -0.394 1.00 22.89 ? 1084 HOH   A O    1 
HETATM 19241 O  O    . HOH   M 7 .   ? 52.680 33.250  27.045 1.00 33.10 ? 1085 HOH   A O    1 
HETATM 19242 O  O    . HOH   M 7 .   ? 3.175  43.002  40.078 1.00 28.25 ? 1086 HOH   A O    1 
HETATM 19243 O  O    . HOH   M 7 .   ? 33.791 27.636  33.387 1.00 14.58 ? 1087 HOH   A O    1 
HETATM 19244 O  O    . HOH   M 7 .   ? 24.580 11.754  43.490 1.00 23.54 ? 1088 HOH   A O    1 
HETATM 19245 O  O    . HOH   M 7 .   ? 32.133 50.905  20.763 1.00 23.14 ? 1089 HOH   A O    1 
HETATM 19246 O  O    . HOH   M 7 .   ? 9.374  57.449  29.140 1.00 35.12 ? 1090 HOH   A O    1 
HETATM 19247 O  O    . HOH   M 7 .   ? 21.381 31.680  25.149 1.00 10.08 ? 1091 HOH   A O    1 
HETATM 19248 O  O    . HOH   M 7 .   ? 43.178 53.164  25.741 1.00 18.99 ? 1092 HOH   A O    1 
HETATM 19249 O  O    . HOH   M 7 .   ? 29.373 51.809  40.524 1.00 37.26 ? 1093 HOH   A O    1 
HETATM 19250 O  O    . HOH   M 7 .   ? 50.540 40.904  39.135 1.00 41.58 ? 1094 HOH   A O    1 
HETATM 19251 O  O    . HOH   M 7 .   ? 15.165 21.742  30.979 1.00 12.36 ? 1095 HOH   A O    1 
HETATM 19252 O  O    . HOH   M 7 .   ? 31.875 37.187  1.410  1.00 34.99 ? 1096 HOH   A O    1 
HETATM 19253 O  O    . HOH   M 7 .   ? 22.653 28.372  25.385 1.00 10.15 ? 1097 HOH   A O    1 
HETATM 19254 O  O    . HOH   M 7 .   ? 52.055 37.334  28.490 1.00 27.31 ? 1098 HOH   A O    1 
HETATM 19255 O  O    . HOH   M 7 .   ? 39.146 51.661  33.628 1.00 20.08 ? 1099 HOH   A O    1 
HETATM 19256 O  O    . HOH   M 7 .   ? 34.749 51.730  17.221 1.00 23.94 ? 1100 HOH   A O    1 
HETATM 19257 O  O    . HOH   M 7 .   ? 8.076  51.791  17.663 1.00 21.62 ? 1101 HOH   A O    1 
HETATM 19258 O  O    . HOH   M 7 .   ? 6.171  6.362   12.361 1.00 31.81 ? 1102 HOH   A O    1 
HETATM 19259 O  O    . HOH   M 7 .   ? 14.750 31.379  41.563 1.00 20.26 ? 1103 HOH   A O    1 
HETATM 19260 O  O    . HOH   M 7 .   ? 33.969 39.640  44.221 1.00 26.80 ? 1104 HOH   A O    1 
HETATM 19261 O  O    . HOH   M 7 .   ? 49.626 41.192  30.738 1.00 17.80 ? 1105 HOH   A O    1 
HETATM 19262 O  O    . HOH   M 7 .   ? 27.394 50.848  36.834 1.00 23.84 ? 1106 HOH   A O    1 
HETATM 19263 O  O    . HOH   M 7 .   ? 54.812 32.982  23.016 1.00 36.54 ? 1107 HOH   A O    1 
HETATM 19264 O  O    . HOH   M 7 .   ? 31.937 30.888  7.129  1.00 20.10 ? 1108 HOH   A O    1 
HETATM 19265 O  O    . HOH   M 7 .   ? 29.733 2.044   21.599 1.00 33.96 ? 1109 HOH   A O    1 
HETATM 19266 O  O    . HOH   M 7 .   ? -1.598 18.842  2.080  1.00 28.10 ? 1110 HOH   A O    1 
HETATM 19267 O  O    . HOH   M 7 .   ? 39.375 54.691  30.220 1.00 19.59 ? 1111 HOH   A O    1 
HETATM 19268 O  O    . HOH   M 7 .   ? 25.494 12.210  -4.366 1.00 22.79 ? 1112 HOH   A O    1 
HETATM 19269 O  O    . HOH   M 7 .   ? 20.164 18.209  9.777  1.00 10.56 ? 1113 HOH   A O    1 
HETATM 19270 O  O    . HOH   M 7 .   ? 9.692  25.133  -2.999 1.00 33.27 ? 1114 HOH   A O    1 
HETATM 19271 O  O    . HOH   M 7 .   ? 16.482 53.191  -1.234 1.00 25.06 ? 1115 HOH   A O    1 
HETATM 19272 O  O    . HOH   M 7 .   ? 44.424 51.997  29.972 1.00 19.78 ? 1116 HOH   A O    1 
HETATM 19273 O  O    . HOH   M 7 .   ? 29.877 35.342  43.341 1.00 20.15 ? 1117 HOH   A O    1 
HETATM 19274 O  O    . HOH   M 7 .   ? 23.967 1.307   0.661  1.00 31.33 ? 1118 HOH   A O    1 
HETATM 19275 O  O    . HOH   M 7 .   ? 34.413 24.599  39.614 1.00 17.73 ? 1119 HOH   A O    1 
HETATM 19276 O  O    . HOH   M 7 .   ? 41.994 44.517  41.750 1.00 25.04 ? 1120 HOH   A O    1 
HETATM 19277 O  O    . HOH   M 7 .   ? 44.479 30.275  14.298 1.00 24.71 ? 1121 HOH   A O    1 
HETATM 19278 O  O    . HOH   M 7 .   ? 2.798  19.206  33.508 1.00 23.41 ? 1122 HOH   A O    1 
HETATM 19279 O  O    . HOH   M 7 .   ? 48.882 46.633  28.729 1.00 26.03 ? 1123 HOH   A O    1 
HETATM 19280 O  O    . HOH   M 7 .   ? 23.264 59.405  15.806 1.00 34.98 ? 1124 HOH   A O    1 
HETATM 19281 O  O    . HOH   M 7 .   ? 6.680  51.137  47.319 1.00 27.32 ? 1125 HOH   A O    1 
HETATM 19282 O  O    . HOH   M 7 .   ? 4.478  23.134  -1.370 1.00 28.93 ? 1126 HOH   A O    1 
HETATM 19283 O  O    . HOH   M 7 .   ? 29.900 30.455  5.293  1.00 26.97 ? 1127 HOH   A O    1 
HETATM 19284 O  O    . HOH   M 7 .   ? 13.519 2.801   28.572 1.00 25.81 ? 1128 HOH   A O    1 
HETATM 19285 O  O    . HOH   M 7 .   ? 49.237 45.275  16.304 1.00 30.55 ? 1129 HOH   A O    1 
HETATM 19286 O  O    . HOH   M 7 .   ? 22.436 29.155  35.873 1.00 14.33 ? 1130 HOH   A O    1 
HETATM 19287 O  O    . HOH   M 7 .   ? -0.904 25.098  21.831 1.00 32.17 ? 1131 HOH   A O    1 
HETATM 19288 O  O    . HOH   M 7 .   ? 40.282 36.621  38.091 1.00 14.29 ? 1132 HOH   A O    1 
HETATM 19289 O  O    . HOH   M 7 .   ? 18.315 38.924  -3.483 1.00 31.38 ? 1133 HOH   A O    1 
HETATM 19290 O  O    . HOH   M 7 .   ? 31.045 14.898  3.742  1.00 14.44 ? 1134 HOH   A O    1 
HETATM 19291 O  O    . HOH   M 7 .   ? 36.379 30.506  44.228 1.00 18.56 ? 1135 HOH   A O    1 
HETATM 19292 O  O    . HOH   M 7 .   ? 32.461 13.020  -2.016 1.00 18.41 ? 1136 HOH   A O    1 
HETATM 19293 O  O    . HOH   M 7 .   ? 41.420 41.900  15.478 1.00 14.67 ? 1137 HOH   A O    1 
HETATM 19294 O  O    . HOH   M 7 .   ? 19.626 40.682  -1.487 1.00 27.91 ? 1138 HOH   A O    1 
HETATM 19295 O  O    . HOH   M 7 .   ? 45.060 41.938  12.787 1.00 23.79 ? 1139 HOH   A O    1 
HETATM 19296 O  O    . HOH   M 7 .   ? 44.805 40.198  37.067 1.00 21.53 ? 1140 HOH   A O    1 
HETATM 19297 O  O    . HOH   M 7 .   ? 30.354 48.095  38.809 1.00 25.53 ? 1141 HOH   A O    1 
HETATM 19298 O  O    . HOH   M 7 .   ? 25.174 40.886  0.041  1.00 24.78 ? 1142 HOH   A O    1 
HETATM 19299 O  O    . HOH   M 7 .   ? 33.200 10.870  25.172 1.00 27.15 ? 1143 HOH   A O    1 
HETATM 19300 O  O    . HOH   M 7 .   ? 18.235 20.627  12.370 1.00 11.21 ? 1144 HOH   A O    1 
HETATM 19301 O  O    . HOH   M 7 .   ? 21.985 58.355  21.984 1.00 22.48 ? 1145 HOH   A O    1 
HETATM 19302 O  O    . HOH   M 7 .   ? 23.652 56.883  11.011 1.00 26.56 ? 1146 HOH   A O    1 
HETATM 19303 O  O    . HOH   M 7 .   ? 15.695 39.209  41.008 1.00 23.54 ? 1147 HOH   A O    1 
HETATM 19304 O  O    . HOH   M 7 .   ? -7.606 37.372  8.733  1.00 38.38 ? 1148 HOH   A O    1 
HETATM 19305 O  O    . HOH   M 7 .   ? 15.438 4.837   22.840 1.00 19.66 ? 1149 HOH   A O    1 
HETATM 19306 O  O    . HOH   M 7 .   ? -3.515 33.624  25.900 1.00 32.09 ? 1150 HOH   A O    1 
HETATM 19307 O  O    . HOH   M 7 .   ? 10.275 50.986  13.698 1.00 24.96 ? 1151 HOH   A O    1 
HETATM 19308 O  O    . HOH   M 7 .   ? 42.116 48.967  17.382 1.00 26.58 ? 1152 HOH   A O    1 
HETATM 19309 O  O    . HOH   M 7 .   ? 1.335  39.579  32.673 1.00 31.37 ? 1153 HOH   A O    1 
HETATM 19310 O  O    . HOH   M 7 .   ? 21.816 31.826  -2.169 1.00 31.95 ? 1154 HOH   A O    1 
HETATM 19311 O  O    . HOH   M 7 .   ? 24.955 55.837  14.780 1.00 25.67 ? 1155 HOH   A O    1 
HETATM 19312 O  O    . HOH   M 7 .   ? 29.250 8.791   41.929 1.00 31.94 ? 1156 HOH   A O    1 
HETATM 19313 O  O    . HOH   M 7 .   ? 13.442 5.040   9.788  1.00 27.27 ? 1157 HOH   A O    1 
HETATM 19314 O  O    . HOH   M 7 .   ? 13.354 5.361   16.899 1.00 25.43 ? 1158 HOH   A O    1 
HETATM 19315 O  O    . HOH   M 7 .   ? 36.989 30.549  41.542 1.00 24.24 ? 1159 HOH   A O    1 
HETATM 19316 O  O    . HOH   M 7 .   ? 28.176 21.110  35.547 1.00 16.04 ? 1160 HOH   A O    1 
HETATM 19317 O  O    . HOH   M 7 .   ? 36.668 11.083  7.700  1.00 22.16 ? 1161 HOH   A O    1 
HETATM 19318 O  O    . HOH   M 7 .   ? 23.890 9.522   32.338 1.00 17.54 ? 1162 HOH   A O    1 
HETATM 19319 O  O    . HOH   M 7 .   ? 23.526 56.557  32.745 1.00 35.51 ? 1163 HOH   A O    1 
HETATM 19320 O  O    . HOH   M 7 .   ? 3.622  46.484  4.232  1.00 29.62 ? 1164 HOH   A O    1 
HETATM 19321 O  O    . HOH   M 7 .   ? 36.888 45.811  46.719 1.00 34.09 ? 1165 HOH   A O    1 
HETATM 19322 O  O    . HOH   M 7 .   ? 17.783 48.834  44.550 1.00 31.11 ? 1166 HOH   A O    1 
HETATM 19323 O  O    . HOH   M 7 .   ? 16.201 45.940  43.689 1.00 28.21 ? 1167 HOH   A O    1 
HETATM 19324 O  O    . HOH   M 7 .   ? 28.242 44.097  44.547 1.00 26.84 ? 1168 HOH   A O    1 
HETATM 19325 O  O    . HOH   M 7 .   ? 8.870  8.837   35.941 1.00 27.39 ? 1169 HOH   A O    1 
HETATM 19326 O  O    . HOH   M 7 .   ? 15.736 62.064  30.201 1.00 38.90 ? 1170 HOH   A O    1 
HETATM 19327 O  O    . HOH   M 7 .   ? 11.140 4.180   23.833 1.00 17.54 ? 1171 HOH   A O    1 
HETATM 19328 O  O    . HOH   M 7 .   ? -1.291 31.279  27.889 1.00 31.53 ? 1172 HOH   A O    1 
HETATM 19329 O  O    . HOH   M 7 .   ? -3.463 23.997  17.200 1.00 29.12 ? 1173 HOH   A O    1 
HETATM 19330 O  O    . HOH   M 7 .   ? 16.622 39.667  8.541  1.00 13.45 ? 1174 HOH   A O    1 
HETATM 19331 O  O    . HOH   M 7 .   ? 24.682 2.240   3.371  1.00 28.06 ? 1175 HOH   A O    1 
HETATM 19332 O  O    . HOH   M 7 .   ? 22.272 7.022   -1.919 1.00 25.83 ? 1176 HOH   A O    1 
HETATM 19333 O  O    . HOH   M 7 .   ? 46.486 26.230  44.490 1.00 22.06 ? 1177 HOH   A O    1 
HETATM 19334 O  O    . HOH   M 7 .   ? 22.491 60.181  23.766 1.00 31.81 ? 1178 HOH   A O    1 
HETATM 19335 O  O    . HOH   M 7 .   ? 42.656 30.479  12.155 1.00 20.86 ? 1179 HOH   A O    1 
HETATM 19336 O  O    . HOH   M 7 .   ? 40.145 37.510  5.867  1.00 23.15 ? 1180 HOH   A O    1 
HETATM 19337 O  O    A HOH   M 7 .   ? 13.181 31.807  -0.146 0.74 32.97 ? 1181 HOH   A O    1 
HETATM 19338 O  O    . HOH   M 7 .   ? 51.051 30.942  33.364 1.00 29.89 ? 1182 HOH   A O    1 
HETATM 19339 O  O    . HOH   M 7 .   ? 14.027 42.687  44.188 1.00 28.01 ? 1183 HOH   A O    1 
HETATM 19340 O  O    . HOH   M 7 .   ? 11.566 7.707   16.564 1.00 11.60 ? 1184 HOH   A O    1 
HETATM 19341 O  O    . HOH   M 7 .   ? -5.292 28.881  18.315 1.00 29.87 ? 1185 HOH   A O    1 
HETATM 19342 O  O    . HOH   M 7 .   ? 49.644 27.312  31.706 1.00 20.06 ? 1186 HOH   A O    1 
HETATM 19343 O  O    . HOH   M 7 .   ? 3.097  47.031  33.154 1.00 36.55 ? 1187 HOH   A O    1 
HETATM 19344 O  O    . HOH   M 7 .   ? -1.020 39.734  6.500  1.00 22.87 ? 1188 HOH   A O    1 
HETATM 19345 O  O    . HOH   M 7 .   ? 38.836 43.958  9.137  1.00 20.80 ? 1189 HOH   A O    1 
HETATM 19346 O  O    . HOH   M 7 .   ? 7.201  5.361   18.108 1.00 31.03 ? 1190 HOH   A O    1 
HETATM 19347 O  O    . HOH   M 7 .   ? 11.961 16.830  41.974 1.00 36.68 ? 1191 HOH   A O    1 
HETATM 19348 O  O    . HOH   M 7 .   ? 46.106 23.369  19.227 1.00 35.09 ? 1192 HOH   A O    1 
HETATM 19349 O  O    . HOH   M 7 .   ? 30.441 -0.997  3.061  1.00 22.49 ? 1193 HOH   A O    1 
HETATM 19350 O  O    . HOH   M 7 .   ? 32.979 47.984  7.992  1.00 23.24 ? 1194 HOH   A O    1 
HETATM 19351 O  O    . HOH   M 7 .   ? 49.323 29.854  35.018 1.00 25.04 ? 1195 HOH   A O    1 
HETATM 19352 O  O    . HOH   M 7 .   ? 4.593  13.001  11.665 1.00 14.85 ? 1196 HOH   A O    1 
HETATM 19353 O  O    . HOH   M 7 .   ? 31.183 50.080  42.531 1.00 35.95 ? 1197 HOH   A O    1 
HETATM 19354 O  O    . HOH   M 7 .   ? 20.073 24.202  32.654 1.00 14.05 ? 1198 HOH   A O    1 
HETATM 19355 O  O    . HOH   M 7 .   ? 12.060 58.432  6.562  1.00 27.82 ? 1199 HOH   A O    1 
HETATM 19356 O  O    . HOH   M 7 .   ? 36.437 10.604  2.197  1.00 18.78 ? 1200 HOH   A O    1 
HETATM 19357 O  O    . HOH   M 7 .   ? 22.077 58.241  31.553 1.00 37.45 ? 1201 HOH   A O    1 
HETATM 19358 O  O    . HOH   M 7 .   ? 6.926  28.423  0.063  1.00 26.92 ? 1202 HOH   A O    1 
HETATM 19359 O  O    . HOH   M 7 .   ? 25.045 2.050   10.706 1.00 17.89 ? 1203 HOH   A O    1 
HETATM 19360 O  O    . HOH   M 7 .   ? 9.199  44.962  -0.182 1.00 15.39 ? 1204 HOH   A O    1 
HETATM 19361 O  O    . HOH   M 7 .   ? 40.231 55.778  32.454 1.00 21.79 ? 1205 HOH   A O    1 
HETATM 19362 O  O    . HOH   M 7 .   ? 17.064 1.790   13.534 1.00 22.97 ? 1206 HOH   A O    1 
HETATM 19363 O  O    . HOH   M 7 .   ? 3.981  46.663  27.889 1.00 28.15 ? 1207 HOH   A O    1 
HETATM 19364 O  O    . HOH   M 7 .   ? 19.987 61.192  5.419  1.00 31.81 ? 1208 HOH   A O    1 
HETATM 19365 O  O    . HOH   M 7 .   ? 20.126 30.113  -0.788 1.00 31.14 ? 1209 HOH   A O    1 
HETATM 19366 O  O    . HOH   M 7 .   ? 21.732 26.450  4.805  1.00 14.92 ? 1210 HOH   A O    1 
HETATM 19367 O  O    . HOH   M 7 .   ? 25.463 33.482  16.873 1.00 8.06  ? 1211 HOH   A O    1 
HETATM 19368 O  O    . HOH   M 7 .   ? 20.563 39.680  27.246 1.00 12.15 ? 1212 HOH   A O    1 
HETATM 19369 O  O    . HOH   M 7 .   ? 14.599 36.736  -0.683 1.00 18.13 ? 1213 HOH   A O    1 
HETATM 19370 O  O    . HOH   M 7 .   ? 48.659 32.870  40.795 1.00 33.90 ? 1214 HOH   A O    1 
HETATM 19371 O  O    . HOH   M 7 .   ? 23.725 16.182  -6.059 1.00 32.08 ? 1215 HOH   A O    1 
HETATM 19372 O  O    . HOH   M 7 .   ? 32.870 20.993  40.780 1.00 21.80 ? 1216 HOH   A O    1 
HETATM 19373 O  O    . HOH   M 7 .   ? 41.441 47.400  14.291 1.00 37.90 ? 1217 HOH   A O    1 
HETATM 19374 O  O    . HOH   M 7 .   ? 27.014 8.490   33.978 1.00 23.45 ? 1218 HOH   A O    1 
HETATM 19375 O  O    . HOH   M 7 .   ? 7.177  46.661  14.091 1.00 27.72 ? 1219 HOH   A O    1 
HETATM 19376 O  O    . HOH   M 7 .   ? -4.592 33.713  7.164  1.00 22.63 ? 1220 HOH   A O    1 
HETATM 19377 O  O    . HOH   M 7 .   ? 36.364 7.560   20.418 1.00 30.16 ? 1221 HOH   A O    1 
HETATM 19378 O  O    . HOH   M 7 .   ? 0.360  14.221  4.912  1.00 23.84 ? 1222 HOH   A O    1 
HETATM 19379 O  O    . HOH   M 7 .   ? 18.776 28.443  18.106 1.00 10.86 ? 1223 HOH   A O    1 
HETATM 19380 O  O    . HOH   M 7 .   ? 20.523 38.935  7.209  1.00 22.25 ? 1224 HOH   A O    1 
HETATM 19381 O  O    . HOH   M 7 .   ? 34.558 28.894  8.573  1.00 25.62 ? 1225 HOH   A O    1 
HETATM 19382 O  O    . HOH   M 7 .   ? 12.983 58.293  23.926 1.00 33.98 ? 1226 HOH   A O    1 
HETATM 19383 O  O    . HOH   M 7 .   ? 23.242 20.270  44.962 1.00 24.52 ? 1227 HOH   A O    1 
HETATM 19384 O  O    . HOH   M 7 .   ? 37.869 45.394  0.908  1.00 35.22 ? 1228 HOH   A O    1 
HETATM 19385 O  O    . HOH   M 7 .   ? 25.807 48.013  27.681 1.00 12.58 ? 1229 HOH   A O    1 
HETATM 19386 O  O    . HOH   M 7 .   ? 1.941  25.968  35.196 1.00 31.12 ? 1230 HOH   A O    1 
HETATM 19387 O  O    . HOH   M 7 .   ? 5.651  36.796  24.295 1.00 18.73 ? 1231 HOH   A O    1 
HETATM 19388 O  O    . HOH   M 7 .   ? 25.724 24.798  40.684 1.00 22.93 ? 1232 HOH   A O    1 
HETATM 19389 O  O    . HOH   M 7 .   ? -5.634 26.359  14.911 1.00 32.93 ? 1233 HOH   A O    1 
HETATM 19390 O  O    . HOH   M 7 .   ? 52.404 33.627  32.374 1.00 29.89 ? 1234 HOH   A O    1 
HETATM 19391 O  O    . HOH   M 7 .   ? 27.507 32.081  2.381  1.00 29.74 ? 1235 HOH   A O    1 
HETATM 19392 O  O    . HOH   M 7 .   ? 42.430 51.822  36.473 1.00 36.97 ? 1236 HOH   A O    1 
HETATM 19393 O  O    . HOH   M 7 .   ? 33.352 25.514  4.428  1.00 32.41 ? 1237 HOH   A O    1 
HETATM 19394 O  O    . HOH   M 7 .   ? 35.032 47.435  40.556 1.00 22.35 ? 1238 HOH   A O    1 
HETATM 19395 O  O    . HOH   M 7 .   ? -0.519 22.816  23.597 1.00 34.86 ? 1239 HOH   A O    1 
HETATM 19396 O  O    . HOH   M 7 .   ? 26.698 19.618  32.128 1.00 12.02 ? 1240 HOH   A O    1 
HETATM 19397 O  O    . HOH   M 7 .   ? 8.655  40.523  44.597 1.00 26.07 ? 1241 HOH   A O    1 
HETATM 19398 O  O    . HOH   M 7 .   ? 8.751  10.252  6.949  1.00 33.23 ? 1242 HOH   A O    1 
HETATM 19399 O  O    . HOH   M 7 .   ? 32.398 15.982  33.968 1.00 38.70 ? 1243 HOH   A O    1 
HETATM 19400 O  O    . HOH   M 7 .   ? 22.570 1.752   22.168 1.00 20.59 ? 1244 HOH   A O    1 
HETATM 19401 O  O    . HOH   M 7 .   ? 31.939 43.258  46.873 1.00 27.04 ? 1245 HOH   A O    1 
HETATM 19402 O  O    . HOH   M 7 .   ? 34.334 60.327  27.935 1.00 28.94 ? 1246 HOH   A O    1 
HETATM 19403 O  O    . HOH   M 7 .   ? 2.863  16.323  30.696 1.00 27.93 ? 1247 HOH   A O    1 
HETATM 19404 O  O    . HOH   M 7 .   ? 9.480  55.365  32.546 1.00 30.21 ? 1248 HOH   A O    1 
HETATM 19405 O  O    . HOH   M 7 .   ? 42.375 34.504  46.739 1.00 19.39 ? 1249 HOH   A O    1 
HETATM 19406 O  O    . HOH   M 7 .   ? -1.238 36.586  4.313  1.00 32.63 ? 1250 HOH   A O    1 
HETATM 19407 O  O    . HOH   M 7 .   ? 21.461 52.633  -2.494 1.00 40.95 ? 1251 HOH   A O    1 
HETATM 19408 O  O    . HOH   M 7 .   ? 29.961 6.730   0.017  1.00 28.19 ? 1252 HOH   A O    1 
HETATM 19409 O  O    . HOH   M 7 .   ? 43.260 18.849  35.143 1.00 33.95 ? 1253 HOH   A O    1 
HETATM 19410 O  O    . HOH   M 7 .   ? -5.606 34.893  23.393 1.00 25.56 ? 1254 HOH   A O    1 
HETATM 19411 O  O    . HOH   M 7 .   ? 26.425 -0.047  3.573  1.00 24.24 ? 1255 HOH   A O    1 
HETATM 19412 O  O    . HOH   M 7 .   ? 13.714 3.691   14.554 1.00 30.34 ? 1256 HOH   A O    1 
HETATM 19413 O  O    . HOH   M 7 .   ? -4.150 38.324  25.631 1.00 37.24 ? 1257 HOH   A O    1 
HETATM 19414 O  O    . HOH   M 7 .   ? 30.219 59.263  25.902 1.00 24.86 ? 1258 HOH   A O    1 
HETATM 19415 O  O    . HOH   M 7 .   ? 11.267 46.749  -4.141 1.00 20.29 ? 1259 HOH   A O    1 
HETATM 19416 O  O    . HOH   M 7 .   ? 44.759 38.779  39.832 1.00 31.63 ? 1260 HOH   A O    1 
HETATM 19417 O  O    . HOH   M 7 .   ? 42.800 16.734  28.453 1.00 29.79 ? 1261 HOH   A O    1 
HETATM 19418 O  O    A HOH   M 7 .   ? 5.467  44.272  24.279 1.00 26.82 ? 1262 HOH   A O    1 
HETATM 19419 O  O    . HOH   M 7 .   ? 5.958  50.656  21.425 1.00 32.28 ? 1263 HOH   A O    1 
HETATM 19420 O  O    . HOH   M 7 .   ? 25.757 21.297  44.101 1.00 29.00 ? 1264 HOH   A O    1 
HETATM 19421 O  O    . HOH   M 7 .   ? 37.564 59.820  31.832 1.00 26.78 ? 1265 HOH   A O    1 
HETATM 19422 O  O    . HOH   M 7 .   ? 19.385 9.757   44.297 1.00 37.97 ? 1266 HOH   A O    1 
HETATM 19423 O  O    . HOH   M 7 .   ? 8.505  14.761  6.138  1.00 17.26 ? 1267 HOH   A O    1 
HETATM 19424 O  O    . HOH   M 7 .   ? 18.069 62.846  1.063  1.00 34.53 ? 1268 HOH   A O    1 
HETATM 19425 O  O    . HOH   M 7 .   ? 34.765 22.933  37.418 1.00 17.85 ? 1269 HOH   A O    1 
HETATM 19426 O  O    . HOH   M 7 .   ? -2.068 25.506  18.942 1.00 25.72 ? 1270 HOH   A O    1 
HETATM 19427 O  O    . HOH   M 7 .   ? 9.950  28.463  42.746 1.00 32.35 ? 1271 HOH   A O    1 
HETATM 19428 O  O    . HOH   M 7 .   ? 3.968  34.726  -3.430 1.00 31.66 ? 1272 HOH   A O    1 
HETATM 19429 O  O    . HOH   M 7 .   ? 31.946 52.305  23.171 1.00 16.83 ? 1273 HOH   A O    1 
HETATM 19430 O  O    . HOH   M 7 .   ? 30.415 25.770  3.182  1.00 22.70 ? 1274 HOH   A O    1 
HETATM 19431 O  O    . HOH   M 7 .   ? 24.145 52.939  43.143 1.00 36.52 ? 1275 HOH   A O    1 
HETATM 19432 O  O    . HOH   M 7 .   ? -1.401 26.707  4.246  1.00 25.89 ? 1276 HOH   A O    1 
HETATM 19433 O  O    . HOH   M 7 .   ? -0.313 36.347  28.061 1.00 33.14 ? 1277 HOH   A O    1 
HETATM 19434 O  O    . HOH   M 7 .   ? 1.616  40.622  8.364  1.00 17.53 ? 1278 HOH   A O    1 
HETATM 19435 O  O    B HOH   M 7 .   ? 18.567 55.239  -2.209 0.61 28.93 ? 1279 HOH   A O    1 
HETATM 19436 O  O    . HOH   M 7 .   ? 47.605 21.025  39.174 1.00 35.89 ? 1280 HOH   A O    1 
HETATM 19437 O  O    . HOH   M 7 .   ? 5.220  49.112  43.251 1.00 28.28 ? 1281 HOH   A O    1 
HETATM 19438 O  O    . HOH   M 7 .   ? 10.632 8.642   9.099  1.00 29.94 ? 1282 HOH   A O    1 
HETATM 19439 O  O    . HOH   M 7 .   ? 22.402 7.971   39.640 1.00 28.82 ? 1283 HOH   A O    1 
HETATM 19440 O  O    . HOH   M 7 .   ? 16.891 21.470  0.947  1.00 16.30 ? 1284 HOH   A O    1 
HETATM 19441 O  O    . HOH   M 7 .   ? 5.406  7.604   17.220 1.00 20.57 ? 1285 HOH   A O    1 
HETATM 19442 O  O    . HOH   M 7 .   ? 51.293 52.011  24.577 1.00 22.69 ? 1286 HOH   A O    1 
HETATM 19443 O  O    . HOH   M 7 .   ? 34.701 50.633  20.475 1.00 22.70 ? 1287 HOH   A O    1 
HETATM 19444 O  O    A HOH   M 7 .   ? 4.935  2.798   19.317 0.87 30.28 ? 1288 HOH   A O    1 
HETATM 19445 O  O    . HOH   M 7 .   ? 49.730 28.373  18.091 1.00 33.32 ? 1289 HOH   A O    1 
HETATM 19446 O  O    . HOH   M 7 .   ? 38.709 -0.489  0.552  1.00 35.79 ? 1290 HOH   A O    1 
HETATM 19447 O  O    . HOH   M 7 .   ? 28.910 41.564  44.956 1.00 24.05 ? 1291 HOH   A O    1 
HETATM 19448 O  O    A HOH   M 7 .   ? 45.593 18.892  28.337 0.95 33.51 ? 1292 HOH   A O    1 
HETATM 19449 O  O    . HOH   M 7 .   ? 32.739 24.141  42.536 0.77 21.84 ? 1293 HOH   A O    1 
HETATM 19450 O  O    . HOH   M 7 .   ? 3.624  8.361   29.630 1.00 32.80 ? 1294 HOH   A O    1 
HETATM 19451 O  O    . HOH   M 7 .   ? -3.546 27.229  16.341 1.00 21.79 ? 1295 HOH   A O    1 
HETATM 19452 O  O    . HOH   M 7 .   ? 23.611 24.318  -1.104 1.00 32.58 ? 1296 HOH   A O    1 
HETATM 19453 O  O    . HOH   M 7 .   ? 16.990 6.911   31.278 1.00 21.27 ? 1297 HOH   A O    1 
HETATM 19454 O  O    . HOH   M 7 .   ? 7.686  27.509  41.911 1.00 29.70 ? 1298 HOH   A O    1 
HETATM 19455 O  O    . HOH   M 7 .   ? 9.938  52.836  6.565  1.00 30.45 ? 1299 HOH   A O    1 
HETATM 19456 O  O    . HOH   M 7 .   ? 19.901 53.960  0.739  1.00 23.92 ? 1300 HOH   A O    1 
HETATM 19457 O  O    . HOH   M 7 .   ? 36.010 58.300  34.142 1.00 35.90 ? 1301 HOH   A O    1 
HETATM 19458 O  O    . HOH   M 7 .   ? 6.970  10.884  34.274 1.00 33.55 ? 1302 HOH   A O    1 
HETATM 19459 O  O    . HOH   M 7 .   ? 11.297 21.017  40.641 1.00 24.03 ? 1303 HOH   A O    1 
HETATM 19460 O  O    . HOH   M 7 .   ? 20.244 40.844  42.747 1.00 27.96 ? 1304 HOH   A O    1 
HETATM 19461 O  O    . HOH   M 7 .   ? 14.340 8.345   32.929 1.00 20.00 ? 1305 HOH   A O    1 
HETATM 19462 O  O    . HOH   M 7 .   ? 40.197 36.580  47.784 1.00 33.01 ? 1306 HOH   A O    1 
HETATM 19463 O  O    . HOH   M 7 .   ? 44.871 47.716  32.169 1.00 33.63 ? 1307 HOH   A O    1 
HETATM 19464 O  O    . HOH   M 7 .   ? 37.149 50.053  34.504 1.00 23.95 ? 1308 HOH   A O    1 
HETATM 19465 O  O    . HOH   M 7 .   ? 48.244 18.306  33.151 1.00 37.85 ? 1309 HOH   A O    1 
HETATM 19466 O  O    . HOH   M 7 .   ? 34.676 2.747   3.244  1.00 35.18 ? 1310 HOH   A O    1 
HETATM 19467 O  O    . HOH   M 7 .   ? 39.116 54.327  34.471 1.00 32.50 ? 1311 HOH   A O    1 
HETATM 19468 O  O    . HOH   M 7 .   ? 1.729  10.298  5.054  1.00 31.65 ? 1312 HOH   A O    1 
HETATM 19469 O  O    . HOH   M 7 .   ? 16.396 8.999   38.635 1.00 34.15 ? 1313 HOH   A O    1 
HETATM 19470 O  O    . HOH   M 7 .   ? 16.443 59.380  37.352 1.00 38.45 ? 1314 HOH   A O    1 
HETATM 19471 O  O    . HOH   M 7 .   ? 33.459 8.758   1.153  1.00 24.01 ? 1315 HOH   A O    1 
HETATM 19472 O  O    . HOH   M 7 .   ? 4.219  10.858  23.914 1.00 30.95 ? 1316 HOH   A O    1 
HETATM 19473 O  O    . HOH   M 7 .   ? 39.872 11.213  10.138 1.00 32.14 ? 1317 HOH   A O    1 
HETATM 19474 O  O    . HOH   M 7 .   ? 10.827 57.349  33.746 1.00 30.72 ? 1318 HOH   A O    1 
HETATM 19475 O  O    . HOH   M 7 .   ? 7.330  55.430  30.272 1.00 25.20 ? 1319 HOH   A O    1 
HETATM 19476 O  O    . HOH   M 7 .   ? 11.346 59.083  26.413 1.00 34.16 ? 1320 HOH   A O    1 
HETATM 19477 O  O    . HOH   M 7 .   ? 23.724 28.879  2.677  1.00 29.01 ? 1321 HOH   A O    1 
HETATM 19478 O  O    . HOH   M 7 .   ? 39.785 41.796  45.310 1.00 31.48 ? 1322 HOH   A O    1 
HETATM 19479 O  O    . HOH   M 7 .   ? 53.453 47.305  16.838 1.00 34.58 ? 1323 HOH   A O    1 
HETATM 19480 O  O    . HOH   M 7 .   ? 30.567 37.838  42.777 1.00 32.06 ? 1324 HOH   A O    1 
HETATM 19481 O  O    . HOH   M 7 .   ? 4.179  41.543  -0.091 1.00 31.91 ? 1325 HOH   A O    1 
HETATM 19482 O  O    . HOH   M 7 .   ? 56.977 33.967  21.747 1.00 36.94 ? 1326 HOH   A O    1 
HETATM 19483 O  O    . HOH   M 7 .   ? 14.395 3.953   25.185 1.00 22.45 ? 1327 HOH   A O    1 
HETATM 19484 O  O    . HOH   M 7 .   ? 38.250 22.622  10.160 1.00 37.90 ? 1328 HOH   A O    1 
HETATM 19485 O  O    . HOH   M 7 .   ? 34.196 21.308  6.492  1.00 24.13 ? 1329 HOH   A O    1 
HETATM 19486 O  O    . HOH   M 7 .   ? 15.520 25.289  25.697 1.00 13.61 ? 1330 HOH   A O    1 
HETATM 19487 O  O    . HOH   M 7 .   ? 5.706  16.305  -1.838 1.00 28.95 ? 1331 HOH   A O    1 
HETATM 19488 O  O    . HOH   M 7 .   ? 41.849 54.847  22.989 1.00 26.24 ? 1332 HOH   A O    1 
HETATM 19489 O  O    . HOH   M 7 .   ? 37.032 48.915  39.043 1.00 22.86 ? 1333 HOH   A O    1 
HETATM 19490 O  O    . HOH   M 7 .   ? 4.560  15.645  36.722 1.00 33.20 ? 1334 HOH   A O    1 
HETATM 19491 O  O    . HOH   M 7 .   ? 38.660 29.331  45.135 1.00 13.88 ? 1335 HOH   A O    1 
HETATM 19492 O  O    . HOH   M 7 .   ? 47.119 47.267  19.349 1.00 29.20 ? 1336 HOH   A O    1 
HETATM 19493 O  O    . HOH   M 7 .   ? 7.796  49.479  11.439 1.00 32.79 ? 1337 HOH   A O    1 
HETATM 19494 O  O    . HOH   M 7 .   ? 14.106 18.658  42.962 1.00 33.11 ? 1338 HOH   A O    1 
HETATM 19495 O  O    . HOH   M 7 .   ? 30.026 27.332  38.339 1.00 23.61 ? 1339 HOH   A O    1 
HETATM 19496 O  O    . HOH   M 7 .   ? 19.408 3.328   0.474  1.00 29.35 ? 1340 HOH   A O    1 
HETATM 19497 O  O    . HOH   M 7 .   ? -6.367 31.774  18.184 1.00 34.79 ? 1341 HOH   A O    1 
HETATM 19498 O  O    . HOH   M 7 .   ? -3.708 34.555  13.805 1.00 16.97 ? 1342 HOH   A O    1 
HETATM 19499 O  O    . HOH   M 7 .   ? -2.963 20.035  18.567 1.00 35.16 ? 1343 HOH   A O    1 
HETATM 19500 O  O    . HOH   M 7 .   ? 19.621 0.437   19.277 1.00 34.11 ? 1344 HOH   A O    1 
HETATM 19501 O  O    . HOH   M 7 .   ? 32.997 48.856  39.484 1.00 23.99 ? 1345 HOH   A O    1 
HETATM 19502 O  O    . HOH   M 7 .   ? 40.068 0.439   13.526 1.00 40.38 ? 1346 HOH   A O    1 
HETATM 19503 O  O    . HOH   M 7 .   ? 12.559 7.042   8.481  1.00 32.13 ? 1347 HOH   A O    1 
HETATM 19504 O  O    . HOH   M 7 .   ? 32.185 32.403  43.732 1.00 27.66 ? 1348 HOH   A O    1 
HETATM 19505 O  O    . HOH   M 7 .   ? 51.727 39.838  29.073 1.00 35.35 ? 1349 HOH   A O    1 
HETATM 19506 O  O    . HOH   M 7 .   ? 0.640  30.402  38.594 1.00 32.50 ? 1350 HOH   A O    1 
HETATM 19507 O  O    . HOH   M 7 .   ? 2.895  38.597  28.999 1.00 28.70 ? 1351 HOH   A O    1 
HETATM 19508 O  O    . HOH   M 7 .   ? 3.728  25.859  -3.061 1.00 37.70 ? 1352 HOH   A O    1 
HETATM 19509 O  O    . HOH   M 7 .   ? 32.674 18.882  6.670  1.00 21.60 ? 1353 HOH   A O    1 
HETATM 19510 O  O    . HOH   M 7 .   ? 12.087 29.645  -0.707 1.00 29.52 ? 1354 HOH   A O    1 
HETATM 19511 O  O    . HOH   M 7 .   ? -2.839 40.058  16.383 1.00 35.87 ? 1355 HOH   A O    1 
HETATM 19512 O  O    . HOH   M 7 .   ? 5.676  50.621  18.767 1.00 32.68 ? 1356 HOH   A O    1 
HETATM 19513 O  O    . HOH   M 7 .   ? 9.496  7.450   14.971 1.00 29.55 ? 1357 HOH   A O    1 
HETATM 19514 O  O    . HOH   M 7 .   ? 32.494 16.735  5.109  1.00 27.67 ? 1358 HOH   A O    1 
HETATM 19515 O  O    . HOH   M 7 .   ? 32.002 50.832  37.174 1.00 31.94 ? 1359 HOH   A O    1 
HETATM 19516 O  O    . HOH   M 7 .   ? 31.078 50.409  8.578  1.00 25.82 ? 1360 HOH   A O    1 
HETATM 19517 O  O    . HOH   M 7 .   ? 21.431 -0.349  5.789  1.00 28.95 ? 1361 HOH   A O    1 
HETATM 19518 O  O    . HOH   M 7 .   ? 31.862 -2.821  6.714  1.00 29.38 ? 1362 HOH   A O    1 
HETATM 19519 O  O    . HOH   M 7 .   ? 38.536 4.948   12.095 1.00 34.52 ? 1363 HOH   A O    1 
HETATM 19520 O  O    . HOH   M 7 .   ? -2.824 41.476  8.141  1.00 40.26 ? 1364 HOH   A O    1 
HETATM 19521 O  O    . HOH   M 7 .   ? 30.917 22.627  -3.835 1.00 38.34 ? 1365 HOH   A O    1 
HETATM 19522 O  O    . HOH   M 7 .   ? 37.911 20.676  11.457 1.00 28.57 ? 1366 HOH   A O    1 
HETATM 19523 O  O    . HOH   M 7 .   ? 44.199 45.099  15.489 1.00 29.26 ? 1367 HOH   A O    1 
HETATM 19524 O  O    . HOH   M 7 .   ? 24.753 58.412  -0.584 1.00 38.34 ? 1368 HOH   A O    1 
HETATM 19525 O  O    . HOH   M 7 .   ? 10.835 24.373  42.201 1.00 31.25 ? 1369 HOH   A O    1 
HETATM 19526 O  O    . HOH   M 7 .   ? 13.946 17.572  0.165  1.00 22.01 ? 1370 HOH   A O    1 
HETATM 19527 O  O    . HOH   M 7 .   ? 13.725 4.179   4.987  1.00 29.78 ? 1371 HOH   A O    1 
HETATM 19528 O  O    . HOH   M 7 .   ? 23.918 44.784  -0.610 1.00 30.03 ? 1372 HOH   A O    1 
HETATM 19529 O  O    . HOH   M 7 .   ? 42.419 52.129  40.635 1.00 33.37 ? 1373 HOH   A O    1 
HETATM 19530 O  O    . HOH   M 7 .   ? 45.499 32.824  12.260 1.00 20.74 ? 1374 HOH   A O    1 
HETATM 19531 O  O    . HOH   M 7 .   ? 46.021 34.108  42.906 1.00 31.52 ? 1375 HOH   A O    1 
HETATM 19532 O  O    . HOH   M 7 .   ? 29.511 52.424  37.674 1.00 31.06 ? 1376 HOH   A O    1 
HETATM 19533 O  O    . HOH   M 7 .   ? 20.256 48.285  45.747 1.00 30.65 ? 1377 HOH   A O    1 
HETATM 19534 O  O    . HOH   M 7 .   ? 32.297 10.920  0.000  0.50 25.40 ? 1378 HOH   A O    1 
HETATM 19535 O  O    . HOH   M 7 .   ? 39.685 50.142  16.310 1.00 29.65 ? 1379 HOH   A O    1 
HETATM 19536 O  O    . HOH   M 7 .   ? 6.623  55.694  17.314 1.00 28.95 ? 1380 HOH   A O    1 
HETATM 19537 O  O    . HOH   M 7 .   ? 10.349 31.920  -0.320 1.00 33.86 ? 1381 HOH   A O    1 
HETATM 19538 O  O    . HOH   M 7 .   ? 39.022 46.850  8.647  1.00 31.33 ? 1382 HOH   A O    1 
HETATM 19539 O  O    . HOH   M 7 .   ? -1.209 33.961  29.005 1.00 36.56 ? 1383 HOH   A O    1 
HETATM 19540 O  O    . HOH   M 7 .   ? 16.152 37.443  -2.738 1.00 25.72 ? 1384 HOH   A O    1 
HETATM 19541 O  O    . HOH   M 7 .   ? 9.422  29.635  -1.332 1.00 35.64 ? 1385 HOH   A O    1 
HETATM 19542 O  O    . HOH   M 7 .   ? 22.591 35.558  -5.425 1.00 30.74 ? 1386 HOH   A O    1 
HETATM 19543 O  O    . HOH   M 7 .   ? 20.200 1.535   2.342  1.00 24.59 ? 1387 HOH   A O    1 
HETATM 19544 O  O    . HOH   M 7 .   ? 25.642 57.080  18.176 1.00 29.66 ? 1388 HOH   A O    1 
HETATM 19545 O  O    . HOH   M 7 .   ? 1.010  38.808  2.140  1.00 34.27 ? 1389 HOH   A O    1 
HETATM 19546 O  O    . HOH   M 7 .   ? -5.350 37.781  11.872 1.00 28.95 ? 1390 HOH   A O    1 
HETATM 19547 O  O    . HOH   M 7 .   ? 1.695  42.516  14.984 1.00 27.09 ? 1391 HOH   A O    1 
HETATM 19548 O  O    . HOH   M 7 .   ? 49.139 19.771  30.019 1.00 40.05 ? 1392 HOH   A O    1 
HETATM 19549 O  O    . HOH   M 7 .   ? 25.759 60.191  7.931  1.00 31.00 ? 1393 HOH   A O    1 
HETATM 19550 O  O    . HOH   M 7 .   ? 3.551  23.562  35.325 1.00 25.68 ? 1394 HOH   A O    1 
HETATM 19551 O  O    . HOH   M 7 .   ? 25.082 7.232   -2.835 1.00 30.68 ? 1395 HOH   A O    1 
HETATM 19552 O  O    . HOH   M 7 .   ? 36.457 15.405  6.305  1.00 33.77 ? 1396 HOH   A O    1 
HETATM 19553 O  O    . HOH   M 7 .   ? 15.722 3.702   8.569  1.00 18.51 ? 1397 HOH   A O    1 
HETATM 19554 O  O    . HOH   M 7 .   ? 4.594  8.900   9.641  1.00 30.95 ? 1398 HOH   A O    1 
HETATM 19555 O  O    . HOH   M 7 .   ? 32.297 19.818  0.000  0.50 25.67 ? 1399 HOH   A O    1 
HETATM 19556 O  O    . HOH   M 7 .   ? 28.187 -0.834  13.764 1.00 34.23 ? 1400 HOH   A O    1 
HETATM 19557 O  O    . HOH   M 7 .   ? 50.499 33.456  15.876 1.00 32.63 ? 1401 HOH   A O    1 
HETATM 19558 O  O    . HOH   M 7 .   ? 19.407 57.392  21.895 1.00 36.79 ? 1402 HOH   A O    1 
HETATM 19559 O  O    . HOH   M 7 .   ? 24.581 7.406   30.582 1.00 28.73 ? 1403 HOH   A O    1 
HETATM 19560 O  O    . HOH   M 7 .   ? 29.497 16.363  -4.419 1.00 34.21 ? 1404 HOH   A O    1 
HETATM 19561 O  O    . HOH   M 7 .   ? 9.119  50.015  15.844 1.00 26.45 ? 1405 HOH   A O    1 
HETATM 19562 O  O    . HOH   M 7 .   ? 34.284 34.045  4.796  1.00 30.37 ? 1406 HOH   A O    1 
HETATM 19563 O  O    . HOH   M 7 .   ? -3.909 15.775  5.491  1.00 29.69 ? 1407 HOH   A O    1 
HETATM 19564 O  O    . HOH   M 7 .   ? 43.782 33.059  9.233  1.00 29.26 ? 1408 HOH   A O    1 
HETATM 19565 O  O    . HOH   M 7 .   ? 35.544 -4.276  13.857 1.00 31.99 ? 1409 HOH   A O    1 
HETATM 19566 O  O    . HOH   M 7 .   ? 11.752 5.504   6.110  1.00 32.08 ? 1410 HOH   A O    1 
HETATM 19567 O  O    . HOH   M 7 .   ? 49.670 37.821  40.590 1.00 39.55 ? 1411 HOH   A O    1 
HETATM 19568 O  O    . HOH   M 7 .   ? 53.405 35.101  29.594 1.00 29.89 ? 1412 HOH   A O    1 
HETATM 19569 O  O    . HOH   M 7 .   ? 22.272 4.555   -2.660 1.00 37.23 ? 1413 HOH   A O    1 
HETATM 19570 O  O    . HOH   M 7 .   ? 23.401 42.272  -1.567 1.00 29.72 ? 1414 HOH   A O    1 
HETATM 19571 O  O    . HOH   M 7 .   ? -3.624 19.945  21.085 1.00 28.95 ? 1415 HOH   A O    1 
HETATM 19572 O  O    . HOH   M 7 .   ? 30.779 17.976  34.565 1.00 24.15 ? 1416 HOH   A O    1 
HETATM 19573 O  O    . HOH   M 7 .   ? -3.948 39.724  12.101 1.00 35.93 ? 1417 HOH   A O    1 
HETATM 19574 O  O    . HOH   M 7 .   ? 18.320 2.020   11.110 1.00 30.82 ? 1418 HOH   A O    1 
HETATM 19575 O  O    . HOH   M 7 .   ? 16.631 58.411  15.264 1.00 33.13 ? 1419 HOH   A O    1 
HETATM 19576 O  O    . HOH   M 7 .   ? -5.284 21.000  9.636  1.00 28.95 ? 1420 HOH   A O    1 
HETATM 19577 O  O    . HOH   M 7 .   ? 1.634  37.768  4.322  1.00 34.66 ? 1421 HOH   A O    1 
HETATM 19578 O  O    . HOH   M 7 .   ? 44.720 28.027  15.574 1.00 27.95 ? 1422 HOH   A O    1 
HETATM 19579 O  O    . HOH   M 7 .   ? 18.615 21.374  -1.328 1.00 26.20 ? 1423 HOH   A O    1 
HETATM 19580 O  O    . HOH   M 7 .   ? 20.065 59.892  13.697 1.00 38.55 ? 1424 HOH   A O    1 
HETATM 19581 O  O    . HOH   M 7 .   ? 46.029 40.115  6.633  1.00 33.32 ? 1425 HOH   A O    1 
HETATM 19582 O  O    . HOH   M 7 .   ? -3.391 30.148  25.100 1.00 36.10 ? 1426 HOH   A O    1 
HETATM 19583 O  O    . HOH   M 7 .   ? 46.678 20.118  23.315 1.00 35.59 ? 1427 HOH   A O    1 
HETATM 19584 O  O    A HOH   M 7 .   ? 44.563 16.251  30.804 0.63 28.95 ? 1428 HOH   A O    1 
HETATM 19585 O  O    . HOH   M 7 .   ? 17.711 61.382  28.583 1.00 36.28 ? 1429 HOH   A O    1 
HETATM 19586 O  O    . HOH   M 7 .   ? 39.469 17.129  9.508  1.00 30.61 ? 1430 HOH   A O    1 
HETATM 19587 O  O    . HOH   M 7 .   ? 14.879 6.490   34.657 1.00 31.33 ? 1431 HOH   A O    1 
HETATM 19588 O  O    . HOH   M 7 .   ? 7.714  15.004  40.146 1.00 23.07 ? 1432 HOH   A O    1 
HETATM 19589 O  O    . HOH   M 7 .   ? 2.005  19.309  28.323 1.00 23.68 ? 1433 HOH   A O    1 
HETATM 19590 O  O    . HOH   M 7 .   ? 34.660 47.806  5.936  1.00 37.21 ? 1434 HOH   A O    1 
HETATM 19591 O  O    . HOH   M 7 .   ? 4.896  45.312  44.307 1.00 36.69 ? 1435 HOH   A O    1 
HETATM 19592 O  O    . HOH   M 7 .   ? 2.856  44.843  14.787 1.00 32.56 ? 1436 HOH   A O    1 
HETATM 19593 O  O    . HOH   M 7 .   ? 4.764  32.646  -4.872 1.00 35.24 ? 1437 HOH   A O    1 
HETATM 19594 O  O    . HOH   M 7 .   ? 30.370 8.192   27.528 1.00 38.31 ? 1438 HOH   A O    1 
HETATM 19595 O  O    . HOH   M 7 .   ? 46.163 17.726  25.881 1.00 37.08 ? 1439 HOH   A O    1 
HETATM 19596 O  O    . HOH   M 7 .   ? 2.322  41.429  28.766 1.00 36.93 ? 1440 HOH   A O    1 
HETATM 19597 O  O    . HOH   M 7 .   ? 16.141 3.686   26.997 1.00 32.23 ? 1441 HOH   A O    1 
HETATM 19598 O  O    . HOH   M 7 .   ? -1.986 39.295  14.009 1.00 25.59 ? 1442 HOH   A O    1 
HETATM 19599 O  O    . HOH   M 7 .   ? 18.565 3.466   9.095  1.00 19.42 ? 1443 HOH   A O    1 
HETATM 19600 O  O    . HOH   M 7 .   ? -0.011 21.175  0.033  0.50 39.45 ? 1444 HOH   A O    1 
HETATM 19601 O  O    . HOH   M 7 .   ? 34.460 39.909  46.871 1.00 31.67 ? 1445 HOH   A O    1 
HETATM 19602 O  O    . HOH   M 7 .   ? 40.309 58.667  33.005 1.00 20.87 ? 1446 HOH   A O    1 
HETATM 19603 O  O    . HOH   M 7 .   ? 9.686  7.076   33.969 1.00 30.55 ? 1447 HOH   A O    1 
HETATM 19604 O  O    . HOH   M 7 .   ? 27.718 53.426  42.806 1.00 38.68 ? 1448 HOH   A O    1 
HETATM 19605 O  O    . HOH   M 7 .   ? 41.769 50.958  34.052 1.00 25.31 ? 1449 HOH   A O    1 
HETATM 19606 O  O    . HOH   M 7 .   ? 49.602 24.929  21.160 1.00 36.90 ? 1450 HOH   A O    1 
HETATM 19607 O  O    . HOH   M 7 .   ? 32.664 3.754   1.733  1.00 30.82 ? 1451 HOH   A O    1 
HETATM 19608 O  O    . HOH   M 7 .   ? 35.625 13.354  29.161 1.00 36.82 ? 1452 HOH   A O    1 
HETATM 19609 O  O    . HOH   M 7 .   ? 2.945  45.242  25.618 1.00 35.96 ? 1453 HOH   A O    1 
HETATM 19610 O  O    . HOH   M 7 .   ? 47.873 25.213  35.413 1.00 24.05 ? 1454 HOH   A O    1 
HETATM 19611 O  O    . HOH   M 7 .   ? 38.375 41.533  47.574 1.00 31.49 ? 1455 HOH   A O    1 
HETATM 19612 O  O    . HOH   M 7 .   ? 5.716  24.463  -3.295 1.00 28.96 ? 1456 HOH   A O    1 
HETATM 19613 O  O    . HOH   M 7 .   ? 42.971 43.355  13.872 1.00 23.37 ? 1457 HOH   A O    1 
HETATM 19614 O  O    . HOH   M 7 .   ? 6.210  42.515  -2.053 1.00 23.05 ? 1458 HOH   A O    1 
HETATM 19615 O  O    . HOH   M 7 .   ? 28.514 -4.664  8.914  1.00 38.48 ? 1459 HOH   A O    1 
HETATM 19616 O  O    . HOH   M 7 .   ? 24.768 29.358  37.005 1.00 16.17 ? 1460 HOH   A O    1 
HETATM 19617 O  O    . HOH   M 7 .   ? 41.093 19.159  39.892 1.00 31.99 ? 1461 HOH   A O    1 
HETATM 19618 O  O    . HOH   M 7 .   ? 45.187 21.034  19.472 1.00 31.54 ? 1462 HOH   A O    1 
HETATM 19619 O  O    . HOH   M 7 .   ? 19.890 5.076   37.096 1.00 35.36 ? 1463 HOH   A O    1 
HETATM 19620 O  O    . HOH   M 7 .   ? 18.506 24.754  2.316  1.00 26.72 ? 1464 HOH   A O    1 
HETATM 19621 O  O    . HOH   M 7 .   ? 36.697 33.217  4.159  1.00 35.52 ? 1465 HOH   A O    1 
HETATM 19622 O  O    . HOH   M 7 .   ? -6.348 34.419  9.708  1.00 30.99 ? 1466 HOH   A O    1 
HETATM 19623 O  O    . HOH   M 7 .   ? 10.093 34.685  -1.295 1.00 24.81 ? 1467 HOH   A O    1 
HETATM 19624 O  O    . HOH   M 7 .   ? 30.466 -2.941  9.365  1.00 27.99 ? 1468 HOH   A O    1 
HETATM 19625 O  O    . HOH   M 7 .   ? 11.976 37.021  -1.540 1.00 25.75 ? 1469 HOH   A O    1 
HETATM 19626 O  O    . HOH   M 7 .   ? 23.316 7.377   41.945 1.00 35.70 ? 1470 HOH   A O    1 
HETATM 19627 O  O    . HOH   M 7 .   ? 2.762  21.900  30.684 1.00 22.72 ? 1471 HOH   A O    1 
HETATM 19628 O  O    . HOH   M 7 .   ? 31.866 24.738  40.138 1.00 23.31 ? 1472 HOH   A O    1 
HETATM 19629 O  O    . HOH   M 7 .   ? 2.782  48.351  44.142 1.00 41.19 ? 1473 HOH   A O    1 
HETATM 19630 O  O    B HOH   M 7 .   ? 12.324 32.919  -1.343 0.90 37.16 ? 1474 HOH   A O    1 
HETATM 19631 O  O    . HOH   M 7 .   ? 37.236 9.896   26.498 1.00 36.58 ? 1475 HOH   A O    1 
HETATM 19632 O  O    . HOH   M 7 .   ? 5.870  14.278  0.894  1.00 28.81 ? 1476 HOH   A O    1 
HETATM 19633 O  O    . HOH   M 7 .   ? 46.915 51.536  29.537 1.00 28.31 ? 1477 HOH   A O    1 
HETATM 19634 O  O    . HOH   M 7 .   ? 19.152 58.110  17.423 1.00 36.87 ? 1478 HOH   A O    1 
HETATM 19635 O  O    . HOH   M 7 .   ? -6.450 30.507  8.137  1.00 37.05 ? 1479 HOH   A O    1 
HETATM 19636 O  O    . HOH   M 7 .   ? 4.742  52.371  36.619 1.00 42.51 ? 1480 HOH   A O    1 
HETATM 19637 O  O    . HOH   M 7 .   ? 48.485 27.331  34.050 1.00 28.54 ? 1481 HOH   A O    1 
HETATM 19638 O  O    . HOH   M 7 .   ? 19.021 45.305  -4.868 1.00 34.23 ? 1482 HOH   A O    1 
HETATM 19639 O  O    . HOH   M 7 .   ? 27.708 35.818  41.740 1.00 23.83 ? 1483 HOH   A O    1 
HETATM 19640 O  O    . HOH   M 7 .   ? 25.874 4.949   31.208 1.00 39.80 ? 1484 HOH   A O    1 
HETATM 19641 O  O    . HOH   M 7 .   ? 48.233 47.698  17.382 1.00 32.89 ? 1485 HOH   A O    1 
HETATM 19642 O  O    . HOH   M 7 .   ? 8.187  32.389  -4.407 1.00 29.28 ? 1486 HOH   A O    1 
HETATM 19643 O  O    . HOH   M 7 .   ? 31.439 12.500  34.181 1.00 35.03 ? 1487 HOH   A O    1 
HETATM 19644 O  O    . HOH   M 7 .   ? 40.495 55.753  20.800 1.00 29.32 ? 1488 HOH   A O    1 
HETATM 19645 O  O    . HOH   M 7 .   ? 22.579 41.532  -6.149 1.00 27.45 ? 1489 HOH   A O    1 
HETATM 19646 O  O    . HOH   M 7 .   ? -2.108 14.783  3.960  1.00 29.58 ? 1490 HOH   A O    1 
HETATM 19647 O  O    . HOH   M 7 .   ? 22.152 59.624  19.814 1.00 36.43 ? 1491 HOH   A O    1 
HETATM 19648 O  O    . HOH   M 7 .   ? 31.199 7.119   24.762 1.00 31.62 ? 1492 HOH   A O    1 
HETATM 19649 O  O    . HOH   M 7 .   ? 35.391 5.428   2.232  1.00 37.90 ? 1493 HOH   A O    1 
HETATM 19650 O  O    . HOH   M 7 .   ? 15.117 2.174   18.568 1.00 33.21 ? 1494 HOH   A O    1 
HETATM 19651 O  O    . HOH   M 7 .   ? 2.996  44.387  42.435 1.00 38.83 ? 1495 HOH   A O    1 
HETATM 19652 O  O    . HOH   M 7 .   ? 27.458 6.091   32.879 1.00 31.91 ? 1496 HOH   A O    1 
HETATM 19653 O  O    . HOH   M 7 .   ? 7.812  46.875  -1.392 1.00 30.38 ? 1497 HOH   A O    1 
HETATM 19654 O  O    . HOH   M 7 .   ? -4.981 18.810  4.918  1.00 34.54 ? 1498 HOH   A O    1 
HETATM 19655 O  O    . HOH   M 7 .   ? 24.219 59.124  18.490 1.00 34.39 ? 1499 HOH   A O    1 
HETATM 19656 O  O    . HOH   M 7 .   ? 15.447 2.479   6.189  1.00 26.07 ? 1500 HOH   A O    1 
HETATM 19657 O  O    . HOH   M 7 .   ? 28.360 23.078  41.814 1.00 28.22 ? 1501 HOH   A O    1 
HETATM 19658 O  O    . HOH   M 7 .   ? 34.731 -2.766  6.521  1.00 25.92 ? 1502 HOH   A O    1 
HETATM 19659 O  O    . HOH   M 7 .   ? -4.003 41.567  10.336 1.00 37.87 ? 1503 HOH   A O    1 
HETATM 19660 O  O    . HOH   M 7 .   ? 4.455  45.798  10.909 1.00 30.12 ? 1504 HOH   A O    1 
HETATM 19661 O  O    . HOH   M 7 .   ? 19.436 1.617   7.267  1.00 23.82 ? 1505 HOH   A O    1 
HETATM 19662 O  O    . HOH   M 7 .   ? 29.880 20.819  37.692 1.00 21.04 ? 1506 HOH   A O    1 
HETATM 19663 O  O    . HOH   M 7 .   ? 12.431 3.286   31.038 1.00 37.68 ? 1507 HOH   A O    1 
HETATM 19664 O  O    . HOH   M 7 .   ? -5.577 22.181  3.947  1.00 28.94 ? 1508 HOH   A O    1 
HETATM 19665 O  O    . HOH   M 7 .   ? 39.994 45.221  46.345 1.00 32.10 ? 1509 HOH   A O    1 
HETATM 19666 O  O    . HOH   M 7 .   ? 44.862 49.145  22.228 1.00 19.56 ? 1510 HOH   A O    1 
HETATM 19667 O  O    B HOH   M 7 .   ? 5.647  44.758  22.519 0.68 28.93 ? 1511 HOH   A O    1 
HETATM 19668 O  O    . HOH   M 7 .   ? 5.158  36.866  45.246 1.00 34.50 ? 1512 HOH   A O    1 
HETATM 19669 O  O    . HOH   M 7 .   ? 47.924 34.087  11.852 1.00 25.68 ? 1513 HOH   A O    1 
HETATM 19670 O  O    . HOH   M 7 .   ? 32.872 21.070  38.067 1.00 20.73 ? 1514 HOH   A O    1 
HETATM 19671 O  O    . HOH   M 7 .   ? 50.407 25.083  23.995 1.00 31.39 ? 1515 HOH   A O    1 
HETATM 19672 O  O    . HOH   M 7 .   ? -8.844 39.366  4.180  1.00 23.93 ? 1516 HOH   A O    1 
HETATM 19673 O  O    . HOH   M 7 .   ? 48.527 24.870  39.747 1.00 24.54 ? 1517 HOH   A O    1 
HETATM 19674 O  O    . HOH   M 7 .   ? 41.992 45.008  11.877 1.00 29.87 ? 1518 HOH   A O    1 
HETATM 19675 O  O    . HOH   M 7 .   ? -5.270 37.308  15.649 1.00 28.95 ? 1519 HOH   A O    1 
HETATM 19676 O  O    . HOH   M 7 .   ? 26.738 55.254  16.602 1.00 32.64 ? 1520 HOH   A O    1 
HETATM 19677 O  O    . HOH   M 7 .   ? -6.303 40.551  3.909  1.00 28.03 ? 1521 HOH   A O    1 
HETATM 19678 O  O    . HOH   M 7 .   ? 28.517 45.445  46.879 1.00 35.11 ? 1522 HOH   A O    1 
HETATM 19679 O  O    . HOH   M 7 .   ? 29.266 19.850  33.403 1.00 15.89 ? 1523 HOH   A O    1 
HETATM 19680 O  O    . HOH   M 7 .   ? 30.286 33.629  3.688  1.00 26.46 ? 1524 HOH   A O    1 
HETATM 19681 O  O    . HOH   M 7 .   ? 3.190  23.036  37.940 1.00 30.15 ? 1525 HOH   A O    1 
HETATM 19682 O  O    . HOH   M 7 .   ? -6.960 33.768  13.567 1.00 33.89 ? 1526 HOH   A O    1 
HETATM 19683 O  O    . HOH   M 7 .   ? 31.464 30.432  40.789 1.00 30.30 ? 1527 HOH   A O    1 
HETATM 19684 O  O    . HOH   M 7 .   ? 21.456 23.811  0.428  1.00 24.36 ? 1528 HOH   A O    1 
HETATM 19685 O  O    . HOH   M 7 .   ? 31.445 4.198   22.569 1.00 32.72 ? 1529 HOH   A O    1 
HETATM 19686 O  O    . HOH   M 7 .   ? 33.515 8.329   23.836 1.00 25.61 ? 1530 HOH   A O    1 
HETATM 19687 O  O    . HOH   M 7 .   ? 52.432 37.312  16.634 1.00 34.13 ? 1531 HOH   A O    1 
HETATM 19688 O  O    . HOH   M 7 .   ? 2.536  21.850  33.419 1.00 28.65 ? 1532 HOH   A O    1 
HETATM 19689 O  O    . HOH   M 7 .   ? 18.265 -0.029  3.760  1.00 33.74 ? 1533 HOH   A O    1 
HETATM 19690 O  O    . HOH   M 7 .   ? 7.284  29.113  -5.250 1.00 40.53 ? 1534 HOH   A O    1 
HETATM 19691 O  O    . HOH   M 7 .   ? 44.683 24.503  14.532 1.00 42.19 ? 1535 HOH   A O    1 
HETATM 19692 O  O    . HOH   M 7 .   ? 27.212 4.656   26.117 1.00 33.29 ? 1536 HOH   A O    1 
HETATM 19693 O  O    . HOH   M 7 .   ? 9.667  48.237  -2.966 1.00 28.95 ? 1537 HOH   A O    1 
HETATM 19694 O  O    . HOH   M 7 .   ? 15.533 57.319  20.459 1.00 35.81 ? 1538 HOH   A O    1 
HETATM 19695 O  O    . HOH   M 7 .   ? 43.816 52.583  32.618 1.00 28.49 ? 1539 HOH   A O    1 
HETATM 19696 O  O    . HOH   M 7 .   ? 33.053 57.374  33.882 1.00 40.55 ? 1540 HOH   A O    1 
HETATM 19697 O  O    . HOH   M 7 .   ? 0.946  36.936  -1.480 1.00 37.04 ? 1541 HOH   A O    1 
HETATM 19698 O  O    . HOH   M 7 .   ? 23.403 60.234  34.319 1.00 46.03 ? 1542 HOH   A O    1 
HETATM 19699 O  O    . HOH   M 7 .   ? 39.306 14.559  28.930 1.00 35.88 ? 1543 HOH   A O    1 
HETATM 19700 O  O    . HOH   M 7 .   ? 33.433 5.030   21.062 1.00 31.17 ? 1544 HOH   A O    1 
HETATM 19701 O  O    . HOH   M 7 .   ? 15.157 4.554   29.787 1.00 34.23 ? 1545 HOH   A O    1 
HETATM 19702 O  O    . HOH   M 7 .   ? 19.929 41.967  -5.536 1.00 33.49 ? 1546 HOH   A O    1 
HETATM 19703 O  O    . HOH   M 7 .   ? 46.804 25.096  17.562 1.00 35.85 ? 1547 HOH   A O    1 
HETATM 19704 O  O    . HOH   M 7 .   ? 25.449 9.542   -4.685 1.00 35.75 ? 1548 HOH   A O    1 
HETATM 19705 O  O    . HOH   M 7 .   ? 7.571  47.845  46.883 1.00 34.21 ? 1549 HOH   A O    1 
HETATM 19706 O  O    . HOH   M 7 .   ? 7.941  27.111  -1.898 1.00 35.63 ? 1550 HOH   A O    1 
HETATM 19707 O  O    . HOH   M 7 .   ? 32.759 9.837   27.610 1.00 28.49 ? 1551 HOH   A O    1 
HETATM 19708 O  O    . HOH   M 7 .   ? -1.544 16.305  1.520  1.00 30.43 ? 1552 HOH   A O    1 
HETATM 19709 O  O    . HOH   M 7 .   ? 36.451 43.410  48.331 1.00 38.15 ? 1553 HOH   A O    1 
HETATM 19710 O  O    . HOH   M 7 .   ? 19.369 60.349  36.842 1.00 32.58 ? 1554 HOH   A O    1 
HETATM 19711 O  O    . HOH   M 7 .   ? 10.205 40.059  -6.541 1.00 28.25 ? 1555 HOH   A O    1 
HETATM 19712 O  O    . HOH   M 7 .   ? 30.712 -4.203  4.915  1.00 38.03 ? 1556 HOH   A O    1 
HETATM 19713 O  O    . HOH   M 7 .   ? 26.727 13.162  -6.553 1.00 26.90 ? 1557 HOH   A O    1 
HETATM 19714 O  O    . HOH   M 7 .   ? 7.365  8.573   38.099 1.00 36.81 ? 1558 HOH   A O    1 
HETATM 19715 O  O    . HOH   M 7 .   ? 36.953 -3.653  10.472 1.00 27.58 ? 1559 HOH   A O    1 
HETATM 19716 O  O    . HOH   M 7 .   ? 52.814 26.748  24.057 1.00 29.04 ? 1560 HOH   A O    1 
HETATM 19717 O  O    . HOH   M 7 .   ? -0.797 43.487  12.287 1.00 28.92 ? 1561 HOH   A O    1 
HETATM 19718 O  O    . HOH   M 7 .   ? 50.539 29.568  37.585 1.00 35.08 ? 1562 HOH   A O    1 
HETATM 19719 O  O    . HOH   M 7 .   ? 29.863 23.448  39.243 1.00 23.80 ? 1563 HOH   A O    1 
HETATM 19720 O  O    . HOH   M 7 .   ? 40.043 13.370  8.311  1.00 37.55 ? 1564 HOH   A O    1 
HETATM 19721 O  O    . HOH   M 7 .   ? 33.538 13.451  30.609 1.00 36.81 ? 1565 HOH   A O    1 
HETATM 19722 O  O    . HOH   M 7 .   ? 47.961 36.696  9.442  1.00 38.25 ? 1566 HOH   A O    1 
HETATM 19723 O  O    . HOH   M 7 .   ? 41.862 28.571  10.170 1.00 22.60 ? 1567 HOH   A O    1 
HETATM 19724 O  O    . HOH   M 7 .   ? 30.202 59.905  29.222 1.00 33.60 ? 1568 HOH   A O    1 
HETATM 19725 O  O    . HOH   M 7 .   ? 1.459  25.946  31.566 1.00 28.95 ? 1569 HOH   A O    1 
HETATM 19726 O  O    . HOH   M 7 .   ? 22.433 47.514  44.529 1.00 34.00 ? 1570 HOH   A O    1 
HETATM 19727 O  O    . HOH   M 7 .   ? 40.819 43.686  7.268  1.00 33.93 ? 1571 HOH   A O    1 
HETATM 19728 O  O    . HOH   M 7 .   ? 40.377 26.086  10.231 1.00 24.49 ? 1572 HOH   A O    1 
HETATM 19729 O  O    . HOH   M 7 .   ? 4.012  49.478  22.756 1.00 37.43 ? 1573 HOH   A O    1 
HETATM 19730 O  O    . HOH   M 7 .   ? 32.864 -4.236  10.597 1.00 26.13 ? 1574 HOH   A O    1 
HETATM 19731 O  O    . HOH   M 7 .   ? 36.484 26.674  8.792  1.00 31.23 ? 1575 HOH   A O    1 
HETATM 19732 O  O    . HOH   M 7 .   ? 2.573  42.521  25.713 1.00 34.25 ? 1576 HOH   A O    1 
HETATM 19733 O  O    . HOH   M 7 .   ? 31.536 47.616  5.522  1.00 29.07 ? 1577 HOH   A O    1 
HETATM 19734 O  O    . HOH   M 7 .   ? 50.628 24.559  36.158 1.00 38.69 ? 1578 HOH   A O    1 
HETATM 19735 O  O    . HOH   M 7 .   ? 35.709 7.178   25.125 1.00 40.11 ? 1579 HOH   A O    1 
HETATM 19736 O  O    . HOH   M 7 .   ? 29.772 24.237  43.609 0.68 28.46 ? 1580 HOH   A O    1 
HETATM 19737 O  O    . HOH   M 7 .   ? 0.000  14.884  0.000  0.50 28.05 ? 1581 HOH   A O    1 
HETATM 19738 O  O    . HOH   M 7 .   ? 50.544 26.423  38.403 1.00 27.59 ? 1582 HOH   A O    1 
HETATM 19739 O  O    . HOH   M 7 .   ? 12.071 32.502  -4.067 1.00 35.93 ? 1583 HOH   A O    1 
HETATM 19740 O  O    . HOH   N 7 .   ? -0.848 27.786  61.330 1.00 28.95 ? 801  HOH   B O    1 
HETATM 19741 O  O    . HOH   N 7 .   ? 38.153 0.313   66.794 1.00 28.95 ? 802  HOH   B O    1 
HETATM 19742 O  O    . HOH   N 7 .   ? 33.003 -7.448  71.177 1.00 28.95 ? 803  HOH   B O    1 
HETATM 19743 O  O    . HOH   N 7 .   ? 50.892 24.082  62.089 1.00 30.28 ? 804  HOH   B O    1 
HETATM 19744 O  O    . HOH   N 7 .   ? 31.221 44.081  81.953 1.00 32.38 ? 805  HOH   B O    1 
HETATM 19745 O  O    . HOH   N 7 .   ? 40.844 30.243  73.771 1.00 34.41 ? 806  HOH   B O    1 
HETATM 19746 O  O    . HOH   N 7 .   ? 4.828  43.918  68.004 1.00 31.96 ? 807  HOH   B O    1 
HETATM 19747 O  O    . HOH   N 7 .   ? 33.502 47.450  76.187 1.00 29.02 ? 808  HOH   B O    1 
HETATM 19748 O  O    . HOH   N 7 .   ? 41.187 33.327  65.315 1.00 34.57 ? 809  HOH   B O    1 
HETATM 19749 O  O    . HOH   N 7 .   ? 14.143 -10.959 86.186 1.00 25.97 ? 810  HOH   B O    1 
HETATM 19750 O  O    . HOH   N 7 .   ? 14.674 22.393  64.281 1.00 12.19 ? 811  HOH   B O    1 
HETATM 19751 O  O    . HOH   N 7 .   ? 15.132 24.681  55.811 1.00 14.33 ? 812  HOH   B O    1 
HETATM 19752 O  O    . HOH   N 7 .   ? 51.249 21.490  61.895 1.00 31.34 ? 813  HOH   B O    1 
HETATM 19753 O  O    . HOH   N 7 .   ? 5.294  23.963  87.025 1.00 18.30 ? 814  HOH   B O    1 
HETATM 19754 O  O    . HOH   N 7 .   ? 5.534  -5.304  66.751 1.00 37.81 ? 815  HOH   B O    1 
HETATM 19755 O  O    . HOH   N 7 .   ? 36.597 0.559   72.041 1.00 31.55 ? 816  HOH   B O    1 
HETATM 19756 O  O    . HOH   N 7 .   ? -1.863 22.924  83.508 1.00 32.83 ? 817  HOH   B O    1 
HETATM 19757 O  O    . HOH   N 7 .   ? 20.441 -9.042  79.024 1.00 29.22 ? 818  HOH   B O    1 
HETATM 19758 O  O    . HOH   N 7 .   ? 30.364 16.305  83.103 1.00 18.15 ? 819  HOH   B O    1 
HETATM 19759 O  O    . HOH   N 7 .   ? 16.317 32.747  74.568 1.00 11.22 ? 820  HOH   B O    1 
HETATM 19760 O  O    . HOH   N 7 .   ? 4.859  10.720  61.835 1.00 25.79 ? 821  HOH   B O    1 
HETATM 19761 O  O    . HOH   N 7 .   ? 26.768 52.123  76.356 1.00 24.15 ? 822  HOH   B O    1 
HETATM 19762 O  O    . HOH   N 7 .   ? 21.091 48.469  82.133 1.00 31.12 ? 823  HOH   B O    1 
HETATM 19763 O  O    . HOH   N 7 .   ? 31.526 5.189   44.223 1.00 33.85 ? 824  HOH   B O    1 
HETATM 19764 O  O    . HOH   N 7 .   ? 4.034  19.652  92.949 1.00 32.45 ? 825  HOH   B O    1 
HETATM 19765 O  O    . HOH   N 7 .   ? 47.985 13.253  49.141 1.00 33.49 ? 826  HOH   B O    1 
HETATM 19766 O  O    . HOH   N 7 .   ? 40.297 9.898   84.416 1.00 32.57 ? 827  HOH   B O    1 
HETATM 19767 O  O    . HOH   N 7 .   ? -4.504 11.885  85.074 1.00 28.95 ? 828  HOH   B O    1 
HETATM 19768 O  O    . HOH   N 7 .   ? 3.098  36.167  83.288 1.00 30.21 ? 829  HOH   B O    1 
HETATM 19769 O  O    . HOH   N 7 .   ? 11.133 36.779  85.161 1.00 25.49 ? 830  HOH   B O    1 
HETATM 19770 O  O    . HOH   N 7 .   ? 33.000 12.052  45.775 1.00 27.44 ? 831  HOH   B O    1 
HETATM 19771 O  O    . HOH   N 7 .   ? 52.131 14.648  56.111 1.00 31.72 ? 832  HOH   B O    1 
HETATM 19772 O  O    . HOH   N 7 .   ? 43.099 14.413  48.578 1.00 15.29 ? 833  HOH   B O    1 
HETATM 19773 O  O    . HOH   N 7 .   ? 7.971  15.988  90.953 1.00 29.57 ? 834  HOH   B O    1 
HETATM 19774 O  O    . HOH   N 7 .   ? 42.394 14.312  81.476 1.00 30.72 ? 835  HOH   B O    1 
HETATM 19775 O  O    . HOH   N 7 .   ? 48.002 9.638   73.252 1.00 26.45 ? 836  HOH   B O    1 
HETATM 19776 O  O    . HOH   N 7 .   ? 40.452 34.482  62.304 1.00 17.33 ? 837  HOH   B O    1 
HETATM 19777 O  O    . HOH   N 7 .   ? 16.435 10.808  70.711 1.00 12.61 ? 838  HOH   B O    1 
HETATM 19778 O  O    . HOH   N 7 .   ? 12.075 -2.486  82.562 1.00 33.09 ? 839  HOH   B O    1 
HETATM 19779 O  O    . HOH   N 7 .   ? 31.374 43.532  65.240 1.00 22.33 ? 840  HOH   B O    1 
HETATM 19780 O  O    . HOH   N 7 .   ? 20.631 1.031   90.711 1.00 31.61 ? 841  HOH   B O    1 
HETATM 19781 O  O    . HOH   N 7 .   ? 17.305 11.742  82.764 1.00 18.13 ? 842  HOH   B O    1 
HETATM 19782 O  O    . HOH   N 7 .   ? 17.310 45.259  75.961 1.00 15.46 ? 843  HOH   B O    1 
HETATM 19783 O  O    . HOH   N 7 .   ? 30.410 32.891  84.824 1.00 33.29 ? 844  HOH   B O    1 
HETATM 19784 O  O    . HOH   N 7 .   ? 19.443 35.797  90.939 1.00 34.95 ? 845  HOH   B O    1 
HETATM 19785 O  O    . HOH   N 7 .   ? 39.445 2.500   52.909 1.00 22.68 ? 846  HOH   B O    1 
HETATM 19786 O  O    . HOH   N 7 .   ? 51.486 16.237  67.038 1.00 24.44 ? 847  HOH   B O    1 
HETATM 19787 O  O    . HOH   N 7 .   ? 2.257  21.645  53.491 1.00 29.14 ? 848  HOH   B O    1 
HETATM 19788 O  O    . HOH   N 7 .   ? -3.661 32.333  66.594 1.00 30.84 ? 849  HOH   B O    1 
HETATM 19789 O  O    . HOH   N 7 .   ? 37.168 33.944  71.568 1.00 18.04 ? 850  HOH   B O    1 
HETATM 19790 O  O    . HOH   N 7 .   ? 2.005  10.487  52.146 1.00 28.66 ? 851  HOH   B O    1 
HETATM 19791 O  O    . HOH   N 7 .   ? 40.715 8.972   77.256 1.00 27.49 ? 852  HOH   B O    1 
HETATM 19792 O  O    . HOH   N 7 .   ? 36.949 22.700  43.731 1.00 20.07 ? 853  HOH   B O    1 
HETATM 19793 O  O    . HOH   N 7 .   ? 50.438 17.468  71.534 1.00 32.09 ? 854  HOH   B O    1 
HETATM 19794 O  O    . HOH   N 7 .   ? 41.902 32.230  51.612 1.00 19.66 ? 855  HOH   B O    1 
HETATM 19795 O  O    . HOH   N 7 .   ? 14.211 25.201  87.845 1.00 25.65 ? 856  HOH   B O    1 
HETATM 19796 O  O    . HOH   N 7 .   ? 12.222 41.318  47.624 1.00 31.47 ? 857  HOH   B O    1 
HETATM 19797 O  O    . HOH   N 7 .   ? 54.496 12.534  66.852 1.00 33.64 ? 858  HOH   B O    1 
HETATM 19798 O  O    . HOH   N 7 .   ? -0.136 16.967  57.171 1.00 32.68 ? 859  HOH   B O    1 
HETATM 19799 O  O    . HOH   N 7 .   ? 2.838  36.415  75.170 1.00 15.33 ? 860  HOH   B O    1 
HETATM 19800 O  O    . HOH   N 7 .   ? 28.033 30.923  47.490 1.00 23.08 ? 861  HOH   B O    1 
HETATM 19801 O  O    . HOH   N 7 .   ? 3.307  28.182  57.756 1.00 17.75 ? 862  HOH   B O    1 
HETATM 19802 O  O    . HOH   N 7 .   ? 43.101 25.770  69.499 1.00 27.24 ? 863  HOH   B O    1 
HETATM 19803 O  O    . HOH   N 7 .   ? 32.218 49.181  82.952 1.00 40.66 ? 864  HOH   B O    1 
HETATM 19804 O  O    . HOH   N 7 .   ? 17.835 -6.132  74.699 1.00 34.50 ? 865  HOH   B O    1 
HETATM 19805 O  O    . HOH   N 7 .   ? 29.525 40.456  63.730 1.00 18.35 ? 866  HOH   B O    1 
HETATM 19806 O  O    . HOH   N 7 .   ? 31.201 1.563   78.531 1.00 23.37 ? 867  HOH   B O    1 
HETATM 19807 O  O    . HOH   N 7 .   ? 23.428 -9.745  55.656 1.00 26.87 ? 868  HOH   B O    1 
HETATM 19808 O  O    . HOH   N 7 .   ? 38.287 20.409  42.985 1.00 21.06 ? 869  HOH   B O    1 
HETATM 19809 O  O    . HOH   N 7 .   ? 34.219 41.565  78.626 1.00 31.39 ? 870  HOH   B O    1 
HETATM 19810 O  O    . HOH   N 7 .   ? 1.816  6.820   81.103 1.00 25.76 ? 871  HOH   B O    1 
HETATM 19811 O  O    . HOH   N 7 .   ? 29.088 37.294  83.201 1.00 21.82 ? 872  HOH   B O    1 
HETATM 19812 O  O    . HOH   N 7 .   ? 21.440 36.553  92.803 1.00 27.69 ? 873  HOH   B O    1 
HETATM 19813 O  O    . HOH   N 7 .   ? 34.103 20.065  48.810 1.00 17.15 ? 874  HOH   B O    1 
HETATM 19814 O  O    . HOH   N 7 .   ? 20.419 28.100  60.107 1.00 13.57 ? 875  HOH   B O    1 
HETATM 19815 O  O    . HOH   N 7 .   ? 42.724 19.319  43.047 1.00 29.33 ? 876  HOH   B O    1 
HETATM 19816 O  O    . HOH   N 7 .   ? 13.183 -5.037  53.760 1.00 25.71 ? 877  HOH   B O    1 
HETATM 19817 O  O    . HOH   N 7 .   ? 46.696 18.564  50.735 1.00 21.32 ? 878  HOH   B O    1 
HETATM 19818 O  O    . HOH   N 7 .   ? 20.569 13.269  53.105 1.00 13.37 ? 879  HOH   B O    1 
HETATM 19819 O  O    . HOH   N 7 .   ? 16.473 9.311   47.714 1.00 22.30 ? 880  HOH   B O    1 
HETATM 19820 O  O    . HOH   N 7 .   ? 15.985 19.562  90.029 1.00 25.95 ? 881  HOH   B O    1 
HETATM 19821 O  O    . HOH   N 7 .   ? 20.999 16.246  46.754 1.00 24.64 ? 882  HOH   B O    1 
HETATM 19822 O  O    . HOH   N 7 .   ? 33.568 42.229  85.010 1.00 36.77 ? 883  HOH   B O    1 
HETATM 19823 O  O    . HOH   N 7 .   ? 24.186 18.466  49.275 1.00 28.59 ? 884  HOH   B O    1 
HETATM 19824 O  O    . HOH   N 7 .   ? 31.043 38.072  88.626 1.00 34.08 ? 885  HOH   B O    1 
HETATM 19825 O  O    . HOH   N 7 .   ? 21.006 -9.989  90.293 1.00 28.80 ? 886  HOH   B O    1 
HETATM 19826 O  O    . HOH   N 7 .   ? 21.863 26.788  55.147 1.00 14.72 ? 887  HOH   B O    1 
HETATM 19827 O  O    . HOH   N 7 .   ? 0.559  8.382   75.270 1.00 23.73 ? 888  HOH   B O    1 
HETATM 19828 O  O    . HOH   N 7 .   ? 21.872 16.052  67.223 1.00 12.81 ? 889  HOH   B O    1 
HETATM 19829 O  O    . HOH   N 7 .   ? 36.814 27.643  76.363 1.00 24.30 ? 890  HOH   B O    1 
HETATM 19830 O  O    . HOH   N 7 .   ? 8.551  1.531   86.027 1.00 26.38 ? 891  HOH   B O    1 
HETATM 19831 O  O    . HOH   N 7 .   ? 41.279 -0.440  56.166 1.00 25.07 ? 892  HOH   B O    1 
HETATM 19832 O  O    . HOH   N 7 .   ? 30.263 39.656  84.711 1.00 22.09 ? 893  HOH   B O    1 
HETATM 19833 O  O    . HOH   N 7 .   ? 4.931  2.968   84.734 1.00 29.96 ? 894  HOH   B O    1 
HETATM 19834 O  O    . HOH   N 7 .   ? 40.477 17.120  73.287 1.00 16.60 ? 895  HOH   B O    1 
HETATM 19835 O  O    . HOH   N 7 .   ? 26.853 51.251  73.720 1.00 29.76 ? 896  HOH   B O    1 
HETATM 19836 O  O    . HOH   N 7 .   ? 10.903 1.833   87.365 1.00 25.75 ? 897  HOH   B O    1 
HETATM 19837 O  O    . HOH   N 7 .   ? 27.034 14.195  54.592 1.00 10.49 ? 898  HOH   B O    1 
HETATM 19838 O  O    . HOH   N 7 .   ? 32.726 35.400  54.704 1.00 27.72 ? 899  HOH   B O    1 
HETATM 19839 O  O    . HOH   N 7 .   ? 13.960 31.540  85.159 1.00 18.95 ? 900  HOH   B O    1 
HETATM 19840 O  O    . HOH   N 7 .   ? 16.530 40.194  62.553 1.00 14.11 ? 901  HOH   B O    1 
HETATM 19841 O  O    . HOH   N 7 .   ? 22.937 40.472  90.541 1.00 27.94 ? 902  HOH   B O    1 
HETATM 19842 O  O    . HOH   N 7 .   ? -2.860 21.324  81.605 1.00 31.20 ? 903  HOH   B O    1 
HETATM 19843 O  O    . HOH   N 7 .   ? 21.830 32.730  55.395 1.00 12.30 ? 904  HOH   B O    1 
HETATM 19844 O  O    . HOH   N 7 .   ? -4.420 29.336  80.735 1.00 28.78 ? 905  HOH   B O    1 
HETATM 19845 O  O    . HOH   N 7 .   ? 27.068 49.169  64.574 1.00 28.01 ? 906  HOH   B O    1 
HETATM 19846 O  O    . HOH   N 7 .   ? 27.165 45.670  86.376 1.00 35.21 ? 907  HOH   B O    1 
HETATM 19847 O  O    . HOH   N 7 .   ? 12.249 -1.694  86.543 1.00 34.25 ? 908  HOH   B O    1 
HETATM 19848 O  O    . HOH   N 7 .   ? 25.306 25.068  71.423 1.00 12.52 ? 909  HOH   B O    1 
HETATM 19849 O  O    . HOH   N 7 .   ? 11.409 15.693  45.411 1.00 29.40 ? 910  HOH   B O    1 
HETATM 19850 O  O    . HOH   N 7 .   ? 10.060 32.797  87.806 1.00 29.81 ? 911  HOH   B O    1 
HETATM 19851 O  O    . HOH   N 7 .   ? -4.228 13.459  77.280 1.00 32.04 ? 912  HOH   B O    1 
HETATM 19852 O  O    . HOH   N 7 .   ? -7.603 17.015  75.960 1.00 32.83 ? 913  HOH   B O    1 
HETATM 19853 O  O    . HOH   N 7 .   ? 37.124 41.662  76.744 1.00 35.06 ? 914  HOH   B O    1 
HETATM 19854 O  O    . HOH   N 7 .   ? 49.059 12.234  75.987 1.00 35.76 ? 915  HOH   B O    1 
HETATM 19855 O  O    . HOH   N 7 .   ? 13.420 -8.772  56.383 1.00 29.12 ? 916  HOH   B O    1 
HETATM 19856 O  O    . HOH   N 7 .   ? 27.712 34.623  49.312 1.00 28.65 ? 917  HOH   B O    1 
HETATM 19857 O  O    . HOH   N 7 .   ? 16.943 24.582  83.395 1.00 17.10 ? 918  HOH   B O    1 
HETATM 19858 O  O    . HOH   N 7 .   ? 43.873 32.397  48.077 1.00 20.01 ? 919  HOH   B O    1 
HETATM 19859 O  O    . HOH   N 7 .   ? 14.888 -7.820  83.139 1.00 28.87 ? 920  HOH   B O    1 
HETATM 19860 O  O    . HOH   N 7 .   ? 12.697 34.460  45.494 1.00 21.22 ? 921  HOH   B O    1 
HETATM 19861 O  O    . HOH   N 7 .   ? 46.834 21.201  43.743 1.00 37.21 ? 922  HOH   B O    1 
HETATM 19862 O  O    . HOH   N 7 .   ? 23.672 5.906   47.261 1.00 25.03 ? 923  HOH   B O    1 
HETATM 19863 O  O    . HOH   N 7 .   ? 43.657 0.384   69.479 1.00 31.54 ? 924  HOH   B O    1 
HETATM 19864 O  O    . HOH   N 7 .   ? 20.018 14.685  84.370 1.00 22.08 ? 925  HOH   B O    1 
HETATM 19865 O  O    . HOH   N 7 .   ? 25.999 22.547  51.639 1.00 13.97 ? 926  HOH   B O    1 
HETATM 19866 O  O    . HOH   N 7 .   ? 21.628 36.028  42.693 1.00 12.54 ? 927  HOH   B O    1 
HETATM 19867 O  O    . HOH   N 7 .   ? 9.040  6.688   44.194 1.00 31.45 ? 928  HOH   B O    1 
HETATM 19868 O  O    . HOH   N 7 .   ? 24.495 29.972  87.524 1.00 25.41 ? 929  HOH   B O    1 
HETATM 19869 O  O    . HOH   N 7 .   ? 37.540 37.066  60.642 1.00 28.55 ? 930  HOH   B O    1 
HETATM 19870 O  O    . HOH   N 7 .   ? 8.807  44.560  62.593 1.00 19.89 ? 931  HOH   B O    1 
HETATM 19871 O  O    . HOH   N 7 .   ? 14.533 3.288   79.546 1.00 18.99 ? 932  HOH   B O    1 
HETATM 19872 O  O    . HOH   N 7 .   ? 37.025 31.493  73.000 1.00 18.68 ? 933  HOH   B O    1 
HETATM 19873 O  O    . HOH   N 7 .   ? 6.491  42.111  68.768 1.00 27.86 ? 934  HOH   B O    1 
HETATM 19874 O  O    . HOH   N 7 .   ? 45.446 11.218  51.655 1.00 24.17 ? 935  HOH   B O    1 
HETATM 19875 O  O    . HOH   N 7 .   ? -3.237 13.868  62.537 1.00 34.17 ? 936  HOH   B O    1 
HETATM 19876 O  O    . HOH   N 7 .   ? 7.269  43.535  73.725 1.00 25.55 ? 937  HOH   B O    1 
HETATM 19877 O  O    . HOH   N 7 .   ? 10.031 -2.238  71.512 1.00 26.23 ? 938  HOH   B O    1 
HETATM 19878 O  O    . HOH   N 7 .   ? 20.788 29.543  84.838 1.00 19.96 ? 939  HOH   B O    1 
HETATM 19879 O  O    . HOH   N 7 .   ? 20.958 -7.702  92.181 1.00 25.33 ? 940  HOH   B O    1 
HETATM 19880 O  O    . HOH   N 7 .   ? -0.008 24.085  78.652 1.00 19.45 ? 941  HOH   B O    1 
HETATM 19881 O  O    . HOH   N 7 .   ? 35.190 38.974  60.159 1.00 30.83 ? 942  HOH   B O    1 
HETATM 19882 O  O    . HOH   N 7 .   ? 10.317 2.527   72.611 1.00 31.15 ? 943  HOH   B O    1 
HETATM 19883 O  O    . HOH   N 7 .   ? 18.639 13.869  81.234 1.00 23.70 ? 944  HOH   B O    1 
HETATM 19884 O  O    . HOH   N 7 .   ? 12.548 0.503   79.220 1.00 25.21 ? 945  HOH   B O    1 
HETATM 19885 O  O    . HOH   N 7 .   ? 5.915  16.238  46.347 1.00 23.57 ? 946  HOH   B O    1 
HETATM 19886 O  O    . HOH   N 7 .   ? 32.122 7.825   86.604 1.00 22.80 ? 947  HOH   B O    1 
HETATM 19887 O  O    . HOH   N 7 .   ? 21.350 23.736  58.464 1.00 11.81 ? 948  HOH   B O    1 
HETATM 19888 O  O    . HOH   N 7 .   ? 4.982  40.521  71.441 1.00 22.59 ? 949  HOH   B O    1 
HETATM 19889 O  O    . HOH   N 7 .   ? 23.409 30.820  85.060 1.00 19.20 ? 950  HOH   B O    1 
HETATM 19890 O  O    . HOH   N 7 .   ? 24.618 -9.661  66.071 1.00 33.97 ? 951  HOH   B O    1 
HETATM 19891 O  O    . HOH   N 7 .   ? 49.691 5.587   68.072 1.00 33.33 ? 952  HOH   B O    1 
HETATM 19892 O  O    . HOH   N 7 .   ? 34.667 32.612  50.618 1.00 22.98 ? 953  HOH   B O    1 
HETATM 19893 O  O    . HOH   N 7 .   ? 6.016  4.859   75.492 1.00 25.76 ? 954  HOH   B O    1 
HETATM 19894 O  O    . HOH   N 7 .   ? 24.857 28.533  78.039 1.00 12.42 ? 955  HOH   B O    1 
HETATM 19895 O  O    . HOH   N 7 .   ? 22.552 24.679  53.417 1.00 13.99 ? 956  HOH   B O    1 
HETATM 19896 O  O    . HOH   N 7 .   ? -3.599 38.927  82.825 1.00 36.57 ? 957  HOH   B O    1 
HETATM 19897 O  O    . HOH   N 7 .   ? 46.882 16.443  48.032 1.00 27.35 ? 958  HOH   B O    1 
HETATM 19898 O  O    . HOH   N 7 .   ? 43.570 6.570   47.645 1.00 23.87 ? 959  HOH   B O    1 
HETATM 19899 O  O    . HOH   N 7 .   ? 10.494 40.590  55.687 1.00 12.94 ? 960  HOH   B O    1 
HETATM 19900 O  O    . HOH   N 7 .   ? 6.497  39.121  80.243 1.00 30.73 ? 961  HOH   B O    1 
HETATM 19901 O  O    . HOH   N 7 .   ? 49.247 29.960  61.351 1.00 31.57 ? 962  HOH   B O    1 
HETATM 19902 O  O    . HOH   N 7 .   ? 12.850 14.080  67.462 1.00 12.98 ? 963  HOH   B O    1 
HETATM 19903 O  O    . HOH   N 7 .   ? 29.537 33.302  78.325 1.00 16.30 ? 964  HOH   B O    1 
HETATM 19904 O  O    . HOH   N 7 .   ? 49.615 8.702   57.459 1.00 31.15 ? 965  HOH   B O    1 
HETATM 19905 O  O    . HOH   N 7 .   ? 18.093 22.170  55.795 1.00 10.51 ? 966  HOH   B O    1 
HETATM 19906 O  O    . HOH   N 7 .   ? 35.725 35.104  76.074 1.00 22.91 ? 967  HOH   B O    1 
HETATM 19907 O  O    . HOH   N 7 .   ? 27.140 28.936  79.131 1.00 14.71 ? 968  HOH   B O    1 
HETATM 19908 O  O    . HOH   N 7 .   ? 37.183 2.840   48.554 1.00 24.09 ? 969  HOH   B O    1 
HETATM 19909 O  O    . HOH   N 7 .   ? 19.156 45.511  88.421 1.00 17.12 ? 970  HOH   B O    1 
HETATM 19910 O  O    . HOH   N 7 .   ? 2.396  16.253  48.010 1.00 34.03 ? 971  HOH   B O    1 
HETATM 19911 O  O    . HOH   N 7 .   ? 46.071 5.332   68.498 1.00 27.21 ? 972  HOH   B O    1 
HETATM 19912 O  O    . HOH   N 7 .   ? 11.540 44.989  69.396 1.00 29.92 ? 973  HOH   B O    1 
HETATM 19913 O  O    . HOH   N 7 .   ? 11.802 29.331  52.269 1.00 15.46 ? 974  HOH   B O    1 
HETATM 19914 O  O    . HOH   N 7 .   ? 40.758 38.873  69.786 1.00 34.50 ? 975  HOH   B O    1 
HETATM 19915 O  O    . HOH   N 7 .   ? 34.519 4.401   80.835 1.00 30.98 ? 976  HOH   B O    1 
HETATM 19916 O  O    . HOH   N 7 .   ? 2.057  12.025  81.144 1.00 17.61 ? 977  HOH   B O    1 
HETATM 19917 O  O    . HOH   N 7 .   ? 23.266 26.783  57.422 1.00 13.17 ? 978  HOH   B O    1 
HETATM 19918 O  O    . HOH   N 7 .   ? 29.189 12.819  48.888 1.00 20.38 ? 979  HOH   B O    1 
HETATM 19919 O  O    . HOH   N 7 .   ? 49.879 8.165   54.768 1.00 35.99 ? 980  HOH   B O    1 
HETATM 19920 O  O    . HOH   N 7 .   ? 39.186 19.225  45.534 1.00 17.36 ? 981  HOH   B O    1 
HETATM 19921 O  O    . HOH   N 7 .   ? 32.426 23.675  48.069 1.00 18.86 ? 982  HOH   B O    1 
HETATM 19922 O  O    . HOH   N 7 .   ? 9.197  16.671  48.516 1.00 25.37 ? 983  HOH   B O    1 
HETATM 19923 O  O    . HOH   N 7 .   ? 12.015 -7.773  84.784 1.00 34.46 ? 984  HOH   B O    1 
HETATM 19924 O  O    . HOH   N 7 .   ? 27.072 -10.141 63.329 1.00 35.85 ? 985  HOH   B O    1 
HETATM 19925 O  O    . HOH   N 7 .   ? 39.977 34.536  71.612 1.00 27.07 ? 986  HOH   B O    1 
HETATM 19926 O  O    . HOH   N 7 .   ? 4.502  33.661  88.819 1.00 36.16 ? 987  HOH   B O    1 
HETATM 19927 O  O    . HOH   N 7 .   ? 43.837 4.017   71.654 1.00 29.08 ? 988  HOH   B O    1 
HETATM 19928 O  O    . HOH   N 7 .   ? 9.097  8.031   89.066 1.00 17.14 ? 989  HOH   B O    1 
HETATM 19929 O  O    . HOH   N 7 .   ? 19.671 27.307  83.526 1.00 23.09 ? 990  HOH   B O    1 
HETATM 19930 O  O    . HOH   N 7 .   ? 19.191 38.182  90.169 1.00 33.90 ? 991  HOH   B O    1 
HETATM 19931 O  O    . HOH   N 7 .   ? 22.556 20.796  47.600 1.00 23.61 ? 992  HOH   B O    1 
HETATM 19932 O  O    . HOH   N 7 .   ? 15.368 46.355  62.736 1.00 17.61 ? 993  HOH   B O    1 
HETATM 19933 O  O    . HOH   N 7 .   ? 27.910 24.623  70.217 1.00 13.69 ? 994  HOH   B O    1 
HETATM 19934 O  O    . HOH   N 7 .   ? -4.012 23.739  80.741 1.00 34.38 ? 995  HOH   B O    1 
HETATM 19935 O  O    . HOH   N 7 .   ? 31.513 21.399  80.802 1.00 25.94 ? 996  HOH   B O    1 
HETATM 19936 O  O    . HOH   N 7 .   ? 32.665 24.231  81.738 1.00 29.62 ? 997  HOH   B O    1 
HETATM 19937 O  O    . HOH   N 7 .   ? 46.842 30.878  58.422 1.00 24.80 ? 998  HOH   B O    1 
HETATM 19938 O  O    . HOH   N 7 .   ? 33.760 27.442  46.150 1.00 26.65 ? 999  HOH   B O    1 
HETATM 19939 O  O    . HOH   N 7 .   ? 17.465 -5.809  91.380 1.00 16.89 ? 1000 HOH   B O    1 
HETATM 19940 O  O    . HOH   N 7 .   ? 31.791 15.523  87.023 1.00 36.25 ? 1001 HOH   B O    1 
HETATM 19941 O  O    . HOH   N 7 .   ? 10.780 -5.473  55.211 1.00 31.13 ? 1002 HOH   B O    1 
HETATM 19942 O  O    . HOH   N 7 .   ? 32.927 33.860  78.292 1.00 28.34 ? 1003 HOH   B O    1 
HETATM 19943 O  O    . HOH   N 7 .   ? 4.224  23.579  47.644 1.00 31.44 ? 1004 HOH   B O    1 
HETATM 19944 O  O    . HOH   N 7 .   ? 26.864 26.811  88.170 1.00 32.81 ? 1005 HOH   B O    1 
HETATM 19945 O  O    . HOH   N 7 .   ? 43.388 19.316  74.536 1.00 21.23 ? 1006 HOH   B O    1 
HETATM 19946 O  O    . HOH   N 7 .   ? 19.223 38.509  52.180 1.00 14.94 ? 1007 HOH   B O    1 
HETATM 19947 O  O    . HOH   N 7 .   ? 34.038 26.215  64.595 1.00 12.66 ? 1008 HOH   B O    1 
HETATM 19948 O  O    . HOH   N 7 .   ? 22.183 49.257  75.368 1.00 19.66 ? 1009 HOH   B O    1 
HETATM 19949 O  O    B HOH   N 7 .   ? 33.667 22.370  44.592 1.00 21.35 ? 1010 HOH   B O    1 
HETATM 19950 O  O    . HOH   N 7 .   ? 2.390  40.364  77.114 1.00 34.86 ? 1011 HOH   B O    1 
HETATM 19951 O  O    . HOH   N 7 .   ? 35.987 -5.751  58.767 1.00 25.49 ? 1012 HOH   B O    1 
HETATM 19952 O  O    . HOH   N 7 .   ? 52.325 15.176  59.844 1.00 26.70 ? 1013 HOH   B O    1 
HETATM 19953 O  O    . HOH   N 7 .   ? 18.203 18.242  79.117 1.00 11.67 ? 1014 HOH   B O    1 
HETATM 19954 O  O    . HOH   N 7 .   ? 24.332 19.409  73.014 1.00 12.39 ? 1015 HOH   B O    1 
HETATM 19955 O  O    . HOH   N 7 .   ? 28.254 2.695   58.721 1.00 16.31 ? 1016 HOH   B O    1 
HETATM 19956 O  O    . HOH   N 7 .   ? 4.795  4.957   55.818 1.00 27.14 ? 1017 HOH   B O    1 
HETATM 19957 O  O    . HOH   N 7 .   ? 14.645 43.294  51.676 1.00 38.10 ? 1018 HOH   B O    1 
HETATM 19958 O  O    . HOH   N 7 .   ? 1.625  28.736  53.882 1.00 27.44 ? 1019 HOH   B O    1 
HETATM 19959 O  O    . HOH   N 7 .   ? 37.130 7.175   87.479 1.00 33.72 ? 1020 HOH   B O    1 
HETATM 19960 O  O    . HOH   N 7 .   ? 25.012 1.521   47.617 1.00 25.60 ? 1021 HOH   B O    1 
HETATM 19961 O  O    . HOH   N 7 .   ? 8.240  -0.307  45.184 1.00 33.14 ? 1022 HOH   B O    1 
HETATM 19962 O  O    . HOH   N 7 .   ? 26.953 28.885  51.822 1.00 12.54 ? 1023 HOH   B O    1 
HETATM 19963 O  O    . HOH   N 7 .   ? 35.165 21.334  79.421 1.00 33.95 ? 1024 HOH   B O    1 
HETATM 19964 O  O    . HOH   N 7 .   ? 20.716 0.046   88.311 1.00 26.78 ? 1025 HOH   B O    1 
HETATM 19965 O  O    . HOH   N 7 .   ? 12.129 45.569  59.289 1.00 28.32 ? 1026 HOH   B O    1 
HETATM 19966 O  O    . HOH   N 7 .   ? 11.967 -0.854  75.352 1.00 27.33 ? 1027 HOH   B O    1 
HETATM 19967 O  O    . HOH   N 7 .   ? 22.232 -9.416  59.529 1.00 35.50 ? 1028 HOH   B O    1 
HETATM 19968 O  O    . HOH   N 7 .   ? 18.751 32.748  77.436 1.00 13.88 ? 1029 HOH   B O    1 
HETATM 19969 O  O    . HOH   N 7 .   ? 28.714 29.051  85.202 1.00 31.13 ? 1030 HOH   B O    1 
HETATM 19970 O  O    . HOH   N 7 .   ? 2.276  7.817   55.739 1.00 32.49 ? 1031 HOH   B O    1 
HETATM 19971 O  O    . HOH   N 7 .   ? 2.304  34.621  55.153 1.00 35.63 ? 1032 HOH   B O    1 
HETATM 19972 O  O    . HOH   N 7 .   ? 17.314 29.332  84.224 1.00 21.93 ? 1033 HOH   B O    1 
HETATM 19973 O  O    . HOH   N 7 .   ? 15.696 49.110  69.133 1.00 20.13 ? 1034 HOH   B O    1 
HETATM 19974 O  O    . HOH   N 7 .   ? 3.328  22.607  88.148 1.00 27.01 ? 1035 HOH   B O    1 
HETATM 19975 O  O    . HOH   N 7 .   ? 25.678 11.545  88.282 1.00 27.78 ? 1036 HOH   B O    1 
HETATM 19976 O  O    . HOH   N 7 .   ? 12.140 45.078  65.705 1.00 24.06 ? 1037 HOH   B O    1 
HETATM 19977 O  O    . HOH   N 7 .   ? 41.583 -3.077  59.818 1.00 16.68 ? 1038 HOH   B O    1 
HETATM 19978 O  O    . HOH   N 7 .   ? 38.692 26.358  45.466 1.00 12.70 ? 1039 HOH   B O    1 
HETATM 19979 O  O    . HOH   N 7 .   ? 13.709 5.376   44.761 1.00 32.02 ? 1040 HOH   B O    1 
HETATM 19980 O  O    . HOH   N 7 .   ? 5.958  30.295  58.642 1.00 16.35 ? 1041 HOH   B O    1 
HETATM 19981 O  O    . HOH   N 7 .   ? 48.833 15.497  75.203 1.00 31.70 ? 1042 HOH   B O    1 
HETATM 19982 O  O    . HOH   N 7 .   ? 8.414  41.766  77.539 1.00 29.64 ? 1043 HOH   B O    1 
HETATM 19983 O  O    . HOH   N 7 .   ? 40.283 15.921  82.591 1.00 29.27 ? 1044 HOH   B O    1 
HETATM 19984 O  O    . HOH   N 7 .   ? 25.427 20.928  83.078 1.00 15.21 ? 1045 HOH   B O    1 
HETATM 19985 O  O    . HOH   N 7 .   ? 36.418 -1.697  66.336 1.00 26.77 ? 1046 HOH   B O    1 
HETATM 19986 O  O    . HOH   N 7 .   ? 29.407 -1.199  52.738 1.00 26.94 ? 1047 HOH   B O    1 
HETATM 19987 O  O    . HOH   N 7 .   ? 24.291 -7.662  67.987 1.00 26.97 ? 1048 HOH   B O    1 
HETATM 19988 O  O    . HOH   N 7 .   ? 2.701  11.942  87.979 1.00 36.60 ? 1049 HOH   B O    1 
HETATM 19989 O  O    . HOH   N 7 .   ? 6.573  20.101  45.934 1.00 33.13 ? 1050 HOH   B O    1 
HETATM 19990 O  O    . HOH   N 7 .   ? 26.401 -1.642  93.596 1.00 28.95 ? 1051 HOH   B O    1 
HETATM 19991 O  O    . HOH   N 7 .   ? 11.812 -8.444  60.520 1.00 35.61 ? 1052 HOH   B O    1 
HETATM 19992 O  O    . HOH   N 7 .   ? 14.936 17.584  46.927 1.00 22.75 ? 1053 HOH   B O    1 
HETATM 19993 O  O    . HOH   N 7 .   ? -1.314 12.537  75.210 1.00 22.03 ? 1054 HOH   B O    1 
HETATM 19994 O  O    . HOH   N 7 .   ? 44.731 3.150   56.018 1.00 30.53 ? 1055 HOH   B O    1 
HETATM 19995 O  O    . HOH   N 7 .   ? 21.684 12.118  83.902 1.00 23.90 ? 1056 HOH   B O    1 
HETATM 19996 O  O    . HOH   N 7 .   ? 30.707 14.031  44.876 1.00 34.37 ? 1057 HOH   B O    1 
HETATM 19997 O  O    . HOH   N 7 .   ? 1.615  7.549   49.011 1.00 33.53 ? 1058 HOH   B O    1 
HETATM 19998 O  O    . HOH   N 7 .   ? 17.493 5.007   92.512 1.00 29.62 ? 1059 HOH   B O    1 
HETATM 19999 O  O    . HOH   N 7 .   ? 26.153 24.714  49.853 1.00 23.29 ? 1060 HOH   B O    1 
HETATM 20000 O  O    . HOH   N 7 .   ? 47.439 5.929   54.394 1.00 28.81 ? 1061 HOH   B O    1 
HETATM 20001 O  O    . HOH   N 7 .   ? 33.567 16.548  84.433 1.00 33.27 ? 1062 HOH   B O    1 
HETATM 20002 O  O    . HOH   N 7 .   ? 2.805  39.152  74.699 1.00 26.26 ? 1063 HOH   B O    1 
HETATM 20003 O  O    . HOH   N 7 .   ? 50.533 21.502  54.489 1.00 21.36 ? 1064 HOH   B O    1 
HETATM 20004 O  O    . HOH   N 7 .   ? 12.122 20.992  88.486 1.00 30.78 ? 1065 HOH   B O    1 
HETATM 20005 O  O    . HOH   N 7 .   ? 16.883 6.572   47.294 1.00 27.82 ? 1066 HOH   B O    1 
HETATM 20006 O  O    . HOH   N 7 .   ? 22.189 51.715  68.747 1.00 37.00 ? 1067 HOH   B O    1 
HETATM 20007 O  O    . HOH   N 7 .   ? 34.642 10.311  44.410 1.00 24.71 ? 1068 HOH   B O    1 
HETATM 20008 O  O    . HOH   N 7 .   ? 8.911  40.137  81.461 1.00 32.53 ? 1069 HOH   B O    1 
HETATM 20009 O  O    . HOH   N 7 .   ? 20.921 11.213  89.558 1.00 28.77 ? 1070 HOH   B O    1 
HETATM 20010 O  O    . HOH   N 7 .   ? 16.938 -4.720  70.487 1.00 23.04 ? 1071 HOH   B O    1 
HETATM 20011 O  O    . HOH   N 7 .   ? 24.757 16.987  88.660 1.00 29.12 ? 1072 HOH   B O    1 
HETATM 20012 O  O    . HOH   N 7 .   ? -1.177 23.309  65.961 1.00 31.52 ? 1073 HOH   B O    1 
HETATM 20013 O  O    . HOH   N 7 .   ? 32.718 20.038  51.243 1.00 17.59 ? 1074 HOH   B O    1 
HETATM 20014 O  O    . HOH   N 7 .   ? 2.162  26.911  48.641 1.00 28.15 ? 1075 HOH   B O    1 
HETATM 20015 O  O    . HOH   N 7 .   ? 50.511 8.881   73.018 1.00 35.94 ? 1076 HOH   B O    1 
HETATM 20016 O  O    . HOH   N 7 .   ? 40.734 14.245  50.411 1.00 12.45 ? 1077 HOH   B O    1 
HETATM 20017 O  O    . HOH   N 7 .   ? 23.077 17.674  45.781 1.00 26.95 ? 1078 HOH   B O    1 
HETATM 20018 O  O    . HOH   N 7 .   ? -0.333 31.014  58.359 1.00 35.55 ? 1079 HOH   B O    1 
HETATM 20019 O  O    . HOH   N 7 .   ? 9.327  41.825  69.912 1.00 16.56 ? 1080 HOH   B O    1 
HETATM 20020 O  O    . HOH   N 7 .   ? 33.108 22.960  54.639 1.00 11.31 ? 1081 HOH   B O    1 
HETATM 20021 O  O    . HOH   N 7 .   ? 45.212 26.374  49.034 1.00 18.42 ? 1082 HOH   B O    1 
HETATM 20022 O  O    . HOH   N 7 .   ? 10.435 31.071  45.460 1.00 30.44 ? 1083 HOH   B O    1 
HETATM 20023 O  O    . HOH   N 7 .   ? 26.551 45.537  62.524 1.00 26.55 ? 1084 HOH   B O    1 
HETATM 20024 O  O    . HOH   N 7 .   ? 14.591 14.362  88.837 1.00 23.21 ? 1085 HOH   B O    1 
HETATM 20025 O  O    . HOH   N 7 .   ? -5.487 19.677  69.326 1.00 32.76 ? 1086 HOH   B O    1 
HETATM 20026 O  O    . HOH   N 7 .   ? 47.232 26.326  68.093 1.00 30.85 ? 1087 HOH   B O    1 
HETATM 20027 O  O    . HOH   N 7 .   ? 43.962 8.701   44.943 1.00 35.20 ? 1088 HOH   B O    1 
HETATM 20028 O  O    . HOH   N 7 .   ? 19.328 25.358  54.910 1.00 13.50 ? 1089 HOH   B O    1 
HETATM 20029 O  O    . HOH   N 7 .   ? 19.063 10.955  91.388 1.00 32.25 ? 1090 HOH   B O    1 
HETATM 20030 O  O    . HOH   N 7 .   ? 25.331 30.135  43.568 1.00 27.47 ? 1091 HOH   B O    1 
HETATM 20031 O  O    . HOH   N 7 .   ? 10.759 45.157  76.391 1.00 30.87 ? 1092 HOH   B O    1 
HETATM 20032 O  O    . HOH   N 7 .   ? 5.410  32.823  49.489 1.00 20.70 ? 1093 HOH   B O    1 
HETATM 20033 O  O    . HOH   N 7 .   ? 45.164 -0.849  66.125 1.00 24.92 ? 1094 HOH   B O    1 
HETATM 20034 O  O    . HOH   N 7 .   ? 12.071 -6.634  57.182 1.00 32.90 ? 1095 HOH   B O    1 
HETATM 20035 O  O    . HOH   N 7 .   ? 22.222 20.560  52.130 1.00 14.73 ? 1096 HOH   B O    1 
HETATM 20036 O  O    . HOH   N 7 .   ? 28.996 10.800  46.625 1.00 32.79 ? 1097 HOH   B O    1 
HETATM 20037 O  O    . HOH   N 7 .   ? 35.721 -0.872  53.932 1.00 21.97 ? 1098 HOH   B O    1 
HETATM 20038 O  O    . HOH   N 7 .   ? 45.642 -1.148  63.467 1.00 23.74 ? 1099 HOH   B O    1 
HETATM 20039 O  O    . HOH   N 7 .   ? 8.601  -5.733  62.132 1.00 27.75 ? 1100 HOH   B O    1 
HETATM 20040 O  O    . HOH   N 7 .   ? 6.111  8.369   62.466 1.00 35.97 ? 1101 HOH   B O    1 
HETATM 20041 O  O    . HOH   N 7 .   ? 41.652 6.360   45.101 1.00 37.46 ? 1102 HOH   B O    1 
HETATM 20042 O  O    . HOH   N 7 .   ? 5.782  -1.790  55.302 1.00 33.66 ? 1103 HOH   B O    1 
HETATM 20043 O  O    . HOH   N 7 .   ? 20.605 54.678  79.257 1.00 41.26 ? 1104 HOH   B O    1 
HETATM 20044 O  O    . HOH   N 7 .   ? 1.451  11.252  54.935 1.00 27.90 ? 1105 HOH   B O    1 
HETATM 20045 O  O    . HOH   N 7 .   ? 48.690 24.751  55.684 1.00 19.36 ? 1106 HOH   B O    1 
HETATM 20046 O  O    . HOH   N 7 .   ? -4.264 27.173  69.609 1.00 40.13 ? 1107 HOH   B O    1 
HETATM 20047 O  O    . HOH   N 7 .   ? -3.884 37.826  75.128 1.00 30.60 ? 1108 HOH   B O    1 
HETATM 20048 O  O    . HOH   N 7 .   ? 17.394 2.569   45.474 1.00 28.44 ? 1109 HOH   B O    1 
HETATM 20049 O  O    . HOH   N 7 .   ? 2.384  34.419  62.579 1.00 23.20 ? 1110 HOH   B O    1 
HETATM 20050 O  O    . HOH   N 7 .   ? 20.687 12.322  80.988 1.00 24.84 ? 1111 HOH   B O    1 
HETATM 20051 O  O    . HOH   N 7 .   ? 10.235 10.550  90.149 1.00 25.41 ? 1112 HOH   B O    1 
HETATM 20052 O  O    . HOH   N 7 .   ? 29.135 50.661  65.838 1.00 33.51 ? 1113 HOH   B O    1 
HETATM 20053 O  O    . HOH   N 7 .   ? 35.987 25.900  45.577 1.00 19.78 ? 1114 HOH   B O    1 
HETATM 20054 O  O    . HOH   N 7 .   ? 21.313 18.583  62.904 1.00 10.25 ? 1115 HOH   B O    1 
HETATM 20055 O  O    . HOH   N 7 .   ? 8.123  22.758  46.002 1.00 30.49 ? 1116 HOH   B O    1 
HETATM 20056 O  O    . HOH   N 7 .   ? 5.947  3.854   52.934 1.00 25.57 ? 1117 HOH   B O    1 
HETATM 20057 O  O    . HOH   N 7 .   ? 21.051 24.864  82.820 1.00 17.73 ? 1118 HOH   B O    1 
HETATM 20058 O  O    . HOH   N 7 .   ? 4.964  0.910   56.455 1.00 32.54 ? 1119 HOH   B O    1 
HETATM 20059 O  O    . HOH   N 7 .   ? 19.471 -0.666  44.932 1.00 36.31 ? 1120 HOH   B O    1 
HETATM 20060 O  O    . HOH   N 7 .   ? 16.505 46.852  60.377 1.00 24.61 ? 1121 HOH   B O    1 
HETATM 20061 O  O    . HOH   N 7 .   ? 25.034 49.478  66.434 1.00 21.43 ? 1122 HOH   B O    1 
HETATM 20062 O  O    . HOH   N 7 .   ? 9.093  37.667  82.902 1.00 35.47 ? 1123 HOH   B O    1 
HETATM 20063 O  O    . HOH   N 7 .   ? 32.604 1.775   50.778 1.00 23.59 ? 1124 HOH   B O    1 
HETATM 20064 O  O    . HOH   N 7 .   ? -1.318 16.425  60.233 1.00 33.55 ? 1125 HOH   B O    1 
HETATM 20065 O  O    . HOH   N 7 .   ? 46.414 5.827   65.730 1.00 21.90 ? 1126 HOH   B O    1 
HETATM 20066 O  O    . HOH   N 7 .   ? 29.429 21.711  82.655 1.00 26.78 ? 1127 HOH   B O    1 
HETATM 20067 O  O    . HOH   N 7 .   ? -1.150 35.324  81.975 1.00 27.25 ? 1128 HOH   B O    1 
HETATM 20068 O  O    . HOH   N 7 .   ? 0.488  19.874  59.954 1.00 36.25 ? 1129 HOH   B O    1 
HETATM 20069 O  O    . HOH   N 7 .   ? 17.206 11.126  79.889 1.00 16.37 ? 1130 HOH   B O    1 
HETATM 20070 O  O    . HOH   N 7 .   ? 42.239 10.944  73.195 1.00 17.15 ? 1131 HOH   B O    1 
HETATM 20071 O  O    . HOH   N 7 .   ? 18.176 -10.988 64.209 1.00 36.92 ? 1132 HOH   B O    1 
HETATM 20072 O  O    . HOH   N 7 .   ? -5.069 13.020  64.794 1.00 32.71 ? 1133 HOH   B O    1 
HETATM 20073 O  O    . HOH   N 7 .   ? 45.678 33.383  52.286 1.00 40.02 ? 1134 HOH   B O    1 
HETATM 20074 O  O    . HOH   N 7 .   ? 45.449 16.248  80.422 1.00 38.81 ? 1135 HOH   B O    1 
HETATM 20075 O  O    . HOH   N 7 .   ? 24.766 43.331  87.837 1.00 31.83 ? 1136 HOH   B O    1 
HETATM 20076 O  O    . HOH   N 7 .   ? 18.476 22.055  69.757 1.00 10.35 ? 1137 HOH   B O    1 
HETATM 20077 O  O    . HOH   N 7 .   ? 47.383 31.617  54.323 1.00 35.72 ? 1138 HOH   B O    1 
HETATM 20078 O  O    . HOH   N 7 .   ? 19.324 21.879  83.936 1.00 14.82 ? 1139 HOH   B O    1 
HETATM 20079 O  O    . HOH   N 7 .   ? 23.784 33.485  40.727 1.00 19.14 ? 1140 HOH   B O    1 
HETATM 20080 O  O    . HOH   N 7 .   ? 0.290  32.858  73.718 1.00 19.09 ? 1141 HOH   B O    1 
HETATM 20081 O  O    . HOH   N 7 .   ? 22.314 21.840  62.465 1.00 11.75 ? 1142 HOH   B O    1 
HETATM 20082 O  O    . HOH   N 7 .   ? 3.705  43.106  74.229 1.00 31.69 ? 1143 HOH   B O    1 
HETATM 20083 O  O    . HOH   N 7 .   ? 33.829 -0.883  66.538 1.00 20.46 ? 1144 HOH   B O    1 
HETATM 20084 O  O    . HOH   N 7 .   ? 31.041 40.193  61.300 1.00 27.22 ? 1145 HOH   B O    1 
HETATM 20085 O  O    . HOH   N 7 .   ? 23.623 0.302   87.671 1.00 32.78 ? 1146 HOH   B O    1 
HETATM 20086 O  O    . HOH   N 7 .   ? -0.506 25.195  82.556 1.00 21.49 ? 1147 HOH   B O    1 
HETATM 20087 O  O    . HOH   N 7 .   ? 3.671  27.170  88.968 1.00 31.21 ? 1148 HOH   B O    1 
HETATM 20088 O  O    . HOH   N 7 .   ? 50.614 11.346  58.024 1.00 20.19 ? 1149 HOH   B O    1 
HETATM 20089 O  O    . HOH   N 7 .   ? 29.860 19.928  49.051 1.00 17.95 ? 1150 HOH   B O    1 
HETATM 20090 O  O    . HOH   N 7 .   ? 31.982 47.176  67.279 1.00 34.76 ? 1151 HOH   B O    1 
HETATM 20091 O  O    . HOH   N 7 .   ? 25.560 17.584  71.241 1.00 12.16 ? 1152 HOH   B O    1 
HETATM 20092 O  O    . HOH   N 7 .   ? -0.695 27.294  63.809 1.00 32.86 ? 1153 HOH   B O    1 
HETATM 20093 O  O    . HOH   N 7 .   ? 12.177 41.879  57.294 1.00 16.54 ? 1154 HOH   B O    1 
HETATM 20094 O  O    . HOH   N 7 .   ? 29.740 26.519  84.394 1.00 27.01 ? 1155 HOH   B O    1 
HETATM 20095 O  O    . HOH   N 7 .   ? 9.900  5.462   88.672 1.00 18.37 ? 1156 HOH   B O    1 
HETATM 20096 O  O    . HOH   N 7 .   ? 23.314 51.801  82.502 1.00 28.29 ? 1157 HOH   B O    1 
HETATM 20097 O  O    . HOH   N 7 .   ? 4.909  -3.024  61.896 1.00 31.47 ? 1158 HOH   B O    1 
HETATM 20098 O  O    . HOH   N 7 .   ? 40.020 13.327  40.640 1.00 35.40 ? 1159 HOH   B O    1 
HETATM 20099 O  O    . HOH   N 7 .   ? 17.414 30.246  88.602 1.00 23.61 ? 1160 HOH   B O    1 
HETATM 20100 O  O    . HOH   N 7 .   ? 21.344 10.418  61.275 1.00 13.98 ? 1161 HOH   B O    1 
HETATM 20101 O  O    . HOH   N 7 .   ? 29.332 43.225  48.317 1.00 32.33 ? 1162 HOH   B O    1 
HETATM 20102 O  O    . HOH   N 7 .   ? 16.502 38.704  46.433 1.00 19.99 ? 1163 HOH   B O    1 
HETATM 20103 O  O    . HOH   N 7 .   ? 39.607 9.242   79.757 1.00 28.58 ? 1164 HOH   B O    1 
HETATM 20104 O  O    . HOH   N 7 .   ? 23.435 40.990  52.879 1.00 23.22 ? 1165 HOH   B O    1 
HETATM 20105 O  O    . HOH   N 7 .   ? 25.405 30.519  55.143 1.00 16.03 ? 1166 HOH   B O    1 
HETATM 20106 O  O    . HOH   N 7 .   ? 12.845 38.293  44.700 1.00 22.97 ? 1167 HOH   B O    1 
HETATM 20107 O  O    . HOH   N 7 .   ? 29.776 29.354  55.633 1.00 13.11 ? 1168 HOH   B O    1 
HETATM 20108 O  O    . HOH   N 7 .   ? 29.398 15.076  41.576 1.00 26.22 ? 1169 HOH   B O    1 
HETATM 20109 O  O    . HOH   N 7 .   ? 17.805 2.215   89.876 1.00 29.22 ? 1170 HOH   B O    1 
HETATM 20110 O  O    . HOH   N 7 .   ? 36.465 19.146  45.910 1.00 18.99 ? 1171 HOH   B O    1 
HETATM 20111 O  O    . HOH   N 7 .   ? 27.191 3.015   46.817 1.00 29.24 ? 1172 HOH   B O    1 
HETATM 20112 O  O    . HOH   N 7 .   ? 33.852 0.031   71.598 1.00 32.12 ? 1173 HOH   B O    1 
HETATM 20113 O  O    . HOH   N 7 .   ? 14.571 48.417  72.823 1.00 25.73 ? 1174 HOH   B O    1 
HETATM 20114 O  O    . HOH   N 7 .   ? 15.718 29.692  86.494 1.00 20.05 ? 1175 HOH   B O    1 
HETATM 20115 O  O    . HOH   N 7 .   ? 51.619 26.455  63.130 1.00 36.07 ? 1176 HOH   B O    1 
HETATM 20116 O  O    . HOH   N 7 .   ? -0.271 9.724   81.693 1.00 26.18 ? 1177 HOH   B O    1 
HETATM 20117 O  O    . HOH   N 7 .   ? 6.902  1.949   78.635 1.00 35.28 ? 1178 HOH   B O    1 
HETATM 20118 O  O    . HOH   N 7 .   ? -4.416 15.576  80.908 1.00 25.24 ? 1179 HOH   B O    1 
HETATM 20119 O  O    . HOH   N 7 .   ? 11.927 4.208   92.761 1.00 26.58 ? 1180 HOH   B O    1 
HETATM 20120 O  O    . HOH   N 7 .   ? 17.016 41.070  49.847 1.00 23.56 ? 1181 HOH   B O    1 
HETATM 20121 O  O    . HOH   N 7 .   ? 1.490  31.512  56.624 1.00 32.41 ? 1182 HOH   B O    1 
HETATM 20122 O  O    . HOH   N 7 .   ? 48.827 22.021  52.568 1.00 23.19 ? 1183 HOH   B O    1 
HETATM 20123 O  O    . HOH   N 7 .   ? 25.402 44.314  43.967 1.00 20.80 ? 1184 HOH   B O    1 
HETATM 20124 O  O    . HOH   N 7 .   ? 9.065  -10.437 64.028 1.00 33.75 ? 1185 HOH   B O    1 
HETATM 20125 O  O    . HOH   N 7 .   ? 45.599 28.772  52.546 1.00 24.57 ? 1186 HOH   B O    1 
HETATM 20126 O  O    . HOH   N 7 .   ? 4.120  15.193  91.370 1.00 34.23 ? 1187 HOH   B O    1 
HETATM 20127 O  O    . HOH   N 7 .   ? 8.081  41.048  47.693 1.00 33.30 ? 1188 HOH   B O    1 
HETATM 20128 O  O    . HOH   N 7 .   ? 8.602  -1.714  51.555 1.00 35.83 ? 1189 HOH   B O    1 
HETATM 20129 O  O    . HOH   N 7 .   ? 37.754 2.373   45.825 1.00 31.62 ? 1190 HOH   B O    1 
HETATM 20130 O  O    . HOH   N 7 .   ? 24.932 -8.276  58.235 1.00 33.76 ? 1191 HOH   B O    1 
HETATM 20131 O  O    . HOH   N 7 .   ? 1.221  8.205   44.396 1.00 40.56 ? 1192 HOH   B O    1 
HETATM 20132 O  O    . HOH   N 7 .   ? 44.265 33.088  58.600 1.00 28.95 ? 1193 HOH   B O    1 
HETATM 20133 O  O    . HOH   N 7 .   ? 43.279 31.811  64.796 1.00 30.65 ? 1194 HOH   B O    1 
HETATM 20134 O  O    . HOH   N 7 .   ? 21.260 42.777  56.470 1.00 31.69 ? 1195 HOH   B O    1 
HETATM 20135 O  O    . HOH   N 7 .   ? 42.459 16.354  41.648 1.00 30.82 ? 1196 HOH   B O    1 
HETATM 20136 O  O    . HOH   N 7 .   ? 9.903  15.786  89.269 1.00 29.53 ? 1197 HOH   B O    1 
HETATM 20137 O  O    . HOH   N 7 .   ? 22.601 50.537  65.776 1.00 24.49 ? 1198 HOH   B O    1 
HETATM 20138 O  O    . HOH   N 7 .   ? 6.828  35.376  80.760 1.00 17.83 ? 1199 HOH   B O    1 
HETATM 20139 O  O    . HOH   N 7 .   ? 39.339 34.987  58.790 1.00 27.99 ? 1200 HOH   B O    1 
HETATM 20140 O  O    . HOH   N 7 .   ? 14.166 27.386  56.512 1.00 10.22 ? 1201 HOH   B O    1 
HETATM 20141 O  O    . HOH   N 7 .   ? -2.408 31.359  85.155 1.00 31.63 ? 1202 HOH   B O    1 
HETATM 20142 O  O    . HOH   N 7 .   ? 45.680 11.566  75.982 1.00 30.12 ? 1203 HOH   B O    1 
HETATM 20143 O  O    . HOH   N 7 .   ? 24.954 27.259  43.291 1.00 17.93 ? 1204 HOH   B O    1 
HETATM 20144 O  O    . HOH   N 7 .   ? -2.504 23.087  68.421 1.00 27.80 ? 1205 HOH   B O    1 
HETATM 20145 O  O    . HOH   N 7 .   ? 33.449 -0.443  47.901 1.00 32.53 ? 1206 HOH   B O    1 
HETATM 20146 O  O    . HOH   N 7 .   ? 27.425 2.469   61.390 1.00 14.27 ? 1207 HOH   B O    1 
HETATM 20147 O  O    . HOH   N 7 .   ? 26.211 -5.091  78.470 1.00 28.18 ? 1208 HOH   B O    1 
HETATM 20148 O  O    . HOH   N 7 .   ? 18.195 49.473  80.872 1.00 34.51 ? 1209 HOH   B O    1 
HETATM 20149 O  O    . HOH   N 7 .   ? -3.821 21.250  71.121 1.00 30.92 ? 1210 HOH   B O    1 
HETATM 20150 O  O    . HOH   N 7 .   ? 15.838 -8.431  66.162 1.00 35.88 ? 1211 HOH   B O    1 
HETATM 20151 O  O    . HOH   N 7 .   ? 7.869  -4.948  73.020 1.00 38.79 ? 1212 HOH   B O    1 
HETATM 20152 O  O    . HOH   N 7 .   ? 27.041 33.796  44.671 1.00 20.86 ? 1213 HOH   B O    1 
HETATM 20153 O  O    . HOH   N 7 .   ? 42.356 22.636  75.605 1.00 26.43 ? 1214 HOH   B O    1 
HETATM 20154 O  O    . HOH   N 7 .   ? 46.629 0.163   59.876 1.00 18.52 ? 1215 HOH   B O    1 
HETATM 20155 O  O    . HOH   N 7 .   ? 23.811 51.460  75.859 1.00 26.94 ? 1216 HOH   B O    1 
HETATM 20156 O  O    . HOH   N 7 .   ? 38.862 -6.722  55.103 1.00 32.96 ? 1217 HOH   B O    1 
HETATM 20157 O  O    . HOH   N 7 .   ? 27.038 -1.685  46.114 1.00 32.67 ? 1218 HOH   B O    1 
HETATM 20158 O  O    . HOH   N 7 .   ? 22.367 43.860  44.542 1.00 24.55 ? 1219 HOH   B O    1 
HETATM 20159 O  O    . HOH   N 7 .   ? 33.357 49.814  77.664 1.00 30.94 ? 1220 HOH   B O    1 
HETATM 20160 O  O    . HOH   N 7 .   ? 32.456 -8.359  63.862 1.00 28.94 ? 1221 HOH   B O    1 
HETATM 20161 O  O    . HOH   N 7 .   ? 35.734 -3.681  54.997 1.00 32.84 ? 1222 HOH   B O    1 
HETATM 20162 O  O    . HOH   N 7 .   ? 24.062 9.204   44.077 1.00 31.08 ? 1223 HOH   B O    1 
HETATM 20163 O  O    . HOH   N 7 .   ? 37.347 10.510  40.674 1.00 28.95 ? 1224 HOH   B O    1 
HETATM 20164 O  O    . HOH   N 7 .   ? 31.886 -2.209  49.008 1.00 27.94 ? 1225 HOH   B O    1 
HETATM 20165 O  O    . HOH   N 7 .   ? 31.065 -8.965  65.777 1.00 30.39 ? 1226 HOH   B O    1 
HETATM 20166 O  O    . HOH   N 7 .   ? 7.488  38.191  45.111 1.00 28.16 ? 1227 HOH   B O    1 
HETATM 20167 O  O    . HOH   N 7 .   ? 53.298 15.627  68.854 1.00 32.84 ? 1228 HOH   B O    1 
HETATM 20168 O  O    . HOH   N 7 .   ? 17.217 30.076  75.057 1.00 12.52 ? 1229 HOH   B O    1 
HETATM 20169 O  O    . HOH   N 7 .   ? 12.460 44.976  83.391 1.00 22.51 ? 1230 HOH   B O    1 
HETATM 20170 O  O    . HOH   N 7 .   ? 38.141 14.413  39.139 1.00 37.47 ? 1231 HOH   B O    1 
HETATM 20171 O  O    . HOH   N 7 .   ? 52.615 18.775  56.061 1.00 24.93 ? 1232 HOH   B O    1 
HETATM 20172 O  O    . HOH   N 7 .   ? 50.457 9.324   59.896 1.00 31.61 ? 1233 HOH   B O    1 
HETATM 20173 O  O    . HOH   N 7 .   ? 21.291 39.671  53.524 1.00 22.82 ? 1234 HOH   B O    1 
HETATM 20174 O  O    . HOH   N 7 .   ? 25.008 24.677  47.200 1.00 17.08 ? 1235 HOH   B O    1 
HETATM 20175 O  O    . HOH   N 7 .   ? 52.778 19.784  60.925 1.00 27.38 ? 1236 HOH   B O    1 
HETATM 20176 O  O    . HOH   N 7 .   ? 3.163  41.410  69.294 1.00 27.70 ? 1237 HOH   B O    1 
HETATM 20177 O  O    . HOH   N 7 .   ? 18.533 39.719  48.099 1.00 22.32 ? 1238 HOH   B O    1 
HETATM 20178 O  O    . HOH   N 7 .   ? 18.721 15.007  46.313 1.00 26.38 ? 1239 HOH   B O    1 
HETATM 20179 O  O    . HOH   N 7 .   ? 44.294 33.868  56.367 1.00 28.95 ? 1240 HOH   B O    1 
HETATM 20180 O  O    . HOH   N 7 .   ? -5.587 31.221  77.008 1.00 38.00 ? 1241 HOH   B O    1 
HETATM 20181 O  O    . HOH   N 7 .   ? 17.792 -1.782  90.431 1.00 18.92 ? 1242 HOH   B O    1 
HETATM 20182 O  O    . HOH   N 7 .   ? 3.833  4.532   49.032 1.00 39.40 ? 1243 HOH   B O    1 
HETATM 20183 O  O    . HOH   N 7 .   ? 39.723 -8.128  57.915 1.00 21.10 ? 1244 HOH   B O    1 
HETATM 20184 O  O    . HOH   N 7 .   ? 10.282 27.316  46.842 1.00 25.77 ? 1245 HOH   B O    1 
HETATM 20185 O  O    . HOH   N 7 .   ? 16.803 -8.132  52.834 1.00 33.33 ? 1246 HOH   B O    1 
HETATM 20186 O  O    . HOH   N 7 .   ? 5.977  11.865  63.901 1.00 26.52 ? 1247 HOH   B O    1 
HETATM 20187 O  O    . HOH   N 7 .   ? 13.454 47.270  65.523 1.00 31.73 ? 1248 HOH   B O    1 
HETATM 20188 O  O    . HOH   N 7 .   ? 27.232 -4.500  74.596 1.00 24.41 ? 1249 HOH   B O    1 
HETATM 20189 O  O    . HOH   N 7 .   ? 25.235 41.627  50.852 1.00 25.71 ? 1250 HOH   B O    1 
HETATM 20190 O  O    . HOH   N 7 .   ? 13.729 21.058  41.980 1.00 27.00 ? 1251 HOH   B O    1 
HETATM 20191 O  O    . HOH   N 7 .   ? 22.619 -11.377 50.781 1.00 38.42 ? 1252 HOH   B O    1 
HETATM 20192 O  O    . HOH   N 7 .   ? 36.344 31.000  75.500 1.00 32.55 ? 1253 HOH   B O    1 
HETATM 20193 O  O    . HOH   N 7 .   ? 37.237 -0.247  75.020 1.00 32.03 ? 1254 HOH   B O    1 
HETATM 20194 O  O    . HOH   N 7 .   ? 50.752 5.805   61.202 1.00 26.26 ? 1255 HOH   B O    1 
HETATM 20195 O  O    . HOH   N 7 .   ? 6.677  4.561   64.631 1.00 25.00 ? 1256 HOH   B O    1 
HETATM 20196 O  O    . HOH   N 7 .   ? 33.693 -7.200  54.852 1.00 33.89 ? 1257 HOH   B O    1 
HETATM 20197 O  O    . HOH   N 7 .   ? 12.973 30.496  44.605 1.00 27.78 ? 1258 HOH   B O    1 
HETATM 20198 O  O    . HOH   N 7 .   ? 28.181 42.443  59.121 1.00 32.51 ? 1259 HOH   B O    1 
HETATM 20199 O  O    . HOH   N 7 .   ? 10.067 42.812  86.373 1.00 28.66 ? 1260 HOH   B O    1 
HETATM 20200 O  O    . HOH   N 7 .   ? 25.753 51.837  68.410 1.00 39.59 ? 1261 HOH   B O    1 
HETATM 20201 O  O    . HOH   N 7 .   ? 11.919 38.472  86.957 1.00 29.95 ? 1262 HOH   B O    1 
HETATM 20202 O  O    . HOH   N 7 .   ? 2.147  9.237   79.949 1.00 15.90 ? 1263 HOH   B O    1 
HETATM 20203 O  O    . HOH   N 7 .   ? 19.398 -10.512 52.998 1.00 32.01 ? 1264 HOH   B O    1 
HETATM 20204 O  O    . HOH   N 7 .   ? 5.225  1.716   61.197 1.00 27.05 ? 1265 HOH   B O    1 
HETATM 20205 O  O    . HOH   N 7 .   ? 26.456 -6.230  57.837 1.00 28.14 ? 1266 HOH   B O    1 
HETATM 20206 O  O    . HOH   N 7 .   ? 6.791  22.020  87.899 1.00 28.34 ? 1267 HOH   B O    1 
HETATM 20207 O  O    . HOH   N 7 .   ? 44.043 22.915  73.458 1.00 25.54 ? 1268 HOH   B O    1 
HETATM 20208 O  O    . HOH   N 7 .   ? 30.702 35.920  81.537 1.00 26.45 ? 1269 HOH   B O    1 
HETATM 20209 O  O    . HOH   N 7 .   ? 47.100 31.798  61.970 1.00 35.94 ? 1270 HOH   B O    1 
HETATM 20210 O  O    . HOH   N 7 .   ? 10.414 21.883  45.022 1.00 35.42 ? 1271 HOH   B O    1 
HETATM 20211 O  O    . HOH   N 7 .   ? 14.557 42.121  55.149 1.00 18.41 ? 1272 HOH   B O    1 
HETATM 20212 O  O    . HOH   N 7 .   ? 2.620  37.338  62.288 1.00 26.91 ? 1273 HOH   B O    1 
HETATM 20213 O  O    . HOH   N 7 .   ? 33.461 28.047  49.856 1.00 26.59 ? 1274 HOH   B O    1 
HETATM 20214 O  O    . HOH   N 7 .   ? 25.366 35.165  42.628 1.00 16.65 ? 1275 HOH   B O    1 
HETATM 20215 O  O    . HOH   N 7 .   ? 52.032 26.694  66.007 1.00 32.33 ? 1276 HOH   B O    1 
HETATM 20216 O  O    . HOH   N 7 .   ? 21.727 -2.278  88.386 1.00 26.70 ? 1277 HOH   B O    1 
HETATM 20217 O  O    . HOH   N 7 .   ? -0.884 12.996  59.984 1.00 36.64 ? 1278 HOH   B O    1 
HETATM 20218 O  O    . HOH   N 7 .   ? 42.388 -4.220  57.595 1.00 24.79 ? 1279 HOH   B O    1 
HETATM 20219 O  O    . HOH   N 7 .   ? 9.009  40.041  84.844 1.00 36.48 ? 1280 HOH   B O    1 
HETATM 20220 O  O    . HOH   N 7 .   ? -7.455 14.022  83.737 1.00 39.10 ? 1281 HOH   B O    1 
HETATM 20221 O  O    . HOH   N 7 .   ? 17.070 -12.131 84.393 1.00 27.60 ? 1282 HOH   B O    1 
HETATM 20222 O  O    . HOH   N 7 .   ? -2.872 9.114   72.097 1.00 36.50 ? 1283 HOH   B O    1 
HETATM 20223 O  O    . HOH   N 7 .   ? 36.399 1.180   68.747 1.00 23.74 ? 1284 HOH   B O    1 
HETATM 20224 O  O    . HOH   N 7 .   ? 48.004 14.986  77.862 1.00 36.29 ? 1285 HOH   B O    1 
HETATM 20225 O  O    . HOH   N 7 .   ? 0.223  16.457  49.587 1.00 37.84 ? 1286 HOH   B O    1 
HETATM 20226 O  O    . HOH   N 7 .   ? 39.115 43.450  73.786 1.00 33.67 ? 1287 HOH   B O    1 
HETATM 20227 O  O    . HOH   N 7 .   ? 11.218 25.103  46.153 1.00 30.72 ? 1288 HOH   B O    1 
HETATM 20228 O  O    . HOH   N 7 .   ? 14.621 34.716  43.358 1.00 18.67 ? 1289 HOH   B O    1 
HETATM 20229 O  O    . HOH   N 7 .   ? 6.705  39.705  50.916 1.00 25.83 ? 1290 HOH   B O    1 
HETATM 20230 O  O    . HOH   N 7 .   ? 37.626 35.653  48.762 1.00 29.95 ? 1291 HOH   B O    1 
HETATM 20231 O  O    . HOH   N 7 .   ? 12.913 44.887  62.714 1.00 17.63 ? 1292 HOH   B O    1 
HETATM 20232 O  O    . HOH   N 7 .   ? 31.706 31.842  46.933 1.00 34.50 ? 1293 HOH   B O    1 
HETATM 20233 O  O    . HOH   N 7 .   ? 1.328  24.491  88.073 1.00 48.04 ? 1294 HOH   B O    1 
HETATM 20234 O  O    . HOH   N 7 .   ? 16.727 49.732  83.173 1.00 33.32 ? 1295 HOH   B O    1 
HETATM 20235 O  O    . HOH   N 7 .   ? 33.898 44.342  65.938 1.00 39.27 ? 1296 HOH   B O    1 
HETATM 20236 O  O    . HOH   N 7 .   ? 7.273  9.363   44.119 1.00 36.71 ? 1297 HOH   B O    1 
HETATM 20237 O  O    A HOH   N 7 .   ? 1.348  24.525  88.044 0.52 48.04 ? 1298 HOH   B O    1 
HETATM 20238 O  O    . HOH   N 7 .   ? 39.114 34.102  56.263 1.00 13.11 ? 1299 HOH   B O    1 
HETATM 20239 O  O    . HOH   N 7 .   ? 33.185 31.085  80.902 1.00 31.38 ? 1300 HOH   B O    1 
HETATM 20240 O  O    . HOH   N 7 .   ? 15.001 24.267  61.786 1.00 12.09 ? 1301 HOH   B O    1 
HETATM 20241 O  O    . HOH   N 7 .   ? 27.232 20.011  85.165 1.00 30.90 ? 1302 HOH   B O    1 
HETATM 20242 O  O    . HOH   N 7 .   ? -3.669 14.345  74.201 1.00 17.51 ? 1303 HOH   B O    1 
HETATM 20243 O  O    . HOH   N 7 .   ? 45.544 7.973   73.154 1.00 34.62 ? 1304 HOH   B O    1 
HETATM 20244 O  O    . HOH   N 7 .   ? 40.827 34.142  54.214 1.00 35.30 ? 1305 HOH   B O    1 
HETATM 20245 O  O    . HOH   N 7 .   ? 41.146 -3.106  55.197 1.00 37.66 ? 1306 HOH   B O    1 
HETATM 20246 O  O    . HOH   N 7 .   ? 21.340 7.495   46.638 1.00 28.93 ? 1307 HOH   B O    1 
HETATM 20247 O  O    . HOH   N 7 .   ? 33.064 2.026   80.489 1.00 31.15 ? 1308 HOH   B O    1 
HETATM 20248 O  O    . HOH   N 7 .   ? 47.959 -0.478  67.150 1.00 35.02 ? 1309 HOH   B O    1 
HETATM 20249 O  O    . HOH   N 7 .   ? 40.264 -2.008  69.168 1.00 38.04 ? 1310 HOH   B O    1 
HETATM 20250 O  O    . HOH   N 7 .   ? -0.546 12.888  84.049 1.00 31.53 ? 1311 HOH   B O    1 
HETATM 20251 O  O    . HOH   N 7 .   ? 49.458 25.402  69.203 1.00 32.53 ? 1312 HOH   B O    1 
HETATM 20252 O  O    . HOH   N 7 .   ? 34.506 18.514  38.330 1.00 33.82 ? 1313 HOH   B O    1 
HETATM 20253 O  O    . HOH   N 7 .   ? 29.639 32.355  52.749 1.00 24.98 ? 1314 HOH   B O    1 
HETATM 20254 O  O    . HOH   N 7 .   ? 12.530 33.427  87.191 1.00 29.31 ? 1315 HOH   B O    1 
HETATM 20255 O  O    . HOH   N 7 .   ? 27.751 20.092  47.386 1.00 32.30 ? 1316 HOH   B O    1 
HETATM 20256 O  O    . HOH   N 7 .   ? 34.265 23.689  79.380 1.00 35.04 ? 1317 HOH   B O    1 
HETATM 20257 O  O    . HOH   N 7 .   ? 39.109 1.105   55.104 1.00 26.41 ? 1318 HOH   B O    1 
HETATM 20258 O  O    . HOH   N 7 .   ? 21.746 -3.829  90.889 1.00 31.53 ? 1319 HOH   B O    1 
HETATM 20259 O  O    . HOH   N 7 .   ? -1.482 24.700  63.940 1.00 41.20 ? 1320 HOH   B O    1 
HETATM 20260 O  O    . HOH   N 7 .   ? 32.304 17.530  44.944 1.00 20.54 ? 1321 HOH   B O    1 
HETATM 20261 O  O    . HOH   N 7 .   ? 12.113 40.529  53.486 1.00 18.70 ? 1322 HOH   B O    1 
HETATM 20262 O  O    . HOH   N 7 .   ? 15.758 -4.177  89.529 1.00 24.96 ? 1323 HOH   B O    1 
HETATM 20263 O  O    . HOH   N 7 .   ? 14.494 39.743  48.267 1.00 29.76 ? 1324 HOH   B O    1 
HETATM 20264 O  O    . HOH   N 7 .   ? 16.112 14.195  44.647 1.00 34.40 ? 1325 HOH   B O    1 
HETATM 20265 O  O    . HOH   N 7 .   ? 42.279 19.273  82.491 1.00 39.13 ? 1326 HOH   B O    1 
HETATM 20266 O  O    . HOH   N 7 .   ? 7.271  -6.358  65.620 1.00 34.62 ? 1327 HOH   B O    1 
HETATM 20267 O  O    . HOH   N 7 .   ? 39.228 1.791   50.145 1.00 31.05 ? 1328 HOH   B O    1 
HETATM 20268 O  O    . HOH   N 7 .   ? 26.395 53.610  83.035 1.00 28.19 ? 1329 HOH   B O    1 
HETATM 20269 O  O    . HOH   N 7 .   ? 29.328 41.425  86.644 1.00 30.06 ? 1330 HOH   B O    1 
HETATM 20270 O  O    . HOH   N 7 .   ? 3.271  9.651   59.389 1.00 31.78 ? 1331 HOH   B O    1 
HETATM 20271 O  O    . HOH   N 7 .   ? 31.255 33.306  80.382 1.00 24.64 ? 1332 HOH   B O    1 
HETATM 20272 O  O    . HOH   N 7 .   ? 9.519  -7.036  59.585 1.00 30.01 ? 1333 HOH   B O    1 
HETATM 20273 O  O    . HOH   N 7 .   ? 9.283  -2.777  48.993 1.00 35.63 ? 1334 HOH   B O    1 
HETATM 20274 O  O    . HOH   N 7 .   ? 38.331 12.934  86.110 1.00 34.00 ? 1335 HOH   B O    1 
HETATM 20275 O  O    . HOH   N 7 .   ? 50.456 13.677  48.704 1.00 40.44 ? 1336 HOH   B O    1 
HETATM 20276 O  O    . HOH   N 7 .   ? 22.902 23.063  85.122 1.00 30.83 ? 1337 HOH   B O    1 
HETATM 20277 O  O    . HOH   N 7 .   ? 14.195 37.430  42.359 1.00 21.37 ? 1338 HOH   B O    1 
HETATM 20278 O  O    . HOH   N 7 .   ? 2.186  12.143  84.042 1.00 30.90 ? 1339 HOH   B O    1 
HETATM 20279 O  O    . HOH   N 7 .   ? -4.804 24.574  69.886 1.00 41.56 ? 1340 HOH   B O    1 
HETATM 20280 O  O    . HOH   N 7 .   ? 40.693 20.735  41.939 1.00 24.78 ? 1341 HOH   B O    1 
HETATM 20281 O  O    . HOH   N 7 .   ? 7.919  3.527   74.089 1.00 35.28 ? 1342 HOH   B O    1 
HETATM 20282 O  O    . HOH   N 7 .   ? 35.203 1.104   49.727 1.00 26.46 ? 1343 HOH   B O    1 
HETATM 20283 O  O    . HOH   N 7 .   ? 7.693  -1.376  70.595 1.00 33.79 ? 1344 HOH   B O    1 
HETATM 20284 O  O    . HOH   N 7 .   ? -5.013 28.529  77.325 1.00 37.21 ? 1345 HOH   B O    1 
HETATM 20285 O  O    . HOH   N 7 .   ? 11.966 42.264  51.655 1.00 34.15 ? 1346 HOH   B O    1 
HETATM 20286 O  O    . HOH   N 7 .   ? 45.222 20.892  75.877 1.00 25.93 ? 1347 HOH   B O    1 
HETATM 20287 O  O    . HOH   N 7 .   ? 33.735 -0.513  52.106 1.00 23.49 ? 1348 HOH   B O    1 
HETATM 20288 O  O    . HOH   N 7 .   ? 53.701 27.798  61.139 1.00 43.45 ? 1349 HOH   B O    1 
HETATM 20289 O  O    . HOH   N 7 .   ? 17.983 5.956   45.074 1.00 36.16 ? 1350 HOH   B O    1 
HETATM 20290 O  O    . HOH   N 7 .   ? 31.630 -2.506  51.694 1.00 30.51 ? 1351 HOH   B O    1 
HETATM 20291 O  O    . HOH   N 7 .   ? 16.376 13.872  91.001 1.00 31.62 ? 1352 HOH   B O    1 
HETATM 20292 O  O    . HOH   N 7 .   ? 15.474 11.155  46.118 1.00 33.49 ? 1353 HOH   B O    1 
HETATM 20293 O  O    . HOH   N 7 .   ? 2.380  6.710   73.668 1.00 27.17 ? 1354 HOH   B O    1 
HETATM 20294 O  O    . HOH   N 7 .   ? 14.517 -7.551  53.959 1.00 21.15 ? 1355 HOH   B O    1 
HETATM 20295 O  O    . HOH   N 7 .   ? 27.598 -6.605  71.163 1.00 37.74 ? 1356 HOH   B O    1 
HETATM 20296 O  O    . HOH   N 7 .   ? 2.701  24.124  52.237 1.00 28.89 ? 1357 HOH   B O    1 
HETATM 20297 O  O    . HOH   N 7 .   ? 34.328 53.470  77.279 1.00 30.29 ? 1358 HOH   B O    1 
HETATM 20298 O  O    . HOH   N 7 .   ? 30.543 22.534  49.582 1.00 23.06 ? 1359 HOH   B O    1 
HETATM 20299 O  O    . HOH   N 7 .   ? 28.486 55.151  79.249 1.00 32.23 ? 1360 HOH   B O    1 
HETATM 20300 O  O    . HOH   N 7 .   ? 4.575  3.262   63.441 1.00 33.36 ? 1361 HOH   B O    1 
HETATM 20301 O  O    . HOH   N 7 .   ? 27.109 41.665  88.707 1.00 30.37 ? 1362 HOH   B O    1 
HETATM 20302 O  O    . HOH   N 7 .   ? 33.285 54.821  75.078 1.00 31.02 ? 1363 HOH   B O    1 
HETATM 20303 O  O    . HOH   N 7 .   ? 7.031  42.069  71.229 1.00 25.52 ? 1364 HOH   B O    1 
HETATM 20304 O  O    . HOH   N 7 .   ? -6.700 33.226  79.072 1.00 28.95 ? 1365 HOH   B O    1 
HETATM 20305 O  O    . HOH   N 7 .   ? 32.360 38.306  85.203 1.00 35.50 ? 1366 HOH   B O    1 
HETATM 20306 O  O    . HOH   N 7 .   ? 42.410 -7.096  56.989 1.00 14.75 ? 1367 HOH   B O    1 
HETATM 20307 O  O    . HOH   N 7 .   ? 34.558 19.725  44.255 1.00 24.81 ? 1368 HOH   B O    1 
HETATM 20308 O  O    . HOH   N 7 .   ? 49.262 15.551  47.321 1.00 39.54 ? 1369 HOH   B O    1 
HETATM 20309 O  O    . HOH   N 7 .   ? -1.701 39.022  72.048 1.00 41.70 ? 1370 HOH   B O    1 
HETATM 20310 O  O    . HOH   N 7 .   ? 12.579 46.922  77.151 1.00 32.94 ? 1371 HOH   B O    1 
HETATM 20311 O  O    . HOH   N 7 .   ? 24.570 45.703  48.473 1.00 31.85 ? 1372 HOH   B O    1 
HETATM 20312 O  O    . HOH   N 7 .   ? 6.421  32.963  46.587 1.00 26.47 ? 1373 HOH   B O    1 
HETATM 20313 O  O    . HOH   N 7 .   ? -6.484 14.652  78.853 1.00 32.34 ? 1374 HOH   B O    1 
HETATM 20314 O  O    . HOH   N 7 .   ? -2.581 7.557   79.032 1.00 35.14 ? 1375 HOH   B O    1 
HETATM 20315 O  O    . HOH   N 7 .   ? 10.587 -0.119  73.245 1.00 30.04 ? 1376 HOH   B O    1 
HETATM 20316 O  O    . HOH   N 7 .   ? 28.627 24.485  48.971 1.00 27.85 ? 1377 HOH   B O    1 
HETATM 20317 O  O    . HOH   N 7 .   ? 0.354  41.233  70.325 1.00 36.61 ? 1378 HOH   B O    1 
HETATM 20318 O  O    . HOH   N 7 .   ? 28.250 14.063  46.397 1.00 30.96 ? 1379 HOH   B O    1 
HETATM 20319 O  O    . HOH   N 7 .   ? 35.476 35.680  52.961 1.00 38.17 ? 1380 HOH   B O    1 
HETATM 20320 O  O    . HOH   N 7 .   ? 43.920 31.333  67.583 1.00 32.85 ? 1381 HOH   B O    1 
HETATM 20321 O  O    . HOH   N 7 .   ? -1.510 9.884   74.453 1.00 24.09 ? 1382 HOH   B O    1 
HETATM 20322 O  O    . HOH   N 7 .   ? 35.839 47.669  74.608 1.00 33.18 ? 1383 HOH   B O    1 
HETATM 20323 O  O    . HOH   N 7 .   ? 7.116  45.051  71.252 1.00 40.22 ? 1384 HOH   B O    1 
HETATM 20324 O  O    . HOH   N 7 .   ? 25.632 -8.626  70.353 1.00 35.60 ? 1385 HOH   B O    1 
HETATM 20325 O  O    . HOH   N 7 .   ? 0.804  28.808  58.989 1.00 26.98 ? 1386 HOH   B O    1 
HETATM 20326 O  O    . HOH   N 7 .   ? 25.364 44.435  50.778 1.00 33.10 ? 1387 HOH   B O    1 
HETATM 20327 O  O    . HOH   N 7 .   ? 19.431 6.197   93.643 1.00 38.83 ? 1388 HOH   B O    1 
HETATM 20328 O  O    . HOH   N 7 .   ? 24.659 52.323  72.127 1.00 41.11 ? 1389 HOH   B O    1 
HETATM 20329 O  O    . HOH   N 7 .   ? 15.716 47.384  76.462 1.00 23.88 ? 1390 HOH   B O    1 
HETATM 20330 O  O    . HOH   N 7 .   ? 12.181 14.244  90.088 1.00 32.17 ? 1391 HOH   B O    1 
HETATM 20331 O  O    . HOH   N 7 .   ? 30.559 41.184  58.716 1.00 30.52 ? 1392 HOH   B O    1 
HETATM 20332 O  O    . HOH   N 7 .   ? -3.654 9.366   76.442 1.00 36.65 ? 1393 HOH   B O    1 
HETATM 20333 O  O    . HOH   N 7 .   ? 44.009 9.930   75.009 1.00 28.00 ? 1394 HOH   B O    1 
HETATM 20334 O  O    . HOH   N 7 .   ? 9.673  44.001  83.965 1.00 35.64 ? 1395 HOH   B O    1 
HETATM 20335 O  O    . HOH   N 7 .   ? 18.149 51.014  69.682 1.00 28.91 ? 1396 HOH   B O    1 
HETATM 20336 O  O    . HOH   N 7 .   ? 16.077 40.494  44.383 1.00 30.48 ? 1397 HOH   B O    1 
HETATM 20337 O  O    . HOH   N 7 .   ? 39.212 18.383  37.314 1.00 32.44 ? 1398 HOH   B O    1 
HETATM 20338 O  O    . HOH   N 7 .   ? -3.599 34.518  83.061 1.00 27.54 ? 1399 HOH   B O    1 
HETATM 20339 O  O    . HOH   N 7 .   ? 50.833 19.851  72.380 1.00 35.40 ? 1400 HOH   B O    1 
HETATM 20340 O  O    . HOH   N 7 .   ? 35.141 -8.963  61.514 1.00 32.80 ? 1401 HOH   B O    1 
HETATM 20341 O  O    . HOH   N 7 .   ? 24.573 20.395  51.053 1.00 15.12 ? 1402 HOH   B O    1 
HETATM 20342 O  O    . HOH   N 7 .   ? 44.281 25.103  72.057 1.00 29.72 ? 1403 HOH   B O    1 
HETATM 20343 O  O    . HOH   N 7 .   ? 18.703 51.726  67.040 1.00 28.53 ? 1404 HOH   B O    1 
HETATM 20344 O  O    . HOH   N 7 .   ? 17.689 26.393  85.203 1.00 25.47 ? 1405 HOH   B O    1 
HETATM 20345 O  O    . HOH   N 7 .   ? 1.786  26.198  56.614 1.00 29.74 ? 1406 HOH   B O    1 
HETATM 20346 O  O    . HOH   N 7 .   ? 43.649 0.407   55.502 1.00 25.71 ? 1407 HOH   B O    1 
HETATM 20347 O  O    B HOH   N 7 .   ? 36.677 -1.226  70.378 0.85 34.88 ? 1408 HOH   B O    1 
HETATM 20348 O  O    . HOH   N 7 .   ? 4.627  17.208  93.084 1.00 36.02 ? 1409 HOH   B O    1 
HETATM 20349 O  O    . HOH   N 7 .   ? 6.803  7.665   90.395 1.00 32.02 ? 1410 HOH   B O    1 
HETATM 20350 O  O    . HOH   N 7 .   ? 46.440 31.113  51.312 1.00 34.59 ? 1411 HOH   B O    1 
HETATM 20351 O  O    . HOH   N 7 .   ? 28.374 46.931  63.885 1.00 34.62 ? 1412 HOH   B O    1 
HETATM 20352 O  O    . HOH   N 7 .   ? 0.921  39.498  72.591 1.00 36.82 ? 1413 HOH   B O    1 
HETATM 20353 O  O    . HOH   N 7 .   ? 10.415 45.348  55.956 1.00 31.52 ? 1414 HOH   B O    1 
HETATM 20354 O  O    . HOH   N 7 .   ? 31.974 24.461  45.606 1.00 32.97 ? 1415 HOH   B O    1 
HETATM 20355 O  O    . HOH   N 7 .   ? 47.282 3.322   56.243 1.00 39.09 ? 1416 HOH   B O    1 
HETATM 20356 O  O    . HOH   N 7 .   ? 20.422 40.391  92.305 1.00 39.31 ? 1417 HOH   B O    1 
HETATM 20357 O  O    . HOH   N 7 .   ? 27.150 55.007  76.662 1.00 30.89 ? 1418 HOH   B O    1 
HETATM 20358 O  O    . HOH   N 7 .   ? 47.962 24.230  43.834 1.00 33.33 ? 1419 HOH   B O    1 
HETATM 20359 O  O    . HOH   N 7 .   ? 34.052 -1.172  45.326 1.00 42.66 ? 1420 HOH   B O    1 
HETATM 20360 O  O    . HOH   N 7 .   ? 31.837 19.660  47.171 1.00 20.64 ? 1421 HOH   B O    1 
HETATM 20361 O  O    . HOH   N 7 .   ? 32.786 57.315  71.151 1.00 35.84 ? 1422 HOH   B O    1 
HETATM 20362 O  O    . HOH   N 7 .   ? 7.943  42.286  82.714 1.00 41.25 ? 1423 HOH   B O    1 
HETATM 20363 O  O    . HOH   N 7 .   ? 20.609 50.946  82.143 1.00 33.18 ? 1424 HOH   B O    1 
HETATM 20364 O  O    . HOH   N 7 .   ? -5.528 11.327  76.444 1.00 37.03 ? 1425 HOH   B O    1 
HETATM 20365 O  O    . HOH   N 7 .   ? 5.876  1.228   45.169 1.00 41.23 ? 1426 HOH   B O    1 
HETATM 20366 O  O    . HOH   N 7 .   ? 11.680 40.629  45.146 1.00 25.17 ? 1427 HOH   B O    1 
HETATM 20367 O  O    . HOH   N 7 .   ? -1.046 7.184   80.965 1.00 28.95 ? 1428 HOH   B O    1 
HETATM 20368 O  O    . HOH   N 7 .   ? 47.836 19.734  76.301 1.00 33.09 ? 1429 HOH   B O    1 
HETATM 20369 O  O    . HOH   N 7 .   ? 46.517 26.476  51.334 1.00 19.70 ? 1430 HOH   B O    1 
HETATM 20370 O  O    . HOH   N 7 .   ? 12.876 44.500  56.995 1.00 28.06 ? 1431 HOH   B O    1 
HETATM 20371 O  O    . HOH   N 7 .   ? 17.777 49.984  85.639 1.00 30.39 ? 1432 HOH   B O    1 
HETATM 20372 O  O    . HOH   N 7 .   ? 1.921  13.931  90.117 1.00 33.90 ? 1433 HOH   B O    1 
HETATM 20373 O  O    . HOH   N 7 .   ? 28.515 43.918  61.554 1.00 32.91 ? 1434 HOH   B O    1 
HETATM 20374 O  O    . HOH   N 7 .   ? 46.929 26.688  47.129 1.00 18.38 ? 1435 HOH   B O    1 
HETATM 20375 O  O    . HOH   N 7 .   ? 24.562 4.759   44.672 1.00 35.71 ? 1436 HOH   B O    1 
HETATM 20376 O  O    . HOH   N 7 .   ? 48.878 20.283  45.648 1.00 36.01 ? 1437 HOH   B O    1 
HETATM 20377 O  O    . HOH   N 7 .   ? 49.132 28.255  65.945 1.00 35.04 ? 1438 HOH   B O    1 
HETATM 20378 O  O    . HOH   N 7 .   ? 25.094 45.767  60.377 1.00 32.29 ? 1439 HOH   B O    1 
HETATM 20379 O  O    . HOH   N 7 .   ? 30.748 30.895  50.332 1.00 34.57 ? 1440 HOH   B O    1 
HETATM 20380 O  O    . HOH   N 7 .   ? 7.788  41.771  52.499 1.00 31.49 ? 1441 HOH   B O    1 
HETATM 20381 O  O    . HOH   N 7 .   ? 32.312 26.612  48.184 1.00 29.26 ? 1442 HOH   B O    1 
HETATM 20382 O  O    . HOH   N 7 .   ? 20.261 50.776  85.353 1.00 30.91 ? 1443 HOH   B O    1 
HETATM 20383 O  O    . HOH   N 7 .   ? 43.134 8.269   76.839 1.00 38.37 ? 1444 HOH   B O    1 
HETATM 20384 O  O    . HOH   N 7 .   ? 37.797 51.790  73.585 1.00 34.80 ? 1445 HOH   B O    1 
HETATM 20385 O  O    . HOH   N 7 .   ? 30.660 46.069  65.005 1.00 31.46 ? 1446 HOH   B O    1 
HETATM 20386 O  O    . HOH   N 7 .   ? 32.654 30.191  83.386 1.00 39.95 ? 1447 HOH   B O    1 
HETATM 20387 O  O    . HOH   N 7 .   ? 24.744 46.012  45.923 1.00 35.74 ? 1448 HOH   B O    1 
HETATM 20388 O  O    . HOH   N 7 .   ? 0.407  22.745  48.525 1.00 42.42 ? 1449 HOH   B O    1 
HETATM 20389 O  O    . HOH   N 7 .   ? 4.100  3.053   46.713 1.00 33.96 ? 1450 HOH   B O    1 
HETATM 20390 O  O    . HOH   N 7 .   ? 31.176 1.726   82.983 1.00 38.61 ? 1451 HOH   B O    1 
HETATM 20391 O  O    . HOH   N 7 .   ? 11.720 -11.028 61.814 1.00 39.11 ? 1452 HOH   B O    1 
HETATM 20392 O  O    . HOH   N 7 .   ? 2.552  24.281  49.634 1.00 34.77 ? 1453 HOH   B O    1 
HETATM 20393 O  O    . HOH   N 7 .   ? 17.445 -7.415  69.647 1.00 35.27 ? 1454 HOH   B O    1 
HETATM 20394 O  O    . HOH   N 7 .   ? 0.721  37.398  83.204 1.00 32.62 ? 1455 HOH   B O    1 
HETATM 20395 O  O    . HOH   N 7 .   ? 14.940 3.336   41.403 1.00 45.55 ? 1456 HOH   B O    1 
HETATM 20396 O  O    . HOH   N 7 .   ? 20.240 -9.535  76.113 1.00 42.68 ? 1457 HOH   B O    1 
HETATM 20397 O  O    . HOH   N 7 .   ? 37.142 -0.142  51.324 1.00 36.09 ? 1458 HOH   B O    1 
HETATM 20398 O  O    . HOH   N 7 .   ? 22.245 -11.260 57.542 1.00 35.27 ? 1459 HOH   B O    1 
HETATM 20399 O  O    . HOH   N 7 .   ? 30.940 43.068  62.651 1.00 27.79 ? 1460 HOH   B O    1 
HETATM 20400 O  O    . HOH   N 7 .   ? 45.323 8.353   47.030 1.00 38.12 ? 1461 HOH   B O    1 
HETATM 20401 O  O    . HOH   N 7 .   ? 29.966 18.755  84.318 1.00 29.76 ? 1462 HOH   B O    1 
HETATM 20402 O  O    . HOH   N 7 .   ? 44.322 34.684  50.244 1.00 38.59 ? 1463 HOH   B O    1 
HETATM 20403 O  O    . HOH   N 7 .   ? 12.589 50.207  70.188 1.00 32.39 ? 1464 HOH   B O    1 
HETATM 20404 O  O    . HOH   N 7 .   ? 44.724 -3.498  66.794 1.00 21.95 ? 1465 HOH   B O    1 
HETATM 20405 O  O    . HOH   N 7 .   ? 29.240 38.144  51.736 1.00 42.93 ? 1466 HOH   B O    1 
HETATM 20406 O  O    . HOH   N 7 .   ? 28.759 29.316  49.721 1.00 18.98 ? 1467 HOH   B O    1 
HETATM 20407 O  O    . HOH   N 7 .   ? 8.880  11.255  92.377 1.00 29.10 ? 1468 HOH   B O    1 
HETATM 20408 O  O    . HOH   N 7 .   ? 10.699 0.698   89.723 1.00 37.84 ? 1469 HOH   B O    1 
HETATM 20409 O  O    A HOH   N 7 .   ? 32.297 40.431  88.298 0.39 28.95 ? 1470 HOH   B O    1 
HETATM 20410 O  O    . HOH   N 7 .   ? 28.089 30.313  53.773 1.00 14.06 ? 1471 HOH   B O    1 
HETATM 20411 O  O    . HOH   N 7 .   ? 35.096 9.597   41.872 1.00 30.72 ? 1472 HOH   B O    1 
HETATM 20412 O  O    . HOH   N 7 .   ? 49.567 28.058  63.216 1.00 30.10 ? 1473 HOH   B O    1 
HETATM 20413 O  O    . HOH   N 7 .   ? 22.215 -11.010 53.296 1.00 36.14 ? 1474 HOH   B O    1 
HETATM 20414 O  O    . HOH   N 7 .   ? 11.735 -7.072  81.916 1.00 42.39 ? 1475 HOH   B O    1 
HETATM 20415 O  O    . HOH   N 7 .   ? 36.469 53.806  67.253 1.00 31.60 ? 1476 HOH   B O    1 
HETATM 20416 O  O    . HOH   N 7 .   ? 0.692  8.167   51.524 1.00 36.22 ? 1477 HOH   B O    1 
HETATM 20417 O  O    . HOH   N 7 .   ? 8.118  18.080  92.827 1.00 35.45 ? 1478 HOH   B O    1 
HETATM 20418 O  O    . HOH   N 7 .   ? 20.452 27.968  87.282 1.00 29.85 ? 1479 HOH   B O    1 
HETATM 20419 O  O    . HOH   N 7 .   ? -7.175 15.063  74.432 1.00 28.95 ? 1480 HOH   B O    1 
HETATM 20420 O  O    . HOH   N 7 .   ? 33.638 36.376  56.998 1.00 32.88 ? 1481 HOH   B O    1 
HETATM 20421 O  O    . HOH   N 7 .   ? 8.728  3.828   90.377 1.00 37.21 ? 1482 HOH   B O    1 
HETATM 20422 O  O    . HOH   N 7 .   ? 16.120 49.594  78.606 1.00 32.98 ? 1483 HOH   B O    1 
HETATM 20423 O  O    . HOH   N 7 .   ? -0.699 6.598   76.841 1.00 27.39 ? 1484 HOH   B O    1 
HETATM 20424 O  O    . HOH   N 7 .   ? 6.919  12.108  41.037 1.00 36.72 ? 1485 HOH   B O    1 
HETATM 20425 O  O    . HOH   N 7 .   ? 47.624 24.581  53.201 1.00 22.22 ? 1486 HOH   B O    1 
HETATM 20426 O  O    . HOH   N 7 .   ? 0.713  5.846   71.539 1.00 34.90 ? 1487 HOH   B O    1 
HETATM 20427 O  O    . HOH   N 7 .   ? 11.690 6.829   43.250 1.00 37.53 ? 1488 HOH   B O    1 
HETATM 20428 O  O    . HOH   N 7 .   ? 35.941 26.474  79.033 1.00 37.66 ? 1489 HOH   B O    1 
HETATM 20429 O  O    . HOH   N 7 .   ? 1.515  25.931  53.881 1.00 28.52 ? 1490 HOH   B O    1 
HETATM 20430 O  O    . HOH   N 7 .   ? 28.646 -4.413  72.384 1.00 30.34 ? 1491 HOH   B O    1 
HETATM 20431 O  O    . HOH   N 7 .   ? 16.011 7.383   43.637 1.00 39.39 ? 1492 HOH   B O    1 
HETATM 20432 O  O    . HOH   N 7 .   ? 2.404  4.444   79.671 1.00 24.58 ? 1493 HOH   B O    1 
HETATM 20433 O  O    . HOH   N 7 .   ? -0.411 19.594  57.377 1.00 38.08 ? 1494 HOH   B O    1 
HETATM 20434 O  O    . HOH   N 7 .   ? 45.036 -1.611  70.537 1.00 33.87 ? 1495 HOH   B O    1 
HETATM 20435 O  O    . HOH   N 7 .   ? 52.361 11.214  56.094 1.00 37.60 ? 1496 HOH   B O    1 
HETATM 20436 O  O    . HOH   N 7 .   ? 31.254 -3.701  46.950 1.00 39.23 ? 1497 HOH   B O    1 
HETATM 20437 O  O    . HOH   N 7 .   ? 42.785 -3.908  68.871 1.00 31.39 ? 1498 HOH   B O    1 
HETATM 20438 O  O    . HOH   N 7 .   ? 2.081  4.131   55.116 1.00 40.98 ? 1499 HOH   B O    1 
HETATM 20439 O  O    . HOH   N 7 .   ? 23.851 0.825   44.966 1.00 37.00 ? 1500 HOH   B O    1 
HETATM 20440 O  O    . HOH   N 7 .   ? 35.961 39.493  80.356 1.00 38.10 ? 1501 HOH   B O    1 
HETATM 20441 O  O    . HOH   N 7 .   ? 28.801 35.100  51.745 1.00 30.10 ? 1502 HOH   B O    1 
HETATM 20442 O  O    . HOH   N 7 .   ? 50.035 22.298  50.241 1.00 33.70 ? 1503 HOH   B O    1 
HETATM 20443 O  O    . HOH   N 7 .   ? 19.620 -2.106  92.245 1.00 36.56 ? 1504 HOH   B O    1 
HETATM 20444 O  O    . HOH   N 7 .   ? 15.070 51.060  72.814 1.00 34.52 ? 1505 HOH   B O    1 
HETATM 20445 O  O    B HOH   N 7 .   ? 30.612 21.694  45.537 0.76 21.34 ? 1506 HOH   B O    1 
HETATM 20446 O  O    . HOH   N 7 .   ? -0.191 22.987  60.480 1.00 35.72 ? 1507 HOH   B O    1 
HETATM 20447 O  O    . HOH   N 7 .   ? 16.614 0.365   91.329 1.00 36.92 ? 1508 HOH   B O    1 
HETATM 20448 O  O    . HOH   N 7 .   ? 29.090 56.264  74.974 1.00 30.75 ? 1509 HOH   B O    1 
HETATM 20449 O  O    . HOH   N 7 .   ? 39.674 27.031  77.280 1.00 35.39 ? 1510 HOH   B O    1 
HETATM 20450 O  O    . HOH   N 7 .   ? 5.528  7.347   64.621 1.00 37.80 ? 1511 HOH   B O    1 
HETATM 20451 O  O    . HOH   N 7 .   ? 10.012 19.096  42.241 1.00 31.58 ? 1512 HOH   B O    1 
HETATM 20452 O  O    . HOH   N 7 .   ? 41.439 24.662  77.652 1.00 31.96 ? 1513 HOH   B O    1 
HETATM 20453 O  O    . HOH   N 7 .   ? 15.401 51.463  75.449 1.00 32.98 ? 1514 HOH   B O    1 
HETATM 20454 O  O    . HOH   N 7 .   ? 52.464 8.602   54.750 1.00 36.49 ? 1515 HOH   B O    1 
HETATM 20455 O  O    . HOH   N 7 .   ? 29.730 26.902  48.454 1.00 24.35 ? 1516 HOH   B O    1 
HETATM 20456 O  O    . HOH   N 7 .   ? 37.000 36.227  55.649 1.00 35.49 ? 1517 HOH   B O    1 
HETATM 20457 O  O    . HOH   N 7 .   ? 31.103 26.598  43.974 1.00 35.00 ? 1518 HOH   B O    1 
HETATM 20458 O  O    . HOH   N 7 .   ? 28.583 22.595  46.458 1.00 32.28 ? 1519 HOH   B O    1 
HETATM 20459 O  O    . HOH   N 7 .   ? 28.775 27.473  45.738 1.00 32.43 ? 1520 HOH   B O    1 
HETATM 20460 O  O    . HOH   N 7 .   ? 49.382 25.837  47.920 1.00 30.76 ? 1521 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N  N   . MET   A 1   ? 0.5747 0.4640 0.6059 -0.0261 -0.0785 -0.0490 1   MET   A N   
2     C  CA  . MET   A 1   ? 0.5705 0.4553 0.5990 -0.0212 -0.0775 -0.0524 1   MET   A CA  
3     C  C   . MET   A 1   ? 0.5073 0.3971 0.5392 -0.0186 -0.0716 -0.0600 1   MET   A C   
4     O  O   . MET   A 1   ? 0.4707 0.3654 0.4973 -0.0216 -0.0692 -0.0614 1   MET   A O   
5     C  CB  . MET   A 1   ? 0.4088 0.3018 0.4645 -0.0206 -0.0789 -0.0430 1   MET   A CB  
6     C  CG  . MET   A 1   ? 0.4031 0.3014 0.4506 -0.0245 -0.0793 -0.0335 1   MET   A CG  
7     S  SD  . MET   A 1   ? 0.4089 0.3102 0.4651 -0.0246 -0.0825 -0.0232 1   MET   A SD  
8     C  CE  . MET   A 1   ? 0.4119 0.3069 0.4708 -0.0274 -0.0892 -0.0198 1   MET   A CE  
20    N  N   . TYR   A 2   ? 0.4188 0.3086 0.4604 -0.0133 -0.0698 -0.0642 2   TYR   A N   
21    C  CA  . TYR   A 2   ? 0.3173 0.2129 0.3621 -0.0108 -0.0642 -0.0708 2   TYR   A CA  
22    C  C   . TYR   A 2   ? 0.2838 0.1866 0.3274 -0.0114 -0.0625 -0.0632 2   TYR   A C   
23    O  O   . TYR   A 2   ? 0.2546 0.1583 0.3089 -0.0106 -0.0650 -0.0560 2   TYR   A O   
24    C  CB  . TYR   A 2   ? 0.3313 0.2227 0.3791 -0.0044 -0.0623 -0.0803 2   TYR   A CB  
25    C  CG  . TYR   A 2   ? 0.3593 0.2421 0.3983 -0.0032 -0.0630 -0.0896 2   TYR   A CG  
26    C  CD1 . TYR   A 2   ? 0.3350 0.2191 0.3673 -0.0062 -0.0608 -0.0959 2   TYR   A CD1 
27    C  CD2 . TYR   A 2   ? 0.3242 0.2017 0.3809 0.0007  -0.0665 -0.0923 2   TYR   A CD2 
28    C  CE1 . TYR   A 2   ? 0.3799 0.2562 0.4044 -0.0055 -0.0614 -0.1044 2   TYR   A CE1 
29    C  CE2 . TYR   A 2   ? 0.3732 0.2424 0.4223 0.0018  -0.0674 -0.1009 2   TYR   A CE2 
30    C  CZ  . TYR   A 2   ? 0.4292 0.2971 0.4598 -0.0013 -0.0646 -0.1075 2   TYR   A CZ  
31    O  OH  . TYR   A 2   ? 0.4659 0.3266 0.4934 -0.0004 -0.0654 -0.1165 2   TYR   A OH  
41    N  N   . GLY   A 3   ? 0.2795 0.1883 0.3150 -0.0131 -0.0588 -0.0646 3   GLY   A N   
42    C  CA  . GLY   A 3   ? 0.2606 0.1766 0.2985 -0.0141 -0.0575 -0.0576 3   GLY   A CA  
43    C  C   . GLY   A 3   ? 0.2295 0.1483 0.2663 -0.0183 -0.0602 -0.0472 3   GLY   A C   
44    O  O   . GLY   A 3   ? 0.2237 0.1467 0.2525 -0.0218 -0.0593 -0.0449 3   GLY   A O   
48    N  N   . TYR   A 4   ? 0.2075 0.1249 0.2535 -0.0178 -0.0635 -0.0408 4   TYR   A N   
49    C  CA  . TYR   A 4   ? 0.2328 0.1520 0.2736 -0.0214 -0.0657 -0.0321 4   TYR   A CA  
50    C  C   . TYR   A 4   ? 0.2173 0.1345 0.2554 -0.0245 -0.0673 -0.0342 4   TYR   A C   
51    O  O   . TYR   A 4   ? 0.2492 0.1587 0.2812 -0.0235 -0.0683 -0.0412 4   TYR   A O   
52    C  CB  . TYR   A 4   ? 0.2332 0.1511 0.2845 -0.0208 -0.0693 -0.0258 4   TYR   A CB  
53    C  CG  . TYR   A 4   ? 0.2296 0.1494 0.2900 -0.0177 -0.0688 -0.0240 4   TYR   A CG  
54    C  CD1 . TYR   A 4   ? 0.2304 0.1451 0.2978 -0.0138 -0.0698 -0.0291 4   TYR   A CD1 
55    C  CD2 . TYR   A 4   ? 0.2261 0.1529 0.2884 -0.0188 -0.0676 -0.0171 4   TYR   A CD2 
56    C  CE1 . TYR   A 4   ? 0.2232 0.1398 0.2988 -0.0109 -0.0698 -0.0271 4   TYR   A CE1 
57    C  CE2 . TYR   A 4   ? 0.2336 0.1615 0.3008 -0.0162 -0.0677 -0.0152 4   TYR   A CE2 
58    C  CZ  . TYR   A 4   ? 0.2051 0.1293 0.2853 -0.0124 -0.0690 -0.0198 4   TYR   A CZ  
59    O  OH  . TYR   A 4   ? 0.2222 0.1476 0.3064 -0.0103 -0.0692 -0.0175 4   TYR   A OH  
69    N  N   . ASP   A 5   ? 0.2337 0.1551 0.2639 -0.0279 -0.0676 -0.0288 5   ASP   A N   
70    C  CA  . ASP   A 5   ? 0.2440 0.1629 0.2672 -0.0310 -0.0698 -0.0294 5   ASP   A CA  
71    C  C   . ASP   A 5   ? 0.2522 0.1666 0.2801 -0.0317 -0.0741 -0.0257 5   ASP   A C   
72    O  O   . ASP   A 5   ? 0.2356 0.1444 0.2640 -0.0330 -0.0768 -0.0295 5   ASP   A O   
73    C  CB  . ASP   A 5   ? 0.2124 0.1394 0.2337 -0.0337 -0.0687 -0.0249 5   ASP   A CB  
74    C  CG  . ASP   A 5   ? 0.2167 0.1467 0.2287 -0.0343 -0.0657 -0.0283 5   ASP   A CG  
75    O  OD1 . ASP   A 5   ? 0.2107 0.1375 0.2198 -0.0334 -0.0643 -0.0355 5   ASP   A OD1 
76    O  OD2 . ASP   A 5   ? 0.2161 0.1526 0.2268 -0.0355 -0.0648 -0.0237 5   ASP   A OD2 
81    N  N   . GLY   A 6   ? 0.2321 0.1509 0.2713 -0.0316 -0.0753 -0.0183 6   GLY   A N   
82    C  CA  . GLY   A 6   ? 0.2618 0.1762 0.3006 -0.0330 -0.0798 -0.0134 6   GLY   A CA  
83    C  C   . GLY   A 6   ? 0.2248 0.1459 0.2679 -0.0362 -0.0811 -0.0060 6   GLY   A C   
84    O  O   . GLY   A 6   ? 0.2107 0.1295 0.2571 -0.0383 -0.0851 -0.0019 6   GLY   A O   
88    N  N   . LYS   A 7   ? 0.2248 0.1529 0.2628 -0.0372 -0.0778 -0.0043 7   LYS   A N   
89    C  CA  . LYS   A 7   ? 0.2176 0.1515 0.2552 -0.0398 -0.0785 0.0017  7   LYS   A CA  
90    C  C   . LYS   A 7   ? 0.2020 0.1447 0.2404 -0.0394 -0.0750 0.0060  7   LYS   A C   
91    O  O   . LYS   A 7   ? 0.1837 0.1289 0.2215 -0.0373 -0.0715 0.0031  7   LYS   A O   
92    C  CB  . LYS   A 7   ? 0.2127 0.1463 0.2478 -0.0419 -0.0796 -0.0007 7   LYS   A CB  
93    C  CG  . LYS   A 7   ? 0.2462 0.1706 0.2776 -0.0431 -0.0834 -0.0048 7   LYS   A CG  
94    C  CD  . LYS   A 7   ? 0.2771 0.1985 0.3125 -0.0452 -0.0882 -0.0005 7   LYS   A CD  
95    C  CE  . LYS   A 7   ? 0.2893 0.2013 0.3276 -0.0457 -0.0924 -0.0048 7   LYS   A CE  
96    N  NZ  . LYS   A 7   ? 0.3419 0.2505 0.3791 -0.0487 -0.0977 -0.0002 7   LYS   A NZ  
110   N  N   . VAL   A 8   ? 0.1825 0.1311 0.2268 -0.0414 -0.0755 0.0123  8   VAL   A N   
111   C  CA  . VAL   A 8   ? 0.1859 0.1435 0.2333 -0.0409 -0.0721 0.0159  8   VAL   A CA  
112   C  C   . VAL   A 8   ? 0.2317 0.1931 0.2700 -0.0431 -0.0722 0.0185  8   VAL   A C   
113   O  O   . VAL   A 8   ? 0.2071 0.1688 0.2550 -0.0458 -0.0752 0.0211  8   VAL   A O   
114   C  CB  . VAL   A 8   ? 0.2028 0.1615 0.2491 -0.0413 -0.0721 0.0205  8   VAL   A CB  
115   C  CG1 . VAL   A 8   ? 0.1963 0.1644 0.2459 -0.0417 -0.0688 0.0237  8   VAL   A CG1 
116   C  CG2 . VAL   A 8   ? 0.1807 0.1348 0.2313 -0.0389 -0.0726 0.0182  8   VAL   A CG2 
126   N  N   . LEU   A 9   ? 0.1666 0.1359 0.2132 -0.0420 -0.0689 0.0182  9   LEU   A N   
127   C  CA  . LEU   A 9   ? 0.1592 0.1342 0.2054 -0.0436 -0.0690 0.0202  9   LEU   A CA  
128   C  C   . LEU   A 9   ? 0.1584 0.1419 0.2081 -0.0442 -0.0667 0.0242  9   LEU   A C   
129   O  O   . LEU   A 9   ? 0.1632 0.1504 0.2130 -0.0422 -0.0636 0.0232  9   LEU   A O   
130   C  CB  . LEU   A 9   ? 0.1712 0.1469 0.2137 -0.0419 -0.0677 0.0172  9   LEU   A CB  
131   C  CG  . LEU   A 9   ? 0.1933 0.1751 0.2384 -0.0426 -0.0680 0.0188  9   LEU   A CG  
132   C  CD1 . LEU   A 9   ? 0.1960 0.1770 0.2426 -0.0457 -0.0716 0.0210  9   LEU   A CD1 
133   C  CD2 . LEU   A 9   ? 0.2297 0.2102 0.2684 -0.0410 -0.0677 0.0162  9   LEU   A CD2 
145   N  N   . ARG   A 10  ? 0.1425 0.1305 0.1986 -0.0476 -0.0682 0.0284  10  ARG   A N   
146   C  CA  . ARG   A 10  ? 0.1522 0.1505 0.2140 -0.0492 -0.0659 0.0321  10  ARG   A CA  
147   C  C   . ARG   A 10  ? 0.1647 0.1709 0.2276 -0.0497 -0.0652 0.0323  10  ARG   A C   
148   O  O   . ARG   A 10  ? 0.1520 0.1580 0.2185 -0.0523 -0.0679 0.0338  10  ARG   A O   
149   C  CB  . ARG   A 10  ? 0.1949 0.1924 0.2536 -0.0528 -0.0679 0.0371  10  ARG   A CB  
150   C  CG  . ARG   A 10  ? 0.1690 0.1790 0.2383 -0.0550 -0.0653 0.0409  10  ARG   A CG  
151   C  CD  . ARG   A 10  ? 0.2221 0.2304 0.2841 -0.0590 -0.0675 0.0466  10  ARG   A CD  
152   N  NE  . ARG   A 10  ? 0.1767 0.1774 0.2432 -0.0579 -0.0695 0.0471  10  ARG   A NE  
153   C  CZ  . ARG   A 10  ? 0.1876 0.1889 0.2502 -0.0571 -0.0678 0.0476  10  ARG   A CZ  
154   N  NH1 . ARG   A 10  ? 0.1901 0.2012 0.2524 -0.0573 -0.0637 0.0476  10  ARG   A NH1 
155   N  NH2 . ARG   A 10  ? 0.2057 0.1981 0.2654 -0.0560 -0.0705 0.0480  10  ARG   A NH2 
169   N  N   . ILE   A 11  ? 0.1684 0.1823 0.2337 -0.0479 -0.0619 0.0306  11  ILE   A N   
170   C  CA  . ILE   A 11  ? 0.1527 0.1751 0.2236 -0.0474 -0.0613 0.0300  11  ILE   A CA  
171   C  C   . ILE   A 11  ? 0.1301 0.1666 0.2109 -0.0486 -0.0582 0.0314  11  ILE   A C   
172   O  O   . ILE   A 11  ? 0.1655 0.2042 0.2410 -0.0468 -0.0555 0.0297  11  ILE   A O   
173   C  CB  . ILE   A 11  ? 0.1515 0.1714 0.2218 -0.0438 -0.0610 0.0260  11  ILE   A CB  
174   C  CG1 . ILE   A 11  ? 0.1811 0.1892 0.2429 -0.0432 -0.0636 0.0245  11  ILE   A CG1 
175   C  CG2 . ILE   A 11  ? 0.1509 0.1792 0.2263 -0.0428 -0.0608 0.0254  11  ILE   A CG2 
176   C  CD1 . ILE   A 11  ? 0.2060 0.2104 0.2629 -0.0403 -0.0635 0.0214  11  ILE   A CD1 
188   N  N   . ASN   A 12  ? 0.1304 0.1748 0.2151 -0.0518 -0.0586 0.0345  12  ASN   A N   
189   C  CA  . ASN   A 12  ? 0.1321 0.1924 0.2268 -0.0531 -0.0553 0.0356  12  ASN   A CA  
190   C  C   . ASN   A 12  ? 0.1583 0.2269 0.2544 -0.0507 -0.0545 0.0327  12  ASN   A C   
191   O  O   . ASN   A 12  ? 0.1251 0.1963 0.2308 -0.0517 -0.0568 0.0337  12  ASN   A O   
192   C  CB  . ASN   A 12  ? 0.1626 0.2280 0.2573 -0.0583 -0.0557 0.0411  12  ASN   A CB  
193   C  CG  . ASN   A 12  ? 0.1850 0.2666 0.2829 -0.0603 -0.0515 0.0424  12  ASN   A CG  
194   O  OD1 . ASN   A 12  ? 0.1648 0.2597 0.2751 -0.0592 -0.0495 0.0405  12  ASN   A OD1 
195   N  ND2 . ASN   A 12  ? 0.1631 0.2467 0.2613 -0.0627 -0.0501 0.0453  12  ASN   A ND2 
202   N  N   . LEU   A 13  ? 0.1366 0.2131 0.2407 -0.0473 -0.0518 0.0287  13  LEU   A N   
203   C  CA  . LEU   A 13  ? 0.1378 0.2216 0.2485 -0.0438 -0.0517 0.0252  13  LEU   A CA  
204   C  C   . LEU   A 13  ? 0.1503 0.2512 0.2710 -0.0453 -0.0496 0.0259  13  LEU   A C   
205   O  O   . LEU   A 13  ? 0.1287 0.2365 0.2609 -0.0429 -0.0506 0.0240  13  LEU   A O   
206   C  CB  . LEU   A 13  ? 0.1196 0.2031 0.2298 -0.0393 -0.0503 0.0207  13  LEU   A CB  
207   C  CG  . LEU   A 13  ? 0.1219 0.1895 0.2235 -0.0370 -0.0524 0.0193  13  LEU   A CG  
208   C  CD1 . LEU   A 13  ? 0.1602 0.2275 0.2569 -0.0331 -0.0511 0.0155  13  LEU   A CD1 
209   C  CD2 . LEU   A 13  ? 0.1296 0.1889 0.2271 -0.0364 -0.0560 0.0198  13  LEU   A CD2 
221   N  N   . LYS   A 14  ? 0.1351 0.2454 0.2609 -0.0492 -0.0468 0.0291  14  LYS   A N   
222   C  CA  . LYS   A 14  ? 0.1347 0.2635 0.2733 -0.0513 -0.0440 0.0304  14  LYS   A CA  
223   C  C   . LYS   A 14  ? 0.1568 0.2825 0.2954 -0.0546 -0.0473 0.0343  14  LYS   A C   
224   O  O   . LYS   A 14  ? 0.1501 0.2859 0.2996 -0.0535 -0.0474 0.0333  14  LYS   A O   
225   C  CB  . LYS   A 14  ? 0.1687 0.3076 0.3041 -0.0552 -0.0395 0.0332  14  LYS   A CB  
226   C  CG  . LYS   A 14  ? 0.1850 0.3432 0.3302 -0.0581 -0.0357 0.0351  14  LYS   A CG  
227   C  CD  . LYS   A 14  ? 0.1906 0.3611 0.3385 -0.0623 -0.0308 0.0382  14  LYS   A CD  
228   C  CE  . LYS   A 14  ? 0.2827 0.4679 0.4330 -0.0671 -0.0280 0.0427  14  LYS   A CE  
229   N  NZ  . LYS   A 14  ? 0.3918 0.5740 0.5278 -0.0739 -0.0280 0.0500  14  LYS   A NZ  
243   N  N   . GLU   A 15  ? 0.1802 0.2923 0.3092 -0.0581 -0.0506 0.0387  15  GLU   A N   
244   C  CA  . GLU   A 15  ? 0.1778 0.2855 0.3066 -0.0616 -0.0547 0.0429  15  GLU   A CA  
245   C  C   . GLU   A 15  ? 0.1627 0.2584 0.2907 -0.0587 -0.0591 0.0407  15  GLU   A C   
246   O  O   . GLU   A 15  ? 0.1706 0.2642 0.3004 -0.0609 -0.0626 0.0432  15  GLU   A O   
247   C  CB  . GLU   A 15  ? 0.1578 0.2580 0.2840 -0.0664 -0.0565 0.0484  15  GLU   A CB  
248   C  CG  . GLU   A 15  ? 0.1952 0.3055 0.3196 -0.0700 -0.0527 0.0520  15  GLU   A CG  
249   C  CD  . GLU   A 15  ? 0.2330 0.3629 0.3683 -0.0728 -0.0496 0.0541  15  GLU   A CD  
250   O  OE1 . GLU   A 15  ? 0.2203 0.3527 0.3624 -0.0737 -0.0518 0.0551  15  GLU   A OE1 
251   O  OE2 . GLU   A 15  ? 0.2881 0.4303 0.4225 -0.0741 -0.0447 0.0547  15  GLU   A OE2 
258   N  N   . ARG   A 16  ? 0.1423 0.2304 0.2654 -0.0542 -0.0591 0.0364  16  ARG   A N   
259   C  CA  . ARG   A 16  ? 0.1328 0.2102 0.2571 -0.0518 -0.0629 0.0346  16  ARG   A CA  
260   C  C   . ARG   A 16  ? 0.1728 0.2343 0.2794 -0.0549 -0.0669 0.0376  16  ARG   A C   
261   O  O   . ARG   A 16  ? 0.1565 0.2147 0.2674 -0.0558 -0.0708 0.0386  16  ARG   A O   
262   C  CB  . ARG   A 16  ? 0.2113 0.2948 0.3353 -0.0501 -0.0643 0.0334  16  ARG   A CB  
263   C  CG  . ARG   A 16  ? 0.2111 0.3089 0.3504 -0.0459 -0.0609 0.0295  16  ARG   A CG  
264   C  CD  . ARG   A 16  ? 0.2690 0.3648 0.4063 -0.0419 -0.0634 0.0267  16  ARG   A CD  
265   N  NE  . ARG   A 16  ? 0.2428 0.3523 0.3961 -0.0374 -0.0606 0.0227  16  ARG   A NE  
266   C  CZ  . ARG   A 16  ? 0.2850 0.3920 0.4373 -0.0328 -0.0625 0.0200  16  ARG   A CZ  
267   N  NH1 . ARG   A 16  ? 0.3080 0.4027 0.4558 -0.0327 -0.0673 0.0216  16  ARG   A NH1 
268   N  NH2 . ARG   A 16  ? 0.2770 0.3949 0.4389 -0.0284 -0.0599 0.0160  16  ARG   A NH2 
282   N  N   . THR   A 17  ? 0.1682 0.2232 0.2702 -0.0563 -0.0664 0.0387  17  THR   A N   
283   C  CA  . THR   A 17  ? 0.1564 0.1987 0.2525 -0.0587 -0.0702 0.0408  17  THR   A CA  
284   C  C   . THR   A 17  ? 0.1792 0.2079 0.2605 -0.0557 -0.0703 0.0373  17  THR   A C   
285   O  O   . THR   A 17  ? 0.1496 0.1813 0.2346 -0.0535 -0.0667 0.0355  17  THR   A O   
286   C  CB  . THR   A 17  ? 0.1477 0.1926 0.2486 -0.0631 -0.0706 0.0456  17  THR   A CB  
287   O  OG1 . THR   A 17  ? 0.1944 0.2413 0.2868 -0.0623 -0.0668 0.0455  17  THR   A OG1 
288   C  CG2 . THR   A 17  ? 0.1866 0.2421 0.2899 -0.0667 -0.0708 0.0496  17  THR   A CG2 
296   N  N   . CYS   A 18  ? 0.1537 0.1725 0.2355 -0.0558 -0.0738 0.0362  18  CYS   A N   
297   C  CA  . CYS   A 18  ? 0.1913 0.1984 0.2611 -0.0533 -0.0739 0.0329  18  CYS   A CA  
298   C  C   . CYS   A 18  ? 0.1889 0.1867 0.2540 -0.0556 -0.0774 0.0341  18  CYS   A C   
299   O  O   . CYS   A 18  ? 0.2190 0.2127 0.2831 -0.0575 -0.0812 0.0346  18  CYS   A O   
300   C  CB  . CYS   A 18  ? 0.2295 0.2321 0.2926 -0.0510 -0.0748 0.0298  18  CYS   A CB  
301   S  SG  . CYS   A 18  ? 0.1992 0.2123 0.2718 -0.0479 -0.0718 0.0285  18  CYS   A SG  
307   N  N   . LYS   A 19  ? 0.1344 0.1294 0.2011 -0.0542 -0.0752 0.0342  19  LYS   A N   
308   C  CA  . LYS   A 19  ? 0.1644 0.1508 0.2275 -0.0577 -0.0804 0.0357  19  LYS   A CA  
309   C  C   . LYS   A 19  ? 0.1822 0.1585 0.2371 -0.0550 -0.0803 0.0316  19  LYS   A C   
310   O  O   . LYS   A 19  ? 0.1917 0.1704 0.2463 -0.0522 -0.0767 0.0299  19  LYS   A O   
311   C  CB  . LYS   A 19  ? 0.1920 0.1835 0.2604 -0.0611 -0.0809 0.0415  19  LYS   A CB  
312   C  CG  . LYS   A 19  ? 0.2352 0.2354 0.3077 -0.0646 -0.0817 0.0458  19  LYS   A CG  
313   C  CD  . LYS   A 19  ? 0.2442 0.2501 0.3219 -0.0687 -0.0822 0.0519  19  LYS   A CD  
314   C  CE  . LYS   A 19  ? 0.2295 0.2459 0.3159 -0.0725 -0.0830 0.0561  19  LYS   A CE  
315   N  NZ  . LYS   A 19  ? 0.2303 0.2500 0.3192 -0.0773 -0.0849 0.0627  19  LYS   A NZ  
329   N  N   . SER   A 20  ? 0.1578 0.1256 0.2136 -0.0556 -0.0843 0.0297  20  SER   A N   
330   C  CA  . SER   A 20  ? 0.1845 0.1439 0.2364 -0.0533 -0.0843 0.0255  20  SER   A CA  
331   C  C   . SER   A 20  ? 0.2240 0.1795 0.2742 -0.0541 -0.0863 0.0287  20  SER   A C   
332   O  O   . SER   A 20  ? 0.2266 0.1831 0.2829 -0.0575 -0.0898 0.0332  20  SER   A O   
333   C  CB  . SER   A 20  ? 0.2219 0.1719 0.2649 -0.0532 -0.0872 0.0204  20  SER   A CB  
334   O  OG  . SER   A 20  ? 0.2286 0.1717 0.2699 -0.0508 -0.0869 0.0157  20  SER   A OG  
340   N  N   . GLU   A 21  ? 0.2078 0.1618 0.2607 -0.0517 -0.0846 0.0269  21  GLU   A N   
341   C  CA  . GLU   A 21  ? 0.2023 0.1528 0.2588 -0.0524 -0.0871 0.0298  21  GLU   A CA  
342   C  C   . GLU   A 21  ? 0.2020 0.1435 0.2567 -0.0490 -0.0879 0.0239  21  GLU   A C   
343   O  O   . GLU   A 21  ? 0.2169 0.1578 0.2660 -0.0462 -0.0845 0.0187  21  GLU   A O   
344   C  CB  . GLU   A 21  ? 0.2198 0.1780 0.2785 -0.0527 -0.0843 0.0348  21  GLU   A CB  
345   C  CG  . GLU   A 21  ? 0.2537 0.2208 0.3116 -0.0563 -0.0834 0.0405  21  GLU   A CG  
346   C  CD  . GLU   A 21  ? 0.2288 0.2054 0.2967 -0.0575 -0.0807 0.0449  21  GLU   A CD  
347   O  OE1 . GLU   A 21  ? 0.2646 0.2374 0.3239 -0.0551 -0.0792 0.0435  21  GLU   A OE1 
348   O  OE2 . GLU   A 21  ? 0.2803 0.2636 0.3430 -0.0610 -0.0801 0.0498  21  GLU   A OE2 
355   N  N   . ASN   A 22  ? 0.2069 0.1417 0.2644 -0.0492 -0.0921 0.0246  22  ASN   A N   
356   C  CA  . ASN   A 22  ? 0.2278 0.1543 0.2850 -0.0458 -0.0928 0.0189  22  ASN   A CA  
357   C  C   . ASN   A 22  ? 0.2400 0.1698 0.2981 -0.0434 -0.0898 0.0196  22  ASN   A C   
358   O  O   . ASN   A 22  ? 0.2437 0.1780 0.3052 -0.0451 -0.0903 0.0260  22  ASN   A O   
359   C  CB  . ASN   A 22  ? 0.2383 0.1557 0.2993 -0.0465 -0.0991 0.0184  22  ASN   A CB  
360   C  CG  . ASN   A 22  ? 0.2610 0.1721 0.3181 -0.0478 -0.1019 0.0142  22  ASN   A CG  
361   O  OD1 . ASN   A 22  ? 0.2542 0.1689 0.3074 -0.0487 -0.0994 0.0124  22  ASN   A OD1 
362   N  ND2 . ASN   A 22  ? 0.2770 0.1793 0.3369 -0.0482 -0.1073 0.0128  22  ASN   A ND2 
369   N  N   . LEU   A 23  ? 0.2322 0.1598 0.2887 -0.0397 -0.0868 0.0134  23  LEU   A N   
370   C  CA  . LEU   A 23  ? 0.2153 0.1462 0.2784 -0.0371 -0.0845 0.0137  23  LEU   A CA  
371   C  C   . LEU   A 23  ? 0.2558 0.1810 0.3211 -0.0367 -0.0891 0.0164  23  LEU   A C   
372   O  O   . LEU   A 23  ? 0.2623 0.1798 0.3301 -0.0363 -0.0932 0.0136  23  LEU   A O   
373   C  CB  . LEU   A 23  ? 0.2410 0.1691 0.2963 -0.0337 -0.0808 0.0062  23  LEU   A CB  
374   C  CG  . LEU   A 23  ? 0.2457 0.1757 0.3030 -0.0308 -0.0784 0.0055  23  LEU   A CG  
375   C  CD1 . LEU   A 23  ? 0.2120 0.1512 0.2702 -0.0315 -0.0746 0.0094  23  LEU   A CD1 
376   C  CD2 . LEU   A 23  ? 0.2571 0.1829 0.3146 -0.0275 -0.0765 -0.0024 23  LEU   A CD2 
388   N  N   . ASP   A 24  ? 0.2794 0.2085 0.3458 -0.0369 -0.0891 0.0216  24  ASP   A N   
389   C  CA  . ASP   A 24  ? 0.2453 0.1716 0.3248 -0.0363 -0.0938 0.0244  24  ASP   A CA  
390   C  C   . ASP   A 24  ? 0.2746 0.1955 0.3490 -0.0314 -0.0922 0.0176  24  ASP   A C   
391   O  O   . ASP   A 24  ? 0.2374 0.1645 0.3177 -0.0301 -0.0888 0.0181  24  ASP   A O   
392   C  CB  . ASP   A 24  ? 0.2608 0.1930 0.3399 -0.0390 -0.0949 0.0329  24  ASP   A CB  
393   C  CG  . ASP   A 24  ? 0.3099 0.2382 0.3931 -0.0390 -0.1006 0.0369  24  ASP   A CG  
394   O  OD1 . ASP   A 24  ? 0.2810 0.2037 0.3715 -0.0355 -0.1025 0.0319  24  ASP   A OD1 
395   O  OD2 . ASP   A 24  ? 0.3656 0.2975 0.4479 -0.0428 -0.1032 0.0448  24  ASP   A OD2 
400   N  N   . LEU   A 25  ? 0.2527 0.1667 0.3354 -0.0291 -0.0942 0.0110  25  LEU   A N   
401   C  CA  . LEU   A 25  ? 0.2592 0.1698 0.3435 -0.0243 -0.0919 0.0035  25  LEU   A CA  
402   C  C   . LEU   A 25  ? 0.2485 0.1607 0.3422 -0.0226 -0.0940 0.0069  25  LEU   A C   
403   O  O   . LEU   A 25  ? 0.2404 0.1547 0.3346 -0.0196 -0.0905 0.0039  25  LEU   A O   
404   C  CB  . LEU   A 25  ? 0.2764 0.1780 0.3618 -0.0223 -0.0937 -0.0047 25  LEU   A CB  
405   C  CG  . LEU   A 25  ? 0.2971 0.1964 0.3860 -0.0174 -0.0903 -0.0143 25  LEU   A CG  
406   C  CD1 . LEU   A 25  ? 0.3049 0.2095 0.3837 -0.0174 -0.0838 -0.0168 25  LEU   A CD1 
407   C  CD2 . LEU   A 25  ? 0.3662 0.2553 0.4493 -0.0156 -0.0920 -0.0224 25  LEU   A CD2 
419   N  N   . ASP   A 26  ? 0.2767 0.1873 0.3741 -0.0248 -0.1000 0.0134  26  ASP   A N   
420   C  CA  . ASP   A 26  ? 0.2944 0.2053 0.3937 -0.0239 -0.1033 0.0180  26  ASP   A CA  
421   C  C   . ASP   A 26  ? 0.2345 0.1559 0.3395 -0.0245 -0.0988 0.0216  26  ASP   A C   
422   O  O   . ASP   A 26  ? 0.2590 0.1810 0.3643 -0.0215 -0.0975 0.0196  26  ASP   A O   
423   C  CB  . ASP   A 26  ? 0.2445 0.1569 0.3653 -0.0274 -0.1110 0.0251  26  ASP   A CB  
424   C  CG  . ASP   A 26  ? 0.4037 0.3030 0.5147 -0.0256 -0.1168 0.0217  26  ASP   A CG  
425   O  OD1 . ASP   A 26  ? 0.3693 0.2654 0.4906 -0.0212 -0.1146 0.0125  26  ASP   A OD1 
426   O  OD2 . ASP   A 26  ? 0.4518 0.3501 0.5716 -0.0288 -0.1237 0.0276  26  ASP   A OD2 
431   N  N   . LYS   A 27  ? 0.2114 0.1388 0.3090 -0.0284 -0.0965 0.0266  27  LYS   A N   
432   C  CA  . LYS   A 27  ? 0.2521 0.1862 0.3394 -0.0291 -0.0923 0.0299  27  LYS   A CA  
433   C  C   . LYS   A 27  ? 0.2090 0.1450 0.2967 -0.0257 -0.0862 0.0232  27  LYS   A C   
434   O  O   . LYS   A 27  ? 0.2187 0.1580 0.3061 -0.0243 -0.0842 0.0235  27  LYS   A O   
435   C  CB  . LYS   A 27  ? 0.2875 0.2278 0.3707 -0.0337 -0.0909 0.0358  27  LYS   A CB  
436   C  CG  . LYS   A 27  ? 0.3293 0.2776 0.4081 -0.0346 -0.0863 0.0384  27  LYS   A CG  
437   C  CD  . LYS   A 27  ? 0.4004 0.3534 0.4683 -0.0388 -0.0843 0.0428  27  LYS   A CD  
438   C  CE  . LYS   A 27  ? 0.3952 0.3476 0.4679 -0.0401 -0.0846 0.0411  27  LYS   A CE  
439   N  NZ  . LYS   A 27  ? 0.4467 0.4033 0.5119 -0.0448 -0.0849 0.0469  27  LYS   A NZ  
453   N  N   . ALA   A 28  ? 0.1723 0.1060 0.2588 -0.0248 -0.0838 0.0171  28  ALA   A N   
454   C  CA  . ALA   A 28  ? 0.2077 0.1415 0.2860 -0.0223 -0.0785 0.0104  28  ALA   A CA  
455   C  C   . ALA   A 28  ? 0.1991 0.1306 0.2858 -0.0182 -0.0783 0.0059  28  ALA   A C   
456   O  O   . ALA   A 28  ? 0.1860 0.1211 0.2721 -0.0167 -0.0745 0.0037  28  ALA   A O   
457   C  CB  . ALA   A 28  ? 0.2265 0.1574 0.2997 -0.0228 -0.0770 0.0053  28  ALA   A CB  
463   N  N   . LYS   A 29  ? 0.2082 0.1335 0.3018 -0.0163 -0.0825 0.0039  29  LYS   A N   
464   C  CA  . LYS   A 29  ? 0.2035 0.1274 0.3098 -0.0121 -0.0827 -0.0006 29  LYS   A CA  
465   C  C   . LYS   A 29  ? 0.2216 0.1490 0.3262 -0.0124 -0.0844 0.0060  29  LYS   A C   
466   O  O   . LYS   A 29  ? 0.1914 0.1225 0.3051 -0.0101 -0.0818 0.0038  29  LYS   A O   
467   C  CB  . LYS   A 29  ? 0.2406 0.1562 0.3512 -0.0096 -0.0866 -0.0056 29  LYS   A CB  
468   C  CG  . LYS   A 29  ? 0.3002 0.2094 0.4025 -0.0080 -0.0842 -0.0145 29  LYS   A CG  
469   C  CD  . LYS   A 29  ? 0.2858 0.1892 0.4040 -0.0061 -0.0886 -0.0190 29  LYS   A CD  
470   C  CE  . LYS   A 29  ? 0.4316 0.3271 0.5339 -0.0035 -0.0857 -0.0297 29  LYS   A CE  
471   N  NZ  . LYS   A 29  ? 0.4715 0.3592 0.5817 -0.0016 -0.0902 -0.0341 29  LYS   A NZ  
485   N  N   . LYS   A 30  ? 0.1852 0.1152 0.2969 -0.0158 -0.0891 0.0140  30  LYS   A N   
486   C  CA  . LYS   A 30  ? 0.1923 0.1268 0.3067 -0.0169 -0.0917 0.0209  30  LYS   A CA  
487   C  C   . LYS   A 30  ? 0.2102 0.1503 0.3137 -0.0175 -0.0865 0.0222  30  LYS   A C   
488   O  O   . LYS   A 30  ? 0.1738 0.1182 0.2877 -0.0164 -0.0869 0.0235  30  LYS   A O   
489   C  CB  . LYS   A 30  ? 0.2095 0.1444 0.3219 -0.0217 -0.0972 0.0292  30  LYS   A CB  
490   C  CG  . LYS   A 30  ? 0.2158 0.1558 0.3330 -0.0239 -0.1009 0.0365  30  LYS   A CG  
491   C  CD  . LYS   A 30  ? 0.2458 0.1859 0.3616 -0.0287 -0.1071 0.0446  30  LYS   A CD  
492   C  CE  . LYS   A 30  ? 0.2614 0.2055 0.3785 -0.0314 -0.1114 0.0514  30  LYS   A CE  
493   N  NZ  . LYS   A 30  ? 0.2282 0.1738 0.3491 -0.0368 -0.1178 0.0592  30  LYS   A NZ  
507   N  N   . PHE   A 31  ? 0.1819 0.1251 0.2796 -0.0191 -0.0823 0.0216  31  PHE   A N   
508   C  CA  . PHE   A 31  ? 0.1547 0.1050 0.2511 -0.0198 -0.0776 0.0225  31  PHE   A CA  
509   C  C   . PHE   A 31  ? 0.1841 0.1315 0.2689 -0.0171 -0.0727 0.0151  31  PHE   A C   
510   O  O   . PHE   A 31  ? 0.1689 0.1219 0.2523 -0.0180 -0.0689 0.0151  31  PHE   A O   
511   C  CB  . PHE   A 31  ? 0.2116 0.1636 0.2890 -0.0238 -0.0770 0.0284  31  PHE   A CB  
512   C  CG  . PHE   A 31  ? 0.1512 0.1074 0.2422 -0.0269 -0.0817 0.0360  31  PHE   A CG  
513   C  CD1 . PHE   A 31  ? 0.1720 0.1307 0.2550 -0.0280 -0.0824 0.0408  31  PHE   A CD1 
514   C  CD2 . PHE   A 31  ? 0.2115 0.1627 0.2948 -0.0291 -0.0860 0.0392  31  PHE   A CD2 
515   C  CE1 . PHE   A 31  ? 0.1839 0.1446 0.2697 -0.0315 -0.0871 0.0480  31  PHE   A CE1 
516   C  CE2 . PHE   A 31  ? 0.2184 0.1720 0.3059 -0.0326 -0.0909 0.0465  31  PHE   A CE2 
517   C  CZ  . PHE   A 31  ? 0.2305 0.1880 0.3137 -0.0340 -0.0914 0.0509  31  PHE   A CZ  
527   N  N   . ILE   A 32  ? 0.1446 0.0881 0.2406 -0.0141 -0.0729 0.0084  32  ILE   A N   
528   C  CA  . ILE   A 32  ? 0.1549 0.0978 0.2493 -0.0120 -0.0686 0.0007  32  ILE   A CA  
529   C  C   . ILE   A 32  ? 0.2152 0.1569 0.2909 -0.0142 -0.0658 -0.0013 32  ILE   A C   
530   O  O   . ILE   A 32  ? 0.1929 0.1323 0.2743 -0.0133 -0.0649 -0.0080 32  ILE   A O   
531   C  CB  . ILE   A 32  ? 0.1510 0.0985 0.2487 -0.0106 -0.0660 0.0006  32  ILE   A CB  
532   C  CG1 . ILE   A 32  ? 0.1686 0.1154 0.2732 -0.0086 -0.0689 0.0032  32  ILE   A CG1 
533   C  CG2 . ILE   A 32  ? 0.1731 0.1196 0.2663 -0.0088 -0.0618 -0.0072 32  ILE   A CG2 
534   C  CD1 . ILE   A 32  ? 0.1600 0.1118 0.2701 -0.0075 -0.0672 0.0042  32  ILE   A CD1 
546   N  N   . GLY   A 33  ? 0.1660 0.1149 0.2440 -0.0168 -0.0644 0.0036  33  GLY   A N   
547   C  CA  . GLY   A 33  ? 0.1750 0.1253 0.2405 -0.0189 -0.0621 0.0022  33  GLY   A CA  
548   C  C   . GLY   A 33  ? 0.1566 0.1139 0.2186 -0.0201 -0.0592 0.0053  33  GLY   A C   
549   O  O   . GLY   A 33  ? 0.1575 0.1176 0.2211 -0.0200 -0.0597 0.0091  33  GLY   A O   
553   N  N   . CYS   A 34  ? 0.1432 0.1030 0.1992 -0.0211 -0.0570 0.0037  34  CYS   A N   
554   C  CA  . CYS   A 34  ? 0.1493 0.1144 0.1982 -0.0219 -0.0545 0.0056  34  CYS   A CA  
555   C  C   . CYS   A 34  ? 0.1254 0.0950 0.1802 -0.0223 -0.0549 0.0110  34  CYS   A C   
556   O  O   . CYS   A 34  ? 0.1518 0.1209 0.2023 -0.0239 -0.0561 0.0144  34  CYS   A O   
557   C  CB  . CYS   A 34  ? 0.1424 0.1089 0.1924 -0.0207 -0.0526 0.0019  34  CYS   A CB  
558   S  SG  . CYS   A 34  ? 0.1449 0.1172 0.1888 -0.0215 -0.0502 0.0028  34  CYS   A SG  
564   N  N   . ARG   A 35  ? 0.1381 0.1094 0.1907 -0.0211 -0.0537 0.0119  35  ARG   A N   
565   C  CA  . ARG   A 35  ? 0.1542 0.1280 0.2039 -0.0219 -0.0540 0.0163  35  ARG   A CA  
566   C  C   . ARG   A 35  ? 0.1352 0.1080 0.1915 -0.0235 -0.0570 0.0206  35  ARG   A C   
567   O  O   . ARG   A 35  ? 0.1277 0.1032 0.1810 -0.0258 -0.0569 0.0237  35  ARG   A O   
568   C  CB  . ARG   A 35  ? 0.1268 0.1023 0.1819 -0.0205 -0.0536 0.0165  35  ARG   A CB  
569   C  CG  . ARG   A 35  ? 0.1058 0.0843 0.1617 -0.0215 -0.0538 0.0202  35  ARG   A CG  
570   C  CD  . ARG   A 35  ? 0.1295 0.1085 0.1839 -0.0200 -0.0533 0.0201  35  ARG   A CD  
571   N  NE  . ARG   A 35  ? 0.1348 0.1155 0.1901 -0.0211 -0.0543 0.0238  35  ARG   A NE  
572   C  CZ  . ARG   A 35  ? 0.1515 0.1320 0.2055 -0.0202 -0.0546 0.0245  35  ARG   A CZ  
573   N  NH1 . ARG   A 35  ? 0.1315 0.1136 0.1924 -0.0187 -0.0535 0.0217  35  ARG   A NH1 
574   N  NH2 . ARG   A 35  ? 0.1310 0.1126 0.1877 -0.0218 -0.0561 0.0282  35  ARG   A NH2 
588   N  N   . GLY   A 36  ? 0.1417 0.1102 0.2036 -0.0223 -0.0598 0.0204  36  GLY   A N   
589   C  CA  . GLY   A 36  ? 0.1536 0.1201 0.2181 -0.0236 -0.0637 0.0251  36  GLY   A CA  
590   C  C   . GLY   A 36  ? 0.1526 0.1181 0.2160 -0.0261 -0.0651 0.0266  36  GLY   A C   
591   O  O   . GLY   A 36  ? 0.1394 0.1068 0.2023 -0.0291 -0.0668 0.0318  36  GLY   A O   
595   N  N   . LEU   A 37  ? 0.1670 0.1293 0.2279 -0.0254 -0.0641 0.0222  37  LEU   A N   
596   C  CA  . LEU   A 37  ? 0.1476 0.1097 0.2096 -0.0275 -0.0656 0.0232  37  LEU   A CA  
597   C  C   . LEU   A 37  ? 0.1446 0.1127 0.2005 -0.0302 -0.0633 0.0264  37  LEU   A C   
598   O  O   . LEU   A 37  ? 0.1629 0.1327 0.2179 -0.0333 -0.0649 0.0307  37  LEU   A O   
599   C  CB  . LEU   A 37  ? 0.1557 0.1133 0.2162 -0.0262 -0.0651 0.0177  37  LEU   A CB  
600   C  CG  . LEU   A 37  ? 0.1728 0.1291 0.2285 -0.0286 -0.0664 0.0181  37  LEU   A CG  
601   C  CD1 . LEU   A 37  ? 0.1553 0.1090 0.2179 -0.0303 -0.0709 0.0223  37  LEU   A CD1 
602   C  CD2 . LEU   A 37  ? 0.1598 0.1130 0.2159 -0.0275 -0.0656 0.0121  37  LEU   A CD2 
614   N  N   . GLY   A 38  ? 0.1248 0.0972 0.1777 -0.0292 -0.0595 0.0240  38  GLY   A N   
615   C  CA  . GLY   A 38  ? 0.1205 0.0995 0.1713 -0.0312 -0.0571 0.0258  38  GLY   A CA  
616   C  C   . GLY   A 38  ? 0.1553 0.1377 0.2008 -0.0338 -0.0576 0.0305  38  GLY   A C   
617   O  O   . GLY   A 38  ? 0.1433 0.1317 0.1917 -0.0368 -0.0571 0.0333  38  GLY   A O   
621   N  N   . VAL   A 39  ? 0.1398 0.1215 0.1888 -0.0329 -0.0583 0.0319  39  VAL   A N   
622   C  CA  . VAL   A 39  ? 0.1222 0.1084 0.1701 -0.0358 -0.0589 0.0367  39  VAL   A CA  
623   C  C   . VAL   A 39  ? 0.1037 0.0902 0.1583 -0.0389 -0.0619 0.0421  39  VAL   A C   
624   O  O   . VAL   A 39  ? 0.1577 0.1488 0.2019 -0.0437 -0.0620 0.0459  39  VAL   A O   
625   C  CB  . VAL   A 39  ? 0.1273 0.1120 0.1768 -0.0344 -0.0595 0.0372  39  VAL   A CB  
626   C  CG1 . VAL   A 39  ? 0.1612 0.1486 0.2055 -0.0381 -0.0611 0.0426  39  VAL   A CG1 
627   C  CG2 . VAL   A 39  ? 0.1331 0.1188 0.1790 -0.0314 -0.0564 0.0324  39  VAL   A CG2 
637   N  N   . LYS   A 40  ? 0.1567 0.1348 0.2075 -0.0380 -0.0662 0.0427  40  LYS   A N   
638   C  CA  . LYS   A 40  ? 0.1530 0.1301 0.2099 -0.0412 -0.0707 0.0480  40  LYS   A CA  
639   C  C   . LYS   A 40  ? 0.1436 0.1245 0.1986 -0.0442 -0.0695 0.0492  40  LYS   A C   
640   O  O   . LYS   A 40  ? 0.1445 0.1294 0.1977 -0.0489 -0.0711 0.0547  40  LYS   A O   
641   C  CB  . LYS   A 40  ? 0.1774 0.1464 0.2392 -0.0384 -0.0751 0.0467  40  LYS   A CB  
642   C  CG  . LYS   A 40  ? 0.1932 0.1601 0.2603 -0.0412 -0.0810 0.0519  40  LYS   A CG  
643   C  CD  . LYS   A 40  ? 0.2394 0.2095 0.3065 -0.0447 -0.0843 0.0594  40  LYS   A CD  
644   C  CE  . LYS   A 40  ? 0.3187 0.2851 0.3857 -0.0472 -0.0912 0.0646  40  LYS   A CE  
645   N  NZ  . LYS   A 40  ? 0.3378 0.3108 0.4033 -0.0534 -0.0933 0.0726  40  LYS   A NZ  
659   N  N   . THR   A 41  ? 0.1530 0.1329 0.2068 -0.0421 -0.0671 0.0439  41  THR   A N   
660   C  CA  . THR   A 41  ? 0.1627 0.1460 0.2133 -0.0447 -0.0659 0.0442  41  THR   A CA  
661   C  C   . THR   A 41  ? 0.1317 0.1268 0.1850 -0.0482 -0.0629 0.0468  41  THR   A C   
662   O  O   . THR   A 41  ? 0.1563 0.1558 0.2059 -0.0524 -0.0635 0.0513  41  THR   A O   
663   C  CB  . THR   A 41  ? 0.1536 0.1352 0.2092 -0.0417 -0.0643 0.0383  41  THR   A CB  
664   O  OG1 . THR   A 41  ? 0.1707 0.1433 0.2251 -0.0392 -0.0672 0.0354  41  THR   A OG1 
665   C  CG2 . THR   A 41  ? 0.1822 0.1671 0.2339 -0.0442 -0.0639 0.0388  41  THR   A CG2 
673   N  N   . LEU   A 42  ? 0.1355 0.1339 0.1833 -0.0461 -0.0593 0.0438  42  LEU   A N   
674   C  CA  . LEU   A 42  ? 0.1294 0.1393 0.1776 -0.0489 -0.0563 0.0444  42  LEU   A CA  
675   C  C   . LEU   A 42  ? 0.1527 0.1661 0.1953 -0.0539 -0.0579 0.0514  42  LEU   A C   
676   O  O   . LEU   A 42  ? 0.1466 0.1703 0.1913 -0.0581 -0.0567 0.0542  42  LEU   A O   
677   C  CB  . LEU   A 42  ? 0.1360 0.1472 0.1794 -0.0455 -0.0532 0.0395  42  LEU   A CB  
678   C  CG  . LEU   A 42  ? 0.1152 0.1393 0.1635 -0.0473 -0.0504 0.0382  42  LEU   A CG  
679   C  CD1 . LEU   A 42  ? 0.1600 0.1889 0.2049 -0.0467 -0.0485 0.0354  42  LEU   A CD1 
680   C  CD2 . LEU   A 42  ? 0.1419 0.1647 0.1821 -0.0444 -0.0492 0.0348  42  LEU   A CD2 
692   N  N   . PHE   A 43  ? 0.1368 0.1449 0.1815 -0.0534 -0.0606 0.0539  43  PHE   A N   
693   C  CA  . PHE   A 43  ? 0.1423 0.1537 0.1850 -0.0581 -0.0633 0.0608  43  PHE   A CA  
694   C  C   . PHE   A 43  ? 0.1615 0.1747 0.2060 -0.0627 -0.0663 0.0666  43  PHE   A C   
695   O  O   . PHE   A 43  ? 0.1812 0.2025 0.2200 -0.0683 -0.0662 0.0719  43  PHE   A O   
696   C  CB  . PHE   A 43  ? 0.1568 0.1601 0.2001 -0.0562 -0.0669 0.0624  43  PHE   A CB  
697   C  CG  . PHE   A 43  ? 0.2065 0.2120 0.2391 -0.0604 -0.0690 0.0681  43  PHE   A CG  
698   C  CD1 . PHE   A 43  ? 0.1686 0.1870 0.2049 -0.0666 -0.0677 0.0723  43  PHE   A CD1 
699   C  CD2 . PHE   A 43  ? 0.1877 0.1878 0.2263 -0.0585 -0.0726 0.0700  43  PHE   A CD2 
700   C  CE1 . PHE   A 43  ? 0.2038 0.2248 0.2292 -0.0712 -0.0698 0.0779  43  PHE   A CE1 
701   C  CE2 . PHE   A 43  ? 0.1683 0.1719 0.2044 -0.0628 -0.0752 0.0757  43  PHE   A CE2 
702   C  CZ  . PHE   A 43  ? 0.1832 0.1970 0.2121 -0.0694 -0.0738 0.0797  43  PHE   A CZ  
712   N  N   . ASP   A 44  ? 0.2002 0.2043 0.2438 -0.0602 -0.0689 0.0657  44  ASP   A N   
713   C  CA  . ASP   A 44  ? 0.1779 0.1832 0.2292 -0.0642 -0.0727 0.0707  44  ASP   A CA  
714   C  C   . ASP   A 44  ? 0.1985 0.2131 0.2453 -0.0675 -0.0692 0.0712  44  ASP   A C   
715   O  O   . ASP   A 44  ? 0.2086 0.2272 0.2570 -0.0723 -0.0716 0.0772  44  ASP   A O   
716   C  CB  . ASP   A 44  ? 0.1866 0.1802 0.2407 -0.0606 -0.0768 0.0687  44  ASP   A CB  
717   C  CG  . ASP   A 44  ? 0.2102 0.1950 0.2671 -0.0580 -0.0818 0.0694  44  ASP   A CG  
718   O  OD1 . ASP   A 44  ? 0.2254 0.2124 0.2799 -0.0600 -0.0837 0.0738  44  ASP   A OD1 
719   O  OD2 . ASP   A 44  ? 0.2230 0.1994 0.2833 -0.0542 -0.0841 0.0655  44  ASP   A OD2 
724   N  N   . GLU   A 45  ? 0.1778 0.1980 0.2279 -0.0651 -0.0640 0.0653  45  GLU   A N   
725   C  CA  . GLU   A 45  ? 0.1901 0.2196 0.2400 -0.0674 -0.0609 0.0644  45  GLU   A CA  
726   C  C   . GLU   A 45  ? 0.1958 0.2405 0.2445 -0.0694 -0.0558 0.0635  45  GLU   A C   
727   O  O   . GLU   A 45  ? 0.2308 0.2856 0.2813 -0.0714 -0.0533 0.0632  45  GLU   A O   
728   C  CB  . GLU   A 45  ? 0.1846 0.2090 0.2399 -0.0628 -0.0603 0.0586  45  GLU   A CB  
729   C  CG  . GLU   A 45  ? 0.2172 0.2278 0.2704 -0.0607 -0.0648 0.0583  45  GLU   A CG  
730   C  CD  . GLU   A 45  ? 0.2180 0.2248 0.2734 -0.0580 -0.0648 0.0535  45  GLU   A CD  
731   O  OE1 . GLU   A 45  ? 0.1879 0.2025 0.2473 -0.0574 -0.0611 0.0504  45  GLU   A OE1 
732   O  OE2 . GLU   A 45  ? 0.2165 0.2138 0.2742 -0.0565 -0.0683 0.0527  45  GLU   A OE2 
739   N  N   . ILE   A 46  ? 0.1572 0.2047 0.2044 -0.0692 -0.0545 0.0628  46  ILE   A N   
740   C  CA  . ILE   A 46  ? 0.1539 0.2176 0.2017 -0.0716 -0.0498 0.0611  46  ILE   A CA  
741   C  C   . ILE   A 46  ? 0.1966 0.2637 0.2291 -0.0763 -0.0502 0.0659  46  ILE   A C   
742   O  O   . ILE   A 46  ? 0.1544 0.2124 0.1916 -0.0761 -0.0543 0.0692  46  ILE   A O   
743   C  CB  . ILE   A 46  ? 0.1861 0.2497 0.2302 -0.0659 -0.0466 0.0528  46  ILE   A CB  
744   C  CG1 . ILE   A 46  ? 0.1931 0.2492 0.2343 -0.0631 -0.0477 0.0504  46  ILE   A CG1 
745   C  CG2 . ILE   A 46  ? 0.1720 0.2298 0.2234 -0.0615 -0.0469 0.0486  46  ILE   A CG2 
746   C  CD1 . ILE   A 46  ? 0.1812 0.2437 0.2235 -0.0600 -0.0449 0.0442  46  ILE   A CD1 
758   N  N   . ASP   A 47  ? 0.1683 0.2540 0.2063 -0.0805 -0.0461 0.0662  47  ASP   A N   
759   C  CA  . ASP   A 47  ? 0.1891 0.2815 0.2168 -0.0853 -0.0459 0.0695  47  ASP   A CA  
760   C  C   . ASP   A 47  ? 0.1937 0.2857 0.2177 -0.0812 -0.0440 0.0622  47  ASP   A C   
761   O  O   . ASP   A 47  ? 0.1443 0.2480 0.1770 -0.0789 -0.0397 0.0559  47  ASP   A O   
762   C  CB  . ASP   A 47  ? 0.1915 0.3031 0.2169 -0.0923 -0.0421 0.0730  47  ASP   A CB  
763   C  CG  . ASP   A 47  ? 0.1958 0.3213 0.2193 -0.0969 -0.0395 0.0731  47  ASP   A CG  
764   O  OD1 . ASP   A 47  ? 0.2280 0.3428 0.2390 -0.0967 -0.0430 0.0743  47  ASP   A OD1 
765   O  OD2 . ASP   A 47  ? 0.2905 0.4326 0.3020 -0.1005 -0.0337 0.0716  47  ASP   A OD2 
770   N  N   . PRO   A 48  ? 0.1827 0.2639 0.2059 -0.0793 -0.0476 0.0627  48  PRO   A N   
771   C  CA  . PRO   A 48  ? 0.1653 0.2451 0.1885 -0.0747 -0.0466 0.0556  48  PRO   A CA  
772   C  C   . PRO   A 48  ? 0.1719 0.2659 0.1876 -0.0755 -0.0419 0.0506  48  PRO   A C   
773   O  O   . PRO   A 48  ? 0.1630 0.2541 0.1786 -0.0694 -0.0403 0.0432  48  PRO   A O   
774   C  CB  . PRO   A 48  ? 0.1722 0.2386 0.1930 -0.0742 -0.0512 0.0594  48  PRO   A CB  
775   C  CG  . PRO   A 48  ? 0.2216 0.2775 0.2387 -0.0752 -0.0547 0.0659  48  PRO   A CG  
776   C  CD  . PRO   A 48  ? 0.1895 0.2586 0.2117 -0.0812 -0.0529 0.0697  48  PRO   A CD  
784   N  N   . LYS   A 49  ? 0.1738 0.2826 0.1868 -0.0817 -0.0390 0.0538  49  LYS   A N   
785   C  CA  . LYS   A 49  ? 0.2012 0.3228 0.2039 -0.0813 -0.0329 0.0481  49  LYS   A CA  
786   C  C   . LYS   A 49  ? 0.1904 0.3214 0.2019 -0.0756 -0.0270 0.0394  49  LYS   A C   
787   O  O   . LYS   A 49  ? 0.2225 0.3616 0.2271 -0.0728 -0.0220 0.0321  49  LYS   A O   
788   C  CB  . LYS   A 49  ? 0.2033 0.3390 0.2017 -0.0907 -0.0316 0.0551  49  LYS   A CB  
789   C  CG  . LYS   A 49  ? 0.2405 0.3693 0.2295 -0.0974 -0.0376 0.0643  49  LYS   A CG  
790   C  CD  . LYS   A 49  ? 0.2681 0.4112 0.2465 -0.1067 -0.0356 0.0702  49  LYS   A CD  
791   C  CE  . LYS   A 49  ? 0.2586 0.4183 0.2418 -0.1114 -0.0309 0.0729  49  LYS   A CE  
792   N  NZ  . LYS   A 49  ? 0.2406 0.3930 0.2316 -0.1145 -0.0365 0.0818  49  LYS   A NZ  
806   N  N   . ILE   A 50  ? 0.1683 0.2968 0.1894 -0.0740 -0.0279 0.0401  50  ILE   A N   
807   C  CA  . ILE   A 50  ? 0.1500 0.2881 0.1800 -0.0693 -0.0231 0.0334  50  ILE   A CA  
808   C  C   . ILE   A 50  ? 0.1359 0.2688 0.1671 -0.0604 -0.0217 0.0231  50  ILE   A C   
809   O  O   . ILE   A 50  ? 0.1428 0.2613 0.1684 -0.0575 -0.0255 0.0224  50  ILE   A O   
810   C  CB  . ILE   A 50  ? 0.1703 0.3052 0.2116 -0.0699 -0.0258 0.0372  50  ILE   A CB  
811   C  CG1 . ILE   A 50  ? 0.1744 0.2904 0.2199 -0.0659 -0.0316 0.0371  50  ILE   A CG1 
812   C  CG2 . ILE   A 50  ? 0.2262 0.3673 0.2641 -0.0789 -0.0269 0.0467  50  ILE   A CG2 
813   C  CD1 . ILE   A 50  ? 0.2441 0.3542 0.2919 -0.0649 -0.0339 0.0381  50  ILE   A CD1 
825   N  N   . ASP   A 51  ? 0.1523 0.2956 0.1865 -0.0559 -0.0166 0.0153  51  ASP   A N   
826   C  CA  . ASP   A 51  ? 0.1650 0.3024 0.2022 -0.0473 -0.0163 0.0059  51  ASP   A CA  
827   C  C   . ASP   A 51  ? 0.1411 0.2653 0.1875 -0.0440 -0.0214 0.0073  51  ASP   A C   
828   O  O   . ASP   A 51  ? 0.1414 0.2687 0.1938 -0.0460 -0.0219 0.0109  51  ASP   A O   
829   C  CB  . ASP   A 51  ? 0.1885 0.3416 0.2325 -0.0432 -0.0103 -0.0025 51  ASP   A CB  
830   C  CG  . ASP   A 51  ? 0.2419 0.3892 0.2911 -0.0343 -0.0109 -0.0114 51  ASP   A CG  
831   O  OD1 . ASP   A 51  ? 0.1768 0.3090 0.2283 -0.0313 -0.0157 -0.0117 51  ASP   A OD1 
832   O  OD2 . ASP   A 51  ? 0.3505 0.5087 0.4023 -0.0305 -0.0068 -0.0179 51  ASP   A OD2 
837   N  N   . ALA   A 52  ? 0.1446 0.2546 0.1894 -0.0396 -0.0250 0.0047  52  ALA   A N   
838   C  CA  . ALA   A 52  ? 0.1733 0.2683 0.2147 -0.0373 -0.0296 0.0059  52  ALA   A CA  
839   C  C   . ALA   A 52  ? 0.1059 0.2071 0.1683 -0.0330 -0.0290 0.0022  52  ALA   A C   
840   O  O   . ALA   A 52  ? 0.0950 0.1876 0.1588 -0.0324 -0.0326 0.0043  52  ALA   A O   
841   C  CB  . ALA   A 52  ? 0.1209 0.2048 0.1676 -0.0340 -0.0327 0.0041  52  ALA   A CB  
847   N  N   . LEU   A 53  ? 0.1225 0.2347 0.1856 -0.0300 -0.0249 -0.0040 53  LEU   A N   
848   C  CA  . LEU   A 53  ? 0.1421 0.2584 0.2134 -0.0253 -0.0246 -0.0083 53  LEU   A CA  
849   C  C   . LEU   A 53  ? 0.1172 0.2494 0.1995 -0.0293 -0.0215 -0.0050 53  LEU   A C   
850   O  O   . LEU   A 53  ? 0.1127 0.2505 0.2048 -0.0263 -0.0215 -0.0074 53  LEU   A O   
851   C  CB  . LEU   A 53  ? 0.1228 0.2424 0.2006 -0.0187 -0.0230 -0.0176 53  LEU   A CB  
852   C  CG  . LEU   A 53  ? 0.1365 0.2403 0.2070 -0.0150 -0.0269 -0.0205 53  LEU   A CG  
853   C  CD1 . LEU   A 53  ? 0.1527 0.2584 0.2261 -0.0085 -0.0259 -0.0297 53  LEU   A CD1 
854   C  CD2 . LEU   A 53  ? 0.1100 0.2013 0.1854 -0.0146 -0.0325 -0.0166 53  LEU   A CD2 
866   N  N   . SER   A 54  ? 0.1141 0.2525 0.1902 -0.0361 -0.0196 0.0011  54  SER   A N   
867   C  CA  . SER   A 54  ? 0.1068 0.2597 0.1897 -0.0412 -0.0173 0.0059  54  SER   A CA  
868   C  C   . SER   A 54  ? 0.1048 0.2490 0.1930 -0.0435 -0.0225 0.0117  54  SER   A C   
869   O  O   . SER   A 54  ? 0.1167 0.2447 0.1995 -0.0437 -0.0273 0.0142  54  SER   A O   
870   C  CB  . SER   A 54  ? 0.1243 0.2855 0.1989 -0.0487 -0.0144 0.0112  54  SER   A CB  
871   O  OG  . SER   A 54  ? 0.1558 0.3041 0.2228 -0.0537 -0.0195 0.0191  54  SER   A OG  
877   N  N   . PRO   A 55  ? 0.0931 0.2492 0.1985 -0.0456 -0.0218 0.0139  55  PRO   A N   
878   C  CA  . PRO   A 55  ? 0.1309 0.2764 0.2323 -0.0480 -0.0272 0.0194  55  PRO   A CA  
879   C  C   . PRO   A 55  ? 0.1433 0.2750 0.2338 -0.0531 -0.0298 0.0261  55  PRO   A C   
880   O  O   . PRO   A 55  ? 0.1336 0.2508 0.2248 -0.0525 -0.0338 0.0281  55  PRO   A O   
881   C  CB  . PRO   A 55  ? 0.1281 0.2884 0.2421 -0.0494 -0.0244 0.0202  55  PRO   A CB  
882   C  CG  . PRO   A 55  ? 0.1553 0.3339 0.2740 -0.0455 -0.0187 0.0133  55  PRO   A CG  
883   C  CD  . PRO   A 55  ? 0.1843 0.3583 0.2855 -0.0451 -0.0160 0.0110  55  PRO   A CD  
891   N  N   . GLU   A 56  ? 0.1218 0.2605 0.2110 -0.0577 -0.0277 0.0296  56  GLU   A N   
892   C  CA  . GLU   A 56  ? 0.1721 0.2976 0.2448 -0.0625 -0.0305 0.0366  56  GLU   A CA  
893   C  C   . GLU   A 56  ? 0.1582 0.2658 0.2276 -0.0594 -0.0346 0.0357  56  GLU   A C   
894   O  O   . GLU   A 56  ? 0.1412 0.2365 0.2078 -0.0613 -0.0378 0.0403  56  GLU   A O   
895   C  CB  . GLU   A 56  ? 0.1471 0.2868 0.2227 -0.0688 -0.0275 0.0413  56  GLU   A CB  
896   C  CG  . GLU   A 56  ? 0.1905 0.3450 0.2662 -0.0727 -0.0238 0.0439  56  GLU   A CG  
897   C  CD  . GLU   A 56  ? 0.2056 0.3766 0.2883 -0.0689 -0.0187 0.0373  56  GLU   A CD  
898   O  OE1 . GLU   A 56  ? 0.1713 0.3530 0.2595 -0.0660 -0.0152 0.0309  56  GLU   A OE1 
899   O  OE2 . GLU   A 56  ? 0.1718 0.3479 0.2683 -0.0685 -0.0185 0.0377  56  GLU   A OE2 
906   N  N   . ASN   A 57  ? 0.1338 0.2406 0.2067 -0.0546 -0.0345 0.0295  57  ASN   A N   
907   C  CA  . ASN   A 57  ? 0.1505 0.2389 0.2144 -0.0511 -0.0379 0.0280  57  ASN   A CA  
908   C  C   . ASN   A 57  ? 0.1493 0.2246 0.2152 -0.0489 -0.0405 0.0285  57  ASN   A C   
909   O  O   . ASN   A 57  ? 0.1416 0.2220 0.2147 -0.0487 -0.0404 0.0280  57  ASN   A O   
910   C  CB  . ASN   A 57  ? 0.1276 0.2170 0.1935 -0.0463 -0.0374 0.0219  57  ASN   A CB  
911   C  CG  . ASN   A 57  ? 0.1177 0.1921 0.1770 -0.0440 -0.0403 0.0211  57  ASN   A CG  
912   O  OD1 . ASN   A 57  ? 0.1211 0.1849 0.1757 -0.0453 -0.0418 0.0251  57  ASN   A OD1 
913   N  ND2 . ASN   A 57  ? 0.1134 0.1853 0.1710 -0.0393 -0.0397 0.0159  57  ASN   A ND2 
920   N  N   . LYS   A 58  ? 0.1357 0.1962 0.1974 -0.0475 -0.0429 0.0292  58  LYS   A N   
921   C  CA  . LYS   A 58  ? 0.1242 0.1730 0.1861 -0.0452 -0.0450 0.0286  58  LYS   A CA  
922   C  C   . LYS   A 58  ? 0.1073 0.1479 0.1684 -0.0402 -0.0455 0.0241  58  LYS   A C   
923   O  O   . LYS   A 58  ? 0.1391 0.1755 0.1922 -0.0392 -0.0453 0.0235  58  LYS   A O   
924   C  CB  . LYS   A 58  ? 0.1504 0.1907 0.2090 -0.0480 -0.0474 0.0336  58  LYS   A CB  
925   C  CG  . LYS   A 58  ? 0.1806 0.2279 0.2392 -0.0534 -0.0476 0.0393  58  LYS   A CG  
926   C  CD  . LYS   A 58  ? 0.1805 0.2219 0.2412 -0.0553 -0.0505 0.0426  58  LYS   A CD  
927   C  CE  . LYS   A 58  ? 0.1714 0.2222 0.2385 -0.0609 -0.0508 0.0485  58  LYS   A CE  
928   N  NZ  . LYS   A 58  ? 0.2424 0.2833 0.3025 -0.0629 -0.0548 0.0525  58  LYS   A NZ  
942   N  N   . PHE   A 59  ? 0.1138 0.1505 0.1740 -0.0376 -0.0461 0.0214  59  PHE   A N   
943   C  CA  . PHE   A 59  ? 0.1293 0.1580 0.1859 -0.0335 -0.0465 0.0177  59  PHE   A CA  
944   C  C   . PHE   A 59  ? 0.1260 0.1435 0.1783 -0.0334 -0.0482 0.0186  59  PHE   A C   
945   O  O   . PHE   A 59  ? 0.1326 0.1486 0.1861 -0.0342 -0.0493 0.0191  59  PHE   A O   
946   C  CB  . PHE   A 59  ? 0.1414 0.1741 0.2005 -0.0312 -0.0466 0.0145  59  PHE   A CB  
947   C  CG  . PHE   A 59  ? 0.1215 0.1476 0.1795 -0.0274 -0.0471 0.0117  59  PHE   A CG  
948   C  CD1 . PHE   A 59  ? 0.1083 0.1348 0.1663 -0.0255 -0.0466 0.0095  59  PHE   A CD1 
949   C  CD2 . PHE   A 59  ? 0.1276 0.1473 0.1849 -0.0266 -0.0485 0.0113  59  PHE   A CD2 
950   C  CE1 . PHE   A 59  ? 0.1408 0.1601 0.1924 -0.0226 -0.0471 0.0079  59  PHE   A CE1 
951   C  CE2 . PHE   A 59  ? 0.1736 0.1863 0.2222 -0.0242 -0.0490 0.0097  59  PHE   A CE2 
952   C  CZ  . PHE   A 59  ? 0.1447 0.1585 0.1970 -0.0221 -0.0482 0.0080  59  PHE   A CZ  
962   N  N   . ILE   A 60  ? 0.1090 0.1203 0.1596 -0.0327 -0.0482 0.0188  60  ILE   A N   
963   C  CA  . ILE   A 60  ? 0.1267 0.1283 0.1727 -0.0324 -0.0499 0.0191  60  ILE   A CA  
964   C  C   . ILE   A 60  ? 0.1500 0.1458 0.1903 -0.0294 -0.0495 0.0158  60  ILE   A C   
965   O  O   . ILE   A 60  ? 0.1368 0.1339 0.1793 -0.0277 -0.0482 0.0148  60  ILE   A O   
966   C  CB  . ILE   A 60  ? 0.1173 0.1160 0.1648 -0.0340 -0.0511 0.0221  60  ILE   A CB  
967   C  CG1 . ILE   A 60  ? 0.1218 0.1263 0.1733 -0.0377 -0.0517 0.0264  60  ILE   A CG1 
968   C  CG2 . ILE   A 60  ? 0.1297 0.1193 0.1742 -0.0330 -0.0529 0.0212  60  ILE   A CG2 
969   C  CD1 . ILE   A 60  ? 0.1847 0.1856 0.2301 -0.0396 -0.0533 0.0302  60  ILE   A CD1 
981   N  N   . ILE   A 61  ? 0.1308 0.1232 0.1731 -0.0293 -0.0508 0.0145  61  ILE   A N   
982   C  CA  . ILE   A 61  ? 0.1309 0.1184 0.1677 -0.0275 -0.0507 0.0118  61  ILE   A CA  
983   C  C   . ILE   A 61  ? 0.1082 0.0907 0.1479 -0.0278 -0.0521 0.0108  61  ILE   A C   
984   O  O   . ILE   A 61  ? 0.1333 0.1130 0.1694 -0.0296 -0.0537 0.0111  61  ILE   A O   
985   C  CB  . ILE   A 61  ? 0.1349 0.1239 0.1741 -0.0270 -0.0512 0.0106  61  ILE   A CB  
986   C  CG1 . ILE   A 61  ? 0.1541 0.1486 0.1956 -0.0262 -0.0505 0.0110  61  ILE   A CG1 
987   C  CG2 . ILE   A 61  ? 0.1839 0.1677 0.2134 -0.0264 -0.0512 0.0085  61  ILE   A CG2 
988   C  CD1 . ILE   A 61  ? 0.2287 0.2233 0.2652 -0.0263 -0.0520 0.0109  61  ILE   A CD1 
1000  N  N   . VAL   A 62  ? 0.1221 0.1013 0.1588 -0.0269 -0.0515 0.0096  62  VAL   A N   
1001  C  CA  . VAL   A 62  ? 0.1435 0.1171 0.1802 -0.0267 -0.0530 0.0084  62  VAL   A CA  
1002  C  C   . VAL   A 62  ? 0.1305 0.1019 0.1681 -0.0257 -0.0524 0.0043  62  VAL   A C   
1003  O  O   . VAL   A 62  ? 0.1385 0.1119 0.1728 -0.0247 -0.0507 0.0041  62  VAL   A O   
1004  C  CB  . VAL   A 62  ? 0.1628 0.1356 0.2016 -0.0269 -0.0540 0.0112  62  VAL   A CB  
1005  C  CG1 . VAL   A 62  ? 0.1400 0.1165 0.1828 -0.0256 -0.0522 0.0124  62  VAL   A CG1 
1006  C  CG2 . VAL   A 62  ? 0.1520 0.1195 0.1966 -0.0265 -0.0562 0.0098  62  VAL   A CG2 
1016  N  N   . THR   A 63  ? 0.1559 0.1219 0.1895 -0.0262 -0.0537 0.0007  63  THR   A N   
1017  C  CA  . THR   A 63  ? 0.1651 0.1286 0.1976 -0.0257 -0.0531 -0.0040 63  THR   A CA  
1018  C  C   . THR   A 63  ? 0.1492 0.1094 0.1907 -0.0241 -0.0539 -0.0059 63  THR   A C   
1019  O  O   . THR   A 63  ? 0.1630 0.1213 0.2052 -0.0237 -0.0556 -0.0027 63  THR   A O   
1020  C  CB  . THR   A 63  ? 0.1833 0.1436 0.2106 -0.0273 -0.0540 -0.0081 63  THR   A CB  
1021  O  OG1 . THR   A 63  ? 0.1871 0.1426 0.2164 -0.0275 -0.0561 -0.0092 63  THR   A OG1 
1022  C  CG2 . THR   A 63  ? 0.1959 0.1596 0.2183 -0.0288 -0.0541 -0.0060 63  THR   A CG2 
1030  N  N   . GLY   A 64  ? 0.1795 0.1368 0.2170 -0.0232 -0.0531 -0.0109 64  GLY   A N   
1031  C  CA  . GLY   A 64  ? 0.1713 0.1246 0.2175 -0.0209 -0.0539 -0.0142 64  GLY   A CA  
1032  C  C   . GLY   A 64  ? 0.1706 0.1178 0.2158 -0.0205 -0.0547 -0.0215 64  GLY   A C   
1033  O  O   . GLY   A 64  ? 0.1891 0.1360 0.2252 -0.0224 -0.0541 -0.0243 64  GLY   A O   
1037  N  N   . PRO   A 65  ? 0.1656 0.1080 0.2209 -0.0177 -0.0560 -0.0248 65  PRO   A N   
1038  C  CA  . PRO   A 65  ? 0.2056 0.1403 0.2527 -0.0164 -0.0561 -0.0331 65  PRO   A CA  
1039  C  C   . PRO   A 65  ? 0.1746 0.1133 0.2216 -0.0160 -0.0523 -0.0408 65  PRO   A C   
1040  O  O   . PRO   A 65  ? 0.1845 0.1191 0.2219 -0.0165 -0.0522 -0.0471 65  PRO   A O   
1041  C  CB  . PRO   A 65  ? 0.2059 0.1370 0.2671 -0.0125 -0.0577 -0.0345 65  PRO   A CB  
1042  C  CG  . PRO   A 65  ? 0.2062 0.1420 0.2732 -0.0116 -0.0574 -0.0285 65  PRO   A CG  
1043  C  CD  . PRO   A 65  ? 0.1941 0.1353 0.2545 -0.0155 -0.0572 -0.0212 65  PRO   A CD  
1051  N  N   . LEU   A 66  ? 0.1939 0.1404 0.2377 -0.0146 -0.0478 -0.0391 66  LEU   A N   
1052  C  CA  . LEU   A 66  ? 0.2036 0.1568 0.2410 -0.0141 -0.0422 -0.0435 66  LEU   A CA  
1053  C  C   . LEU   A 66  ? 0.2011 0.1581 0.2256 -0.0186 -0.0419 -0.0401 66  LEU   A C   
1054  O  O   . LEU   A 66  ? 0.1667 0.1294 0.1870 -0.0196 -0.0381 -0.0434 66  LEU   A O   
1055  C  CB  . LEU   A 66  ? 0.2046 0.1648 0.2501 -0.0105 -0.0379 -0.0433 66  LEU   A CB  
1056  C  CG  . LEU   A 66  ? 0.2005 0.1582 0.2626 -0.0055 -0.0383 -0.0470 66  LEU   A CG  
1057  C  CD1 . LEU   A 66  ? 0.2398 0.2049 0.3029 -0.0021 -0.0335 -0.0475 66  LEU   A CD1 
1058  C  CD2 . LEU   A 66  ? 0.2419 0.1914 0.2977 -0.0034 -0.0388 -0.0559 66  LEU   A CD2 
1070  N  N   . THR   A 67  ? 0.1901 0.1470 0.2175 -0.0214 -0.0457 -0.0331 67  THR   A N   
1071  C  CA  . THR   A 67  ? 0.2061 0.1650 0.2204 -0.0255 -0.0466 -0.0296 67  THR   A CA  
1072  C  C   . THR   A 67  ? 0.1922 0.1491 0.2001 -0.0280 -0.0473 -0.0347 67  THR   A C   
1073  O  O   . THR   A 67  ? 0.1841 0.1339 0.1925 -0.0284 -0.0507 -0.0374 67  THR   A O   
1074  C  CB  . THR   A 67  ? 0.1667 0.1267 0.1910 -0.0273 -0.0508 -0.0225 67  THR   A CB  
1075  O  OG1 . THR   A 67  ? 0.1738 0.1358 0.2012 -0.0254 -0.0499 -0.0186 67  THR   A OG1 
1076  C  CG2 . THR   A 67  ? 0.1992 0.1614 0.2113 -0.0304 -0.0515 -0.0191 67  THR   A CG2 
1084  N  N   . GLY   A 68  ? 0.1930 0.1548 0.1910 -0.0302 -0.0445 -0.0360 68  GLY   A N   
1085  C  CA  . GLY   A 68  ? 0.1889 0.1493 0.1790 -0.0334 -0.0456 -0.0404 68  GLY   A CA  
1086  C  C   . GLY   A 68  ? 0.2430 0.2012 0.2220 -0.0314 -0.0415 -0.0498 68  GLY   A C   
1087  O  O   . GLY   A 68  ? 0.2233 0.1819 0.1966 -0.0344 -0.0413 -0.0541 68  GLY   A O   
1091  N  N   . ALA   A 69  ? 0.2261 0.1857 0.2192 -0.0263 -0.0381 -0.0535 69  ALA   A N   
1092  C  CA  . ALA   A 69  ? 0.2189 0.1787 0.2105 -0.0232 -0.0336 -0.0634 69  ALA   A CA  
1093  C  C   . ALA   A 69  ? 0.2053 0.1773 0.1944 -0.0242 -0.0268 -0.0650 69  ALA   A C   
1094  O  O   . ALA   A 69  ? 0.2114 0.1891 0.1985 -0.0255 -0.0258 -0.0577 69  ALA   A O   
1095  C  CB  . ALA   A 69  ? 0.2104 0.1669 0.2163 -0.0174 -0.0333 -0.0663 69  ALA   A CB  
1101  N  N   . PRO   A 70  ? 0.2573 0.2308 0.2320 -0.0238 -0.0222 -0.0742 70  PRO   A N   
1102  C  CA  . PRO   A 70  ? 0.2244 0.2115 0.1992 -0.0254 -0.0153 -0.0757 70  PRO   A CA  
1103  C  C   . PRO   A 70  ? 0.2134 0.2079 0.1989 -0.0204 -0.0099 -0.0757 70  PRO   A C   
1104  O  O   . PRO   A 70  ? 0.2239 0.2241 0.2095 -0.0174 -0.0038 -0.0839 70  PRO   A O   
1105  C  CB  . PRO   A 70  ? 0.2592 0.2452 0.2195 -0.0262 -0.0124 -0.0864 70  PRO   A CB  
1106  C  CG  . PRO   A 70  ? 0.2847 0.2586 0.2503 -0.0216 -0.0158 -0.0931 70  PRO   A CG  
1107  C  CD  . PRO   A 70  ? 0.2731 0.2392 0.2478 -0.0221 -0.0232 -0.0842 70  PRO   A CD  
1115  N  N   . VAL   A 71  ? 0.2068 0.2015 0.2017 -0.0196 -0.0124 -0.0671 71  VAL   A N   
1116  C  CA  . VAL   A 71  ? 0.1984 0.2002 0.2059 -0.0155 -0.0086 -0.0652 71  VAL   A CA  
1117  C  C   . VAL   A 71  ? 0.1769 0.1849 0.1842 -0.0196 -0.0095 -0.0550 71  VAL   A C   
1118  O  O   . VAL   A 71  ? 0.1632 0.1668 0.1634 -0.0237 -0.0142 -0.0492 71  VAL   A O   
1119  C  CB  . VAL   A 71  ? 0.2036 0.1989 0.2310 -0.0099 -0.0118 -0.0662 71  VAL   A CB  
1120  C  CG1 . VAL   A 71  ? 0.2587 0.2463 0.2818 -0.0054 -0.0112 -0.0766 71  VAL   A CG1 
1121  C  CG2 . VAL   A 71  ? 0.2573 0.2423 0.2787 -0.0119 -0.0191 -0.0582 71  VAL   A CG2 
1131  N  N   . PRO   A 72  ? 0.1802 0.1974 0.1931 -0.0182 -0.0054 -0.0522 72  PRO   A N   
1132  C  CA  . PRO   A 72  ? 0.1652 0.1881 0.1813 -0.0224 -0.0069 -0.0427 72  PRO   A CA  
1133  C  C   . PRO   A 72  ? 0.1580 0.1726 0.1755 -0.0226 -0.0136 -0.0349 72  PRO   A C   
1134  O  O   . PRO   A 72  ? 0.1487 0.1591 0.1763 -0.0185 -0.0153 -0.0351 72  PRO   A O   
1135  C  CB  . PRO   A 72  ? 0.2137 0.2463 0.2302 -0.0203 -0.0013 -0.0431 72  PRO   A CB  
1136  C  CG  . PRO   A 72  ? 0.1457 0.1786 0.1826 -0.0134 0.0009  -0.0507 72  PRO   A CG  
1137  C  CD  . PRO   A 72  ? 0.1674 0.1915 0.1920 -0.0130 0.0002  -0.0582 72  PRO   A CD  
1145  N  N   . THR   A 73  ? 0.1745 0.1872 0.1834 -0.0273 -0.0175 -0.0283 73  THR   A N   
1146  C  CA  . THR   A 73  ? 0.1749 0.1816 0.1866 -0.0277 -0.0234 -0.0217 73  THR   A CA  
1147  C  C   . THR   A 73  ? 0.1575 0.1551 0.1725 -0.0261 -0.0276 -0.0230 73  THR   A C   
1148  O  O   . THR   A 73  ? 0.1665 0.1606 0.1871 -0.0244 -0.0307 -0.0196 73  THR   A O   
1149  C  CB  . THR   A 73  ? 0.1626 0.1738 0.1871 -0.0256 -0.0226 -0.0177 73  THR   A CB  
1150  O  OG1 . THR   A 73  ? 0.1658 0.1741 0.1989 -0.0204 -0.0223 -0.0208 73  THR   A OG1 
1151  C  CG2 . THR   A 73  ? 0.1660 0.1873 0.1895 -0.0274 -0.0185 -0.0163 73  THR   A CG2 
1159  N  N   . SER   A 74  ? 0.1494 0.1430 0.1579 -0.0270 -0.0282 -0.0279 74  SER   A N   
1160  C  CA  . SER   A 74  ? 0.1657 0.1503 0.1739 -0.0259 -0.0322 -0.0294 74  SER   A CA  
1161  C  C   . SER   A 74  ? 0.1633 0.1441 0.1675 -0.0293 -0.0376 -0.0241 74  SER   A C   
1162  O  O   . SER   A 74  ? 0.1641 0.1388 0.1672 -0.0301 -0.0409 -0.0255 74  SER   A O   
1163  C  CB  . SER   A 74  ? 0.1878 0.1690 0.1914 -0.0254 -0.0307 -0.0376 74  SER   A CB  
1164  O  OG  . SER   A 74  ? 0.2033 0.1867 0.1946 -0.0294 -0.0301 -0.0391 74  SER   A OG  
1170  N  N   . GLY   A 75  ? 0.1618 0.1464 0.1649 -0.0317 -0.0388 -0.0181 75  GLY   A N   
1171  C  CA  . GLY   A 75  ? 0.1669 0.1483 0.1669 -0.0342 -0.0438 -0.0136 75  GLY   A CA  
1172  C  C   . GLY   A 75  ? 0.1594 0.1398 0.1688 -0.0322 -0.0463 -0.0094 75  GLY   A C   
1173  O  O   . GLY   A 75  ? 0.1910 0.1699 0.1974 -0.0334 -0.0496 -0.0059 75  GLY   A O   
1177  N  N   . ARG   A 76  ? 0.1415 0.1217 0.1578 -0.0289 -0.0445 -0.0097 76  ARG   A N   
1178  C  CA  . ARG   A 76  ? 0.1297 0.1103 0.1554 -0.0277 -0.0465 -0.0059 76  ARG   A CA  
1179  C  C   . ARG   A 76  ? 0.1512 0.1272 0.1750 -0.0266 -0.0480 -0.0053 76  ARG   A C   
1180  O  O   . ARG   A 76  ? 0.1520 0.1245 0.1782 -0.0266 -0.0487 -0.0088 76  ARG   A O   
1181  C  CB  . ARG   A 76  ? 0.1497 0.1318 0.1767 -0.0251 -0.0440 -0.0053 76  ARG   A CB  
1182  C  CG  . ARG   A 76  ? 0.1252 0.1138 0.1567 -0.0255 -0.0413 -0.0050 76  ARG   A CG  
1183  C  CD  . ARG   A 76  ? 0.1715 0.1604 0.1914 -0.0281 -0.0430 -0.0012 76  ARG   A CD  
1184  N  NE  . ARG   A 76  ? 0.1277 0.1170 0.1567 -0.0275 -0.0459 0.0024  76  ARG   A NE  
1185  C  CZ  . ARG   A 76  ? 0.1201 0.1113 0.1497 -0.0279 -0.0464 0.0062  76  ARG   A CZ  
1186  N  NH1 . ARG   A 76  ? 0.1455 0.1382 0.1677 -0.0312 -0.0471 0.0073  76  ARG   A NH1 
1187  N  NH2 . ARG   A 76  ? 0.1575 0.1460 0.1828 -0.0252 -0.0462 0.0080  76  ARG   A NH2 
1201  N  N   . PHE   A 77  ? 0.1429 0.1210 0.1688 -0.0255 -0.0477 -0.0013 77  PHE   A N   
1202  C  CA  . PHE   A 77  ? 0.1371 0.1139 0.1640 -0.0244 -0.0482 0.0003  77  PHE   A CA  
1203  C  C   . PHE   A 77  ? 0.1284 0.1080 0.1580 -0.0228 -0.0474 0.0039  77  PHE   A C   
1204  O  O   . PHE   A 77  ? 0.1088 0.0906 0.1397 -0.0223 -0.0468 0.0046  77  PHE   A O   
1205  C  CB  . PHE   A 77  ? 0.1246 0.1012 0.1500 -0.0258 -0.0493 0.0003  77  PHE   A CB  
1206  C  CG  . PHE   A 77  ? 0.1390 0.1175 0.1600 -0.0256 -0.0491 0.0027  77  PHE   A CG  
1207  C  CD1 . PHE   A 77  ? 0.1275 0.1073 0.1467 -0.0268 -0.0495 0.0024  77  PHE   A CD1 
1208  C  CD2 . PHE   A 77  ? 0.1478 0.1284 0.1710 -0.0246 -0.0492 0.0050  77  PHE   A CD2 
1209  C  CE1 . PHE   A 77  ? 0.1429 0.1235 0.1589 -0.0265 -0.0502 0.0047  77  PHE   A CE1 
1210  C  CE2 . PHE   A 77  ? 0.1399 0.1225 0.1639 -0.0243 -0.0497 0.0064  77  PHE   A CE2 
1211  C  CZ  . PHE   A 77  ? 0.1403 0.1223 0.1605 -0.0249 -0.0502 0.0065  77  PHE   A CZ  
1221  N  N   . MET   A 78  ? 0.1275 0.1077 0.1599 -0.0226 -0.0477 0.0057  78  MET   A N   
1222  C  CA  . MET   A 78  ? 0.1246 0.1073 0.1568 -0.0217 -0.0470 0.0083  78  MET   A CA  
1223  C  C   . MET   A 78  ? 0.0946 0.0813 0.1333 -0.0224 -0.0470 0.0097  78  MET   A C   
1224  O  O   . MET   A 78  ? 0.1379 0.1220 0.1705 -0.0236 -0.0480 0.0097  78  MET   A O   
1225  C  CB  . MET   A 78  ? 0.1139 0.0968 0.1537 -0.0215 -0.0471 0.0095  78  MET   A CB  
1226  C  CG  . MET   A 78  ? 0.1572 0.1385 0.1945 -0.0205 -0.0470 0.0084  78  MET   A CG  
1227  S  SD  . MET   A 78  ? 0.1693 0.1505 0.2114 -0.0200 -0.0478 0.0109  78  MET   A SD  
1228  C  CE  . MET   A 78  ? 0.1578 0.1422 0.1995 -0.0202 -0.0475 0.0135  78  MET   A CE  
1238  N  N   . VAL   A 79  ? 0.1093 0.0985 0.1445 -0.0218 -0.0464 0.0103  79  VAL   A N   
1239  C  CA  . VAL   A 79  ? 0.1264 0.1200 0.1632 -0.0228 -0.0463 0.0112  79  VAL   A CA  
1240  C  C   . VAL   A 79  ? 0.1327 0.1280 0.1692 -0.0238 -0.0462 0.0131  79  VAL   A C   
1241  O  O   . VAL   A 79  ? 0.1028 0.0988 0.1418 -0.0230 -0.0457 0.0132  79  VAL   A O   
1242  C  CB  . VAL   A 79  ? 0.1331 0.1297 0.1691 -0.0215 -0.0460 0.0098  79  VAL   A CB  
1243  C  CG1 . VAL   A 79  ? 0.1289 0.1328 0.1699 -0.0224 -0.0458 0.0100  79  VAL   A CG1 
1244  C  CG2 . VAL   A 79  ? 0.1092 0.1045 0.1469 -0.0210 -0.0469 0.0090  79  VAL   A CG2 
1254  N  N   . VAL   A 80  ? 0.1339 0.1315 0.1731 -0.0263 -0.0467 0.0153  80  VAL   A N   
1255  C  CA  . VAL   A 80  ? 0.1165 0.1168 0.1576 -0.0282 -0.0472 0.0183  80  VAL   A CA  
1256  C  C   . VAL   A 80  ? 0.0988 0.1079 0.1451 -0.0309 -0.0467 0.0195  80  VAL   A C   
1257  O  O   . VAL   A 80  ? 0.1442 0.1535 0.1866 -0.0318 -0.0471 0.0199  80  VAL   A O   
1258  C  CB  . VAL   A 80  ? 0.1214 0.1166 0.1652 -0.0293 -0.0490 0.0209  80  VAL   A CB  
1259  C  CG1 . VAL   A 80  ? 0.1560 0.1525 0.1965 -0.0317 -0.0501 0.0249  80  VAL   A CG1 
1260  C  CG2 . VAL   A 80  ? 0.1348 0.1234 0.1758 -0.0267 -0.0495 0.0189  80  VAL   A CG2 
1270  N  N   . THR   A 81  ? 0.1103 0.1247 0.1512 -0.0320 -0.0460 0.0198  81  THR   A N   
1271  C  CA  . THR   A 81  ? 0.0895 0.1153 0.1360 -0.0345 -0.0454 0.0204  81  THR   A CA  
1272  C  C   . THR   A 81  ? 0.1016 0.1333 0.1468 -0.0359 -0.0452 0.0206  81  THR   A C   
1273  O  O   . THR   A 81  ? 0.1346 0.1600 0.1726 -0.0339 -0.0459 0.0198  81  THR   A O   
1274  C  CB  . THR   A 81  ? 0.0923 0.1234 0.1455 -0.0324 -0.0448 0.0165  81  THR   A CB  
1275  O  OG1 . THR   A 81  ? 0.1585 0.1999 0.2081 -0.0348 -0.0439 0.0170  81  THR   A OG1 
1276  C  CG2 . THR   A 81  ? 0.1274 0.1558 0.1733 -0.0287 -0.0448 0.0125  81  THR   A CG2 
1284  N  N   . LYS   A 82  ? 0.1339 0.1763 0.1769 -0.0394 -0.0445 0.0219  82  LYS   A N   
1285  C  CA  . LYS   A 82  ? 0.1568 0.2056 0.1937 -0.0410 -0.0443 0.0212  82  LYS   A CA  
1286  C  C   . LYS   A 82  ? 0.1466 0.1950 0.1842 -0.0360 -0.0438 0.0147  82  LYS   A C   
1287  O  O   . LYS   A 82  ? 0.1100 0.1624 0.1568 -0.0333 -0.0429 0.0114  82  LYS   A O   
1288  C  CB  . LYS   A 82  ? 0.1192 0.1825 0.1601 -0.0456 -0.0419 0.0233  82  LYS   A CB  
1289  C  CG  . LYS   A 82  ? 0.1284 0.1967 0.1608 -0.0459 -0.0399 0.0214  82  LYS   A CG  
1290  C  CD  . LYS   A 82  ? 0.1500 0.2289 0.1738 -0.0517 -0.0376 0.0250  82  LYS   A CD  
1291  C  CE  . LYS   A 82  ? 0.1028 0.1861 0.1257 -0.0530 -0.0368 0.0241  82  LYS   A CE  
1292  N  NZ  . LYS   A 82  ? 0.1518 0.2482 0.1627 -0.0575 -0.0330 0.0249  82  LYS   A NZ  
1306  N  N   . ALA   A 83  ? 0.1116 0.1565 0.1492 -0.0345 -0.0447 0.0128  83  ALA   A N   
1307  C  CA  . ALA   A 83  ? 0.1108 0.1524 0.1475 -0.0296 -0.0448 0.0073  83  ALA   A CA  
1308  C  C   . ALA   A 83  ? 0.1288 0.1780 0.1589 -0.0282 -0.0419 0.0021  83  ALA   A C   
1309  O  O   . ALA   A 83  ? 0.1044 0.1581 0.1328 -0.0304 -0.0410 0.0027  83  ALA   A O   
1310  C  CB  . ALA   A 83  ? 0.1194 0.1517 0.1516 -0.0291 -0.0474 0.0083  83  ALA   A CB  
1316  N  N   . PRO   A 84  ? 0.1012 0.1557 0.1425 -0.0244 -0.0406 -0.0031 84  PRO   A N   
1317  C  CA  . PRO   A 84  ? 0.1241 0.1869 0.1625 -0.0222 -0.0374 -0.0094 84  PRO   A CA  
1318  C  C   . PRO   A 84  ? 0.1309 0.1887 0.1619 -0.0200 -0.0386 -0.0139 84  PRO   A C   
1319  O  O   . PRO   A 84  ? 0.1310 0.1961 0.1588 -0.0200 -0.0360 -0.0180 84  PRO   A O   
1320  C  CB  . PRO   A 84  ? 0.1518 0.2175 0.1973 -0.0181 -0.0370 -0.0132 84  PRO   A CB  
1321  C  CG  . PRO   A 84  ? 0.1482 0.2032 0.1967 -0.0174 -0.0410 -0.0101 84  PRO   A CG  
1322  C  CD  . PRO   A 84  ? 0.1075 0.1581 0.1549 -0.0220 -0.0422 -0.0036 84  PRO   A CD  
1330  N  N   . LEU   A 85  ? 0.1156 0.1621 0.1474 -0.0182 -0.0426 -0.0135 85  LEU   A N   
1331  C  CA  . LEU   A 85  ? 0.0984 0.1396 0.1281 -0.0164 -0.0450 -0.0172 85  LEU   A CA  
1332  C  C   . LEU   A 85  ? 0.1148 0.1563 0.1329 -0.0206 -0.0447 -0.0146 85  LEU   A C   
1333  O  O   . LEU   A 85  ? 0.1100 0.1534 0.1236 -0.0200 -0.0445 -0.0192 85  LEU   A O   
1334  C  CB  . LEU   A 85  ? 0.1090 0.1384 0.1394 -0.0146 -0.0494 -0.0163 85  LEU   A CB  
1335  C  CG  . LEU   A 85  ? 0.1273 0.1489 0.1530 -0.0133 -0.0527 -0.0189 85  LEU   A CG  
1336  C  CD1 . LEU   A 85  ? 0.1075 0.1306 0.1372 -0.0088 -0.0531 -0.0269 85  LEU   A CD1 
1337  C  CD2 . LEU   A 85  ? 0.1373 0.1494 0.1655 -0.0135 -0.0566 -0.0149 85  LEU   A CD2 
1349  N  N   . THR   A 86  ? 0.1256 0.1657 0.1411 -0.0246 -0.0455 -0.0073 86  THR   A N   
1350  C  CA  . THR   A 86  ? 0.1017 0.1420 0.1158 -0.0287 -0.0468 -0.0029 86  THR   A CA  
1351  C  C   . THR   A 86  ? 0.1198 0.1688 0.1262 -0.0338 -0.0443 0.0006  86  THR   A C   
1352  O  O   . THR   A 86  ? 0.1461 0.1965 0.1436 -0.0372 -0.0451 0.0025  86  THR   A O   
1353  C  CB  . THR   A 86  ? 0.1404 0.1697 0.1485 -0.0299 -0.0504 0.0028  86  THR   A CB  
1354  O  OG1 . THR   A 86  ? 0.1260 0.1578 0.1445 -0.0307 -0.0496 0.0064  86  THR   A OG1 
1355  C  CG2 . THR   A 86  ? 0.0925 0.1152 0.1104 -0.0264 -0.0531 0.0006  86  THR   A CG2 
1363  N  N   . GLY   A 87  ? 0.1217 0.1767 0.1313 -0.0346 -0.0416 0.0027  87  GLY   A N   
1364  C  CA  . GLY   A 87  ? 0.1087 0.1726 0.1190 -0.0403 -0.0401 0.0080  87  GLY   A CA  
1365  C  C   . GLY   A 87  ? 0.1468 0.2026 0.1524 -0.0442 -0.0438 0.0163  87  GLY   A C   
1366  O  O   . GLY   A 87  ? 0.1518 0.2131 0.1581 -0.0494 -0.0440 0.0221  87  GLY   A O   
1370  N  N   . THR   A 88  ? 0.1144 0.1604 0.1290 -0.0413 -0.0470 0.0171  88  THR   A N   
1371  C  CA  . THR   A 88  ? 0.1216 0.1599 0.1388 -0.0432 -0.0503 0.0233  88  THR   A CA  
1372  C  C   . THR   A 88  ? 0.1394 0.1725 0.1584 -0.0412 -0.0493 0.0244  88  THR   A C   
1373  O  O   . THR   A 88  ? 0.1004 0.1397 0.1279 -0.0402 -0.0479 0.0214  88  THR   A O   
1374  C  CB  . THR   A 88  ? 0.1447 0.1723 0.1587 -0.0397 -0.0517 0.0225  88  THR   A CB  
1375  O  OG1 . THR   A 88  ? 0.1292 0.1524 0.1491 -0.0349 -0.0507 0.0184  88  THR   A OG1 
1376  C  CG2 . THR   A 88  ? 0.1628 0.1920 0.1706 -0.0407 -0.0531 0.0210  88  THR   A CG2 
1384  N  N   . ILE   A 89  ? 0.1278 0.1529 0.1527 -0.0409 -0.0504 0.0282  89  ILE   A N   
1385  C  CA  . ILE   A 89  ? 0.1285 0.1475 0.1564 -0.0385 -0.0497 0.0280  89  ILE   A CA  
1386  C  C   . ILE   A 89  ? 0.0971 0.1141 0.1308 -0.0336 -0.0483 0.0226  89  ILE   A C   
1387  O  O   . ILE   A 89  ? 0.1098 0.1236 0.1381 -0.0318 -0.0487 0.0207  89  ILE   A O   
1388  C  CB  . ILE   A 89  ? 0.1357 0.1468 0.1683 -0.0382 -0.0516 0.0322  89  ILE   A CB  
1389  C  CG1 . ILE   A 89  ? 0.1456 0.1506 0.1787 -0.0361 -0.0513 0.0313  89  ILE   A CG1 
1390  C  CG2 . ILE   A 89  ? 0.1648 0.1702 0.1937 -0.0362 -0.0525 0.0318  89  ILE   A CG2 
1391  C  CD1 . ILE   A 89  ? 0.1149 0.1241 0.1529 -0.0388 -0.0513 0.0330  89  ILE   A CD1 
1403  N  N   . GLY   A 90  ? 0.1163 0.1320 0.1479 -0.0321 -0.0471 0.0204  90  GLY   A N   
1404  C  CA  . GLY   A 90  ? 0.0939 0.1064 0.1305 -0.0281 -0.0464 0.0166  90  GLY   A CA  
1405  C  C   . GLY   A 90  ? 0.1128 0.1171 0.1469 -0.0266 -0.0465 0.0172  90  GLY   A C   
1406  O  O   . GLY   A 90  ? 0.1229 0.1268 0.1597 -0.0277 -0.0466 0.0188  90  GLY   A O   
1410  N  N   . ILE   A 91  ? 0.0909 0.0909 0.1277 -0.0245 -0.0462 0.0164  91  ILE   A N   
1411  C  CA  . ILE   A 91  ? 0.1075 0.1013 0.1419 -0.0229 -0.0466 0.0165  91  ILE   A CA  
1412  C  C   . ILE   A 91  ? 0.1097 0.1022 0.1449 -0.0209 -0.0456 0.0140  91  ILE   A C   
1413  O  O   . ILE   A 91  ? 0.1267 0.1178 0.1607 -0.0201 -0.0460 0.0142  91  ILE   A O   
1414  C  CB  . ILE   A 91  ? 0.0845 0.0767 0.1264 -0.0237 -0.0480 0.0194  91  ILE   A CB  
1415  C  CG1 . ILE   A 91  ? 0.1071 0.1001 0.1436 -0.0243 -0.0485 0.0208  91  ILE   A CG1 
1416  C  CG2 . ILE   A 91  ? 0.1204 0.1105 0.1588 -0.0254 -0.0495 0.0220  91  ILE   A CG2 
1417  C  CD1 . ILE   A 91  ? 0.1251 0.1146 0.1633 -0.0243 -0.0503 0.0234  91  ILE   A CD1 
1429  N  N   . SER   A 92  ? 0.0969 0.0896 0.1322 -0.0200 -0.0451 0.0121  92  SER   A N   
1430  C  CA  . SER   A 92  ? 0.0958 0.0870 0.1306 -0.0188 -0.0450 0.0106  92  SER   A CA  
1431  C  C   . SER   A 92  ? 0.1054 0.0940 0.1396 -0.0190 -0.0450 0.0101  92  SER   A C   
1432  O  O   . SER   A 92  ? 0.1288 0.1170 0.1608 -0.0195 -0.0454 0.0097  92  SER   A O   
1433  C  CB  . SER   A 92  ? 0.1172 0.1107 0.1513 -0.0179 -0.0452 0.0090  92  SER   A CB  
1434  O  OG  . SER   A 92  ? 0.1580 0.1546 0.1897 -0.0181 -0.0455 0.0086  92  SER   A OG  
1440  N  N   . ASN   A 93  ? 0.1204 0.1070 0.1501 -0.0186 -0.0451 0.0099  93  ASN   A N   
1441  C  CA  . ASN   A 93  ? 0.0855 0.0725 0.1224 -0.0196 -0.0453 0.0089  93  ASN   A CA  
1442  C  C   . ASN   A 93  ? 0.1220 0.1070 0.1484 -0.0201 -0.0456 0.0085  93  ASN   A C   
1443  O  O   . ASN   A 93  ? 0.1187 0.1043 0.1465 -0.0197 -0.0459 0.0095  93  ASN   A O   
1444  C  CB  . ASN   A 93  ? 0.1212 0.1065 0.1528 -0.0197 -0.0453 0.0088  93  ASN   A CB  
1445  C  CG  . ASN   A 93  ? 0.0959 0.0820 0.1362 -0.0210 -0.0457 0.0064  93  ASN   A CG  
1446  O  OD1 . ASN   A 93  ? 0.1268 0.1124 0.1581 -0.0226 -0.0454 0.0054  93  ASN   A OD1 
1447  N  ND2 . ASN   A 93  ? 0.1345 0.1178 0.1725 -0.0205 -0.0461 0.0053  93  ASN   A ND2 
1454  N  N   . SER   A 94  ? 0.1195 0.1042 0.1458 -0.0216 -0.0463 0.0073  94  SER   A N   
1455  C  CA  . SER   A 94  ? 0.1131 0.0977 0.1361 -0.0231 -0.0471 0.0078  94  SER   A CA  
1456  C  C   . SER   A 94  ? 0.1195 0.1040 0.1407 -0.0257 -0.0476 0.0060  94  SER   A C   
1457  O  O   . SER   A 94  ? 0.1251 0.1084 0.1456 -0.0260 -0.0473 0.0038  94  SER   A O   
1458  C  CB  . SER   A 94  ? 0.1074 0.0913 0.1301 -0.0225 -0.0483 0.0084  94  SER   A CB  
1459  O  OG  . SER   A 94  ? 0.1131 0.0961 0.1327 -0.0233 -0.0498 0.0096  94  SER   A OG  
1465  N  N   . GLY   A 95  ? 0.1486 0.1330 0.1621 -0.0280 -0.0486 0.0069  95  GLY   A N   
1466  C  CA  . GLY   A 95  ? 0.1312 0.1168 0.1427 -0.0317 -0.0492 0.0049  95  GLY   A CA  
1467  C  C   . GLY   A 95  ? 0.1207 0.1058 0.1295 -0.0336 -0.0510 0.0061  95  GLY   A C   
1468  O  O   . GLY   A 95  ? 0.1433 0.1254 0.1487 -0.0320 -0.0514 0.0064  95  GLY   A O   
1472  N  N   . GLY   A 96  ? 0.1572 0.1429 0.1556 -0.0377 -0.0520 0.0070  96  GLY   A N   
1473  C  CA  . GLY   A 96  ? 0.1681 0.1525 0.1613 -0.0402 -0.0542 0.0087  96  GLY   A CA  
1474  C  C   . GLY   A 96  ? 0.1750 0.1580 0.1617 -0.0422 -0.0543 0.0047  96  GLY   A C   
1475  O  O   . GLY   A 96  ? 0.1849 0.1697 0.1688 -0.0446 -0.0530 0.0008  96  GLY   A O   
1479  N  N   . LYS   A 97  ? 0.1442 0.1253 0.1334 -0.0411 -0.0559 0.0053  97  LYS   A N   
1480  C  CA  . LYS   A 97  ? 0.1486 0.1279 0.1331 -0.0433 -0.0567 0.0018  97  LYS   A CA  
1481  C  C   . LYS   A 97  ? 0.1376 0.1140 0.1273 -0.0400 -0.0567 0.0016  97  LYS   A C   
1482  O  O   . LYS   A 97  ? 0.1523 0.1264 0.1372 -0.0413 -0.0569 -0.0029 97  LYS   A O   
1483  C  CB  . LYS   A 97  ? 0.2090 0.1876 0.1825 -0.0474 -0.0591 0.0042  97  LYS   A CB  
1484  C  CG  . LYS   A 97  ? 0.2556 0.2378 0.2255 -0.0518 -0.0593 0.0064  97  LYS   A CG  
1485  C  CD  . LYS   A 97  ? 0.3686 0.3490 0.3256 -0.0559 -0.0621 0.0102  97  LYS   A CD  
1486  C  CE  . LYS   A 97  ? 0.4374 0.4215 0.3830 -0.0621 -0.0617 0.0110  97  LYS   A CE  
1487  N  NZ  . LYS   A 97  ? 0.4347 0.4230 0.3859 -0.0629 -0.0611 0.0148  97  LYS   A NZ  
1501  N  N   . TRP   A 98  ? 0.1658 0.1140 0.1485 -0.0199 -0.0492 0.0192  98  TRP   A N   
1502  C  CA  . TRP   A 98  ? 0.1961 0.1415 0.1794 -0.0224 -0.0551 0.0218  98  TRP   A CA  
1503  C  C   . TRP   A 98  ? 0.1957 0.1424 0.1803 -0.0246 -0.0547 0.0228  98  TRP   A C   
1504  O  O   . TRP   A 98  ? 0.1852 0.1288 0.1716 -0.0290 -0.0613 0.0258  98  TRP   A O   
1505  C  CB  . TRP   A 98  ? 0.1399 0.0905 0.1385 -0.0198 -0.0543 0.0206  98  TRP   A CB  
1506  C  CG  . TRP   A 98  ? 0.1697 0.1183 0.1705 -0.0223 -0.0610 0.0229  98  TRP   A CG  
1507  C  CD1 . TRP   A 98  ? 0.1486 0.1004 0.1631 -0.0237 -0.0653 0.0224  98  TRP   A CD1 
1508  C  CD2 . TRP   A 98  ? 0.1604 0.1156 0.1663 -0.0243 -0.0586 0.0210  98  TRP   A CD2 
1509  N  NE1 . TRP   A 98  ? 0.1620 0.1215 0.1822 -0.0266 -0.0650 0.0202  98  TRP   A NE1 
1510  C  CE2 . TRP   A 98  ? 0.1362 0.0992 0.1583 -0.0269 -0.0610 0.0191  98  TRP   A CE2 
1511  C  CE3 . TRP   A 98  ? 0.1393 0.0965 0.1426 -0.0239 -0.0544 0.0203  98  TRP   A CE3 
1512  C  CZ2 . TRP   A 98  ? 0.1393 0.1095 0.1658 -0.0294 -0.0591 0.0170  98  TRP   A CZ2 
1513  C  CZ3 . TRP   A 98  ? 0.1324 0.0967 0.1429 -0.0264 -0.0526 0.0181  98  TRP   A CZ3 
1514  C  CH2 . TRP   A 98  ? 0.1573 0.1270 0.1757 -0.0293 -0.0550 0.0163  98  TRP   A CH2 
1525  N  N   . GLY   A 99  ? 0.2049 0.1559 0.1848 -0.0222 -0.0474 0.0203  99  GLY   A N   
1526  C  CA  . GLY   A 99  ? 0.1800 0.1324 0.1607 -0.0239 -0.0466 0.0207  99  GLY   A CA  
1527  C  C   . GLY   A 99  ? 0.1987 0.1465 0.1703 -0.0272 -0.0488 0.0223  99  GLY   A C   
1528  O  O   . GLY   A 99  ? 0.1909 0.1379 0.1631 -0.0304 -0.0512 0.0238  99  GLY   A O   
1532  N  N   . VAL   A 100 ? 0.1892 0.1355 0.1592 -0.0267 -0.0479 0.0220  100 VAL   A N   
1533  C  CA  . VAL   A 100 ? 0.1733 0.1159 0.1414 -0.0296 -0.0502 0.0233  100 VAL   A CA  
1534  C  C   . VAL   A 100 ? 0.1999 0.1363 0.1672 -0.0347 -0.0599 0.0272  100 VAL   A C   
1535  O  O   . VAL   A 100 ? 0.2372 0.1699 0.1986 -0.0388 -0.0633 0.0291  100 VAL   A O   
1536  C  CB  . VAL   A 100 ? 0.1934 0.1360 0.1566 -0.0272 -0.0463 0.0217  100 VAL   A CB  
1537  C  CG1 . VAL   A 100 ? 0.2184 0.1553 0.1742 -0.0307 -0.0496 0.0234  100 VAL   A CG1 
1538  C  CG2 . VAL   A 100 ? 0.2116 0.1609 0.1739 -0.0223 -0.0373 0.0187  100 VAL   A CG2 
1548  N  N   . ASP   A 101 ? 0.2127 0.1475 0.1827 -0.0347 -0.0644 0.0283  101 ASP   A N   
1549  C  CA  . ASP   A 101 ? 0.1883 0.1248 0.1690 -0.0389 -0.0710 0.0287  101 ASP   A CA  
1550  C  C   . ASP   A 101 ? 0.1820 0.1260 0.1698 -0.0411 -0.0700 0.0263  101 ASP   A C   
1551  O  O   . ASP   A 101 ? 0.1868 0.1327 0.1759 -0.0454 -0.0731 0.0254  101 ASP   A O   
1552  C  CB  . ASP   A 101 ? 0.2064 0.1426 0.1918 -0.0383 -0.0744 0.0289  101 ASP   A CB  
1553  C  CG  . ASP   A 101 ? 0.2350 0.1643 0.2153 -0.0395 -0.0784 0.0310  101 ASP   A CG  
1554  O  OD1 . ASP   A 101 ? 0.2339 0.1650 0.2180 -0.0434 -0.0829 0.0306  101 ASP   A OD1 
1555  O  OD2 . ASP   A 101 ? 0.2525 0.1780 0.2269 -0.0363 -0.0755 0.0312  101 ASP   A OD2 
1560  N  N   . LEU   A 102 ? 0.2061 0.1535 0.1929 -0.0386 -0.0659 0.0246  102 LEU   A N   
1561  C  CA  . LEU   A 102 ? 0.1690 0.1248 0.1673 -0.0408 -0.0642 0.0222  102 LEU   A CA  
1562  C  C   . LEU   A 102 ? 0.1788 0.1322 0.1681 -0.0432 -0.0635 0.0224  102 LEU   A C   
1563  O  O   . LEU   A 102 ? 0.1748 0.1320 0.1704 -0.0473 -0.0656 0.0212  102 LEU   A O   
1564  C  CB  . LEU   A 102 ? 0.1700 0.1288 0.1688 -0.0372 -0.0594 0.0207  102 LEU   A CB  
1565  C  CG  . LEU   A 102 ? 0.1661 0.1319 0.1718 -0.0393 -0.0570 0.0181  102 LEU   A CG  
1566  C  CD1 . LEU   A 102 ? 0.1643 0.1369 0.1826 -0.0425 -0.0606 0.0170  102 LEU   A CD1 
1567  C  CD2 . LEU   A 102 ? 0.1537 0.1222 0.1600 -0.0356 -0.0519 0.0168  102 LEU   A CD2 
1579  N  N   . LYS   A 103 ? 0.1743 0.1228 0.1549 -0.0412 -0.0606 0.0240  103 LYS   A N   
1580  C  CA  . LYS   A 103 ? 0.1950 0.1414 0.1681 -0.0430 -0.0594 0.0243  103 LYS   A CA  
1581  C  C   . LYS   A 103 ? 0.2002 0.1434 0.1722 -0.0470 -0.0643 0.0249  103 LYS   A C   
1582  O  O   . LYS   A 103 ? 0.2158 0.1603 0.1881 -0.0504 -0.0654 0.0238  103 LYS   A O   
1583  C  CB  . LYS   A 103 ? 0.2264 0.1677 0.1860 -0.0398 -0.0553 0.0262  103 LYS   A CB  
1584  C  CG  . LYS   A 103 ? 0.2185 0.1588 0.1737 -0.0412 -0.0532 0.0263  103 LYS   A CG  
1585  C  CD  . LYS   A 103 ? 0.2138 0.1594 0.1719 -0.0408 -0.0494 0.0244  103 LYS   A CD  
1586  C  CE  . LYS   A 103 ? 0.2418 0.1851 0.1905 -0.0421 -0.0472 0.0245  103 LYS   A CE  
1587  N  NZ  . LYS   A 103 ? 0.2340 0.1805 0.1829 -0.0372 -0.0400 0.0217  103 LYS   A NZ  
1601  N  N   . LYS   A 104 ? 0.1924 0.1320 0.1640 -0.0467 -0.0675 0.0265  104 LYS   A N   
1602  C  CA  . LYS   A 104 ? 0.2128 0.1495 0.1843 -0.0508 -0.0725 0.0272  104 LYS   A CA  
1603  C  C   . LYS   A 104 ? 0.2393 0.1815 0.2187 -0.0545 -0.0768 0.0253  104 LYS   A C   
1604  O  O   . LYS   A 104 ? 0.2542 0.1959 0.2346 -0.0583 -0.0807 0.0252  104 LYS   A O   
1605  C  CB  . LYS   A 104 ? 0.2463 0.1757 0.2084 -0.0495 -0.0744 0.0295  104 LYS   A CB  
1606  C  CG  . LYS   A 104 ? 0.2495 0.1724 0.2012 -0.0471 -0.0711 0.0318  104 LYS   A CG  
1607  C  CD  . LYS   A 104 ? 0.2383 0.1577 0.1899 -0.0459 -0.0717 0.0326  104 LYS   A CD  
1608  C  CE  . LYS   A 104 ? 0.2904 0.2104 0.2343 -0.0431 -0.0650 0.0301  104 LYS   A CE  
1609  N  NZ  . LYS   A 104 ? 0.3409 0.2591 0.2817 -0.0414 -0.0643 0.0293  104 LYS   A NZ  
1623  N  N   . ALA   A 105 ? 0.2249 0.1736 0.2140 -0.0536 -0.0759 0.0239  105 ALA   A N   
1624  C  CA  . ALA   A 105 ? 0.1845 0.1414 0.1897 -0.0572 -0.0794 0.0225  105 ALA   A CA  
1625  C  C   . ALA   A 105 ? 0.2012 0.1617 0.2067 -0.0600 -0.0781 0.0210  105 ALA   A C   
1626  O  O   . ALA   A 105 ? 0.2068 0.1732 0.2214 -0.0636 -0.0810 0.0202  105 ALA   A O   
1627  C  CB  . ALA   A 105 ? 0.1855 0.1471 0.1966 -0.0552 -0.0790 0.0220  105 ALA   A CB  
1633  N  N   . GLY   A 106 ? 0.2152 0.1726 0.2129 -0.0584 -0.0738 0.0208  106 GLY   A N   
1634  C  CA  . GLY   A 106 ? 0.2224 0.1825 0.2216 -0.0610 -0.0725 0.0192  106 GLY   A CA  
1635  C  C   . GLY   A 106 ? 0.2181 0.1827 0.2200 -0.0591 -0.0677 0.0178  106 GLY   A C   
1636  O  O   . GLY   A 106 ? 0.2030 0.1711 0.2107 -0.0617 -0.0668 0.0165  106 GLY   A O   
1640  N  N   . TRP   A 107 ? 0.1905 0.1563 0.1951 -0.0550 -0.0647 0.0177  107 TRP   A N   
1641  C  CA  . TRP   A 107 ? 0.1745 0.1456 0.1848 -0.0532 -0.0603 0.0161  107 TRP   A CA  
1642  C  C   . TRP   A 107 ? 0.1917 0.1583 0.1888 -0.0486 -0.0552 0.0163  107 TRP   A C   
1643  O  O   . TRP   A 107 ? 0.1868 0.1493 0.1795 -0.0455 -0.0549 0.0179  107 TRP   A O   
1644  C  CB  . TRP   A 107 ? 0.1840 0.1604 0.2033 -0.0525 -0.0610 0.0154  107 TRP   A CB  
1645  C  CG  . TRP   A 107 ? 0.2017 0.1821 0.2285 -0.0567 -0.0663 0.0157  107 TRP   A CG  
1646  C  CD1 . TRP   A 107 ? 0.2033 0.1830 0.2334 -0.0572 -0.0707 0.0170  107 TRP   A CD1 
1647  C  CD2 . TRP   A 107 ? 0.1756 0.1640 0.2179 -0.0612 -0.0676 0.0150  107 TRP   A CD2 
1648  N  NE1 . TRP   A 107 ? 0.1801 0.1666 0.2230 -0.0616 -0.0748 0.0170  107 TRP   A NE1 
1649  C  CE2 . TRP   A 107 ? 0.1983 0.1889 0.2430 -0.0642 -0.0731 0.0159  107 TRP   A CE2 
1650  C  CE3 . TRP   A 107 ? 0.1996 0.1904 0.2402 -0.0631 -0.0649 0.0137  107 TRP   A CE3 
1651  C  CZ2 . TRP   A 107 ? 0.2109 0.2093 0.2689 -0.0690 -0.0758 0.0159  107 TRP   A CZ2 
1652  C  CZ3 . TRP   A 107 ? 0.1913 0.1896 0.2468 -0.0680 -0.0677 0.0136  107 TRP   A CZ3 
1653  C  CH2 . TRP   A 107 ? 0.2501 0.2503 0.3049 -0.0707 -0.0729 0.0148  107 TRP   A CH2 
1664  N  N   . ASP   A 108 ? 0.1805 0.1495 0.1788 -0.0485 -0.0513 0.0150  108 ASP   A N   
1665  C  CA  . ASP   A 108 ? 0.1872 0.1539 0.1770 -0.0443 -0.0463 0.0151  108 ASP   A CA  
1666  C  C   . ASP   A 108 ? 0.1846 0.1550 0.1772 -0.0414 -0.0434 0.0137  108 ASP   A C   
1667  O  O   . ASP   A 108 ? 0.1621 0.1312 0.1518 -0.0374 -0.0401 0.0144  108 ASP   A O   
1668  C  CB  . ASP   A 108 ? 0.1988 0.1658 0.1842 -0.0454 -0.0436 0.0144  108 ASP   A CB  
1669  C  CG  . ASP   A 108 ? 0.2063 0.1691 0.1872 -0.0480 -0.0458 0.0155  108 ASP   A CG  
1670  O  OD1 . ASP   A 108 ? 0.2089 0.1661 0.1792 -0.0464 -0.0457 0.0176  108 ASP   A OD1 
1671  O  OD2 . ASP   A 108 ? 0.2418 0.2058 0.2240 -0.0515 -0.0474 0.0144  108 ASP   A OD2 
1676  N  N   . MET   A 109 ? 0.1641 0.1409 0.1705 -0.0434 -0.0440 0.0119  109 MET   A N   
1677  C  CA  . MET   A 109 ? 0.1476 0.1294 0.1620 -0.0413 -0.0409 0.0099  109 MET   A CA  
1678  C  C   . MET   A 109 ? 0.1642 0.1513 0.1870 -0.0438 -0.0432 0.0091  109 MET   A C   
1679  O  O   . MET   A 109 ? 0.1532 0.1432 0.1845 -0.0481 -0.0464 0.0096  109 MET   A O   
1680  C  CB  . MET   A 109 ? 0.1520 0.1355 0.1646 -0.0409 -0.0362 0.0082  109 MET   A CB  
1681  C  CG  . MET   A 109 ? 0.1801 0.1684 0.1969 -0.0397 -0.0325 0.0058  109 MET   A CG  
1682  S  SD  . MET   A 109 ? 0.1886 0.1770 0.2017 -0.0381 -0.0269 0.0042  109 MET   A SD  
1683  C  CE  . MET   A 109 ? 0.1861 0.1759 0.2027 -0.0433 -0.0285 0.0040  109 MET   A CE  
1693  N  N   . ILE   A 110 ? 0.1368 0.1275 0.1684 -0.0415 -0.0418 0.0083  110 ILE   A N   
1694  C  CA  . ILE   A 110 ? 0.1241 0.1224 0.1701 -0.0438 -0.0432 0.0077  110 ILE   A CA  
1695  C  C   . ILE   A 110 ? 0.1442 0.1464 0.1912 -0.0430 -0.0383 0.0055  110 ILE   A C   
1696  O  O   . ILE   A 110 ? 0.1566 0.1565 0.1992 -0.0387 -0.0348 0.0048  110 ILE   A O   
1697  C  CB  . ILE   A 110 ? 0.1431 0.1403 0.1892 -0.0423 -0.0468 0.0090  110 ILE   A CB  
1698  C  CG1 . ILE   A 110 ? 0.1585 0.1498 0.1992 -0.0428 -0.0512 0.0112  110 ILE   A CG1 
1699  C  CG2 . ILE   A 110 ? 0.1282 0.1344 0.1891 -0.0449 -0.0483 0.0089  110 ILE   A CG2 
1700  C  CD1 . ILE   A 110 ? 0.1720 0.1619 0.2141 -0.0413 -0.0546 0.0123  110 ILE   A CD1 
1712  N  N   . ILE   A 111 ? 0.1222 0.1323 0.1821 -0.0466 -0.0376 0.0050  111 ILE   A N   
1713  C  CA  . ILE   A 111 ? 0.1389 0.1532 0.1996 -0.0463 -0.0329 0.0033  111 ILE   A CA  
1714  C  C   . ILE   A 111 ? 0.1276 0.1510 0.2040 -0.0477 -0.0346 0.0041  111 ILE   A C   
1715  O  O   . ILE   A 111 ? 0.1233 0.1523 0.2086 -0.0519 -0.0378 0.0054  111 ILE   A O   
1716  C  CB  . ILE   A 111 ? 0.0960 0.1135 0.1626 -0.0492 -0.0301 0.0022  111 ILE   A CB  
1717  C  CG1 . ILE   A 111 ? 0.1074 0.1174 0.1632 -0.0477 -0.0289 0.0018  111 ILE   A CG1 
1718  C  CG2 . ILE   A 111 ? 0.0922 0.1142 0.1614 -0.0488 -0.0251 0.0008  111 ILE   A CG2 
1719  C  CD1 . ILE   A 111 ? 0.1739 0.1837 0.2244 -0.0509 -0.0278 0.0013  111 ILE   A CD1 
1731  N  N   . VAL   A 112 ? 0.1136 0.1383 0.1934 -0.0444 -0.0328 0.0037  112 VAL   A N   
1732  C  CA  . VAL   A 112 ? 0.1169 0.1498 0.2063 -0.0451 -0.0343 0.0045  112 VAL   A CA  
1733  C  C   . VAL   A 112 ? 0.1004 0.1413 0.2005 -0.0456 -0.0294 0.0038  112 VAL   A C   
1734  O  O   . VAL   A 112 ? 0.1303 0.1668 0.2207 -0.0425 -0.0252 0.0026  112 VAL   A O   
1735  C  CB  . VAL   A 112 ? 0.1058 0.1359 0.1972 -0.0411 -0.0361 0.0049  112 VAL   A CB  
1736  C  CG1 . VAL   A 112 ? 0.1098 0.1498 0.2131 -0.0418 -0.0379 0.0060  112 VAL   A CG1 
1737  C  CG2 . VAL   A 112 ? 0.1141 0.1361 0.1960 -0.0406 -0.0407 0.0060  112 VAL   A CG2 
1747  N  N   . GLU   A 113 ? 0.1021 0.1533 0.2125 -0.0495 -0.0301 0.0053  113 GLU   A N   
1748  C  CA  . GLU   A 113 ? 0.1013 0.1614 0.2225 -0.0504 -0.0254 0.0053  113 GLU   A CA  
1749  C  C   . GLU   A 113 ? 0.1164 0.1874 0.2467 -0.0497 -0.0252 0.0067  113 GLU   A C   
1750  O  O   . GLU   A 113 ? 0.1185 0.1943 0.2574 -0.0503 -0.0296 0.0081  113 GLU   A O   
1751  C  CB  . GLU   A 113 ? 0.1403 0.2036 0.2601 -0.0554 -0.0252 0.0058  113 GLU   A CB  
1752  C  CG  . GLU   A 113 ? 0.1411 0.1960 0.2555 -0.0566 -0.0254 0.0047  113 GLU   A CG  
1753  C  CD  . GLU   A 113 ? 0.1973 0.2544 0.3074 -0.0616 -0.0260 0.0055  113 GLU   A CD  
1754  O  OE1 . GLU   A 113 ? 0.1555 0.2234 0.2857 -0.0648 -0.0288 0.0076  113 GLU   A OE1 
1755  O  OE2 . GLU   A 113 ? 0.1627 0.2162 0.2739 -0.0625 -0.0240 0.0044  113 GLU   A OE2 
1762  N  N   . ASP   A 114 ? 0.0975 0.1746 0.2353 -0.0483 -0.0203 0.0066  114 ASP   A N   
1763  C  CA  . ASP   A 114 ? 0.1160 0.2060 0.2646 -0.0473 -0.0192 0.0082  114 ASP   A CA  
1764  C  C   . ASP   A 114 ? 0.1041 0.1947 0.2571 -0.0434 -0.0218 0.0082  114 ASP   A C   
1765  O  O   . ASP   A 114 ? 0.0936 0.1723 0.2362 -0.0404 -0.0228 0.0068  114 ASP   A O   
1766  C  CB  . ASP   A 114 ? 0.1113 0.2149 0.2782 -0.0519 -0.0206 0.0102  114 ASP   A CB  
1767  C  CG  . ASP   A 114 ? 0.1710 0.2874 0.3427 -0.0517 -0.0163 0.0116  114 ASP   A CG  
1768  O  OD1 . ASP   A 114 ? 0.1462 0.2713 0.3311 -0.0478 -0.0157 0.0119  114 ASP   A OD1 
1769  O  OD2 . ASP   A 114 ? 0.1551 0.2769 0.3352 -0.0549 -0.0135 0.0121  114 ASP   A OD2 
1774  N  N   . LYS   A 115 ? 0.1076 0.2118 0.2750 -0.0429 -0.0229 0.0099  115 LYS   A N   
1775  C  CA  . LYS   A 115 ? 0.1189 0.2245 0.2884 -0.0387 -0.0254 0.0101  115 LYS   A CA  
1776  C  C   . LYS   A 115 ? 0.1099 0.2281 0.2960 -0.0403 -0.0301 0.0121  115 LYS   A C   
1777  O  O   . LYS   A 115 ? 0.1248 0.2553 0.3202 -0.0428 -0.0289 0.0136  115 LYS   A O   
1778  C  CB  . LYS   A 115 ? 0.0886 0.2012 0.2676 -0.0339 -0.0204 0.0096  115 LYS   A CB  
1779  C  CG  . LYS   A 115 ? 0.1302 0.2458 0.3105 -0.0289 -0.0220 0.0097  115 LYS   A CG  
1780  C  CD  . LYS   A 115 ? 0.1577 0.2826 0.3450 -0.0239 -0.0170 0.0096  115 LYS   A CD  
1781  C  CE  . LYS   A 115 ? 0.1793 0.3079 0.3738 -0.0183 -0.0184 0.0094  115 LYS   A CE  
1782  N  NZ  . LYS   A 115 ? 0.2538 0.3878 0.4459 -0.0124 -0.0129 0.0088  115 LYS   A NZ  
1796  N  N   . ALA   A 116 ? 0.1101 0.2237 0.2925 -0.0389 -0.0352 0.0123  116 ALA   A N   
1797  C  CA  . ALA   A 116 ? 0.0878 0.2068 0.2756 -0.0372 -0.0372 0.0125  116 ALA   A CA  
1798  C  C   . ALA   A 116 ? 0.1201 0.2590 0.3267 -0.0352 -0.0380 0.0148  116 ALA   A C   
1799  O  O   . ALA   A 116 ? 0.1125 0.2489 0.3184 -0.0305 -0.0345 0.0136  116 ALA   A O   
1800  C  CB  . ALA   A 116 ? 0.1316 0.2466 0.3189 -0.0395 -0.0464 0.0141  116 ALA   A CB  
1806  N  N   . ASP   A 117 ? 0.1147 0.2704 0.3419 -0.0361 -0.0397 0.0169  117 ASP   A N   
1807  C  CA  . ASP   A 117 ? 0.1603 0.3303 0.3955 -0.0311 -0.0373 0.0176  117 ASP   A CA  
1808  C  C   . ASP   A 117 ? 0.1533 0.3230 0.3924 -0.0260 -0.0409 0.0174  117 ASP   A C   
1809  O  O   . ASP   A 117 ? 0.1915 0.3713 0.4369 -0.0204 -0.0388 0.0175  117 ASP   A O   
1810  C  CB  . ASP   A 117 ? 0.1444 0.3330 0.4015 -0.0336 -0.0375 0.0197  117 ASP   A CB  
1811  C  CG  . ASP   A 117 ? 0.1874 0.3781 0.4524 -0.0381 -0.0445 0.0215  117 ASP   A CG  
1812  O  OD1 . ASP   A 117 ? 0.1855 0.3638 0.4364 -0.0383 -0.0494 0.0210  117 ASP   A OD1 
1813  O  OD2 . ASP   A 117 ? 0.3523 0.5517 0.6150 -0.0414 -0.0450 0.0233  117 ASP   A OD2 
1818  N  N   . SER   A 118 ? 0.1124 0.2700 0.3448 -0.0275 -0.0464 0.0171  118 SER   A N   
1819  C  CA  . SER   A 118 ? 0.1277 0.2815 0.3564 -0.0231 -0.0506 0.0170  118 SER   A CA  
1820  C  C   . SER   A 118 ? 0.1178 0.2520 0.3304 -0.0250 -0.0536 0.0156  118 SER   A C   
1821  O  O   . SER   A 118 ? 0.1075 0.2337 0.3122 -0.0300 -0.0541 0.0156  118 SER   A O   
1822  C  CB  . SER   A 118 ? 0.1667 0.3331 0.4084 -0.0231 -0.0559 0.0191  118 SER   A CB  
1823  O  OG  . SER   A 118 ? 0.2245 0.3855 0.4610 -0.0289 -0.0613 0.0202  118 SER   A OG  
1829  N  N   . PRO   A 119 ? 0.1431 0.2672 0.3429 -0.0208 -0.0552 0.0146  119 PRO   A N   
1830  C  CA  . PRO   A 119 ? 0.0889 0.1892 0.2694 -0.0204 -0.0537 0.0124  119 PRO   A CA  
1831  C  C   . PRO   A 119 ? 0.1005 0.2026 0.2844 -0.0272 -0.0630 0.0147  119 PRO   A C   
1832  O  O   . PRO   A 119 ? 0.1066 0.2177 0.3009 -0.0281 -0.0675 0.0164  119 PRO   A O   
1833  C  CB  . PRO   A 119 ? 0.1036 0.2063 0.2917 -0.0169 -0.0599 0.0128  119 PRO   A CB  
1834  C  CG  . PRO   A 119 ? 0.1415 0.2571 0.3376 -0.0117 -0.0559 0.0128  119 PRO   A CG  
1835  C  CD  . PRO   A 119 ? 0.1396 0.2720 0.3506 -0.0142 -0.0547 0.0145  119 PRO   A CD  
1843  N  N   . VAL   A 120 ? 0.0934 0.1769 0.2553 -0.0284 -0.0582 0.0128  120 VAL   A N   
1844  C  CA  . VAL   A 120 ? 0.1000 0.1791 0.2587 -0.0327 -0.0628 0.0140  120 VAL   A CA  
1845  C  C   . VAL   A 120 ? 0.1032 0.1670 0.2496 -0.0337 -0.0662 0.0136  120 VAL   A C   
1846  O  O   . VAL   A 120 ? 0.0995 0.1569 0.2422 -0.0313 -0.0641 0.0123  120 VAL   A O   
1847  C  CB  . VAL   A 120 ? 0.1253 0.2156 0.2947 -0.0399 -0.0659 0.0157  120 VAL   A CB  
1848  C  CG1 . VAL   A 120 ? 0.1040 0.2077 0.2836 -0.0379 -0.0610 0.0157  120 VAL   A CG1 
1849  C  CG2 . VAL   A 120 ? 0.1031 0.1859 0.2667 -0.0399 -0.0599 0.0140  120 VAL   A CG2 
1859  N  N   . TYR   A 121 ? 0.1051 0.1610 0.2417 -0.0351 -0.0677 0.0143  121 TYR   A N   
1860  C  CA  . TYR   A 121 ? 0.1166 0.1612 0.2472 -0.0377 -0.0732 0.0147  121 TYR   A CA  
1861  C  C   . TYR   A 121 ? 0.1233 0.1671 0.2502 -0.0425 -0.0748 0.0156  121 TYR   A C   
1862  O  O   . TYR   A 121 ? 0.1234 0.1772 0.2603 -0.0456 -0.0771 0.0168  121 TYR   A O   
1863  C  CB  . TYR   A 121 ? 0.1305 0.1666 0.2545 -0.0356 -0.0774 0.0153  121 TYR   A CB  
1864  C  CG  . TYR   A 121 ? 0.1212 0.1600 0.2497 -0.0365 -0.0811 0.0169  121 TYR   A CG  
1865  C  CD1 . TYR   A 121 ? 0.1400 0.1923 0.2841 -0.0370 -0.0870 0.0181  121 TYR   A CD1 
1866  C  CD2 . TYR   A 121 ? 0.1409 0.1742 0.2637 -0.0410 -0.0877 0.0186  121 TYR   A CD2 
1867  C  CE1 . TYR   A 121 ? 0.1733 0.2293 0.3210 -0.0393 -0.0932 0.0199  121 TYR   A CE1 
1868  C  CE2 . TYR   A 121 ? 0.1509 0.1884 0.2804 -0.0435 -0.0938 0.0203  121 TYR   A CE2 
1869  C  CZ  . TYR   A 121 ? 0.1866 0.2348 0.3269 -0.0427 -0.0969 0.0210  121 TYR   A CZ  
1870  O  OH  . TYR   A 121 ? 0.2156 0.2679 0.3605 -0.0448 -0.1032 0.0229  121 TYR   A OH  
1880  N  N   . ILE   A 122 ? 0.1176 0.1498 0.2314 -0.0423 -0.0730 0.0152  122 ILE   A N   
1881  C  CA  . ILE   A 122 ? 0.1139 0.1417 0.2169 -0.0429 -0.0690 0.0150  122 ILE   A CA  
1882  C  C   . ILE   A 122 ? 0.1206 0.1391 0.2146 -0.0436 -0.0737 0.0165  122 ILE   A C   
1883  O  O   . ILE   A 122 ? 0.1291 0.1404 0.2192 -0.0435 -0.0781 0.0169  122 ILE   A O   
1884  C  CB  . ILE   A 122 ? 0.1380 0.1647 0.2385 -0.0467 -0.0689 0.0144  122 ILE   A CB  
1885  C  CG1 . ILE   A 122 ? 0.1303 0.1673 0.2412 -0.0467 -0.0646 0.0133  122 ILE   A CG1 
1886  C  CG2 . ILE   A 122 ? 0.1204 0.1433 0.2157 -0.0487 -0.0687 0.0146  122 ILE   A CG2 
1887  C  CD1 . ILE   A 122 ? 0.1051 0.1378 0.2103 -0.0448 -0.0580 0.0114  122 ILE   A CD1 
1899  N  N   . GLU   A 123 ? 0.1284 0.1495 0.2242 -0.0474 -0.0780 0.0177  123 GLU   A N   
1900  C  CA  . GLU   A 123 ? 0.1355 0.1493 0.2264 -0.0484 -0.0826 0.0192  123 GLU   A CA  
1901  C  C   . GLU   A 123 ? 0.1436 0.1543 0.2286 -0.0530 -0.0850 0.0196  123 GLU   A C   
1902  O  O   . GLU   A 123 ? 0.1442 0.1610 0.2338 -0.0555 -0.0844 0.0194  123 GLU   A O   
1903  C  CB  . GLU   A 123 ? 0.1561 0.1784 0.2593 -0.0542 -0.0946 0.0212  123 GLU   A CB  
1904  C  CG  . GLU   A 123 ? 0.1506 0.1636 0.2465 -0.0513 -0.0937 0.0221  123 GLU   A CG  
1905  C  CD  . GLU   A 123 ? 0.2066 0.2280 0.3133 -0.0567 -0.1057 0.0240  123 GLU   A CD  
1906  O  OE1 . GLU   A 123 ? 0.2220 0.2547 0.3417 -0.0562 -0.1060 0.0240  123 GLU   A OE1 
1907  O  OE2 . GLU   A 123 ? 0.2285 0.2449 0.3306 -0.0584 -0.1103 0.0254  123 GLU   A OE2 
1914  N  N   . ILE   A 124 ? 0.1587 0.1591 0.2321 -0.0539 -0.0872 0.0201  124 ILE   A N   
1915  C  CA  . ILE   A 124 ? 0.1430 0.1390 0.2082 -0.0524 -0.0817 0.0198  124 ILE   A CA  
1916  C  C   . ILE   A 124 ? 0.1645 0.1526 0.2214 -0.0576 -0.0911 0.0218  124 ILE   A C   
1917  O  O   . ILE   A 124 ? 0.1673 0.1483 0.2180 -0.0543 -0.0909 0.0225  124 ILE   A O   
1918  C  CB  . ILE   A 124 ? 0.1688 0.1602 0.2259 -0.0538 -0.0809 0.0191  124 ILE   A CB  
1919  C  CG1 . ILE   A 124 ? 0.1824 0.1810 0.2457 -0.0529 -0.0764 0.0175  124 ILE   A CG1 
1920  C  CG2 . ILE   A 124 ? 0.1508 0.1386 0.2026 -0.0563 -0.0809 0.0192  124 ILE   A CG2 
1921  C  CD1 . ILE   A 124 ? 0.1520 0.1467 0.2115 -0.0493 -0.0706 0.0163  124 ILE   A CD1 
1933  N  N   . VAL   A 125 ? 0.1588 0.1484 0.2157 -0.0577 -0.0893 0.0221  125 VAL   A N   
1934  C  CA  . VAL   A 125 ? 0.1908 0.1731 0.2417 -0.0638 -0.0987 0.0235  125 VAL   A CA  
1935  C  C   . VAL   A 125 ? 0.2086 0.1892 0.2523 -0.0668 -0.0981 0.0230  125 VAL   A C   
1936  O  O   . VAL   A 125 ? 0.1917 0.1796 0.2472 -0.0711 -0.1011 0.0227  125 VAL   A O   
1937  C  CB  . VAL   A 125 ? 0.2015 0.1876 0.2620 -0.0662 -0.1055 0.0248  125 VAL   A CB  
1938  C  CG1 . VAL   A 125 ? 0.2848 0.2609 0.3279 -0.0681 -0.1088 0.0259  125 VAL   A CG1 
1939  C  CG2 . VAL   A 125 ? 0.2179 0.2047 0.2786 -0.0632 -0.1061 0.0252  125 VAL   A CG2 
1949  N  N   . ASP   A 126 ? 0.1812 0.1556 0.2190 -0.0649 -0.0943 0.0227  126 ASP   A N   
1950  C  CA  . ASP   A 126 ? 0.2018 0.1746 0.2332 -0.0674 -0.0931 0.0221  126 ASP   A CA  
1951  C  C   . ASP   A 126 ? 0.1981 0.1797 0.2392 -0.0691 -0.0912 0.0207  126 ASP   A C   
1952  O  O   . ASP   A 126 ? 0.1702 0.1548 0.2160 -0.0660 -0.0869 0.0199  126 ASP   A O   
1953  C  CB  . ASP   A 126 ? 0.2166 0.1867 0.2458 -0.0714 -0.0982 0.0228  126 ASP   A CB  
1954  C  CG  . ASP   A 126 ? 0.2576 0.2174 0.2718 -0.0697 -0.0989 0.0241  126 ASP   A CG  
1955  O  OD1 . ASP   A 126 ? 0.2525 0.2075 0.2605 -0.0660 -0.0943 0.0243  126 ASP   A OD1 
1956  O  OD2 . ASP   A 126 ? 0.2611 0.2195 0.2763 -0.0722 -0.1038 0.0249  126 ASP   A OD2 
1961  N  N   . ASP   A 127 ? 0.2048 0.1908 0.2521 -0.0739 -0.0943 0.0206  127 ASP   A N   
1962  C  CA  . ASP   A 127 ? 0.1866 0.1827 0.2517 -0.0761 -0.0927 0.0196  127 ASP   A CA  
1963  C  C   . ASP   A 127 ? 0.2116 0.2164 0.2844 -0.0772 -0.0948 0.0200  127 ASP   A C   
1964  O  O   . ASP   A 127 ? 0.2368 0.2492 0.3176 -0.0789 -0.0930 0.0196  127 ASP   A O   
1965  C  CB  . ASP   A 127 ? 0.2770 0.2717 0.3348 -0.0807 -0.0947 0.0194  127 ASP   A CB  
1966  C  CG  . ASP   A 127 ? 0.3471 0.3444 0.4125 -0.0850 -0.1015 0.0203  127 ASP   A CG  
1967  O  OD1 . ASP   A 127 ? 0.3471 0.3383 0.4042 -0.0844 -0.1043 0.0210  127 ASP   A OD1 
1968  O  OD2 . ASP   A 127 ? 0.4606 0.4636 0.5283 -0.0891 -0.1038 0.0205  127 ASP   A OD2 
1973  N  N   . LYS   A 128 ? 0.2147 0.2197 0.2899 -0.0765 -0.0984 0.0211  128 LYS   A N   
1974  C  CA  . LYS   A 128 ? 0.2155 0.2308 0.3042 -0.0771 -0.1007 0.0218  128 LYS   A CA  
1975  C  C   . LYS   A 128 ? 0.2003 0.2171 0.2888 -0.0725 -0.0959 0.0210  128 LYS   A C   
1976  O  O   . LYS   A 128 ? 0.1697 0.1799 0.2534 -0.0681 -0.0938 0.0208  128 LYS   A O   
1977  C  CB  . LYS   A 128 ? 0.2394 0.2550 0.3316 -0.0782 -0.1068 0.0232  128 LYS   A CB  
1978  C  CG  . LYS   A 128 ? 0.2863 0.3141 0.3957 -0.0796 -0.1103 0.0242  128 LYS   A CG  
1979  C  CD  . LYS   A 128 ? 0.4205 0.4460 0.5238 -0.0791 -0.1154 0.0255  128 LYS   A CD  
1980  C  CE  . LYS   A 128 ? 0.4695 0.5088 0.5929 -0.0802 -0.1186 0.0266  128 LYS   A CE  
1981  N  NZ  . LYS   A 128 ? 0.5540 0.5915 0.6730 -0.0804 -0.1245 0.0280  128 LYS   A NZ  
1995  N  N   . VAL   A 129 ? 0.1656 0.1915 0.2651 -0.0708 -0.0905 0.0201  129 VAL   A N   
1996  C  CA  . VAL   A 129 ? 0.1506 0.1783 0.2517 -0.0644 -0.0830 0.0186  129 VAL   A CA  
1997  C  C   . VAL   A 129 ? 0.1732 0.2150 0.2898 -0.0699 -0.0897 0.0202  129 VAL   A C   
1998  O  O   . VAL   A 129 ? 0.1554 0.2035 0.2788 -0.0696 -0.0856 0.0197  129 VAL   A O   
1999  C  CB  . VAL   A 129 ? 0.1584 0.1859 0.2586 -0.0677 -0.0821 0.0179  129 VAL   A CB  
2000  C  CG1 . VAL   A 129 ? 0.1691 0.1979 0.2696 -0.0633 -0.0773 0.0168  129 VAL   A CG1 
2001  C  CG2 . VAL   A 129 ? 0.1752 0.1915 0.2605 -0.0671 -0.0811 0.0175  129 VAL   A CG2 
2011  N  N   . GLU   A 130 ? 0.1471 0.1889 0.2655 -0.0623 -0.0843 0.0195  130 GLU   A N   
2012  C  CA  . GLU   A 130 ? 0.1473 0.2016 0.2789 -0.0627 -0.0856 0.0201  130 GLU   A CA  
2013  C  C   . GLU   A 130 ? 0.1450 0.2043 0.2848 -0.0612 -0.0850 0.0199  130 GLU   A C   
2014  O  O   . GLU   A 130 ? 0.1503 0.2006 0.2820 -0.0584 -0.0844 0.0191  130 GLU   A O   
2015  C  CB  . GLU   A 130 ? 0.1547 0.2122 0.2930 -0.0638 -0.0921 0.0218  130 GLU   A CB  
2016  C  CG  . GLU   A 130 ? 0.1976 0.2543 0.3414 -0.0716 -0.1027 0.0239  130 GLU   A CG  
2017  C  CD  . GLU   A 130 ? 0.3164 0.3734 0.4568 -0.0724 -0.1094 0.0255  130 GLU   A CD  
2018  O  OE1 . GLU   A 130 ? 0.3248 0.3731 0.4588 -0.0700 -0.1108 0.0255  130 GLU   A OE1 
2019  O  OE2 . GLU   A 130 ? 0.3580 0.4265 0.5121 -0.0752 -0.1130 0.0269  130 GLU   A OE2 
2026  N  N   . ILE   A 131 ? 0.1359 0.2048 0.2826 -0.0586 -0.0792 0.0192  131 ILE   A N   
2027  C  CA  . ILE   A 131 ? 0.1282 0.2010 0.2792 -0.0543 -0.0753 0.0183  131 ILE   A CA  
2028  C  C   . ILE   A 131 ? 0.1316 0.2135 0.2938 -0.0533 -0.0797 0.0197  131 ILE   A C   
2029  O  O   . ILE   A 131 ? 0.1378 0.2297 0.3096 -0.0566 -0.0832 0.0211  131 ILE   A O   
2030  C  CB  . ILE   A 131 ? 0.1236 0.2049 0.2816 -0.0548 -0.0699 0.0174  131 ILE   A CB  
2031  C  CG1 . ILE   A 131 ? 0.1286 0.2055 0.2844 -0.0594 -0.0703 0.0173  131 ILE   A CG1 
2032  C  CG2 . ILE   A 131 ? 0.1321 0.2239 0.3043 -0.0539 -0.0710 0.0181  131 ILE   A CG2 
2033  C  CD1 . ILE   A 131 ? 0.1255 0.2100 0.2867 -0.0608 -0.0653 0.0169  131 ILE   A CD1 
2045  N  N   . LYS   A 132 ? 0.1382 0.2212 0.3070 -0.0522 -0.0849 0.0205  132 LYS   A N   
2046  C  CA  . LYS   A 132 ? 0.1402 0.2312 0.3188 -0.0507 -0.0895 0.0217  132 LYS   A CA  
2047  C  C   . LYS   A 132 ? 0.1346 0.2303 0.3168 -0.0454 -0.0861 0.0210  132 LYS   A C   
2048  O  O   . LYS   A 132 ? 0.1185 0.2018 0.2845 -0.0400 -0.0763 0.0180  132 LYS   A O   
2049  C  CB  . LYS   A 132 ? 0.1606 0.2411 0.3317 -0.0510 -0.0950 0.0225  132 LYS   A CB  
2050  C  CG  . LYS   A 132 ? 0.2110 0.2882 0.3758 -0.0561 -0.0994 0.0237  132 LYS   A CG  
2051  C  CD  . LYS   A 132 ? 0.2231 0.2926 0.3857 -0.0565 -0.1050 0.0246  132 LYS   A CD  
2052  C  CE  . LYS   A 132 ? 0.3030 0.3711 0.4601 -0.0616 -0.1098 0.0260  132 LYS   A CE  
2053  N  NZ  . LYS   A 132 ? 0.3557 0.4155 0.5048 -0.0619 -0.1152 0.0270  132 LYS   A NZ  
2067  N  N   . ASP   A 133 ? 0.1288 0.2316 0.3166 -0.0412 -0.0842 0.0211  133 ASP   A N   
2068  C  CA  . ASP   A 133 ? 0.1504 0.2653 0.3529 -0.0380 -0.0866 0.0218  133 ASP   A CA  
2069  C  C   . ASP   A 133 ? 0.1210 0.2164 0.3031 -0.0323 -0.0818 0.0193  133 ASP   A C   
2070  O  O   . ASP   A 133 ? 0.1294 0.2199 0.3089 -0.0339 -0.0891 0.0206  133 ASP   A O   
2071  C  CB  . ASP   A 133 ? 0.1977 0.3297 0.4183 -0.0367 -0.0900 0.0238  133 ASP   A CB  
2072  C  CG  . ASP   A 133 ? 0.2513 0.3939 0.4811 -0.0306 -0.0867 0.0235  133 ASP   A CG  
2073  O  OD1 . ASP   A 133 ? 0.2260 0.3606 0.4492 -0.0270 -0.0831 0.0216  133 ASP   A OD1 
2074  O  OD2 . ASP   A 133 ? 0.3263 0.4844 0.5676 -0.0293 -0.0877 0.0251  133 ASP   A OD2 
2079  N  N   . ALA   A 134 ? 0.1132 0.2048 0.2893 -0.0284 -0.0767 0.0174  134 ALA   A N   
2080  C  CA  . ALA   A 134 ? 0.1160 0.1990 0.2903 -0.0263 -0.0803 0.0170  134 ALA   A CA  
2081  C  C   . ALA   A 134 ? 0.1350 0.2260 0.3152 -0.0209 -0.0808 0.0169  134 ALA   A C   
2082  O  O   . ALA   A 134 ? 0.1044 0.1803 0.2703 -0.0162 -0.0738 0.0143  134 ALA   A O   
2083  C  CB  . ALA   A 134 ? 0.1184 0.1899 0.2815 -0.0267 -0.0765 0.0152  134 ALA   A CB  
2089  N  N   . SER   A 135 ? 0.1188 0.2281 0.3207 -0.0195 -0.0820 0.0185  135 SER   A N   
2090  C  CA  . SER   A 135 ? 0.1595 0.2776 0.3670 -0.0129 -0.0811 0.0185  135 SER   A CA  
2091  C  C   . SER   A 135 ? 0.1894 0.2973 0.3869 -0.0098 -0.0852 0.0183  135 SER   A C   
2092  O  O   . SER   A 135 ? 0.1848 0.2941 0.3878 -0.0041 -0.0831 0.0173  135 SER   A O   
2093  C  CB  . SER   A 135 ? 0.1442 0.2831 0.3727 -0.0120 -0.0823 0.0206  135 SER   A CB  
2094  O  OG  . SER   A 135 ? 0.1802 0.3207 0.4089 -0.0149 -0.0891 0.0227  135 SER   A OG  
2100  N  N   . GLN   A 136 ? 0.1256 0.2263 0.3252 -0.0130 -0.0899 0.0191  136 GLN   A N   
2101  C  CA  . GLN   A 136 ? 0.1771 0.2687 0.3675 -0.0109 -0.0955 0.0193  136 GLN   A CA  
2102  C  C   . GLN   A 136 ? 0.1851 0.2564 0.3561 -0.0110 -0.0934 0.0170  136 GLN   A C   
2103  O  O   . GLN   A 136 ? 0.1887 0.2516 0.3562 -0.0089 -0.0962 0.0168  136 GLN   A O   
2104  C  CB  . GLN   A 136 ? 0.2258 0.3183 0.4177 -0.0143 -0.1026 0.0216  136 GLN   A CB  
2105  C  CG  . GLN   A 136 ? 0.2361 0.3491 0.4510 -0.0142 -0.1052 0.0239  136 GLN   A CG  
2106  C  CD  . GLN   A 136 ? 0.3460 0.4690 0.5594 -0.0073 -0.1036 0.0242  136 GLN   A CD  
2107  O  OE1 . GLN   A 136 ? 0.3089 0.4477 0.5429 -0.0055 -0.0995 0.0243  136 GLN   A OE1 
2108  N  NE2 . GLN   A 136 ? 0.3157 0.4370 0.5374 -0.0031 -0.1065 0.0244  136 GLN   A NE2 
2117  N  N   . LEU   A 137 ? 0.1372 0.2027 0.3048 -0.0133 -0.0887 0.0156  137 LEU   A N   
2118  C  CA  . LEU   A 137 ? 0.1382 0.1849 0.2876 -0.0130 -0.0859 0.0135  137 LEU   A CA  
2119  C  C   . LEU   A 137 ? 0.1172 0.1643 0.2682 -0.0091 -0.0799 0.0111  137 LEU   A C   
2120  O  O   . LEU   A 137 ? 0.1519 0.1853 0.2894 -0.0068 -0.0786 0.0092  137 LEU   A O   
2121  C  CB  . LEU   A 137 ? 0.1540 0.1928 0.2953 -0.0177 -0.0850 0.0139  137 LEU   A CB  
2122  C  CG  . LEU   A 137 ? 0.1827 0.2202 0.3202 -0.0220 -0.0905 0.0160  137 LEU   A CG  
2123  C  CD1 . LEU   A 137 ? 0.1696 0.2042 0.3040 -0.0261 -0.0887 0.0163  137 LEU   A CD1 
2124  C  CD2 . LEU   A 137 ? 0.1953 0.2204 0.3253 -0.0213 -0.0945 0.0165  137 LEU   A CD2 
2136  N  N   . TRP   A 138 ? 0.1050 0.1665 0.2669 -0.0082 -0.0762 0.0112  138 TRP   A N   
2137  C  CA  . TRP   A 138 ? 0.1523 0.2139 0.3082 -0.0044 -0.0699 0.0093  138 TRP   A CA  
2138  C  C   . TRP   A 138 ? 0.1414 0.1987 0.2963 0.0011  -0.0704 0.0078  138 TRP   A C   
2139  O  O   . TRP   A 138 ? 0.1073 0.1740 0.2744 0.0041  -0.0740 0.0093  138 TRP   A O   
2140  C  CB  . TRP   A 138 ? 0.1225 0.2036 0.2966 -0.0035 -0.0665 0.0102  138 TRP   A CB  
2141  C  CG  . TRP   A 138 ? 0.1170 0.1993 0.2915 -0.0017 -0.0594 0.0087  138 TRP   A CG  
2142  C  CD1 . TRP   A 138 ? 0.1520 0.2415 0.3284 0.0039  -0.0552 0.0080  138 TRP   A CD1 
2143  C  CD2 . TRP   A 138 ? 0.1272 0.2016 0.2920 -0.0057 -0.0554 0.0075  138 TRP   A CD2 
2144  N  NE1 . TRP   A 138 ? 0.1666 0.2542 0.3395 0.0034  -0.0491 0.0065  138 TRP   A NE1 
2145  C  CE2 . TRP   A 138 ? 0.1644 0.2421 0.3276 -0.0024 -0.0492 0.0062  138 TRP   A CE2 
2146  C  CE3 . TRP   A 138 ? 0.1216 0.1866 0.2772 -0.0108 -0.0565 0.0076  138 TRP   A CE3 
2147  C  CZ2 . TRP   A 138 ? 0.1556 0.2282 0.3138 -0.0048 -0.0443 0.0049  138 TRP   A CZ2 
2148  C  CZ3 . TRP   A 138 ? 0.1281 0.1880 0.2770 -0.0125 -0.0516 0.0065  138 TRP   A CZ3 
2149  C  CH2 . TRP   A 138 ? 0.1418 0.2052 0.2922 -0.0098 -0.0457 0.0051  138 TRP   A CH2 
2160  N  N   . GLY   A 139 ? 0.1162 0.1613 0.2633 0.0025  -0.0670 0.0051  139 GLY   A N   
2161  C  CA  . GLY   A 139 ? 0.1093 0.1489 0.2531 0.0074  -0.0670 0.0032  139 GLY   A CA  
2162  C  C   . GLY   A 139 ? 0.1399 0.1613 0.2700 0.0057  -0.0706 0.0019  139 GLY   A C   
2163  O  O   . GLY   A 139 ? 0.1616 0.1753 0.2845 0.0084  -0.0702 -0.0004 139 GLY   A O   
2167  N  N   . LYS   A 140 ? 0.1605 0.1744 0.2836 0.0012  -0.0738 0.0033  140 LYS   A N   
2168  C  CA  . LYS   A 140 ? 0.1622 0.1596 0.2734 0.0001  -0.0773 0.0030  140 LYS   A CA  
2169  C  C   . LYS   A 140 ? 0.1579 0.1384 0.2565 -0.0004 -0.0732 0.0009  140 LYS   A C   
2170  O  O   . LYS   A 140 ? 0.1379 0.1192 0.2351 -0.0014 -0.0693 0.0012  140 LYS   A O   
2171  C  CB  . LYS   A 140 ? 0.1414 0.1406 0.2571 -0.0034 -0.0827 0.0061  140 LYS   A CB  
2172  C  CG  . LYS   A 140 ? 0.1472 0.1600 0.2744 -0.0025 -0.0877 0.0083  140 LYS   A CG  
2173  C  CD  . LYS   A 140 ? 0.1767 0.1906 0.3076 -0.0064 -0.0932 0.0112  140 LYS   A CD  
2174  C  CE  . LYS   A 140 ? 0.2722 0.2965 0.4109 -0.0050 -0.0986 0.0131  140 LYS   A CE  
2175  N  NZ  . LYS   A 140 ? 0.3748 0.4136 0.5209 -0.0003 -0.0970 0.0131  140 LYS   A NZ  
2189  N  N   . VAL   A 141 ? 0.1867 0.1515 0.2707 0.0006  -0.0741 -0.0007 141 VAL   A N   
2190  C  CA  . VAL   A 141 ? 0.1478 0.1062 0.2221 0.0011  -0.0674 -0.0016 141 VAL   A CA  
2191  C  C   . VAL   A 141 ? 0.1519 0.1074 0.2152 -0.0012 -0.0675 0.0030  141 VAL   A C   
2192  O  O   . VAL   A 141 ? 0.1637 0.1165 0.2347 -0.0032 -0.0749 0.0050  141 VAL   A O   
2193  C  CB  . VAL   A 141 ? 0.1892 0.1437 0.2473 0.0023  -0.0645 -0.0038 141 VAL   A CB  
2194  C  CG1 . VAL   A 141 ? 0.1674 0.1251 0.2310 0.0042  -0.0636 -0.0075 141 VAL   A CG1 
2195  C  CG2 . VAL   A 141 ? 0.2205 0.1696 0.2797 0.0014  -0.0715 -0.0021 141 VAL   A CG2 
2205  N  N   . THR   A 142 ? 0.1453 0.1065 0.1899 -0.0190 -0.0743 0.0349  142 THR   A N   
2206  C  CA  . THR   A 142 ? 0.1776 0.1443 0.2121 -0.0261 -0.0696 0.0391  142 THR   A CA  
2207  C  C   . THR   A 142 ? 0.1700 0.1343 0.2026 -0.0290 -0.0722 0.0425  142 THR   A C   
2208  O  O   . THR   A 142 ? 0.1783 0.1488 0.2097 -0.0290 -0.0700 0.0426  142 THR   A O   
2209  C  CB  . THR   A 142 ? 0.1625 0.1300 0.1946 -0.0316 -0.0660 0.0401  142 THR   A CB  
2210  O  OG1 . THR   A 142 ? 0.1563 0.1269 0.1936 -0.0282 -0.0633 0.0363  142 THR   A OG1 
2211  C  CG2 . THR   A 142 ? 0.1544 0.1284 0.1796 -0.0336 -0.0603 0.0414  142 THR   A CG2 
2219  N  N   . SER   A 143 ? 0.1768 0.1312 0.2017 -0.0317 -0.0766 0.0451  143 SER   A N   
2220  C  CA  . SER   A 143 ? 0.1774 0.1304 0.1978 -0.0352 -0.0793 0.0490  143 SER   A CA  
2221  C  C   . SER   A 143 ? 0.2116 0.1638 0.2303 -0.0287 -0.0821 0.0481  143 SER   A C   
2222  O  O   . SER   A 143 ? 0.1873 0.1459 0.2082 -0.0305 -0.0813 0.0499  143 SER   A O   
2223  C  CB  . SER   A 143 ? 0.1831 0.1254 0.1941 -0.0399 -0.0840 0.0523  143 SER   A CB  
2224  O  OG  . SER   A 143 ? 0.2045 0.1329 0.2142 -0.0339 -0.0900 0.0508  143 SER   A OG  
2230  N  N   . GLU   A 144 ? 0.1962 0.1453 0.2243 -0.0202 -0.0861 0.0449  144 GLU   A N   
2231  C  CA  . GLU   A 144 ? 0.1880 0.1421 0.2224 -0.0122 -0.0894 0.0430  144 GLU   A CA  
2232  C  C   . GLU   A 144 ? 0.1694 0.1414 0.2099 -0.0118 -0.0844 0.0410  144 GLU   A C   
2233  O  O   . GLU   A 144 ? 0.1872 0.1659 0.2264 -0.0112 -0.0855 0.0417  144 GLU   A O   
2234  C  CB  . GLU   A 144 ? 0.2403 0.1875 0.2744 -0.0018 -0.0951 0.0388  144 GLU   A CB  
2235  C  CG  . GLU   A 144 ? 0.2771 0.2044 0.3100 -0.0021 -0.1021 0.0404  144 GLU   A CG  
2236  C  CD  . GLU   A 144 ? 0.4578 0.3730 0.4774 0.0099  -0.1088 0.0345  144 GLU   A CD  
2237  O  OE1 . GLU   A 144 ? 0.4297 0.3618 0.4671 0.0205  -0.1079 0.0286  144 GLU   A OE1 
2238  O  OE2 . GLU   A 144 ? 0.5175 0.4133 0.5328 0.0086  -0.1148 0.0352  144 GLU   A OE2 
2245  N  N   . THR   A 145 ? 0.1518 0.1316 0.1981 -0.0127 -0.0795 0.0382  145 THR   A N   
2246  C  CA  . THR   A 145 ? 0.1612 0.1552 0.2080 -0.0152 -0.0747 0.0368  145 THR   A CA  
2247  C  C   . THR   A 145 ? 0.1490 0.1410 0.1917 -0.0216 -0.0731 0.0400  145 THR   A C   
2248  O  O   . THR   A 145 ? 0.1616 0.1614 0.2042 -0.0223 -0.0733 0.0394  145 THR   A O   
2249  C  CB  . THR   A 145 ? 0.1283 0.1292 0.1853 -0.0167 -0.0695 0.0343  145 THR   A CB  
2250  O  OG1 . THR   A 145 ? 0.1547 0.1610 0.2146 -0.0094 -0.0709 0.0301  145 THR   A OG1 
2251  C  CG2 . THR   A 145 ? 0.1402 0.1507 0.1936 -0.0213 -0.0649 0.0339  145 THR   A CG2 
2259  N  N   . THR   A 146 ? 0.1401 0.1227 0.1750 -0.0265 -0.0719 0.0427  146 THR   A N   
2260  C  CA  . THR   A 146 ? 0.1591 0.1417 0.1865 -0.0311 -0.0703 0.0443  146 THR   A CA  
2261  C  C   . THR   A 146 ? 0.1958 0.1778 0.2174 -0.0301 -0.0746 0.0462  146 THR   A C   
2262  O  O   . THR   A 146 ? 0.1885 0.1756 0.2100 -0.0310 -0.0745 0.0453  146 THR   A O   
2263  C  CB  . THR   A 146 ? 0.1848 0.1631 0.2022 -0.0352 -0.0678 0.0457  146 THR   A CB  
2264  O  OG1 . THR   A 146 ? 0.2048 0.1835 0.2241 -0.0349 -0.0642 0.0436  146 THR   A OG1 
2265  C  CG2 . THR   A 146 ? 0.1773 0.1591 0.1873 -0.0376 -0.0662 0.0457  146 THR   A CG2 
2273  N  N   . LYS   A 147 ? 0.2081 0.1838 0.2288 -0.0282 -0.0792 0.0486  147 LYS   A N   
2274  C  CA  . LYS   A 147 ? 0.1939 0.1693 0.2146 -0.0268 -0.0838 0.0511  147 LYS   A CA  
2275  C  C   . LYS   A 147 ? 0.2009 0.1858 0.2259 -0.0217 -0.0856 0.0482  147 LYS   A C   
2276  O  O   . LYS   A 147 ? 0.2078 0.1974 0.2303 -0.0225 -0.0868 0.0488  147 LYS   A O   
2277  C  CB  . LYS   A 147 ? 0.2125 0.1761 0.2297 -0.0257 -0.0892 0.0543  147 LYS   A CB  
2278  C  CG  . LYS   A 147 ? 0.2903 0.2450 0.2909 -0.0334 -0.0888 0.0584  147 LYS   A CG  
2279  C  CD  . LYS   A 147 ? 0.2570 0.2214 0.2609 -0.0396 -0.0857 0.0611  147 LYS   A CD  
2280  C  CE  . LYS   A 147 ? 0.3314 0.2913 0.3171 -0.0476 -0.0862 0.0664  147 LYS   A CE  
2281  N  NZ  . LYS   A 147 ? 0.3172 0.2901 0.3015 -0.0520 -0.0821 0.0678  147 LYS   A NZ  
2295  N  N   . GLU   A 148 ? 0.1920 0.1831 0.2263 -0.0165 -0.0858 0.0447  148 GLU   A N   
2296  C  CA  . GLU   A 148 ? 0.1772 0.1841 0.2212 -0.0121 -0.0874 0.0416  148 GLU   A CA  
2297  C  C   . GLU   A 148 ? 0.1645 0.1796 0.2081 -0.0184 -0.0839 0.0406  148 GLU   A C   
2298  O  O   . GLU   A 148 ? 0.1673 0.1914 0.2115 -0.0185 -0.0861 0.0398  148 GLU   A O   
2299  C  CB  . GLU   A 148 ? 0.1963 0.2122 0.2478 -0.0051 -0.0876 0.0374  148 GLU   A CB  
2300  C  CG  . GLU   A 148 ? 0.1961 0.2046 0.2531 0.0040  -0.0934 0.0368  148 GLU   A CG  
2301  C  CD  . GLU   A 148 ? 0.2987 0.3057 0.3432 0.0107  -0.0998 0.0376  148 GLU   A CD  
2302  O  OE1 . GLU   A 148 ? 0.2683 0.2931 0.3237 0.0103  -0.0999 0.0366  148 GLU   A OE1 
2303  O  OE2 . GLU   A 148 ? 0.3157 0.3077 0.3592 0.0155  -0.1052 0.0391  148 GLU   A OE2 
2310  N  N   . LEU   A 149 ? 0.1684 0.1785 0.2071 -0.0238 -0.0789 0.0404  149 LEU   A N   
2311  C  CA  . LEU   A 149 ? 0.1475 0.1613 0.1881 -0.0294 -0.0766 0.0394  149 LEU   A CA  
2312  C  C   . LEU   A 149 ? 0.1879 0.1950 0.2152 -0.0315 -0.0786 0.0404  149 LEU   A C   
2313  O  O   . LEU   A 149 ? 0.1904 0.2011 0.2169 -0.0341 -0.0799 0.0390  149 LEU   A O   
2314  C  CB  . LEU   A 149 ? 0.1635 0.1718 0.1989 -0.0324 -0.0719 0.0386  149 LEU   A CB  
2315  C  CG  . LEU   A 149 ? 0.1691 0.1873 0.2125 -0.0326 -0.0695 0.0369  149 LEU   A CG  
2316  C  CD1 . LEU   A 149 ? 0.1593 0.1711 0.2004 -0.0342 -0.0653 0.0368  149 LEU   A CD1 
2317  C  CD2 . LEU   A 149 ? 0.1854 0.2146 0.2315 -0.0367 -0.0704 0.0359  149 LEU   A CD2 
2329  N  N   . GLU   A 150 ? 0.2077 0.2078 0.2293 -0.0306 -0.0790 0.0428  150 GLU   A N   
2330  C  CA  . GLU   A 150 ? 0.2267 0.2248 0.2378 -0.0320 -0.0803 0.0436  150 GLU   A CA  
2331  C  C   . GLU   A 150 ? 0.1828 0.1887 0.2023 -0.0299 -0.0851 0.0438  150 GLU   A C   
2332  O  O   . GLU   A 150 ? 0.2137 0.2200 0.2210 -0.0311 -0.0867 0.0426  150 GLU   A O   
2333  C  CB  . GLU   A 150 ? 0.2567 0.2492 0.2591 -0.0329 -0.0795 0.0467  150 GLU   A CB  
2334  C  CG  . GLU   A 150 ? 0.2152 0.2068 0.2210 -0.0349 -0.0749 0.0459  150 GLU   A CG  
2335  C  CD  . GLU   A 150 ? 0.2530 0.2426 0.2487 -0.0374 -0.0739 0.0494  150 GLU   A CD  
2336  O  OE1 . GLU   A 150 ? 0.2483 0.2361 0.2423 -0.0387 -0.0771 0.0537  150 GLU   A OE1 
2337  O  OE2 . GLU   A 150 ? 0.2961 0.2871 0.2867 -0.0389 -0.0701 0.0480  150 GLU   A OE2 
2344  N  N   . LYS   A 151 ? 0.2128 0.2218 0.2335 -0.0260 -0.0878 0.0444  151 LYS   A N   
2345  C  CA  . LYS   A 151 ? 0.2168 0.2343 0.2403 -0.0226 -0.0930 0.0441  151 LYS   A CA  
2346  C  C   . LYS   A 151 ? 0.1926 0.2222 0.2236 -0.0255 -0.0933 0.0404  151 LYS   A C   
2347  O  O   . LYS   A 151 ? 0.2150 0.2508 0.2426 -0.0250 -0.0971 0.0397  151 LYS   A O   
2348  C  CB  . LYS   A 151 ? 0.2177 0.2383 0.2479 -0.0152 -0.0965 0.0448  151 LYS   A CB  
2349  C  CG  . LYS   A 151 ? 0.2197 0.2271 0.2487 -0.0125 -0.0988 0.0487  151 LYS   A CG  
2350  C  CD  . LYS   A 151 ? 0.3017 0.3073 0.3280 -0.0035 -0.1032 0.0481  151 LYS   A CD  
2351  C  CE  . LYS   A 151 ? 0.3216 0.3107 0.3519 -0.0022 -0.1064 0.0519  151 LYS   A CE  
2352  N  NZ  . LYS   A 151 ? 0.4980 0.4807 0.5156 0.0082  -0.1115 0.0499  151 LYS   A NZ  
2366  N  N   . ILE   A 152 ? 0.1815 0.2126 0.2160 -0.0293 -0.0897 0.0385  152 ILE   A N   
2367  C  CA  . ILE   A 152 ? 0.1912 0.2330 0.2303 -0.0341 -0.0903 0.0358  152 ILE   A CA  
2368  C  C   . ILE   A 152 ? 0.2100 0.2410 0.2390 -0.0408 -0.0884 0.0351  152 ILE   A C   
2369  O  O   . ILE   A 152 ? 0.1895 0.2266 0.2248 -0.0464 -0.0887 0.0341  152 ILE   A O   
2370  C  CB  . ILE   A 152 ? 0.1971 0.2547 0.2466 -0.0319 -0.0895 0.0340  152 ILE   A CB  
2371  C  CG1 . ILE   A 152 ? 0.1771 0.2308 0.2337 -0.0320 -0.0847 0.0343  152 ILE   A CG1 
2372  C  CG2 . ILE   A 152 ? 0.2056 0.2750 0.2615 -0.0231 -0.0937 0.0331  152 ILE   A CG2 
2373  C  CD1 . ILE   A 152 ? 0.2433 0.3128 0.3033 -0.0280 -0.0838 0.0319  152 ILE   A CD1 
2385  N  N   . THR   A 153 ? 0.1982 0.2163 0.2212 -0.0402 -0.0870 0.0354  153 THR   A N   
2386  C  CA  . THR   A 153 ? 0.2072 0.2137 0.2194 -0.0442 -0.0865 0.0336  153 THR   A CA  
2387  C  C   . THR   A 153 ? 0.1981 0.1994 0.2019 -0.0423 -0.0894 0.0312  153 THR   A C   
2388  O  O   . THR   A 153 ? 0.1872 0.1929 0.1898 -0.0387 -0.0899 0.0325  153 THR   A O   
2389  C  CB  . THR   A 153 ? 0.2008 0.2008 0.2161 -0.0436 -0.0820 0.0342  153 THR   A CB  
2390  O  OG1 . THR   A 153 ? 0.2152 0.2128 0.2255 -0.0395 -0.0799 0.0353  153 THR   A OG1 
2391  C  CG2 . THR   A 153 ? 0.2331 0.2386 0.2522 -0.0458 -0.0796 0.0355  153 THR   A CG2 
2399  N  N   . GLU   A 154 ? 0.2104 0.2024 0.2055 -0.0442 -0.0915 0.0278  154 GLU   A N   
2400  C  CA  . GLU   A 154 ? 0.2273 0.2164 0.2119 -0.0411 -0.0946 0.0236  154 GLU   A CA  
2401  C  C   . GLU   A 154 ? 0.2052 0.1973 0.1872 -0.0358 -0.0909 0.0235  154 GLU   A C   
2402  O  O   . GLU   A 154 ? 0.2300 0.2181 0.2097 -0.0352 -0.0868 0.0244  154 GLU   A O   
2403  C  CB  . GLU   A 154 ? 0.2716 0.2483 0.2496 -0.0427 -0.0989 0.0189  154 GLU   A CB  
2404  C  CG  . GLU   A 154 ? 0.3568 0.3304 0.3268 -0.0469 -0.1053 0.0169  154 GLU   A CG  
2405  C  CD  . GLU   A 154 ? 0.3713 0.3319 0.3416 -0.0466 -0.1113 0.0111  154 GLU   A CD  
2406  O  OE1 . GLU   A 154 ? 0.4031 0.3596 0.3547 -0.0395 -0.1115 0.0061  154 GLU   A OE1 
2407  O  OE2 . GLU   A 154 ? 0.5328 0.4805 0.4853 -0.0532 -0.1160 0.0118  154 GLU   A OE2 
2414  N  N   . ASN   A 155 ? 0.2023 0.2017 0.1783 -0.0324 -0.0922 0.0227  155 ASN   A N   
2415  C  CA  . ASN   A 155 ? 0.2267 0.2313 0.1930 -0.0285 -0.0888 0.0230  155 ASN   A CA  
2416  C  C   . ASN   A 155 ? 0.2100 0.2118 0.1739 -0.0255 -0.0869 0.0181  155 ASN   A C   
2417  O  O   . ASN   A 155 ? 0.2226 0.2171 0.1801 -0.0248 -0.0904 0.0127  155 ASN   A O   
2418  C  CB  . ASN   A 155 ? 0.2240 0.2397 0.1891 -0.0254 -0.0913 0.0228  155 ASN   A CB  
2419  C  CG  . ASN   A 155 ? 0.2774 0.2938 0.2361 -0.0273 -0.0933 0.0280  155 ASN   A CG  
2420  O  OD1 . ASN   A 155 ? 0.2358 0.2509 0.2136 -0.0296 -0.0929 0.0319  155 ASN   A OD1 
2421  N  ND2 . ASN   A 155 ? 0.2058 0.2325 0.1700 -0.0248 -0.0962 0.0279  155 ASN   A ND2 
2428  N  N   . LYS   A 156 ? 0.2081 0.2140 0.1719 -0.0241 -0.0822 0.0199  156 LYS   A N   
2429  C  CA  . LYS   A 156 ? 0.2477 0.2537 0.2012 -0.0200 -0.0803 0.0147  156 LYS   A CA  
2430  C  C   . LYS   A 156 ? 0.2240 0.2178 0.1850 -0.0223 -0.0793 0.0148  156 LYS   A C   
2431  O  O   . LYS   A 156 ? 0.2421 0.2340 0.1975 -0.0185 -0.0784 0.0103  156 LYS   A O   
2432  C  CB  . LYS   A 156 ? 0.2543 0.2666 0.2014 -0.0141 -0.0839 0.0067  156 LYS   A CB  
2433  C  CG  . LYS   A 156 ? 0.2869 0.3162 0.2283 -0.0106 -0.0848 0.0055  156 LYS   A CG  
2434  C  CD  . LYS   A 156 ? 0.3587 0.4025 0.2900 -0.0045 -0.0860 -0.0021 156 LYS   A CD  
2435  C  CE  . LYS   A 156 ? 0.4672 0.5199 0.3934 -0.0026 -0.0822 -0.0042 156 LYS   A CE  
2436  N  NZ  . LYS   A 156 ? 0.5812 0.6291 0.4903 -0.0030 -0.0860 -0.0086 156 LYS   A NZ  
2450  N  N   . SER   A 157 ? 0.1795 0.1672 0.1536 -0.0278 -0.0795 0.0196  157 SER   A N   
2451  C  CA  . SER   A 157 ? 0.2218 0.1979 0.1915 -0.0306 -0.0780 0.0209  157 SER   A CA  
2452  C  C   . SER   A 157 ? 0.1709 0.1535 0.1549 -0.0296 -0.0726 0.0230  157 SER   A C   
2453  O  O   . SER   A 157 ? 0.2332 0.2211 0.2107 -0.0304 -0.0705 0.0266  157 SER   A O   
2454  C  CB  . SER   A 157 ? 0.1998 0.1750 0.1844 -0.0359 -0.0796 0.0247  157 SER   A CB  
2455  O  OG  . SER   A 157 ? 0.2144 0.1839 0.1936 -0.0382 -0.0848 0.0228  157 SER   A OG  
2461  N  N   . LYS   A 158 ? 0.1848 0.1601 0.1592 -0.0286 -0.0713 0.0211  158 LYS   A N   
2462  C  CA  . LYS   A 158 ? 0.1530 0.1338 0.1378 -0.0282 -0.0665 0.0226  158 LYS   A CA  
2463  C  C   . LYS   A 158 ? 0.1859 0.1604 0.1711 -0.0323 -0.0650 0.0269  158 LYS   A C   
2464  O  O   . LYS   A 158 ? 0.1664 0.1356 0.1573 -0.0348 -0.0677 0.0272  158 LYS   A O   
2465  C  CB  . LYS   A 158 ? 0.1969 0.1774 0.1685 -0.0231 -0.0657 0.0172  158 LYS   A CB  
2466  C  CG  . LYS   A 158 ? 0.2311 0.2202 0.1923 -0.0169 -0.0673 0.0118  158 LYS   A CG  
2467  C  CD  . LYS   A 158 ? 0.2304 0.2346 0.1911 -0.0173 -0.0652 0.0140  158 LYS   A CD  
2468  C  CE  . LYS   A 158 ? 0.2055 0.2247 0.1601 -0.0104 -0.0664 0.0082  158 LYS   A CE  
2469  N  NZ  . LYS   A 158 ? 0.2190 0.2334 0.1668 -0.0088 -0.0712 0.0047  158 LYS   A NZ  
2483  N  N   . VAL   A 159 ? 0.1606 0.1406 0.1579 -0.0331 -0.0614 0.0299  159 VAL   A N   
2484  C  CA  . VAL   A 159 ? 0.1764 0.1551 0.1780 -0.0349 -0.0602 0.0329  159 VAL   A CA  
2485  C  C   . VAL   A 159 ? 0.1537 0.1327 0.1593 -0.0339 -0.0569 0.0324  159 VAL   A C   
2486  O  O   . VAL   A 159 ? 0.1488 0.1303 0.1528 -0.0331 -0.0549 0.0321  159 VAL   A O   
2487  C  CB  . VAL   A 159 ? 0.1627 0.1462 0.1750 -0.0349 -0.0608 0.0365  159 VAL   A CB  
2488  C  CG1 . VAL   A 159 ? 0.1633 0.1497 0.1832 -0.0342 -0.0598 0.0374  159 VAL   A CG1 
2489  C  CG2 . VAL   A 159 ? 0.1680 0.1530 0.1789 -0.0357 -0.0644 0.0371  159 VAL   A CG2 
2499  N  N   . LEU   A 160 ? 0.1453 0.1224 0.1520 -0.0347 -0.0565 0.0324  160 LEU   A N   
2500  C  CA  . LEU   A 160 ? 0.1289 0.1080 0.1410 -0.0337 -0.0536 0.0319  160 LEU   A CA  
2501  C  C   . LEU   A 160 ? 0.1537 0.1395 0.1708 -0.0342 -0.0518 0.0333  160 LEU   A C   
2502  O  O   . LEU   A 160 ? 0.1663 0.1559 0.1870 -0.0364 -0.0532 0.0344  160 LEU   A O   
2503  C  CB  . LEU   A 160 ? 0.1568 0.1268 0.1551 -0.0345 -0.0552 0.0304  160 LEU   A CB  
2504  C  CG  . LEU   A 160 ? 0.1154 0.0888 0.1231 -0.0341 -0.0529 0.0300  160 LEU   A CG  
2505  C  CD1 . LEU   A 160 ? 0.1741 0.1351 0.1636 -0.0325 -0.0556 0.0270  160 LEU   A CD1 
2506  C  CD2 . LEU   A 160 ? 0.1363 0.1131 0.1417 -0.0375 -0.0520 0.0326  160 LEU   A CD2 
2518  N  N   . CYS   A 161 ? 0.1391 0.1294 0.1630 -0.0321 -0.0491 0.0327  161 CYS   A N   
2519  C  CA  . CYS   A 161 ? 0.1191 0.1184 0.1530 -0.0314 -0.0486 0.0323  161 CYS   A CA  
2520  C  C   . CYS   A 161 ? 0.1126 0.1164 0.1555 -0.0293 -0.0460 0.0300  161 CYS   A C   
2521  O  O   . CYS   A 161 ? 0.1548 0.1522 0.1874 -0.0286 -0.0446 0.0295  161 CYS   A O   
2522  C  CB  . CYS   A 161 ? 0.0948 0.0961 0.1374 -0.0302 -0.0522 0.0334  161 CYS   A CB  
2523  S  SG  . CYS   A 161 ? 0.1459 0.1371 0.1804 -0.0282 -0.0547 0.0347  161 CYS   A SG  
2529  N  N   . ILE   A 162 ? 0.1367 0.1507 0.1832 -0.0279 -0.0458 0.0283  162 ILE   A N   
2530  C  CA  . ILE   A 162 ? 0.1085 0.1288 0.1691 -0.0246 -0.0450 0.0251  162 ILE   A CA  
2531  C  C   . ILE   A 162 ? 0.1349 0.1532 0.1956 -0.0189 -0.0506 0.0235  162 ILE   A C   
2532  O  O   . ILE   A 162 ? 0.1380 0.1583 0.2020 -0.0179 -0.0536 0.0249  162 ILE   A O   
2533  C  CB  . ILE   A 162 ? 0.1550 0.1889 0.2110 -0.0252 -0.0414 0.0231  162 ILE   A CB  
2534  C  CG1 . ILE   A 162 ? 0.1355 0.1859 0.2032 -0.0262 -0.0421 0.0232  162 ILE   A CG1 
2535  C  CG2 . ILE   A 162 ? 0.1299 0.1600 0.1836 -0.0295 -0.0379 0.0248  162 ILE   A CG2 
2536  C  CD1 . ILE   A 162 ? 0.1313 0.2044 0.2075 -0.0239 -0.0400 0.0197  162 ILE   A CD1 
2548  N  N   . GLY   A 163 ? 0.1257 0.1400 0.1917 -0.0152 -0.0530 0.0208  163 GLY   A N   
2549  C  CA  . GLY   A 163 ? 0.1308 0.1397 0.1989 -0.0074 -0.0594 0.0183  163 GLY   A CA  
2550  C  C   . GLY   A 163 ? 0.1154 0.1400 0.1945 0.0014  -0.0591 0.0111  163 GLY   A C   
2551  O  O   . GLY   A 163 ? 0.1187 0.1611 0.2005 -0.0006 -0.0536 0.0099  163 GLY   A O   
2555  N  N   . PRO   A 164 ? 0.1289 0.1476 0.2128 0.0117  -0.0657 0.0063  164 PRO   A N   
2556  C  CA  . PRO   A 164 ? 0.1694 0.2028 0.2525 0.0230  -0.0660 -0.0027 164 PRO   A CA  
2557  C  C   . PRO   A 164 ? 0.1240 0.1685 0.2131 0.0215  -0.0589 -0.0066 164 PRO   A C   
2558  O  O   . PRO   A 164 ? 0.1074 0.1764 0.2032 0.0263  -0.0555 -0.0114 164 PRO   A O   
2559  C  CB  . PRO   A 164 ? 0.1761 0.1886 0.2591 0.0332  -0.0760 -0.0067 164 PRO   A CB  
2560  C  CG  . PRO   A 164 ? 0.1816 0.1747 0.2577 0.0274  -0.0804 0.0012  164 PRO   A CG  
2561  C  CD  . PRO   A 164 ? 0.1923 0.1852 0.2617 0.0133  -0.0740 0.0088  164 PRO   A CD  
2569  N  N   . ALA   A 165 ? 0.1199 0.1468 0.1987 0.0148  -0.0565 -0.0041 165 ALA   A N   
2570  C  CA  . ALA   A 165 ? 0.0880 0.1235 0.1705 0.0137  -0.0507 -0.0076 165 ALA   A CA  
2571  C  C   . ALA   A 165 ? 0.0909 0.1480 0.1730 0.0076  -0.0432 -0.0046 165 ALA   A C   
2572  O  O   . ALA   A 165 ? 0.1012 0.1768 0.1869 0.0106  -0.0392 -0.0090 165 ALA   A O   
2573  C  CB  . ALA   A 165 ? 0.1236 0.1382 0.1927 0.0069  -0.0502 -0.0050 165 ALA   A CB  
2579  N  N   . GLY   A 166 ? 0.0795 0.1339 0.1609 -0.0015 -0.0418 0.0030  166 GLY   A N   
2580  C  CA  . GLY   A 166 ? 0.1021 0.1709 0.1795 -0.0089 -0.0372 0.0074  166 GLY   A CA  
2581  C  C   . GLY   A 166 ? 0.0588 0.1557 0.1542 -0.0066 -0.0368 0.0058  166 GLY   A C   
2582  O  O   . GLY   A 166 ? 0.0977 0.2114 0.1867 -0.0112 -0.0323 0.0069  166 GLY   A O   
2586  N  N   . GLU   A 167 ? 0.0952 0.1936 0.1888 0.0000  -0.0420 0.0032  167 GLU   A N   
2587  C  CA  . GLU   A 167 ? 0.0874 0.2147 0.1943 0.0040  -0.0423 0.0001  167 GLU   A CA  
2588  C  C   . GLU   A 167 ? 0.1137 0.2555 0.2164 0.0117  -0.0380 -0.0068 167 GLU   A C   
2589  O  O   . GLU   A 167 ? 0.0699 0.2344 0.1809 0.0096  -0.0332 -0.0071 167 GLU   A O   
2590  C  CB  . GLU   A 167 ? 0.0862 0.2092 0.1957 0.0121  -0.0487 -0.0010 167 GLU   A CB  
2591  C  CG  . GLU   A 167 ? 0.1242 0.2282 0.2249 0.0054  -0.0517 0.0048  167 GLU   A CG  
2592  C  CD  . GLU   A 167 ? 0.1332 0.2282 0.2325 0.0140  -0.0584 0.0037  167 GLU   A CD  
2593  O  OE1 . GLU   A 167 ? 0.1257 0.2227 0.2303 0.0261  -0.0617 -0.0028 167 GLU   A OE1 
2594  O  OE2 . GLU   A 167 ? 0.0981 0.1840 0.1972 0.0088  -0.0603 0.0086  167 GLU   A OE2 
2601  N  N   . ARG   A 168 ? 0.0931 0.2249 0.2011 0.0203  -0.0400 -0.0134 168 ARG   A N   
2602  C  CA  . ARG   A 168 ? 0.1332 0.2753 0.2320 0.0295  -0.0371 -0.0221 168 ARG   A CA  
2603  C  C   . ARG   A 168 ? 0.0666 0.2148 0.1724 0.0217  -0.0298 -0.0194 168 ARG   A C   
2604  O  O   . ARG   A 168 ? 0.1006 0.2595 0.1985 0.0289  -0.0278 -0.0269 168 ARG   A O   
2605  C  CB  . ARG   A 168 ? 0.1207 0.2455 0.2264 0.0432  -0.0445 -0.0311 168 ARG   A CB  
2606  C  CG  . ARG   A 168 ? 0.1616 0.2807 0.2639 0.0527  -0.0514 -0.0345 168 ARG   A CG  
2607  C  CD  . ARG   A 168 ? 0.1754 0.2624 0.2761 0.0608  -0.0615 -0.0383 168 ARG   A CD  
2608  N  NE  . ARG   A 168 ? 0.2372 0.3190 0.3346 0.0695  -0.0679 -0.0409 168 ARG   A NE  
2609  C  CZ  . ARG   A 168 ? 0.2988 0.3884 0.3925 0.0829  -0.0709 -0.0508 168 ARG   A CZ  
2610  N  NH1 . ARG   A 168 ? 0.2909 0.3893 0.3859 0.0898  -0.0692 -0.0601 168 ARG   A NH1 
2611  N  NH2 . ARG   A 168 ? 0.3133 0.4042 0.4092 0.0895  -0.0757 -0.0518 168 ARG   A NH2 
2625  N  N   . LEU   A 169 ? 0.0951 0.2370 0.1894 0.0092  -0.0280 -0.0112 169 LEU   A N   
2626  C  CA  . LEU   A 169 ? 0.0602 0.2072 0.1555 0.0020  -0.0220 -0.0081 169 LEU   A CA  
2627  C  C   . LEU   A 169 ? 0.0984 0.2319 0.1841 0.0074  -0.0224 -0.0137 169 LEU   A C   
2628  O  O   . LEU   A 169 ? 0.0726 0.2179 0.1591 0.0064  -0.0180 -0.0150 169 LEU   A O   
2629  C  CB  . LEU   A 169 ? 0.0713 0.2421 0.1627 0.0006  -0.0166 -0.0081 169 LEU   A CB  
2630  C  CG  . LEU   A 169 ? 0.1001 0.2837 0.1925 -0.0050 -0.0160 -0.0036 169 LEU   A CG  
2631  C  CD1 . LEU   A 169 ? 0.1516 0.3595 0.2378 -0.0097 -0.0108 -0.0022 169 LEU   A CD1 
2632  C  CD2 . LEU   A 169 ? 0.0888 0.2551 0.1781 -0.0164 -0.0182 0.0052  169 LEU   A CD2 
2644  N  N   . SER   A 170 ? 0.1184 0.2267 0.2020 0.0118  -0.0275 -0.0164 170 SER   A N   
2645  C  CA  . SER   A 170 ? 0.0989 0.1902 0.1784 0.0139  -0.0283 -0.0204 170 SER   A CA  
2646  C  C   . SER   A 170 ? 0.0834 0.1692 0.1561 0.0042  -0.0237 -0.0140 170 SER   A C   
2647  O  O   . SER   A 170 ? 0.0667 0.1441 0.1359 -0.0033 -0.0235 -0.0063 170 SER   A O   
2648  C  CB  . SER   A 170 ? 0.0968 0.1621 0.1741 0.0167  -0.0353 -0.0220 170 SER   A CB  
2649  O  OG  . SER   A 170 ? 0.1048 0.1538 0.1749 0.0133  -0.0356 -0.0228 170 SER   A OG  
2655  N  N   . LEU   A 171 ? 0.1005 0.1893 0.1667 0.0055  -0.0208 -0.0176 171 LEU   A N   
2656  C  CA  . LEU   A 171 ? 0.0776 0.1636 0.1414 -0.0017 -0.0171 -0.0124 171 LEU   A CA  
2657  C  C   . LEU   A 171 ? 0.1175 0.1803 0.1687 -0.0050 -0.0196 -0.0102 171 LEU   A C   
2658  O  O   . LEU   A 171 ? 0.1161 0.1765 0.1645 -0.0088 -0.0176 -0.0070 171 LEU   A O   
2659  C  CB  . LEU   A 171 ? 0.0855 0.1851 0.1445 0.0013  -0.0134 -0.0167 171 LEU   A CB  
2660  C  CG  . LEU   A 171 ? 0.0986 0.2255 0.1615 0.0028  -0.0101 -0.0175 171 LEU   A CG  
2661  C  CD1 . LEU   A 171 ? 0.1033 0.2434 0.1614 0.0043  -0.0063 -0.0205 171 LEU   A CD1 
2662  C  CD2 . LEU   A 171 ? 0.1240 0.2563 0.1845 -0.0064 -0.0087 -0.0076 171 LEU   A CD2 
2674  N  N   . MET   A 172 ? 0.0832 0.1337 0.1417 -0.0035 -0.0244 -0.0118 172 MET   A N   
2675  C  CA  . MET   A 172 ? 0.0917 0.1255 0.1432 -0.0088 -0.0264 -0.0086 172 MET   A CA  
2676  C  C   . MET   A 172 ? 0.0972 0.1237 0.1489 -0.0120 -0.0290 -0.0026 172 MET   A C   
2677  O  O   . MET   A 172 ? 0.1106 0.1253 0.1581 -0.0158 -0.0316 0.0000  172 MET   A O   
2678  C  CB  . MET   A 172 ? 0.0935 0.1157 0.1445 -0.0081 -0.0307 -0.0134 172 MET   A CB  
2679  C  CG  . MET   A 172 ? 0.1105 0.1233 0.1653 -0.0030 -0.0371 -0.0170 172 MET   A CG  
2680  S  SD  . MET   A 172 ? 0.1591 0.1511 0.2062 -0.0057 -0.0443 -0.0211 172 MET   A SD  
2681  C  CE  . MET   A 172 ? 0.1729 0.1752 0.2215 0.0009  -0.0424 -0.0308 172 MET   A CE  
2691  N  N   . ALA   A 173 ? 0.0873 0.1226 0.1434 -0.0110 -0.0283 0.0000  173 ALA   A N   
2692  C  CA  . ALA   A 173 ? 0.0853 0.1160 0.1451 -0.0139 -0.0311 0.0048  173 ALA   A CA  
2693  C  C   . ALA   A 173 ? 0.1010 0.1248 0.1514 -0.0198 -0.0303 0.0102  173 ALA   A C   
2694  O  O   . ALA   A 173 ? 0.1149 0.1421 0.1589 -0.0213 -0.0271 0.0111  173 ALA   A O   
2695  C  CB  . ALA   A 173 ? 0.1389 0.1823 0.1994 -0.0122 -0.0309 0.0051  173 ALA   A CB  
2701  N  N   . ALA   A 174 ? 0.1347 0.1483 0.1792 -0.0221 -0.0334 0.0134  174 ALA   A N   
2702  C  CA  . ALA   A 174 ? 0.1361 0.1450 0.1737 -0.0254 -0.0329 0.0165  174 ALA   A CA  
2703  C  C   . ALA   A 174 ? 0.1397 0.1460 0.1746 -0.0261 -0.0343 0.0200  174 ALA   A C   
2704  O  O   . ALA   A 174 ? 0.1402 0.1495 0.1820 -0.0256 -0.0361 0.0207  174 ALA   A O   
2705  C  CB  . ALA   A 174 ? 0.1292 0.1327 0.1626 -0.0267 -0.0336 0.0168  174 ALA   A CB  
2711  N  N   . VAL   A 175 ? 0.1282 0.1297 0.1549 -0.0273 -0.0349 0.0217  175 VAL   A N   
2712  C  CA  . VAL   A 175 ? 0.1031 0.1018 0.1331 -0.0285 -0.0374 0.0243  175 VAL   A CA  
2713  C  C   . VAL   A 175 ? 0.1686 0.1609 0.1821 -0.0283 -0.0392 0.0249  175 VAL   A C   
2714  O  O   . VAL   A 175 ? 0.1357 0.1305 0.1515 -0.0283 -0.0388 0.0232  175 VAL   A O   
2715  C  CB  . VAL   A 175 ? 0.1507 0.1427 0.1650 -0.0302 -0.0393 0.0255  175 VAL   A CB  
2716  C  CG1 . VAL   A 175 ? 0.1343 0.1204 0.1473 -0.0316 -0.0431 0.0273  175 VAL   A CG1 
2717  C  CG2 . VAL   A 175 ? 0.1586 0.1563 0.1781 -0.0327 -0.0376 0.0267  175 VAL   A CG2 
2727  N  N   . MET   A 176 ? 0.1408 0.1333 0.1635 -0.0284 -0.0411 0.0273  176 MET   A N   
2728  C  CA  . MET   A 176 ? 0.1384 0.1282 0.1544 -0.0300 -0.0431 0.0291  176 MET   A CA  
2729  C  C   . MET   A 176 ? 0.1140 0.1027 0.1295 -0.0307 -0.0454 0.0298  176 MET   A C   
2730  O  O   . MET   A 176 ? 0.1414 0.1271 0.1536 -0.0305 -0.0466 0.0300  176 MET   A O   
2731  C  CB  . MET   A 176 ? 0.1257 0.1139 0.1502 -0.0303 -0.0458 0.0315  176 MET   A CB  
2732  C  CG  . MET   A 176 ? 0.1583 0.1452 0.1840 -0.0291 -0.0454 0.0296  176 MET   A CG  
2733  S  SD  . MET   A 176 ? 0.1513 0.1406 0.1747 -0.0312 -0.0425 0.0277  176 MET   A SD  
2734  C  CE  . MET   A 176 ? 0.1555 0.1440 0.1702 -0.0364 -0.0443 0.0325  176 MET   A CE  
2744  N  N   . ASN   A 177 ? 0.1317 0.1216 0.1367 -0.0315 -0.0458 0.0296  177 ASN   A N   
2745  C  CA  . ASN   A 177 ? 0.1345 0.1236 0.1343 -0.0311 -0.0482 0.0284  177 ASN   A CA  
2746  C  C   . ASN   A 177 ? 0.1335 0.1293 0.1285 -0.0327 -0.0483 0.0301  177 ASN   A C   
2747  O  O   . ASN   A 177 ? 0.1368 0.1399 0.1309 -0.0343 -0.0461 0.0302  177 ASN   A O   
2748  C  CB  . ASN   A 177 ? 0.1343 0.1206 0.1273 -0.0271 -0.0492 0.0236  177 ASN   A CB  
2749  C  CG  . ASN   A 177 ? 0.1281 0.1222 0.1186 -0.0234 -0.0475 0.0195  177 ASN   A CG  
2750  O  OD1 . ASN   A 177 ? 0.1556 0.1490 0.1442 -0.0230 -0.0460 0.0190  177 ASN   A OD1 
2751  N  ND2 . ASN   A 177 ? 0.1480 0.1499 0.1284 -0.0197 -0.0478 0.0164  177 ASN   A ND2 
2758  N  N   . ASP   A 178 ? 0.1105 0.1065 0.1069 -0.0333 -0.0505 0.0314  178 ASP   A N   
2759  C  CA  . ASP   A 178 ? 0.1410 0.1442 0.1275 -0.0356 -0.0507 0.0336  178 ASP   A CA  
2760  C  C   . ASP   A 178 ? 0.1365 0.1391 0.1298 -0.0420 -0.0509 0.0401  178 ASP   A C   
2761  O  O   . ASP   A 178 ? 0.1508 0.1620 0.1370 -0.0464 -0.0496 0.0426  178 ASP   A O   
2762  C  CB  . ASP   A 178 ? 0.1339 0.1496 0.1155 -0.0313 -0.0491 0.0281  178 ASP   A CB  
2763  C  CG  . ASP   A 178 ? 0.1444 0.1569 0.1225 -0.0241 -0.0517 0.0215  178 ASP   A CG  
2764  O  OD1 . ASP   A 178 ? 0.1957 0.2037 0.1680 -0.0237 -0.0543 0.0215  178 ASP   A OD1 
2765  O  OD2 . ASP   A 178 ? 0.1482 0.1598 0.1215 -0.0192 -0.0513 0.0165  178 ASP   A OD2 
2770  N  N   . VAL   A 179 ? 0.1529 0.1446 0.1506 -0.0426 -0.0531 0.0427  179 VAL   A N   
2771  C  CA  . VAL   A 179 ? 0.1493 0.1350 0.1515 -0.0474 -0.0564 0.0480  179 VAL   A CA  
2772  C  C   . VAL   A 179 ? 0.1509 0.1385 0.1494 -0.0485 -0.0545 0.0480  179 VAL   A C   
2773  O  O   . VAL   A 179 ? 0.1647 0.1464 0.1667 -0.0456 -0.0575 0.0470  179 VAL   A O   
2774  C  CB  . VAL   A 179 ? 0.1771 0.1635 0.1741 -0.0536 -0.0601 0.0526  179 VAL   A CB  
2775  C  CG1 . VAL   A 179 ? 0.2096 0.1884 0.2058 -0.0560 -0.0661 0.0548  179 VAL   A CG1 
2776  C  CG2 . VAL   A 179 ? 0.1750 0.1611 0.1716 -0.0501 -0.0615 0.0522  179 VAL   A CG2 
2786  N  N   . ASP   A 180 ? 0.1332 0.1332 0.1290 -0.0513 -0.0504 0.0469  180 ASP   A N   
2787  C  CA  . ASP   A 180 ? 0.1552 0.1592 0.1456 -0.0545 -0.0481 0.0467  180 ASP   A CA  
2788  C  C   . ASP   A 180 ? 0.1413 0.1586 0.1344 -0.0506 -0.0426 0.0396  180 ASP   A C   
2789  O  O   . ASP   A 180 ? 0.1558 0.1808 0.1462 -0.0538 -0.0400 0.0389  180 ASP   A O   
2790  C  CB  . ASP   A 180 ? 0.1727 0.1825 0.1560 -0.0641 -0.0501 0.0537  180 ASP   A CB  
2791  C  CG  . ASP   A 180 ? 0.1899 0.2140 0.1698 -0.0676 -0.0478 0.0545  180 ASP   A CG  
2792  O  OD1 . ASP   A 180 ? 0.1574 0.1976 0.1385 -0.0620 -0.0430 0.0477  180 ASP   A OD1 
2793  O  OD2 . ASP   A 180 ? 0.2305 0.2507 0.2077 -0.0729 -0.0517 0.0595  180 ASP   A OD2 
2798  N  N   . ARG   A 181 ? 0.1293 0.1477 0.1234 -0.0433 -0.0417 0.0340  181 ARG   A N   
2799  C  CA  . ARG   A 181 ? 0.1378 0.1635 0.1282 -0.0372 -0.0390 0.0271  181 ARG   A CA  
2800  C  C   . ARG   A 181 ? 0.1371 0.1518 0.1334 -0.0341 -0.0394 0.0254  181 ARG   A C   
2801  O  O   . ARG   A 181 ? 0.1438 0.1485 0.1455 -0.0345 -0.0411 0.0279  181 ARG   A O   
2802  C  CB  . ARG   A 181 ? 0.1162 0.1493 0.1024 -0.0306 -0.0396 0.0221  181 ARG   A CB  
2803  C  CG  . ARG   A 181 ? 0.1146 0.1610 0.0962 -0.0332 -0.0389 0.0237  181 ARG   A CG  
2804  C  CD  . ARG   A 181 ? 0.1433 0.2056 0.1193 -0.0395 -0.0350 0.0255  181 ARG   A CD  
2805  N  NE  . ARG   A 181 ? 0.1045 0.1810 0.0846 -0.0327 -0.0319 0.0187  181 ARG   A NE  
2806  C  CZ  . ARG   A 181 ? 0.1112 0.2081 0.0892 -0.0362 -0.0279 0.0181  181 ARG   A CZ  
2807  N  NH1 . ARG   A 181 ? 0.1286 0.2353 0.1044 -0.0479 -0.0264 0.0252  181 ARG   A NH1 
2808  N  NH2 . ARG   A 181 ? 0.1198 0.2269 0.0961 -0.0281 -0.0255 0.0112  181 ARG   A NH2 
2822  N  N   . THR   A 182 ? 0.1033 0.1231 0.1037 -0.0309 -0.0375 0.0211  182 THR   A N   
2823  C  CA  . THR   A 182 ? 0.1267 0.1371 0.1273 -0.0294 -0.0373 0.0204  182 THR   A CA  
2824  C  C   . THR   A 182 ? 0.1091 0.1219 0.1093 -0.0245 -0.0374 0.0163  182 THR   A C   
2825  O  O   . THR   A 182 ? 0.0944 0.1177 0.0907 -0.0222 -0.0358 0.0131  182 THR   A O   
2826  C  CB  . THR   A 182 ? 0.1209 0.1297 0.1308 -0.0326 -0.0356 0.0218  182 THR   A CB  
2827  O  OG1 . THR   A 182 ? 0.1155 0.1209 0.1302 -0.0299 -0.0346 0.0202  182 THR   A OG1 
2828  C  CG2 . THR   A 182 ? 0.1283 0.1459 0.1357 -0.0354 -0.0335 0.0208  182 THR   A CG2 
2836  N  N   . ALA   A 183 ? 0.1180 0.1211 0.1176 -0.0233 -0.0390 0.0166  183 ALA   A N   
2837  C  CA  . ALA   A 183 ? 0.1180 0.1191 0.1172 -0.0195 -0.0384 0.0146  183 ALA   A CA  
2838  C  C   . ALA   A 183 ? 0.1374 0.1411 0.1402 -0.0227 -0.0346 0.0155  183 ALA   A C   
2839  O  O   . ALA   A 183 ? 0.1141 0.1161 0.1273 -0.0251 -0.0349 0.0177  183 ALA   A O   
2840  C  CB  . ALA   A 183 ? 0.1419 0.1297 0.1320 -0.0190 -0.0425 0.0157  183 ALA   A CB  
2846  N  N   . ALA   A 184 ? 0.1074 0.1204 0.1171 -0.0225 -0.0320 0.0132  184 ALA   A N   
2847  C  CA  . ALA   A 184 ? 0.1064 0.1209 0.1227 -0.0251 -0.0297 0.0127  184 ALA   A CA  
2848  C  C   . ALA   A 184 ? 0.1050 0.1234 0.1264 -0.0231 -0.0271 0.0102  184 ALA   A C   
2849  O  O   . ALA   A 184 ? 0.1087 0.1264 0.1345 -0.0235 -0.0266 0.0098  184 ALA   A O   
2850  C  CB  . ALA   A 184 ? 0.1055 0.1255 0.1220 -0.0286 -0.0294 0.0121  184 ALA   A CB  
2856  N  N   . ARG   A 185 ? 0.1459 0.1672 0.1562 -0.0198 -0.0258 0.0080  185 ARG   A N   
2857  C  CA  . ARG   A 185 ? 0.1155 0.1434 0.1329 -0.0180 -0.0231 0.0050  185 ARG   A CA  
2858  C  C   . ARG   A 185 ? 0.1312 0.1563 0.1431 -0.0169 -0.0226 0.0073  185 ARG   A C   
2859  O  O   . ARG   A 185 ? 0.1175 0.1357 0.1275 -0.0180 -0.0252 0.0109  185 ARG   A O   
2860  C  CB  . ARG   A 185 ? 0.1207 0.1567 0.1327 -0.0156 -0.0221 0.0014  185 ARG   A CB  
2861  C  CG  . ARG   A 185 ? 0.1475 0.1889 0.1546 -0.0190 -0.0227 0.0002  185 ARG   A CG  
2862  C  CD  . ARG   A 185 ? 0.0943 0.1496 0.1082 -0.0199 -0.0212 -0.0036 185 ARG   A CD  
2863  N  NE  . ARG   A 185 ? 0.0986 0.1522 0.1150 -0.0231 -0.0206 -0.0056 185 ARG   A NE  
2864  C  CZ  . ARG   A 185 ? 0.1029 0.1644 0.1178 -0.0227 -0.0194 -0.0099 185 ARG   A CZ  
2865  N  NH1 . ARG   A 185 ? 0.0896 0.1640 0.1027 -0.0193 -0.0182 -0.0124 185 ARG   A NH1 
2866  N  NH2 . ARG   A 185 ? 0.0786 0.1370 0.1008 -0.0245 -0.0198 -0.0124 185 ARG   A NH2 
2880  N  N   . GLY   A 186 ? 0.1210 0.1539 0.1387 -0.0160 -0.0200 0.0052  186 GLY   A N   
2881  C  CA  . GLY   A 186 ? 0.1323 0.1675 0.1453 -0.0166 -0.0189 0.0079  186 GLY   A CA  
2882  C  C   . GLY   A 186 ? 0.1005 0.1428 0.1262 -0.0192 -0.0181 0.0096  186 GLY   A C   
2883  O  O   . GLY   A 186 ? 0.1077 0.1567 0.1292 -0.0214 -0.0167 0.0122  186 GLY   A O   
2887  N  N   . GLY   A 187 ? 0.1225 0.1621 0.1508 -0.0193 -0.0192 0.0084  187 GLY   A N   
2888  C  CA  . GLY   A 187 ? 0.1028 0.1507 0.1419 -0.0204 -0.0193 0.0094  187 GLY   A CA  
2889  C  C   . GLY   A 187 ? 0.1069 0.1515 0.1421 -0.0259 -0.0217 0.0164  187 GLY   A C   
2890  O  O   . GLY   A 187 ? 0.1195 0.1757 0.1598 -0.0285 -0.0209 0.0175  187 GLY   A O   
2894  N  N   . VAL   A 188 ? 0.1246 0.1521 0.1216 -0.0325 -0.0397 0.0413  188 VAL   A N   
2895  C  CA  . VAL   A 188 ? 0.1415 0.1634 0.1393 -0.0309 -0.0408 0.0446  188 VAL   A CA  
2896  C  C   . VAL   A 188 ? 0.1362 0.1547 0.1403 -0.0293 -0.0427 0.0423  188 VAL   A C   
2897  O  O   . VAL   A 188 ? 0.1229 0.1409 0.1326 -0.0294 -0.0433 0.0441  188 VAL   A O   
2898  C  CB  . VAL   A 188 ? 0.1130 0.1302 0.1220 -0.0281 -0.0406 0.0448  188 VAL   A CB  
2899  C  CG1 . VAL   A 188 ? 0.1759 0.1956 0.1755 -0.0295 -0.0397 0.0480  188 VAL   A CG1 
2900  C  CG2 . VAL   A 188 ? 0.1640 0.1735 0.1613 -0.0256 -0.0403 0.0407  188 VAL   A CG2 
2910  N  N   . GLY   A 189 ? 0.1422 0.1573 0.1456 -0.0279 -0.0423 0.0374  189 GLY   A N   
2911  C  CA  . GLY   A 189 ? 0.1398 0.1512 0.1508 -0.0260 -0.0429 0.0343  189 GLY   A CA  
2912  C  C   . GLY   A 189 ? 0.1670 0.1835 0.1779 -0.0273 -0.0399 0.0319  189 GLY   A C   
2913  O  O   . GLY   A 189 ? 0.1207 0.1368 0.1449 -0.0261 -0.0409 0.0312  189 GLY   A O   
2917  N  N   . ALA   A 190 ? 0.1514 0.1773 0.1627 -0.0301 -0.0362 0.0302  190 ALA   A N   
2918  C  CA  . ALA   A 190 ? 0.1057 0.1413 0.1261 -0.0320 -0.0321 0.0271  190 ALA   A CA  
2919  C  C   . ALA   A 190 ? 0.1081 0.1465 0.1279 -0.0335 -0.0326 0.0326  190 ALA   A C   
2920  O  O   . ALA   A 190 ? 0.1117 0.1547 0.1382 -0.0344 -0.0302 0.0308  190 ALA   A O   
2921  C  CB  . ALA   A 190 ? 0.1301 0.1738 0.1414 -0.0356 -0.0280 0.0231  190 ALA   A CB  
2927  N  N   . VAL   A 191 ? 0.1060 0.1422 0.1225 -0.0345 -0.0353 0.0394  191 VAL   A N   
2928  C  CA  . VAL   A 191 ? 0.1110 0.1489 0.1313 -0.0360 -0.0364 0.0455  191 VAL   A CA  
2929  C  C   . VAL   A 191 ? 0.1145 0.1453 0.1427 -0.0333 -0.0390 0.0444  191 VAL   A C   
2930  O  O   . VAL   A 191 ? 0.1294 0.1637 0.1626 -0.0344 -0.0380 0.0451  191 VAL   A O   
2931  C  CB  . VAL   A 191 ? 0.1262 0.1627 0.1433 -0.0371 -0.0396 0.0528  191 VAL   A CB  
2932  C  CG1 . VAL   A 191 ? 0.1521 0.1880 0.1733 -0.0385 -0.0413 0.0590  191 VAL   A CG1 
2933  C  CG2 . VAL   A 191 ? 0.1256 0.1700 0.1351 -0.0402 -0.0380 0.0549  191 VAL   A CG2 
2943  N  N   . MET   A 192 ? 0.1197 0.1411 0.1474 -0.0297 -0.0422 0.0427  192 MET   A N   
2944  C  CA  . MET   A 192 ? 0.1429 0.1579 0.1764 -0.0276 -0.0454 0.0415  192 MET   A CA  
2945  C  C   . MET   A 192 ? 0.1565 0.1753 0.1952 -0.0273 -0.0431 0.0376  192 MET   A C   
2946  O  O   . MET   A 192 ? 0.1419 0.1622 0.1900 -0.0276 -0.0443 0.0384  192 MET   A O   
2947  C  CB  . MET   A 192 ? 0.1745 0.1806 0.2038 -0.0250 -0.0487 0.0401  192 MET   A CB  
2948  C  CG  . MET   A 192 ? 0.2176 0.2159 0.2432 -0.0238 -0.0520 0.0403  192 MET   A CG  
2949  S  SD  . MET   A 192 ? 0.1620 0.1541 0.1879 -0.0225 -0.0512 0.0370  192 MET   A SD  
2950  C  CE  . MET   A 192 ? 0.1637 0.1507 0.1892 -0.0213 -0.0543 0.0353  192 MET   A CE  
2960  N  N   . GLY   A 193 ? 0.1538 0.1753 0.1928 -0.0267 -0.0404 0.0328  193 GLY   A N   
2961  C  CA  . GLY   A 193 ? 0.1311 0.1574 0.1803 -0.0259 -0.0378 0.0280  193 GLY   A CA  
2962  C  C   . GLY   A 193 ? 0.1199 0.1572 0.1765 -0.0289 -0.0336 0.0280  193 GLY   A C   
2963  O  O   . GLY   A 193 ? 0.1557 0.1947 0.2181 -0.0279 -0.0330 0.0260  193 GLY   A O   
2967  N  N   . SER   A 194 ? 0.1331 0.1761 0.1784 -0.0323 -0.0309 0.0306  194 SER   A N   
2968  C  CA  . SER   A 194 ? 0.1102 0.1660 0.1631 -0.0364 -0.0268 0.0322  194 SER   A CA  
2969  C  C   . SER   A 194 ? 0.1420 0.1950 0.1970 -0.0367 -0.0297 0.0371  194 SER   A C   
2970  O  O   . SER   A 194 ? 0.1391 0.2018 0.2018 -0.0397 -0.0264 0.0378  194 SER   A O   
2971  C  CB  . SER   A 194 ? 0.1308 0.1928 0.1698 -0.0410 -0.0248 0.0360  194 SER   A CB  
2972  O  OG  . SER   A 194 ? 0.1387 0.1953 0.1745 -0.0413 -0.0293 0.0440  194 SER   A OG  
2978  N  N   . LYS   A 195 ? 0.1340 0.1765 0.1921 -0.0342 -0.0355 0.0404  195 LYS   A N   
2979  C  CA  . LYS   A 195 ? 0.1493 0.1884 0.2111 -0.0351 -0.0389 0.0446  195 LYS   A CA  
2980  C  C   . LYS   A 195 ? 0.1513 0.1870 0.2234 -0.0321 -0.0414 0.0412  195 LYS   A C   
2981  O  O   . LYS   A 195 ? 0.1433 0.1766 0.2223 -0.0326 -0.0449 0.0437  195 LYS   A O   
2982  C  CB  . LYS   A 195 ? 0.1285 0.1593 0.1869 -0.0348 -0.0434 0.0495  195 LYS   A CB  
2983  C  CG  . LYS   A 195 ? 0.1123 0.1468 0.1672 -0.0377 -0.0423 0.0548  195 LYS   A CG  
2984  C  CD  . LYS   A 195 ? 0.1495 0.1759 0.2010 -0.0380 -0.0464 0.0602  195 LYS   A CD  
2985  C  CE  . LYS   A 195 ? 0.1655 0.1968 0.2149 -0.0413 -0.0457 0.0671  195 LYS   A CE  
2986  N  NZ  . LYS   A 195 ? 0.1575 0.2012 0.2108 -0.0461 -0.0420 0.0706  195 LYS   A NZ  
3000  N  N   . ASN   A 196 ? 0.1473 0.1827 0.2220 -0.0294 -0.0404 0.0359  196 ASN   A N   
3001  C  CA  . ASN   A 196 ? 0.1373 0.1695 0.2236 -0.0264 -0.0440 0.0338  196 ASN   A CA  
3002  C  C   . ASN   A 196 ? 0.1710 0.1913 0.2470 -0.0250 -0.0507 0.0364  196 ASN   A C   
3003  O  O   . ASN   A 196 ? 0.1508 0.1701 0.2383 -0.0244 -0.0551 0.0372  196 ASN   A O   
3004  C  CB  . ASN   A 196 ? 0.1362 0.1764 0.2366 -0.0275 -0.0426 0.0335  196 ASN   A CB  
3005  C  CG  . ASN   A 196 ? 0.1957 0.2422 0.2989 -0.0261 -0.0377 0.0276  196 ASN   A CG  
3006  O  OD1 . ASN   A 196 ? 0.1748 0.2194 0.2842 -0.0232 -0.0373 0.0236  196 ASN   A OD1 
3007  N  ND2 . ASN   A 196 ? 0.1743 0.2328 0.2924 -0.0282 -0.0336 0.0268  196 ASN   A ND2 
3014  N  N   . LEU   A 197 ? 0.1503 0.1660 0.2192 -0.0253 -0.0515 0.0379  197 LEU   A N   
3015  C  CA  . LEU   A 197 ? 0.1412 0.1484 0.2057 -0.0244 -0.0571 0.0394  197 LEU   A CA  
3016  C  C   . LEU   A 197 ? 0.1524 0.1537 0.2071 -0.0221 -0.0581 0.0373  197 LEU   A C   
3017  O  O   . LEU   A 197 ? 0.1426 0.1449 0.1937 -0.0219 -0.0556 0.0366  197 LEU   A O   
3018  C  CB  . LEU   A 197 ? 0.1716 0.1745 0.2235 -0.0260 -0.0572 0.0419  197 LEU   A CB  
3019  C  CG  . LEU   A 197 ? 0.1263 0.1215 0.1806 -0.0250 -0.0589 0.0409  197 LEU   A CG  
3020  C  CD1 . LEU   A 197 ? 0.1428 0.1342 0.1955 -0.0254 -0.0619 0.0403  197 LEU   A CD1 
3021  C  CD2 . LEU   A 197 ? 0.1740 0.1654 0.2172 -0.0260 -0.0585 0.0427  197 LEU   A CD2 
3033  N  N   . LYS   A 198 ? 0.1315 0.1288 0.1912 -0.0207 -0.0602 0.0364  198 LYS   A N   
3034  C  CA  . LYS   A 198 ? 0.1457 0.1377 0.1990 -0.0191 -0.0609 0.0354  198 LYS   A CA  
3035  C  C   . LYS   A 198 ? 0.1403 0.1264 0.1832 -0.0200 -0.0606 0.0349  198 LYS   A C   
3036  O  O   . LYS   A 198 ? 0.1464 0.1306 0.1822 -0.0195 -0.0595 0.0342  198 LYS   A O   
3037  C  CB  . LYS   A 198 ? 0.1514 0.1423 0.2121 -0.0182 -0.0638 0.0356  198 LYS   A CB  
3038  C  CG  . LYS   A 198 ? 0.1281 0.1149 0.1895 -0.0177 -0.0652 0.0358  198 LYS   A CG  
3039  C  CD  . LYS   A 198 ? 0.1402 0.1270 0.2006 -0.0162 -0.0644 0.0346  198 LYS   A CD  
3040  C  CE  . LYS   A 198 ? 0.1245 0.1078 0.1902 -0.0160 -0.0664 0.0357  198 LYS   A CE  
3041  N  NZ  . LYS   A 198 ? 0.1592 0.1411 0.2213 -0.0150 -0.0659 0.0345  198 LYS   A NZ  
3055  N  N   . ALA   A 199 ? 0.1509 0.1345 0.1881 -0.0211 -0.0617 0.0350  199 ALA   A N   
3056  C  CA  . ALA   A 199 ? 0.1358 0.1164 0.1698 -0.0218 -0.0619 0.0340  199 ALA   A CA  
3057  C  C   . ALA   A 199 ? 0.1599 0.1373 0.1858 -0.0232 -0.0634 0.0334  199 ALA   A C   
3058  O  O   . ALA   A 199 ? 0.1515 0.1305 0.1865 -0.0237 -0.0649 0.0345  199 ALA   A O   
3059  C  CB  . ALA   A 199 ? 0.1884 0.1658 0.2135 -0.0222 -0.0638 0.0341  199 ALA   A CB  
3065  N  N   . ILE   A 200 ? 0.1469 0.1223 0.1690 -0.0234 -0.0633 0.0319  200 ILE   A N   
3066  C  CA  . ILE   A 200 ? 0.1553 0.1283 0.1758 -0.0245 -0.0658 0.0306  200 ILE   A CA  
3067  C  C   . ILE   A 200 ? 0.1920 0.1630 0.2008 -0.0250 -0.0675 0.0283  200 ILE   A C   
3068  O  O   . ILE   A 200 ? 0.1778 0.1500 0.1841 -0.0247 -0.0653 0.0276  200 ILE   A O   
3069  C  CB  . ILE   A 200 ? 0.1406 0.1133 0.1649 -0.0241 -0.0653 0.0307  200 ILE   A CB  
3070  C  CG1 . ILE   A 200 ? 0.1731 0.1485 0.2006 -0.0241 -0.0629 0.0341  200 ILE   A CG1 
3071  C  CG2 . ILE   A 200 ? 0.1363 0.1056 0.1610 -0.0252 -0.0690 0.0291  200 ILE   A CG2 
3072  C  CD1 . ILE   A 200 ? 0.1858 0.1614 0.2167 -0.0244 -0.0625 0.0359  200 ILE   A CD1 
3084  N  N   . THR   A 201 ? 0.1877 0.1592 0.1973 -0.0265 -0.0707 0.0273  201 THR   A N   
3085  C  CA  . THR   A 201 ? 0.1708 0.1442 0.1768 -0.0282 -0.0722 0.0248  201 THR   A CA  
3086  C  C   . THR   A 201 ? 0.2030 0.1733 0.1989 -0.0295 -0.0740 0.0198  201 THR   A C   
3087  O  O   . THR   A 201 ? 0.1759 0.1456 0.1848 -0.0295 -0.0757 0.0192  201 THR   A O   
3088  C  CB  . THR   A 201 ? 0.2061 0.1801 0.2054 -0.0298 -0.0747 0.0266  201 THR   A CB  
3089  O  OG1 . THR   A 201 ? 0.1987 0.1732 0.2035 -0.0313 -0.0778 0.0251  201 THR   A OG1 
3090  C  CG2 . THR   A 201 ? 0.2042 0.1789 0.2109 -0.0287 -0.0737 0.0306  201 THR   A CG2 
3098  N  N   . VAL   A 202 ? 0.1712 0.1441 0.1655 -0.0305 -0.0738 0.0159  202 VAL   A N   
3099  C  CA  . VAL   A 202 ? 0.1791 0.1505 0.1721 -0.0320 -0.0752 0.0089  202 VAL   A CA  
3100  C  C   . VAL   A 202 ? 0.1895 0.1641 0.1699 -0.0351 -0.0756 0.0030  202 VAL   A C   
3101  O  O   . VAL   A 202 ? 0.1928 0.1711 0.1670 -0.0353 -0.0736 0.0044  202 VAL   A O   
3102  C  CB  . VAL   A 202 ? 0.1908 0.1585 0.1875 -0.0300 -0.0740 0.0082  202 VAL   A CB  
3103  C  CG1 . VAL   A 202 ? 0.1699 0.1403 0.1615 -0.0292 -0.0717 0.0084  202 VAL   A CG1 
3104  C  CG2 . VAL   A 202 ? 0.2088 0.1728 0.2122 -0.0311 -0.0756 0.0014  202 VAL   A CG2 
3114  N  N   . LYS   A 203 ? 0.1602 0.1362 0.1447 -0.0378 -0.0775 -0.0035 203 LYS   A N   
3115  C  CA  . LYS   A 203 ? 0.1878 0.1676 0.1594 -0.0414 -0.0776 -0.0112 203 LYS   A CA  
3116  C  C   . LYS   A 203 ? 0.1836 0.1602 0.1640 -0.0424 -0.0775 -0.0216 203 LYS   A C   
3117  O  O   . LYS   A 203 ? 0.2149 0.1865 0.2001 -0.0424 -0.0791 -0.0226 203 LYS   A O   
3118  C  CB  . LYS   A 203 ? 0.1990 0.1851 0.1674 -0.0443 -0.0798 -0.0103 203 LYS   A CB  
3119  C  CG  . LYS   A 203 ? 0.2493 0.2411 0.2043 -0.0486 -0.0800 -0.0186 203 LYS   A CG  
3120  C  CD  . LYS   A 203 ? 0.2587 0.2573 0.2073 -0.0514 -0.0827 -0.0160 203 LYS   A CD  
3121  C  CE  . LYS   A 203 ? 0.2324 0.2396 0.1762 -0.0557 -0.0828 -0.0240 203 LYS   A CE  
3122  N  NZ  . LYS   A 203 ? 0.2870 0.2990 0.2181 -0.0585 -0.0861 -0.0198 203 LYS   A NZ  
3136  N  N   . GLY   A 204 ? 0.2068 0.1831 0.1805 -0.0431 -0.0752 -0.0293 204 GLY   A N   
3137  C  CA  . GLY   A 204 ? 0.2362 0.2076 0.2140 -0.0429 -0.0733 -0.0405 204 GLY   A CA  
3138  C  C   . GLY   A 204 ? 0.2264 0.2045 0.1980 -0.0472 -0.0718 -0.0523 204 GLY   A C   
3139  O  O   . GLY   A 204 ? 0.2232 0.2080 0.1814 -0.0488 -0.0693 -0.0521 204 GLY   A O   
3143  N  N   . THR   A 205 ? 0.2526 0.2288 0.2268 -0.0498 -0.0728 -0.0623 205 THR   A N   
3144  C  CA  . THR   A 205 ? 0.2915 0.2742 0.2542 -0.0549 -0.0706 -0.0751 205 THR   A CA  
3145  C  C   . THR   A 205 ? 0.2910 0.2697 0.2650 -0.0522 -0.0649 -0.0881 205 THR   A C   
3146  O  O   . THR   A 205 ? 0.3099 0.2933 0.2757 -0.0548 -0.0610 -0.0980 205 THR   A O   
3147  C  CB  . THR   A 205 ? 0.2946 0.2833 0.2569 -0.0596 -0.0734 -0.0766 205 THR   A CB  
3148  O  OG1 . THR   A 205 ? 0.2732 0.2517 0.2485 -0.0590 -0.0741 -0.0791 205 THR   A OG1 
3149  C  CG2 . THR   A 205 ? 0.3273 0.3207 0.2833 -0.0585 -0.0776 -0.0638 205 THR   A CG2 
3157  N  N   . GLY   A 206 ? 0.2680 0.2386 0.2627 -0.0460 -0.0633 -0.0859 206 GLY   A N   
3158  C  CA  . GLY   A 206 ? 0.2989 0.2638 0.3034 -0.0425 -0.0581 -0.0969 206 GLY   A CA  
3159  C  C   . GLY   A 206 ? 0.2828 0.2528 0.2916 -0.0388 -0.0512 -0.0998 206 GLY   A C   
3160  O  O   . GLY   A 206 ? 0.2863 0.2636 0.2798 -0.0397 -0.0501 -0.0933 206 GLY   A O   
3164  N  N   . LYS   A 207 ? 0.2892 0.2549 0.3135 -0.0348 -0.0466 -0.1091 207 LYS   A N   
3165  C  CA  . LYS   A 207 ? 0.3132 0.2842 0.3476 -0.0306 -0.0396 -0.1127 207 LYS   A CA  
3166  C  C   . LYS   A 207 ? 0.3295 0.2885 0.3760 -0.0235 -0.0393 -0.1072 207 LYS   A C   
3167  O  O   . LYS   A 207 ? 0.3243 0.2751 0.3900 -0.0230 -0.0430 -0.1071 207 LYS   A O   
3168  C  CB  . LYS   A 207 ? 0.4359 0.4131 0.4642 -0.0330 -0.0337 -0.1310 207 LYS   A CB  
3169  C  CG  . LYS   A 207 ? 0.6332 0.6204 0.6299 -0.0403 -0.0330 -0.1353 207 LYS   A CG  
3170  C  CD  . LYS   A 207 ? 0.7261 0.7219 0.7204 -0.0415 -0.0252 -0.1490 207 LYS   A CD  
3171  C  CE  . LYS   A 207 ? 0.7392 0.7309 0.7496 -0.0410 -0.0238 -0.1599 207 LYS   A CE  
3172  N  NZ  . LYS   A 207 ? 0.7890 0.7895 0.7922 -0.0428 -0.0164 -0.1735 207 LYS   A NZ  
3186  N  N   . ILE   A 208 ? 0.2455 0.2094 0.3079 -0.0190 -0.0356 -0.1024 208 ILE   A N   
3187  C  CA  . ILE   A 208 ? 0.2687 0.2230 0.3438 -0.0126 -0.0355 -0.0971 208 ILE   A CA  
3188  C  C   . ILE   A 208 ? 0.2453 0.1976 0.3452 -0.0099 -0.0314 -0.1126 208 ILE   A C   
3189  O  O   . ILE   A 208 ? 0.2332 0.1936 0.3278 -0.0106 -0.0253 -0.1246 208 ILE   A O   
3190  C  CB  . ILE   A 208 ? 0.2232 0.1834 0.3042 -0.0091 -0.0339 -0.0856 208 ILE   A CB  
3191  C  CG1 . ILE   A 208 ? 0.2259 0.1846 0.2920 -0.0103 -0.0387 -0.0695 208 ILE   A CG1 
3192  C  CG2 . ILE   A 208 ? 0.2136 0.1694 0.3156 -0.0027 -0.0318 -0.0852 208 ILE   A CG2 
3193  C  CD1 . ILE   A 208 ? 0.2003 0.1646 0.2482 -0.0160 -0.0408 -0.0679 208 ILE   A CD1 
3205  N  N   . ALA   A 209 ? 0.2591 0.2001 0.3792 -0.0074 -0.0343 -0.1129 209 ALA   A N   
3206  C  CA  . ALA   A 209 ? 0.2681 0.2058 0.4088 -0.0044 -0.0305 -0.1253 209 ALA   A CA  
3207  C  C   . ALA   A 209 ? 0.2483 0.1886 0.4053 0.0019  -0.0258 -0.1269 209 ALA   A C   
3208  O  O   . ALA   A 209 ? 0.2575 0.1947 0.4217 0.0054  -0.0287 -0.1128 209 ALA   A O   
3209  C  CB  . ALA   A 209 ? 0.2853 0.2139 0.4406 -0.0032 -0.0346 -0.1200 209 ALA   A CB  
3215  N  N   . LEU   A 210 ? 0.2295 0.1822 0.3906 0.0030  -0.0179 -0.1360 210 LEU   A N   
3216  C  CA  . LEU   A 210 ? 0.3002 0.2504 0.4699 0.0091  -0.0133 -0.1444 210 LEU   A CA  
3217  C  C   . LEU   A 210 ? 0.2816 0.2304 0.4828 0.0129  -0.0113 -0.1502 210 LEU   A C   
3218  O  O   . LEU   A 210 ? 0.2534 0.2094 0.4507 0.0096  -0.0084 -0.1567 210 LEU   A O   
3219  C  CB  . LEU   A 210 ? 0.2478 0.2133 0.4105 0.0068  -0.0062 -0.1550 210 LEU   A CB  
3220  C  CG  . LEU   A 210 ? 0.2627 0.2349 0.3896 0.0013  -0.0079 -0.1450 210 LEU   A CG  
3221  C  CD1 . LEU   A 210 ? 0.2795 0.2669 0.3911 -0.0022 -0.0007 -0.1549 210 LEU   A CD1 
3222  C  CD2 . LEU   A 210 ? 0.2059 0.1776 0.3380 0.0042  -0.0121 -0.1251 210 LEU   A CD2 
3234  N  N   . ALA   A 211 ? 0.2617 0.2079 0.4912 0.0187  -0.0129 -0.1417 211 ALA   A N   
3235  C  CA  . ALA   A 211 ? 0.2900 0.2342 0.5457 0.0223  -0.0115 -0.1462 211 ALA   A CA  
3236  C  C   . ALA   A 211 ? 0.3250 0.2779 0.5770 0.0227  -0.0026 -0.1651 211 ALA   A C   
3237  O  O   . ALA   A 211 ? 0.3118 0.2652 0.5830 0.0231  -0.0006 -0.1750 211 ALA   A O   
3238  C  CB  . ALA   A 211 ? 0.3218 0.2622 0.5953 0.0272  -0.0154 -0.1318 211 ALA   A CB  
3244  N  N   . ASP   A 212 ? 0.2841 0.2489 0.5314 0.0224  0.0030  -0.1701 212 ASP   A N   
3245  C  CA  . ASP   A 212 ? 0.3324 0.3093 0.5783 0.0221  0.0122  -0.1865 212 ASP   A CA  
3246  C  C   . ASP   A 212 ? 0.3610 0.3475 0.5718 0.0178  0.0167  -0.1909 212 ASP   A C   
3247  O  O   . ASP   A 212 ? 0.3349 0.3283 0.5501 0.0204  0.0192  -0.1867 212 ASP   A O   
3248  C  CB  . ASP   A 212 ? 0.4205 0.3986 0.6862 0.0285  0.0150  -0.1871 212 ASP   A CB  
3249  C  CG  . ASP   A 212 ? 0.4212 0.4129 0.6995 0.0283  0.0245  -0.2044 212 ASP   A CG  
3250  O  OD1 . ASP   A 212 ? 0.4257 0.4258 0.6796 0.0230  0.0296  -0.2154 212 ASP   A OD1 
3251  O  OD2 . ASP   A 212 ? 0.4679 0.4596 0.7667 0.0329  0.0263  -0.2064 212 ASP   A OD2 
3256  N  N   . LYS   A 213 ? 0.3539 0.3453 0.5454 0.0108  0.0175  -0.1980 213 LYS   A N   
3257  C  CA  . LYS   A 213 ? 0.3947 0.3963 0.5525 0.0050  0.0204  -0.2001 213 LYS   A CA  
3258  C  C   . LYS   A 213 ? 0.3687 0.3849 0.5272 0.0064  0.0293  -0.2073 213 LYS   A C   
3259  O  O   . LYS   A 213 ? 0.3059 0.3292 0.4577 0.0059  0.0304  -0.2014 213 LYS   A O   
3260  C  CB  . LYS   A 213 ? 0.4283 0.4353 0.5721 -0.0029 0.0201  -0.2071 213 LYS   A CB  
3261  C  CG  . LYS   A 213 ? 0.5947 0.5883 0.7235 -0.0055 0.0116  -0.1998 213 LYS   A CG  
3262  C  CD  . LYS   A 213 ? 0.7470 0.7433 0.8496 -0.0132 0.0109  -0.2060 213 LYS   A CD  
3263  C  CE  . LYS   A 213 ? 0.7407 0.7272 0.8422 -0.0158 0.0024  -0.1982 213 LYS   A CE  
3264  N  NZ  . LYS   A 213 ? 0.6957 0.6876 0.7835 -0.0230 0.0016  -0.2043 213 LYS   A NZ  
3278  N  N   . GLU   A 214 ? 0.3667 0.3900 0.5400 0.0075  0.0359  -0.2204 214 GLU   A N   
3279  C  CA  . GLU   A 214 ? 0.3549 0.3947 0.5332 0.0077  0.0450  -0.2282 214 GLU   A CA  
3280  C  C   . GLU   A 214 ? 0.3691 0.4066 0.5600 0.0151  0.0449  -0.2191 214 GLU   A C   
3281  O  O   . GLU   A 214 ? 0.3713 0.4214 0.5565 0.0144  0.0498  -0.2185 214 GLU   A O   
3282  C  CB  . GLU   A 214 ? 0.3771 0.4240 0.5608 0.0065  0.0516  -0.2449 214 GLU   A CB  
3283  C  CG  . GLU   A 214 ? 0.3983 0.4507 0.5654 -0.0016 0.0526  -0.2539 214 GLU   A CG  
3284  C  CD  . GLU   A 214 ? 0.4798 0.5177 0.6470 -0.0019 0.0463  -0.2546 214 GLU   A CD  
3285  O  OE1 . GLU   A 214 ? 0.4469 0.4722 0.6403 0.0043  0.0415  -0.2485 214 GLU   A OE1 
3286  O  OE2 . GLU   A 214 ? 0.5604 0.6008 0.7072 -0.0086 0.0459  -0.2600 214 GLU   A OE2 
3293  N  N   . LYS   A 215 ? 0.3189 0.3443 0.5405 0.0216  0.0393  -0.2110 215 LYS   A N   
3294  C  CA  . LYS   A 215 ? 0.3057 0.3298 0.5475 0.0284  0.0375  -0.1993 215 LYS   A CA  
3295  C  C   . LYS   A 215 ? 0.2959 0.3180 0.5141 0.0277  0.0339  -0.1867 215 LYS   A C   
3296  O  O   . LYS   A 215 ? 0.2654 0.2968 0.4892 0.0303  0.0367  -0.1819 215 LYS   A O   
3297  C  CB  . LYS   A 215 ? 0.3681 0.3779 0.6355 0.0339  0.0307  -0.1905 215 LYS   A CB  
3298  C  CG  . LYS   A 215 ? 0.4223 0.4319 0.7112 0.0402  0.0286  -0.1783 215 LYS   A CG  
3299  C  CD  . LYS   A 215 ? 0.4659 0.4615 0.7671 0.0432  0.0185  -0.1611 215 LYS   A CD  
3300  C  CE  . LYS   A 215 ? 0.4522 0.4404 0.7814 0.0445  0.0151  -0.1619 215 LYS   A CE  
3301  N  NZ  . LYS   A 215 ? 0.5038 0.4781 0.8310 0.0439  0.0056  -0.1473 215 LYS   A NZ  
3315  N  N   . VAL   A 216 ? 0.2644 0.2777 0.4697 0.0241  0.0274  -0.1805 216 VAL   A N   
3316  C  CA  . VAL   A 216 ? 0.2615 0.2750 0.4403 0.0206  0.0216  -0.1616 216 VAL   A CA  
3317  C  C   . VAL   A 216 ? 0.2622 0.2922 0.4182 0.0154  0.0279  -0.1644 216 VAL   A C   
3318  O  O   . VAL   A 216 ? 0.2316 0.2677 0.3831 0.0156  0.0268  -0.1514 216 VAL   A O   
3319  C  CB  . VAL   A 216 ? 0.2322 0.2358 0.4013 0.0161  0.0135  -0.1534 216 VAL   A CB  
3320  C  CG1 . VAL   A 216 ? 0.2545 0.2607 0.3925 0.0113  0.0095  -0.1383 216 VAL   A CG1 
3321  C  CG2 . VAL   A 216 ? 0.2487 0.2359 0.4349 0.0207  0.0068  -0.1467 216 VAL   A CG2 
3331  N  N   . LYS   A 217 ? 0.2721 0.3106 0.4163 0.0105  0.0342  -0.1812 217 LYS   A N   
3332  C  CA  . LYS   A 217 ? 0.2842 0.3391 0.4030 0.0042  0.0404  -0.1850 217 LYS   A CA  
3333  C  C   . LYS   A 217 ? 0.2353 0.3028 0.3736 0.0087  0.0473  -0.1860 217 LYS   A C   
3334  O  O   . LYS   A 217 ? 0.2358 0.3128 0.3560 0.0054  0.0485  -0.1769 217 LYS   A O   
3335  C  CB  . LYS   A 217 ? 0.2877 0.3524 0.3973 -0.0023 0.0464  -0.2034 217 LYS   A CB  
3336  C  CG  . LYS   A 217 ? 0.3756 0.4579 0.4565 -0.0091 0.0532  -0.2072 217 LYS   A CG  
3337  C  CD  . LYS   A 217 ? 0.4105 0.4973 0.4642 -0.0173 0.0485  -0.1954 217 LYS   A CD  
3338  C  CE  . LYS   A 217 ? 0.4783 0.5828 0.5122 -0.0229 0.0541  -0.1926 217 LYS   A CE  
3339  N  NZ  . LYS   A 217 ? 0.5685 0.6731 0.5708 -0.0302 0.0478  -0.1779 217 LYS   A NZ  
3353  N  N   . LYS   A 218 ? 0.2503 0.3153 0.4142 0.0156  0.0515  -0.1967 218 LYS   A N   
3354  C  CA  . LYS   A 218 ? 0.2403 0.3164 0.4217 0.0187  0.0560  -0.1935 218 LYS   A CA  
3355  C  C   . LYS   A 218 ? 0.2216 0.2951 0.4101 0.0238  0.0517  -0.1778 218 LYS   A C   
3356  O  O   . LYS   A 218 ? 0.2165 0.3023 0.3980 0.0222  0.0549  -0.1723 218 LYS   A O   
3357  C  CB  . LYS   A 218 ? 0.2524 0.3256 0.4605 0.0231  0.0579  -0.2016 218 LYS   A CB  
3358  C  CG  . LYS   A 218 ? 0.2533 0.3355 0.4840 0.0276  0.0627  -0.2026 218 LYS   A CG  
3359  C  CD  . LYS   A 218 ? 0.2695 0.3508 0.5231 0.0304  0.0658  -0.2136 218 LYS   A CD  
3360  C  CE  . LYS   A 218 ? 0.2712 0.3608 0.5458 0.0349  0.0699  -0.2139 218 LYS   A CE  
3361  N  NZ  . LYS   A 218 ? 0.2807 0.3885 0.5444 0.0309  0.0797  -0.2245 218 LYS   A NZ  
3375  N  N   . VAL   A 219 ? 0.2137 0.2714 0.4125 0.0276  0.0424  -0.1652 219 VAL   A N   
3376  C  CA  . VAL   A 219 ? 0.1984 0.2527 0.4016 0.0302  0.0351  -0.1444 219 VAL   A CA  
3377  C  C   . VAL   A 219 ? 0.2106 0.2702 0.3811 0.0232  0.0330  -0.1327 219 VAL   A C   
3378  O  O   . VAL   A 219 ? 0.2156 0.2829 0.3849 0.0233  0.0332  -0.1233 219 VAL   A O   
3379  C  CB  . VAL   A 219 ? 0.1936 0.2312 0.4144 0.0341  0.0257  -0.1337 219 VAL   A CB  
3380  C  CG1 . VAL   A 219 ? 0.2222 0.2565 0.4355 0.0347  0.0182  -0.1127 219 VAL   A CG1 
3381  C  CG2 . VAL   A 219 ? 0.2066 0.2374 0.4580 0.0414  0.0267  -0.1424 219 VAL   A CG2 
3391  N  N   . SER   A 220 ? 0.2090 0.2648 0.3565 0.0169  0.0304  -0.1325 220 SER   A N   
3392  C  CA  . SER   A 220 ? 0.2362 0.2955 0.3527 0.0104  0.0276  -0.1217 220 SER   A CA  
3393  C  C   . SER   A 220 ? 0.2342 0.3102 0.3396 0.0068  0.0351  -0.1251 220 SER   A C   
3394  O  O   . SER   A 220 ? 0.2232 0.3039 0.3228 0.0053  0.0332  -0.1127 220 SER   A O   
3395  C  CB  . SER   A 220 ? 0.2577 0.3115 0.3533 0.0045  0.0241  -0.1225 220 SER   A CB  
3396  O  OG  . SER   A 220 ? 0.2851 0.3442 0.3541 -0.0021 0.0227  -0.1145 220 SER   A OG  
3402  N  N   . VAL   A 221 ? 0.2124 0.2993 0.3201 0.0051  0.0439  -0.1423 221 VAL   A N   
3403  C  CA  . VAL   A 221 ? 0.2074 0.3132 0.3090 0.0005  0.0520  -0.1472 221 VAL   A CA  
3404  C  C   . VAL   A 221 ? 0.2560 0.3661 0.3650 0.0055  0.0538  -0.1405 221 VAL   A C   
3405  O  O   . VAL   A 221 ? 0.2533 0.3753 0.3558 0.0013  0.0558  -0.1339 221 VAL   A O   
3406  C  CB  . VAL   A 221 ? 0.2431 0.3592 0.3376 -0.0022 0.0616  -0.1683 221 VAL   A CB  
3407  C  CG1 . VAL   A 221 ? 0.2514 0.3870 0.3442 -0.0048 0.0712  -0.1742 221 VAL   A CG1 
3408  C  CG2 . VAL   A 221 ? 0.2835 0.3972 0.3528 -0.0098 0.0598  -0.1732 221 VAL   A CG2 
3418  N  N   . GLU   A 222 ? 0.1959 0.3016 0.3431 0.0139  0.0528  -0.1414 222 GLU   A N   
3419  C  CA  . GLU   A 222 ? 0.2111 0.3223 0.3779 0.0191  0.0534  -0.1346 222 GLU   A CA  
3420  C  C   . GLU   A 222 ? 0.2212 0.3270 0.3718 0.0175  0.0450  -0.1141 222 GLU   A C   
3421  O  O   . GLU   A 222 ? 0.2030 0.3204 0.3543 0.0156  0.0469  -0.1082 222 GLU   A O   
3422  C  CB  . GLU   A 222 ? 0.2591 0.3632 0.4582 0.0283  0.0527  -0.1393 222 GLU   A CB  
3423  C  CG  . GLU   A 222 ? 0.3063 0.4125 0.5299 0.0338  0.0494  -0.1278 222 GLU   A CG  
3424  C  CD  . GLU   A 222 ? 0.3921 0.4868 0.6441 0.0422  0.0444  -0.1257 222 GLU   A CD  
3425  O  OE1 . GLU   A 222 ? 0.4034 0.4911 0.6679 0.0449  0.0462  -0.1379 222 GLU   A OE1 
3426  O  OE2 . GLU   A 222 ? 0.4367 0.5300 0.7014 0.0458  0.0384  -0.1118 222 GLU   A OE2 
3433  N  N   . LYS   A 223 ? 0.1858 0.2776 0.3357 0.0178  0.0360  -0.1037 223 LYS   A N   
3434  C  CA  . LYS   A 223 ? 0.1818 0.2683 0.3202 0.0166  0.0279  -0.0853 223 LYS   A CA  
3435  C  C   . LYS   A 223 ? 0.1982 0.2908 0.3054 0.0087  0.0289  -0.0803 223 LYS   A C   
3436  O  O   . LYS   A 223 ? 0.1584 0.2564 0.2684 0.0074  0.0267  -0.0696 223 LYS   A O   
3437  C  CB  . LYS   A 223 ? 0.1502 0.2210 0.2934 0.0183  0.0194  -0.0778 223 LYS   A CB  
3438  C  CG  . LYS   A 223 ? 0.1538 0.2166 0.3239 0.0251  0.0177  -0.0819 223 LYS   A CG  
3439  C  CD  . LYS   A 223 ? 0.2088 0.2753 0.4005 0.0314  0.0188  -0.0806 223 LYS   A CD  
3440  C  CE  . LYS   A 223 ? 0.1802 0.2383 0.4054 0.0381  0.0158  -0.0822 223 LYS   A CE  
3441  N  NZ  . LYS   A 223 ? 0.1649 0.2297 0.4186 0.0444  0.0178  -0.0831 223 LYS   A NZ  
3455  N  N   . ILE   A 224 ? 0.1618 0.2576 0.2569 0.0033  0.0317  -0.0878 224 ILE   A N   
3456  C  CA  . ILE   A 224 ? 0.1959 0.2975 0.2623 -0.0047 0.0320  -0.0831 224 ILE   A CA  
3457  C  C   . ILE   A 224 ? 0.2036 0.3210 0.2688 -0.0068 0.0390  -0.0846 224 ILE   A C   
3458  O  O   . ILE   A 224 ? 0.1951 0.3169 0.2513 -0.0110 0.0371  -0.0742 224 ILE   A O   
3459  C  CB  . ILE   A 224 ? 0.2328 0.3329 0.2761 -0.0104 0.0329  -0.0902 224 ILE   A CB  
3460  C  CG1 . ILE   A 224 ? 0.2184 0.3042 0.2652 -0.0094 0.0253  -0.0866 224 ILE   A CG1 
3461  C  CG2 . ILE   A 224 ? 0.2376 0.3477 0.2602 -0.0189 0.0344  -0.0861 224 ILE   A CG2 
3462  C  CD1 . ILE   A 224 ? 0.3000 0.3825 0.3278 -0.0131 0.0262  -0.0968 224 ILE   A CD1 
3474  N  N   . THR   A 225 ? 0.1779 0.3061 0.2627 -0.0039 0.0472  -0.0981 225 THR   A N   
3475  C  CA  . THR   A 225 ? 0.2033 0.3483 0.2916 -0.0055 0.0549  -0.1014 225 THR   A CA  
3476  C  C   . THR   A 225 ? 0.2122 0.3566 0.3089 -0.0024 0.0506  -0.0879 225 THR   A C   
3477  O  O   . THR   A 225 ? 0.1963 0.3507 0.2868 -0.0074 0.0519  -0.0812 225 THR   A O   
3478  C  CB  . THR   A 225 ? 0.2165 0.3714 0.3209 -0.0018 0.0647  -0.1196 225 THR   A CB  
3479  O  OG1 . THR   A 225 ? 0.1976 0.3549 0.2898 -0.0066 0.0691  -0.1321 225 THR   A OG1 
3480  C  CG2 . THR   A 225 ? 0.2400 0.4127 0.3537 -0.0024 0.0728  -0.1228 225 THR   A CG2 
3488  N  N   . THR   A 226 ? 0.1897 0.3248 0.3090 0.0048  0.0452  -0.0834 226 THR   A N   
3489  C  CA  . THR   A 226 ? 0.1733 0.3080 0.3038 0.0077  0.0399  -0.0704 226 THR   A CA  
3490  C  C   . THR   A 226 ? 0.1821 0.3112 0.2860 0.0017  0.0335  -0.0565 226 THR   A C   
3491  O  O   . THR   A 226 ? 0.1318 0.2702 0.2418 -0.0008 0.0332  -0.0490 226 THR   A O   
3492  C  CB  . THR   A 226 ? 0.1394 0.2645 0.2972 0.0156  0.0343  -0.0674 226 THR   A CB  
3493  O  OG1 . THR   A 226 ? 0.1473 0.2747 0.3228 0.0211  0.0404  -0.0811 226 THR   A OG1 
3494  C  CG2 . THR   A 226 ? 0.1433 0.2696 0.3104 0.0180  0.0289  -0.0546 226 THR   A CG2 
3502  N  N   . LEU   A 227 ? 0.1364 0.2553 0.2337 -0.0005 0.0283  -0.0531 227 LEU   A N   
3503  C  CA  . LEU   A 227 ? 0.1911 0.3023 0.2590 -0.0056 0.0221  -0.0410 227 LEU   A CA  
3504  C  C   . LEU   A 227 ? 0.1865 0.3091 0.2410 -0.0130 0.0263  -0.0404 227 LEU   A C   
3505  O  O   . LEU   A 227 ? 0.1480 0.2733 0.2003 -0.0162 0.0234  -0.0306 227 LEU   A O   
3506  C  CB  . LEU   A 227 ? 0.1518 0.2510 0.2191 -0.0061 0.0167  -0.0394 227 LEU   A CB  
3507  C  CG  . LEU   A 227 ? 0.2098 0.2946 0.2774 -0.0002 0.0107  -0.0357 227 LEU   A CG  
3508  C  CD1 . LEU   A 227 ? 0.1600 0.2351 0.2277 -0.0012 0.0070  -0.0366 227 LEU   A CD1 
3509  C  CD2 . LEU   A 227 ? 0.1713 0.2563 0.2530 0.0007  0.0051  -0.0234 227 LEU   A CD2 
3521  N  N   . LYS   A 228 ? 0.1883 0.3186 0.2349 -0.0163 0.0329  -0.0506 228 LYS   A N   
3522  C  CA  . LYS   A 228 ? 0.1719 0.3146 0.2072 -0.0243 0.0371  -0.0502 228 LYS   A CA  
3523  C  C   . LYS   A 228 ? 0.2115 0.3662 0.2477 -0.0248 0.0419  -0.0486 228 LYS   A C   
3524  O  O   . LYS   A 228 ? 0.1912 0.3539 0.2215 -0.0315 0.0423  -0.0420 228 LYS   A O   
3525  C  CB  . LYS   A 228 ? 0.2081 0.3561 0.2279 -0.0282 0.0428  -0.0617 228 LYS   A CB  
3526  C  CG  . LYS   A 228 ? 0.2699 0.4063 0.2702 -0.0308 0.0379  -0.0617 228 LYS   A CG  
3527  C  CD  . LYS   A 228 ? 0.2882 0.4340 0.2808 -0.0358 0.0433  -0.0728 228 LYS   A CD  
3528  C  CE  . LYS   A 228 ? 0.3702 0.5039 0.3386 -0.0386 0.0377  -0.0721 228 LYS   A CE  
3529  N  NZ  . LYS   A 228 ? 0.3336 0.4720 0.2879 -0.0473 0.0346  -0.0634 228 LYS   A NZ  
3543  N  N   . ASN   A 229 ? 0.1713 0.3319 0.2379 -0.0180 0.0450  -0.0539 229 ASN   A N   
3544  C  CA  . ASN   A 229 ? 0.1828 0.3573 0.2620 -0.0177 0.0495  -0.0534 229 ASN   A CA  
3545  C  C   . ASN   A 229 ? 0.1936 0.3624 0.2744 -0.0163 0.0421  -0.0398 229 ASN   A C   
3546  O  O   . ASN   A 229 ? 0.1473 0.3290 0.2427 -0.0176 0.0443  -0.0368 229 ASN   A O   
3547  C  CB  . ASN   A 229 ? 0.1838 0.3683 0.2891 -0.0114 0.0570  -0.0666 229 ASN   A CB  
3548  C  CG  . ASN   A 229 ? 0.2727 0.4679 0.3714 -0.0147 0.0669  -0.0813 229 ASN   A CG  
3549  O  OD1 . ASN   A 229 ? 0.3372 0.5389 0.4099 -0.0229 0.0699  -0.0804 229 ASN   A OD1 
3550  N  ND2 . ASN   A 229 ? 0.3550 0.5496 0.4635 -0.0087 0.0718  -0.0948 229 ASN   A ND2 
3557  N  N   . ASP   A 230 ? 0.1637 0.3184 0.2478 -0.0141 0.0333  -0.0321 230 ASP   A N   
3558  C  CA  . ASP   A 230 ? 0.1744 0.3236 0.2586 -0.0132 0.0259  -0.0199 230 ASP   A CA  
3559  C  C   . ASP   A 230 ? 0.1631 0.3139 0.2336 -0.0210 0.0234  -0.0112 230 ASP   A C   
3560  O  O   . ASP   A 230 ? 0.1738 0.3185 0.2234 -0.0254 0.0227  -0.0107 230 ASP   A O   
3561  C  CB  . ASP   A 230 ? 0.1644 0.2992 0.2552 -0.0087 0.0181  -0.0153 230 ASP   A CB  
3562  C  CG  . ASP   A 230 ? 0.1618 0.2933 0.2552 -0.0085 0.0107  -0.0038 230 ASP   A CG  
3563  O  OD1 . ASP   A 230 ? 0.1413 0.2789 0.2554 -0.0043 0.0098  -0.0021 230 ASP   A OD1 
3564  O  OD2 . ASP   A 230 ? 0.1604 0.2848 0.2394 -0.0127 0.0059  0.0031  230 ASP   A OD2 
3569  N  N   . PRO   A 231 ? 0.1828 0.3396 0.2563 -0.0229 0.0217  -0.0039 231 PRO   A N   
3570  C  CA  . PRO   A 231 ? 0.2057 0.3622 0.2623 -0.0303 0.0192  0.0042  231 PRO   A CA  
3571  C  C   . PRO   A 231 ? 0.1286 0.2716 0.1792 -0.0322 0.0119  0.0106  231 PRO   A C   
3572  O  O   . PRO   A 231 ? 0.1974 0.3362 0.2235 -0.0383 0.0111  0.0141  231 PRO   A O   
3573  C  CB  . PRO   A 231 ? 0.2416 0.4063 0.3126 -0.0303 0.0176  0.0095  231 PRO   A CB  
3574  C  CG  . PRO   A 231 ? 0.2272 0.4014 0.3188 -0.0240 0.0222  0.0028  231 PRO   A CG  
3575  C  CD  . PRO   A 231 ? 0.1619 0.3278 0.2620 -0.0183 0.0218  -0.0032 231 PRO   A CD  
3583  N  N   . VAL   A 232 ? 0.1175 0.2493 0.1679 -0.0270 0.0062  0.0125  232 VAL   A N   
3584  C  CA  . VAL   A 232 ? 0.1380 0.2551 0.1737 -0.0283 -0.0002 0.0179  232 VAL   A CA  
3585  C  C   . VAL   A 232 ? 0.1449 0.2550 0.1732 -0.0278 0.0006  0.0131  232 VAL   A C   
3586  O  O   . VAL   A 232 ? 0.1769 0.2813 0.1871 -0.0325 -0.0009 0.0156  232 VAL   A O   
3587  C  CB  . VAL   A 232 ? 0.1150 0.2279 0.1669 -0.0245 -0.0067 0.0230  232 VAL   A CB  
3588  C  CG1 . VAL   A 232 ? 0.1410 0.2395 0.1739 -0.0259 -0.0123 0.0273  232 VAL   A CG1 
3589  C  CG2 . VAL   A 232 ? 0.1972 0.3162 0.2488 -0.0255 -0.0082 0.0278  232 VAL   A CG2 
3599  N  N   . ALA   A 233 ? 0.1512 0.2596 0.1859 -0.0224 0.0027  0.0063  233 ALA   A N   
3600  C  CA  . ALA   A 233 ? 0.1523 0.2535 0.1808 -0.0219 0.0030  0.0009  233 ALA   A CA  
3601  C  C   . ALA   A 233 ? 0.1625 0.2711 0.1798 -0.0270 0.0085  -0.0043 233 ALA   A C   
3602  O  O   . ALA   A 233 ? 0.2141 0.3155 0.2132 -0.0296 0.0069  -0.0049 233 ALA   A O   
3603  C  CB  . ALA   A 233 ? 0.1630 0.2609 0.2035 -0.0152 0.0037  -0.0051 233 ALA   A CB  
3609  N  N   . GLY   A 234 ? 0.1718 0.2938 0.1918 -0.0287 0.0149  -0.0080 234 GLY   A N   
3610  C  CA  . GLY   A 234 ? 0.2083 0.3396 0.2164 -0.0341 0.0209  -0.0133 234 GLY   A CA  
3611  C  C   . GLY   A 234 ? 0.2465 0.3802 0.2323 -0.0423 0.0202  -0.0055 234 GLY   A C   
3612  O  O   . GLY   A 234 ? 0.1938 0.3358 0.1771 -0.0478 0.0234  -0.0077 234 GLY   A O   
3616  N  N   . GLN   A 235 ? 0.1737 0.3079 0.1747 -0.0436 0.0159  0.0039  235 GLN   A N   
3617  C  CA  . GLN   A 235 ? 0.2184 0.3541 0.1993 -0.0513 0.0149  0.0118  235 GLN   A CA  
3618  C  C   . GLN   A 235 ? 0.1629 0.2878 0.1472 -0.0525 0.0068  0.0215  235 GLN   A C   
3619  O  O   . GLN   A 235 ? 0.1661 0.2844 0.1349 -0.0569 0.0035  0.0265  235 GLN   A O   
3620  C  CB  . GLN   A 235 ? 0.2190 0.3719 0.2174 -0.0535 0.0205  0.0113  235 GLN   A CB  
3621  C  CG  . GLN   A 235 ? 0.3174 0.4839 0.3111 -0.0545 0.0296  0.0021  235 GLN   A CG  
3622  C  CD  . GLN   A 235 ? 0.3952 0.5672 0.3734 -0.0625 0.0319  0.0023  235 GLN   A CD  
3623  O  OE1 . GLN   A 235 ? 0.3779 0.5448 0.3440 -0.0683 0.0271  0.0118  235 GLN   A OE1 
3624  N  NE2 . GLN   A 235 ? 0.5158 0.6964 0.4846 -0.0630 0.0392  -0.0078 235 GLN   A NE2 
3633  N  N   . GLY   A 236 ? 0.1654 0.2867 0.1580 -0.0484 0.0036  0.0242  236 GLY   A N   
3634  C  CA  . GLY   A 236 ? 0.1725 0.2836 0.1613 -0.0500 -0.0032 0.0317  236 GLY   A CA  
3635  C  C   . GLY   A 236 ? 0.1616 0.2593 0.1448 -0.0488 -0.0080 0.0329  236 GLY   A C   
3636  O  O   . GLY   A 236 ? 0.1847 0.2755 0.1573 -0.0531 -0.0120 0.0387  236 GLY   A O   
3640  N  N   A MET   A 237 ? 0.1609 0.2537 0.1460 -0.0431 -0.0084 0.0283  237 MET   A N   
3641  N  N   B MET   A 237 ? 0.1608 0.2536 0.1460 -0.0431 -0.0084 0.0283  237 MET   A N   
3642  C  CA  A MET   A 237 ? 0.1809 0.2605 0.1570 -0.0416 -0.0130 0.0290  237 MET   A CA  
3643  C  CA  B MET   A 237 ? 0.1810 0.2605 0.1570 -0.0416 -0.0130 0.0290  237 MET   A CA  
3644  C  C   A MET   A 237 ? 0.1666 0.2454 0.1326 -0.0461 -0.0130 0.0295  237 MET   A C   
3645  C  C   B MET   A 237 ? 0.1665 0.2453 0.1325 -0.0461 -0.0130 0.0295  237 MET   A C   
3646  O  O   A MET   A 237 ? 0.1729 0.2423 0.1305 -0.0478 -0.0177 0.0341  237 MET   A O   
3647  O  O   B MET   A 237 ? 0.1729 0.2423 0.1305 -0.0478 -0.0177 0.0340  237 MET   A O   
3648  C  CB  A MET   A 237 ? 0.1790 0.2552 0.1657 -0.0351 -0.0132 0.0243  237 MET   A CB  
3649  C  CB  B MET   A 237 ? 0.1792 0.2552 0.1658 -0.0351 -0.0132 0.0242  237 MET   A CB  
3650  C  CG  A MET   A 237 ? 0.1994 0.2751 0.1957 -0.0312 -0.0154 0.0262  237 MET   A CG  
3651  C  CG  B MET   A 237 ? 0.2011 0.2786 0.1993 -0.0308 -0.0143 0.0250  237 MET   A CG  
3652  S  SD  A MET   A 237 ? 0.2026 0.2683 0.1962 -0.0322 -0.0221 0.0326  237 MET   A SD  
3653  S  SD  B MET   A 237 ? 0.2143 0.2804 0.2150 -0.0268 -0.0200 0.0275  237 MET   A SD  
3654  C  CE  A MET   A 237 ? 0.1955 0.2530 0.1925 -0.0269 -0.0244 0.0307  237 MET   A CE  
3655  C  CE  B MET   A 237 ? 0.2233 0.2837 0.2154 -0.0315 -0.0246 0.0339  237 MET   A CE  
3674  N  N   . PRO   A 238 ? 0.1789 0.2656 0.1388 -0.0478 -0.0078 0.0242  238 PRO   A N   
3675  C  CA  . PRO   A 238 ? 0.1741 0.2618 0.1248 -0.0526 -0.0083 0.0250  238 PRO   A CA  
3676  C  C   . PRO   A 238 ? 0.2039 0.2904 0.1406 -0.0595 -0.0111 0.0343  238 PRO   A C   
3677  O  O   . PRO   A 238 ? 0.2028 0.2832 0.1345 -0.0622 -0.0156 0.0390  238 PRO   A O   
3678  C  CB  . PRO   A 238 ? 0.2193 0.3172 0.1618 -0.0536 -0.0013 0.0165  238 PRO   A CB  
3679  C  CG  . PRO   A 238 ? 0.1958 0.3008 0.1570 -0.0487 0.0030  0.0116  238 PRO   A CG  
3680  C  CD  . PRO   A 238 ? 0.1931 0.2872 0.1612 -0.0435 -0.0022 0.0154  238 PRO   A CD  
3688  N  N   . THR   A 239 ? 0.1734 0.2684 0.1180 -0.0619 -0.0087 0.0371  239 THR   A N   
3689  C  CA  . THR   A 239 ? 0.1592 0.2555 0.1003 -0.0691 -0.0108 0.0458  239 THR   A CA  
3690  C  C   . THR   A 239 ? 0.1536 0.2372 0.0994 -0.0683 -0.0175 0.0518  239 THR   A C   
3691  O  O   . THR   A 239 ? 0.1815 0.2571 0.1233 -0.0701 -0.0213 0.0551  239 THR   A O   
3692  C  CB  . THR   A 239 ? 0.1777 0.2875 0.1231 -0.0725 -0.0056 0.0463  239 THR   A CB  
3693  O  OG1 . THR   A 239 ? 0.1892 0.3109 0.1312 -0.0727 0.0014  0.0388  239 THR   A OG1 
3694  C  CG2 . THR   A 239 ? 0.2236 0.3327 0.1637 -0.0790 -0.0081 0.0537  239 THR   A CG2 
3702  N  N   . TYR   A 240 ? 0.1697 0.2491 0.1220 -0.0633 -0.0187 0.0500  240 TYR   A N   
3703  C  CA  . TYR   A 240 ? 0.1904 0.2598 0.1459 -0.0633 -0.0240 0.0544  240 TYR   A CA  
3704  C  C   . TYR   A 240 ? 0.1953 0.2540 0.1516 -0.0576 -0.0274 0.0519  240 TYR   A C   
3705  O  O   . TYR   A 240 ? 0.1732 0.2238 0.1359 -0.0571 -0.0310 0.0531  240 TYR   A O   
3706  C  CB  . TYR   A 240 ? 0.1876 0.2633 0.1528 -0.0644 -0.0229 0.0555  240 TYR   A CB  
3707  C  CG  . TYR   A 240 ? 0.2014 0.2877 0.1652 -0.0705 -0.0196 0.0585  240 TYR   A CG  
3708  C  CD1 . TYR   A 240 ? 0.2094 0.2928 0.1722 -0.0754 -0.0221 0.0633  240 TYR   A CD1 
3709  C  CD2 . TYR   A 240 ? 0.1983 0.2980 0.1687 -0.0698 -0.0138 0.0549  240 TYR   A CD2 
3710  C  CE1 . TYR   A 240 ? 0.2363 0.3289 0.1977 -0.0804 -0.0194 0.0655  240 TYR   A CE1 
3711  C  CE2 . TYR   A 240 ? 0.2188 0.3297 0.1881 -0.0757 -0.0101 0.0576  240 TYR   A CE2 
3712  C  CZ  . TYR   A 240 ? 0.2503 0.3575 0.2138 -0.0814 -0.0131 0.0634  240 TYR   A CZ  
3713  O  OH  . TYR   A 240 ? 0.2782 0.3951 0.2415 -0.0861 -0.0102 0.0652  240 TYR   A OH  
3723  N  N   . GLY   A 241 ? 0.1853 0.2448 0.1434 -0.0529 -0.0257 0.0464  241 GLY   A N   
3724  C  CA  . GLY   A 241 ? 0.1706 0.2216 0.1320 -0.0479 -0.0286 0.0444  241 GLY   A CA  
3725  C  C   . GLY   A 241 ? 0.1687 0.2189 0.1374 -0.0450 -0.0291 0.0433  241 GLY   A C   
3726  O  O   . GLY   A 241 ? 0.1757 0.2340 0.1495 -0.0461 -0.0276 0.0444  241 GLY   A O   
3730  N  N   . THR   A 242 ? 0.1266 0.1505 0.1172 -0.0480 -0.0168 0.0275  242 THR   A N   
3731  C  CA  . THR   A 242 ? 0.1341 0.1571 0.1300 -0.0456 -0.0164 0.0257  242 THR   A CA  
3732  C  C   . THR   A 242 ? 0.1524 0.1722 0.1452 -0.0489 -0.0200 0.0294  242 THR   A C   
3733  O  O   . THR   A 242 ? 0.1494 0.1728 0.1496 -0.0485 -0.0193 0.0293  242 THR   A O   
3734  C  CB  . THR   A 242 ? 0.1481 0.1648 0.1438 -0.0407 -0.0172 0.0222  242 THR   A CB  
3735  O  OG1 . THR   A 242 ? 0.1208 0.1303 0.1172 -0.0414 -0.0220 0.0234  242 THR   A OG1 
3736  C  CG2 . THR   A 242 ? 0.1604 0.1793 0.1566 -0.0377 -0.0135 0.0184  242 THR   A CG2 
3744  N  N   . ALA   A 243 ? 0.1114 0.1266 0.1059 -0.0527 -0.0241 0.0327  243 ALA   A N   
3745  C  CA  . ALA   A 243 ? 0.1242 0.1353 0.1166 -0.0564 -0.0283 0.0366  243 ALA   A CA  
3746  C  C   . ALA   A 243 ? 0.1583 0.1767 0.1491 -0.0607 -0.0260 0.0390  243 ALA   A C   
3747  O  O   . ALA   A 243 ? 0.1563 0.1731 0.1510 -0.0637 -0.0288 0.0414  243 ALA   A O   
3748  C  CB  . ALA   A 243 ? 0.1233 0.1273 0.1097 -0.0597 -0.0322 0.0400  243 ALA   A CB  
3754  N  N   . ILE   A 244 ? 0.1421 0.1712 0.1363 -0.0605 -0.0208 0.0382  244 ILE   A N   
3755  C  CA  . ILE   A 244 ? 0.1418 0.1808 0.1386 -0.0636 -0.0182 0.0400  244 ILE   A CA  
3756  C  C   . ILE   A 244 ? 0.1499 0.1892 0.1494 -0.0618 -0.0185 0.0386  244 ILE   A C   
3757  O  O   . ILE   A 244 ? 0.1447 0.1904 0.1492 -0.0654 -0.0183 0.0409  244 ILE   A O   
3758  C  CB  . ILE   A 244 ? 0.1503 0.2002 0.1484 -0.0620 -0.0123 0.0381  244 ILE   A CB  
3759  C  CG1 . ILE   A 244 ? 0.1939 0.2542 0.1881 -0.0661 -0.0096 0.0407  244 ILE   A CG1 
3760  C  CG2 . ILE   A 244 ? 0.1708 0.2208 0.1687 -0.0552 -0.0092 0.0330  244 ILE   A CG2 
3761  C  CD1 . ILE   A 244 ? 0.1892 0.2607 0.1855 -0.0643 -0.0038 0.0389  244 ILE   A CD1 
3773  N  N   . LEU   A 245 ? 0.1126 0.1477 0.1199 -0.0567 -0.0193 0.0352  245 LEU   A N   
3774  C  CA  . LEU   A 245 ? 0.1286 0.1647 0.1383 -0.0542 -0.0193 0.0335  245 LEU   A CA  
3775  C  C   . LEU   A 245 ? 0.1307 0.1613 0.1418 -0.0576 -0.0243 0.0357  245 LEU   A C   
3776  O  O   . LEU   A 245 ? 0.1328 0.1670 0.1476 -0.0575 -0.0243 0.0352  245 LEU   A O   
3777  C  CB  . LEU   A 245 ? 0.1375 0.1700 0.1489 -0.0476 -0.0184 0.0292  245 LEU   A CB  
3778  C  CG  . LEU   A 245 ? 0.1338 0.1722 0.1477 -0.0436 -0.0131 0.0265  245 LEU   A CG  
3779  C  CD1 . LEU   A 245 ? 0.1289 0.1605 0.1416 -0.0387 -0.0132 0.0230  245 LEU   A CD1 
3780  C  CD2 . LEU   A 245 ? 0.1541 0.2012 0.1706 -0.0417 -0.0096 0.0259  245 LEU   A CD2 
3792  N  N   . VAL   A 246 ? 0.1374 0.1590 0.1448 -0.0609 -0.0286 0.0379  246 VAL   A N   
3793  C  CA  . VAL   A 246 ? 0.1530 0.1664 0.1580 -0.0636 -0.0338 0.0395  246 VAL   A CA  
3794  C  C   . VAL   A 246 ? 0.1345 0.1556 0.1453 -0.0680 -0.0335 0.0415  246 VAL   A C   
3795  O  O   . VAL   A 246 ? 0.1283 0.1496 0.1421 -0.0665 -0.0345 0.0395  246 VAL   A O   
3796  C  CB  . VAL   A 246 ? 0.1475 0.1514 0.1517 -0.0667 -0.0385 0.0423  246 VAL   A CB  
3797  C  CG1 . VAL   A 246 ? 0.1942 0.1897 0.1929 -0.0685 -0.0427 0.0435  246 VAL   A CG1 
3798  C  CG2 . VAL   A 246 ? 0.1440 0.1400 0.1438 -0.0617 -0.0395 0.0400  246 VAL   A CG2 
3808  N  N   . ASN   A 247 ? 0.1407 0.1680 0.1495 -0.0722 -0.0317 0.0447  247 ASN   A N   
3809  C  CA  . ASN   A 247 ? 0.1685 0.2020 0.1774 -0.0754 -0.0311 0.0464  247 ASN   A CA  
3810  C  C   . ASN   A 247 ? 0.1506 0.1966 0.1676 -0.0730 -0.0272 0.0442  247 ASN   A C   
3811  O  O   . ASN   A 247 ? 0.1453 0.1945 0.1638 -0.0741 -0.0279 0.0442  247 ASN   A O   
3812  C  CB  . ASN   A 247 ? 0.2037 0.2406 0.2078 -0.0802 -0.0307 0.0503  247 ASN   A CB  
3813  C  CG  . ASN   A 247 ? 0.2183 0.2440 0.2197 -0.0830 -0.0354 0.0529  247 ASN   A CG  
3814  O  OD1 . ASN   A 247 ? 0.2383 0.2531 0.2366 -0.0818 -0.0394 0.0521  247 ASN   A OD1 
3815  N  ND2 . ASN   A 247 ? 0.2518 0.2781 0.2453 -0.0860 -0.0349 0.0560  247 ASN   A ND2 
3822  N  N   . ILE   A 248 ? 0.1707 0.2225 0.1874 -0.0699 -0.0232 0.0425  248 ILE   A N   
3823  C  CA  . ILE   A 248 ? 0.1674 0.2302 0.1884 -0.0660 -0.0190 0.0401  248 ILE   A CA  
3824  C  C   . ILE   A 248 ? 0.1447 0.2046 0.1729 -0.0624 -0.0213 0.0375  248 ILE   A C   
3825  O  O   . ILE   A 248 ? 0.1504 0.2173 0.1814 -0.0636 -0.0212 0.0377  248 ILE   A O   
3826  C  CB  . ILE   A 248 ? 0.1438 0.2118 0.1695 -0.0606 -0.0139 0.0376  248 ILE   A CB  
3827  C  CG1 . ILE   A 248 ? 0.1538 0.2264 0.1724 -0.0640 -0.0115 0.0398  248 ILE   A CG1 
3828  C  CG2 . ILE   A 248 ? 0.1752 0.2507 0.2012 -0.0555 -0.0102 0.0351  248 ILE   A CG2 
3829  C  CD1 . ILE   A 248 ? 0.1645 0.2398 0.1812 -0.0593 -0.0069 0.0370  248 ILE   A CD1 
3841  N  N   . ILE   A 249 ? 0.1418 0.1904 0.1656 -0.0584 -0.0234 0.0351  249 ILE   A N   
3842  C  CA  . ILE   A 249 ? 0.1088 0.1550 0.1406 -0.0546 -0.0252 0.0322  249 ILE   A CA  
3843  C  C   . ILE   A 249 ? 0.1305 0.1721 0.1575 -0.0594 -0.0300 0.0337  249 ILE   A C   
3844  O  O   . ILE   A 249 ? 0.1278 0.1737 0.1601 -0.0583 -0.0308 0.0324  249 ILE   A O   
3845  C  CB  . ILE   A 249 ? 0.1348 0.1701 0.1594 -0.0494 -0.0261 0.0292  249 ILE   A CB  
3846  C  CG1 . ILE   A 249 ? 0.1317 0.1702 0.1563 -0.0453 -0.0214 0.0279  249 ILE   A CG1 
3847  C  CG2 . ILE   A 249 ? 0.1334 0.1664 0.1618 -0.0454 -0.0277 0.0267  249 ILE   A CG2 
3848  C  CD1 . ILE   A 249 ? 0.1141 0.1634 0.1437 -0.0422 -0.0169 0.0268  249 ILE   A CD1 
3860  N  N   . ASN   A 250 ? 0.1270 0.1610 0.1513 -0.0637 -0.0333 0.0359  250 ASN   A N   
3861  C  CA  . ASN   A 250 ? 0.1274 0.1564 0.1535 -0.0666 -0.0370 0.0368  250 ASN   A CA  
3862  C  C   . ASN   A 250 ? 0.1902 0.2280 0.2112 -0.0696 -0.0354 0.0382  250 ASN   A C   
3863  O  O   . ASN   A 250 ? 0.1640 0.2023 0.1921 -0.0699 -0.0374 0.0369  250 ASN   A O   
3864  C  CB  . ASN   A 250 ? 0.1439 0.1613 0.1618 -0.0696 -0.0404 0.0391  250 ASN   A CB  
3865  C  CG  . ASN   A 250 ? 0.1867 0.1948 0.1988 -0.0715 -0.0448 0.0391  250 ASN   A CG  
3866  O  OD1 . ASN   A 250 ? 0.1644 0.1675 0.1811 -0.0683 -0.0470 0.0362  250 ASN   A OD1 
3867  N  ND2 . ASN   A 250 ? 0.1975 0.2058 0.2095 -0.0765 -0.0458 0.0424  250 ASN   A ND2 
3874  N  N   . GLU   A 251 ? 0.1927 0.2410 0.2169 -0.0717 -0.0317 0.0405  251 GLU   A N   
3875  C  CA  . GLU   A 251 ? 0.1654 0.2258 0.1970 -0.0747 -0.0299 0.0419  251 GLU   A CA  
3876  C  C   . GLU   A 251 ? 0.1645 0.2325 0.1962 -0.0708 -0.0283 0.0394  251 GLU   A C   
3877  O  O   . GLU   A 251 ? 0.1531 0.2282 0.1902 -0.0729 -0.0284 0.0399  251 GLU   A O   
3878  C  CB  . GLU   A 251 ? 0.2111 0.2809 0.2439 -0.0769 -0.0262 0.0447  251 GLU   A CB  
3879  C  CG  . GLU   A 251 ? 0.3852 0.4474 0.4016 -0.0823 -0.0282 0.0480  251 GLU   A CG  
3880  C  CD  . GLU   A 251 ? 0.4488 0.5189 0.4618 -0.0842 -0.0247 0.0504  251 GLU   A CD  
3881  O  OE1 . GLU   A 251 ? 0.3818 0.4666 0.4079 -0.0823 -0.0203 0.0496  251 GLU   A OE1 
3882  O  OE2 . GLU   A 251 ? 0.4447 0.5102 0.4594 -0.0871 -0.0263 0.0529  251 GLU   A OE2 
3889  N  N   . ASN   A 252 ? 0.1245 0.1940 0.1645 -0.0658 -0.0269 0.0368  252 ASN   A N   
3890  C  CA  . ASN   A 252 ? 0.1494 0.2262 0.1911 -0.0614 -0.0255 0.0347  252 ASN   A CA  
3891  C  C   . ASN   A 252 ? 0.1461 0.2152 0.1893 -0.0602 -0.0298 0.0324  252 ASN   A C   
3892  O  O   . ASN   A 252 ? 0.1718 0.2463 0.2166 -0.0569 -0.0293 0.0307  252 ASN   A O   
3893  C  CB  . ASN   A 252 ? 0.1701 0.2529 0.2156 -0.0562 -0.0215 0.0334  252 ASN   A CB  
3894  C  CG  . ASN   A 252 ? 0.1993 0.2934 0.2442 -0.0558 -0.0165 0.0346  252 ASN   A CG  
3895  O  OD1 . ASN   A 252 ? 0.2331 0.3379 0.2819 -0.0537 -0.0140 0.0345  252 ASN   A OD1 
3896  N  ND2 . ASN   A 252 ? 0.1603 0.2527 0.2051 -0.0571 -0.0147 0.0356  252 ASN   A ND2 
3903  N  N   . GLY   A 253 ? 0.1366 0.1926 0.1753 -0.0624 -0.0339 0.0322  253 GLY   A N   
3904  C  CA  . GLY   A 253 ? 0.1436 0.1911 0.1795 -0.0611 -0.0378 0.0296  253 GLY   A CA  
3905  C  C   . GLY   A 253 ? 0.1239 0.1690 0.1624 -0.0553 -0.0380 0.0267  253 GLY   A C   
3906  O  O   . GLY   A 253 ? 0.1061 0.1509 0.1467 -0.0531 -0.0399 0.0243  253 GLY   A O   
3910  N  N   . VAL   A 254 ? 0.1219 0.1655 0.1596 -0.0527 -0.0361 0.0267  254 VAL   A N   
3911  C  CA  . VAL   A 254 ? 0.1107 0.1510 0.1502 -0.0456 -0.0347 0.0236  254 VAL   A CA  
3912  C  C   . VAL   A 254 ? 0.1183 0.1471 0.1520 -0.0449 -0.0360 0.0231  254 VAL   A C   
3913  O  O   . VAL   A 254 ? 0.1244 0.1517 0.1570 -0.0398 -0.0335 0.0213  254 VAL   A O   
3914  C  CB  . VAL   A 254 ? 0.1281 0.1777 0.1682 -0.0408 -0.0293 0.0232  254 VAL   A CB  
3915  C  CG1 . VAL   A 254 ? 0.1257 0.1848 0.1709 -0.0394 -0.0288 0.0227  254 VAL   A CG1 
3916  C  CG2 . VAL   A 254 ? 0.1325 0.1881 0.1729 -0.0430 -0.0258 0.0254  254 VAL   A CG2 
3926  N  N   . HIS   A 255 ? 0.1257 0.1468 0.1557 -0.0497 -0.0400 0.0248  255 HIS   A N   
3927  C  CA  . HIS   A 255 ? 0.1284 0.1386 0.1545 -0.0490 -0.0417 0.0247  255 HIS   A CA  
3928  C  C   . HIS   A 255 ? 0.1279 0.1283 0.1526 -0.0471 -0.0462 0.0220  255 HIS   A C   
3929  O  O   . HIS   A 255 ? 0.1204 0.1161 0.1438 -0.0494 -0.0492 0.0225  255 HIS   A O   
3930  C  CB  . HIS   A 255 ? 0.1355 0.1430 0.1574 -0.0547 -0.0427 0.0284  255 HIS   A CB  
3931  C  CG  . HIS   A 255 ? 0.1296 0.1278 0.1512 -0.0542 -0.0447 0.0289  255 HIS   A CG  
3932  N  ND1 . HIS   A 255 ? 0.1704 0.1680 0.1844 -0.0516 -0.0422 0.0287  255 HIS   A ND1 
3933  C  CD2 . HIS   A 255 ? 0.1547 0.1410 0.1674 -0.0550 -0.0486 0.0296  255 HIS   A CD2 
3934  C  CE1 . HIS   A 255 ? 0.1566 0.1455 0.1701 -0.0517 -0.0452 0.0293  255 HIS   A CE1 
3935  N  NE2 . HIS   A 255 ? 0.1516 0.1333 0.1636 -0.0536 -0.0490 0.0301  255 HIS   A NE2 
3943  N  N   . PRO   A 256 ? 0.1335 0.1309 0.1590 -0.0408 -0.0457 0.0189  256 PRO   A N   
3944  C  CA  . PRO   A 256 ? 0.1584 0.1475 0.1805 -0.0383 -0.0496 0.0158  256 PRO   A CA  
3945  C  C   . PRO   A 256 ? 0.1656 0.1430 0.1835 -0.0405 -0.0540 0.0165  256 PRO   A C   
3946  O  O   . PRO   A 256 ? 0.1470 0.1208 0.1652 -0.0412 -0.0541 0.0181  256 PRO   A O   
3947  C  CB  . PRO   A 256 ? 0.1418 0.1317 0.1669 -0.0319 -0.0473 0.0132  256 PRO   A CB  
3948  C  CG  . PRO   A 256 ? 0.1366 0.1353 0.1628 -0.0308 -0.0419 0.0144  256 PRO   A CG  
3949  C  CD  . PRO   A 256 ? 0.1300 0.1309 0.1558 -0.0364 -0.0414 0.0180  256 PRO   A CD  
3957  N  N   . VAL   A 257 ? 0.1491 0.1223 0.1685 -0.0407 -0.0568 0.0149  257 VAL   A N   
3958  C  CA  . VAL   A 257 ? 0.1495 0.1115 0.1655 -0.0418 -0.0606 0.0155  257 VAL   A CA  
3959  C  C   . VAL   A 257 ? 0.1599 0.1149 0.1734 -0.0371 -0.0634 0.0113  257 VAL   A C   
3960  O  O   . VAL   A 257 ? 0.1666 0.1261 0.1825 -0.0357 -0.0631 0.0085  257 VAL   A O   
3961  C  CB  . VAL   A 257 ? 0.1676 0.1290 0.1803 -0.0477 -0.0615 0.0185  257 VAL   A CB  
3962  C  CG1 . VAL   A 257 ? 0.1978 0.1471 0.2059 -0.0486 -0.0657 0.0187  257 VAL   A CG1 
3963  C  CG2 . VAL   A 257 ? 0.1453 0.1138 0.1599 -0.0521 -0.0588 0.0225  257 VAL   A CG2 
3973  N  N   . LYS   A 258 ? 0.1524 0.0986 0.1652 -0.0344 -0.0660 0.0105  258 LYS   A N   
3974  C  CA  . LYS   A 258 ? 0.1748 0.1140 0.1847 -0.0296 -0.0688 0.0063  258 LYS   A CA  
3975  C  C   . LYS   A 258 ? 0.1556 0.1020 0.1699 -0.0250 -0.0668 0.0026  258 LYS   A C   
3976  O  O   . LYS   A 258 ? 0.1662 0.1136 0.1801 -0.0238 -0.0674 -0.0003 258 LYS   A O   
3977  C  CB  . LYS   A 258 ? 0.2005 0.1344 0.2091 -0.0319 -0.0718 0.0058  258 LYS   A CB  
3978  C  CG  . LYS   A 258 ? 0.2257 0.1506 0.2308 -0.0350 -0.0749 0.0086  258 LYS   A CG  
3979  C  CD  . LYS   A 258 ? 0.2471 0.1677 0.2536 -0.0381 -0.0776 0.0083  258 LYS   A CD  
3980  C  CE  . LYS   A 258 ? 0.3293 0.2388 0.3274 -0.0402 -0.0812 0.0107  258 LYS   A CE  
3981  N  NZ  . LYS   A 258 ? 0.3725 0.2755 0.3689 -0.0419 -0.0842 0.0090  258 LYS   A NZ  
3995  N  N   . ASN   A 259 ? 0.1381 0.0894 0.1553 -0.0231 -0.0642 0.0026  259 ASN   A N   
3996  C  CA  . ASN   A 259 ? 0.1520 0.1096 0.1714 -0.0183 -0.0625 -0.0004 259 ASN   A CA  
3997  C  C   . ASN   A 259 ? 0.1663 0.1322 0.1838 -0.0198 -0.0604 -0.0006 259 ASN   A C   
3998  O  O   . ASN   A 259 ? 0.1357 0.1063 0.1593 -0.0163 -0.0600 -0.0035 259 ASN   A O   
3999  C  CB  . ASN   A 259 ? 0.1710 0.1230 0.1871 -0.0130 -0.0647 -0.0047 259 ASN   A CB  
4000  C  CG  . ASN   A 259 ? 0.1602 0.1193 0.1798 -0.0075 -0.0618 -0.0073 259 ASN   A CG  
4001  O  OD1 . ASN   A 259 ? 0.1448 0.1085 0.1665 -0.0066 -0.0581 -0.0054 259 ASN   A OD1 
4002  N  ND2 . ASN   A 259 ? 0.1649 0.1248 0.1845 -0.0037 -0.0627 -0.0110 259 ASN   A ND2 
4009  N  N   . PHE   A 260 ? 0.1357 0.1078 0.1591 -0.0247 -0.0587 0.0029  260 PHE   A N   
4010  C  CA  . PHE   A 260 ? 0.1287 0.1110 0.1555 -0.0260 -0.0563 0.0035  260 PHE   A CA  
4011  C  C   . PHE   A 260 ? 0.1482 0.1295 0.1738 -0.0278 -0.0587 0.0020  260 PHE   A C   
4012  O  O   . PHE   A 260 ? 0.1679 0.1574 0.1937 -0.0286 -0.0576 0.0017  260 PHE   A O   
4013  C  CB  . PHE   A 260 ? 0.1403 0.1299 0.1660 -0.0207 -0.0518 0.0023  260 PHE   A CB  
4014  C  CG  . PHE   A 260 ? 0.1187 0.1124 0.1494 -0.0193 -0.0476 0.0042  260 PHE   A CG  
4015  C  CD1 . PHE   A 260 ? 0.1360 0.1234 0.1613 -0.0171 -0.0475 0.0038  260 PHE   A CD1 
4016  C  CD2 . PHE   A 260 ? 0.1335 0.1352 0.1622 -0.0199 -0.0433 0.0064  260 PHE   A CD2 
4017  C  CE1 . PHE   A 260 ? 0.1274 0.1179 0.1552 -0.0161 -0.0438 0.0053  260 PHE   A CE1 
4018  C  CE2 . PHE   A 260 ? 0.1093 0.1144 0.1428 -0.0186 -0.0395 0.0076  260 PHE   A CE2 
4019  C  CZ  . PHE   A 260 ? 0.1394 0.1374 0.1663 -0.0170 -0.0397 0.0069  260 PHE   A CZ  
4029  N  N   . GLN   A 261 ? 0.1693 0.1399 0.1891 -0.0288 -0.0621 0.0008  261 GLN   A N   
4030  C  CA  . GLN   A 261 ? 0.1632 0.1331 0.1863 -0.0308 -0.0644 -0.0005 261 GLN   A CA  
4031  C  C   . GLN   A 261 ? 0.1823 0.1568 0.2046 -0.0371 -0.0635 0.0029  261 GLN   A C   
4032  O  O   . GLN   A 261 ? 0.2054 0.1841 0.2263 -0.0391 -0.0639 0.0019  261 GLN   A O   
4033  C  CB  . GLN   A 261 ? 0.2013 0.1579 0.2156 -0.0297 -0.0682 -0.0028 261 GLN   A CB  
4034  C  CG  . GLN   A 261 ? 0.1953 0.1491 0.2112 -0.0234 -0.0693 -0.0072 261 GLN   A CG  
4035  C  CD  . GLN   A 261 ? 0.1967 0.1391 0.2096 -0.0219 -0.0730 -0.0093 261 GLN   A CD  
4036  O  OE1 . GLN   A 261 ? 0.1964 0.1365 0.2077 -0.0224 -0.0751 -0.0120 261 GLN   A OE1 
4037  N  NE2 . GLN   A 261 ? 0.2110 0.1459 0.2211 -0.0201 -0.0742 -0.0084 261 GLN   A NE2 
4046  N  N   . GLU   A 262 ? 0.2024 0.1755 0.2200 -0.0401 -0.0622 0.0068  262 GLU   A N   
4047  C  CA  . GLU   A 262 ? 0.1597 0.1401 0.1852 -0.0461 -0.0608 0.0106  262 GLU   A CA  
4048  C  C   . GLU   A 262 ? 0.1507 0.1385 0.1741 -0.0461 -0.0568 0.0134  262 GLU   A C   
4049  O  O   . GLU   A 262 ? 0.1473 0.1342 0.1715 -0.0424 -0.0559 0.0125  262 GLU   A O   
4050  C  CB  . GLU   A 262 ? 0.2082 0.1783 0.2244 -0.0502 -0.0633 0.0129  262 GLU   A CB  
4051  C  CG  . GLU   A 262 ? 0.2205 0.1842 0.2398 -0.0510 -0.0670 0.0106  262 GLU   A CG  
4052  C  CD  . GLU   A 262 ? 0.3063 0.2588 0.3161 -0.0548 -0.0698 0.0130  262 GLU   A CD  
4053  O  OE1 . GLU   A 262 ? 0.3142 0.2708 0.3262 -0.0603 -0.0691 0.0165  262 GLU   A OE1 
4054  O  OE2 . GLU   A 262 ? 0.3356 0.2774 0.3435 -0.0522 -0.0728 0.0116  262 GLU   A OE2 
4061  N  N   . SER   A 263 ? 0.1364 0.1327 0.1634 -0.0505 -0.0548 0.0165  263 SER   A N   
4062  C  CA  . SER   A 263 ? 0.1482 0.1535 0.1751 -0.0504 -0.0507 0.0188  263 SER   A CA  
4063  C  C   . SER   A 263 ? 0.1511 0.1579 0.1768 -0.0559 -0.0496 0.0229  263 SER   A C   
4064  O  O   . SER   A 263 ? 0.1212 0.1379 0.1515 -0.0563 -0.0461 0.0250  263 SER   A O   
4065  C  CB  . SER   A 263 ? 0.1295 0.1482 0.1662 -0.0488 -0.0484 0.0179  263 SER   A CB  
4066  O  OG  . SER   A 263 ? 0.1860 0.2019 0.2171 -0.0443 -0.0499 0.0145  263 SER   A OG  
4072  N  N   . TYR   A 264 ? 0.1599 0.1587 0.1847 -0.0590 -0.0525 0.0244  264 TYR   A N   
4073  C  CA  . TYR   A 264 ? 0.2036 0.2027 0.2227 -0.0646 -0.0520 0.0285  264 TYR   A CA  
4074  C  C   . TYR   A 264 ? 0.1936 0.1798 0.2093 -0.0665 -0.0558 0.0297  264 TYR   A C   
4075  O  O   . TYR   A 264 ? 0.1987 0.1773 0.2135 -0.0655 -0.0591 0.0275  264 TYR   A O   
4076  C  CB  . TYR   A 264 ? 0.2151 0.2243 0.2398 -0.0686 -0.0508 0.0297  264 TYR   A CB  
4077  C  CG  . TYR   A 264 ? 0.2516 0.2626 0.2741 -0.0743 -0.0503 0.0340  264 TYR   A CG  
4078  C  CD1 . TYR   A 264 ? 0.3050 0.3073 0.3222 -0.0784 -0.0537 0.0355  264 TYR   A CD1 
4079  C  CD2 . TYR   A 264 ? 0.2510 0.2717 0.2729 -0.0757 -0.0465 0.0366  264 TYR   A CD2 
4080  C  CE1 . TYR   A 264 ? 0.3346 0.3389 0.3505 -0.0838 -0.0535 0.0396  264 TYR   A CE1 
4081  C  CE2 . TYR   A 264 ? 0.2333 0.2580 0.2605 -0.0809 -0.0459 0.0404  264 TYR   A CE2 
4082  C  CZ  . TYR   A 264 ? 0.3531 0.3675 0.3675 -0.0851 -0.0496 0.0422  264 TYR   A CZ  
4083  O  OH  . TYR   A 264 ? 0.4306 0.4475 0.4422 -0.0904 -0.0492 0.0463  264 TYR   A OH  
4093  N  N   . THR   A 265 ? 0.1737 0.1582 0.1891 -0.0689 -0.0557 0.0331  265 THR   A N   
4094  C  CA  . THR   A 265 ? 0.2099 0.1818 0.2167 -0.0711 -0.0594 0.0352  265 THR   A CA  
4095  C  C   . THR   A 265 ? 0.2266 0.2008 0.2282 -0.0768 -0.0588 0.0401  265 THR   A C   
4096  O  O   . THR   A 265 ? 0.2110 0.1939 0.2177 -0.0774 -0.0553 0.0419  265 THR   A O   
4097  C  CB  . THR   A 265 ? 0.2071 0.1698 0.2119 -0.0665 -0.0613 0.0342  265 THR   A CB  
4098  O  OG1 . THR   A 265 ? 0.2032 0.1555 0.2043 -0.0685 -0.0651 0.0362  265 THR   A OG1 
4099  C  CG2 . THR   A 265 ? 0.2009 0.1690 0.2067 -0.0652 -0.0580 0.0351  265 THR   A CG2 
4107  N  N   . ASN   A 266 ? 0.1762 0.1469 0.1828 -0.0810 -0.0617 0.0419  266 ASN   A N   
4108  C  CA  . ASN   A 266 ? 0.1939 0.1669 0.1997 -0.0868 -0.0616 0.0468  266 ASN   A CA  
4109  C  C   . ASN   A 266 ? 0.2424 0.2056 0.2336 -0.0864 -0.0632 0.0493  266 ASN   A C   
4110  O  O   . ASN   A 266 ? 0.2359 0.2014 0.2297 -0.0909 -0.0633 0.0534  266 ASN   A O   
4111  C  CB  . ASN   A 266 ? 0.2713 0.2393 0.2672 -0.0917 -0.0642 0.0479  266 ASN   A CB  
4112  C  CG  . ASN   A 266 ? 0.2646 0.2195 0.2636 -0.0905 -0.0692 0.0461  266 ASN   A CG  
4113  O  OD1 . ASN   A 266 ? 0.2539 0.1995 0.2495 -0.0868 -0.0713 0.0454  266 ASN   A OD1 
4114  N  ND2 . ASN   A 266 ? 0.2962 0.2488 0.2932 -0.0935 -0.0712 0.0452  266 ASN   A ND2 
4121  N  N   . GLN   A 267 ? 0.2011 0.1592 0.1998 -0.0812 -0.0645 0.0472  267 GLN   A N   
4122  C  CA  . GLN   A 267 ? 0.2419 0.1918 0.2301 -0.0800 -0.0662 0.0490  267 GLN   A CA  
4123  C  C   . GLN   A 267 ? 0.2052 0.1629 0.1985 -0.0781 -0.0627 0.0491  267 GLN   A C   
4124  O  O   . GLN   A 267 ? 0.2156 0.1681 0.2032 -0.0769 -0.0639 0.0507  267 GLN   A O   
4125  C  CB  . GLN   A 267 ? 0.2619 0.1990 0.2492 -0.0757 -0.0707 0.0466  267 GLN   A CB  
4126  C  CG  . GLN   A 267 ? 0.2421 0.1719 0.2323 -0.0779 -0.0746 0.0465  267 GLN   A CG  
4127  C  CD  . GLN   A 267 ? 0.2673 0.1939 0.2480 -0.0841 -0.0762 0.0512  267 GLN   A CD  
4128  O  OE1 . GLN   A 267 ? 0.2354 0.1587 0.2181 -0.0848 -0.0778 0.0542  267 GLN   A OE1 
4129  N  NE2 . GLN   A 267 ? 0.2409 0.1725 0.2280 -0.0890 -0.0757 0.0523  267 GLN   A NE2 
4138  N  N   . ALA   A 268 ? 0.1958 0.1645 0.1929 -0.0771 -0.0583 0.0476  268 ALA   A N   
4139  C  CA  . ALA   A 268 ? 0.2246 0.1977 0.2168 -0.0743 -0.0550 0.0466  268 ALA   A CA  
4140  C  C   . ALA   A 268 ? 0.1980 0.1754 0.1936 -0.0773 -0.0536 0.0504  268 ALA   A C   
4141  O  O   . ALA   A 268 ? 0.1929 0.1687 0.1845 -0.0750 -0.0530 0.0498  268 ALA   A O   
4142  C  CB  . ALA   A 268 ? 0.1906 0.1766 0.1939 -0.0732 -0.0506 0.0444  268 ALA   A CB  
4148  N  N   . ASP   A 269 ? 0.2355 0.2155 0.2234 -0.0825 -0.0534 0.0541  269 ASP   A N   
4149  C  CA  . ASP   A 269 ? 0.2122 0.1978 0.2021 -0.0855 -0.0518 0.0576  269 ASP   A CA  
4150  C  C   . ASP   A 269 ? 0.2078 0.1827 0.1912 -0.0848 -0.0555 0.0591  269 ASP   A C   
4151  O  O   . ASP   A 269 ? 0.2441 0.2214 0.2218 -0.0857 -0.0543 0.0610  269 ASP   A O   
4152  C  CB  . ASP   A 269 ? 0.2480 0.2400 0.2339 -0.0914 -0.0507 0.0611  269 ASP   A CB  
4153  C  CG  . ASP   A 269 ? 0.2731 0.2715 0.2554 -0.0942 -0.0484 0.0643  269 ASP   A CG  
4154  O  OD1 . ASP   A 269 ? 0.2741 0.2807 0.2583 -0.0923 -0.0442 0.0630  269 ASP   A OD1 
4155  O  OD2 . ASP   A 269 ? 0.2819 0.2773 0.2608 -0.0983 -0.0508 0.0679  269 ASP   A OD2 
4160  N  N   . LYS   A 270 ? 0.1857 0.1487 0.1680 -0.0829 -0.0603 0.0583  270 LYS   A N   
4161  C  CA  . LYS   A 270 ? 0.1838 0.1374 0.1635 -0.0808 -0.0639 0.0589  270 LYS   A CA  
4162  C  C   . LYS   A 270 ? 0.1864 0.1404 0.1657 -0.0766 -0.0626 0.0570  270 LYS   A C   
4163  O  O   . LYS   A 270 ? 0.1970 0.1462 0.1710 -0.0760 -0.0645 0.0584  270 LYS   A O   
4164  C  CB  . LYS   A 270 ? 0.2215 0.1622 0.1977 -0.0794 -0.0691 0.0582  270 LYS   A CB  
4165  C  CG  . LYS   A 270 ? 0.2413 0.1787 0.2164 -0.0842 -0.0715 0.0607  270 LYS   A CG  
4166  C  CD  . LYS   A 270 ? 0.2492 0.1741 0.2226 -0.0822 -0.0765 0.0593  270 LYS   A CD  
4167  C  CE  . LYS   A 270 ? 0.2269 0.1425 0.2005 -0.0802 -0.0807 0.0606  270 LYS   A CE  
4168  N  NZ  . LYS   A 270 ? 0.2539 0.1574 0.2225 -0.0800 -0.0853 0.0602  270 LYS   A NZ  
4182  N  N   . ILE   A 271 ? 0.2061 0.1646 0.1859 -0.0735 -0.0593 0.0534  271 ILE   A N   
4183  C  CA  . ILE   A 271 ? 0.1806 0.1409 0.1661 -0.0696 -0.0579 0.0510  271 ILE   A CA  
4184  C  C   . ILE   A 271 ? 0.1808 0.1522 0.1634 -0.0705 -0.0522 0.0506  271 ILE   A C   
4185  O  O   . ILE   A 271 ? 0.1692 0.1437 0.1574 -0.0671 -0.0501 0.0476  271 ILE   A O   
4186  C  CB  . ILE   A 271 ? 0.2051 0.1591 0.1929 -0.0638 -0.0598 0.0466  271 ILE   A CB  
4187  C  CG1 . ILE   A 271 ? 0.2175 0.1763 0.2085 -0.0630 -0.0574 0.0435  271 ILE   A CG1 
4188  C  CG2 . ILE   A 271 ? 0.2521 0.1937 0.2338 -0.0622 -0.0652 0.0467  271 ILE   A CG2 
4189  C  CD1 . ILE   A 271 ? 0.2304 0.1845 0.2238 -0.0574 -0.0589 0.0391  271 ILE   A CD1 
4201  N  N   . SER   A 272 ? 0.1449 0.1271 0.1315 -0.0717 -0.0487 0.0516  272 SER   A N   
4202  C  CA  . SER   A 272 ? 0.1738 0.1663 0.1596 -0.0759 -0.0440 0.0529  272 SER   A CA  
4203  C  C   . SER   A 272 ? 0.1993 0.1937 0.1785 -0.0767 -0.0422 0.0542  272 SER   A C   
4204  O  O   . SER   A 272 ? 0.1850 0.1742 0.1628 -0.0777 -0.0452 0.0568  272 SER   A O   
4205  C  CB  . SER   A 272 ? 0.1768 0.1782 0.1639 -0.0803 -0.0418 0.0551  272 SER   A CB  
4206  O  OG  . SER   A 272 ? 0.1897 0.1904 0.1713 -0.0845 -0.0432 0.0591  272 SER   A OG  
4212  N  N   . GLY   A 273 ? 0.1816 0.1862 0.1648 -0.0752 -0.0370 0.0521  273 GLY   A N   
4213  C  CA  . GLY   A 273 ? 0.1565 0.1664 0.1388 -0.0750 -0.0345 0.0523  273 GLY   A CA  
4214  C  C   . GLY   A 273 ? 0.1939 0.2067 0.1665 -0.0816 -0.0342 0.0576  273 GLY   A C   
4215  O  O   . GLY   A 273 ? 0.1886 0.2008 0.1582 -0.0829 -0.0350 0.0597  273 GLY   A O   
4219  N  N   . GLU   A 274 ? 0.1905 0.2085 0.1668 -0.0841 -0.0339 0.0591  274 GLU   A N   
4220  C  CA  . GLU   A 274 ? 0.1812 0.2043 0.1594 -0.0889 -0.0340 0.0630  274 GLU   A CA  
4221  C  C   . GLU   A 274 ? 0.2130 0.2227 0.1780 -0.0905 -0.0398 0.0660  274 GLU   A C   
4222  O  O   . GLU   A 274 ? 0.2091 0.2210 0.1726 -0.0930 -0.0401 0.0689  274 GLU   A O   
4223  C  CB  . GLU   A 274 ? 0.2461 0.2744 0.2188 -0.0913 -0.0325 0.0636  274 GLU   A CB  
4224  C  CG  . GLU   A 274 ? 0.2297 0.2728 0.2136 -0.0899 -0.0266 0.0611  274 GLU   A CG  
4225  C  CD  . GLU   A 274 ? 0.2761 0.3178 0.2580 -0.0859 -0.0255 0.0573  274 GLU   A CD  
4226  O  OE1 . GLU   A 274 ? 0.2271 0.2600 0.2175 -0.0836 -0.0291 0.0560  274 GLU   A OE1 
4227  O  OE2 . GLU   A 274 ? 0.2632 0.3172 0.2548 -0.0847 -0.0211 0.0556  274 GLU   A OE2 
4234  N  N   . THR   A 275 ? 0.1820 0.1822 0.1547 -0.0887 -0.0443 0.0655  275 THR   A N   
4235  C  CA  . THR   A 275 ? 0.2167 0.2042 0.1812 -0.0894 -0.0500 0.0678  275 THR   A CA  
4236  C  C   . THR   A 275 ? 0.1913 0.1759 0.1571 -0.0870 -0.0510 0.0678  275 THR   A C   
4237  O  O   . THR   A 275 ? 0.2275 0.2075 0.1837 -0.0890 -0.0535 0.0711  275 THR   A O   
4238  C  CB  . THR   A 275 ? 0.2418 0.2186 0.2064 -0.0876 -0.0542 0.0666  275 THR   A CB  
4239  O  OG1 . THR   A 275 ? 0.2127 0.1954 0.1853 -0.0904 -0.0531 0.0669  275 THR   A OG1 
4240  C  CG2 . THR   A 275 ? 0.2128 0.1789 0.1796 -0.0875 -0.0599 0.0685  275 THR   A CG2 
4248  N  N   . LEU   A 276 ? 0.1981 0.1826 0.1622 -0.0828 -0.0492 0.0643  276 LEU   A N   
4249  C  CA  . LEU   A 276 ? 0.2020 0.1828 0.1619 -0.0803 -0.0501 0.0638  276 LEU   A CA  
4250  C  C   . LEU   A 276 ? 0.1965 0.1859 0.1540 -0.0834 -0.0473 0.0664  276 LEU   A C   
4251  O  O   . LEU   A 276 ? 0.2082 0.1931 0.1588 -0.0834 -0.0504 0.0684  276 LEU   A O   
4252  C  CB  . LEU   A 276 ? 0.1828 0.1654 0.1503 -0.0751 -0.0478 0.0589  276 LEU   A CB  
4253  C  CG  . LEU   A 276 ? 0.2210 0.1993 0.1789 -0.0703 -0.0488 0.0561  276 LEU   A CG  
4254  C  CD1 . LEU   A 276 ? 0.2107 0.1783 0.1728 -0.0688 -0.0550 0.0578  276 LEU   A CD1 
4255  C  CD2 . LEU   A 276 ? 0.1575 0.1419 0.1281 -0.0646 -0.0453 0.0497  276 LEU   A CD2 
4267  N  N   . THR   A 277 ? 0.2144 0.2151 0.1705 -0.0852 -0.0419 0.0657  277 THR   A N   
4268  C  CA  . THR   A 277 ? 0.2228 0.2325 0.1729 -0.0876 -0.0386 0.0671  277 THR   A CA  
4269  C  C   . THR   A 277 ? 0.2040 0.2133 0.1555 -0.0918 -0.0416 0.0716  277 THR   A C   
4270  O  O   . THR   A 277 ? 0.2322 0.2427 0.1739 -0.0929 -0.0415 0.0732  277 THR   A O   
4271  C  CB  . THR   A 277 ? 0.2126 0.2365 0.1710 -0.0882 -0.0321 0.0648  277 THR   A CB  
4272  O  OG1 . THR   A 277 ? 0.2352 0.2591 0.1918 -0.0827 -0.0295 0.0593  277 THR   A OG1 
4273  C  CG2 . THR   A 277 ? 0.2646 0.2973 0.2120 -0.0907 -0.0287 0.0660  277 THR   A CG2 
4281  N  N   . ALA   A 278 ? 0.2266 0.2315 0.1770 -0.0940 -0.0440 0.0736  278 ALA   A N   
4282  C  CA  . ALA   A 278 ? 0.2535 0.2573 0.2017 -0.0985 -0.0467 0.0782  278 ALA   A CA  
4283  C  C   . ALA   A 278 ? 0.2763 0.2669 0.2183 -0.0975 -0.0525 0.0802  278 ALA   A C   
4284  O  O   . ALA   A 278 ? 0.2766 0.2659 0.2174 -0.1009 -0.0548 0.0841  278 ALA   A O   
4285  C  CB  . ALA   A 278 ? 0.2749 0.2796 0.2242 -0.1016 -0.0469 0.0794  278 ALA   A CB  
4291  N  N   . ASN   A 279 ? 0.2525 0.2359 0.2001 -0.0928 -0.0549 0.0776  279 ASN   A N   
4292  C  CA  . ASN   A 279 ? 0.2740 0.2449 0.2184 -0.0911 -0.0606 0.0789  279 ASN   A CA  
4293  C  C   . ASN   A 279 ? 0.3189 0.2853 0.2526 -0.0865 -0.0616 0.0772  279 ASN   A C   
4294  O  O   . ASN   A 279 ? 0.2895 0.2607 0.2282 -0.0875 -0.0616 0.0793  279 ASN   A O   
4295  C  CB  . ASN   A 279 ? 0.2634 0.2254 0.2146 -0.0895 -0.0644 0.0779  279 ASN   A CB  
4296  C  CG  . ASN   A 279 ? 0.3313 0.2920 0.2739 -0.0941 -0.0648 0.0803  279 ASN   A CG  
4297  O  OD1 . ASN   A 279 ? 0.3116 0.2692 0.2582 -0.0972 -0.0677 0.0840  279 ASN   A OD1 
4298  N  ND2 . ASN   A 279 ? 0.2999 0.2684 0.2535 -0.0949 -0.0617 0.0784  279 ASN   A ND2 
4305  N  N   . GLN   A 280 ? 0.2253 0.1902 0.1758 -0.0818 -0.0622 0.0734  280 GLN   A N   
4306  C  CA  . GLN   A 280 ? 0.2467 0.2070 0.1904 -0.0770 -0.0641 0.0714  280 GLN   A CA  
4307  C  C   . GLN   A 280 ? 0.2713 0.2398 0.2067 -0.0763 -0.0597 0.0696  280 GLN   A C   
4308  O  O   . GLN   A 280 ? 0.2134 0.1824 0.1555 -0.0729 -0.0612 0.0682  280 GLN   A O   
4309  C  CB  . GLN   A 280 ? 0.2385 0.1906 0.1881 -0.0720 -0.0667 0.0682  280 GLN   A CB  
4310  C  CG  . GLN   A 280 ? 0.2619 0.2040 0.2114 -0.0719 -0.0712 0.0690  280 GLN   A CG  
4311  C  CD  . GLN   A 280 ? 0.2714 0.2134 0.2225 -0.0739 -0.0702 0.0682  280 GLN   A CD  
4312  O  OE1 . GLN   A 280 ? 0.2285 0.1802 0.1852 -0.0767 -0.0659 0.0682  280 GLN   A OE1 
4313  N  NE2 . GLN   A 280 ? 0.2690 0.2028 0.2249 -0.0722 -0.0738 0.0673  280 GLN   A NE2 
4322  N  N   . LEU   A 281 ? 0.2286 0.2085 0.1728 -0.0790 -0.0545 0.0692  281 LEU   A N   
4323  C  CA  . LEU   A 281 ? 0.2410 0.2291 0.1788 -0.0775 -0.0500 0.0659  281 LEU   A CA  
4324  C  C   . LEU   A 281 ? 0.2168 0.2096 0.1531 -0.0793 -0.0505 0.0681  281 LEU   A C   
4325  O  O   . LEU   A 281 ? 0.2469 0.2415 0.1761 -0.0834 -0.0502 0.0716  281 LEU   A O   
4326  C  CB  . LEU   A 281 ? 0.2342 0.2327 0.1761 -0.0790 -0.0438 0.0635  281 LEU   A CB  
4327  C  CG  . LEU   A 281 ? 0.2059 0.2131 0.1477 -0.0759 -0.0386 0.0577  281 LEU   A CG  
4328  C  CD1 . LEU   A 281 ? 0.1741 0.1783 0.1243 -0.0696 -0.0386 0.0518  281 LEU   A CD1 
4329  C  CD2 . LEU   A 281 ? 0.1656 0.1844 0.1126 -0.0780 -0.0328 0.0568  281 LEU   A CD2 
4341  N  N   . VAL   A 282 ? 0.2351 0.2280 0.1636 -0.0754 -0.0506 0.0646  282 VAL   A N   
4342  C  CA  . VAL   A 282 ? 0.1974 0.1960 0.1243 -0.0769 -0.0509 0.0659  282 VAL   A CA  
4343  C  C   . VAL   A 282 ? 0.1774 0.1880 0.1056 -0.0772 -0.0442 0.0615  282 VAL   A C   
4344  O  O   . VAL   A 282 ? 0.2191 0.2351 0.1346 -0.0811 -0.0426 0.0646  282 VAL   A O   
4345  C  CB  . VAL   A 282 ? 0.2342 0.2271 0.1580 -0.0728 -0.0552 0.0647  282 VAL   A CB  
4346  C  CG1 . VAL   A 282 ? 0.2573 0.2559 0.1739 -0.0735 -0.0546 0.0645  282 VAL   A CG1 
4347  C  CG2 . VAL   A 282 ? 0.2635 0.2452 0.1882 -0.0709 -0.0605 0.0670  282 VAL   A CG2 
4357  N  N   . ARG   A 283 ? 0.2134 0.2245 0.1386 -0.0732 -0.0410 0.0552  283 ARG   A N   
4358  C  CA  . ARG   A 283 ? 0.1821 0.2048 0.1156 -0.0726 -0.0349 0.0502  283 ARG   A CA  
4359  C  C   . ARG   A 283 ? 0.2231 0.2432 0.1533 -0.0680 -0.0318 0.0439  283 ARG   A C   
4360  O  O   . ARG   A 283 ? 0.1930 0.2074 0.1351 -0.0650 -0.0347 0.0432  283 ARG   A O   
4361  C  CB  . ARG   A 283 ? 0.2167 0.2413 0.1377 -0.0722 -0.0351 0.0483  283 ARG   A CB  
4362  C  CG  . ARG   A 283 ? 0.2151 0.2342 0.1406 -0.0683 -0.0394 0.0460  283 ARG   A CG  
4363  C  CD  . ARG   A 283 ? 0.2529 0.2752 0.1705 -0.0669 -0.0381 0.0414  283 ARG   A CD  
4364  N  NE  . ARG   A 283 ? 0.2209 0.2397 0.1464 -0.0636 -0.0426 0.0397  283 ARG   A NE  
4365  C  CZ  . ARG   A 283 ? 0.2504 0.2657 0.1761 -0.0596 -0.0419 0.0344  283 ARG   A CZ  
4366  N  NH1 . ARG   A 283 ? 0.1866 0.2045 0.1227 -0.0580 -0.0373 0.0304  283 ARG   A NH1 
4367  N  NH2 . ARG   A 283 ? 0.2893 0.3015 0.2168 -0.0571 -0.0462 0.0335  283 ARG   A NH2 
4381  N  N   . LYS   A 284 ? 0.1795 0.2093 0.1205 -0.0669 -0.0262 0.0393  284 LYS   A N   
4382  C  CA  . LYS   A 284 ? 0.2218 0.2491 0.1589 -0.0622 -0.0232 0.0332  284 LYS   A CA  
4383  C  C   . LYS   A 284 ? 0.1693 0.1948 0.1173 -0.0591 -0.0256 0.0298  284 LYS   A C   
4384  O  O   . LYS   A 284 ? 0.2183 0.2427 0.1532 -0.0605 -0.0277 0.0304  284 LYS   A O   
4385  C  CB  . LYS   A 284 ? 0.2053 0.2433 0.1529 -0.0619 -0.0169 0.0297  284 LYS   A CB  
4386  C  CG  . LYS   A 284 ? 0.2803 0.3224 0.2183 -0.0651 -0.0141 0.0330  284 LYS   A CG  
4387  C  CD  . LYS   A 284 ? 0.2416 0.2948 0.1897 -0.0637 -0.0079 0.0291  284 LYS   A CD  
4388  C  CE  . LYS   A 284 ? 0.2944 0.3521 0.2329 -0.0640 -0.0055 0.0262  284 LYS   A CE  
4389  N  NZ  . LYS   A 284 ? 0.3606 0.4279 0.2937 -0.0648 0.0001  0.0248  284 LYS   A NZ  
4403  N  N   . ASN   A 285 ? 0.1590 0.1760 0.1258 -0.0624 -0.0477 0.0427  285 ASN   A N   
4404  C  CA  . ASN   A 285 ? 0.1713 0.1881 0.1454 -0.0579 -0.0500 0.0401  285 ASN   A CA  
4405  C  C   . ASN   A 285 ? 0.1833 0.2034 0.1590 -0.0564 -0.0467 0.0349  285 ASN   A C   
4406  O  O   . ASN   A 285 ? 0.1819 0.2009 0.1669 -0.0535 -0.0455 0.0333  285 ASN   A O   
4407  C  CB  . ASN   A 285 ? 0.2037 0.2147 0.1788 -0.0549 -0.0523 0.0418  285 ASN   A CB  
4408  C  CG  . ASN   A 285 ? 0.1844 0.1972 0.1669 -0.0510 -0.0549 0.0393  285 ASN   A CG  
4409  O  OD1 . ASN   A 285 ? 0.1832 0.1983 0.1610 -0.0505 -0.0567 0.0380  285 ASN   A OD1 
4410  N  ND2 . ASN   A 285 ? 0.1826 0.1942 0.1718 -0.0482 -0.0548 0.0380  285 ASN   A ND2 
4417  N  N   . PRO   A 286 ? 0.1534 0.1792 0.1300 -0.0580 -0.0453 0.0319  286 PRO   A N   
4418  C  CA  . PRO   A 286 ? 0.1528 0.1806 0.1313 -0.0566 -0.0425 0.0270  286 PRO   A CA  
4419  C  C   . PRO   A 286 ? 0.1371 0.1639 0.1225 -0.0537 -0.0434 0.0235  286 PRO   A C   
4420  O  O   . PRO   A 286 ? 0.1360 0.1628 0.1191 -0.0532 -0.0459 0.0227  286 PRO   A O   
4421  C  CB  . PRO   A 286 ? 0.1681 0.2012 0.1395 -0.0593 -0.0416 0.0249  286 PRO   A CB  
4422  C  CG  . PRO   A 286 ? 0.1695 0.2029 0.1338 -0.0627 -0.0426 0.0295  286 PRO   A CG  
4423  C  CD  . PRO   A 286 ? 0.1756 0.2031 0.1390 -0.0609 -0.0461 0.0330  286 PRO   A CD  
4431  N  N   . CYS   A 287 ? 0.1465 0.1716 0.1368 -0.0521 -0.0409 0.0211  287 CYS   A N   
4432  C  CA  . CYS   A 287 ? 0.1594 0.1827 0.1522 -0.0506 -0.0411 0.0174  287 CYS   A CA  
4433  C  C   . CYS   A 287 ? 0.1310 0.1582 0.1267 -0.0524 -0.0417 0.0133  287 CYS   A C   
4434  O  O   . CYS   A 287 ? 0.1465 0.1758 0.1318 -0.0539 -0.0417 0.0129  287 CYS   A O   
4435  C  CB  . CYS   A 287 ? 0.1620 0.1826 0.1606 -0.0491 -0.0387 0.0165  287 CYS   A CB  
4436  S  SG  . CYS   A 287 ? 0.1422 0.1600 0.1460 -0.0460 -0.0365 0.0193  287 CYS   A SG  
4441  N  N   . TYR   A 288 ? 0.1748 0.1992 0.1668 -0.0523 -0.0419 0.0092  288 TYR   A N   
4442  C  CA  . TYR   A 288 ? 0.1584 0.1846 0.1515 -0.0540 -0.0424 0.0042  288 TYR   A CA  
4443  C  C   . TYR   A 288 ? 0.1492 0.1755 0.1389 -0.0552 -0.0407 0.0022  288 TYR   A C   
4444  O  O   . TYR   A 288 ? 0.1365 0.1599 0.1287 -0.0545 -0.0389 0.0031  288 TYR   A O   
4445  C  CB  . TYR   A 288 ? 0.1582 0.1816 0.1562 -0.0546 -0.0421 0.0004  288 TYR   A CB  
4446  C  CG  . TYR   A 288 ? 0.1609 0.1848 0.1569 -0.0566 -0.0433 -0.0055 288 TYR   A CG  
4447  C  CD1 . TYR   A 288 ? 0.1692 0.1975 0.1637 -0.0568 -0.0462 -0.0075 288 TYR   A CD1 
4448  C  CD2 . TYR   A 288 ? 0.1561 0.1762 0.1541 -0.0585 -0.0415 -0.0093 288 TYR   A CD2 
4449  C  CE1 . TYR   A 288 ? 0.1731 0.2023 0.1671 -0.0588 -0.0471 -0.0132 288 TYR   A CE1 
4450  C  CE2 . TYR   A 288 ? 0.2222 0.2399 0.2104 -0.0605 -0.0422 -0.0152 288 TYR   A CE2 
4451  C  CZ  . TYR   A 288 ? 0.2066 0.2301 0.1966 -0.0607 -0.0449 -0.0174 288 TYR   A CZ  
4452  O  OH  . TYR   A 288 ? 0.2028 0.2260 0.1916 -0.0626 -0.0456 -0.0237 288 TYR   A OH  
4462  N  N   . SER   A 289 ? 0.1736 0.2033 0.1560 -0.0568 -0.0414 -0.0010 289 SER   A N   
4463  C  CA  . SER   A 289 ? 0.1998 0.2286 0.1750 -0.0556 -0.0384 -0.0044 289 SER   A CA  
4464  C  C   . SER   A 289 ? 0.1557 0.1873 0.1398 -0.0536 -0.0355 -0.0012 289 SER   A C   
4465  O  O   . SER   A 289 ? 0.1739 0.2024 0.1549 -0.0506 -0.0328 -0.0037 289 SER   A O   
4466  C  CB  . SER   A 289 ? 0.1881 0.2118 0.1700 -0.0549 -0.0369 -0.0095 289 SER   A CB  
4467  O  OG  . SER   A 289 ? 0.1961 0.2194 0.1729 -0.0528 -0.0346 -0.0142 289 SER   A OG  
4473  N  N   . CYS   A 290 ? 0.1731 0.2075 0.1525 -0.0548 -0.0364 0.0040  290 CYS   A N   
4474  C  CA  . CYS   A 290 ? 0.1841 0.2197 0.1631 -0.0536 -0.0340 0.0068  290 CYS   A CA  
4475  C  C   . CYS   A 290 ? 0.1750 0.2184 0.1525 -0.0552 -0.0321 0.0076  290 CYS   A C   
4476  O  O   . CYS   A 290 ? 0.1920 0.2361 0.1634 -0.0582 -0.0338 0.0110  290 CYS   A O   
4477  C  CB  . CYS   A 290 ? 0.1455 0.1801 0.1351 -0.0541 -0.0355 0.0116  290 CYS   A CB  
4478  S  SG  . CYS   A 290 ? 0.1757 0.2110 0.1637 -0.0521 -0.0323 0.0135  290 CYS   A SG  
4483  N  N   . PRO   A 291 ? 0.1693 0.2174 0.1476 -0.0535 -0.0286 0.0047  291 PRO   A N   
4484  C  CA  . PRO   A 291 ? 0.1812 0.2367 0.1545 -0.0556 -0.0258 0.0053  291 PRO   A CA  
4485  C  C   . PRO   A 291 ? 0.1964 0.2536 0.1697 -0.0574 -0.0249 0.0096  291 PRO   A C   
4486  O  O   . PRO   A 291 ? 0.1717 0.2356 0.1458 -0.0605 -0.0225 0.0107  291 PRO   A O   
4487  C  CB  . PRO   A 291 ? 0.1834 0.2436 0.1583 -0.0521 -0.0227 -0.0007 291 PRO   A CB  
4488  C  CG  . PRO   A 291 ? 0.2069 0.2603 0.1845 -0.0479 -0.0233 -0.0019 291 PRO   A CG  
4489  C  CD  . PRO   A 291 ? 0.1834 0.2291 0.1645 -0.0491 -0.0267 0.0006  291 PRO   A CD  
4497  N  N   . ILE   A 292 ? 0.1818 0.2350 0.1640 -0.0559 -0.0265 0.0117  292 ILE   A N   
4498  C  CA  . ILE   A 292 ? 0.1720 0.2267 0.1576 -0.0573 -0.0259 0.0151  292 ILE   A CA  
4499  C  C   . ILE   A 292 ? 0.1750 0.2258 0.1590 -0.0612 -0.0281 0.0206  292 ILE   A C   
4500  O  O   . ILE   A 292 ? 0.2099 0.2628 0.1884 -0.0649 -0.0265 0.0231  292 ILE   A O   
4501  C  CB  . ILE   A 292 ? 0.1534 0.2053 0.1455 -0.0533 -0.0263 0.0143  292 ILE   A CB  
4502  C  CG1 . ILE   A 292 ? 0.1501 0.2046 0.1458 -0.0486 -0.0246 0.0094  292 ILE   A CG1 
4503  C  CG2 . ILE   A 292 ? 0.1199 0.1743 0.1181 -0.0550 -0.0261 0.0170  292 ILE   A CG2 
4504  C  CD1 . ILE   A 292 ? 0.1595 0.2094 0.1587 -0.0441 -0.0252 0.0090  292 ILE   A CD1 
4516  N  N   . GLY   A 293 ? 0.1743 0.2181 0.1561 -0.0604 -0.0317 0.0224  293 GLY   A N   
4517  C  CA  . GLY   A 293 ? 0.1656 0.2048 0.1444 -0.0629 -0.0343 0.0271  293 GLY   A CA  
4518  C  C   . GLY   A 293 ? 0.1514 0.1878 0.1350 -0.0631 -0.0338 0.0307  293 GLY   A C   
4519  O  O   . GLY   A 293 ? 0.1753 0.2099 0.1511 -0.0675 -0.0345 0.0345  293 GLY   A O   
4523  N  N   . CYS   A 294 ? 0.1598 0.1936 0.1479 -0.0590 -0.0325 0.0293  294 CYS   A N   
4524  C  CA  . CYS   A 294 ? 0.1730 0.2029 0.1611 -0.0581 -0.0321 0.0314  294 CYS   A CA  
4525  C  C   . CYS   A 294 ? 0.1478 0.1714 0.1400 -0.0576 -0.0353 0.0349  294 CYS   A C   
4526  O  O   . CYS   A 294 ? 0.1784 0.1976 0.1654 -0.0582 -0.0357 0.0372  294 CYS   A O   
4527  C  CB  . CYS   A 294 ? 0.1668 0.1977 0.1625 -0.0541 -0.0305 0.0286  294 CYS   A CB  
4528  S  SG  . CYS   A 294 ? 0.1469 0.1716 0.1479 -0.0484 -0.0311 0.0271  294 CYS   A SG  
4533  N  N   . GLY   A 295 ? 0.1615 0.1827 0.1503 -0.0562 -0.0375 0.0348  295 GLY   A N   
4534  C  CA  . GLY   A 295 ? 0.1873 0.2024 0.1734 -0.0554 -0.0409 0.0375  295 GLY   A CA  
4535  C  C   . GLY   A 295 ? 0.1681 0.1812 0.1538 -0.0595 -0.0437 0.0426  295 GLY   A C   
4536  O  O   . GLY   A 295 ? 0.1899 0.2050 0.1660 -0.0641 -0.0437 0.0439  295 GLY   A O   
4540  N  N   . ARG   A 296 ? 0.1820 0.1883 0.1650 -0.0585 -0.0464 0.0452  296 ARG   A N   
4541  C  CA  . ARG   A 296 ? 0.1724 0.1737 0.1525 -0.0630 -0.0497 0.0502  296 ARG   A CA  
4542  C  C   . ARG   A 296 ? 0.1677 0.1642 0.1459 -0.0601 -0.0538 0.0520  296 ARG   A C   
4543  O  O   . ARG   A 296 ? 0.1727 0.1690 0.1553 -0.0557 -0.0552 0.0500  296 ARG   A O   
4544  C  CB  . ARG   A 296 ? 0.1844 0.1817 0.1647 -0.0607 -0.0481 0.0493  296 ARG   A CB  
4545  C  CG  . ARG   A 296 ? 0.1569 0.1599 0.1432 -0.0599 -0.0430 0.0456  296 ARG   A CG  
4546  C  CD  . ARG   A 296 ? 0.1577 0.1637 0.1384 -0.0642 -0.0398 0.0456  296 ARG   A CD  
4547  N  NE  . ARG   A 296 ? 0.1607 0.1736 0.1415 -0.0661 -0.0382 0.0444  296 ARG   A NE  
4548  C  CZ  . ARG   A 296 ? 0.2109 0.2267 0.1799 -0.0704 -0.0355 0.0446  296 ARG   A CZ  
4549  N  NH1 . ARG   A 296 ? 0.1879 0.2028 0.1598 -0.0735 -0.0339 0.0459  296 ARG   A NH1 
4550  N  NH2 . ARG   A 296 ? 0.1782 0.2019 0.1528 -0.0719 -0.0345 0.0429  296 ARG   A NH2 
4564  N  N   . TRP   A 297 ? 0.1841 0.1759 0.1523 -0.0611 -0.0543 0.0547  297 TRP   A N   
4565  C  CA  . TRP   A 297 ? 0.1928 0.1791 0.1570 -0.0573 -0.0583 0.0563  297 TRP   A CA  
4566  C  C   . TRP   A 297 ? 0.1729 0.1510 0.1375 -0.0584 -0.0582 0.0597  297 TRP   A C   
4567  O  O   . TRP   A 297 ? 0.1888 0.1646 0.1410 -0.0623 -0.0552 0.0612  297 TRP   A O   
4568  C  CB  . TRP   A 297 ? 0.2081 0.1975 0.1657 -0.0567 -0.0593 0.0559  297 TRP   A CB  
4569  C  CG  . TRP   A 297 ? 0.1902 0.1786 0.1541 -0.0514 -0.0638 0.0563  297 TRP   A CG  
4570  C  CD1 . TRP   A 297 ? 0.2479 0.2285 0.1951 -0.0498 -0.0661 0.0595  297 TRP   A CD1 
4571  C  CD2 . TRP   A 297 ? 0.2393 0.2307 0.2055 -0.0466 -0.0663 0.0529  297 TRP   A CD2 
4572  N  NE1 . TRP   A 297 ? 0.2570 0.2390 0.2095 -0.0439 -0.0705 0.0583  297 TRP   A NE1 
4573  C  CE2 . TRP   A 297 ? 0.2827 0.2708 0.2427 -0.0421 -0.0707 0.0541  297 TRP   A CE2 
4574  C  CE3 . TRP   A 297 ? 0.2419 0.2393 0.2191 -0.0455 -0.0650 0.0487  297 TRP   A CE3 
4575  C  CZ2 . TRP   A 297 ? 0.3000 0.2930 0.2677 -0.0370 -0.0738 0.0508  297 TRP   A CZ2 
4576  C  CZ3 . TRP   A 297 ? 0.2584 0.2593 0.2413 -0.0409 -0.0673 0.0457  297 TRP   A CZ3 
4577  C  CH2 . TRP   A 297 ? 0.2758 0.2756 0.2561 -0.0368 -0.0719 0.0466  297 TRP   A CH2 
4588  N  N   . VAL   A 298 ? 0.2314 0.2009 0.1904 -0.0548 -0.0606 0.0603  298 VAL   A N   
4589  C  CA  . VAL   A 298 ? 0.2147 0.1752 0.1739 -0.0556 -0.0600 0.0628  298 VAL   A CA  
4590  C  C   . VAL   A 298 ? 0.2198 0.1708 0.1728 -0.0507 -0.0641 0.0654  298 VAL   A C   
4591  O  O   . VAL   A 298 ? 0.2146 0.1687 0.1715 -0.0457 -0.0678 0.0645  298 VAL   A O   
4592  C  CB  . VAL   A 298 ? 0.2062 0.1664 0.1719 -0.0563 -0.0582 0.0606  298 VAL   A CB  
4593  C  CG1 . VAL   A 298 ? 0.2111 0.1802 0.1802 -0.0600 -0.0543 0.0579  298 VAL   A CG1 
4594  C  CG2 . VAL   A 298 ? 0.1896 0.1494 0.1638 -0.0513 -0.0614 0.0592  298 VAL   A CG2 
4604  N  N   . ARG   A 299 ? 0.2168 0.1572 0.1631 -0.0516 -0.0632 0.0683  299 ARG   A N   
4605  C  CA  . ARG   A 299 ? 0.1999 0.1336 0.1503 -0.0458 -0.0655 0.0691  299 ARG   A CA  
4606  C  C   . ARG   A 299 ? 0.2409 0.1633 0.1860 -0.0442 -0.0678 0.0704  299 ARG   A C   
4607  O  O   . ARG   A 299 ? 0.2695 0.1877 0.2138 -0.0484 -0.0642 0.0704  299 ARG   A O   
4608  C  CB  . ARG   A 299 ? 0.2942 0.2150 0.2210 -0.0490 -0.0655 0.0756  299 ARG   A CB  
4609  C  CG  . ARG   A 299 ? 0.3551 0.2646 0.2768 -0.0435 -0.0691 0.0794  299 ARG   A CG  
4610  C  CD  . ARG   A 299 ? 0.4460 0.3475 0.3539 -0.0464 -0.0671 0.0840  299 ARG   A CD  
4611  N  NE  . ARG   A 299 ? 0.5523 0.4608 0.4484 -0.0495 -0.0655 0.0841  299 ARG   A NE  
4612  C  CZ  . ARG   A 299 ? 0.5207 0.4333 0.4144 -0.0568 -0.0603 0.0839  299 ARG   A CZ  
4613  N  NH1 . ARG   A 299 ? 0.4846 0.3965 0.3888 -0.0617 -0.0561 0.0832  299 ARG   A NH1 
4614  N  NH2 . ARG   A 299 ? 0.3964 0.3184 0.2970 -0.0587 -0.0592 0.0841  299 ARG   A NH2 
4628  N  N   . LEU   A 300 ? 0.2270 0.1495 0.1814 -0.0376 -0.0720 0.0693  300 LEU   A N   
4629  C  CA  . LEU   A 300 ? 0.2748 0.1891 0.2289 -0.0346 -0.0731 0.0685  300 LEU   A CA  
4630  C  C   . LEU   A 300 ? 0.2828 0.1823 0.2290 -0.0339 -0.0732 0.0722  300 LEU   A C   
4631  O  O   . LEU   A 300 ? 0.2888 0.1842 0.2249 -0.0346 -0.0732 0.0759  300 LEU   A O   
4632  C  CB  . LEU   A 300 ? 0.2816 0.2008 0.2446 -0.0272 -0.0775 0.0660  300 LEU   A CB  
4633  C  CG  . LEU   A 300 ? 0.2586 0.1925 0.2354 -0.0277 -0.0772 0.0621  300 LEU   A CG  
4634  C  CD1 . LEU   A 300 ? 0.2606 0.1984 0.2439 -0.0208 -0.0809 0.0592  300 LEU   A CD1 
4635  C  CD2 . LEU   A 300 ? 0.2722 0.2086 0.2505 -0.0334 -0.0729 0.0604  300 LEU   A CD2 
4647  N  N   . LYS   A 301 ? 0.2911 0.1825 0.2410 -0.0328 -0.0729 0.0717  301 LYS   A N   
4648  C  CA  . LYS   A 301 ? 0.3515 0.2261 0.2888 -0.0323 -0.0727 0.0751  301 LYS   A CA  
4649  C  C   . LYS   A 301 ? 0.3879 0.2556 0.3133 -0.0254 -0.0774 0.0786  301 LYS   A C   
4650  O  O   . LYS   A 301 ? 0.3671 0.2250 0.2887 -0.0261 -0.0766 0.0832  301 LYS   A O   
4651  C  CB  . LYS   A 301 ? 0.3474 0.2158 0.2954 -0.0312 -0.0722 0.0731  301 LYS   A CB  
4652  C  CG  . LYS   A 301 ? 0.4638 0.3134 0.3969 -0.0314 -0.0714 0.0760  301 LYS   A CG  
4653  C  CD  . LYS   A 301 ? 0.5507 0.3950 0.4974 -0.0305 -0.0709 0.0734  301 LYS   A CD  
4654  C  CE  . LYS   A 301 ? 0.8177 0.6402 0.7398 -0.0308 -0.0699 0.0762  301 LYS   A CE  
4655  N  NZ  . LYS   A 301 ? 0.9085 0.7248 0.8388 -0.0300 -0.0694 0.0729  301 LYS   A NZ  
4669  N  N   . ASP   A 302 ? 0.3213 0.1993 0.2638 -0.0187 -0.0818 0.0766  302 ASP   A N   
4670  C  CA  . ASP   A 302 ? 0.3626 0.2360 0.2937 -0.0107 -0.0870 0.0789  302 ASP   A CA  
4671  C  C   . ASP   A 302 ? 0.3810 0.2601 0.3037 -0.0120 -0.0874 0.0813  302 ASP   A C   
4672  O  O   . ASP   A 302 ? 0.3621 0.2409 0.2838 -0.0055 -0.0917 0.0835  302 ASP   A O   
4673  C  CB  . ASP   A 302 ? 0.3457 0.2274 0.2932 -0.0024 -0.0916 0.0751  302 ASP   A CB  
4674  C  CG  . ASP   A 302 ? 0.4141 0.3107 0.3590 -0.0024 -0.0923 0.0709  302 ASP   A CG  
4675  O  OD1 . ASP   A 302 ? 0.3341 0.2399 0.2899 -0.0086 -0.0893 0.0711  302 ASP   A OD1 
4676  O  OD2 . ASP   A 302 ? 0.3886 0.2947 0.3523 0.0037  -0.0954 0.0673  302 ASP   A OD2 
4681  N  N   . GLY   A 303 ? 0.3591 0.2457 0.2844 -0.0198 -0.0832 0.0811  303 GLY   A N   
4682  C  CA  . GLY   A 303 ? 0.3512 0.2439 0.2703 -0.0215 -0.0831 0.0827  303 GLY   A CA  
4683  C  C   . GLY   A 303 ? 0.3523 0.2605 0.2777 -0.0199 -0.0850 0.0785  303 GLY   A C   
4684  O  O   . GLY   A 303 ? 0.3659 0.2806 0.2874 -0.0221 -0.0846 0.0791  303 GLY   A O   
4688  N  N   . THR   A 304 ? 0.3136 0.2295 0.2552 -0.0164 -0.0867 0.0743  304 THR   A N   
4689  C  CA  . THR   A 304 ? 0.3280 0.2584 0.2750 -0.0155 -0.0878 0.0696  304 THR   A CA  
4690  C  C   . THR   A 304 ? 0.3083 0.2457 0.2579 -0.0236 -0.0830 0.0684  304 THR   A C   
4691  O  O   . THR   A 304 ? 0.3188 0.2522 0.2696 -0.0286 -0.0792 0.0686  304 THR   A O   
4692  C  CB  . THR   A 304 ? 0.3193 0.2576 0.2903 -0.0111 -0.0898 0.0655  304 THR   A CB  
4693  O  OG1 . THR   A 304 ? 0.4321 0.3621 0.3880 -0.0030 -0.0941 0.0661  304 THR   A OG1 
4694  C  CG2 . THR   A 304 ? 0.3888 0.3399 0.3571 -0.0108 -0.0899 0.0607  304 THR   A CG2 
4702  N  N   . GLU   A 305 ? 0.2595 0.2080 0.2129 -0.0246 -0.0831 0.0665  305 GLU   A N   
4703  C  CA  . GLU   A 305 ? 0.2587 0.2145 0.2144 -0.0314 -0.0786 0.0649  305 GLU   A CA  
4704  C  C   . GLU   A 305 ? 0.2945 0.2601 0.2572 -0.0307 -0.0784 0.0599  305 GLU   A C   
4705  O  O   . GLU   A 305 ? 0.3075 0.2795 0.2776 -0.0256 -0.0817 0.0574  305 GLU   A O   
4706  C  CB  . GLU   A 305 ? 0.2755 0.2338 0.2212 -0.0336 -0.0782 0.0663  305 GLU   A CB  
4707  C  CG  . GLU   A 305 ? 0.3435 0.2914 0.2750 -0.0363 -0.0766 0.0712  305 GLU   A CG  
4708  C  CD  . GLU   A 305 ? 0.4328 0.3830 0.3518 -0.0388 -0.0755 0.0725  305 GLU   A CD  
4709  O  OE1 . GLU   A 305 ? 0.4046 0.3661 0.3300 -0.0396 -0.0754 0.0690  305 GLU   A OE1 
4710  O  OE2 . GLU   A 305 ? 0.5159 0.4573 0.4212 -0.0401 -0.0746 0.0768  305 GLU   A OE2 
4717  N  N   . CYS   A 306 ? 0.2554 0.2250 0.2278 -0.0355 -0.0744 0.0583  306 CYS   A N   
4718  C  CA  . CYS   A 306 ? 0.2374 0.2153 0.2174 -0.0348 -0.0732 0.0538  306 CYS   A CA  
4719  C  C   . CYS   A 306 ? 0.1994 0.1813 0.1862 -0.0406 -0.0686 0.0528  306 CYS   A C   
4720  O  O   . CYS   A 306 ? 0.2035 0.1806 0.1819 -0.0447 -0.0665 0.0555  306 CYS   A O   
4721  C  CB  . CYS   A 306 ? 0.2069 0.1844 0.2007 -0.0305 -0.0752 0.0525  306 CYS   A CB  
4722  S  SG  . CYS   A 306 ? 0.2549 0.2209 0.2421 -0.0325 -0.0735 0.0547  306 CYS   A SG  
4728  N  N   . GLY   A 307 ? 0.2014 0.1900 0.1932 -0.0401 -0.0665 0.0491  307 GLY   A N   
4729  C  CA  . GLY   A 307 ? 0.1854 0.1772 0.1817 -0.0441 -0.0623 0.0480  307 GLY   A CA  
4730  C  C   . GLY   A 307 ? 0.1922 0.1775 0.1852 -0.0463 -0.0617 0.0502  307 GLY   A C   
4731  O  O   . GLY   A 307 ? 0.1763 0.1581 0.1756 -0.0432 -0.0638 0.0504  307 GLY   A O   
4735  N  N   . GLY   A 308 ? 0.1700 0.1568 0.1640 -0.0510 -0.0591 0.0513  308 GLY   A N   
4736  C  CA  . GLY   A 308 ? 0.1890 0.1712 0.1790 -0.0530 -0.0577 0.0519  308 GLY   A CA  
4737  C  C   . GLY   A 308 ? 0.1693 0.1562 0.1673 -0.0509 -0.0546 0.0487  308 GLY   A C   
4738  O  O   . GLY   A 308 ? 0.1724 0.1639 0.1733 -0.0486 -0.0522 0.0462  308 GLY   A O   
4742  N  N   . PRO   A 309 ? 0.1553 0.1399 0.1535 -0.0506 -0.0520 0.0472  309 PRO   A N   
4743  C  CA  . PRO   A 309 ? 0.1531 0.1408 0.1554 -0.0476 -0.0486 0.0435  309 PRO   A CA  
4744  C  C   . PRO   A 309 ? 0.1570 0.1506 0.1579 -0.0477 -0.0437 0.0408  309 PRO   A C   
4745  O  O   . PRO   A 309 ? 0.1435 0.1390 0.1426 -0.0510 -0.0423 0.0413  309 PRO   A O   
4746  C  CB  . PRO   A 309 ? 0.1364 0.1187 0.1404 -0.0479 -0.0488 0.0435  309 PRO   A CB  
4747  C  CG  . PRO   A 309 ? 0.1454 0.1230 0.1416 -0.0519 -0.0491 0.0459  309 PRO   A CG  
4748  C  CD  . PRO   A 309 ? 0.1482 0.1261 0.1421 -0.0529 -0.0521 0.0486  309 PRO   A CD  
4756  N  N   . GLU   A 310 ? 0.1414 0.1387 0.1478 -0.0446 -0.0412 0.0377  310 GLU   A N   
4757  C  CA  . GLU   A 310 ? 0.1282 0.1300 0.1337 -0.0442 -0.0375 0.0350  310 GLU   A CA  
4758  C  C   . GLU   A 310 ? 0.0990 0.1018 0.1114 -0.0446 -0.0363 0.0335  310 GLU   A C   
4759  O  O   . GLU   A 310 ? 0.1414 0.1386 0.1482 -0.0446 -0.0379 0.0339  310 GLU   A O   
4760  C  CB  . GLU   A 310 ? 0.1139 0.1189 0.1252 -0.0413 -0.0362 0.0329  310 GLU   A CB  
4761  C  CG  . GLU   A 310 ? 0.1387 0.1432 0.1486 -0.0408 -0.0374 0.0334  310 GLU   A CG  
4762  C  CD  . GLU   A 310 ? 0.1751 0.1809 0.1751 -0.0429 -0.0366 0.0335  310 GLU   A CD  
4763  O  OE1 . GLU   A 310 ? 0.1228 0.1335 0.1301 -0.0446 -0.0353 0.0331  310 GLU   A OE1 
4764  O  OE2 . GLU   A 310 ? 0.1313 0.1393 0.1397 -0.0430 -0.0379 0.0334  310 GLU   A OE2 
4771  N  N   . TYR   A 311 ? 0.1203 0.1271 0.1286 -0.0451 -0.0338 0.0312  311 TYR   A N   
4772  C  CA  . TYR   A 311 ? 0.1283 0.1362 0.1381 -0.0459 -0.0327 0.0289  311 TYR   A CA  
4773  C  C   . TYR   A 311 ? 0.1288 0.1337 0.1421 -0.0433 -0.0336 0.0281  311 TYR   A C   
4774  O  O   . TYR   A 311 ? 0.1212 0.1234 0.1353 -0.0447 -0.0345 0.0277  311 TYR   A O   
4775  C  CB  . TYR   A 311 ? 0.1131 0.1289 0.1277 -0.0459 -0.0308 0.0263  311 TYR   A CB  
4776  C  CG  . TYR   A 311 ? 0.1348 0.1523 0.1472 -0.0459 -0.0303 0.0236  311 TYR   A CG  
4777  C  CD1 . TYR   A 311 ? 0.0927 0.1103 0.1121 -0.0493 -0.0300 0.0229  311 TYR   A CD1 
4778  C  CD2 . TYR   A 311 ? 0.1335 0.1555 0.1524 -0.0434 -0.0305 0.0215  311 TYR   A CD2 
4779  C  CE1 . TYR   A 311 ? 0.1232 0.1428 0.1407 -0.0496 -0.0300 0.0199  311 TYR   A CE1 
4780  C  CE2 . TYR   A 311 ? 0.1492 0.1739 0.1679 -0.0435 -0.0308 0.0187  311 TYR   A CE2 
4781  C  CZ  . TYR   A 311 ? 0.1260 0.1503 0.1466 -0.0465 -0.0305 0.0177  311 TYR   A CZ  
4782  O  OH  . TYR   A 311 ? 0.0898 0.1184 0.1157 -0.0470 -0.0313 0.0141  311 TYR   A OH  
4792  N  N   . GLU   A 312 ? 0.1372 0.1427 0.1500 -0.0405 -0.0335 0.0274  312 GLU   A N   
4793  C  CA  . GLU   A 312 ? 0.1021 0.1066 0.1214 -0.0386 -0.0343 0.0263  312 GLU   A CA  
4794  C  C   . GLU   A 312 ? 0.1190 0.1172 0.1351 -0.0386 -0.0364 0.0276  312 GLU   A C   
4795  O  O   . GLU   A 312 ? 0.1009 0.0976 0.1214 -0.0381 -0.0371 0.0262  312 GLU   A O   
4796  C  CB  . GLU   A 312 ? 0.0942 0.0997 0.1125 -0.0363 -0.0335 0.0262  312 GLU   A CB  
4797  C  CG  . GLU   A 312 ? 0.0886 0.0986 0.1086 -0.0361 -0.0324 0.0253  312 GLU   A CG  
4798  C  CD  . GLU   A 312 ? 0.1318 0.1461 0.1494 -0.0364 -0.0324 0.0235  312 GLU   A CD  
4799  O  OE1 . GLU   A 312 ? 0.1456 0.1601 0.1642 -0.0363 -0.0329 0.0224  312 GLU   A OE1 
4800  O  OE2 . GLU   A 312 ? 0.1492 0.1679 0.1665 -0.0367 -0.0317 0.0230  312 GLU   A OE2 
4807  N  N   . THR   A 313 ? 0.1193 0.1156 0.1367 -0.0391 -0.0379 0.0300  313 THR   A N   
4808  C  CA  . THR   A 313 ? 0.1326 0.1237 0.1520 -0.0392 -0.0408 0.0318  313 THR   A CA  
4809  C  C   . THR   A 313 ? 0.1868 0.1713 0.1955 -0.0419 -0.0417 0.0323  313 THR   A C   
4810  O  O   . THR   A 313 ? 0.1584 0.1392 0.1764 -0.0421 -0.0436 0.0320  313 THR   A O   
4811  C  CB  . THR   A 313 ? 0.1347 0.1250 0.1534 -0.0391 -0.0431 0.0341  313 THR   A CB  
4812  O  OG1 . THR   A 313 ? 0.1463 0.1402 0.1651 -0.0368 -0.0415 0.0329  313 THR   A OG1 
4813  C  CG2 . THR   A 313 ? 0.1510 0.1348 0.1691 -0.0389 -0.0473 0.0362  313 THR   A CG2 
4821  N  N   . LEU   A 314 ? 0.1310 0.1197 0.1482 -0.0450 -0.0401 0.0328  314 LEU   A N   
4822  C  CA  . LEU   A 314 ? 0.1803 0.1625 0.1835 -0.0482 -0.0400 0.0328  314 LEU   A CA  
4823  C  C   . LEU   A 314 ? 0.1469 0.1308 0.1603 -0.0485 -0.0389 0.0295  314 LEU   A C   
4824  O  O   . LEU   A 314 ? 0.1538 0.1314 0.1660 -0.0497 -0.0399 0.0291  314 LEU   A O   
4825  C  CB  . LEU   A 314 ? 0.1248 0.1135 0.1369 -0.0518 -0.0377 0.0335  314 LEU   A CB  
4826  C  CG  . LEU   A 314 ? 0.1811 0.1659 0.1793 -0.0529 -0.0392 0.0369  314 LEU   A CG  
4827  C  CD1 . LEU   A 314 ? 0.1428 0.1356 0.1454 -0.0552 -0.0364 0.0366  314 LEU   A CD1 
4828  C  CD2 . LEU   A 314 ? 0.1865 0.1632 0.1851 -0.0556 -0.0411 0.0396  314 LEU   A CD2 
4840  N  N   . TRP   A 315 ? 0.1170 0.1075 0.1343 -0.0461 -0.0375 0.0269  315 TRP   A N   
4841  C  CA  . TRP   A 315 ? 0.1312 0.1224 0.1473 -0.0463 -0.0370 0.0236  315 TRP   A CA  
4842  C  C   . TRP   A 315 ? 0.1146 0.1009 0.1354 -0.0443 -0.0392 0.0229  315 TRP   A C   
4843  O  O   . TRP   A 315 ? 0.1286 0.1105 0.1482 -0.0458 -0.0399 0.0211  315 TRP   A O   
4844  C  CB  . TRP   A 315 ? 0.1236 0.1233 0.1439 -0.0447 -0.0356 0.0212  315 TRP   A CB  
4845  C  CG  . TRP   A 315 ? 0.1335 0.1347 0.1551 -0.0437 -0.0362 0.0182  315 TRP   A CG  
4846  C  CD1 . TRP   A 315 ? 0.1486 0.1506 0.1689 -0.0461 -0.0364 0.0149  315 TRP   A CD1 
4847  C  CD2 . TRP   A 315 ? 0.1311 0.1324 0.1521 -0.0407 -0.0370 0.0176  315 TRP   A CD2 
4848  N  NE1 . TRP   A 315 ? 0.1120 0.1164 0.1376 -0.0443 -0.0377 0.0124  315 TRP   A NE1 
4849  C  CE2 . TRP   A 315 ? 0.1125 0.1160 0.1370 -0.0413 -0.0381 0.0143  315 TRP   A CE2 
4850  C  CE3 . TRP   A 315 ? 0.1140 0.1153 0.1377 -0.0383 -0.0371 0.0194  315 TRP   A CE3 
4851  C  CZ2 . TRP   A 315 ? 0.1147 0.1192 0.1391 -0.0391 -0.0394 0.0131  315 TRP   A CZ2 
4852  C  CZ3 . TRP   A 315 ? 0.1174 0.1197 0.1413 -0.0367 -0.0379 0.0184  315 TRP   A CZ3 
4853  C  CH2 . TRP   A 315 ? 0.1277 0.1309 0.1506 -0.0370 -0.0390 0.0154  315 TRP   A CH2 
4864  N  N   . CYS   A 316 ? 0.1074 0.0942 0.1310 -0.0411 -0.0401 0.0241  316 CYS   A N   
4865  C  CA  . CYS   A 316 ? 0.1518 0.1347 0.1746 -0.0394 -0.0418 0.0228  316 CYS   A CA  
4866  C  C   . CYS   A 316 ? 0.1627 0.1371 0.1874 -0.0398 -0.0446 0.0239  316 CYS   A C   
4867  O  O   . CYS   A 316 ? 0.1657 0.1362 0.1931 -0.0387 -0.0464 0.0216  316 CYS   A O   
4868  C  CB  . CYS   A 316 ? 0.1548 0.1420 0.1820 -0.0366 -0.0415 0.0234  316 CYS   A CB  
4869  S  SG  . CYS   A 316 ? 0.1727 0.1587 0.1991 -0.0366 -0.0429 0.0266  316 CYS   A SG  
4875  N  N   . PHE   A 317 ? 0.1658 0.1361 0.1876 -0.0410 -0.0459 0.0270  317 PHE   A N   
4876  C  CA  . PHE   A 317 ? 0.1627 0.1230 0.1857 -0.0413 -0.0489 0.0286  317 PHE   A CA  
4877  C  C   . PHE   A 317 ? 0.1772 0.1317 0.1927 -0.0450 -0.0477 0.0288  317 PHE   A C   
4878  O  O   . PHE   A 317 ? 0.1763 0.1213 0.1905 -0.0456 -0.0495 0.0306  317 PHE   A O   
4879  C  CB  . PHE   A 317 ? 0.1859 0.1436 0.2051 -0.0398 -0.0517 0.0323  317 PHE   A CB  
4880  C  CG  . PHE   A 317 ? 0.1605 0.1220 0.1885 -0.0366 -0.0534 0.0317  317 PHE   A CG  
4881  C  CD1 . PHE   A 317 ? 0.1569 0.1152 0.1898 -0.0336 -0.0550 0.0291  317 PHE   A CD1 
4882  C  CD2 . PHE   A 317 ? 0.1520 0.1211 0.1815 -0.0360 -0.0531 0.0329  317 PHE   A CD2 
4883  C  CE1 . PHE   A 317 ? 0.1722 0.1366 0.2070 -0.0290 -0.0547 0.0273  317 PHE   A CE1 
4884  C  CE2 . PHE   A 317 ? 0.1539 0.1275 0.1882 -0.0333 -0.0539 0.0316  317 PHE   A CE2 
4885  C  CZ  . PHE   A 317 ? 0.1436 0.1167 0.1841 -0.0294 -0.0540 0.0286  317 PHE   A CZ  
4895  N  N   . GLY   A 318 ? 0.1673 0.1289 0.1843 -0.0476 -0.0445 0.0267  318 GLY   A N   
4896  C  CA  . GLY   A 318 ? 0.1756 0.1335 0.1874 -0.0519 -0.0426 0.0259  318 GLY   A CA  
4897  C  C   . GLY   A 318 ? 0.1466 0.1085 0.1669 -0.0534 -0.0415 0.0211  318 GLY   A C   
4898  O  O   . GLY   A 318 ? 0.1900 0.1448 0.2053 -0.0523 -0.0430 0.0190  318 GLY   A O   
4902  N  N   . SER   A 319 ? 0.1652 0.1352 0.1813 -0.0552 -0.0388 0.0190  319 SER   A N   
4903  C  CA  . SER   A 319 ? 0.1602 0.1347 0.1788 -0.0569 -0.0380 0.0140  319 SER   A CA  
4904  C  C   . SER   A 319 ? 0.1510 0.1261 0.1738 -0.0536 -0.0400 0.0112  319 SER   A C   
4905  O  O   . SER   A 319 ? 0.1456 0.1190 0.1690 -0.0549 -0.0406 0.0073  319 SER   A O   
4906  C  CB  . SER   A 319 ? 0.1387 0.1250 0.1620 -0.0582 -0.0358 0.0125  319 SER   A CB  
4907  O  OG  . SER   A 319 ? 0.1558 0.1419 0.1747 -0.0611 -0.0339 0.0149  319 SER   A OG  
4913  N  N   . ASP   A 320 ? 0.1625 0.1400 0.1838 -0.0496 -0.0408 0.0129  320 ASP   A N   
4914  C  CA  . ASP   A 320 ? 0.1467 0.1256 0.1703 -0.0468 -0.0424 0.0106  320 ASP   A CA  
4915  C  C   . ASP   A 320 ? 0.1405 0.1094 0.1658 -0.0465 -0.0446 0.0087  320 ASP   A C   
4916  O  O   . ASP   A 320 ? 0.1371 0.1062 0.1633 -0.0455 -0.0462 0.0050  320 ASP   A O   
4917  C  CB  . ASP   A 320 ? 0.1187 0.1027 0.1457 -0.0432 -0.0422 0.0124  320 ASP   A CB  
4918  C  CG  . ASP   A 320 ? 0.1287 0.1172 0.1559 -0.0413 -0.0429 0.0099  320 ASP   A CG  
4919  O  OD1 . ASP   A 320 ? 0.1381 0.1300 0.1634 -0.0424 -0.0434 0.0065  320 ASP   A OD1 
4920  O  OD2 . ASP   A 320 ? 0.1492 0.1381 0.1757 -0.0387 -0.0432 0.0111  320 ASP   A OD2 
4925  N  N   . CYS   A 321 ? 0.1455 0.1054 0.1699 -0.0466 -0.0455 0.0117  321 CYS   A N   
4926  C  CA  . CYS   A 321 ? 0.1626 0.1110 0.1872 -0.0455 -0.0481 0.0107  321 CYS   A CA  
4927  C  C   . CYS   A 321 ? 0.1819 0.1211 0.2006 -0.0494 -0.0474 0.0097  321 CYS   A C   
4928  O  O   . CYS   A 321 ? 0.1538 0.0824 0.1752 -0.0480 -0.0492 0.0093  321 CYS   A O   
4929  C  CB  . CYS   A 321 ? 0.1712 0.1141 0.1962 -0.0424 -0.0503 0.0143  321 CYS   A CB  
4930  S  SG  . CYS   A 321 ? 0.1733 0.1246 0.2034 -0.0381 -0.0510 0.0139  321 CYS   A SG  
4936  N  N   . GLY   A 322 ? 0.1789 0.1248 0.2007 -0.0536 -0.0448 0.0092  322 GLY   A N   
4937  C  CA  . GLY   A 322 ? 0.2128 0.1510 0.2278 -0.0584 -0.0434 0.0084  322 GLY   A CA  
4938  C  C   . GLY   A 322 ? 0.1853 0.1140 0.2005 -0.0593 -0.0435 0.0132  322 GLY   A C   
4939  O  O   . GLY   A 322 ? 0.1812 0.0997 0.1930 -0.0623 -0.0430 0.0125  322 GLY   A O   
4943  N  N   . SER   A 323 ? 0.1901 0.1202 0.2019 -0.0567 -0.0444 0.0177  323 SER   A N   
4944  C  CA  . SER   A 323 ? 0.1803 0.1023 0.1904 -0.0570 -0.0451 0.0230  323 SER   A CA  
4945  C  C   . SER   A 323 ? 0.2104 0.1385 0.2146 -0.0605 -0.0425 0.0256  323 SER   A C   
4946  O  O   . SER   A 323 ? 0.2196 0.1600 0.2272 -0.0597 -0.0412 0.0250  323 SER   A O   
4947  C  CB  . SER   A 323 ? 0.1902 0.1083 0.2004 -0.0514 -0.0487 0.0259  323 SER   A CB  
4948  O  OG  . SER   A 323 ? 0.2517 0.1593 0.2517 -0.0511 -0.0502 0.0303  323 SER   A OG  
4954  N  N   . TYR   A 324 ? 0.2074 0.1279 0.2075 -0.0641 -0.0412 0.0285  324 TYR   A N   
4955  C  CA  . TYR   A 324 ? 0.1977 0.1245 0.1974 -0.0678 -0.0386 0.0308  324 TYR   A CA  
4956  C  C   . TYR   A 324 ? 0.2295 0.1466 0.2188 -0.0673 -0.0401 0.0366  324 TYR   A C   
4957  O  O   . TYR   A 324 ? 0.2404 0.1565 0.2267 -0.0717 -0.0376 0.0387  324 TYR   A O   
4958  C  CB  . TYR   A 324 ? 0.1997 0.1291 0.1997 -0.0740 -0.0347 0.0277  324 TYR   A CB  
4959  C  CG  . TYR   A 324 ? 0.2101 0.1490 0.2151 -0.0735 -0.0341 0.0220  324 TYR   A CG  
4960  C  CD1 . TYR   A 324 ? 0.1960 0.1492 0.2060 -0.0721 -0.0332 0.0203  324 TYR   A CD1 
4961  C  CD2 . TYR   A 324 ? 0.2100 0.1446 0.2214 -0.0738 -0.0349 0.0180  324 TYR   A CD2 
4962  C  CE1 . TYR   A 324 ? 0.1851 0.1475 0.2029 -0.0709 -0.0333 0.0154  324 TYR   A CE1 
4963  C  CE2 . TYR   A 324 ? 0.2706 0.2126 0.2797 -0.0732 -0.0348 0.0127  324 TYR   A CE2 
4964  C  CZ  . TYR   A 324 ? 0.2353 0.1925 0.2527 -0.0717 -0.0341 0.0115  324 TYR   A CZ  
4965  O  OH  . TYR   A 324 ? 0.2573 0.2231 0.2775 -0.0705 -0.0345 0.0064  324 TYR   A OH  
4975  N  N   . ASP   A 325 ? 0.2172 0.1291 0.2075 -0.0621 -0.0441 0.0388  325 ASP   A N   
4976  C  CA  . ASP   A 325 ? 0.2151 0.1193 0.2007 -0.0602 -0.0467 0.0439  325 ASP   A CA  
4977  C  C   . ASP   A 325 ? 0.2248 0.1388 0.2066 -0.0586 -0.0477 0.0456  325 ASP   A C   
4978  O  O   . ASP   A 325 ? 0.1947 0.1149 0.1857 -0.0542 -0.0501 0.0445  325 ASP   A O   
4979  C  CB  . ASP   A 325 ? 0.2377 0.1292 0.2212 -0.0552 -0.0507 0.0447  325 ASP   A CB  
4980  C  CG  . ASP   A 325 ? 0.2779 0.1595 0.2525 -0.0522 -0.0537 0.0497  325 ASP   A CG  
4981  O  OD1 . ASP   A 325 ? 0.2430 0.1303 0.2177 -0.0533 -0.0536 0.0524  325 ASP   A OD1 
4982  O  OD2 . ASP   A 325 ? 0.3222 0.1909 0.2939 -0.0485 -0.0561 0.0505  325 ASP   A OD2 
4987  N  N   . LEU   A 326 ? 0.2074 0.1250 0.1871 -0.0621 -0.0456 0.0481  326 LEU   A N   
4988  C  CA  . LEU   A 326 ? 0.1840 0.1127 0.1684 -0.0612 -0.0462 0.0492  326 LEU   A CA  
4989  C  C   . LEU   A 326 ? 0.2071 0.1301 0.1830 -0.0567 -0.0508 0.0523  326 LEU   A C   
4990  O  O   . LEU   A 326 ? 0.1827 0.1146 0.1667 -0.0538 -0.0530 0.0515  326 LEU   A O   
4991  C  CB  . LEU   A 326 ? 0.2303 0.1618 0.2040 -0.0664 -0.0427 0.0504  326 LEU   A CB  
4992  C  CG  . LEU   A 326 ? 0.2303 0.1728 0.2046 -0.0664 -0.0424 0.0507  326 LEU   A CG  
4993  C  CD1 . LEU   A 326 ? 0.2169 0.1704 0.2010 -0.0630 -0.0428 0.0474  326 LEU   A CD1 
4994  C  CD2 . LEU   A 326 ? 0.2047 0.1527 0.1784 -0.0719 -0.0382 0.0508  326 LEU   A CD2 
5006  N  N   . ASP   A 327 ? 0.2071 0.1186 0.1807 -0.0560 -0.0528 0.0559  327 ASP   A N   
5007  C  CA  . ASP   A 327 ? 0.2498 0.1556 0.2171 -0.0505 -0.0577 0.0584  327 ASP   A CA  
5008  C  C   . ASP   A 327 ? 0.2385 0.1480 0.2160 -0.0452 -0.0608 0.0556  327 ASP   A C   
5009  O  O   . ASP   A 327 ? 0.2354 0.1505 0.2170 -0.0413 -0.0637 0.0562  327 ASP   A O   
5010  C  CB  . ASP   A 327 ? 0.2539 0.1447 0.2157 -0.0490 -0.0590 0.0621  327 ASP   A CB  
5011  C  CG  . ASP   A 327 ? 0.2723 0.1594 0.2272 -0.0533 -0.0568 0.0660  327 ASP   A CG  
5012  O  OD1 . ASP   A 327 ? 0.2774 0.1720 0.2269 -0.0551 -0.0562 0.0668  327 ASP   A OD1 
5013  O  OD2 . ASP   A 327 ? 0.3594 0.2323 0.3000 -0.0551 -0.0553 0.0682  327 ASP   A OD2 
5018  N  N   . ALA   A 328 ? 0.2131 0.1203 0.1984 -0.0447 -0.0598 0.0529  328 ALA   A N   
5019  C  CA  . ALA   A 328 ? 0.2424 0.1506 0.2288 -0.0399 -0.0623 0.0498  328 ALA   A CA  
5020  C  C   . ALA   A 328 ? 0.1903 0.1144 0.1914 -0.0403 -0.0615 0.0478  328 ALA   A C   
5021  O  O   . ALA   A 328 ? 0.1967 0.1236 0.1999 -0.0361 -0.0641 0.0470  328 ALA   A O   
5022  C  CB  . ALA   A 328 ? 0.2340 0.1369 0.2270 -0.0402 -0.0610 0.0468  328 ALA   A CB  
5028  N  N   . ILE   A 329 ? 0.2036 0.1350 0.1996 -0.0448 -0.0575 0.0467  329 ILE   A N   
5029  C  CA  . ILE   A 329 ? 0.1849 0.1296 0.1888 -0.0448 -0.0561 0.0449  329 ILE   A CA  
5030  C  C   . ILE   A 329 ? 0.2262 0.1730 0.2234 -0.0437 -0.0587 0.0475  329 ILE   A C   
5031  O  O   . ILE   A 329 ? 0.2098 0.1643 0.2180 -0.0417 -0.0598 0.0467  329 ILE   A O   
5032  C  CB  . ILE   A 329 ? 0.1604 0.1132 0.1664 -0.0484 -0.0513 0.0426  329 ILE   A CB  
5033  C  CG1 . ILE   A 329 ? 0.2021 0.1517 0.2045 -0.0493 -0.0491 0.0394  329 ILE   A CG1 
5034  C  CG2 . ILE   A 329 ? 0.1758 0.1389 0.1805 -0.0474 -0.0499 0.0412  329 ILE   A CG2 
5035  C  CD1 . ILE   A 329 ? 0.2180 0.1723 0.2196 -0.0534 -0.0451 0.0376  329 ILE   A CD1 
5047  N  N   . ASN   A 330 ? 0.1877 0.1321 0.1867 -0.0454 -0.0595 0.0507  330 ASN   A N   
5048  C  CA  . ASN   A 330 ? 0.2348 0.1799 0.2224 -0.0441 -0.0621 0.0531  330 ASN   A CA  
5049  C  C   . ASN   A 330 ? 0.1912 0.1359 0.1909 -0.0379 -0.0667 0.0530  330 ASN   A C   
5050  O  O   . ASN   A 330 ? 0.1881 0.1400 0.1896 -0.0362 -0.0682 0.0525  330 ASN   A O   
5051  C  CB  . ASN   A 330 ? 0.2209 0.1623 0.2053 -0.0465 -0.0617 0.0563  330 ASN   A CB  
5052  C  CG  . ASN   A 330 ? 0.2280 0.1732 0.2069 -0.0521 -0.0571 0.0560  330 ASN   A CG  
5053  O  OD1 . ASN   A 330 ? 0.2050 0.1599 0.1904 -0.0535 -0.0546 0.0532  330 ASN   A OD1 
5054  N  ND2 . ASN   A 330 ? 0.2429 0.1818 0.2137 -0.0552 -0.0557 0.0585  330 ASN   A ND2 
5061  N  N   . GLU   A 331 ? 0.1967 0.1316 0.1941 -0.0346 -0.0686 0.0531  331 GLU   A N   
5062  C  CA  . GLU   A 331 ? 0.1995 0.1334 0.2025 -0.0273 -0.0729 0.0521  331 GLU   A CA  
5063  C  C   . GLU   A 331 ? 0.1884 0.1310 0.2012 -0.0257 -0.0725 0.0489  331 GLU   A C   
5064  O  O   . GLU   A 331 ? 0.1786 0.1292 0.1974 -0.0215 -0.0746 0.0475  331 GLU   A O   
5065  C  CB  . GLU   A 331 ? 0.2249 0.1465 0.2268 -0.0237 -0.0747 0.0526  331 GLU   A CB  
5066  C  CG  . GLU   A 331 ? 0.2990 0.2202 0.3063 -0.0153 -0.0793 0.0517  331 GLU   A CG  
5067  C  CD  . GLU   A 331 ? 0.4698 0.3861 0.4610 -0.0119 -0.0823 0.0545  331 GLU   A CD  
5068  O  OE1 . GLU   A 331 ? 0.4991 0.4122 0.4854 -0.0163 -0.0808 0.0578  331 GLU   A OE1 
5069  O  OE2 . GLU   A 331 ? 0.5008 0.4205 0.4996 -0.0048 -0.0861 0.0531  331 GLU   A OE2 
5076  N  N   . ALA   A 332 ? 0.1883 0.1299 0.2029 -0.0286 -0.0694 0.0471  332 ALA   A N   
5077  C  CA  . ALA   A 332 ? 0.1722 0.1233 0.1971 -0.0274 -0.0671 0.0427  332 ALA   A CA  
5078  C  C   . ALA   A 332 ? 0.1882 0.1507 0.2116 -0.0288 -0.0654 0.0418  332 ALA   A C   
5079  O  O   . ALA   A 332 ? 0.1584 0.1305 0.1938 -0.0259 -0.0649 0.0385  332 ALA   A O   
5080  C  CB  . ALA   A 332 ? 0.1652 0.1136 0.1893 -0.0310 -0.0637 0.0406  332 ALA   A CB  
5086  N  N   . ASN   A 333 ? 0.1597 0.1243 0.1827 -0.0334 -0.0641 0.0441  333 ASN   A N   
5087  C  CA  . ASN   A 333 ? 0.1534 0.1285 0.1788 -0.0354 -0.0625 0.0432  333 ASN   A CA  
5088  C  C   . ASN   A 333 ? 0.1682 0.1466 0.1914 -0.0313 -0.0659 0.0429  333 ASN   A C   
5089  O  O   . ASN   A 333 ? 0.1291 0.1173 0.1631 -0.0302 -0.0637 0.0395  333 ASN   A O   
5090  C  CB  . ASN   A 333 ? 0.1749 0.1492 0.1901 -0.0405 -0.0605 0.0455  333 ASN   A CB  
5091  C  CG  . ASN   A 333 ? 0.1536 0.1374 0.1723 -0.0408 -0.0573 0.0437  333 ASN   A CG  
5092  O  OD1 . ASN   A 333 ? 0.1641 0.1523 0.1838 -0.0385 -0.0530 0.0401  333 ASN   A OD1 
5093  N  ND2 . ASN   A 333 ? 0.1482 0.1329 0.1618 -0.0424 -0.0588 0.0454  333 ASN   A ND2 
5100  N  N   . MET   A 334 ? 0.1609 0.1339 0.1820 -0.0295 -0.0696 0.0457  334 MET   A N   
5101  C  CA  . MET   A 334 ? 0.1479 0.1263 0.1755 -0.0251 -0.0721 0.0444  334 MET   A CA  
5102  C  C   . MET   A 334 ? 0.1801 0.1618 0.2071 -0.0201 -0.0729 0.0404  334 MET   A C   
5103  O  O   . MET   A 334 ? 0.1272 0.1206 0.1686 -0.0190 -0.0723 0.0371  334 MET   A O   
5104  C  CB  . MET   A 334 ? 0.1915 0.1599 0.2053 -0.0228 -0.0756 0.0475  334 MET   A CB  
5105  C  CG  . MET   A 334 ? 0.1956 0.1693 0.2137 -0.0175 -0.0790 0.0463  334 MET   A CG  
5106  S  SD  . MET   A 334 ? 0.2192 0.1917 0.2449 -0.0093 -0.0826 0.0442  334 MET   A SD  
5107  C  CE  . MET   A 334 ? 0.2948 0.2486 0.3061 -0.0090 -0.0839 0.0483  334 MET   A CE  
5117  N  N   . LEU   A 335 ? 0.1353 0.1132 0.1738 -0.0178 -0.0743 0.0403  335 LEU   A N   
5118  C  CA  . LEU   A 335 ? 0.1401 0.1236 0.1883 -0.0125 -0.0753 0.0363  335 LEU   A CA  
5119  C  C   . LEU   A 335 ? 0.1707 0.1638 0.2182 -0.0151 -0.0702 0.0321  335 LEU   A C   
5120  O  O   . LEU   A 335 ? 0.1287 0.1329 0.1913 -0.0126 -0.0700 0.0284  335 LEU   A O   
5121  C  CB  . LEU   A 335 ? 0.1702 0.1429 0.2139 -0.0096 -0.0755 0.0360  335 LEU   A CB  
5122  C  CG  . LEU   A 335 ? 0.1813 0.1428 0.2239 -0.0051 -0.0809 0.0392  335 LEU   A CG  
5123  C  CD1 . LEU   A 335 ? 0.2280 0.1774 0.2641 -0.0030 -0.0805 0.0383  335 LEU   A CD1 
5124  C  CD2 . LEU   A 335 ? 0.2095 0.1767 0.2513 0.0012  -0.0841 0.0372  335 LEU   A CD2 
5136  N  N   . CYS   A 336 ? 0.1347 0.1276 0.1849 -0.0202 -0.0658 0.0326  336 CYS   A N   
5137  C  CA  . CYS   A 336 ? 0.1147 0.1161 0.1703 -0.0227 -0.0610 0.0296  336 CYS   A CA  
5138  C  C   . CYS   A 336 ? 0.1205 0.1280 0.1736 -0.0236 -0.0589 0.0283  336 CYS   A C   
5139  O  O   . CYS   A 336 ? 0.1062 0.1215 0.1663 -0.0234 -0.0560 0.0249  336 CYS   A O   
5140  C  CB  . CYS   A 336 ? 0.1324 0.1296 0.1813 -0.0267 -0.0572 0.0303  336 CYS   A CB  
5141  S  SG  . CYS   A 336 ? 0.1415 0.1322 0.1898 -0.0252 -0.0555 0.0287  336 CYS   A SG  
5147  N  N   . ASN   A 337 ? 0.1248 0.1298 0.1722 -0.0250 -0.0603 0.0308  337 ASN   A N   
5148  C  CA  . ASN   A 337 ? 0.1207 0.1320 0.1691 -0.0256 -0.0592 0.0294  337 ASN   A CA  
5149  C  C   . ASN   A 337 ? 0.1488 0.1658 0.1987 -0.0219 -0.0621 0.0266  337 ASN   A C   
5150  O  O   . ASN   A 337 ? 0.1379 0.1637 0.1962 -0.0225 -0.0602 0.0234  337 ASN   A O   
5151  C  CB  . ASN   A 337 ? 0.1135 0.1205 0.1530 -0.0279 -0.0601 0.0325  337 ASN   A CB  
5152  C  CG  . ASN   A 337 ? 0.1188 0.1224 0.1523 -0.0316 -0.0561 0.0340  337 ASN   A CG  
5153  O  OD1 . ASN   A 337 ? 0.1252 0.1306 0.1599 -0.0321 -0.0519 0.0318  337 ASN   A OD1 
5154  N  ND2 . ASN   A 337 ? 0.1222 0.1213 0.1485 -0.0341 -0.0574 0.0372  337 ASN   A ND2 
5161  N  N   . GLU   A 338 ? 0.1044 0.1204 0.1630 -0.0175 -0.0671 0.0275  338 GLU   A N   
5162  C  CA  . GLU   A 338 ? 0.1192 0.1416 0.1814 -0.0127 -0.0705 0.0248  338 GLU   A CA  
5163  C  C   . GLU   A 338 ? 0.1278 0.1587 0.1990 -0.0112 -0.0684 0.0201  338 GLU   A C   
5164  O  O   . GLU   A 338 ? 0.1128 0.1549 0.1928 -0.0104 -0.0678 0.0162  338 GLU   A O   
5165  C  CB  . GLU   A 338 ? 0.1382 0.1528 0.1944 -0.0078 -0.0763 0.0278  338 GLU   A CB  
5166  C  CG  . GLU   A 338 ? 0.1370 0.1463 0.1863 -0.0090 -0.0786 0.0316  338 GLU   A CG  
5167  C  CD  . GLU   A 338 ? 0.1760 0.1930 0.2206 -0.0074 -0.0804 0.0294  338 GLU   A CD  
5168  O  OE1 . GLU   A 338 ? 0.1482 0.1745 0.2005 -0.0108 -0.0771 0.0265  338 GLU   A OE1 
5169  O  OE2 . GLU   A 338 ? 0.1779 0.1941 0.2227 -0.0025 -0.0851 0.0306  338 GLU   A OE2 
5176  N  N   . TYR   A 339 ? 0.1198 0.1476 0.1958 -0.0108 -0.0671 0.0203  339 TYR   A N   
5177  C  CA  . TYR   A 339 ? 0.1207 0.1564 0.2042 -0.0100 -0.0644 0.0160  339 TYR   A CA  
5178  C  C   . TYR   A 339 ? 0.0931 0.1350 0.1826 -0.0156 -0.0578 0.0142  339 TYR   A C   
5179  O  O   . TYR   A 339 ? 0.1329 0.1826 0.2252 -0.0160 -0.0549 0.0103  339 TYR   A O   
5180  C  CB  . TYR   A 339 ? 0.1193 0.1496 0.2066 -0.0073 -0.0650 0.0162  339 TYR   A CB  
5181  C  CG  . TYR   A 339 ? 0.1288 0.1524 0.2155 -0.0008 -0.0706 0.0171  339 TYR   A CG  
5182  C  CD1 . TYR   A 339 ? 0.1325 0.1626 0.2250 0.0051  -0.0747 0.0149  339 TYR   A CD1 
5183  C  CD2 . TYR   A 339 ? 0.1520 0.1615 0.2300 -0.0001 -0.0712 0.0201  339 TYR   A CD2 
5184  C  CE1 . TYR   A 339 ? 0.1539 0.1760 0.2437 0.0120  -0.0798 0.0160  339 TYR   A CE1 
5185  C  CE2 . TYR   A 339 ? 0.1709 0.1718 0.2466 0.0057  -0.0761 0.0211  339 TYR   A CE2 
5186  C  CZ  . TYR   A 339 ? 0.1791 0.1857 0.2603 0.0125  -0.0811 0.0195  339 TYR   A CZ  
5187  O  OH  . TYR   A 339 ? 0.1989 0.1953 0.2767 0.0190  -0.0857 0.0207  339 TYR   A OH  
5197  N  N   . GLY   A 340 ? 0.0947 0.1302 0.1739 -0.0197 -0.0554 0.0168  340 GLY   A N   
5198  C  CA  . GLY   A 340 ? 0.1314 0.1677 0.2038 -0.0242 -0.0494 0.0155  340 GLY   A CA  
5199  C  C   . GLY   A 340 ? 0.0899 0.1255 0.1699 -0.0257 -0.0456 0.0158  340 GLY   A C   
5200  O  O   . GLY   A 340 ? 0.0938 0.1338 0.1744 -0.0272 -0.0417 0.0131  340 GLY   A O   
5204  N  N   . ILE   A 341 ? 0.1272 0.1527 0.1941 -0.0257 -0.0466 0.0186  341 ILE   A N   
5205  C  CA  . ILE   A 341 ? 0.0953 0.1191 0.1655 -0.0270 -0.0434 0.0188  341 ILE   A CA  
5206  C  C   . ILE   A 341 ? 0.0961 0.1123 0.1548 -0.0287 -0.0418 0.0215  341 ILE   A C   
5207  O  O   . ILE   A 341 ? 0.0965 0.1085 0.1501 -0.0284 -0.0442 0.0240  341 ILE   A O   
5208  C  CB  . ILE   A 341 ? 0.1098 0.1305 0.1783 -0.0236 -0.0448 0.0177  341 ILE   A CB  
5209  C  CG1 . ILE   A 341 ? 0.0908 0.1051 0.1608 -0.0215 -0.0497 0.0201  341 ILE   A CG1 
5210  C  CG2 . ILE   A 341 ? 0.0917 0.1211 0.1720 -0.0208 -0.0441 0.0138  341 ILE   A CG2 
5211  C  CD1 . ILE   A 341 ? 0.1255 0.1343 0.1918 -0.0176 -0.0505 0.0184  341 ILE   A CD1 
5223  N  N   . ASP   A 342 ? 0.1060 0.1210 0.1610 -0.0301 -0.0380 0.0214  342 ASP   A N   
5224  C  CA  . ASP   A 342 ? 0.1162 0.1259 0.1621 -0.0310 -0.0367 0.0230  342 ASP   A CA  
5225  C  C   . ASP   A 342 ? 0.1149 0.1197 0.1583 -0.0303 -0.0395 0.0242  342 ASP   A C   
5226  O  O   . ASP   A 342 ? 0.0957 0.1007 0.1451 -0.0300 -0.0405 0.0229  342 ASP   A O   
5227  C  CB  . ASP   A 342 ? 0.0968 0.1074 0.1433 -0.0322 -0.0329 0.0225  342 ASP   A CB  
5228  C  CG  . ASP   A 342 ? 0.0993 0.1064 0.1401 -0.0323 -0.0325 0.0237  342 ASP   A CG  
5229  O  OD1 . ASP   A 342 ? 0.1262 0.1311 0.1601 -0.0321 -0.0334 0.0246  342 ASP   A OD1 
5230  O  OD2 . ASP   A 342 ? 0.1133 0.1198 0.1511 -0.0329 -0.0312 0.0233  342 ASP   A OD2 
5235  N  N   . THR   A 343 ? 0.0928 0.0951 0.1357 -0.0307 -0.0407 0.0264  343 THR   A N   
5236  C  CA  . THR   A 343 ? 0.1294 0.1257 0.1651 -0.0312 -0.0431 0.0275  343 THR   A CA  
5237  C  C   . THR   A 343 ? 0.1383 0.1335 0.1720 -0.0317 -0.0412 0.0259  343 THR   A C   
5238  O  O   . THR   A 343 ? 0.1252 0.1180 0.1637 -0.0315 -0.0430 0.0251  343 THR   A O   
5239  C  CB  . THR   A 343 ? 0.1188 0.1130 0.1508 -0.0329 -0.0436 0.0300  343 THR   A CB  
5240  O  OG1 . THR   A 343 ? 0.1131 0.1106 0.1420 -0.0330 -0.0403 0.0292  343 THR   A OG1 
5241  C  CG2 . THR   A 343 ? 0.1119 0.1051 0.1451 -0.0328 -0.0472 0.0322  343 THR   A CG2 
5249  N  N   . ILE   A 344 ? 0.1060 0.1050 0.1414 -0.0319 -0.0381 0.0253  344 ILE   A N   
5250  C  CA  . ILE   A 344 ? 0.1119 0.1105 0.1425 -0.0325 -0.0372 0.0241  344 ILE   A CA  
5251  C  C   . ILE   A 344 ? 0.1137 0.1125 0.1482 -0.0322 -0.0378 0.0222  344 ILE   A C   
5252  O  O   . ILE   A 344 ? 0.1017 0.0987 0.1374 -0.0324 -0.0392 0.0205  344 ILE   A O   
5253  C  CB  . ILE   A 344 ? 0.0975 0.0997 0.1288 -0.0326 -0.0350 0.0244  344 ILE   A CB  
5254  C  CG1 . ILE   A 344 ? 0.1302 0.1315 0.1537 -0.0329 -0.0347 0.0256  344 ILE   A CG1 
5255  C  CG2 . ILE   A 344 ? 0.1134 0.1158 0.1393 -0.0331 -0.0353 0.0233  344 ILE   A CG2 
5256  C  CD1 . ILE   A 344 ? 0.1275 0.1315 0.1507 -0.0329 -0.0333 0.0256  344 ILE   A CD1 
5268  N  N   . THR   A 345 ? 0.1104 0.1123 0.1494 -0.0313 -0.0360 0.0215  345 THR   A N   
5269  C  CA  . THR   A 345 ? 0.1229 0.1255 0.1625 -0.0289 -0.0343 0.0189  345 THR   A CA  
5270  C  C   . THR   A 345 ? 0.1343 0.1341 0.1763 -0.0272 -0.0366 0.0174  345 THR   A C   
5271  O  O   . THR   A 345 ? 0.1360 0.1344 0.1784 -0.0251 -0.0360 0.0147  345 THR   A O   
5272  C  CB  . THR   A 345 ? 0.1211 0.1274 0.1619 -0.0288 -0.0307 0.0184  345 THR   A CB  
5273  O  OG1 . THR   A 345 ? 0.1368 0.1427 0.1723 -0.0296 -0.0281 0.0196  345 THR   A OG1 
5274  C  CG2 . THR   A 345 ? 0.0926 0.1015 0.1382 -0.0266 -0.0284 0.0156  345 THR   A CG2 
5282  N  N   . CYS   A 346 ? 0.1221 0.1213 0.1702 -0.0271 -0.0395 0.0189  346 CYS   A N   
5283  C  CA  . CYS   A 346 ? 0.1503 0.1449 0.1975 -0.0245 -0.0423 0.0178  346 CYS   A CA  
5284  C  C   . CYS   A 346 ? 0.1451 0.1329 0.1903 -0.0254 -0.0440 0.0174  346 CYS   A C   
5285  O  O   . CYS   A 346 ? 0.1282 0.1136 0.1744 -0.0230 -0.0439 0.0143  346 CYS   A O   
5286  C  CB  . CYS   A 346 ? 0.1510 0.1452 0.2019 -0.0241 -0.0457 0.0200  346 CYS   A CB  
5287  S  SG  . CYS   A 346 ? 0.1411 0.1294 0.1948 -0.0194 -0.0499 0.0195  346 CYS   A SG  
5293  N  N   . GLY   A 347 ? 0.1592 0.1438 0.1990 -0.0289 -0.0454 0.0199  347 GLY   A N   
5294  C  CA  . GLY   A 347 ? 0.1446 0.1233 0.1832 -0.0312 -0.0466 0.0197  347 GLY   A CA  
5295  C  C   . GLY   A 347 ? 0.1428 0.1230 0.1794 -0.0312 -0.0448 0.0162  347 GLY   A C   
5296  O  O   . GLY   A 347 ? 0.1469 0.1220 0.1824 -0.0310 -0.0460 0.0138  347 GLY   A O   
5300  N  N   . ALA   A 348 ? 0.1412 0.1279 0.1758 -0.0312 -0.0425 0.0158  348 ALA   A N   
5301  C  CA  . ALA   A 348 ? 0.1272 0.1169 0.1624 -0.0308 -0.0411 0.0129  348 ALA   A CA  
5302  C  C   . ALA   A 348 ? 0.1397 0.1285 0.1726 -0.0271 -0.0398 0.0094  348 ALA   A C   
5303  O  O   . ALA   A 348 ? 0.1444 0.1332 0.1752 -0.0264 -0.0393 0.0062  348 ALA   A O   
5304  C  CB  . ALA   A 348 ? 0.1572 0.1519 0.1859 -0.0312 -0.0392 0.0140  348 ALA   A CB  
5310  N  N   . THR   A 349 ? 0.1335 0.1236 0.1719 -0.0247 -0.0388 0.0095  349 THR   A N   
5311  C  CA  . THR   A 349 ? 0.1490 0.1389 0.1856 -0.0210 -0.0373 0.0059  349 THR   A CA  
5312  C  C   . THR   A 349 ? 0.1415 0.1246 0.1824 -0.0199 -0.0402 0.0035  349 THR   A C   
5313  O  O   . THR   A 349 ? 0.1499 0.1316 0.1890 -0.0179 -0.0395 -0.0005 349 THR   A O   
5314  C  CB  . THR   A 349 ? 0.1079 0.1050 0.1574 -0.0188 -0.0351 0.0058  349 THR   A CB  
5315  O  OG1 . THR   A 349 ? 0.1131 0.1138 0.1551 -0.0206 -0.0319 0.0077  349 THR   A OG1 
5316  C  CG2 . THR   A 349 ? 0.1687 0.1656 0.2132 -0.0151 -0.0334 0.0017  349 THR   A CG2 
5324  N  N   . ILE   A 350 ? 0.1318 0.1094 0.1742 -0.0209 -0.0433 0.0062  350 ILE   A N   
5325  C  CA  . ILE   A 350 ? 0.1351 0.1030 0.1765 -0.0202 -0.0462 0.0049  350 ILE   A CA  
5326  C  C   . ILE   A 350 ? 0.1388 0.1036 0.1772 -0.0235 -0.0464 0.0024  350 ILE   A C   
5327  O  O   . ILE   A 350 ? 0.1604 0.1188 0.1958 -0.0223 -0.0473 -0.0015 350 ILE   A O   
5328  C  CB  . ILE   A 350 ? 0.1365 0.0988 0.1830 -0.0212 -0.0495 0.0088  350 ILE   A CB  
5329  C  CG1 . ILE   A 350 ? 0.1780 0.1427 0.2226 -0.0168 -0.0503 0.0103  350 ILE   A CG1 
5330  C  CG2 . ILE   A 350 ? 0.1964 0.1445 0.2329 -0.0212 -0.0521 0.0082  350 ILE   A CG2 
5331  C  CD1 . ILE   A 350 ? 0.1832 0.1433 0.2288 -0.0175 -0.0537 0.0148  350 ILE   A CD1 
5343  N  N   . ALA   A 351 ? 0.1476 0.1160 0.1810 -0.0275 -0.0458 0.0043  351 ALA   A N   
5344  C  CA  . ALA   A 351 ? 0.1365 0.1048 0.1684 -0.0310 -0.0462 0.0016  351 ALA   A CA  
5345  C  C   . ALA   A 351 ? 0.1374 0.1092 0.1684 -0.0284 -0.0447 -0.0033 351 ALA   A C   
5346  O  O   . ALA   A 351 ? 0.1579 0.1257 0.1849 -0.0291 -0.0458 -0.0076 351 ALA   A O   
5347  C  CB  . ALA   A 351 ? 0.1357 0.1097 0.1656 -0.0350 -0.0459 0.0044  351 ALA   A CB  
5353  N  N   . ALA   A 352 ? 0.1458 0.1242 0.1744 -0.0251 -0.0419 -0.0034 352 ALA   A N   
5354  C  CA  . ALA   A 352 ? 0.1403 0.1223 0.1676 -0.0224 -0.0402 -0.0076 352 ALA   A CA  
5355  C  C   . ALA   A 352 ? 0.1373 0.1135 0.1651 -0.0193 -0.0404 -0.0121 352 ALA   A C   
5356  O  O   . ALA   A 352 ? 0.1349 0.1100 0.1607 -0.0186 -0.0406 -0.0170 352 ALA   A O   
5357  C  CB  . ALA   A 352 ? 0.1481 0.1369 0.1734 -0.0201 -0.0366 -0.0059 352 ALA   A CB  
5363  N  N   . ALA   A 353 ? 0.1238 0.0975 0.1595 -0.0170 -0.0407 -0.0109 353 ALA   A N   
5364  C  CA  . ALA   A 353 ? 0.1632 0.1303 0.1983 -0.0131 -0.0417 -0.0148 353 ALA   A CA  
5365  C  C   . ALA   A 353 ? 0.1714 0.1275 0.2029 -0.0152 -0.0447 -0.0174 353 ALA   A C   
5366  O  O   . ALA   A 353 ? 0.1574 0.1100 0.1907 -0.0132 -0.0449 -0.0228 353 ALA   A O   
5367  C  CB  . ALA   A 353 ? 0.1792 0.1454 0.2197 -0.0098 -0.0423 -0.0128 353 ALA   A CB  
5373  N  N   . MET   A 354 ? 0.1504 0.1030 0.1846 -0.0203 -0.0469 -0.0137 354 MET   A N   
5374  C  CA  . MET   A 354 ? 0.1647 0.1061 0.1944 -0.0237 -0.0494 -0.0154 354 MET   A CA  
5375  C  C   . MET   A 354 ? 0.1786 0.1235 0.2057 -0.0260 -0.0489 -0.0209 354 MET   A C   
5376  O  O   . MET   A 354 ? 0.2022 0.1387 0.2269 -0.0268 -0.0503 -0.0256 354 MET   A O   
5377  C  CB  . MET   A 354 ? 0.1532 0.0913 0.1849 -0.0294 -0.0510 -0.0099 354 MET   A CB  
5378  C  CG  . MET   A 354 ? 0.1832 0.1137 0.2134 -0.0275 -0.0526 -0.0052 354 MET   A CG  
5379  S  SD  . MET   A 354 ? 0.1940 0.1212 0.2251 -0.0341 -0.0540 0.0014  354 MET   A SD  
5380  C  CE  . MET   A 354 ? 0.2539 0.1669 0.2798 -0.0298 -0.0566 0.0052  354 MET   A CE  
5390  N  N   . GLU   A 355 ? 0.1687 0.1252 0.1947 -0.0267 -0.0472 -0.0206 355 GLU   A N   
5391  C  CA  . GLU   A 355 ? 0.1765 0.1375 0.1965 -0.0278 -0.0472 -0.0256 355 GLU   A CA  
5392  C  C   . GLU   A 355 ? 0.1796 0.1404 0.1972 -0.0227 -0.0459 -0.0314 355 GLU   A C   
5393  O  O   . GLU   A 355 ? 0.1537 0.1126 0.1719 -0.0234 -0.0470 -0.0374 355 GLU   A O   
5394  C  CB  . GLU   A 355 ? 0.1542 0.1270 0.1753 -0.0290 -0.0465 -0.0234 355 GLU   A CB  
5395  C  CG  . GLU   A 355 ? 0.1777 0.1557 0.1913 -0.0290 -0.0471 -0.0284 355 GLU   A CG  
5396  C  CD  . GLU   A 355 ? 0.1775 0.1642 0.1888 -0.0316 -0.0483 -0.0271 355 GLU   A CD  
5397  O  OE1 . GLU   A 355 ? 0.1502 0.1411 0.1656 -0.0318 -0.0473 -0.0216 355 GLU   A OE1 
5398  O  OE2 . GLU   A 355 ? 0.1707 0.1613 0.1820 -0.0333 -0.0501 -0.0318 355 GLU   A OE2 
5405  N  N   . LEU   A 356 ? 0.1645 0.1299 0.1880 -0.0179 -0.0431 -0.0303 356 LEU   A N   
5406  C  CA  . LEU   A 356 ? 0.2024 0.1678 0.2203 -0.0128 -0.0410 -0.0355 356 LEU   A CA  
5407  C  C   . LEU   A 356 ? 0.2040 0.1584 0.2249 -0.0117 -0.0432 -0.0404 356 LEU   A C   
5408  O  O   . LEU   A 356 ? 0.2020 0.1555 0.2209 -0.0097 -0.0426 -0.0470 356 LEU   A O   
5409  C  CB  . LEU   A 356 ? 0.1914 0.1628 0.2124 -0.0089 -0.0375 -0.0329 356 LEU   A CB  
5410  C  CG  . LEU   A 356 ? 0.1435 0.1268 0.1702 -0.0094 -0.0344 -0.0294 356 LEU   A CG  
5411  C  CD1 . LEU   A 356 ? 0.1963 0.1827 0.2175 -0.0063 -0.0307 -0.0276 356 LEU   A CD1 
5412  C  CD2 . LEU   A 356 ? 0.1841 0.1698 0.1945 -0.0089 -0.0331 -0.0329 356 LEU   A CD2 
5424  N  N   . TYR   A 357 ? 0.1948 0.1408 0.2215 -0.0124 -0.0454 -0.0373 357 TYR   A N   
5425  C  CA  . TYR   A 357 ? 0.2100 0.1414 0.2337 -0.0112 -0.0477 -0.0409 357 TYR   A CA  
5426  C  C   . TYR   A 357 ? 0.1858 0.1126 0.2106 -0.0170 -0.0497 -0.0451 357 TYR   A C   
5427  O  O   . TYR   A 357 ? 0.1948 0.1147 0.2152 -0.0153 -0.0502 -0.0517 357 TYR   A O   
5428  C  CB  . TYR   A 357 ? 0.1970 0.1198 0.2280 -0.0108 -0.0500 -0.0359 357 TYR   A CB  
5429  C  CG  . TYR   A 357 ? 0.2154 0.1216 0.2448 -0.0093 -0.0525 -0.0392 357 TYR   A CG  
5430  C  CD1 . TYR   A 357 ? 0.2276 0.1307 0.2598 -0.0019 -0.0523 -0.0440 357 TYR   A CD1 
5431  C  CD2 . TYR   A 357 ? 0.2232 0.1171 0.2505 -0.0154 -0.0551 -0.0384 357 TYR   A CD2 
5432  C  CE1 . TYR   A 357 ? 0.2525 0.1389 0.2816 0.0004  -0.0548 -0.0475 357 TYR   A CE1 
5433  C  CE2 . TYR   A 357 ? 0.2426 0.1193 0.2671 -0.0141 -0.0572 -0.0413 357 TYR   A CE2 
5434  C  CZ  . TYR   A 357 ? 0.2457 0.1186 0.2747 -0.0060 -0.0574 -0.0460 357 TYR   A CZ  
5435  O  OH  . TYR   A 357 ? 0.2818 0.1358 0.3054 -0.0038 -0.0597 -0.0491 357 TYR   A OH  
5445  N  N   . GLN   A 358 ? 0.2013 0.1299 0.2216 -0.0232 -0.0509 -0.0414 358 GLN   A N   
5446  C  CA  . GLN   A 358 ? 0.1906 0.1174 0.2122 -0.0295 -0.0526 -0.0453 358 GLN   A CA  
5447  C  C   . GLN   A 358 ? 0.2056 0.1370 0.2196 -0.0276 -0.0521 -0.0531 358 GLN   A C   
5448  O  O   . GLN   A 358 ? 0.1910 0.1165 0.2054 -0.0301 -0.0538 -0.0594 358 GLN   A O   
5449  C  CB  . GLN   A 358 ? 0.2203 0.1543 0.2399 -0.0354 -0.0530 -0.0408 358 GLN   A CB  
5450  C  CG  . GLN   A 358 ? 0.2554 0.1925 0.2696 -0.0414 -0.0545 -0.0452 358 GLN   A CG  
5451  C  CD  . GLN   A 358 ? 0.2163 0.1663 0.2359 -0.0452 -0.0545 -0.0417 358 GLN   A CD  
5452  O  OE1 . GLN   A 358 ? 0.1970 0.1470 0.2185 -0.0468 -0.0540 -0.0350 358 GLN   A OE1 
5453  N  NE2 . GLN   A 358 ? 0.2188 0.1789 0.2352 -0.0462 -0.0554 -0.0459 358 GLN   A NE2 
5462  N  N   . ARG   A 359 ? 0.2057 0.1496 0.2200 -0.0232 -0.0497 -0.0532 359 ARG   A N   
5463  C  CA  . ARG   A 359 ? 0.2247 0.1748 0.2302 -0.0213 -0.0489 -0.0593 359 ARG   A CA  
5464  C  C   . ARG   A 359 ? 0.2339 0.1824 0.2410 -0.0148 -0.0468 -0.0645 359 ARG   A C   
5465  O  O   . ARG   A 359 ? 0.2345 0.1899 0.2365 -0.0123 -0.0453 -0.0690 359 ARG   A O   
5466  C  CB  . ARG   A 359 ? 0.1754 0.1406 0.1854 -0.0212 -0.0478 -0.0558 359 ARG   A CB  
5467  C  CG  . ARG   A 359 ? 0.2264 0.1940 0.2302 -0.0268 -0.0500 -0.0518 359 ARG   A CG  
5468  C  CD  . ARG   A 359 ? 0.2261 0.2062 0.2270 -0.0259 -0.0493 -0.0491 359 ARG   A CD  
5469  N  NE  . ARG   A 359 ? 0.1844 0.1706 0.1936 -0.0307 -0.0516 -0.0465 359 ARG   A NE  
5470  C  CZ  . ARG   A 359 ? 0.2405 0.2292 0.2416 -0.0345 -0.0546 -0.0507 359 ARG   A CZ  
5471  N  NH1 . ARG   A 359 ? 0.2622 0.2514 0.2618 -0.0341 -0.0559 -0.0581 359 ARG   A NH1 
5472  N  NH2 . ARG   A 359 ? 0.2122 0.2069 0.2207 -0.0389 -0.0561 -0.0482 359 ARG   A NH2 
5486  N  N   . GLY   A 360 ? 0.2390 0.1784 0.2508 -0.0117 -0.0465 -0.0641 360 GLY   A N   
5487  C  CA  . GLY   A 360 ? 0.2510 0.1878 0.2641 -0.0055 -0.0449 -0.0700 360 GLY   A CA  
5488  C  C   . GLY   A 360 ? 0.2868 0.2318 0.2910 0.0003  -0.0406 -0.0690 360 GLY   A C   
5489  O  O   . GLY   A 360 ? 0.2204 0.1684 0.2358 0.0054  -0.0384 -0.0749 360 GLY   A O   
5493  N  N   . TYR   A 361 ? 0.2145 0.1717 0.2344 -0.0008 -0.0388 -0.0619 361 TYR   A N   
5494  C  CA  . TYR   A 361 ? 0.2711 0.2352 0.2789 0.0035  -0.0343 -0.0604 361 TYR   A CA  
5495  C  C   . TYR   A 361 ? 0.2366 0.2002 0.2618 0.0079  -0.0336 -0.0597 361 TYR   A C   
5496  O  O   . TYR   A 361 ? 0.2521 0.2204 0.2761 0.0128  -0.0302 -0.0630 361 TYR   A O   
5497  C  CB  . TYR   A 361 ? 0.2164 0.1916 0.2312 0.0006  -0.0326 -0.0538 361 TYR   A CB  
5498  C  CG  . TYR   A 361 ? 0.2163 0.1965 0.2204 -0.0017 -0.0325 -0.0548 361 TYR   A CG  
5499  C  CD1 . TYR   A 361 ? 0.2333 0.2210 0.2302 0.0009  -0.0286 -0.0572 361 TYR   A CD1 
5500  C  CD2 . TYR   A 361 ? 0.2120 0.1906 0.2146 -0.0063 -0.0363 -0.0535 361 TYR   A CD2 
5501  C  CE1 . TYR   A 361 ? 0.2526 0.2445 0.2400 -0.0003 -0.0292 -0.0579 361 TYR   A CE1 
5502  C  CE2 . TYR   A 361 ? 0.2335 0.2177 0.2276 -0.0076 -0.0370 -0.0549 361 TYR   A CE2 
5503  C  CZ  . TYR   A 361 ? 0.2572 0.2482 0.2445 -0.0043 -0.0337 -0.0570 361 TYR   A CZ  
5504  O  OH  . TYR   A 361 ? 0.2983 0.2940 0.2746 -0.0049 -0.0350 -0.0579 361 TYR   A OH  
5514  N  N   . ILE   A 362 ? 0.2338 0.1891 0.2621 0.0064  -0.0370 -0.0552 362 ILE   A N   
5515  C  CA  . ILE   A 362 ? 0.2447 0.1953 0.2771 0.0110  -0.0380 -0.0540 362 ILE   A CA  
5516  C  C   . ILE   A 362 ? 0.2383 0.1750 0.2748 0.0132  -0.0414 -0.0589 362 ILE   A C   
5517  O  O   . ILE   A 362 ? 0.2620 0.1878 0.2929 0.0083  -0.0446 -0.0579 362 ILE   A O   
5518  C  CB  . ILE   A 362 ? 0.2130 0.1650 0.2534 0.0085  -0.0395 -0.0458 362 ILE   A CB  
5519  C  CG1 . ILE   A 362 ? 0.2059 0.1708 0.2451 0.0062  -0.0362 -0.0412 362 ILE   A CG1 
5520  C  CG2 . ILE   A 362 ? 0.2215 0.1692 0.2667 0.0138  -0.0414 -0.0448 362 ILE   A CG2 
5521  C  CD1 . ILE   A 362 ? 0.2179 0.1827 0.2571 0.0023  -0.0379 -0.0336 362 ILE   A CD1 
5533  N  N   . LYS   A 363 ? 0.2364 0.1709 0.2738 0.0203  -0.0407 -0.0644 363 LYS   A N   
5534  C  CA  . LYS   A 363 ? 0.2108 0.1315 0.2544 0.0237  -0.0437 -0.0696 363 LYS   A CA  
5535  C  C   . LYS   A 363 ? 0.2322 0.1425 0.2776 0.0268  -0.0475 -0.0651 363 LYS   A C   
5536  O  O   . LYS   A 363 ? 0.2537 0.1715 0.3014 0.0287  -0.0471 -0.0600 363 LYS   A O   
5537  C  CB  . LYS   A 363 ? 0.2628 0.1859 0.3020 0.0304  -0.0410 -0.0788 363 LYS   A CB  
5538  C  CG  . LYS   A 363 ? 0.3204 0.2537 0.3509 0.0282  -0.0370 -0.0834 363 LYS   A CG  
5539  C  CD  . LYS   A 363 ? 0.3232 0.2516 0.3524 0.0214  -0.0391 -0.0848 363 LYS   A CD  
5540  C  CE  . LYS   A 363 ? 0.4028 0.3390 0.4196 0.0208  -0.0361 -0.0906 363 LYS   A CE  
5541  N  NZ  . LYS   A 363 ? 0.4457 0.3760 0.4558 0.0150  -0.0390 -0.0935 363 LYS   A NZ  
5555  N  N   . ASP   A 364 ? 0.2708 0.1623 0.3114 0.0276  -0.0513 -0.0666 364 ASP   A N   
5556  C  CA  . ASP   A 364 ? 0.2867 0.1661 0.3307 0.0312  -0.0555 -0.0625 364 ASP   A CA  
5557  C  C   . ASP   A 364 ? 0.2831 0.1710 0.3351 0.0410  -0.0549 -0.0643 364 ASP   A C   
5558  O  O   . ASP   A 364 ? 0.2655 0.1539 0.3223 0.0434  -0.0573 -0.0582 364 ASP   A O   
5559  C  CB  . ASP   A 364 ? 0.3020 0.1591 0.3428 0.0312  -0.0589 -0.0652 364 ASP   A CB  
5560  C  CG  . ASP   A 364 ? 0.3467 0.1933 0.3774 0.0207  -0.0602 -0.0626 364 ASP   A CG  
5561  O  OD1 . ASP   A 364 ? 0.3132 0.1674 0.3472 0.0147  -0.0599 -0.0554 364 ASP   A OD1 
5562  O  OD2 . ASP   A 364 ? 0.3821 0.2156 0.4092 0.0187  -0.0612 -0.0679 364 ASP   A OD2 
5567  N  N   . GLU   A 365 ? 0.2924 0.1882 0.3486 0.0468  -0.0518 -0.0724 365 GLU   A N   
5568  C  CA  . GLU   A 365 ? 0.3228 0.2275 0.3858 0.0566  -0.0508 -0.0760 365 GLU   A CA  
5569  C  C   . GLU   A 365 ? 0.2451 0.1693 0.3197 0.0556  -0.0487 -0.0704 365 GLU   A C   
5570  O  O   . GLU   A 365 ? 0.2651 0.1927 0.3417 0.0622  -0.0503 -0.0696 365 GLU   A O   
5571  C  CB  . GLU   A 365 ? 0.4174 0.3282 0.4847 0.0618  -0.0471 -0.0864 365 GLU   A CB  
5572  C  CG  . GLU   A 365 ? 0.5750 0.4665 0.6341 0.0645  -0.0496 -0.0932 365 GLU   A CG  
5573  C  CD  . GLU   A 365 ? 0.7190 0.6149 0.7746 0.0693  -0.0458 -0.1042 365 GLU   A CD  
5574  O  OE1 . GLU   A 365 ? 0.8110 0.7258 0.8680 0.0691  -0.0404 -0.1064 365 GLU   A OE1 
5575  O  OE2 . GLU   A 365 ? 0.6956 0.5770 0.7531 0.0730  -0.0480 -0.1106 365 GLU   A OE2 
5582  N  N   . GLU   A 366 ? 0.2446 0.1778 0.3116 0.0477  -0.0453 -0.0667 366 GLU   A N   
5583  C  CA  . GLU   A 366 ? 0.2444 0.1946 0.3163 0.0457  -0.0425 -0.0619 366 GLU   A CA  
5584  C  C   . GLU   A 366 ? 0.2681 0.2124 0.3359 0.0447  -0.0471 -0.0540 366 GLU   A C   
5585  O  O   . GLU   A 366 ? 0.2157 0.1745 0.2993 0.0464  -0.0462 -0.0515 366 GLU   A O   
5586  C  CB  . GLU   A 366 ? 0.2276 0.1877 0.2968 0.0382  -0.0379 -0.0603 366 GLU   A CB  
5587  C  CG  . GLU   A 366 ? 0.2626 0.2375 0.3349 0.0352  -0.0349 -0.0553 366 GLU   A CG  
5588  C  CD  . GLU   A 366 ? 0.3473 0.3325 0.4048 0.0319  -0.0285 -0.0567 366 GLU   A CD  
5589  O  OE1 . GLU   A 366 ? 0.2375 0.2227 0.3022 0.0294  -0.0274 -0.0592 366 GLU   A OE1 
5590  O  OE2 . GLU   A 366 ? 0.3422 0.3427 0.4146 0.0318  -0.0249 -0.0554 366 GLU   A OE2 
5597  N  N   . ILE   A 367 ? 0.2150 0.1445 0.2863 0.0416  -0.0515 -0.0498 367 ILE   A N   
5598  C  CA  . ILE   A 367 ? 0.2196 0.1439 0.2904 0.0398  -0.0557 -0.0416 367 ILE   A CA  
5599  C  C   . ILE   A 367 ? 0.2577 0.1658 0.3262 0.0467  -0.0614 -0.0413 367 ILE   A C   
5600  O  O   . ILE   A 367 ? 0.2984 0.2008 0.3643 0.0460  -0.0652 -0.0344 367 ILE   A O   
5601  C  CB  . ILE   A 367 ? 0.2450 0.1631 0.3033 0.0299  -0.0559 -0.0358 367 ILE   A CB  
5602  C  CG1 . ILE   A 367 ? 0.2474 0.1510 0.3001 0.0263  -0.0568 -0.0384 367 ILE   A CG1 
5603  C  CG2 . ILE   A 367 ? 0.2184 0.1534 0.2807 0.0245  -0.0514 -0.0340 367 ILE   A CG2 
5604  C  CD1 . ILE   A 367 ? 0.2369 0.1343 0.2846 0.0171  -0.0577 -0.0331 367 ILE   A CD1 
5616  N  N   . ALA   A 368 ? 0.2494 0.1499 0.3198 0.0534  -0.0621 -0.0480 368 ALA   A N   
5617  C  CA  . ALA   A 368 ? 0.2598 0.1435 0.3330 0.0606  -0.0677 -0.0482 368 ALA   A CA  
5618  C  C   . ALA   A 368 ? 0.3078 0.1982 0.3825 0.0680  -0.0709 -0.0452 368 ALA   A C   
5619  O  O   . ALA   A 368 ? 0.2928 0.1708 0.3669 0.0701  -0.0763 -0.0396 368 ALA   A O   
5620  C  CB  . ALA   A 368 ? 0.3080 0.1819 0.3743 0.0669  -0.0674 -0.0568 368 ALA   A CB  
5626  N  N   . GLY   A 369 ? 0.3367 0.2486 0.4208 0.0716  -0.0676 -0.0489 369 GLY   A N   
5627  C  CA  . GLY   A 369 ? 0.3191 0.2429 0.4148 0.0782  -0.0704 -0.0473 369 GLY   A CA  
5628  C  C   . GLY   A 369 ? 0.3201 0.2442 0.4093 0.0727  -0.0729 -0.0384 369 GLY   A C   
5629  O  O   . GLY   A 369 ? 0.3121 0.2393 0.4095 0.0786  -0.0776 -0.0357 369 GLY   A O   
5633  N  N   . ASP   A 370 ? 0.2537 0.1786 0.3445 0.0619  -0.0703 -0.0335 370 ASP   A N   
5634  C  CA  . ASP   A 370 ? 0.2842 0.2076 0.3630 0.0560  -0.0721 -0.0252 370 ASP   A CA  
5635  C  C   . ASP   A 370 ? 0.2865 0.1897 0.3627 0.0551  -0.0776 -0.0189 370 ASP   A C   
5636  O  O   . ASP   A 370 ? 0.3292 0.2307 0.3978 0.0526  -0.0803 -0.0122 370 ASP   A O   
5637  C  CB  . ASP   A 370 ? 0.2412 0.1746 0.3235 0.0456  -0.0669 -0.0231 370 ASP   A CB  
5638  C  CG  . ASP   A 370 ? 0.2421 0.1969 0.3333 0.0452  -0.0613 -0.0274 370 ASP   A CG  
5639  O  OD1 . ASP   A 370 ? 0.3021 0.2685 0.3928 0.0454  -0.0611 -0.0255 370 ASP   A OD1 
5640  O  OD2 . ASP   A 370 ? 0.2599 0.2169 0.3460 0.0443  -0.0569 -0.0324 370 ASP   A OD2 
5645  N  N   . ASN   A 371 ? 0.3063 0.1905 0.3733 0.0566  -0.0788 -0.0211 371 ASN   A N   
5646  C  CA  . ASN   A 371 ? 0.3251 0.1861 0.3822 0.0549  -0.0833 -0.0153 371 ASN   A CA  
5647  C  C   . ASN   A 371 ? 0.3023 0.1616 0.3524 0.0430  -0.0814 -0.0090 371 ASN   A C   
5648  O  O   . ASN   A 371 ? 0.3216 0.1711 0.3632 0.0401  -0.0838 -0.0019 371 ASN   A O   
5649  C  CB  . ASN   A 371 ? 0.3662 0.2265 0.4266 0.0617  -0.0873 -0.0118 371 ASN   A CB  
5650  C  CG  . ASN   A 371 ? 0.4935 0.3583 0.5579 0.0731  -0.0885 -0.0182 371 ASN   A CG  
5651  O  OD1 . ASN   A 371 ? 0.5896 0.4523 0.6513 0.0759  -0.0863 -0.0254 371 ASN   A OD1 
5652  N  ND2 . ASN   A 371 ? 0.5510 0.4209 0.6142 0.0795  -0.0918 -0.0162 371 ASN   A ND2 
5659  N  N   . LEU   A 372 ? 0.2648 0.1372 0.3181 0.0359  -0.0762 -0.0110 372 LEU   A N   
5660  C  CA  . LEU   A 372 ? 0.2752 0.1475 0.3206 0.0250  -0.0740 -0.0062 372 LEU   A CA  
5661  C  C   . LEU   A 372 ? 0.2701 0.1412 0.3138 0.0193  -0.0703 -0.0108 372 LEU   A C   
5662  O  O   . LEU   A 372 ? 0.2925 0.1697 0.3385 0.0231  -0.0681 -0.0176 372 LEU   A O   
5663  C  CB  . LEU   A 372 ? 0.2802 0.1711 0.3285 0.0224  -0.0721 -0.0031 372 LEU   A CB  
5664  C  CG  . LEU   A 372 ? 0.2504 0.1472 0.3048 0.0272  -0.0756 0.0010  372 LEU   A CG  
5665  C  CD1 . LEU   A 372 ? 0.2254 0.1417 0.2852 0.0243  -0.0726 0.0019  372 LEU   A CD1 
5666  C  CD2 . LEU   A 372 ? 0.2733 0.1542 0.3175 0.0251  -0.0797 0.0082  372 LEU   A CD2 
5678  N  N   . SER   A 373 ? 0.2600 0.1244 0.2965 0.0100  -0.0695 -0.0075 373 SER   A N   
5679  C  CA  . SER   A 373 ? 0.2482 0.1135 0.2840 0.0038  -0.0665 -0.0119 373 SER   A CA  
5680  C  C   . SER   A 373 ? 0.2486 0.1303 0.2812 -0.0016 -0.0629 -0.0108 373 SER   A C   
5681  O  O   . SER   A 373 ? 0.2025 0.0942 0.2423 -0.0020 -0.0629 -0.0061 373 SER   A O   
5682  C  CB  . SER   A 373 ? 0.2752 0.1218 0.2991 -0.0028 -0.0678 -0.0102 373 SER   A CB  
5683  O  OG  . SER   A 373 ? 0.2399 0.0925 0.2657 -0.0120 -0.0662 -0.0059 373 SER   A OG  
5689  N  N   . LEU   A 374 ? 0.2325 0.1190 0.2653 -0.0058 -0.0603 -0.0153 374 LEU   A N   
5690  C  CA  . LEU   A 374 ? 0.1823 0.0846 0.2228 -0.0111 -0.0574 -0.0143 374 LEU   A CA  
5691  C  C   . LEU   A 374 ? 0.2261 0.1202 0.2515 -0.0192 -0.0575 -0.0147 374 LEU   A C   
5692  O  O   . LEU   A 374 ? 0.2045 0.1092 0.2346 -0.0223 -0.0555 -0.0175 374 LEU   A O   
5693  C  CB  . LEU   A 374 ? 0.2177 0.1318 0.2534 -0.0073 -0.0543 -0.0192 374 LEU   A CB  
5694  C  CG  . LEU   A 374 ? 0.2134 0.1396 0.2560 -0.0022 -0.0527 -0.0179 374 LEU   A CG  
5695  C  CD1 . LEU   A 374 ? 0.2255 0.1624 0.2696 0.0010  -0.0490 -0.0234 374 LEU   A CD1 
5696  C  CD2 . LEU   A 374 ? 0.1921 0.1261 0.2364 -0.0061 -0.0522 -0.0116 374 LEU   A CD2 
5708  N  N   . LYS   A 375 ? 0.2031 0.0836 0.2318 -0.0227 -0.0597 -0.0120 375 LYS   A N   
5709  C  CA  . LYS   A 375 ? 0.2338 0.1080 0.2548 -0.0312 -0.0592 -0.0126 375 LYS   A CA  
5710  C  C   . LYS   A 375 ? 0.2278 0.1120 0.2504 -0.0369 -0.0572 -0.0066 375 LYS   A C   
5711  O  O   . LYS   A 375 ? 0.2418 0.1239 0.2610 -0.0355 -0.0579 -0.0005 375 LYS   A O   
5712  C  CB  . LYS   A 375 ? 0.2524 0.1108 0.2709 -0.0312 -0.0594 -0.0131 375 LYS   A CB  
5713  C  CG  . LYS   A 375 ? 0.2914 0.1407 0.3131 -0.0255 -0.0607 -0.0195 375 LYS   A CG  
5714  C  CD  . LYS   A 375 ? 0.4112 0.2428 0.4250 -0.0226 -0.0617 -0.0183 375 LYS   A CD  
5715  C  CE  . LYS   A 375 ? 0.5218 0.3441 0.5324 -0.0158 -0.0630 -0.0253 375 LYS   A CE  
5716  N  NZ  . LYS   A 375 ? 0.5398 0.3689 0.5553 -0.0180 -0.0617 -0.0335 375 LYS   A NZ  
5730  N  N   . TRP   A 376 ? 0.2465 0.1402 0.2660 -0.0424 -0.0549 -0.0083 376 TRP   A N   
5731  C  CA  . TRP   A 376 ? 0.2449 0.1475 0.2629 -0.0471 -0.0524 -0.0037 376 TRP   A CA  
5732  C  C   . TRP   A 376 ? 0.2250 0.1181 0.2401 -0.0494 -0.0516 0.0016  376 TRP   A C   
5733  O  O   . TRP   A 376 ? 0.2382 0.1191 0.2501 -0.0507 -0.0517 -0.0002 376 TRP   A O   
5734  C  CB  . TRP   A 376 ? 0.2349 0.1478 0.2548 -0.0524 -0.0502 -0.0076 376 TRP   A CB  
5735  C  CG  . TRP   A 376 ? 0.2217 0.1439 0.2436 -0.0505 -0.0512 -0.0129 376 TRP   A CG  
5736  C  CD1 . TRP   A 376 ? 0.2363 0.1568 0.2558 -0.0508 -0.0520 -0.0199 376 TRP   A CD1 
5737  C  CD2 . TRP   A 376 ? 0.1879 0.1228 0.2147 -0.0480 -0.0514 -0.0117 376 TRP   A CD2 
5738  N  NE1 . TRP   A 376 ? 0.1984 0.1303 0.2241 -0.0484 -0.0531 -0.0229 376 TRP   A NE1 
5739  C  CE2 . TRP   A 376 ? 0.2118 0.1502 0.2317 -0.0467 -0.0527 -0.0179 376 TRP   A CE2 
5740  C  CE3 . TRP   A 376 ? 0.1814 0.1223 0.2066 -0.0467 -0.0507 -0.0062 376 TRP   A CE3 
5741  C  CZ2 . TRP   A 376 ? 0.1529 0.1057 0.1819 -0.0428 -0.0512 -0.0174 376 TRP   A CZ2 
5742  C  CZ3 . TRP   A 376 ? 0.1695 0.1213 0.1974 -0.0441 -0.0505 -0.0065 376 TRP   A CZ3 
5743  C  CH2 . TRP   A 376 ? 0.1841 0.1410 0.2077 -0.0417 -0.0502 -0.0117 376 TRP   A CH2 
5754  N  N   . GLY   A 377 ? 0.1884 0.0873 0.2077 -0.0498 -0.0510 0.0073  377 GLY   A N   
5755  C  CA  . GLY   A 377 ? 0.2627 0.1514 0.2687 -0.0522 -0.0502 0.0123  377 GLY   A CA  
5756  C  C   . GLY   A 377 ? 0.2713 0.1473 0.2753 -0.0470 -0.0533 0.0155  377 GLY   A C   
5757  O  O   . GLY   A 377 ? 0.2640 0.1337 0.2658 -0.0485 -0.0528 0.0202  377 GLY   A O   
5761  N  N   . ASP   A 378 ? 0.2358 0.1094 0.2483 -0.0407 -0.0564 0.0133  378 ASP   A N   
5762  C  CA  . ASP   A 378 ? 0.2644 0.1266 0.2718 -0.0339 -0.0600 0.0156  378 ASP   A CA  
5763  C  C   . ASP   A 378 ? 0.2486 0.1192 0.2587 -0.0317 -0.0615 0.0207  378 ASP   A C   
5764  O  O   . ASP   A 378 ? 0.2248 0.1011 0.2413 -0.0267 -0.0637 0.0194  378 ASP   A O   
5765  C  CB  . ASP   A 378 ? 0.2819 0.1377 0.2935 -0.0272 -0.0625 0.0106  378 ASP   A CB  
5766  C  CG  . ASP   A 378 ? 0.2939 0.1379 0.3016 -0.0195 -0.0659 0.0124  378 ASP   A CG  
5767  O  OD1 . ASP   A 378 ? 0.2653 0.1072 0.2730 -0.0196 -0.0669 0.0181  378 ASP   A OD1 
5768  O  OD2 . ASP   A 378 ? 0.2725 0.1123 0.2872 -0.0131 -0.0679 0.0076  378 ASP   A OD2 
5773  N  N   . THR   A 379 ? 0.2656 0.1366 0.2702 -0.0353 -0.0602 0.0257  379 THR   A N   
5774  C  CA  . THR   A 379 ? 0.2775 0.1562 0.2807 -0.0341 -0.0615 0.0302  379 THR   A CA  
5775  C  C   . THR   A 379 ? 0.2382 0.1144 0.2496 -0.0258 -0.0661 0.0314  379 THR   A C   
5776  O  O   . THR   A 379 ? 0.2615 0.1466 0.2732 -0.0232 -0.0675 0.0318  379 THR   A O   
5777  C  CB  . THR   A 379 ? 0.2963 0.1733 0.2906 -0.0389 -0.0594 0.0349  379 THR   A CB  
5778  O  OG1 . THR   A 379 ? 0.2440 0.1238 0.2428 -0.0455 -0.0553 0.0328  379 THR   A OG1 
5779  C  CG2 . THR   A 379 ? 0.2912 0.1799 0.2895 -0.0393 -0.0597 0.0381  379 THR   A CG2 
5787  N  N   . GLU   A 380 ? 0.2610 0.1231 0.2660 -0.0215 -0.0684 0.0318  380 GLU   A N   
5788  C  CA  . GLU   A 380 ? 0.3043 0.1632 0.3090 -0.0125 -0.0730 0.0326  380 GLU   A CA  
5789  C  C   . GLU   A 380 ? 0.2617 0.1293 0.2809 -0.0070 -0.0744 0.0277  380 GLU   A C   
5790  O  O   . GLU   A 380 ? 0.2597 0.1347 0.2813 -0.0016 -0.0771 0.0284  380 GLU   A O   
5791  C  CB  . GLU   A 380 ? 0.3587 0.2021 0.3605 -0.0083 -0.0748 0.0333  380 GLU   A CB  
5792  C  CG  . GLU   A 380 ? 0.4402 0.2816 0.4421 0.0005  -0.0793 0.0353  380 GLU   A CG  
5793  C  CD  . GLU   A 380 ? 0.5620 0.3855 0.5518 0.0044  -0.0809 0.0369  380 GLU   A CD  
5794  O  OE1 . GLU   A 380 ? 0.5994 0.4134 0.5819 -0.0017 -0.0784 0.0402  380 GLU   A OE1 
5795  O  OE2 . GLU   A 380 ? 0.5848 0.4057 0.5794 0.0135  -0.0843 0.0347  380 GLU   A OE2 
5802  N  N   . SER   A 381 ? 0.2804 0.1455 0.2985 -0.0082 -0.0726 0.0223  381 SER   A N   
5803  C  CA  . SER   A 381 ? 0.2686 0.1438 0.2954 -0.0033 -0.0720 0.0164  381 SER   A CA  
5804  C  C   . SER   A 381 ? 0.2292 0.1240 0.2636 -0.0064 -0.0688 0.0165  381 SER   A C   
5805  O  O   . SER   A 381 ? 0.2243 0.1309 0.2637 -0.0013 -0.0683 0.0144  381 SER   A O   
5806  C  CB  . SER   A 381 ? 0.2672 0.1375 0.2970 -0.0039 -0.0703 0.0101  381 SER   A CB  
5807  O  OG  . SER   A 381 ? 0.2908 0.1442 0.3160 0.0011  -0.0732 0.0086  381 SER   A OG  
5813  N  N   . MET   A 382 ? 0.2290 0.1258 0.2583 -0.0146 -0.0665 0.0189  382 MET   A N   
5814  C  CA  . MET   A 382 ? 0.2282 0.1413 0.2607 -0.0177 -0.0637 0.0197  382 MET   A CA  
5815  C  C   . MET   A 382 ? 0.2199 0.1399 0.2561 -0.0141 -0.0655 0.0231  382 MET   A C   
5816  O  O   . MET   A 382 ? 0.2177 0.1503 0.2579 -0.0119 -0.0638 0.0206  382 MET   A O   
5817  C  CB  . MET   A 382 ? 0.2495 0.1618 0.2748 -0.0261 -0.0617 0.0222  382 MET   A CB  
5818  C  CG  . MET   A 382 ? 0.2261 0.1531 0.2545 -0.0290 -0.0593 0.0233  382 MET   A CG  
5819  S  SD  . MET   A 382 ? 0.1969 0.1271 0.2232 -0.0362 -0.0566 0.0263  382 MET   A SD  
5820  C  CE  . MET   A 382 ? 0.2455 0.1686 0.2613 -0.0358 -0.0588 0.0320  382 MET   A CE  
5830  N  N   A ILE   A 383 ? 0.2380 0.1486 0.2667 -0.0142 -0.0688 0.0280  383 ILE   A N   
5831  N  N   B ILE   A 383 ? 0.2380 0.1486 0.2667 -0.0142 -0.0688 0.0280  383 ILE   A N   
5832  C  CA  A ILE   A 383 ? 0.2335 0.1502 0.2645 -0.0109 -0.0714 0.0312  383 ILE   A CA  
5833  C  CA  B ILE   A 383 ? 0.2335 0.1502 0.2645 -0.0109 -0.0714 0.0312  383 ILE   A CA  
5834  C  C   A ILE   A 383 ? 0.2055 0.1285 0.2473 -0.0022 -0.0732 0.0273  383 ILE   A C   
5835  C  C   B ILE   A 383 ? 0.2055 0.1285 0.2473 -0.0022 -0.0732 0.0273  383 ILE   A C   
5836  O  O   A ILE   A 383 ? 0.2351 0.1705 0.2782 -0.0004 -0.0728 0.0263  383 ILE   A O   
5837  O  O   B ILE   A 383 ? 0.2351 0.1705 0.2782 -0.0004 -0.0728 0.0263  383 ILE   A O   
5838  C  CB  A ILE   A 383 ? 0.2622 0.1679 0.2885 -0.0121 -0.0748 0.0375  383 ILE   A CB  
5839  C  CB  B ILE   A 383 ? 0.2622 0.1679 0.2885 -0.0121 -0.0748 0.0375  383 ILE   A CB  
5840  C  CG1 A ILE   A 383 ? 0.3018 0.2096 0.3189 -0.0205 -0.0712 0.0402  383 ILE   A CG1 
5841  C  CG1 B ILE   A 383 ? 0.3018 0.2095 0.3189 -0.0205 -0.0712 0.0402  383 ILE   A CG1 
5842  C  CG2 A ILE   A 383 ? 0.3329 0.2410 0.3533 -0.0059 -0.0788 0.0393  383 ILE   A CG2 
5843  C  CG2 B ILE   A 383 ? 0.3330 0.2410 0.3533 -0.0059 -0.0788 0.0393  383 ILE   A CG2 
5844  C  CD1 A ILE   A 383 ? 0.3698 0.2681 0.3730 -0.0227 -0.0712 0.0438  383 ILE   A CD1 
5845  C  CD1 B ILE   A 383 ? 0.3698 0.2681 0.3730 -0.0227 -0.0712 0.0438  383 ILE   A CD1 
5868  N  N   . GLY   A 384 ? 0.2143 0.1270 0.2536 0.0027  -0.0750 0.0248  384 GLY   A N   
5869  C  CA  . GLY   A 384 ? 0.2308 0.1486 0.2765 0.0115  -0.0768 0.0205  384 GLY   A CA  
5870  C  C   . GLY   A 384 ? 0.2206 0.1545 0.2725 0.0120  -0.0724 0.0149  384 GLY   A C   
5871  O  O   . GLY   A 384 ? 0.1915 0.1371 0.2564 0.0175  -0.0731 0.0120  384 GLY   A O   
5876  N  N   . TRP   A 385 ? 0.1605 0.0995 0.2209 0.0059  -0.0678 0.0133  385 TRP   A N   
5877  C  CA  . TRP   A 385 ? 0.2183 0.1682 0.2704 0.0063  -0.0633 0.0086  385 TRP   A CA  
5878  C  C   . TRP   A 385 ? 0.1660 0.1325 0.2351 0.0046  -0.0619 0.0099  385 TRP   A C   
5879  O  O   . TRP   A 385 ? 0.1800 0.1574 0.2508 0.0063  -0.0587 0.0060  385 TRP   A O   
5880  C  CB  . TRP   A 385 ? 0.1571 0.1085 0.2185 0.0009  -0.0595 0.0066  385 TRP   A CB  
5881  C  CG  . TRP   A 385 ? 0.1917 0.1323 0.2443 0.0034  -0.0595 0.0023  385 TRP   A CG  
5882  C  CD1 . TRP   A 385 ? 0.1988 0.1274 0.2472 -0.0003 -0.0603 0.0025  385 TRP   A CD1 
5883  C  CD2 . TRP   A 385 ? 0.1689 0.1128 0.2321 0.0101  -0.0590 -0.0037 385 TRP   A CD2 
5884  N  NE1 . TRP   A 385 ? 0.1966 0.1191 0.2462 0.0037  -0.0604 -0.0028 385 TRP   A NE1 
5885  C  CE2 . TRP   A 385 ? 0.1962 0.1271 0.2518 0.0103  -0.0596 -0.0067 385 TRP   A CE2 
5886  C  CE3 . TRP   A 385 ? 0.1819 0.1369 0.2502 0.0158  -0.0577 -0.0073 385 TRP   A CE3 
5887  C  CZ2 . TRP   A 385 ? 0.2156 0.1452 0.2742 0.0165  -0.0591 -0.0131 385 TRP   A CZ2 
5888  C  CZ3 . TRP   A 385 ? 0.1953 0.1502 0.2674 0.0218  -0.0570 -0.0134 385 TRP   A CZ3 
5889  C  CH2 . TRP   A 385 ? 0.2175 0.1593 0.2834 0.0225  -0.0578 -0.0163 385 TRP   A CH2 
5900  N  N   . ILE   A 386 ? 0.1827 0.1473 0.2434 0.0012  -0.0637 0.0150  386 ILE   A N   
5901  C  CA  . ILE   A 386 ? 0.1786 0.1553 0.2429 -0.0012 -0.0624 0.0162  386 ILE   A CA  
5902  C  C   . ILE   A 386 ? 0.1616 0.1496 0.2385 0.0044  -0.0636 0.0131  386 ILE   A C   
5903  O  O   . ILE   A 386 ? 0.1696 0.1689 0.2492 0.0034  -0.0599 0.0101  386 ILE   A O   
5904  C  CB  . ILE   A 386 ? 0.1817 0.1551 0.2428 -0.0054 -0.0646 0.0218  386 ILE   A CB  
5905  C  CG1 . ILE   A 386 ? 0.2007 0.1657 0.2515 -0.0113 -0.0627 0.0242  386 ILE   A CG1 
5906  C  CG2 . ILE   A 386 ? 0.2203 0.2045 0.2801 -0.0076 -0.0634 0.0222  386 ILE   A CG2 
5907  C  CD1 . ILE   A 386 ? 0.2231 0.1827 0.2660 -0.0153 -0.0645 0.0293  386 ILE   A CD1 
5919  N  N   . LYS   A 387 ? 0.1966 0.1789 0.2687 0.0102  -0.0689 0.0136  387 LYS   A N   
5920  C  CA  . LYS   A 387 ? 0.1612 0.1563 0.2498 0.0161  -0.0711 0.0103  387 LYS   A CA  
5921  C  C   . LYS   A 387 ? 0.1605 0.1635 0.2562 0.0193  -0.0672 0.0038  387 LYS   A C   
5922  O  O   . LYS   A 387 ? 0.1656 0.1826 0.2672 0.0202  -0.0650 0.0003  387 LYS   A O   
5923  C  CB  . LYS   A 387 ? 0.2026 0.1893 0.2852 0.0231  -0.0781 0.0121  387 LYS   A CB  
5924  C  CG  . LYS   A 387 ? 0.2053 0.2049 0.3024 0.0308  -0.0813 0.0080  387 LYS   A CG  
5925  C  CD  . LYS   A 387 ? 0.2628 0.2540 0.3594 0.0388  -0.0889 0.0099  387 LYS   A CD  
5926  C  CE  . LYS   A 387 ? 0.3902 0.3908 0.4861 0.0472  -0.0905 0.0042  387 LYS   A CE  
5927  N  NZ  . LYS   A 387 ? 0.3680 0.3716 0.4794 0.0525  -0.0888 -0.0015 387 LYS   A NZ  
5941  N  N   . ARG   A 388 ? 0.2090 0.2009 0.2947 0.0207  -0.0657 0.0019  388 ARG   A N   
5942  C  CA  . ARG   A 388 ? 0.1655 0.1658 0.2654 0.0244  -0.0621 -0.0045 388 ARG   A CA  
5943  C  C   . ARG   A 388 ? 0.1375 0.1485 0.2376 0.0185  -0.0552 -0.0065 388 ARG   A C   
5944  O  O   . ARG   A 388 ? 0.1651 0.1867 0.2688 0.0205  -0.0515 -0.0113 388 ARG   A O   
5945  C  CB  . ARG   A 388 ? 0.2360 0.2212 0.3256 0.0273  -0.0630 -0.0063 388 ARG   A CB  
5946  C  CG  . ARG   A 388 ? 0.2754 0.2462 0.3622 0.0325  -0.0695 -0.0039 388 ARG   A CG  
5947  C  CD  . ARG   A 388 ? 0.3044 0.2629 0.3883 0.0372  -0.0703 -0.0075 388 ARG   A CD  
5948  N  NE  . ARG   A 388 ? 0.3005 0.2692 0.3959 0.0442  -0.0687 -0.0146 388 ARG   A NE  
5949  C  CZ  . ARG   A 388 ? 0.3223 0.2929 0.4216 0.0533  -0.0726 -0.0175 388 ARG   A CZ  
5950  N  NH1 . ARG   A 388 ? 0.3566 0.3235 0.4555 0.0565  -0.0786 -0.0131 388 ARG   A NH1 
5951  N  NH2 . ARG   A 388 ? 0.2709 0.2491 0.3817 0.0597  -0.0706 -0.0247 388 ARG   A NH2 
5965  N  N   . MET   A 389 ? 0.1324 0.1393 0.2242 0.0115  -0.0531 -0.0023 389 MET   A N   
5966  C  CA  . MET   A 389 ? 0.1531 0.1680 0.2422 0.0061  -0.0471 -0.0028 389 MET   A CA  
5967  C  C   . MET   A 389 ? 0.1557 0.1837 0.2530 0.0048  -0.0459 -0.0032 389 MET   A C   
5968  O  O   . MET   A 389 ? 0.1657 0.2037 0.2673 0.0038  -0.0409 -0.0065 389 MET   A O   
5969  C  CB  . MET   A 389 ? 0.1522 0.1600 0.2338 -0.0001 -0.0460 0.0012  389 MET   A CB  
5970  C  CG  . MET   A 389 ? 0.1715 0.1679 0.2482 0.0000  -0.0471 0.0014  389 MET   A CG  
5971  S  SD  . MET   A 389 ? 0.2575 0.2435 0.3119 -0.0071 -0.0478 0.0065  389 MET   A SD  
5972  C  CE  . MET   A 389 ? 0.1257 0.1255 0.1969 -0.0111 -0.0436 0.0081  389 MET   A CE  
5982  N  N   . VAL   A 390 ? 0.1478 0.1757 0.2471 0.0045  -0.0505 0.0001  390 VAL   A N   
5983  C  CA  . VAL   A 390 ? 0.1637 0.2027 0.2659 0.0028  -0.0503 -0.0004 390 VAL   A CA  
5984  C  C   . VAL   A 390 ? 0.1402 0.1929 0.2578 0.0074  -0.0494 -0.0062 390 VAL   A C   
5985  O  O   . VAL   A 390 ? 0.1356 0.2000 0.2584 0.0040  -0.0451 -0.0086 390 VAL   A O   
5986  C  CB  . VAL   A 390 ? 0.1492 0.1854 0.2520 0.0027  -0.0563 0.0038  390 VAL   A CB  
5987  C  CG1 . VAL   A 390 ? 0.1466 0.1958 0.2572 0.0026  -0.0576 0.0019  390 VAL   A CG1 
5988  C  CG2 . VAL   A 390 ? 0.1517 0.1786 0.2438 -0.0029 -0.0561 0.0089  390 VAL   A CG2 
5998  N  N   . TYR   A 391 ? 0.1401 0.1903 0.2603 0.0148  -0.0532 -0.0088 391 TYR   A N   
5999  C  CA  . TYR   A 391 ? 0.1389 0.2025 0.2707 0.0206  -0.0533 -0.0148 391 TYR   A CA  
6000  C  C   . TYR   A 391 ? 0.1146 0.1805 0.2500 0.0231  -0.0481 -0.0199 391 TYR   A C   
6001  O  O   . TYR   A 391 ? 0.0910 0.1672 0.2366 0.0291  -0.0482 -0.0254 391 TYR   A O   
6002  C  CB  . TYR   A 391 ? 0.1537 0.2148 0.2873 0.0286  -0.0614 -0.0144 391 TYR   A CB  
6003  C  CG  . TYR   A 391 ? 0.1314 0.1963 0.2712 0.0270  -0.0665 -0.0110 391 TYR   A CG  
6004  C  CD1 . TYR   A 391 ? 0.1634 0.2440 0.3075 0.0267  -0.0667 -0.0141 391 TYR   A CD1 
6005  C  CD2 . TYR   A 391 ? 0.1724 0.2219 0.2956 0.0255  -0.0708 -0.0044 391 TYR   A CD2 
6006  C  CE1 . TYR   A 391 ? 0.1641 0.2463 0.3061 0.0248  -0.0702 -0.0112 391 TYR   A CE1 
6007  C  CE2 . TYR   A 391 ? 0.1866 0.2384 0.3075 0.0242  -0.0752 -0.0014 391 TYR   A CE2 
6008  C  CZ  . TYR   A 391 ? 0.1529 0.2212 0.2856 0.0237  -0.0743 -0.0048 391 TYR   A CZ  
6009  O  OH  . TYR   A 391 ? 0.1514 0.2205 0.2774 0.0218  -0.0766 -0.0023 391 TYR   A OH  
6019  N  N   . SER   A 392 ? 0.1295 0.1866 0.2555 0.0192  -0.0439 -0.0186 392 SER   A N   
6020  C  CA  . SER   A 392 ? 0.1439 0.2026 0.2693 0.0210  -0.0388 -0.0235 392 SER   A CA  
6021  C  C   . SER   A 392 ? 0.1804 0.2355 0.3079 0.0304  -0.0427 -0.0276 392 SER   A C   
6022  O  O   . SER   A 392 ? 0.1844 0.2508 0.3226 0.0344  -0.0397 -0.0339 392 SER   A O   
6023  C  CB  . SER   A 392 ? 0.0950 0.1705 0.2321 0.0177  -0.0318 -0.0271 392 SER   A CB  
6024  O  OG  . SER   A 392 ? 0.1393 0.2130 0.2647 0.0095  -0.0277 -0.0233 392 SER   A OG  
6030  N  N   . GLU   A 393 ? 0.1546 0.1962 0.2826 0.0335  -0.0492 -0.0245 393 GLU   A N   
6031  C  CA  . GLU   A 393 ? 0.1977 0.2317 0.3243 0.0427  -0.0538 -0.0277 393 GLU   A CA  
6032  C  C   . GLU   A 393 ? 0.2185 0.2391 0.3340 0.0428  -0.0518 -0.0295 393 GLU   A C   
6033  O  O   . GLU   A 393 ? 0.2028 0.2123 0.3124 0.0372  -0.0521 -0.0249 393 GLU   A O   
6034  C  CB  . GLU   A 393 ? 0.2320 0.2564 0.3564 0.0463  -0.0618 -0.0231 393 GLU   A CB  
6035  C  CG  . GLU   A 393 ? 0.2605 0.2972 0.3918 0.0467  -0.0648 -0.0217 393 GLU   A CG  
6036  C  CD  . GLU   A 393 ? 0.2929 0.3211 0.4250 0.0485  -0.0724 -0.0157 393 GLU   A CD  
6037  O  OE1 . GLU   A 393 ? 0.3656 0.3751 0.4775 0.0452  -0.0739 -0.0105 393 GLU   A OE1 
6038  O  OE2 . GLU   A 393 ? 0.3713 0.4064 0.5007 0.0529  -0.0768 -0.0164 393 GLU   A OE2 
6045  N  N   . GLY   A 394 ? 0.1905 0.2154 0.3159 0.0489  -0.0498 -0.0364 394 GLY   A N   
6046  C  CA  . GLY   A 394 ? 0.2229 0.2352 0.3363 0.0492  -0.0480 -0.0392 394 GLY   A CA  
6047  C  C   . GLY   A 394 ? 0.2096 0.2213 0.3176 0.0403  -0.0431 -0.0370 394 GLY   A C   
6048  O  O   . GLY   A 394 ? 0.1779 0.2029 0.2888 0.0361  -0.0377 -0.0374 394 GLY   A O   
6052  N  N   . PHE   A 395 ? 0.2472 0.2424 0.3401 0.0373  -0.0447 -0.0347 395 PHE   A N   
6053  C  CA  . PHE   A 395 ? 0.2001 0.1952 0.2908 0.0297  -0.0411 -0.0327 395 PHE   A CA  
6054  C  C   . PHE   A 395 ? 0.2002 0.1991 0.2841 0.0230  -0.0404 -0.0263 395 PHE   A C   
6055  O  O   . PHE   A 395 ? 0.1676 0.1713 0.2515 0.0176  -0.0363 -0.0250 395 PHE   A O   
6056  C  CB  . PHE   A 395 ? 0.2042 0.1821 0.2820 0.0280  -0.0436 -0.0326 395 PHE   A CB  
6057  C  CG  . PHE   A 395 ? 0.1754 0.1541 0.2531 0.0206  -0.0410 -0.0302 395 PHE   A CG  
6058  C  CD1 . PHE   A 395 ? 0.2501 0.2320 0.3114 0.0195  -0.0361 -0.0345 395 PHE   A CD1 
6059  C  CD2 . PHE   A 395 ? 0.2112 0.1821 0.2761 0.0147  -0.0433 -0.0241 395 PHE   A CD2 
6060  C  CE1 . PHE   A 395 ? 0.1894 0.1738 0.2556 0.0136  -0.0344 -0.0324 395 PHE   A CE1 
6061  C  CE2 . PHE   A 395 ? 0.2255 0.1973 0.2855 0.0087  -0.0413 -0.0226 395 PHE   A CE2 
6062  C  CZ  . PHE   A 395 ? 0.2468 0.2235 0.2998 0.0083  -0.0372 -0.0266 395 PHE   A CZ  
6072  N  N   . GLY   A 396 ? 0.1693 0.1684 0.2609 0.0239  -0.0447 -0.0220 396 GLY   A N   
6073  C  CA  . GLY   A 396 ? 0.1718 0.1750 0.2601 0.0178  -0.0444 -0.0166 396 GLY   A CA  
6074  C  C   . GLY   A 396 ? 0.1522 0.1698 0.2440 0.0148  -0.0381 -0.0180 396 GLY   A C   
6075  O  O   . GLY   A 396 ? 0.1301 0.1496 0.2199 0.0089  -0.0361 -0.0140 396 GLY   A O   
6079  N  N   . ALA   A 397 ? 0.1358 0.1644 0.2388 0.0189  -0.0349 -0.0237 397 ALA   A N   
6080  C  CA  . ALA   A 397 ? 0.1804 0.2208 0.2784 0.0156  -0.0283 -0.0256 397 ALA   A CA  
6081  C  C   . ALA   A 397 ? 0.1376 0.1776 0.2364 0.0103  -0.0235 -0.0242 397 ALA   A C   
6082  O  O   . ALA   A 397 ? 0.1626 0.2084 0.2550 0.0057  -0.0186 -0.0229 397 ALA   A O   
6083  C  CB  . ALA   A 397 ? 0.1479 0.2014 0.2627 0.0209  -0.0257 -0.0321 397 ALA   A CB  
6089  N  N   . LYS   A 398 ? 0.1645 0.1927 0.2486 0.0112  -0.0246 -0.0249 398 LYS   A N   
6090  C  CA  . LYS   A 398 ? 0.1476 0.1742 0.2262 0.0070  -0.0210 -0.0243 398 LYS   A CA  
6091  C  C   . LYS   A 398 ? 0.1391 0.1601 0.2103 0.0016  -0.0227 -0.0180 398 LYS   A C   
6092  O  O   . LYS   A 398 ? 0.1505 0.1713 0.2130 -0.0019 -0.0195 -0.0164 398 LYS   A O   
6093  C  CB  . LYS   A 398 ? 0.1858 0.2049 0.2577 0.0102  -0.0217 -0.0288 398 LYS   A CB  
6094  C  CG  . LYS   A 398 ? 0.2264 0.2508 0.3021 0.0158  -0.0190 -0.0359 398 LYS   A CG  
6095  C  CD  . LYS   A 398 ? 0.2665 0.2869 0.3335 0.0169  -0.0169 -0.0406 398 LYS   A CD  
6096  C  CE  . LYS   A 398 ? 0.2571 0.2862 0.3302 0.0215  -0.0125 -0.0478 398 LYS   A CE  
6097  N  NZ  . LYS   A 398 ? 0.2642 0.2871 0.3302 0.0239  -0.0124 -0.0532 398 LYS   A NZ  
6111  N  N   . MET   A 399 ? 0.1467 0.1625 0.2178 0.0011  -0.0278 -0.0141 399 MET   A N   
6112  C  CA  . MET   A 399 ? 0.1381 0.1497 0.2073 -0.0036 -0.0297 -0.0086 399 MET   A CA  
6113  C  C   . MET   A 399 ? 0.1563 0.1735 0.2234 -0.0063 -0.0288 -0.0053 399 MET   A C   
6114  O  O   . MET   A 399 ? 0.1167 0.1328 0.1848 -0.0103 -0.0290 -0.0013 399 MET   A O   
6115  C  CB  . MET   A 399 ? 0.1574 0.1582 0.2231 -0.0031 -0.0355 -0.0067 399 MET   A CB  
6116  C  CG  . MET   A 399 ? 0.1994 0.1910 0.2577 -0.0025 -0.0368 -0.0090 399 MET   A CG  
6117  S  SD  . MET   A 399 ? 0.2171 0.1954 0.2720 -0.0042 -0.0426 -0.0059 399 MET   A SD  
6118  C  CE  . MET   A 399 ? 0.1965 0.1722 0.2602 0.0025  -0.0462 -0.0072 399 MET   A CE  
6128  N  N   . THR   A 400 ? 0.1412 0.1681 0.2211 -0.0043 -0.0275 -0.0076 400 THR   A N   
6129  C  CA  . THR   A 400 ? 0.1442 0.1774 0.2271 -0.0069 -0.0270 -0.0055 400 THR   A CA  
6130  C  C   . THR   A 400 ? 0.1537 0.1873 0.2294 -0.0125 -0.0229 -0.0026 400 THR   A C   
6131  O  O   . THR   A 400 ? 0.1383 0.1726 0.2173 -0.0156 -0.0241 0.0008  400 THR   A O   
6132  C  CB  . THR   A 400 ? 0.1134 0.1594 0.2123 -0.0043 -0.0254 -0.0097 400 THR   A CB  
6133  O  OG1 . THR   A 400 ? 0.1463 0.1895 0.2444 0.0022  -0.0296 -0.0126 400 THR   A OG1 
6134  C  CG2 . THR   A 400 ? 0.1294 0.1822 0.2294 -0.0072 -0.0254 -0.0086 400 THR   A CG2 
6142  N  N   . ASN   A 401 ? 0.1249 0.1596 0.1999 -0.0134 -0.0180 -0.0037 401 ASN   A N   
6143  C  CA  . ASN   A 401 ? 0.1381 0.1721 0.2028 -0.0182 -0.0135 -0.0010 401 ASN   A CA  
6144  C  C   . ASN   A 401 ? 0.1155 0.1422 0.1746 -0.0191 -0.0146 0.0018  401 ASN   A C   
6145  O  O   . ASN   A 401 ? 0.1520 0.1767 0.1999 -0.0216 -0.0109 0.0037  401 ASN   A O   
6146  C  CB  . ASN   A 401 ? 0.1305 0.1725 0.2009 -0.0192 -0.0067 -0.0036 401 ASN   A CB  
6147  C  CG  . ASN   A 401 ? 0.1612 0.2136 0.2425 -0.0195 -0.0051 -0.0064 401 ASN   A CG  
6148  O  OD1 . ASN   A 401 ? 0.1128 0.1671 0.2000 -0.0207 -0.0081 -0.0049 401 ASN   A OD1 
6149  N  ND2 . ASN   A 401 ? 0.2721 0.3308 0.3508 -0.0184 -0.0004 -0.0107 401 ASN   A ND2 
6156  N  N   . GLY   A 402 ? 0.1138 0.1341 0.1684 -0.0177 -0.0196 0.0023  402 GLY   A N   
6157  C  CA  . GLY   A 402 ? 0.1199 0.1342 0.1667 -0.0189 -0.0209 0.0045  402 GLY   A CA  
6158  C  C   . GLY   A 402 ? 0.1414 0.1521 0.1791 -0.0171 -0.0211 0.0018  402 GLY   A C   
6159  O  O   . GLY   A 402 ? 0.1230 0.1372 0.1649 -0.0148 -0.0185 -0.0017 402 GLY   A O   
6163  N  N   . SER   A 403 ? 0.1287 0.1358 0.1638 -0.0181 -0.0234 0.0033  403 SER   A N   
6164  C  CA  . SER   A 403 ? 0.1302 0.1343 0.1583 -0.0170 -0.0245 0.0003  403 SER   A CA  
6165  C  C   . SER   A 403 ? 0.1352 0.1419 0.1568 -0.0158 -0.0205 -0.0011 403 SER   A C   
6166  O  O   . SER   A 403 ? 0.1308 0.1374 0.1506 -0.0136 -0.0200 -0.0053 403 SER   A O   
6167  C  CB  . SER   A 403 ? 0.1130 0.1145 0.1405 -0.0191 -0.0281 0.0020  403 SER   A CB  
6168  O  OG  . SER   A 403 ? 0.1351 0.1375 0.1544 -0.0201 -0.0269 0.0047  403 SER   A OG  
6174  N  N   . TYR   A 404 ? 0.1333 0.1418 0.1510 -0.0172 -0.0172 0.0020  404 TYR   A N   
6175  C  CA  . TYR   A 404 ? 0.1249 0.1348 0.1365 -0.0162 -0.0131 0.0017  404 TYR   A CA  
6176  C  C   . TYR   A 404 ? 0.1477 0.1606 0.1574 -0.0146 -0.0092 -0.0021 404 TYR   A C   
6177  O  O   . TYR   A 404 ? 0.1456 0.1591 0.1520 -0.0126 -0.0079 -0.0055 404 TYR   A O   
6178  C  CB  . TYR   A 404 ? 0.1346 0.1433 0.1400 -0.0180 -0.0102 0.0064  404 TYR   A CB  
6179  C  CG  . TYR   A 404 ? 0.1758 0.1831 0.1678 -0.0169 -0.0062 0.0072  404 TYR   A CG  
6180  C  CD1 . TYR   A 404 ? 0.1532 0.1645 0.1509 -0.0175 -0.0001 0.0063  404 TYR   A CD1 
6181  C  CD2 . TYR   A 404 ? 0.2084 0.2129 0.1908 -0.0154 -0.0079 0.0086  404 TYR   A CD2 
6182  C  CE1 . TYR   A 404 ? 0.2400 0.2480 0.2194 -0.0170 0.0041  0.0071  404 TYR   A CE1 
6183  C  CE2 . TYR   A 404 ? 0.2271 0.2306 0.2010 -0.0140 -0.0044 0.0097  404 TYR   A CE2 
6184  C  CZ  . TYR   A 404 ? 0.2822 0.2855 0.2478 -0.0150 0.0018  0.0092  404 TYR   A CZ  
6185  O  OH  . TYR   A 404 ? 0.2888 0.2906 0.2462 -0.0140 0.0058  0.0107  404 TYR   A OH  
6195  N  N   . ARG   A 405 ? 0.1312 0.1482 0.1525 -0.0154 -0.0070 -0.0025 405 ARG   A N   
6196  C  CA  . ARG   A 405 ? 0.1391 0.1621 0.1669 -0.0139 -0.0028 -0.0064 405 ARG   A CA  
6197  C  C   . ARG   A 405 ? 0.1800 0.2007 0.2032 -0.0102 -0.0059 -0.0117 405 ARG   A C   
6198  O  O   . ARG   A 405 ? 0.1455 0.1706 0.1738 -0.0078 -0.0026 -0.0161 405 ARG   A O   
6199  C  CB  . ARG   A 405 ? 0.1658 0.1932 0.1972 -0.0158 -0.0001 -0.0055 405 ARG   A CB  
6200  C  CG  . ARG   A 405 ? 0.1584 0.1872 0.1885 -0.0197 0.0052  -0.0020 405 ARG   A CG  
6201  C  CD  . ARG   A 405 ? 0.1552 0.1866 0.1928 -0.0229 0.0053  0.0003  405 ARG   A CD  
6202  N  NE  . ARG   A 405 ? 0.1700 0.1995 0.1998 -0.0272 0.0102  0.0037  405 ARG   A NE  
6203  C  CZ  . ARG   A 405 ? 0.1344 0.1581 0.1625 -0.0293 0.0090  0.0083  405 ARG   A CZ  
6204  N  NH1 . ARG   A 405 ? 0.1220 0.1410 0.1475 -0.0276 0.0031  0.0099  405 ARG   A NH1 
6205  N  NH2 . ARG   A 405 ? 0.1458 0.1668 0.1677 -0.0332 0.0140  0.0111  405 ARG   A NH2 
6219  N  N   . LEU   A 406 ? 0.1533 0.1709 0.1867 -0.0098 -0.0116 -0.0113 406 LEU   A N   
6220  C  CA  . LEU   A 406 ? 0.1467 0.1607 0.1822 -0.0065 -0.0152 -0.0157 406 LEU   A CA  
6221  C  C   . LEU   A 406 ? 0.1598 0.1710 0.1863 -0.0056 -0.0152 -0.0191 406 LEU   A C   
6222  O  O   . LEU   A 406 ? 0.1576 0.1695 0.1846 -0.0026 -0.0141 -0.0245 406 LEU   A O   
6223  C  CB  . LEU   A 406 ? 0.1358 0.1441 0.1767 -0.0074 -0.0209 -0.0134 406 LEU   A CB  
6224  C  CG  . LEU   A 406 ? 0.1664 0.1669 0.2049 -0.0058 -0.0252 -0.0168 406 LEU   A CG  
6225  C  CD1 . LEU   A 406 ? 0.1866 0.1866 0.2310 -0.0012 -0.0256 -0.0210 406 LEU   A CD1 
6226  C  CD2 . LEU   A 406 ? 0.1649 0.1590 0.2035 -0.0087 -0.0299 -0.0131 406 LEU   A CD2 
6238  N  N   . CYS   A 407 ? 0.1720 0.1807 0.1895 -0.0079 -0.0165 -0.0163 407 CYS   A N   
6239  C  CA  . CYS   A 407 ? 0.1573 0.1645 0.1668 -0.0072 -0.0175 -0.0193 407 CYS   A CA  
6240  C  C   . CYS   A 407 ? 0.1593 0.1707 0.1619 -0.0054 -0.0122 -0.0215 407 CYS   A C   
6241  O  O   . CYS   A 407 ? 0.1701 0.1813 0.1680 -0.0035 -0.0124 -0.0265 407 CYS   A O   
6242  C  CB  . CYS   A 407 ? 0.1300 0.1357 0.1383 -0.0096 -0.0210 -0.0160 407 CYS   A CB  
6243  S  SG  . CYS   A 407 ? 0.1578 0.1578 0.1680 -0.0120 -0.0267 -0.0148 407 CYS   A SG  
6249  N  N   . GLU   A 408 ? 0.1431 0.1590 0.1483 -0.0067 -0.0075 -0.0178 408 GLU   A N   
6250  C  CA  . GLU   A 408 ? 0.2024 0.2206 0.1945 -0.0058 -0.0012 -0.0191 408 GLU   A CA  
6251  C  C   . GLU   A 408 ? 0.1843 0.2067 0.1828 -0.0029 0.0010  -0.0256 408 GLU   A C   
6252  O  O   . GLU   A 408 ? 0.1837 0.2078 0.1765 -0.0010 0.0036  -0.0296 408 GLU   A O   
6253  C  CB  . GLU   A 408 ? 0.2202 0.2416 0.2147 -0.0086 0.0039  -0.0142 408 GLU   A CB  
6254  C  CG  . GLU   A 408 ? 0.2630 0.2872 0.2492 -0.0086 0.0107  -0.0142 408 GLU   A CG  
6255  C  CD  . GLU   A 408 ? 0.3443 0.3686 0.3314 -0.0120 0.0154  -0.0082 408 GLU   A CD  
6256  O  OE1 . GLU   A 408 ? 0.4302 0.4463 0.3983 -0.0126 0.0130  -0.0036 408 GLU   A OE1 
6257  O  OE2 . GLU   A 408 ? 0.4992 0.5247 0.4750 -0.0142 0.0215  -0.0085 408 GLU   A OE2 
6264  N  N   . GLY   A 409 ? 0.1382 0.1635 0.1547 -0.0022 -0.0002 -0.0272 409 GLY   A N   
6265  C  CA  . GLY   A 409 ? 0.1859 0.2136 0.2024 0.0015  0.0016  -0.0336 409 GLY   A CA  
6266  C  C   . GLY   A 409 ? 0.1985 0.2215 0.2102 0.0046  -0.0014 -0.0395 409 GLY   A C   
6267  O  O   . GLY   A 409 ? 0.2022 0.2294 0.2158 0.0076  0.0020  -0.0453 409 GLY   A O   
6271  N  N   . TYR   A 410 ? 0.1470 0.1638 0.1626 0.0034  -0.0073 -0.0384 410 TYR   A N   
6272  C  CA  . TYR   A 410 ? 0.1694 0.1800 0.1769 0.0054  -0.0110 -0.0441 410 TYR   A CA  
6273  C  C   . TYR   A 410 ? 0.1924 0.2040 0.1888 0.0045  -0.0103 -0.0454 410 TYR   A C   
6274  O  O   . TYR   A 410 ? 0.2124 0.2200 0.2037 0.0057  -0.0132 -0.0504 410 TYR   A O   
6275  C  CB  . TYR   A 410 ? 0.1505 0.1537 0.1681 0.0041  -0.0174 -0.0432 410 TYR   A CB  
6276  C  CG  . TYR   A 410 ? 0.2059 0.2047 0.2260 0.0068  -0.0188 -0.0441 410 TYR   A CG  
6277  C  CD1 . TYR   A 410 ? 0.2083 0.2044 0.2358 0.0110  -0.0196 -0.0510 410 TYR   A CD1 
6278  C  CD2 . TYR   A 410 ? 0.1702 0.1715 0.2038 0.0054  -0.0197 -0.0388 410 TYR   A CD2 
6279  C  CE1 . TYR   A 410 ? 0.2056 0.1989 0.2413 0.0145  -0.0212 -0.0517 410 TYR   A CE1 
6280  C  CE2 . TYR   A 410 ? 0.1775 0.1765 0.2178 0.0086  -0.0216 -0.0395 410 TYR   A CE2 
6281  C  CZ  . TYR   A 410 ? 0.1827 0.1785 0.2299 0.0133  -0.0226 -0.0460 410 TYR   A CZ  
6282  O  OH  . TYR   A 410 ? 0.2465 0.2386 0.2951 0.0175  -0.0248 -0.0466 410 TYR   A OH  
6292  N  N   . GLY   A 411 ? 0.2057 0.2212 0.1938 0.0031  -0.0066 -0.0408 411 GLY   A N   
6293  C  CA  . GLY   A 411 ? 0.2096 0.2257 0.1859 0.0029  -0.0067 -0.0406 411 GLY   A CA  
6294  C  C   . GLY   A 411 ? 0.2202 0.2319 0.1914 0.0012  -0.0131 -0.0396 411 GLY   A C   
6295  O  O   . GLY   A 411 ? 0.2244 0.2367 0.1890 0.0021  -0.0152 -0.0430 411 GLY   A O   
6299  N  N   . ALA   A 412 ? 0.1856 0.1956 0.1688 -0.0013 -0.0165 -0.0353 412 ALA   A N   
6300  C  CA  . ALA   A 412 ? 0.2111 0.2172 0.1886 -0.0036 -0.0223 -0.0340 412 ALA   A CA  
6301  C  C   . ALA   A 412 ? 0.1741 0.1821 0.1583 -0.0058 -0.0227 -0.0264 412 ALA   A C   
6302  O  O   . ALA   A 412 ? 0.1727 0.1777 0.1610 -0.0081 -0.0258 -0.0245 412 ALA   A O   
6303  C  CB  . ALA   A 412 ? 0.2107 0.2124 0.1986 -0.0047 -0.0262 -0.0376 412 ALA   A CB  
6309  N  N   . PRO   A 413 ? 0.1992 0.2088 0.1716 -0.0053 -0.0194 -0.0222 413 PRO   A N   
6310  C  CA  . PRO   A 413 ? 0.1984 0.2076 0.1712 -0.0068 -0.0194 -0.0154 413 PRO   A CA  
6311  C  C   . PRO   A 413 ? 0.1760 0.1860 0.1541 -0.0082 -0.0250 -0.0143 413 PRO   A C   
6312  O  O   . PRO   A 413 ? 0.1922 0.2007 0.1695 -0.0099 -0.0258 -0.0099 413 PRO   A O   
6313  C  CB  . PRO   A 413 ? 0.1967 0.2072 0.1609 -0.0055 -0.0152 -0.0125 413 PRO   A CB  
6314  C  CG  . PRO   A 413 ? 0.2125 0.2241 0.1666 -0.0028 -0.0151 -0.0174 413 PRO   A CG  
6315  C  CD  . PRO   A 413 ? 0.2055 0.2176 0.1683 -0.0028 -0.0156 -0.0235 413 PRO   A CD  
6323  N  N   . GLU   A 414 ? 0.2030 0.2129 0.1730 -0.0076 -0.0288 -0.0191 414 GLU   A N   
6324  C  CA  . GLU   A 414 ? 0.1894 0.2026 0.1658 -0.0091 -0.0340 -0.0193 414 GLU   A CA  
6325  C  C   . GLU   A 414 ? 0.1978 0.2075 0.1792 -0.0129 -0.0363 -0.0182 414 GLU   A C   
6326  O  O   . GLU   A 414 ? 0.1897 0.2023 0.1750 -0.0145 -0.0395 -0.0173 414 GLU   A O   
6327  C  CB  . GLU   A 414 ? 0.2447 0.2591 0.2094 -0.0081 -0.0373 -0.0254 414 GLU   A CB  
6328  C  CG  . GLU   A 414 ? 0.2364 0.2488 0.2085 -0.0093 -0.0378 -0.0317 414 GLU   A CG  
6329  C  CD  . GLU   A 414 ? 0.2499 0.2616 0.2152 -0.0060 -0.0343 -0.0355 414 GLU   A CD  
6330  O  OE1 . GLU   A 414 ? 0.2317 0.2438 0.1950 -0.0042 -0.0294 -0.0318 414 GLU   A OE1 
6331  O  OE2 . GLU   A 414 ? 0.2813 0.2926 0.2432 -0.0056 -0.0361 -0.0422 414 GLU   A OE2 
6338  N  N   . TYR   A 415 ? 0.1787 0.1850 0.1698 -0.0138 -0.0348 -0.0186 415 TYR   A N   
6339  C  CA  . TYR   A 415 ? 0.1777 0.1801 0.1768 -0.0172 -0.0369 -0.0177 415 TYR   A CA  
6340  C  C   . TYR   A 415 ? 0.1777 0.1793 0.1781 -0.0176 -0.0356 -0.0126 415 TYR   A C   
6341  O  O   . TYR   A 415 ? 0.1648 0.1637 0.1744 -0.0205 -0.0368 -0.0101 415 TYR   A O   
6342  C  CB  . TYR   A 415 ? 0.1823 0.1792 0.1835 -0.0172 -0.0378 -0.0228 415 TYR   A CB  
6343  C  CG  . TYR   A 415 ? 0.1672 0.1650 0.1665 -0.0173 -0.0400 -0.0292 415 TYR   A CG  
6344  C  CD1 . TYR   A 415 ? 0.1841 0.1845 0.1815 -0.0201 -0.0436 -0.0308 415 TYR   A CD1 
6345  C  CD2 . TYR   A 415 ? 0.1595 0.1570 0.1581 -0.0141 -0.0384 -0.0344 415 TYR   A CD2 
6346  C  CE1 . TYR   A 415 ? 0.2062 0.2078 0.1991 -0.0205 -0.0459 -0.0370 415 TYR   A CE1 
6347  C  CE2 . TYR   A 415 ? 0.2375 0.2340 0.2230 -0.0142 -0.0404 -0.0407 415 TYR   A CE2 
6348  C  CZ  . TYR   A 415 ? 0.2161 0.2167 0.2080 -0.0174 -0.0445 -0.0423 415 TYR   A CZ  
6349  O  OH  . TYR   A 415 ? 0.2547 0.2560 0.2382 -0.0177 -0.0471 -0.0492 415 TYR   A OH  
6359  N  N   . SER   A 416 ? 0.1723 0.1747 0.1428 0.0082  -0.0483 -0.0360 416 SER   A N   
6360  C  CA  . SER   A 416 ? 0.1477 0.1525 0.1251 0.0076  -0.0454 -0.0307 416 SER   A CA  
6361  C  C   . SER   A 416 ? 0.1452 0.1476 0.1209 0.0016  -0.0441 -0.0219 416 SER   A C   
6362  O  O   . SER   A 416 ? 0.1488 0.1602 0.1229 -0.0011 -0.0418 -0.0188 416 SER   A O   
6363  C  CB  . SER   A 416 ? 0.1870 0.2045 0.1593 0.0098  -0.0408 -0.0318 416 SER   A CB  
6364  O  OG  . SER   A 416 ? 0.1298 0.1503 0.1139 0.0076  -0.0380 -0.0259 416 SER   A OG  
6370  N  N   . MET   A 417 ? 0.1449 0.1368 0.1223 -0.0003 -0.0458 -0.0181 417 MET   A N   
6371  C  CA  . MET   A 417 ? 0.1432 0.1342 0.1221 -0.0054 -0.0444 -0.0108 417 MET   A CA  
6372  C  C   . MET   A 417 ? 0.1282 0.1260 0.1135 -0.0054 -0.0406 -0.0066 417 MET   A C   
6373  O  O   . MET   A 417 ? 0.1426 0.1343 0.1276 -0.0060 -0.0401 -0.0039 417 MET   A O   
6374  C  CB  . MET   A 417 ? 0.1429 0.1226 0.1242 -0.0081 -0.0474 -0.0092 417 MET   A CB  
6375  C  CG  . MET   A 417 ? 0.1836 0.1559 0.1567 -0.0093 -0.0520 -0.0125 417 MET   A CG  
6376  S  SD  . MET   A 417 ? 0.1539 0.1368 0.1328 -0.0124 -0.0520 -0.0129 417 MET   A SD  
6377  C  CE  . MET   A 417 ? 0.1957 0.1804 0.1636 -0.0075 -0.0541 -0.0210 417 MET   A CE  
6387  N  N   . THR   A 418 ? 0.1386 0.1461 0.1213 -0.0055 -0.0374 -0.0056 418 THR   A N   
6388  C  CA  . THR   A 418 ? 0.1265 0.1404 0.1150 -0.0059 -0.0341 -0.0021 418 THR   A CA  
6389  C  C   . THR   A 418 ? 0.1321 0.1524 0.1195 -0.0093 -0.0320 0.0035  418 THR   A C   
6390  O  O   . THR   A 418 ? 0.1312 0.1549 0.1154 -0.0103 -0.0332 0.0035  418 THR   A O   
6391  C  CB  . THR   A 418 ? 0.1266 0.1479 0.1159 -0.0028 -0.0323 -0.0065 418 THR   A CB  
6392  O  OG1 . THR   A 418 ? 0.1269 0.1547 0.1111 -0.0017 -0.0321 -0.0101 418 THR   A OG1 
6393  C  CG2 . THR   A 418 ? 0.1480 0.1630 0.1372 0.0012  -0.0343 -0.0107 418 THR   A CG2 
6401  N  N   . VAL   A 419 ? 0.1298 0.1513 0.1216 -0.0107 -0.0300 0.0081  419 VAL   A N   
6402  C  CA  . VAL   A 419 ? 0.1242 0.1508 0.1168 -0.0138 -0.0286 0.0139  419 VAL   A CA  
6403  C  C   . VAL   A 419 ? 0.1370 0.1688 0.1302 -0.0143 -0.0258 0.0149  419 VAL   A C   
6404  O  O   . VAL   A 419 ? 0.1237 0.1523 0.1242 -0.0134 -0.0255 0.0138  419 VAL   A O   
6405  C  CB  . VAL   A 419 ? 0.1010 0.1232 0.0999 -0.0153 -0.0302 0.0187  419 VAL   A CB  
6406  C  CG1 . VAL   A 419 ? 0.1425 0.1670 0.1367 -0.0177 -0.0300 0.0247  419 VAL   A CG1 
6407  C  CG2 . VAL   A 419 ? 0.1052 0.1228 0.0997 -0.0151 -0.0326 0.0175  419 VAL   A CG2 
6417  N  N   . LYS   A 420 ? 0.1145 0.1562 0.1090 -0.0162 -0.0236 0.0166  420 LYS   A N   
6418  C  CA  . LYS   A 420 ? 0.1169 0.1653 0.1138 -0.0179 -0.0207 0.0171  420 LYS   A CA  
6419  C  C   . LYS   A 420 ? 0.1158 0.1657 0.1139 -0.0137 -0.0203 0.0100  420 LYS   A C   
6420  O  O   . LYS   A 420 ? 0.0933 0.1452 0.0995 -0.0143 -0.0191 0.0097  420 LYS   A O   
6421  C  CB  . LYS   A 420 ? 0.1213 0.1651 0.1237 -0.0209 -0.0209 0.0235  420 LYS   A CB  
6422  C  CG  . LYS   A 420 ? 0.1466 0.1873 0.1450 -0.0243 -0.0222 0.0306  420 LYS   A CG  
6423  C  CD  . LYS   A 420 ? 0.1370 0.1709 0.1434 -0.0259 -0.0235 0.0357  420 LYS   A CD  
6424  C  CE  . LYS   A 420 ? 0.1566 0.1862 0.1581 -0.0282 -0.0260 0.0424  420 LYS   A CE  
6425  N  NZ  . LYS   A 420 ? 0.1349 0.1621 0.1376 -0.0254 -0.0287 0.0415  420 LYS   A NZ  
6439  N  N   . LYS   A 421 ? 0.1097 0.1587 0.1060 -0.0101 -0.0218 0.0038  421 LYS   A N   
6440  C  CA  . LYS   A 421 ? 0.1062 0.1565 0.1068 -0.0053 -0.0226 -0.0034 421 LYS   A CA  
6441  C  C   . LYS   A 421 ? 0.1274 0.1659 0.1284 -0.0033 -0.0252 -0.0037 421 LYS   A C   
6442  O  O   . LYS   A 421 ? 0.1256 0.1641 0.1297 0.0006  -0.0264 -0.0084 421 LYS   A O   
6443  C  CB  . LYS   A 421 ? 0.1244 0.1887 0.1266 -0.0050 -0.0189 -0.0060 421 LYS   A CB  
6444  C  CG  . LYS   A 421 ? 0.1579 0.2347 0.1547 -0.0083 -0.0153 -0.0046 421 LYS   A CG  
6445  C  CD  . LYS   A 421 ? 0.1576 0.2513 0.1624 -0.0091 -0.0111 -0.0067 421 LYS   A CD  
6446  C  CE  . LYS   A 421 ? 0.2199 0.3268 0.2176 -0.0138 -0.0069 -0.0040 421 LYS   A CE  
6447  N  NZ  . LYS   A 421 ? 0.2823 0.4060 0.2815 -0.0155 -0.0021 -0.0060 421 LYS   A NZ  
6461  N  N   . GLN   A 422 ? 0.1365 0.1662 0.1374 -0.0058 -0.0262 0.0013  422 GLN   A N   
6462  C  CA  . GLN   A 422 ? 0.1262 0.1461 0.1283 -0.0045 -0.0285 0.0013  422 GLN   A CA  
6463  C  C   . GLN   A 422 ? 0.1102 0.1212 0.1105 -0.0043 -0.0312 0.0011  422 GLN   A C   
6464  O  O   . GLN   A 422 ? 0.1147 0.1255 0.1121 -0.0069 -0.0307 0.0039  422 GLN   A O   
6465  C  CB  . GLN   A 422 ? 0.1096 0.1288 0.1191 -0.0069 -0.0274 0.0051  422 GLN   A CB  
6466  C  CG  . GLN   A 422 ? 0.1356 0.1461 0.1422 -0.0055 -0.0293 0.0046  422 GLN   A CG  
6467  C  CD  . GLN   A 422 ? 0.1232 0.1345 0.1369 -0.0074 -0.0285 0.0064  422 GLN   A CD  
6468  O  OE1 . GLN   A 422 ? 0.1150 0.1313 0.1319 -0.0069 -0.0282 0.0048  422 GLN   A OE1 
6469  N  NE2 . GLN   A 422 ? 0.1376 0.1440 0.1500 -0.0092 -0.0281 0.0095  422 GLN   A NE2 
6478  N  N   . GLU   A 423 ? 0.1146 0.1170 0.1115 -0.0022 -0.0338 -0.0015 423 GLU   A N   
6479  C  CA  . GLU   A 423 ? 0.1093 0.1029 0.1045 -0.0028 -0.0367 -0.0018 423 GLU   A CA  
6480  C  C   . GLU   A 423 ? 0.1342 0.1237 0.1263 -0.0067 -0.0359 0.0030  423 GLU   A C   
6481  O  O   . GLU   A 423 ? 0.1313 0.1204 0.1274 -0.0072 -0.0348 0.0051  423 GLU   A O   
6482  C  CB  . GLU   A 423 ? 0.1150 0.1003 0.1085 0.0006  -0.0405 -0.0051 423 GLU   A CB  
6483  C  CG  . GLU   A 423 ? 0.1616 0.1474 0.1484 0.0051  -0.0424 -0.0113 423 GLU   A CG  
6484  C  CD  . GLU   A 423 ? 0.1194 0.1186 0.1184 0.0081  -0.0400 -0.0145 423 GLU   A CD  
6485  O  OE1 . GLU   A 423 ? 0.1329 0.1353 0.1308 0.0067  -0.0377 -0.0114 423 GLU   A OE1 
6486  O  OE2 . GLU   A 423 ? 0.1426 0.1461 0.1369 0.0118  -0.0405 -0.0200 423 GLU   A OE2 
6493  N  N   . ILE   A 424 ? 0.1201 0.1091 0.1125 -0.0089 -0.0367 0.0043  424 ILE   A N   
6494  C  CA  . ILE   A 424 ? 0.1053 0.0941 0.1042 -0.0123 -0.0361 0.0081  424 ILE   A CA  
6495  C  C   . ILE   A 424 ? 0.1437 0.1230 0.1350 -0.0134 -0.0372 0.0084  424 ILE   A C   
6496  O  O   . ILE   A 424 ? 0.1623 0.1349 0.1496 -0.0127 -0.0400 0.0064  424 ILE   A O   
6497  C  CB  . ILE   A 424 ? 0.1586 0.1491 0.1527 -0.0144 -0.0370 0.0088  424 ILE   A CB  
6498  C  CG1 . ILE   A 424 ? 0.1877 0.1861 0.1813 -0.0138 -0.0359 0.0097  424 ILE   A CG1 
6499  C  CG2 . ILE   A 424 ? 0.1890 0.1783 0.1837 -0.0177 -0.0368 0.0115  424 ILE   A CG2 
6500  C  CD1 . ILE   A 424 ? 0.1981 0.1990 0.1893 -0.0148 -0.0380 0.0086  424 ILE   A CD1 
6512  N  N   . PRO   A 425 ? 0.1493 0.1290 0.1436 -0.0153 -0.0353 0.0112  425 PRO   A N   
6513  C  CA  . PRO   A 425 ? 0.1451 0.1180 0.1359 -0.0171 -0.0360 0.0122  425 PRO   A CA  
6514  C  C   . PRO   A 425 ? 0.1519 0.1216 0.1403 -0.0217 -0.0369 0.0137  425 PRO   A C   
6515  O  O   . PRO   A 425 ? 0.1539 0.1251 0.1434 -0.0226 -0.0384 0.0132  425 PRO   A O   
6516  C  CB  . PRO   A 425 ? 0.1433 0.1200 0.1370 -0.0169 -0.0332 0.0131  425 PRO   A CB  
6517  C  CG  . PRO   A 425 ? 0.1613 0.1451 0.1595 -0.0166 -0.0311 0.0140  425 PRO   A CG  
6518  C  CD  . PRO   A 425 ? 0.1735 0.1590 0.1703 -0.0154 -0.0325 0.0129  425 PRO   A CD  
6526  N  N   . ALA   A 426 ? 0.1574 0.1246 0.1440 -0.0248 -0.0361 0.0160  426 ALA   A N   
6527  C  CA  . ALA   A 426 ? 0.1748 0.1376 0.1548 -0.0303 -0.0369 0.0182  426 ALA   A CA  
6528  C  C   . ALA   A 426 ? 0.1343 0.1080 0.1273 -0.0338 -0.0342 0.0191  426 ALA   A C   
6529  O  O   . ALA   A 426 ? 0.1497 0.1243 0.1385 -0.0388 -0.0328 0.0213  426 ALA   A O   
6530  C  CB  . ALA   A 426 ? 0.1535 0.1111 0.1324 -0.0326 -0.0370 0.0206  426 ALA   A CB  
6536  N  N   . TYR   A 427 ? 0.1441 0.1240 0.1402 -0.0319 -0.0343 0.0179  427 TYR   A N   
6537  C  CA  . TYR   A 427 ? 0.1671 0.1554 0.1659 -0.0346 -0.0329 0.0184  427 TYR   A CA  
6538  C  C   . TYR   A 427 ? 0.1596 0.1499 0.1613 -0.0337 -0.0359 0.0172  427 TYR   A C   
6539  O  O   . TYR   A 427 ? 0.1395 0.1314 0.1442 -0.0297 -0.0362 0.0160  427 TYR   A O   
6540  C  CB  . TYR   A 427 ? 0.1275 0.1260 0.1380 -0.0326 -0.0294 0.0185  427 TYR   A CB  
6541  C  CG  . TYR   A 427 ? 0.1394 0.1356 0.1434 -0.0316 -0.0266 0.0187  427 TYR   A CG  
6542  C  CD1 . TYR   A 427 ? 0.1212 0.1140 0.1263 -0.0277 -0.0268 0.0176  427 TYR   A CD1 
6543  C  CD2 . TYR   A 427 ? 0.1428 0.1429 0.1469 -0.0355 -0.0237 0.0196  427 TYR   A CD2 
6544  C  CE1 . TYR   A 427 ? 0.1491 0.1396 0.1466 -0.0267 -0.0251 0.0175  427 TYR   A CE1 
6545  C  CE2 . TYR   A 427 ? 0.1265 0.1259 0.1285 -0.0347 -0.0215 0.0192  427 TYR   A CE2 
6546  C  CZ  . TYR   A 427 ? 0.1299 0.1244 0.1307 -0.0304 -0.0223 0.0183  427 TYR   A CZ  
6547  O  OH  . TYR   A 427 ? 0.1664 0.1593 0.1588 -0.0297 -0.0208 0.0174  427 TYR   A OH  
6557  N  N   . ASP   A 428 ? 0.1288 0.1209 0.1358 -0.0380 -0.0379 0.0171  428 ASP   A N   
6558  C  CA  . ASP   A 428 ? 0.1342 0.1279 0.1398 -0.0374 -0.0414 0.0153  428 ASP   A CA  
6559  C  C   . ASP   A 428 ? 0.1323 0.1374 0.1448 -0.0360 -0.0405 0.0162  428 ASP   A C   
6560  O  O   . ASP   A 428 ? 0.1269 0.1395 0.1471 -0.0390 -0.0395 0.0173  428 ASP   A O   
6561  C  CB  . ASP   A 428 ? 0.1243 0.1138 0.1305 -0.0426 -0.0450 0.0145  428 ASP   A CB  
6562  C  CG  . ASP   A 428 ? 0.1480 0.1375 0.1526 -0.0416 -0.0485 0.0114  428 ASP   A CG  
6563  O  OD1 . ASP   A 428 ? 0.1430 0.1389 0.1477 -0.0380 -0.0489 0.0111  428 ASP   A OD1 
6564  O  OD2 . ASP   A 428 ? 0.2082 0.1898 0.2053 -0.0435 -0.0510 0.0097  428 ASP   A OD2 
6569  N  N   . PRO   A 429 ? 0.1149 0.1237 0.1317 -0.0315 -0.0407 0.0161  429 PRO   A N   
6570  C  CA  . PRO   A 429 ? 0.1348 0.1516 0.1528 -0.0297 -0.0410 0.0178  429 PRO   A CA  
6571  C  C   . PRO   A 429 ? 0.1324 0.1556 0.1554 -0.0318 -0.0446 0.0174  429 PRO   A C   
6572  O  O   . PRO   A 429 ? 0.1263 0.1575 0.1572 -0.0305 -0.0453 0.0186  429 PRO   A O   
6573  C  CB  . PRO   A 429 ? 0.1157 0.1318 0.1348 -0.0256 -0.0411 0.0184  429 PRO   A CB  
6574  C  CG  . PRO   A 429 ? 0.1497 0.1589 0.1568 -0.0257 -0.0423 0.0162  429 PRO   A CG  
6575  C  CD  . PRO   A 429 ? 0.1437 0.1465 0.1500 -0.0282 -0.0417 0.0149  429 PRO   A CD  
6583  N  N   . ARG   A 430 ? 0.1178 0.1378 0.1397 -0.0348 -0.0471 0.0154  430 ARG   A N   
6584  C  CA  . ARG   A 430 ? 0.1494 0.1727 0.1669 -0.0363 -0.0495 0.0139  430 ARG   A CA  
6585  C  C   . ARG   A 430 ? 0.1099 0.1430 0.1436 -0.0392 -0.0480 0.0147  430 ARG   A C   
6586  O  O   . ARG   A 430 ? 0.1275 0.1675 0.1631 -0.0387 -0.0498 0.0144  430 ARG   A O   
6587  C  CB  . ARG   A 430 ? 0.1306 0.1479 0.1482 -0.0388 -0.0520 0.0107  430 ARG   A CB  
6588  C  CG  . ARG   A 430 ? 0.1624 0.1739 0.1681 -0.0356 -0.0537 0.0083  430 ARG   A CG  
6589  C  CD  . ARG   A 430 ? 0.1678 0.1719 0.1697 -0.0370 -0.0563 0.0041  430 ARG   A CD  
6590  N  NE  . ARG   A 430 ? 0.1806 0.1741 0.1789 -0.0388 -0.0560 0.0036  430 ARG   A NE  
6591  C  CZ  . ARG   A 430 ? 0.1842 0.1678 0.1781 -0.0385 -0.0583 -0.0001 430 ARG   A CZ  
6592  N  NH1 . ARG   A 430 ? 0.1965 0.1800 0.1863 -0.0375 -0.0612 -0.0046 430 ARG   A NH1 
6593  N  NH2 . ARG   A 430 ? 0.1876 0.1612 0.1786 -0.0391 -0.0579 0.0004  430 ARG   A NH2 
6607  N  N   . GLY   A 431 ? 0.0979 0.1301 0.1330 -0.0415 -0.0447 0.0159  431 GLY   A N   
6608  C  CA  . GLY   A 431 ? 0.1070 0.1494 0.1513 -0.0441 -0.0421 0.0161  431 GLY   A CA  
6609  C  C   . GLY   A 431 ? 0.1407 0.1884 0.1862 -0.0410 -0.0392 0.0171  431 GLY   A C   
6610  O  O   . GLY   A 431 ? 0.1225 0.1799 0.1795 -0.0434 -0.0359 0.0168  431 GLY   A O   
6614  N  N   . ILE   A 432 ? 0.1122 0.1569 0.1596 -0.0356 -0.0393 0.0180  432 ILE   A N   
6615  C  CA  . ILE   A 432 ? 0.0886 0.1365 0.1418 -0.0310 -0.0364 0.0179  432 ILE   A CA  
6616  C  C   . ILE   A 432 ? 0.0900 0.1363 0.1428 -0.0255 -0.0392 0.0194  432 ILE   A C   
6617  O  O   . ILE   A 432 ? 0.0984 0.1361 0.1428 -0.0235 -0.0390 0.0204  432 ILE   A O   
6618  C  CB  . ILE   A 432 ? 0.1193 0.1588 0.1628 -0.0314 -0.0323 0.0178  432 ILE   A CB  
6619  C  CG1 . ILE   A 432 ? 0.1393 0.1738 0.1763 -0.0372 -0.0314 0.0180  432 ILE   A CG1 
6620  C  CG2 . ILE   A 432 ? 0.1000 0.1461 0.1514 -0.0285 -0.0285 0.0163  432 ILE   A CG2 
6621  C  CD1 . ILE   A 432 ? 0.1291 0.1546 0.1602 -0.0371 -0.0292 0.0183  432 ILE   A CD1 
6633  N  N   . GLN   A 433 ? 0.1107 0.1641 0.1681 -0.0233 -0.0425 0.0198  433 GLN   A N   
6634  C  CA  . GLN   A 433 ? 0.1048 0.1565 0.1638 -0.0191 -0.0462 0.0224  433 GLN   A CA  
6635  C  C   . GLN   A 433 ? 0.1110 0.1562 0.1659 -0.0150 -0.0448 0.0238  433 GLN   A C   
6636  O  O   . GLN   A 433 ? 0.0894 0.1288 0.1407 -0.0140 -0.0461 0.0263  433 GLN   A O   
6637  C  CB  . GLN   A 433 ? 0.1146 0.1735 0.1782 -0.0169 -0.0494 0.0220  433 GLN   A CB  
6638  C  CG  . GLN   A 433 ? 0.1170 0.1803 0.1808 -0.0208 -0.0507 0.0202  433 GLN   A CG  
6639  C  CD  . GLN   A 433 ? 0.1373 0.1937 0.1892 -0.0222 -0.0529 0.0209  433 GLN   A CD  
6640  O  OE1 . GLN   A 433 ? 0.1261 0.1774 0.1725 -0.0197 -0.0539 0.0233  433 GLN   A OE1 
6641  N  NE2 . GLN   A 433 ? 0.1645 0.2210 0.2127 -0.0263 -0.0535 0.0187  433 GLN   A NE2 
6650  N  N   . GLY   A 434 ? 0.0925 0.1411 0.1574 -0.0124 -0.0422 0.0218  434 GLY   A N   
6651  C  CA  . GLY   A 434 ? 0.0868 0.1291 0.1516 -0.0085 -0.0417 0.0225  434 GLY   A CA  
6652  C  C   . GLY   A 434 ? 0.0913 0.1249 0.1468 -0.0105 -0.0385 0.0227  434 GLY   A C   
6653  O  O   . GLY   A 434 ? 0.0911 0.1183 0.1428 -0.0093 -0.0397 0.0251  434 GLY   A O   
6657  N  N   . HIS   A 435 ? 0.1060 0.1391 0.1553 -0.0141 -0.0353 0.0208  435 HIS   A N   
6658  C  CA  . HIS   A 435 ? 0.0922 0.1183 0.1369 -0.0152 -0.0331 0.0205  435 HIS   A CA  
6659  C  C   . HIS   A 435 ? 0.1091 0.1297 0.1432 -0.0161 -0.0351 0.0227  435 HIS   A C   
6660  O  O   . HIS   A 435 ? 0.1129 0.1288 0.1436 -0.0154 -0.0341 0.0230  435 HIS   A O   
6661  C  CB  . HIS   A 435 ? 0.1133 0.1385 0.1515 -0.0191 -0.0301 0.0186  435 HIS   A CB  
6662  C  CG  . HIS   A 435 ? 0.1190 0.1374 0.1521 -0.0191 -0.0281 0.0181  435 HIS   A CG  
6663  N  ND1 . HIS   A 435 ? 0.1095 0.1268 0.1454 -0.0166 -0.0264 0.0168  435 HIS   A ND1 
6664  C  CD2 . HIS   A 435 ? 0.1525 0.1641 0.1753 -0.0212 -0.0282 0.0180  435 HIS   A CD2 
6665  C  CE1 . HIS   A 435 ? 0.1548 0.1649 0.1792 -0.0172 -0.0254 0.0164  435 HIS   A CE1 
6666  N  NE2 . HIS   A 435 ? 0.1495 0.1573 0.1717 -0.0199 -0.0266 0.0171  435 HIS   A NE2 
6674  N  N   . GLY   A 436 ? 0.1039 0.1279 0.1382 -0.0175 -0.0379 0.0236  436 GLY   A N   
6675  C  CA  . GLY   A 436 ? 0.1149 0.1360 0.1406 -0.0179 -0.0399 0.0249  436 GLY   A CA  
6676  C  C   . GLY   A 436 ? 0.1030 0.1232 0.1302 -0.0160 -0.0408 0.0282  436 GLY   A C   
6677  O  O   . GLY   A 436 ? 0.1167 0.1346 0.1360 -0.0163 -0.0403 0.0288  436 GLY   A O   
6681  N  N   . ILE   A 437 ? 0.0968 0.1189 0.1309 -0.0133 -0.0423 0.0302  437 ILE   A N   
6682  C  CA  . ILE   A 437 ? 0.1149 0.1327 0.1458 -0.0120 -0.0437 0.0342  437 ILE   A CA  
6683  C  C   . ILE   A 437 ? 0.0852 0.0994 0.1202 -0.0122 -0.0404 0.0335  437 ILE   A C   
6684  O  O   . ILE   A 437 ? 0.1221 0.1331 0.1469 -0.0133 -0.0401 0.0359  437 ILE   A O   
6685  C  CB  . ILE   A 437 ? 0.1055 0.1250 0.1486 -0.0088 -0.0468 0.0358  437 ILE   A CB  
6686  C  CG1 . ILE   A 437 ? 0.1043 0.1297 0.1510 -0.0080 -0.0494 0.0353  437 ILE   A CG1 
6687  C  CG2 . ILE   A 437 ? 0.1216 0.1346 0.1622 -0.0077 -0.0482 0.0400  437 ILE   A CG2 
6688  C  CD1 . ILE   A 437 ? 0.1303 0.1564 0.1827 -0.0040 -0.0520 0.0355  437 ILE   A CD1 
6700  N  N   . THR   A 438 ? 0.0981 0.1099 0.1312 -0.0115 -0.0377 0.0298  438 THR   A N   
6701  C  CA  . THR   A 438 ? 0.0852 0.0932 0.1191 -0.0116 -0.0351 0.0283  438 THR   A CA  
6702  C  C   . THR   A 438 ? 0.0920 0.0993 0.1184 -0.0136 -0.0340 0.0283  438 THR   A C   
6703  O  O   . THR   A 438 ? 0.0993 0.1048 0.1229 -0.0142 -0.0333 0.0295  438 THR   A O   
6704  C  CB  . THR   A 438 ? 0.0924 0.1004 0.1293 -0.0107 -0.0326 0.0240  438 THR   A CB  
6705  O  OG1 . THR   A 438 ? 0.1138 0.1229 0.1556 -0.0080 -0.0332 0.0230  438 THR   A OG1 
6706  C  CG2 . THR   A 438 ? 0.1088 0.1124 0.1405 -0.0111 -0.0304 0.0221  438 THR   A CG2 
6714  N  N   . TYR   A 439 ? 0.1166 0.1253 0.1369 -0.0147 -0.0338 0.0263  439 TYR   A N   
6715  C  CA  . TYR   A 439 ? 0.1287 0.1366 0.1401 -0.0155 -0.0331 0.0249  439 TYR   A CA  
6716  C  C   . TYR   A 439 ? 0.1018 0.1139 0.1162 -0.0161 -0.0338 0.0280  439 TYR   A C   
6717  O  O   . TYR   A 439 ? 0.1278 0.1398 0.1358 -0.0165 -0.0320 0.0275  439 TYR   A O   
6718  C  CB  . TYR   A 439 ? 0.1063 0.1154 0.1186 -0.0162 -0.0341 0.0224  439 TYR   A CB  
6719  C  CG  . TYR   A 439 ? 0.1173 0.1223 0.1272 -0.0172 -0.0334 0.0199  439 TYR   A CG  
6720  C  CD1 . TYR   A 439 ? 0.1031 0.1055 0.1160 -0.0164 -0.0314 0.0191  439 TYR   A CD1 
6721  C  CD2 . TYR   A 439 ? 0.1207 0.1258 0.1310 -0.0190 -0.0349 0.0186  439 TYR   A CD2 
6722  C  CE1 . TYR   A 439 ? 0.1127 0.1120 0.1236 -0.0176 -0.0309 0.0177  439 TYR   A CE1 
6723  C  CE2 . TYR   A 439 ? 0.1391 0.1402 0.1466 -0.0209 -0.0341 0.0174  439 TYR   A CE2 
6724  C  CZ  . TYR   A 439 ? 0.1263 0.1255 0.1373 -0.0202 -0.0320 0.0173  439 TYR   A CZ  
6725  O  OH  . TYR   A 439 ? 0.1659 0.1611 0.1714 -0.0226 -0.0315 0.0169  439 TYR   A OH  
6735  N  N   . ALA   A 440 ? 0.1104 0.1245 0.1216 -0.0166 -0.0360 0.0313  440 ALA   A N   
6736  C  CA  . ALA   A 440 ? 0.1166 0.1344 0.1260 -0.0179 -0.0372 0.0350  440 ALA   A CA  
6737  C  C   . ALA   A 440 ? 0.1181 0.1338 0.1278 -0.0190 -0.0365 0.0394  440 ALA   A C   
6738  O  O   . ALA   A 440 ? 0.1368 0.1557 0.1405 -0.0210 -0.0350 0.0410  440 ALA   A O   
6739  C  CB  . ALA   A 440 ? 0.1708 0.1903 0.1739 -0.0181 -0.0407 0.0375  440 ALA   A CB  
6745  N  N   . VAL   A 441 ? 0.1142 0.1250 0.1300 -0.0177 -0.0375 0.0405  441 VAL   A N   
6746  C  CA  . VAL   A 441 ? 0.1087 0.1157 0.1289 -0.0190 -0.0380 0.0452  441 VAL   A CA  
6747  C  C   . VAL   A 441 ? 0.1105 0.1145 0.1336 -0.0190 -0.0355 0.0424  441 VAL   A C   
6748  O  O   . VAL   A 441 ? 0.1314 0.1318 0.1542 -0.0211 -0.0360 0.0455  441 VAL   A O   
6749  C  CB  . VAL   A 441 ? 0.1268 0.1295 0.1517 -0.0171 -0.0423 0.0485  441 VAL   A CB  
6750  C  CG1 . VAL   A 441 ? 0.1386 0.1442 0.1591 -0.0168 -0.0445 0.0505  441 VAL   A CG1 
6751  C  CG2 . VAL   A 441 ? 0.1478 0.1476 0.1782 -0.0136 -0.0421 0.0439  441 VAL   A CG2 
6761  N  N   . ASN   A 442 ? 0.1173 0.1214 0.1398 -0.0172 -0.0334 0.0367  442 ASN   A N   
6762  C  CA  . ASN   A 442 ? 0.1201 0.1218 0.1453 -0.0172 -0.0317 0.0335  442 ASN   A CA  
6763  C  C   . ASN   A 442 ? 0.1120 0.1159 0.1383 -0.0202 -0.0305 0.0355  442 ASN   A C   
6764  O  O   . ASN   A 442 ? 0.1327 0.1420 0.1517 -0.0214 -0.0289 0.0357  442 ASN   A O   
6765  C  CB  . ASN   A 442 ? 0.1359 0.1378 0.1582 -0.0154 -0.0301 0.0282  442 ASN   A CB  
6766  C  CG  . ASN   A 442 ? 0.1301 0.1288 0.1543 -0.0146 -0.0291 0.0248  442 ASN   A CG  
6767  O  OD1 . ASN   A 442 ? 0.1203 0.1183 0.1491 -0.0158 -0.0290 0.0254  442 ASN   A OD1 
6768  N  ND2 . ASN   A 442 ? 0.1075 0.1055 0.1331 -0.0131 -0.0285 0.0216  442 ASN   A ND2 
6775  N  N   . ASN   A 443 ? 0.1247 0.1240 0.1533 -0.0214 -0.0312 0.0373  443 ASN   A N   
6776  C  CA  . ASN   A 443 ? 0.1310 0.1325 0.1602 -0.0256 -0.0302 0.0398  443 ASN   A CA  
6777  C  C   . ASN   A 443 ? 0.1161 0.1251 0.1468 -0.0255 -0.0273 0.0352  443 ASN   A C   
6778  O  O   . ASN   A 443 ? 0.1567 0.1710 0.1826 -0.0287 -0.0256 0.0368  443 ASN   A O   
6779  C  CB  . ASN   A 443 ? 0.1447 0.1393 0.1810 -0.0272 -0.0323 0.0421  443 ASN   A CB  
6780  C  CG  . ASN   A 443 ? 0.1808 0.1670 0.2124 -0.0272 -0.0360 0.0475  443 ASN   A CG  
6781  O  OD1 . ASN   A 443 ? 0.1551 0.1450 0.1894 -0.0292 -0.0368 0.0528  443 ASN   A OD1 
6782  N  ND2 . ASN   A 443 ? 0.1273 0.1071 0.1723 -0.0248 -0.0387 0.0455  443 ASN   A ND2 
6789  N  N   . ARG   A 444 ? 0.1115 0.1188 0.1399 -0.0219 -0.0271 0.0295  444 ARG   A N   
6790  C  CA  . ARG   A 444 ? 0.1183 0.1303 0.1457 -0.0209 -0.0255 0.0250  444 ARG   A CA  
6791  C  C   . ARG   A 444 ? 0.1372 0.1527 0.1563 -0.0187 -0.0249 0.0224  444 ARG   A C   
6792  O  O   . ARG   A 444 ? 0.1152 0.1348 0.1376 -0.0168 -0.0243 0.0183  444 ARG   A O   
6793  C  CB  . ARG   A 444 ? 0.1090 0.1164 0.1392 -0.0188 -0.0266 0.0208  444 ARG   A CB  
6794  C  CG  . ARG   A 444 ? 0.1157 0.1190 0.1409 -0.0154 -0.0270 0.0177  444 ARG   A CG  
6795  C  CD  . ARG   A 444 ? 0.1025 0.1025 0.1306 -0.0139 -0.0279 0.0142  444 ARG   A CD  
6796  N  NE  . ARG   A 444 ? 0.1238 0.1204 0.1448 -0.0118 -0.0283 0.0118  444 ARG   A NE  
6797  C  CZ  . ARG   A 444 ? 0.1221 0.1165 0.1388 -0.0103 -0.0292 0.0089  444 ARG   A CZ  
6798  N  NH1 . ARG   A 444 ? 0.0943 0.0919 0.1177 -0.0101 -0.0303 0.0070  444 ARG   A NH1 
6799  N  NH2 . ARG   A 444 ? 0.0925 0.0846 0.1084 -0.0090 -0.0297 0.0082  444 ARG   A NH2 
6813  N  N   . GLY   A 445 ? 0.1186 0.1348 0.1381 -0.0187 -0.0253 0.0246  445 GLY   A N   
6814  C  CA  . GLY   A 445 ? 0.1242 0.1428 0.1376 -0.0169 -0.0253 0.0220  445 GLY   A CA  
6815  C  C   . GLY   A 445 ? 0.1333 0.1453 0.1426 -0.0149 -0.0268 0.0201  445 GLY   A C   
6816  O  O   . GLY   A 445 ? 0.1196 0.1274 0.1346 -0.0147 -0.0274 0.0207  445 GLY   A O   
6820  N  N   . GLY   A 446 ? 0.1089 0.1219 0.1174 -0.0135 -0.0275 0.0170  446 GLY   A N   
6821  C  CA  . GLY   A 446 ? 0.1134 0.1210 0.1200 -0.0127 -0.0291 0.0158  446 GLY   A CA  
6822  C  C   . GLY   A 446 ? 0.1383 0.1395 0.1426 -0.0120 -0.0291 0.0147  446 GLY   A C   
6823  O  O   . GLY   A 446 ? 0.1224 0.1231 0.1295 -0.0103 -0.0294 0.0122  446 GLY   A O   
6827  N  N   . CYS   A 447 ? 0.1157 0.1159 0.1270 -0.0130 -0.0289 0.0165  447 CYS   A N   
6828  C  CA  . CYS   A 447 ? 0.1189 0.1151 0.1296 -0.0126 -0.0284 0.0157  447 CYS   A CA  
6829  C  C   . CYS   A 447 ? 0.0993 0.0962 0.1154 -0.0131 -0.0280 0.0168  447 CYS   A C   
6830  O  O   . CYS   A 447 ? 0.1002 0.0992 0.1177 -0.0136 -0.0283 0.0189  447 CYS   A O   
6831  C  CB  . CYS   A 447 ? 0.1280 0.1246 0.1417 -0.0119 -0.0278 0.0150  447 CYS   A CB  
6832  S  SG  . CYS   A 447 ? 0.1316 0.1254 0.1479 -0.0114 -0.0274 0.0139  447 CYS   A SG  
6838  N  N   . HIS   A 448 ? 0.1196 0.1140 0.1314 -0.0136 -0.0275 0.0154  448 HIS   A N   
6839  C  CA  . HIS   A 448 ? 0.1180 0.1151 0.1339 -0.0145 -0.0263 0.0155  448 HIS   A CA  
6840  C  C   . HIS   A 448 ? 0.1336 0.1307 0.1506 -0.0127 -0.0249 0.0140  448 HIS   A C   
6841  O  O   . HIS   A 448 ? 0.1071 0.1086 0.1338 -0.0120 -0.0247 0.0138  448 HIS   A O   
6842  C  CB  . HIS   A 448 ? 0.0997 0.0962 0.1149 -0.0165 -0.0258 0.0151  448 HIS   A CB  
6843  C  CG  . HIS   A 448 ? 0.1600 0.1499 0.1596 -0.0164 -0.0253 0.0137  448 HIS   A CG  
6844  N  ND1 . HIS   A 448 ? 0.1288 0.1168 0.1347 -0.0147 -0.0272 0.0132  448 HIS   A ND1 
6845  C  CD2 . HIS   A 448 ? 0.1113 0.1034 0.1189 -0.0174 -0.0239 0.0132  448 HIS   A CD2 
6846  C  CE1 . HIS   A 448 ? 0.1536 0.1375 0.1513 -0.0148 -0.0271 0.0121  448 HIS   A CE1 
6847  N  NE2 . HIS   A 448 ? 0.1481 0.1339 0.1451 -0.0165 -0.0252 0.0123  448 HIS   A NE2 
6855  N  N   . ILE   A 449 ? 0.1158 0.1111 0.1360 -0.0121 -0.0250 0.0123  449 ILE   A N   
6856  C  CA  . ILE   A 449 ? 0.1465 0.1407 0.1625 -0.0105 -0.0237 0.0095  449 ILE   A CA  
6857  C  C   . ILE   A 449 ? 0.1376 0.1316 0.1625 -0.0089 -0.0248 0.0093  449 ILE   A C   
6858  O  O   . ILE   A 449 ? 0.1113 0.1060 0.1421 -0.0071 -0.0241 0.0061  449 ILE   A O   
6859  C  CB  . ILE   A 449 ? 0.1046 0.0974 0.1233 -0.0107 -0.0239 0.0079  449 ILE   A CB  
6860  C  CG1 . ILE   A 449 ? 0.1066 0.1006 0.1199 -0.0103 -0.0218 0.0046  449 ILE   A CG1 
6861  C  CG2 . ILE   A 449 ? 0.1619 0.1509 0.1735 -0.0099 -0.0256 0.0074  449 ILE   A CG2 
6862  C  CD1 . ILE   A 449 ? 0.1234 0.1217 0.1347 -0.0119 -0.0196 0.0048  449 ILE   A CD1 
6874  N  N   . LYS   A 450 ? 0.1169 0.1105 0.1469 -0.0094 -0.0263 0.0122  450 LYS   A N   
6875  C  CA  . LYS   A 450 ? 0.1133 0.1050 0.1507 -0.0081 -0.0280 0.0133  450 LYS   A CA  
6876  C  C   . LYS   A 450 ? 0.1429 0.1354 0.1802 -0.0067 -0.0287 0.0142  450 LYS   A C   
6877  O  O   . LYS   A 450 ? 0.1345 0.1251 0.1805 -0.0052 -0.0310 0.0155  450 LYS   A O   
6878  C  CB  . LYS   A 450 ? 0.1241 0.1137 0.1578 -0.0101 -0.0291 0.0167  450 LYS   A CB  
6879  C  CG  . LYS   A 450 ? 0.1050 0.0955 0.1391 -0.0115 -0.0288 0.0152  450 LYS   A CG  
6880  C  CD  . LYS   A 450 ? 0.1182 0.1054 0.1515 -0.0106 -0.0290 0.0115  450 LYS   A CD  
6881  C  CE  . LYS   A 450 ? 0.1238 0.1115 0.1533 -0.0094 -0.0281 0.0077  450 LYS   A CE  
6882  N  NZ  . LYS   A 450 ? 0.1325 0.1180 0.1616 -0.0088 -0.0288 0.0038  450 LYS   A NZ  
6896  N  N   . GLY   A 451 ? 0.1176 0.1160 0.1582 -0.0070 -0.0276 0.0142  451 GLY   A N   
6897  C  CA  . GLY   A 451 ? 0.1212 0.1234 0.1657 -0.0053 -0.0283 0.0145  451 GLY   A CA  
6898  C  C   . GLY   A 451 ? 0.1286 0.1366 0.1708 -0.0067 -0.0262 0.0129  451 GLY   A C   
6899  O  O   . GLY   A 451 ? 0.1305 0.1416 0.1730 -0.0083 -0.0270 0.0152  451 GLY   A O   
6903  N  N   . TYR   A 452 ? 0.1153 0.1265 0.1603 -0.0065 -0.0232 0.0091  452 TYR   A N   
6904  C  CA  . TYR   A 452 ? 0.1627 0.1774 0.1972 -0.0093 -0.0206 0.0081  452 TYR   A CA  
6905  C  C   . TYR   A 452 ? 0.1316 0.1568 0.1798 -0.0086 -0.0203 0.0073  452 TYR   A C   
6906  O  O   . TYR   A 452 ? 0.1246 0.1567 0.1752 -0.0079 -0.0175 0.0037  452 TYR   A O   
6907  C  CB  . TYR   A 452 ? 0.1349 0.1511 0.1703 -0.0100 -0.0178 0.0053  452 TYR   A CB  
6908  C  CG  . TYR   A 452 ? 0.1359 0.1522 0.1605 -0.0145 -0.0159 0.0065  452 TYR   A CG  
6909  C  CD1 . TYR   A 452 ? 0.1115 0.1231 0.1347 -0.0172 -0.0177 0.0099  452 TYR   A CD1 
6910  C  CD2 . TYR   A 452 ? 0.1171 0.1410 0.1443 -0.0164 -0.0123 0.0044  452 TYR   A CD2 
6911  C  CE1 . TYR   A 452 ? 0.1449 0.1542 0.1570 -0.0213 -0.0170 0.0115  452 TYR   A CE1 
6912  C  CE2 . TYR   A 452 ? 0.1426 0.1656 0.1592 -0.0213 -0.0110 0.0067  452 TYR   A CE2 
6913  C  CZ  . TYR   A 452 ? 0.1425 0.1579 0.1549 -0.0239 -0.0136 0.0106  452 TYR   A CZ  
6914  O  OH  . TYR   A 452 ? 0.1483 0.1613 0.1528 -0.0292 -0.0131 0.0132  452 TYR   A OH  
6924  N  N   . MET   A 453 ? 0.1335 0.1592 0.1818 -0.0091 -0.0229 0.0102  453 MET   A N   
6925  C  CA  . MET   A 453 ? 0.0992 0.1354 0.1595 -0.0085 -0.0233 0.0097  453 MET   A CA  
6926  C  C   . MET   A 453 ? 0.1130 0.1556 0.1689 -0.0133 -0.0203 0.0087  453 MET   A C   
6927  O  O   . MET   A 453 ? 0.1155 0.1685 0.1790 -0.0137 -0.0194 0.0075  453 MET   A O   
6928  C  CB  . MET   A 453 ? 0.1079 0.1426 0.1681 -0.0084 -0.0277 0.0133  453 MET   A CB  
6929  C  CG  . MET   A 453 ? 0.1286 0.1598 0.1926 -0.0037 -0.0315 0.0146  453 MET   A CG  
6930  S  SD  . MET   A 453 ? 0.1276 0.1655 0.2067 0.0021  -0.0323 0.0105  453 MET   A SD  
6931  C  CE  . MET   A 453 ? 0.1628 0.2097 0.2459 0.0026  -0.0358 0.0119  453 MET   A CE  
6941  N  N   . ILE   A 454 ? 0.1145 0.1516 0.1615 -0.0172 -0.0183 0.0098  454 ILE   A N   
6942  C  CA  . ILE   A 454 ? 0.1206 0.1620 0.1627 -0.0225 -0.0153 0.0098  454 ILE   A CA  
6943  C  C   . ILE   A 454 ? 0.1197 0.1729 0.1704 -0.0215 -0.0109 0.0059  454 ILE   A C   
6944  O  O   . ILE   A 454 ? 0.1480 0.2104 0.1986 -0.0255 -0.0085 0.0055  454 ILE   A O   
6945  C  CB  . ILE   A 454 ? 0.1062 0.1383 0.1409 -0.0255 -0.0150 0.0118  454 ILE   A CB  
6946  C  CG1 . ILE   A 454 ? 0.1093 0.1316 0.1370 -0.0257 -0.0190 0.0146  454 ILE   A CG1 
6947  C  CG2 . ILE   A 454 ? 0.1580 0.1918 0.1822 -0.0314 -0.0122 0.0127  454 ILE   A CG2 
6948  C  CD1 . ILE   A 454 ? 0.1284 0.1527 0.1560 -0.0291 -0.0210 0.0161  454 ILE   A CD1 
6960  N  N   . ASN   A 455 ? 0.1262 0.1782 0.1775 -0.0165 -0.0104 0.0024  455 ASN   A N   
6961  C  CA  . ASN   A 455 ? 0.1364 0.1995 0.1927 -0.0144 -0.0063 -0.0030 455 ASN   A CA  
6962  C  C   . ASN   A 455 ? 0.1347 0.2118 0.2042 -0.0134 -0.0059 -0.0050 455 ASN   A C   
6963  O  O   . ASN   A 455 ? 0.1173 0.2065 0.1885 -0.0173 -0.0015 -0.0064 455 ASN   A O   
6964  C  CB  . ASN   A 455 ? 0.1419 0.2008 0.1996 -0.0086 -0.0067 -0.0072 455 ASN   A CB  
6965  C  CG  . ASN   A 455 ? 0.1687 0.2218 0.2149 -0.0102 -0.0046 -0.0080 455 ASN   A CG  
6966  O  OD1 . ASN   A 455 ? 0.1714 0.2208 0.2082 -0.0155 -0.0040 -0.0043 455 ASN   A OD1 
6967  N  ND2 . ASN   A 455 ? 0.1935 0.2452 0.2394 -0.0058 -0.0044 -0.0130 455 ASN   A ND2 
6974  N  N   . PRO   A 456 ? 0.1656 0.2412 0.2380 -0.0083 -0.0101 -0.0052 456 PRO   A N   
6975  C  CA  . PRO   A 456 ? 0.1272 0.2184 0.2204 -0.0064 -0.0106 -0.0075 456 PRO   A CA  
6976  C  C   . PRO   A 456 ? 0.1349 0.2303 0.2243 -0.0126 -0.0116 -0.0036 456 PRO   A C   
6977  O  O   . PRO   A 456 ? 0.1106 0.2214 0.2121 -0.0141 -0.0096 -0.0057 456 PRO   A O   
6978  C  CB  . PRO   A 456 ? 0.1264 0.2119 0.2255 0.0010  -0.0163 -0.0078 456 PRO   A CB  
6979  C  CG  . PRO   A 456 ? 0.1512 0.2193 0.2364 -0.0001 -0.0192 -0.0030 456 PRO   A CG  
6980  C  CD  . PRO   A 456 ? 0.1143 0.1796 0.1963 -0.0040 -0.0151 -0.0033 456 PRO   A CD  
6988  N  N   . GLU   A 457 ? 0.1177 0.2018 0.2012 -0.0157 -0.0148 0.0016  457 GLU   A N   
6989  C  CA  . GLU   A 457 ? 0.0959 0.1834 0.1818 -0.0212 -0.0171 0.0048  457 GLU   A CA  
6990  C  C   . GLU   A 457 ? 0.1341 0.2242 0.2100 -0.0295 -0.0131 0.0057  457 GLU   A C   
6991  O  O   . GLU   A 457 ? 0.1060 0.2048 0.1905 -0.0344 -0.0136 0.0068  457 GLU   A O   
6992  C  CB  . GLU   A 457 ? 0.0889 0.1636 0.1689 -0.0207 -0.0222 0.0088  457 GLU   A CB  
6993  C  CG  . GLU   A 457 ? 0.1309 0.2024 0.2098 -0.0143 -0.0270 0.0094  457 GLU   A CG  
6994  C  CD  . GLU   A 457 ? 0.1073 0.1697 0.1829 -0.0148 -0.0315 0.0135  457 GLU   A CD  
6995  O  OE1 . GLU   A 457 ? 0.1077 0.1594 0.1745 -0.0147 -0.0311 0.0150  457 GLU   A OE1 
6996  O  OE2 . GLU   A 457 ? 0.0877 0.1544 0.1673 -0.0154 -0.0354 0.0148  457 GLU   A OE2 
7003  N  N   . ILE   A 458 ? 0.1400 0.2254 0.2099 -0.0316 -0.0092 0.0062  458 ILE   A N   
7004  C  CA  . ILE   A 458 ? 0.1544 0.2399 0.2141 -0.0403 -0.0061 0.0085  458 ILE   A CA  
7005  C  C   . ILE   A 458 ? 0.1298 0.2259 0.1918 -0.0417 0.0003  0.0058  458 ILE   A C   
7006  O  O   . ILE   A 458 ? 0.1030 0.2107 0.1682 -0.0484 0.0039  0.0062  458 ILE   A O   
7007  C  CB  . ILE   A 458 ? 0.1487 0.2175 0.2009 -0.0429 -0.0087 0.0126  458 ILE   A CB  
7008  C  CG1 . ILE   A 458 ? 0.1965 0.2562 0.2438 -0.0420 -0.0144 0.0146  458 ILE   A CG1 
7009  C  CG2 . ILE   A 458 ? 0.1717 0.2373 0.2109 -0.0513 -0.0062 0.0157  458 ILE   A CG2 
7010  C  CD1 . ILE   A 458 ? 0.2254 0.2863 0.2726 -0.0490 -0.0163 0.0166  458 ILE   A CD1 
7022  N  N   . LEU   A 459 ? 0.1405 0.2330 0.1984 -0.0361 0.0019  0.0029  459 LEU   A N   
7023  C  CA  . LEU   A 459 ? 0.1395 0.2411 0.1983 -0.0375 0.0080  -0.0003 459 LEU   A CA  
7024  C  C   . LEU   A 459 ? 0.1731 0.2917 0.2383 -0.0326 0.0116  -0.0072 459 LEU   A C   
7025  O  O   . LEU   A 459 ? 0.1744 0.3048 0.2403 -0.0350 0.0173  -0.0101 459 LEU   A O   
7026  C  CB  . LEU   A 459 ? 0.1815 0.2683 0.2223 -0.0345 0.0071  -0.0001 459 LEU   A CB  
7027  C  CG  . LEU   A 459 ? 0.1706 0.2414 0.2042 -0.0382 0.0036  0.0059  459 LEU   A CG  
7028  C  CD1 . LEU   A 459 ? 0.1775 0.2365 0.2006 -0.0339 0.0021  0.0048  459 LEU   A CD1 
7029  C  CD2 . LEU   A 459 ? 0.2096 0.2797 0.2308 -0.0475 0.0055  0.0105  459 LEU   A CD2 
7041  N  N   . GLY   A 460 ? 0.1516 0.2742 0.2345 -0.0254 0.0080  -0.0104 460 GLY   A N   
7042  C  CA  . GLY   A 460 ? 0.1833 0.3215 0.2744 -0.0195 0.0102  -0.0177 460 GLY   A CA  
7043  C  C   . GLY   A 460 ? 0.1570 0.2924 0.2512 -0.0111 0.0103  -0.0239 460 GLY   A C   
7044  O  O   . GLY   A 460 ? 0.1190 0.2697 0.2245 -0.0067 0.0139  -0.0312 460 GLY   A O   
7048  N  N   . TYR   A 461 ? 0.1506 0.2682 0.2393 -0.0088 0.0067  -0.0215 461 TYR   A N   
7049  C  CA  . TYR   A 461 ? 0.1831 0.2927 0.2633 -0.0013 0.0056  -0.0269 461 TYR   A CA  
7050  C  C   . TYR   A 461 ? 0.1268 0.2278 0.2263 0.0051  -0.0014 -0.0258 461 TYR   A C   
7051  O  O   . TYR   A 461 ? 0.1552 0.2427 0.2419 0.0024  -0.0052 -0.0192 461 TYR   A O   
7052  C  CB  . TYR   A 461 ? 0.1441 0.2453 0.2193 -0.0042 0.0072  -0.0257 461 TYR   A CB  
7053  C  CG  . TYR   A 461 ? 0.1710 0.2815 0.2332 -0.0092 0.0139  -0.0276 461 TYR   A CG  
7054  C  CD1 . TYR   A 461 ? 0.1720 0.2874 0.2312 -0.0183 0.0168  -0.0220 461 TYR   A CD1 
7055  C  CD2 . TYR   A 461 ? 0.1648 0.2818 0.2272 -0.0055 0.0173  -0.0351 461 TYR   A CD2 
7056  C  CE1 . TYR   A 461 ? 0.2191 0.3424 0.2639 -0.0238 0.0228  -0.0226 461 TYR   A CE1 
7057  C  CE2 . TYR   A 461 ? 0.1643 0.2919 0.2188 -0.0104 0.0236  -0.0367 461 TYR   A CE2 
7058  C  CZ  . TYR   A 461 ? 0.1777 0.3094 0.2257 -0.0200 0.0266  -0.0298 461 TYR   A CZ  
7059  O  OH  . TYR   A 461 ? 0.1813 0.3229 0.2184 -0.0259 0.0327  -0.0302 461 TYR   A OH  
7069  N  N   . PRO   A 462 ? 0.1714 0.2730 0.2740 0.0136  -0.0036 -0.0321 462 PRO   A N   
7070  C  CA  . PRO   A 462 ? 0.1695 0.2872 0.2827 0.0179  0.0007  -0.0413 462 PRO   A CA  
7071  C  C   . PRO   A 462 ? 0.1624 0.3000 0.2878 0.0173  0.0028  -0.0430 462 PRO   A C   
7072  O  O   . PRO   A 462 ? 0.1734 0.3275 0.3040 0.0194  0.0077  -0.0506 462 PRO   A O   
7073  C  CB  . PRO   A 462 ? 0.1757 0.2855 0.2983 0.0275  -0.0046 -0.0463 462 PRO   A CB  
7074  C  CG  . PRO   A 462 ? 0.2223 0.3184 0.3405 0.0281  -0.0117 -0.0391 462 PRO   A CG  
7075  C  CD  . PRO   A 462 ? 0.1770 0.2669 0.2892 0.0194  -0.0107 -0.0307 462 PRO   A CD  
7083  N  N   . GLU   A 463 ? 0.1592 0.2949 0.2866 0.0147  -0.0010 -0.0369 463 GLU   A N   
7084  C  CA  . GLU   A 463 ? 0.1352 0.2899 0.2778 0.0130  -0.0001 -0.0372 463 GLU   A CA  
7085  C  C   . GLU   A 463 ? 0.1353 0.2847 0.2680 0.0038  -0.0012 -0.0284 463 GLU   A C   
7086  O  O   . GLU   A 463 ? 0.1560 0.2872 0.2759 0.0014  -0.0040 -0.0227 463 GLU   A O   
7087  C  CB  . GLU   A 463 ? 0.1761 0.3333 0.3311 0.0220  -0.0064 -0.0401 463 GLU   A CB  
7088  C  CG  . GLU   A 463 ? 0.2222 0.3621 0.3753 0.0230  -0.0146 -0.0331 463 GLU   A CG  
7089  C  CD  . GLU   A 463 ? 0.2579 0.3951 0.4254 0.0326  -0.0221 -0.0345 463 GLU   A CD  
7090  O  OE1 . GLU   A 463 ? 0.2807 0.4259 0.4510 0.0338  -0.0236 -0.0344 463 GLU   A OE1 
7091  O  OE2 . GLU   A 463 ? 0.3337 0.4542 0.4927 0.0378  -0.0260 -0.0347 463 GLU   A OE2 
7098  N  N   . LYS   A 464 ? 0.1293 0.2941 0.2685 -0.0014 0.0008  -0.0275 464 LYS   A N   
7099  C  CA  . LYS   A 464 ? 0.1443 0.3043 0.2776 -0.0099 -0.0013 -0.0202 464 LYS   A CA  
7100  C  C   . LYS   A 464 ? 0.1486 0.3056 0.2891 -0.0061 -0.0090 -0.0177 464 LYS   A C   
7101  O  O   . LYS   A 464 ? 0.1519 0.3231 0.3071 -0.0011 -0.0107 -0.0218 464 LYS   A O   
7102  C  CB  . LYS   A 464 ? 0.1528 0.3291 0.2863 -0.0191 0.0043  -0.0196 464 LYS   A CB  
7103  C  CG  . LYS   A 464 ? 0.1432 0.3130 0.2709 -0.0287 0.0025  -0.0126 464 LYS   A CG  
7104  C  CD  . LYS   A 464 ? 0.1516 0.3009 0.2633 -0.0325 0.0018  -0.0070 464 LYS   A CD  
7105  C  CE  . LYS   A 464 ? 0.2014 0.3421 0.3008 -0.0415 -0.0005 -0.0009 464 LYS   A CE  
7106  N  NZ  . LYS   A 464 ? 0.1835 0.3227 0.2921 -0.0397 -0.0072 0.0007  464 LYS   A NZ  
7120  N  N   . LEU   A 465 ? 0.1466 0.2865 0.2772 -0.0080 -0.0140 -0.0114 465 LEU   A N   
7121  C  CA  . LEU   A 465 ? 0.1232 0.2608 0.2605 -0.0056 -0.0215 -0.0080 465 LEU   A CA  
7122  C  C   . LEU   A 465 ? 0.1496 0.2871 0.2779 -0.0144 -0.0224 -0.0039 465 LEU   A C   
7123  O  O   . LEU   A 465 ? 0.1489 0.2826 0.2707 -0.0217 -0.0183 -0.0019 465 LEU   A O   
7124  C  CB  . LEU   A 465 ? 0.1187 0.2372 0.2478 -0.0010 -0.0262 -0.0048 465 LEU   A CB  
7125  C  CG  . LEU   A 465 ? 0.1307 0.2447 0.2664 0.0069  -0.0268 -0.0082 465 LEU   A CG  
7126  C  CD1 . LEU   A 465 ? 0.1843 0.2782 0.3045 0.0091  -0.0311 -0.0036 465 LEU   A CD1 
7127  C  CD2 . LEU   A 465 ? 0.1783 0.3029 0.3231 0.0147  -0.0295 -0.0131 465 LEU   A CD2 
7139  N  N   . ASP   A 466 ? 0.1100 0.2538 0.2504 -0.0138 -0.0281 -0.0027 466 ASP   A N   
7140  C  CA  . ASP   A 466 ? 0.1144 0.2561 0.2496 -0.0217 -0.0302 0.0008  466 ASP   A CA  
7141  C  C   . ASP   A 466 ? 0.1251 0.2472 0.2446 -0.0225 -0.0333 0.0057  466 ASP   A C   
7142  O  O   . ASP   A 466 ? 0.1292 0.2438 0.2462 -0.0170 -0.0382 0.0072  466 ASP   A O   
7143  C  CB  . ASP   A 466 ? 0.1441 0.2938 0.2872 -0.0197 -0.0346 -0.0015 466 ASP   A CB  
7144  C  CG  . ASP   A 466 ? 0.2038 0.3465 0.3346 -0.0259 -0.0375 0.0006  466 ASP   A CG  
7145  O  OD1 . ASP   A 466 ? 0.1846 0.3179 0.3093 -0.0318 -0.0354 0.0035  466 ASP   A OD1 
7146  O  OD2 . ASP   A 466 ? 0.1975 0.3472 0.3382 -0.0242 -0.0415 -0.0012 466 ASP   A OD2 
7151  N  N   . ARG   A 467 ? 0.1481 0.2606 0.2526 -0.0292 -0.0303 0.0078  467 ARG   A N   
7152  C  CA  . ARG   A 467 ? 0.1228 0.2180 0.2159 -0.0292 -0.0324 0.0111  467 ARG   A CA  
7153  C  C   . ARG   A 467 ? 0.1087 0.1999 0.2004 -0.0293 -0.0384 0.0129  467 ARG   A C   
7154  O  O   . ARG   A 467 ? 0.1299 0.2092 0.2101 -0.0273 -0.0407 0.0152  467 ARG   A O   
7155  C  CB  . ARG   A 467 ? 0.1176 0.2054 0.2029 -0.0358 -0.0285 0.0125  467 ARG   A CB  
7156  C  CG  . ARG   A 467 ? 0.1674 0.2593 0.2477 -0.0442 -0.0278 0.0127  467 ARG   A CG  
7157  C  CD  . ARG   A 467 ? 0.1672 0.2528 0.2417 -0.0505 -0.0238 0.0144  467 ARG   A CD  
7158  N  NE  . ARG   A 467 ? 0.1770 0.2619 0.2490 -0.0575 -0.0227 0.0151  467 ARG   A NE  
7159  C  CZ  . ARG   A 467 ? 0.2045 0.2762 0.2659 -0.0608 -0.0258 0.0166  467 ARG   A CZ  
7160  N  NH1 . ARG   A 467 ? 0.1737 0.2350 0.2318 -0.0571 -0.0300 0.0169  467 ARG   A NH1 
7161  N  NH2 . ARG   A 467 ? 0.2361 0.3065 0.2954 -0.0675 -0.0247 0.0176  467 ARG   A NH2 
7175  N  N   . PHE   A 468 ? 0.1165 0.2156 0.2116 -0.0313 -0.0398 0.0112  468 PHE   A N   
7176  C  CA  . PHE   A 468 ? 0.1318 0.2272 0.2245 -0.0312 -0.0449 0.0116  468 PHE   A CA  
7177  C  C   . PHE   A 468 ? 0.1392 0.2371 0.2334 -0.0240 -0.0493 0.0119  468 PHE   A C   
7178  O  O   . PHE   A 468 ? 0.1598 0.2529 0.2478 -0.0228 -0.0533 0.0133  468 PHE   A O   
7179  C  CB  . PHE   A 468 ? 0.1736 0.2745 0.2641 -0.0369 -0.0449 0.0095  468 PHE   A CB  
7180  C  CG  . PHE   A 468 ? 0.1478 0.2457 0.2406 -0.0445 -0.0411 0.0098  468 PHE   A CG  
7181  C  CD1 . PHE   A 468 ? 0.1501 0.2332 0.2293 -0.0471 -0.0417 0.0116  468 PHE   A CD1 
7182  C  CD2 . PHE   A 468 ? 0.1937 0.3007 0.2894 -0.0489 -0.0367 0.0085  468 PHE   A CD2 
7183  C  CE1 . PHE   A 468 ? 0.2034 0.2793 0.2725 -0.0532 -0.0390 0.0124  468 PHE   A CE1 
7184  C  CE2 . PHE   A 468 ? 0.2247 0.3256 0.3126 -0.0561 -0.0334 0.0099  468 PHE   A CE2 
7185  C  CZ  . PHE   A 468 ? 0.2019 0.2875 0.2811 -0.0582 -0.0349 0.0120  468 PHE   A CZ  
7195  N  N   . ALA   A 469 ? 0.1125 0.2188 0.2207 -0.0188 -0.0484 0.0108  469 ALA   A N   
7196  C  CA  . ALA   A 469 ? 0.1554 0.2627 0.2629 -0.0116 -0.0528 0.0111  469 ALA   A CA  
7197  C  C   . ALA   A 469 ? 0.1409 0.2344 0.2405 -0.0078 -0.0551 0.0153  469 ALA   A C   
7198  O  O   . ALA   A 469 ? 0.1003 0.1860 0.1963 -0.0094 -0.0523 0.0167  469 ALA   A O   
7199  C  CB  . ALA   A 469 ? 0.1689 0.2887 0.2912 -0.0070 -0.0513 0.0076  469 ALA   A CB  
7205  N  N   . LEU   A 470 ? 0.1523 0.2438 0.2511 -0.0032 -0.0600 0.0175  470 LEU   A N   
7206  C  CA  . LEU   A 470 ? 0.1626 0.2418 0.2543 -0.0003 -0.0621 0.0218  470 LEU   A CA  
7207  C  C   . LEU   A 470 ? 0.1616 0.2382 0.2568 0.0065  -0.0638 0.0224  470 LEU   A C   
7208  O  O   . LEU   A 470 ? 0.1251 0.1920 0.2200 0.0078  -0.0632 0.0248  470 LEU   A O   
7209  C  CB  . LEU   A 470 ? 0.1933 0.2682 0.2710 -0.0011 -0.0664 0.0248  470 LEU   A CB  
7210  C  CG  . LEU   A 470 ? 0.1429 0.2202 0.2243 -0.0069 -0.0659 0.0240  470 LEU   A CG  
7211  C  CD1 . LEU   A 470 ? 0.2380 0.3105 0.2989 -0.0065 -0.0704 0.0262  470 LEU   A CD1 
7212  C  CD2 . LEU   A 470 ? 0.1717 0.2391 0.2360 -0.0106 -0.0617 0.0244  470 LEU   A CD2 
7224  N  N   . ASP   A 471 ? 0.1532 0.2399 0.2624 0.0108  -0.0662 0.0199  471 ASP   A N   
7225  C  CA  . ASP   A 471 ? 0.1722 0.2555 0.2851 0.0178  -0.0686 0.0197  471 ASP   A CA  
7226  C  C   . ASP   A 471 ? 0.1398 0.2199 0.2596 0.0196  -0.0647 0.0176  471 ASP   A C   
7227  O  O   . ASP   A 471 ? 0.1345 0.2230 0.2587 0.0176  -0.0600 0.0132  471 ASP   A O   
7228  C  CB  . ASP   A 471 ? 0.1785 0.2768 0.3085 0.0221  -0.0712 0.0165  471 ASP   A CB  
7229  C  CG  . ASP   A 471 ? 0.2621 0.3618 0.3833 0.0219  -0.0765 0.0189  471 ASP   A CG  
7230  O  OD1 . ASP   A 471 ? 0.2624 0.3521 0.3747 0.0197  -0.0790 0.0237  471 ASP   A OD1 
7231  O  OD2 . ASP   A 471 ? 0.2849 0.3985 0.4173 0.0237  -0.0784 0.0160  471 ASP   A OD2 
7236  N  N   . GLY   A 472 ? 0.1455 0.2120 0.2608 0.0225  -0.0664 0.0204  472 GLY   A N   
7237  C  CA  . GLY   A 472 ? 0.1632 0.2241 0.2789 0.0250  -0.0635 0.0176  472 GLY   A CA  
7238  C  C   . GLY   A 472 ? 0.1400 0.1948 0.2496 0.0203  -0.0596 0.0188  472 GLY   A C   
7239  O  O   . GLY   A 472 ? 0.1132 0.1631 0.2268 0.0223  -0.0579 0.0167  472 GLY   A O   
7243  N  N   . LYS   A 473 ? 0.1250 0.1803 0.2273 0.0142  -0.0583 0.0216  473 LYS   A N   
7244  C  CA  . LYS   A 473 ? 0.1228 0.1726 0.2138 0.0095  -0.0546 0.0228  473 LYS   A CA  
7245  C  C   . LYS   A 473 ? 0.0968 0.1341 0.1867 0.0095  -0.0555 0.0269  473 LYS   A C   
7246  O  O   . LYS   A 473 ? 0.1171 0.1494 0.2017 0.0088  -0.0527 0.0259  473 LYS   A O   
7247  C  CB  . LYS   A 473 ? 0.0859 0.1408 0.1769 0.0033  -0.0533 0.0237  473 LYS   A CB  
7248  C  CG  . LYS   A 473 ? 0.1185 0.1853 0.2107 0.0011  -0.0513 0.0197  473 LYS   A CG  
7249  C  CD  . LYS   A 473 ? 0.1110 0.1846 0.2136 0.0007  -0.0466 0.0153  473 LYS   A CD  
7250  C  CE  . LYS   A 473 ? 0.1278 0.2152 0.2352 -0.0024 -0.0439 0.0117  473 LYS   A CE  
7251  N  NZ  . LYS   A 473 ? 0.1284 0.2156 0.2298 -0.0097 -0.0433 0.0134  473 LYS   A NZ  
7265  N  N   . ALA   A 474 ? 0.1218 0.1517 0.2017 0.0097  -0.0590 0.0316  474 ALA   A N   
7266  C  CA  . ALA   A 474 ? 0.1298 0.1483 0.2047 0.0086  -0.0598 0.0361  474 ALA   A CA  
7267  C  C   . ALA   A 474 ? 0.1174 0.1301 0.2010 0.0125  -0.0600 0.0338  474 ALA   A C   
7268  O  O   . ALA   A 474 ? 0.1383 0.1436 0.2148 0.0107  -0.0581 0.0343  474 ALA   A O   
7269  C  CB  . ALA   A 474 ? 0.1710 0.1848 0.2368 0.0079  -0.0635 0.0415  474 ALA   A CB  
7275  N  N   . ALA   A 475 ? 0.1450 0.1592 0.2341 0.0180  -0.0625 0.0307  475 ALA   A N   
7276  C  CA  . ALA   A 475 ? 0.1551 0.1638 0.2538 0.0226  -0.0633 0.0270  475 ALA   A CA  
7277  C  C   . ALA   A 475 ? 0.1338 0.1469 0.2361 0.0228  -0.0587 0.0213  475 ALA   A C   
7278  O  O   . ALA   A 475 ? 0.1487 0.1531 0.2495 0.0237  -0.0582 0.0196  475 ALA   A O   
7279  C  CB  . ALA   A 475 ? 0.2118 0.2225 0.3150 0.0288  -0.0669 0.0242  475 ALA   A CB  
7285  N  N   . TYR   A 476 ? 0.1201 0.1457 0.2249 0.0218  -0.0554 0.0178  476 TYR   A N   
7286  C  CA  . TYR   A 476 ? 0.1149 0.1473 0.2249 0.0212  -0.0504 0.0123  476 TYR   A CA  
7287  C  C   . TYR   A 476 ? 0.1382 0.1608 0.2319 0.0159  -0.0470 0.0148  476 TYR   A C   
7288  O  O   . TYR   A 476 ? 0.1352 0.1551 0.2294 0.0163  -0.0438 0.0107  476 TYR   A O   
7289  C  CB  . TYR   A 476 ? 0.1501 0.1965 0.2584 0.0192  -0.0464 0.0085  476 TYR   A CB  
7290  C  CG  . TYR   A 476 ? 0.1352 0.1933 0.2596 0.0215  -0.0413 0.0005  476 TYR   A CG  
7291  C  CD1 . TYR   A 476 ? 0.2077 0.2622 0.3187 0.0187  -0.0356 -0.0024 476 TYR   A CD1 
7292  C  CD2 . TYR   A 476 ? 0.1967 0.2657 0.3273 0.0268  -0.0423 -0.0048 476 TYR   A CD2 
7293  C  CE1 . TYR   A 476 ? 0.2861 0.3488 0.3951 0.0204  -0.0307 -0.0096 476 TYR   A CE1 
7294  C  CE2 . TYR   A 476 ? 0.2605 0.3391 0.3924 0.0289  -0.0369 -0.0126 476 TYR   A CE2 
7295  C  CZ  . TYR   A 476 ? 0.2358 0.3146 0.3707 0.0255  -0.0309 -0.0151 476 TYR   A CZ  
7296  O  OH  . TYR   A 476 ? 0.3034 0.3914 0.4323 0.0271  -0.0255 -0.0228 476 TYR   A OH  
7306  N  N   . ALA   A 477 ? 0.1287 0.1487 0.2149 0.0112  -0.0481 0.0207  477 ALA   A N   
7307  C  CA  . ALA   A 477 ? 0.1138 0.1275 0.1913 0.0067  -0.0451 0.0232  477 ALA   A CA  
7308  C  C   . ALA   A 477 ? 0.1221 0.1245 0.1980 0.0079  -0.0471 0.0247  477 ALA   A C   
7309  O  O   . ALA   A 477 ? 0.1250 0.1239 0.1978 0.0065  -0.0440 0.0224  477 ALA   A O   
7310  C  CB  . ALA   A 477 ? 0.1217 0.1356 0.1897 0.0025  -0.0462 0.0280  477 ALA   A CB  
7316  N  N   . LYS   A 478 ? 0.1233 0.1202 0.2032 0.0103  -0.0526 0.0286  478 LYS   A N   
7317  C  CA  . LYS   A 478 ? 0.1242 0.1102 0.2081 0.0105  -0.0544 0.0298  478 LYS   A CA  
7318  C  C   . LYS   A 478 ? 0.1577 0.1400 0.2404 0.0146  -0.0537 0.0229  478 LYS   A C   
7319  O  O   . LYS   A 478 ? 0.1385 0.1153 0.2240 0.0125  -0.0525 0.0222  478 LYS   A O   
7320  C  CB  . LYS   A 478 ? 0.1718 0.1505 0.2495 0.0116  -0.0589 0.0334  478 LYS   A CB  
7321  C  CG  . LYS   A 478 ? 0.1661 0.1339 0.2484 0.0110  -0.0614 0.0349  478 LYS   A CG  
7322  C  CD  . LYS   A 478 ? 0.1975 0.1586 0.2785 0.0121  -0.0664 0.0386  478 LYS   A CD  
7323  C  CE  . LYS   A 478 ? 0.2194 0.1688 0.2997 0.0103  -0.0691 0.0401  478 LYS   A CE  
7324  N  NZ  . LYS   A 478 ? 0.2117 0.1578 0.3002 0.0139  -0.0688 0.0332  478 LYS   A NZ  
7338  N  N   . LEU   A 479 ? 0.1225 0.1141 0.2225 0.0198  -0.0535 0.0166  479 LEU   A N   
7339  C  CA  . LEU   A 479 ? 0.1829 0.1728 0.2780 0.0241  -0.0512 0.0081  479 LEU   A CA  
7340  C  C   . LEU   A 479 ? 0.1503 0.1447 0.2456 0.0197  -0.0449 0.0050  479 LEU   A C   
7341  O  O   . LEU   A 479 ? 0.1644 0.1521 0.2563 0.0201  -0.0444 0.0013  479 LEU   A O   
7342  C  CB  . LEU   A 479 ? 0.1533 0.1571 0.2697 0.0298  -0.0511 0.0017  479 LEU   A CB  
7343  C  CG  . LEU   A 479 ? 0.2324 0.2416 0.3513 0.0334  -0.0469 -0.0083 479 LEU   A CG  
7344  C  CD1 . LEU   A 479 ? 0.2652 0.2616 0.3840 0.0382  -0.0508 -0.0122 479 LEU   A CD1 
7345  C  CD2 . LEU   A 479 ? 0.3356 0.3589 0.4551 0.0375  -0.0448 -0.0139 479 LEU   A CD2 
7357  N  N   . PHE   A 480 ? 0.1435 0.1459 0.2318 0.0158  -0.0408 0.0063  480 PHE   A N   
7358  C  CA  . PHE   A 480 ? 0.1623 0.1660 0.2393 0.0116  -0.0356 0.0044  480 PHE   A CA  
7359  C  C   . PHE   A 480 ? 0.1268 0.1217 0.2012 0.0084  -0.0364 0.0079  480 PHE   A C   
7360  O  O   . PHE   A 480 ? 0.1350 0.1275 0.2032 0.0071  -0.0344 0.0047  480 PHE   A O   
7361  C  CB  . PHE   A 480 ? 0.1822 0.1952 0.2561 0.0080  -0.0322 0.0055  480 PHE   A CB  
7362  C  CG  . PHE   A 480 ? 0.1940 0.2168 0.2723 0.0077  -0.0273 0.0000  480 PHE   A CG  
7363  C  CD1 . PHE   A 480 ? 0.2500 0.2825 0.3321 0.0106  -0.0262 -0.0040 480 PHE   A CD1 
7364  C  CD2 . PHE   A 480 ? 0.2430 0.2631 0.3067 0.0045  -0.0237 -0.0013 480 PHE   A CD2 
7365  C  CE1 . PHE   A 480 ? 0.3119 0.3531 0.3890 0.0094  -0.0211 -0.0088 480 PHE   A CE1 
7366  C  CE2 . PHE   A 480 ? 0.2553 0.2840 0.3202 0.0037  -0.0194 -0.0055 480 PHE   A CE2 
7367  C  CZ  . PHE   A 480 ? 0.2884 0.3279 0.3595 0.0057  -0.0177 -0.0091 480 PHE   A CZ  
7377  N  N   . HIS   A 481 ? 0.1250 0.1146 0.1964 0.0064  -0.0398 0.0146  481 HIS   A N   
7378  C  CA  . HIS   A 481 ? 0.1393 0.1216 0.2039 0.0024  -0.0402 0.0185  481 HIS   A CA  
7379  C  C   . HIS   A 481 ? 0.1174 0.0923 0.1910 0.0039  -0.0424 0.0159  481 HIS   A C   
7380  O  O   . HIS   A 481 ? 0.1412 0.1124 0.2069 0.0015  -0.0410 0.0144  481 HIS   A O   
7381  C  CB  . HIS   A 481 ? 0.1512 0.1323 0.2127 -0.0003 -0.0429 0.0261  481 HIS   A CB  
7382  C  CG  . HIS   A 481 ? 0.1415 0.1303 0.1986 -0.0022 -0.0410 0.0280  481 HIS   A CG  
7383  N  ND1 . HIS   A 481 ? 0.1562 0.1460 0.2084 -0.0037 -0.0434 0.0332  481 HIS   A ND1 
7384  C  CD2 . HIS   A 481 ? 0.1132 0.1083 0.1688 -0.0032 -0.0373 0.0248  481 HIS   A CD2 
7385  C  CE1 . HIS   A 481 ? 0.1186 0.1158 0.1713 -0.0050 -0.0413 0.0326  481 HIS   A CE1 
7386  N  NE2 . HIS   A 481 ? 0.1279 0.1267 0.1766 -0.0050 -0.0379 0.0277  481 HIS   A NE2 
7394  N  N   . ASP   A 482 ? 0.1490 0.1187 0.2263 0.0085  -0.0465 0.0146  482 ASP   A N   
7395  C  CA  . ASP   A 482 ? 0.1703 0.1299 0.2519 0.0102  -0.0496 0.0118  482 ASP   A CA  
7396  C  C   . ASP   A 482 ? 0.1627 0.1259 0.2470 0.0129  -0.0465 0.0024  482 ASP   A C   
7397  O  O   . ASP   A 482 ? 0.1714 0.1284 0.2537 0.0114  -0.0468 -0.0003 482 ASP   A O   
7398  C  CB  . ASP   A 482 ? 0.1701 0.1240 0.2598 0.0141  -0.0551 0.0133  482 ASP   A CB  
7399  C  CG  . ASP   A 482 ? 0.1754 0.1278 0.2607 0.0102  -0.0573 0.0222  482 ASP   A CG  
7400  O  OD1 . ASP   A 482 ? 0.1610 0.1149 0.2404 0.0045  -0.0553 0.0276  482 ASP   A OD1 
7401  O  OD2 . ASP   A 482 ? 0.1909 0.1411 0.2787 0.0129  -0.0606 0.0233  482 ASP   A OD2 
7406  N  N   . LEU   A 483 ? 0.1613 0.1345 0.2463 0.0163  -0.0433 -0.0029 483 LEU   A N   
7407  C  CA  . LEU   A 483 ? 0.1577 0.1354 0.2406 0.0184  -0.0396 -0.0114 483 LEU   A CA  
7408  C  C   . LEU   A 483 ? 0.1383 0.1170 0.2133 0.0134  -0.0363 -0.0112 483 LEU   A C   
7409  O  O   . LEU   A 483 ? 0.1355 0.1120 0.2085 0.0139  -0.0359 -0.0164 483 LEU   A O   
7410  C  CB  . LEU   A 483 ? 0.1471 0.1377 0.2339 0.0217  -0.0361 -0.0163 483 LEU   A CB  
7411  C  CG  . LEU   A 483 ? 0.1297 0.1290 0.2199 0.0234  -0.0317 -0.0249 483 LEU   A CG  
7412  C  CD1 . LEU   A 483 ? 0.1904 0.1819 0.2781 0.0285  -0.0344 -0.0325 483 LEU   A CD1 
7413  C  CD2 . LEU   A 483 ? 0.1424 0.1554 0.2296 0.0248  -0.0275 -0.0277 483 LEU   A CD2 
7425  N  N   . THR   A 484 ? 0.1265 0.1091 0.1977 0.0092  -0.0344 -0.0052 484 THR   A N   
7426  C  CA  . THR   A 484 ? 0.1707 0.1518 0.2236 0.0050  -0.0318 -0.0044 484 THR   A CA  
7427  C  C   . THR   A 484 ? 0.1224 0.0971 0.1842 0.0029  -0.0347 -0.0035 484 THR   A C   
7428  O  O   . THR   A 484 ? 0.1230 0.0968 0.1790 0.0017  -0.0339 -0.0067 484 THR   A O   
7429  C  CB  . THR   A 484 ? 0.1177 0.1057 0.1741 0.0015  -0.0298 0.0006  484 THR   A CB  
7430  O  OG1 . THR   A 484 ? 0.1088 0.1042 0.1639 0.0028  -0.0277 -0.0007 484 THR   A OG1 
7431  C  CG2 . THR   A 484 ? 0.1220 0.1093 0.1682 -0.0015 -0.0282 0.0013  484 THR   A CG2 
7439  N  N   . ALA   A 485 ? 0.1088 0.0771 0.1760 0.0022  -0.0383 0.0012  485 ALA   A N   
7440  C  CA  . ALA   A 485 ? 0.1499 0.1099 0.2161 -0.0010 -0.0412 0.0029  485 ALA   A CA  
7441  C  C   . ALA   A 485 ? 0.1543 0.1090 0.2242 0.0017  -0.0431 -0.0047 485 ALA   A C   
7442  O  O   . ALA   A 485 ? 0.1563 0.1080 0.2252 -0.0013 -0.0439 -0.0062 485 ALA   A O   
7443  C  CB  . ALA   A 485 ? 0.1808 0.1348 0.2485 -0.0032 -0.0445 0.0102  485 ALA   A CB  
7449  N  N   . VAL   A 486 ? 0.1537 0.1080 0.2293 0.0070  -0.0439 -0.0101 486 VAL   A N   
7450  C  CA  . VAL   A 486 ? 0.1697 0.1195 0.2451 0.0109  -0.0453 -0.0189 486 VAL   A CA  
7451  C  C   . VAL   A 486 ? 0.1529 0.1106 0.2244 0.0099  -0.0415 -0.0241 486 VAL   A C   
7452  O  O   . VAL   A 486 ? 0.1681 0.1210 0.2367 0.0084  -0.0432 -0.0276 486 VAL   A O   
7453  C  CB  . VAL   A 486 ? 0.1500 0.1013 0.2385 0.0177  -0.0467 -0.0245 486 VAL   A CB  
7454  C  CG1 . VAL   A 486 ? 0.1718 0.1212 0.2579 0.0222  -0.0472 -0.0353 486 VAL   A CG1 
7455  C  CG2 . VAL   A 486 ? 0.1733 0.1149 0.2650 0.0193  -0.0521 -0.0196 486 VAL   A CG2 
7465  N  N   . ILE   A 487 ? 0.1409 0.1085 0.2060 0.0106  -0.0370 -0.0246 487 ILE   A N   
7466  C  CA  . ILE   A 487 ? 0.1331 0.1072 0.1893 0.0097  -0.0333 -0.0288 487 ILE   A CA  
7467  C  C   . ILE   A 487 ? 0.1218 0.0941 0.1757 0.0053  -0.0342 -0.0257 487 ILE   A C   
7468  O  O   . ILE   A 487 ? 0.1445 0.1155 0.1907 0.0049  -0.0348 -0.0304 487 ILE   A O   
7469  C  CB  . ILE   A 487 ? 0.1322 0.1170 0.1852 0.0100  -0.0285 -0.0283 487 ILE   A CB  
7470  C  CG1 . ILE   A 487 ? 0.1434 0.1330 0.2024 0.0149  -0.0275 -0.0319 487 ILE   A CG1 
7471  C  CG2 . ILE   A 487 ? 0.1381 0.1280 0.1802 0.0084  -0.0255 -0.0309 487 ILE   A CG2 
7472  C  CD1 . ILE   A 487 ? 0.1555 0.1557 0.2125 0.0140  -0.0233 -0.0298 487 ILE   A CD1 
7484  N  N   . ASP   A 488 ? 0.1488 0.1190 0.1960 0.0018  -0.0345 -0.0181 488 ASP   A N   
7485  C  CA  . ASP   A 488 ? 0.1061 0.0775 0.1606 -0.0020 -0.0354 -0.0152 488 ASP   A CA  
7486  C  C   . ASP   A 488 ? 0.1681 0.1304 0.2151 -0.0031 -0.0393 -0.0185 488 ASP   A C   
7487  O  O   . ASP   A 488 ? 0.1478 0.1125 0.1979 -0.0044 -0.0401 -0.0210 488 ASP   A O   
7488  C  CB  . ASP   A 488 ? 0.1392 0.1099 0.1842 -0.0053 -0.0352 -0.0077 488 ASP   A CB  
7489  C  CG  . ASP   A 488 ? 0.1177 0.0955 0.1629 -0.0056 -0.0323 -0.0047 488 ASP   A CG  
7490  O  OD1 . ASP   A 488 ? 0.1602 0.1400 0.1939 -0.0048 -0.0305 -0.0077 488 ASP   A OD1 
7491  O  OD2 . ASP   A 488 ? 0.1317 0.1099 0.1727 -0.0071 -0.0320 0.0006  488 ASP   A OD2 
7496  N  N   . SER   A 489 ? 0.1455 0.1018 0.2057 -0.0026 -0.0422 -0.0178 489 SER   A N   
7497  C  CA  . SER   A 489 ? 0.1356 0.0842 0.2030 -0.0048 -0.0466 -0.0199 489 SER   A CA  
7498  C  C   . SER   A 489 ? 0.1775 0.1226 0.2383 -0.0018 -0.0480 -0.0297 489 SER   A C   
7499  O  O   . SER   A 489 ? 0.1647 0.1077 0.2320 -0.0041 -0.0508 -0.0316 489 SER   A O   
7500  C  CB  . SER   A 489 ? 0.1260 0.0665 0.2003 -0.0057 -0.0498 -0.0151 489 SER   A CB  
7501  O  OG  . SER   A 489 ? 0.1594 0.1015 0.2296 -0.0089 -0.0484 -0.0062 489 SER   A OG  
7507  N  N   . LEU   A 490 ? 0.1488 0.0998 0.2127 0.0031  -0.0457 -0.0354 490 LEU   A N   
7508  C  CA  . LEU   A 490 ? 0.1612 0.1112 0.2207 0.0067  -0.0465 -0.0457 490 LEU   A CA  
7509  C  C   . LEU   A 490 ? 0.1642 0.1201 0.2151 0.0048  -0.0454 -0.0483 490 LEU   A C   
7510  O  O   . LEU   A 490 ? 0.1655 0.1197 0.2146 0.0059  -0.0476 -0.0560 490 LEU   A O   
7511  C  CB  . LEU   A 490 ? 0.1625 0.1178 0.2239 0.0124  -0.0436 -0.0507 490 LEU   A CB  
7512  C  CG  . LEU   A 490 ? 0.1790 0.1286 0.2499 0.0168  -0.0461 -0.0522 490 LEU   A CG  
7513  C  CD1 . LEU   A 490 ? 0.1818 0.1405 0.2521 0.0221  -0.0420 -0.0561 490 LEU   A CD1 
7514  C  CD2 . LEU   A 490 ? 0.2086 0.1485 0.2826 0.0184  -0.0509 -0.0577 490 LEU   A CD2 
7526  N  N   . GLY   A 491 ? 0.1665 0.1287 0.2109 0.0022  -0.0426 -0.0422 491 GLY   A N   
7527  C  CA  . GLY   A 491 ? 0.1692 0.1364 0.2036 0.0011  -0.0419 -0.0438 491 GLY   A CA  
7528  C  C   . GLY   A 491 ? 0.1604 0.1351 0.1876 0.0036  -0.0379 -0.0461 491 GLY   A C   
7529  O  O   . GLY   A 491 ? 0.1721 0.1494 0.1887 0.0034  -0.0379 -0.0492 491 GLY   A O   
7533  N  N   . LEU   A 492 ? 0.1690 0.1462 0.1947 0.0053  -0.0341 -0.0444 492 LEU   A N   
7534  C  CA  . LEU   A 492 ? 0.1435 0.1297 0.1656 0.0067  -0.0296 -0.0457 492 LEU   A CA  
7535  C  C   . LEU   A 492 ? 0.1618 0.1508 0.1767 0.0039  -0.0267 -0.0375 492 LEU   A C   
7536  O  O   . LEU   A 492 ? 0.1555 0.1412 0.1765 0.0020  -0.0283 -0.0316 492 LEU   A O   
7537  C  CB  . LEU   A 492 ? 0.1332 0.1226 0.1621 0.0110  -0.0277 -0.0520 492 LEU   A CB  
7538  C  CG  . LEU   A 492 ? 0.1809 0.1663 0.2082 0.0147  -0.0301 -0.0621 492 LEU   A CG  
7539  C  CD1 . LEU   A 492 ? 0.1706 0.1622 0.2052 0.0197  -0.0274 -0.0688 492 LEU   A CD1 
7540  C  CD2 . LEU   A 492 ? 0.2060 0.1934 0.2237 0.0134  -0.0307 -0.0664 492 LEU   A CD2 
7552  N  N   . CYS   A 493 ? 0.1551 0.1516 0.1641 0.0033  -0.0227 -0.0371 493 CYS   A N   
7553  C  CA  . CYS   A 493 ? 0.1541 0.1527 0.1588 0.0001  -0.0206 -0.0299 493 CYS   A CA  
7554  C  C   . CYS   A 493 ? 0.1276 0.1311 0.1422 0.0010  -0.0178 -0.0282 493 CYS   A C   
7555  O  O   . CYS   A 493 ? 0.1488 0.1573 0.1631 0.0037  -0.0153 -0.0334 493 CYS   A O   
7556  C  CB  . CYS   A 493 ? 0.1904 0.1924 0.1791 -0.0021 -0.0185 -0.0290 493 CYS   A CB  
7557  S  SG  . CYS   A 493 ? 0.1624 0.1655 0.1500 -0.0066 -0.0166 -0.0199 493 CYS   A SG  
7562  N  N   . ILE   A 494 ? 0.1395 0.1404 0.1527 -0.0008 -0.0182 -0.0216 494 ILE   A N   
7563  C  CA  . ILE   A 494 ? 0.1257 0.1314 0.1477 -0.0004 -0.0165 -0.0193 494 ILE   A CA  
7564  C  C   . ILE   A 494 ? 0.1428 0.1580 0.1608 -0.0016 -0.0120 -0.0208 494 ILE   A C   
7565  O  O   . ILE   A 494 ? 0.1672 0.1885 0.1908 0.0000  -0.0102 -0.0221 494 ILE   A O   
7566  C  CB  . ILE   A 494 ? 0.1268 0.1286 0.1479 -0.0028 -0.0181 -0.0123 494 ILE   A CB  
7567  C  CG1 . ILE   A 494 ? 0.1090 0.1147 0.1431 -0.0017 -0.0179 -0.0105 494 ILE   A CG1 
7568  C  CG2 . ILE   A 494 ? 0.1339 0.1356 0.1461 -0.0065 -0.0171 -0.0087 494 ILE   A CG2 
7569  C  CD1 . ILE   A 494 ? 0.1728 0.1746 0.2092 0.0021  -0.0202 -0.0129 494 ILE   A CD1 
7581  N  N   . PHE   A 495 ? 0.1461 0.1629 0.1528 -0.0046 -0.0102 -0.0204 495 PHE   A N   
7582  C  CA  . PHE   A 495 ? 0.1489 0.1759 0.1530 -0.0074 -0.0054 -0.0205 495 PHE   A CA  
7583  C  C   . PHE   A 495 ? 0.1843 0.2193 0.1849 -0.0040 -0.0020 -0.0285 495 PHE   A C   
7584  O  O   . PHE   A 495 ? 0.1511 0.1985 0.1560 -0.0065 0.0029  -0.0295 495 PHE   A O   
7585  C  CB  . PHE   A 495 ? 0.1755 0.1984 0.1604 -0.0123 -0.0053 -0.0159 495 PHE   A CB  
7586  C  CG  . PHE   A 495 ? 0.1373 0.1541 0.1280 -0.0153 -0.0081 -0.0088 495 PHE   A CG  
7587  C  CD1 . PHE   A 495 ? 0.1755 0.1910 0.1663 -0.0156 -0.0086 -0.0055 495 PHE   A CD1 
7588  C  CD2 . PHE   A 495 ? 0.1836 0.1912 0.1572 -0.0169 -0.0113 -0.0054 495 PHE   A CD2 
7589  C  CE1 . PHE   A 495 ? 0.1859 0.1944 0.1751 -0.0179 -0.0112 -0.0002 495 PHE   A CE1 
7590  C  CE2 . PHE   A 495 ? 0.2016 0.2017 0.1733 -0.0188 -0.0142 0.0000  495 PHE   A CE2 
7591  C  CZ  . PHE   A 495 ? 0.1864 0.1876 0.1676 -0.0192 -0.0141 0.0024  495 PHE   A CZ  
7601  N  N   . THR   A 496 ? 0.1572 0.1902 0.1701 0.0008  -0.0044 -0.0348 496 THR   A N   
7602  C  CA  . THR   A 496 ? 0.1649 0.2051 0.1782 0.0056  -0.0019 -0.0440 496 THR   A CA  
7603  C  C   . THR   A 496 ? 0.1364 0.1861 0.1701 0.0080  -0.0003 -0.0446 496 THR   A C   
7604  O  O   . THR   A 496 ? 0.1703 0.2294 0.2030 0.0117  0.0028  -0.0521 496 THR   A O   
7605  C  CB  . THR   A 496 ? 0.1234 0.1581 0.1498 0.0103  -0.0060 -0.0505 496 THR   A CB  
7606  O  OG1 . THR   A 496 ? 0.1648 0.1865 0.1900 0.0112  -0.0111 -0.0463 496 THR   A OG1 
7607  C  CG2 . THR   A 496 ? 0.1821 0.2118 0.1878 0.0088  -0.0070 -0.0528 496 THR   A CG2 
7615  N  N   . THR   A 497 ? 0.1695 0.2132 0.2016 0.0064  -0.0026 -0.0376 497 THR   A N   
7616  C  CA  . THR   A 497 ? 0.1542 0.2064 0.2030 0.0085  -0.0020 -0.0370 497 THR   A CA  
7617  C  C   . THR   A 497 ? 0.1842 0.2501 0.2232 0.0052  0.0039  -0.0377 497 THR   A C   
7618  O  O   . THR   A 497 ? 0.1341 0.2111 0.1913 0.0068  0.0050  -0.0391 497 THR   A O   
7619  C  CB  . THR   A 497 ? 0.1755 0.2186 0.2245 0.0069  -0.0062 -0.0293 497 THR   A CB  
7620  O  OG1 . THR   A 497 ? 0.1913 0.2307 0.2299 0.0009  -0.0056 -0.0229 497 THR   A OG1 
7621  C  CG2 . THR   A 497 ? 0.1838 0.2146 0.2369 0.0102  -0.0116 -0.0289 497 THR   A CG2 
7629  N  N   . PHE   A 498 ? 0.1470 0.2176 0.1817 -0.0001 0.0075  -0.0363 498 PHE   A N   
7630  C  CA  . PHE   A 498 ? 0.1563 0.2417 0.1865 -0.0048 0.0136  -0.0365 498 PHE   A CA  
7631  C  C   . PHE   A 498 ? 0.1877 0.2851 0.2167 -0.0005 0.0181  -0.0467 498 PHE   A C   
7632  O  O   . PHE   A 498 ? 0.1870 0.2906 0.2074 -0.0039 0.0220  -0.0481 498 PHE   A O   
7633  C  CB  . PHE   A 498 ? 0.1668 0.2474 0.1806 -0.0129 0.0148  -0.0290 498 PHE   A CB  
7634  C  CG  . PHE   A 498 ? 0.1615 0.2333 0.1790 -0.0168 0.0111  -0.0201 498 PHE   A CG  
7635  C  CD1 . PHE   A 498 ? 0.2029 0.2787 0.2216 -0.0183 0.0114  -0.0174 498 PHE   A CD1 
7636  C  CD2 . PHE   A 498 ? 0.2070 0.2631 0.2100 -0.0187 0.0071  -0.0150 498 PHE   A CD2 
7637  C  CE1 . PHE   A 498 ? 0.1754 0.2438 0.1998 -0.0216 0.0079  -0.0106 498 PHE   A CE1 
7638  C  CE2 . PHE   A 498 ? 0.2314 0.2790 0.2332 -0.0215 0.0038  -0.0084 498 PHE   A CE2 
7639  C  CZ  . PHE   A 498 ? 0.2161 0.2692 0.2267 -0.0229 0.0042  -0.0063 498 PHE   A CZ  
7649  N  N   . GLY   A 499 ? 0.1713 0.2736 0.2185 0.0072  0.0167  -0.0539 499 GLY   A N   
7650  C  CA  . GLY   A 499 ? 0.2006 0.3140 0.2480 0.0128  0.0202  -0.0654 499 GLY   A CA  
7651  C  C   . GLY   A 499 ? 0.1756 0.2816 0.2378 0.0222  0.0149  -0.0727 499 GLY   A C   
7652  O  O   . GLY   A 499 ? 0.1886 0.3049 0.2579 0.0288  0.0164  -0.0824 499 GLY   A O   
7656  N  N   . LEU   A 500 ? 0.1841 0.2706 0.2424 0.0226  0.0084  -0.0684 500 LEU   A N   
7657  C  CA  . LEU   A 500 ? 0.1828 0.2581 0.2496 0.0302  0.0023  -0.0738 500 LEU   A CA  
7658  C  C   . LEU   A 500 ? 0.1862 0.2521 0.2640 0.0326  -0.0035 -0.0687 500 LEU   A C   
7659  O  O   . LEU   A 500 ? 0.1787 0.2420 0.2547 0.0273  -0.0041 -0.0590 500 LEU   A O   
7660  C  CB  . LEU   A 500 ? 0.1858 0.2479 0.2422 0.0286  -0.0006 -0.0743 500 LEU   A CB  
7661  C  CG  . LEU   A 500 ? 0.1959 0.2646 0.2387 0.0267  0.0037  -0.0797 500 LEU   A CG  
7662  C  CD1 . LEU   A 500 ? 0.2126 0.2677 0.2481 0.0266  -0.0009 -0.0810 500 LEU   A CD1 
7663  C  CD2 . LEU   A 500 ? 0.1688 0.2535 0.2183 0.0323  0.0081  -0.0914 500 LEU   A CD2 
7675  N  N   . GLY   A 501 ? 0.1917 0.2523 0.2812 0.0403  -0.0082 -0.0745 501 GLY   A N   
7676  C  CA  . GLY   A 501 ? 0.1922 0.2421 0.2917 0.0430  -0.0147 -0.0698 501 GLY   A CA  
7677  C  C   . GLY   A 501 ? 0.1919 0.2240 0.2928 0.0468  -0.0216 -0.0718 501 GLY   A C   
7678  O  O   . GLY   A 501 ? 0.1532 0.1822 0.2518 0.0469  -0.0210 -0.0774 501 GLY   A O   
7682  N  N   . ILE   A 502 ? 0.1893 0.2112 0.3019 0.0499  -0.0282 -0.0679 502 ILE   A N   
7683  C  CA  . ILE   A 502 ? 0.2053 0.2077 0.3193 0.0517  -0.0354 -0.0680 502 ILE   A CA  
7684  C  C   . ILE   A 502 ? 0.1961 0.1967 0.3121 0.0578  -0.0365 -0.0804 502 ILE   A C   
7685  O  O   . ILE   A 502 ? 0.1932 0.1824 0.3058 0.0552  -0.0392 -0.0809 502 ILE   A O   
7686  C  CB  . ILE   A 502 ? 0.2139 0.2073 0.3411 0.0542  -0.0425 -0.0614 502 ILE   A CB  
7687  C  CG1 . ILE   A 502 ? 0.2569 0.2298 0.3749 0.0513  -0.0488 -0.0570 502 ILE   A CG1 
7688  C  CG2 . ILE   A 502 ? 0.2512 0.2522 0.3817 0.0602  -0.0429 -0.0660 502 ILE   A CG2 
7689  C  CD1 . ILE   A 502 ? 0.2349 0.2003 0.3498 0.0445  -0.0489 -0.0505 502 ILE   A CD1 
7701  N  N   . GLN   A 503 ? 0.1637 0.1775 0.2903 0.0632  -0.0343 -0.0885 503 GLN   A N   
7702  C  CA  . GLN   A 503 ? 0.2084 0.2204 0.3308 0.0674  -0.0353 -0.0989 503 GLN   A CA  
7703  C  C   . GLN   A 503 ? 0.2172 0.2323 0.3289 0.0647  -0.0311 -0.1045 503 GLN   A C   
7704  O  O   . GLN   A 503 ? 0.2130 0.2195 0.3233 0.0652  -0.0344 -0.1088 503 GLN   A O   
7705  C  CB  . GLN   A 503 ? 0.2249 0.2517 0.3580 0.0736  -0.0334 -0.1066 503 GLN   A CB  
7706  C  CG  . GLN   A 503 ? 0.2804 0.3044 0.4130 0.0787  -0.0358 -0.1165 503 GLN   A CG  
7707  C  CD  . GLN   A 503 ? 0.3183 0.3199 0.4473 0.0792  -0.0448 -0.1139 503 GLN   A CD  
7708  O  OE1 . GLN   A 503 ? 0.2595 0.2540 0.4040 0.0794  -0.0501 -0.1065 503 GLN   A OE1 
7709  N  NE2 . GLN   A 503 ? 0.2629 0.2595 0.3979 0.0789  -0.0468 -0.1192 503 GLN   A NE2 
7718  N  N   . ASP   A 504 ? 0.2110 0.2388 0.3160 0.0617  -0.0239 -0.1043 504 ASP   A N   
7719  C  CA  . ASP   A 504 ? 0.1939 0.2260 0.2867 0.0575  -0.0197 -0.1076 504 ASP   A CA  
7720  C  C   . ASP   A 504 ? 0.2033 0.2167 0.2872 0.0527  -0.0250 -0.1023 504 ASP   A C   
7721  O  O   . ASP   A 504 ? 0.1885 0.1995 0.2683 0.0525  -0.0256 -0.1088 504 ASP   A O   
7722  C  CB  . ASP   A 504 ? 0.1857 0.2339 0.2698 0.0511  -0.0116 -0.1027 504 ASP   A CB  
7723  C  CG  . ASP   A 504 ? 0.2018 0.2703 0.2927 0.0545  -0.0058 -0.1076 504 ASP   A CG  
7724  O  OD1 . ASP   A 504 ? 0.2349 0.3128 0.3248 0.0604  -0.0031 -0.1198 504 ASP   A OD1 
7725  O  OD2 . ASP   A 504 ? 0.2229 0.2969 0.3144 0.0516  -0.0042 -0.1000 504 ASP   A OD2 
7730  N  N   . TYR   A 505 ? 0.1877 0.1905 0.2749 0.0489  -0.0288 -0.0911 505 TYR   A N   
7731  C  CA  . TYR   A 505 ? 0.1595 0.1476 0.2470 0.0438  -0.0337 -0.0849 505 TYR   A CA  
7732  C  C   . TYR   A 505 ? 0.2045 0.1778 0.2911 0.0473  -0.0405 -0.0898 505 TYR   A C   
7733  O  O   . TYR   A 505 ? 0.1724 0.1401 0.2598 0.0440  -0.0429 -0.0908 505 TYR   A O   
7734  C  CB  . TYR   A 505 ? 0.1537 0.1372 0.2376 0.0382  -0.0346 -0.0716 505 TYR   A CB  
7735  C  CG  . TYR   A 505 ? 0.1631 0.1589 0.2392 0.0335  -0.0284 -0.0653 505 TYR   A CG  
7736  C  CD1 . TYR   A 505 ? 0.1798 0.1798 0.2419 0.0290  -0.0248 -0.0652 505 TYR   A CD1 
7737  C  CD2 . TYR   A 505 ? 0.1725 0.1745 0.2501 0.0335  -0.0265 -0.0598 505 TYR   A CD2 
7738  C  CE1 . TYR   A 505 ? 0.1748 0.1844 0.2314 0.0247  -0.0199 -0.0597 505 TYR   A CE1 
7739  C  CE2 . TYR   A 505 ? 0.1526 0.1655 0.2274 0.0288  -0.0214 -0.0547 505 TYR   A CE2 
7740  C  CZ  . TYR   A 505 ? 0.1881 0.2029 0.2455 0.0243  -0.0182 -0.0544 505 TYR   A CZ  
7741  O  OH  . TYR   A 505 ? 0.1845 0.2077 0.2375 0.0194  -0.0138 -0.0490 505 TYR   A OH  
7751  N  N   . VAL   A 506 ? 0.1976 0.1705 0.2987 0.0518  -0.0435 -0.0901 506 VAL   A N   
7752  C  CA  . VAL   A 506 ? 0.2038 0.1666 0.3117 0.0539  -0.0496 -0.0931 506 VAL   A CA  
7753  C  C   . VAL   A 506 ? 0.2519 0.2184 0.3487 0.0565  -0.0479 -0.1044 506 VAL   A C   
7754  O  O   . VAL   A 506 ? 0.2367 0.1949 0.3373 0.0548  -0.0519 -0.1058 506 VAL   A O   
7755  C  CB  . VAL   A 506 ? 0.2086 0.1694 0.3252 0.0590  -0.0531 -0.0922 506 VAL   A CB  
7756  C  CG1 . VAL   A 506 ? 0.2431 0.1951 0.3623 0.0626  -0.0587 -0.0980 506 VAL   A CG1 
7757  C  CG2 . VAL   A 506 ? 0.1952 0.1489 0.3146 0.0557  -0.0560 -0.0803 506 VAL   A CG2 
7767  N  N   . ASP   A 507 ? 0.2215 0.2054 0.3215 0.0603  -0.0418 -0.1123 507 ASP   A N   
7768  C  CA  . ASP   A 507 ? 0.2067 0.1994 0.3064 0.0629  -0.0393 -0.1233 507 ASP   A CA  
7769  C  C   . ASP   A 507 ? 0.2579 0.2437 0.3390 0.0573  -0.0396 -0.1227 507 ASP   A C   
7770  O  O   . ASP   A 507 ? 0.2667 0.2475 0.3480 0.0580  -0.0429 -0.1279 507 ASP   A O   
7771  C  CB  . ASP   A 507 ? 0.2645 0.2759 0.3554 0.0659  -0.0315 -0.1300 507 ASP   A CB  
7772  C  CG  . ASP   A 507 ? 0.2931 0.3121 0.3928 0.0719  -0.0310 -0.1326 507 ASP   A CG  
7773  O  OD1 . ASP   A 507 ? 0.2374 0.2468 0.3521 0.0751  -0.0377 -0.1324 507 ASP   A OD1 
7774  O  OD2 . ASP   A 507 ? 0.3072 0.3442 0.4093 0.0726  -0.0242 -0.1345 507 ASP   A OD2 
7779  N  N   . MET   A 508 ? 0.2618 0.2497 0.3362 0.0520  -0.0366 -0.1164 508 MET   A N   
7780  C  CA  . MET   A 508 ? 0.2512 0.2360 0.3153 0.0466  -0.0369 -0.1151 508 MET   A CA  
7781  C  C   . MET   A 508 ? 0.2520 0.2207 0.3204 0.0431  -0.0440 -0.1099 508 MET   A C   
7782  O  O   . MET   A 508 ? 0.2742 0.2393 0.3368 0.0416  -0.0462 -0.1132 508 MET   A O   
7783  C  CB  . MET   A 508 ? 0.2372 0.2281 0.2929 0.0419  -0.0324 -0.1100 508 MET   A CB  
7784  C  CG  . MET   A 508 ? 0.2424 0.2508 0.2900 0.0432  -0.0248 -0.1143 508 MET   A CG  
7785  S  SD  . MET   A 508 ? 0.2532 0.2679 0.2867 0.0345  -0.0198 -0.1017 508 MET   A SD  
7786  C  CE  . MET   A 508 ? 0.2303 0.2454 0.2755 0.0336  -0.0192 -0.0913 508 MET   A CE  
7796  N  N   . TYR   A 509 ? 0.2404 0.2004 0.3184 0.0416  -0.0473 -0.1013 509 TYR   A N   
7797  C  CA  . TYR   A 509 ? 0.2738 0.2188 0.3505 0.0372  -0.0533 -0.0947 509 TYR   A CA  
7798  C  C   . TYR   A 509 ? 0.2858 0.2247 0.3686 0.0402  -0.0579 -0.1014 509 TYR   A C   
7799  O  O   . TYR   A 509 ? 0.2858 0.2193 0.3678 0.0367  -0.0607 -0.1017 509 TYR   A O   
7800  C  CB  . TYR   A 509 ? 0.2280 0.1670 0.3167 0.0352  -0.0557 -0.0844 509 TYR   A CB  
7801  C  CG  . TYR   A 509 ? 0.2270 0.1547 0.3220 0.0298  -0.0608 -0.0769 509 TYR   A CG  
7802  C  CD1 . TYR   A 509 ? 0.3043 0.2206 0.3967 0.0314  -0.0662 -0.0776 509 TYR   A CD1 
7803  C  CD2 . TYR   A 509 ? 0.2615 0.1863 0.3459 0.0228  -0.0604 -0.0688 509 TYR   A CD2 
7804  C  CE1 . TYR   A 509 ? 0.3000 0.2065 0.3968 0.0259  -0.0703 -0.0710 509 TYR   A CE1 
7805  C  CE2 . TYR   A 509 ? 0.2668 0.1833 0.3549 0.0175  -0.0642 -0.0624 509 TYR   A CE2 
7806  C  CZ  . TYR   A 509 ? 0.2639 0.1713 0.3598 0.0187  -0.0692 -0.0631 509 TYR   A CZ  
7807  O  OH  . TYR   A 509 ? 0.2513 0.1506 0.3488 0.0129  -0.0726 -0.0565 509 TYR   A OH  
7817  N  N   . ASN   A 510 ? 0.2688 0.2097 0.3619 0.0467  -0.0588 -0.1068 510 ASN   A N   
7818  C  CA  . ASN   A 510 ? 0.2908 0.2234 0.3845 0.0503  -0.0639 -0.1136 510 ASN   A CA  
7819  C  C   . ASN   A 510 ? 0.3029 0.2416 0.3917 0.0515  -0.0624 -0.1236 510 ASN   A C   
7820  O  O   . ASN   A 510 ? 0.3002 0.2302 0.3908 0.0501  -0.0670 -0.1260 510 ASN   A O   
7821  C  CB  . ASN   A 510 ? 0.2398 0.1748 0.3504 0.0573  -0.0656 -0.1167 510 ASN   A CB  
7822  C  CG  . ASN   A 510 ? 0.2843 0.2088 0.3968 0.0558  -0.0695 -0.1067 510 ASN   A CG  
7823  O  OD1 . ASN   A 510 ? 0.2747 0.1900 0.3874 0.0493  -0.0720 -0.0975 510 ASN   A OD1 
7824  N  ND2 . ASN   A 510 ? 0.3244 0.2515 0.4423 0.0613  -0.0701 -0.1081 510 ASN   A ND2 
7831  N  N   . ALA   A 511 ? 0.2997 0.2532 0.3833 0.0536  -0.0560 -0.1294 511 ALA   A N   
7832  C  CA  . ALA   A 511 ? 0.3233 0.2832 0.3936 0.0543  -0.0538 -0.1382 511 ALA   A CA  
7833  C  C   . ALA   A 511 ? 0.2957 0.2498 0.3651 0.0478  -0.0564 -0.1346 511 ALA   A C   
7834  O  O   . ALA   A 511 ? 0.3437 0.2952 0.4049 0.0483  -0.0587 -0.1412 511 ALA   A O   
7835  C  CB  . ALA   A 511 ? 0.3164 0.2939 0.3822 0.0559  -0.0461 -0.1421 511 ALA   A CB  
7841  N  N   . VAL   A 512 ? 0.2757 0.2260 0.3428 0.0418  -0.0565 -0.1244 512 VAL   A N   
7842  C  CA  . VAL   A 512 ? 0.3014 0.2467 0.3593 0.0356  -0.0584 -0.1200 512 VAL   A CA  
7843  C  C   . VAL   A 512 ? 0.2967 0.2285 0.3644 0.0325  -0.0649 -0.1162 512 VAL   A C   
7844  O  O   . VAL   A 512 ? 0.3105 0.2382 0.3761 0.0303  -0.0681 -0.1192 512 VAL   A O   
7845  C  CB  . VAL   A 512 ? 0.2924 0.2423 0.3434 0.0307  -0.0551 -0.1120 512 VAL   A CB  
7846  C  CG1 . VAL   A 512 ? 0.2516 0.1974 0.3045 0.0244  -0.0581 -0.1065 512 VAL   A CG1 
7847  C  CG2 . VAL   A 512 ? 0.2856 0.2491 0.3287 0.0325  -0.0492 -0.1160 512 VAL   A CG2 
7857  N  N   . VAL   A 513 ? 0.2779 0.2031 0.3568 0.0319  -0.0670 -0.1089 513 VAL   A N   
7858  C  CA  . VAL   A 513 ? 0.3122 0.2245 0.3955 0.0274  -0.0723 -0.1023 513 VAL   A CA  
7859  C  C   . VAL   A 513 ? 0.3556 0.2578 0.4423 0.0310  -0.0777 -0.1080 513 VAL   A C   
7860  O  O   . VAL   A 513 ? 0.3372 0.2317 0.4312 0.0276  -0.0822 -0.1080 513 VAL   A O   
7861  C  CB  . VAL   A 513 ? 0.3024 0.2123 0.3905 0.0238  -0.0717 -0.0905 513 VAL   A CB  
7862  C  CG1 . VAL   A 513 ? 0.3585 0.2554 0.4494 0.0195  -0.0770 -0.0839 513 VAL   A CG1 
7863  C  CG2 . VAL   A 513 ? 0.2634 0.1807 0.3456 0.0192  -0.0677 -0.0848 513 VAL   A CG2 
7873  N  N   . GLY   A 514 ? 0.3349 0.2404 0.4334 0.0380  -0.0773 -0.1130 514 GLY   A N   
7874  C  CA  . GLY   A 514 ? 0.3822 0.2772 0.4822 0.0423  -0.0829 -0.1181 514 GLY   A CA  
7875  C  C   . GLY   A 514 ? 0.3701 0.2680 0.4784 0.0493  -0.0826 -0.1204 514 GLY   A C   
7876  O  O   . GLY   A 514 ? 0.3413 0.2414 0.4531 0.0482  -0.0808 -0.1124 514 GLY   A O   
7880  N  N   . GLU   A 515 ? 0.3736 0.2733 0.4894 0.0564  -0.0844 -0.1312 515 GLU   A N   
7881  C  CA  . GLU   A 515 ? 0.4396 0.3411 0.5518 0.0640  -0.0843 -0.1351 515 GLU   A CA  
7882  C  C   . GLU   A 515 ? 0.3551 0.2486 0.4884 0.0628  -0.0890 -0.1251 515 GLU   A C   
7883  O  O   . GLU   A 515 ? 0.3801 0.2574 0.5088 0.0591  -0.0952 -0.1206 515 GLU   A O   
7884  C  CB  . GLU   A 515 ? 0.4385 0.3435 0.5665 0.0715  -0.0868 -0.1486 515 GLU   A CB  
7885  C  CG  . GLU   A 515 ? 0.5363 0.4469 0.6681 0.0798  -0.0867 -0.1544 515 GLU   A CG  
7886  C  CD  . GLU   A 515 ? 0.6667 0.5858 0.7913 0.0874  -0.0850 -0.1692 515 GLU   A CD  
7887  O  OE1 . GLU   A 515 ? 0.5577 0.4720 0.6935 0.0883  -0.0891 -0.1761 515 GLU   A OE1 
7888  O  OE2 . GLU   A 515 ? 0.7780 0.7129 0.9036 0.0920  -0.0793 -0.1741 515 GLU   A OE2 
7895  N  N   . SER   A 516 ? 0.3765 0.2746 0.5037 0.0652  -0.0863 -0.1212 516 SER   A N   
7896  C  CA  . SER   A 516 ? 0.3469 0.2372 0.4871 0.0649  -0.0909 -0.1122 516 SER   A CA  
7897  C  C   . SER   A 516 ? 0.3358 0.2156 0.4727 0.0560  -0.0930 -0.0985 516 SER   A C   
7898  O  O   . SER   A 516 ? 0.3705 0.2383 0.5074 0.0551  -0.0985 -0.0917 516 SER   A O   
7899  C  CB  . SER   A 516 ? 0.4100 0.2903 0.5535 0.0711  -0.0978 -0.1186 516 SER   A CB  
7900  O  OG  . SER   A 516 ? 0.4520 0.3428 0.5970 0.0795  -0.0956 -0.1314 516 SER   A OG  
7906  N  N   . THR   A 517 ? 0.3542 0.2369 0.4797 0.0492  -0.0888 -0.0938 517 THR   A N   
7907  C  CA  . THR   A 517 ? 0.3471 0.2232 0.4725 0.0407  -0.0900 -0.0810 517 THR   A CA  
7908  C  C   . THR   A 517 ? 0.3718 0.2501 0.4944 0.0404  -0.0883 -0.0721 517 THR   A C   
7909  O  O   . THR   A 517 ? 0.3762 0.2461 0.5030 0.0363  -0.0920 -0.0623 517 THR   A O   
7910  C  CB  . THR   A 517 ? 0.3403 0.2205 0.4603 0.0341  -0.0865 -0.0792 517 THR   A CB  
7911  O  OG1 . THR   A 517 ? 0.3553 0.2344 0.4703 0.0359  -0.0875 -0.0891 517 THR   A OG1 
7912  C  CG2 . THR   A 517 ? 0.3747 0.2466 0.4893 0.0254  -0.0883 -0.0678 517 THR   A CG2 
7920  N  N   . TYR   A 518 ? 0.3357 0.2270 0.4587 0.0445  -0.0829 -0.0754 518 TYR   A N   
7921  C  CA  . TYR   A 518 ? 0.2762 0.1739 0.4081 0.0444  -0.0810 -0.0679 518 TYR   A CA  
7922  C  C   . TYR   A 518 ? 0.3258 0.2289 0.4498 0.0526  -0.0798 -0.0746 518 TYR   A C   
7923  O  O   . TYR   A 518 ? 0.2842 0.1958 0.4171 0.0581  -0.0780 -0.0857 518 TYR   A O   
7924  C  CB  . TYR   A 518 ? 0.3182 0.2212 0.4318 0.0390  -0.0752 -0.0622 518 TYR   A CB  
7925  C  CG  . TYR   A 518 ? 0.2733 0.1715 0.3896 0.0307  -0.0761 -0.0501 518 TYR   A CG  
7926  C  CD1 . TYR   A 518 ? 0.2805 0.1741 0.3959 0.0289  -0.0785 -0.0403 518 TYR   A CD1 
7927  C  CD2 . TYR   A 518 ? 0.2619 0.1588 0.3711 0.0245  -0.0750 -0.0479 518 TYR   A CD2 
7928  C  CE1 . TYR   A 518 ? 0.2761 0.1662 0.3892 0.0212  -0.0789 -0.0296 518 TYR   A CE1 
7929  C  CE2 . TYR   A 518 ? 0.2456 0.1397 0.3552 0.0170  -0.0753 -0.0376 518 TYR   A CE2 
7930  C  CZ  . TYR   A 518 ? 0.2816 0.1717 0.3893 0.0151  -0.0770 -0.0280 518 TYR   A CZ  
7931  O  OH  . TYR   A 518 ? 0.3121 0.2001 0.4159 0.0075  -0.0768 -0.0180 518 TYR   A OH  
7941  N  N   . ASP   A 519 ? 0.2987 0.2043 0.4350 0.0536  -0.0808 -0.0680 519 ASP   A N   
7942  C  CA  . ASP   A 519 ? 0.3390 0.2526 0.4699 0.0610  -0.0791 -0.0730 519 ASP   A CA  
7943  C  C   . ASP   A 519 ? 0.2477 0.1735 0.3877 0.0581  -0.0731 -0.0658 519 ASP   A C   
7944  O  O   . ASP   A 519 ? 0.2689 0.1894 0.3975 0.0513  -0.0732 -0.0574 519 ASP   A O   
7945  C  CB  . ASP   A 519 ? 0.3166 0.2235 0.4633 0.0659  -0.0861 -0.0730 519 ASP   A CB  
7946  C  CG  . ASP   A 519 ? 0.3102 0.2137 0.4769 0.0626  -0.0901 -0.0608 519 ASP   A CG  
7947  O  OD1 . ASP   A 519 ? 0.4394 0.3414 0.5751 0.0574  -0.0864 -0.0530 519 ASP   A OD1 
7948  O  OD2 . ASP   A 519 ? 0.5878 0.4742 0.7264 0.0654  -0.0969 -0.0595 519 ASP   A OD2 
7953  N  N   . ALA   A 520 ? 0.2637 0.1567 0.3826 0.0525  -0.0428 -0.0421 520 ALA   A N   
7954  C  CA  . ALA   A 520 ? 0.2816 0.1865 0.4004 0.0509  -0.0397 -0.0357 520 ALA   A CA  
7955  C  C   . ALA   A 520 ? 0.2742 0.1835 0.4018 0.0455  -0.0474 -0.0269 520 ALA   A C   
7956  O  O   . ALA   A 520 ? 0.2938 0.2092 0.4120 0.0415  -0.0478 -0.0225 520 ALA   A O   
7957  C  CB  . ALA   A 520 ? 0.3216 0.2315 0.4417 0.0564  -0.0328 -0.0375 520 ALA   A CB  
7963  N  N   . ASP   A 521 ? 0.3235 0.2265 0.4532 0.0451  -0.0533 -0.0241 521 ASP   A N   
7964  C  CA  . ASP   A 521 ? 0.2711 0.1802 0.4178 0.0395  -0.0609 -0.0155 521 ASP   A CA  
7965  C  C   . ASP   A 521 ? 0.2672 0.1730 0.4018 0.0334  -0.0671 -0.0117 521 ASP   A C   
7966  O  O   . ASP   A 521 ? 0.2650 0.1778 0.3980 0.0288  -0.0693 -0.0056 521 ASP   A O   
7967  C  CB  . ASP   A 521 ? 0.3319 0.2368 0.4899 0.0405  -0.0657 -0.0136 521 ASP   A CB  
7968  C  CG  . ASP   A 521 ? 0.4496 0.3556 0.6119 0.0467  -0.0598 -0.0166 521 ASP   A CG  
7969  O  OD1 . ASP   A 521 ? 0.5250 0.4240 0.6841 0.0523  -0.0556 -0.0237 521 ASP   A OD1 
7970  O  OD2 . ASP   A 521 ? 0.4889 0.4023 0.6543 0.0458  -0.0595 -0.0120 521 ASP   A OD2 
7975  N  N   . SER   A 522 ? 0.2530 0.1501 0.3879 0.0334  -0.0699 -0.0152 522 SER   A N   
7976  C  CA  . SER   A 522 ? 0.2849 0.1779 0.4072 0.0274  -0.0767 -0.0114 522 SER   A CA  
7977  C  C   . SER   A 522 ? 0.2177 0.1188 0.3393 0.0254  -0.0726 -0.0107 522 SER   A C   
7978  O  O   . SER   A 522 ? 0.2626 0.1658 0.3734 0.0197  -0.0769 -0.0044 522 SER   A O   
7979  C  CB  . SER   A 522 ? 0.2775 0.1604 0.4073 0.0281  -0.0802 -0.0157 522 SER   A CB  
7980  O  OG  . SER   A 522 ? 0.3268 0.2035 0.4459 0.0334  -0.0732 -0.0249 522 SER   A OG  
7986  N  N   . LEU   A 523 ? 0.2228 0.1241 0.3330 0.0297  -0.0644 -0.0173 523 LEU   A N   
7987  C  CA  . LEU   A 523 ? 0.2458 0.1512 0.3415 0.0279  -0.0605 -0.0176 523 LEU   A CA  
7988  C  C   . LEU   A 523 ? 0.2062 0.1241 0.3082 0.0256  -0.0594 -0.0115 523 LEU   A C   
7989  O  O   . LEU   A 523 ? 0.1991 0.1202 0.2942 0.0216  -0.0611 -0.0072 523 LEU   A O   
7990  C  CB  . LEU   A 523 ? 0.2361 0.1413 0.3288 0.0327  -0.0523 -0.0259 523 LEU   A CB  
7991  C  CG  . LEU   A 523 ? 0.2262 0.1338 0.3064 0.0309  -0.0491 -0.0275 523 LEU   A CG  
7992  C  CD1 . LEU   A 523 ? 0.1947 0.0971 0.2736 0.0255  -0.0556 -0.0250 523 LEU   A CD1 
7993  C  CD2 . LEU   A 523 ? 0.2050 0.1125 0.2828 0.0353  -0.0416 -0.0355 523 LEU   A CD2 
8005  N  N   . LEU   A 524 ? 0.2165 0.1388 0.3233 0.0286  -0.0565 -0.0109 524 LEU   A N   
8006  C  CA  . LEU   A 524 ? 0.2447 0.1757 0.3487 0.0262  -0.0559 -0.0055 524 LEU   A CA  
8007  C  C   . LEU   A 524 ? 0.1873 0.1201 0.3001 0.0201  -0.0638 0.0022  524 LEU   A C   
8008  O  O   . LEU   A 524 ? 0.1633 0.1018 0.2698 0.0167  -0.0639 0.0065  524 LEU   A O   
8009  C  CB  . LEU   A 524 ? 0.2584 0.1939 0.3714 0.0301  -0.0521 -0.0063 524 LEU   A CB  
8010  C  CG  . LEU   A 524 ? 0.2644 0.2067 0.3763 0.0339  -0.0438 -0.0099 524 LEU   A CG  
8011  C  CD1 . LEU   A 524 ? 0.3302 0.2744 0.4436 0.0375  -0.0411 -0.0100 524 LEU   A CD1 
8012  C  CD2 . LEU   A 524 ? 0.2498 0.1992 0.3533 0.0308  -0.0419 -0.0074 524 LEU   A CD2 
8024  N  N   . GLU   A 525 ? 0.2226 0.1477 0.3360 0.0189  -0.0702 0.0039  525 GLU   A N   
8025  C  CA  . GLU   A 525 ? 0.2018 0.1285 0.3231 0.0125  -0.0783 0.0117  525 GLU   A CA  
8026  C  C   . GLU   A 525 ? 0.1987 0.1251 0.3075 0.0082  -0.0798 0.0143  525 GLU   A C   
8027  O  O   . GLU   A 525 ? 0.1706 0.1025 0.2800 0.0027  -0.0828 0.0210  525 GLU   A O   
8028  C  CB  . GLU   A 525 ? 0.2311 0.1509 0.3607 0.0122  -0.0852 0.0132  525 GLU   A CB  
8029  C  CG  . GLU   A 525 ? 0.2793 0.2006 0.4143 0.0052  -0.0937 0.0216  525 GLU   A CG  
8030  C  CD  . GLU   A 525 ? 0.3626 0.2765 0.5020 0.0045  -0.1010 0.0235  525 GLU   A CD  
8031  O  OE1 . GLU   A 525 ? 0.3790 0.2860 0.5233 0.0060  -0.1033 0.0200  525 GLU   A OE1 
8032  O  OE2 . GLU   A 525 ? 0.3240 0.2424 0.4788 0.0024  -0.1048 0.0283  525 GLU   A OE2 
8039  N  N   . ALA   A 526 ? 0.2005 0.1221 0.3042 0.0103  -0.0776 0.0092  526 ALA   A N   
8040  C  CA  . ALA   A 526 ? 0.1952 0.1178 0.2934 0.0063  -0.0787 0.0112  526 ALA   A CA  
8041  C  C   . ALA   A 526 ? 0.1870 0.1181 0.2771 0.0051  -0.0737 0.0133  526 ALA   A C   
8042  O  O   . ALA   A 526 ? 0.1716 0.1066 0.2581 0.0000  -0.0756 0.0189  526 ALA   A O   
8043  C  CB  . ALA   A 526 ? 0.2541 0.1676 0.3423 0.0087  -0.0773 0.0050  526 ALA   A CB  
8049  N  N   . GLY   A 527 ? 0.2016 0.1359 0.2884 0.0098  -0.0670 0.0089  527 GLY   A N   
8050  C  CA  . GLY   A 527 ? 0.1644 0.1079 0.2505 0.0091  -0.0623 0.0104  527 GLY   A CA  
8051  C  C   . GLY   A 527 ? 0.1417 0.0908 0.2308 0.0050  -0.0652 0.0175  527 GLY   A C   
8052  O  O   . GLY   A 527 ? 0.1529 0.1065 0.2338 0.0016  -0.0640 0.0210  527 GLY   A O   
8056  N  N   . ASP   A 528 ? 0.1609 0.1077 0.2528 0.0045  -0.0690 0.0196  528 ASP   A N   
8057  C  CA  . ASP   A 528 ? 0.1468 0.0985 0.2445 -0.0003 -0.0727 0.0266  528 ASP   A CA  
8058  C  C   . ASP   A 528 ? 0.1397 0.0913 0.2335 -0.0068 -0.0775 0.0326  528 ASP   A C   
8059  O  O   . ASP   A 528 ? 0.1305 0.0878 0.2177 -0.0108 -0.0765 0.0377  528 ASP   A O   
8060  C  CB  . ASP   A 528 ? 0.1874 0.1364 0.2912 0.0003  -0.0763 0.0279  528 ASP   A CB  
8061  C  CG  . ASP   A 528 ? 0.2122 0.1645 0.3150 -0.0046 -0.0802 0.0350  528 ASP   A CG  
8062  O  OD1 . ASP   A 528 ? 0.1856 0.1432 0.2866 -0.0090 -0.0799 0.0393  528 ASP   A OD1 
8063  O  OD2 . ASP   A 528 ? 0.1849 0.1374 0.3009 -0.0041 -0.0830 0.0361  528 ASP   A OD2 
8068  N  N   A ARG   A 529 ? 0.1627 0.1078 0.2550 -0.0076 -0.0817 0.0325  529 ARG   A N   
8069  N  N   B ARG   A 529 ? 0.1627 0.1078 0.2550 -0.0076 -0.0817 0.0325  529 ARG   A N   
8070  C  CA  A ARG   A 529 ? 0.1607 0.1066 0.2519 -0.0140 -0.0862 0.0382  529 ARG   A CA  
8071  C  CA  B ARG   A 529 ? 0.1608 0.1066 0.2519 -0.0140 -0.0862 0.0381  529 ARG   A CA  
8072  C  C   A ARG   A 529 ? 0.1366 0.0882 0.2217 -0.0156 -0.0813 0.0392  529 ARG   A C   
8073  C  C   B ARG   A 529 ? 0.1366 0.0882 0.2217 -0.0157 -0.0813 0.0393  529 ARG   A C   
8074  O  O   A ARG   A 529 ? 0.1729 0.1288 0.2492 -0.0212 -0.0820 0.0455  529 ARG   A O   
8075  O  O   B ARG   A 529 ? 0.1729 0.1289 0.2492 -0.0213 -0.0820 0.0456  529 ARG   A O   
8076  C  CB  A ARG   A 529 ? 0.1925 0.1298 0.2847 -0.0137 -0.0916 0.0367  529 ARG   A CB  
8077  C  CB  B ARG   A 529 ? 0.1925 0.1298 0.2848 -0.0137 -0.0916 0.0367  529 ARG   A CB  
8078  C  CG  A ARG   A 529 ? 0.1844 0.1231 0.2779 -0.0195 -0.0957 0.0415  529 ARG   A CG  
8079  C  CG  B ARG   A 529 ? 0.1844 0.1231 0.2779 -0.0196 -0.0957 0.0415  529 ARG   A CG  
8080  C  CD  A ARG   A 529 ? 0.2227 0.1529 0.3185 -0.0197 -0.1024 0.0407  529 ARG   A CD  
8081  C  CD  B ARG   A 529 ? 0.2227 0.1528 0.3185 -0.0197 -0.1024 0.0407  529 ARG   A CD  
8082  N  NE  A ARG   A 529 ? 0.2675 0.1882 0.3593 -0.0130 -0.1002 0.0321  529 ARG   A NE  
8083  N  NE  B ARG   A 529 ? 0.2675 0.1882 0.3593 -0.0130 -0.1002 0.0321  529 ARG   A NE  
8084  C  CZ  A ARG   A 529 ? 0.2248 0.1408 0.3329 -0.0086 -0.1017 0.0276  529 ARG   A CZ  
8085  C  CZ  B ARG   A 529 ? 0.2248 0.1409 0.3329 -0.0086 -0.1017 0.0276  529 ARG   A CZ  
8086  N  NH1 A ARG   A 529 ? 0.2529 0.1689 0.3634 -0.0100 -0.1059 0.0314  529 ARG   A NH1 
8087  N  NH1 B ARG   A 529 ? 0.2529 0.1689 0.3634 -0.0101 -0.1059 0.0314  529 ARG   A NH1 
8088  N  NH2 A ARG   A 529 ? 0.2575 0.1641 0.3572 -0.0033 -0.0988 0.0197  529 ARG   A NH2 
8089  N  NH2 B ARG   A 529 ? 0.2575 0.1641 0.3572 -0.0033 -0.0988 0.0196  529 ARG   A NH2 
8116  N  N   . ILE   A 530 ? 0.1490 0.0994 0.2283 -0.0110 -0.0764 0.0333  530 ILE   A N   
8117  C  CA  . ILE   A 530 ? 0.2000 0.1529 0.2628 -0.0122 -0.0716 0.0338  530 ILE   A CA  
8118  C  C   . ILE   A 530 ? 0.1145 0.0793 0.1874 -0.0132 -0.0674 0.0368  530 ILE   A C   
8119  O  O   . ILE   A 530 ? 0.1241 0.0940 0.1862 -0.0173 -0.0659 0.0413  530 ILE   A O   
8120  C  CB  . ILE   A 530 ? 0.1757 0.1271 0.2446 -0.0073 -0.0678 0.0269  530 ILE   A CB  
8121  C  CG1 . ILE   A 530 ? 0.1521 0.0951 0.2236 -0.0073 -0.0718 0.0241  530 ILE   A CG1 
8122  C  CG2 . ILE   A 530 ? 0.1841 0.1417 0.2468 -0.0079 -0.0625 0.0275  530 ILE   A CG2 
8123  C  CD1 . ILE   A 530 ? 0.1899 0.1263 0.2554 -0.0018 -0.0683 0.0160  530 ILE   A CD1 
8136  N  N   . TRP   A 531 ? 0.1344 0.0989 0.2030 -0.0091 -0.0648 0.0341  531 TRP   A N   
8137  C  CA  . TRP   A 531 ? 0.1408 0.1130 0.2065 -0.0097 -0.0616 0.0363  531 TRP   A CA  
8138  C  C   . TRP   A 531 ? 0.1420 0.1176 0.2058 -0.0157 -0.0650 0.0440  531 TRP   A C   
8139  O  O   . TRP   A 531 ? 0.1436 0.1267 0.2016 -0.0176 -0.0620 0.0470  531 TRP   A O   
8140  C  CB  . TRP   A 531 ? 0.1328 0.1055 0.2029 -0.0051 -0.0597 0.0323  531 TRP   A CB  
8141  C  CG  . TRP   A 531 ? 0.1322 0.1115 0.1981 -0.0049 -0.0568 0.0336  531 TRP   A CG  
8142  C  CD1 . TRP   A 531 ? 0.1333 0.1162 0.1989 -0.0086 -0.0594 0.0386  531 TRP   A CD1 
8143  C  CD2 . TRP   A 531 ? 0.1288 0.1137 0.1927 -0.0016 -0.0510 0.0297  531 TRP   A CD2 
8144  N  NE1 . TRP   A 531 ? 0.1662 0.1543 0.2234 -0.0071 -0.0559 0.0378  531 TRP   A NE1 
8145  C  CE2 . TRP   A 531 ? 0.1379 0.1282 0.1979 -0.0030 -0.0509 0.0323  531 TRP   A CE2 
8146  C  CE3 . TRP   A 531 ? 0.1288 0.1146 0.1927 0.0022  -0.0462 0.0243  531 TRP   A CE3 
8147  C  CZ2 . TRP   A 531 ? 0.1198 0.1162 0.1786 -0.0002 -0.0465 0.0292  531 TRP   A CZ2 
8148  C  CZ3 . TRP   A 531 ? 0.1414 0.1330 0.2014 0.0044  -0.0415 0.0219  531 TRP   A CZ3 
8149  C  CH2 . TRP   A 531 ? 0.1265 0.1234 0.1857 0.0032  -0.0418 0.0240  531 TRP   A CH2 
8160  N  N   . THR   A 532 ? 0.1386 0.1097 0.2074 -0.0183 -0.0709 0.0468  532 THR   A N   
8161  C  CA  . THR   A 532 ? 0.1306 0.1056 0.2001 -0.0247 -0.0746 0.0544  532 THR   A CA  
8162  C  C   . THR   A 532 ? 0.1127 0.0937 0.1808 -0.0299 -0.0719 0.0565  532 THR   A C   
8163  O  O   . THR   A 532 ? 0.1668 0.1529 0.2231 -0.0337 -0.0730 0.0642  532 THR   A O   
8164  C  CB  . THR   A 532 ? 0.1575 0.1263 0.2322 -0.0264 -0.0814 0.0565  532 THR   A CB  
8165  O  OG1 . THR   A 532 ? 0.1618 0.1286 0.2434 -0.0213 -0.0806 0.0521  532 THR   A OG1 
8166  C  CG2 . THR   A 532 ? 0.1314 0.1058 0.2090 -0.0333 -0.0838 0.0631  532 THR   A CG2 
8174  N  N   . LEU   A 533 ? 0.1489 0.1232 0.2122 -0.0289 -0.0750 0.0566  533 LEU   A N   
8175  C  CA  . LEU   A 533 ? 0.1479 0.1270 0.2099 -0.0336 -0.0745 0.0601  533 LEU   A CA  
8176  C  C   . LEU   A 533 ? 0.1388 0.1270 0.1934 -0.0328 -0.0675 0.0609  533 LEU   A C   
8177  O  O   . LEU   A 533 ? 0.1255 0.1222 0.1778 -0.0375 -0.0661 0.0663  533 LEU   A O   
8178  C  CB  . LEU   A 533 ? 0.1552 0.1273 0.2191 -0.0324 -0.0771 0.0571  533 LEU   A CB  
8179  C  CG  . LEU   A 533 ? 0.1550 0.1319 0.2212 -0.0372 -0.0775 0.0606  533 LEU   A CG  
8180  C  CD1 . LEU   A 533 ? 0.2005 0.1782 0.2645 -0.0434 -0.0832 0.0672  533 LEU   A CD1 
8181  C  CD2 . LEU   A 533 ? 0.1832 0.1527 0.2441 -0.0349 -0.0786 0.0561  533 LEU   A CD2 
8193  N  N   . GLU   A 534 ? 0.1378 0.1257 0.1900 -0.0275 -0.0628 0.0554  534 GLU   A N   
8194  C  CA  . GLU   A 534 ? 0.1277 0.1254 0.1769 -0.0262 -0.0565 0.0551  534 GLU   A CA  
8195  C  C   . GLU   A 534 ? 0.1525 0.1570 0.1929 -0.0284 -0.0559 0.0594  534 GLU   A C   
8196  O  O   . GLU   A 534 ? 0.1283 0.1432 0.1679 -0.0307 -0.0523 0.0625  534 GLU   A O   
8197  C  CB  . GLU   A 534 ? 0.1323 0.1281 0.1811 -0.0200 -0.0530 0.0484  534 GLU   A CB  
8198  C  CG  . GLU   A 534 ? 0.1580 0.1471 0.2074 -0.0181 -0.0530 0.0444  534 GLU   A CG  
8199  C  CD  . GLU   A 534 ? 0.1680 0.1550 0.2176 -0.0120 -0.0498 0.0375  534 GLU   A CD  
8200  O  OE1 . GLU   A 534 ? 0.1338 0.1241 0.1884 -0.0089 -0.0480 0.0352  534 GLU   A OE1 
8201  O  OE2 . GLU   A 534 ? 0.1600 0.1445 0.2133 -0.0108 -0.0492 0.0346  534 GLU   A OE2 
8208  N  N   . LYS   A 535 ? 0.1501 0.1518 0.1948 -0.0279 -0.0590 0.0593  535 LYS   A N   
8209  C  CA  . LYS   A 535 ? 0.1530 0.1612 0.1928 -0.0306 -0.0594 0.0633  535 LYS   A CA  
8210  C  C   . LYS   A 535 ? 0.1456 0.1605 0.1845 -0.0374 -0.0608 0.0704  535 LYS   A C   
8211  O  O   . LYS   A 535 ? 0.1443 0.1692 0.1758 -0.0394 -0.0579 0.0731  535 LYS   A O   
8212  C  CB  . LYS   A 535 ? 0.1504 0.1529 0.1946 -0.0296 -0.0636 0.0627  535 LYS   A CB  
8213  C  CG  . LYS   A 535 ? 0.1555 0.1631 0.1941 -0.0333 -0.0655 0.0671  535 LYS   A CG  
8214  C  CD  . LYS   A 535 ? 0.1402 0.1566 0.1756 -0.0316 -0.0616 0.0652  535 LYS   A CD  
8215  C  CE  . LYS   A 535 ? 0.1986 0.2177 0.2208 -0.0350 -0.0638 0.0685  535 LYS   A CE  
8216  N  NZ  . LYS   A 535 ? 0.1664 0.1947 0.1861 -0.0339 -0.0605 0.0660  535 LYS   A NZ  
8230  N  N   . LEU   A 536 ? 0.1596 0.1690 0.2016 -0.0406 -0.0655 0.0735  536 LEU   A N   
8231  C  CA  . LEU   A 536 ? 0.1436 0.1595 0.1863 -0.0474 -0.0676 0.0805  536 LEU   A CA  
8232  C  C   . LEU   A 536 ? 0.1152 0.1418 0.1601 -0.0481 -0.0613 0.0804  536 LEU   A C   
8233  O  O   . LEU   A 536 ? 0.1579 0.1941 0.1927 -0.0521 -0.0608 0.0864  536 LEU   A O   
8234  C  CB  . LEU   A 536 ? 0.1297 0.1383 0.1839 -0.0500 -0.0739 0.0820  536 LEU   A CB  
8235  C  CG  . LEU   A 536 ? 0.1537 0.1544 0.2157 -0.0499 -0.0801 0.0825  536 LEU   A CG  
8236  C  CD1 . LEU   A 536 ? 0.2059 0.1967 0.2706 -0.0513 -0.0868 0.0823  536 LEU   A CD1 
8237  C  CD2 . LEU   A 536 ? 0.1980 0.2039 0.2525 -0.0545 -0.0822 0.0886  536 LEU   A CD2 
8249  N  N   . PHE   A 537 ? 0.1382 0.1601 0.1774 -0.0445 -0.0594 0.0770  537 PHE   A N   
8250  C  CA  . PHE   A 537 ? 0.1205 0.1520 0.1598 -0.0449 -0.0544 0.0777  537 PHE   A CA  
8251  C  C   . PHE   A 537 ? 0.1186 0.1616 0.1533 -0.0440 -0.0489 0.0781  537 PHE   A C   
8252  O  O   . PHE   A 537 ? 0.1609 0.2146 0.1890 -0.0466 -0.0462 0.0819  537 PHE   A O   
8253  C  CB  . PHE   A 537 ? 0.1121 0.1383 0.1546 -0.0414 -0.0524 0.0727  537 PHE   A CB  
8254  C  CG  . PHE   A 537 ? 0.1267 0.1618 0.1658 -0.0414 -0.0474 0.0734  537 PHE   A CG  
8255  C  CD1 . PHE   A 537 ? 0.1107 0.1540 0.1483 -0.0383 -0.0412 0.0718  537 PHE   A CD1 
8256  C  CD2 . PHE   A 537 ? 0.1211 0.1593 0.1677 -0.0444 -0.0488 0.0758  537 PHE   A CD2 
8257  C  CE1 . PHE   A 537 ? 0.1052 0.1582 0.1445 -0.0380 -0.0366 0.0727  537 PHE   A CE1 
8258  C  CE2 . PHE   A 537 ? 0.1472 0.1939 0.1905 -0.0440 -0.0445 0.0768  537 PHE   A CE2 
8259  C  CZ  . PHE   A 537 ? 0.1221 0.1769 0.1653 -0.0406 -0.0382 0.0750  537 PHE   A CZ  
8269  N  N   . ASN   A 538 ? 0.1267 0.1666 0.1561 -0.0396 -0.0477 0.0735  538 ASN   A N   
8270  C  CA  . ASN   A 538 ? 0.1503 0.1991 0.1698 -0.0383 -0.0433 0.0727  538 ASN   A CA  
8271  C  C   . ASN   A 538 ? 0.1297 0.1876 0.1482 -0.0432 -0.0443 0.0779  538 ASN   A C   
8272  O  O   . ASN   A 538 ? 0.1763 0.2449 0.1842 -0.0444 -0.0398 0.0791  538 ASN   A O   
8273  C  CB  . ASN   A 538 ? 0.1545 0.1984 0.1739 -0.0329 -0.0431 0.0665  538 ASN   A CB  
8274  C  CG  . ASN   A 538 ? 0.1349 0.1774 0.1602 -0.0279 -0.0399 0.0612  538 ASN   A CG  
8275  O  OD1 . ASN   A 538 ? 0.1078 0.1521 0.1359 -0.0286 -0.0377 0.0624  538 ASN   A OD1 
8276  N  ND2 . ASN   A 538 ? 0.1644 0.2033 0.1886 -0.0232 -0.0400 0.0555  538 ASN   A ND2 
8283  N  N   . LEU   A 539 ? 0.1144 0.1663 0.1355 -0.0461 -0.0497 0.0800  539 LEU   A N   
8284  C  CA  . LEU   A 539 ? 0.1578 0.2164 0.1705 -0.0516 -0.0521 0.0865  539 LEU   A CA  
8285  C  C   . LEU   A 539 ? 0.1759 0.2454 0.1897 -0.0557 -0.0503 0.0915  539 LEU   A C   
8286  O  O   . LEU   A 539 ? 0.1906 0.2723 0.1983 -0.0580 -0.0470 0.0938  539 LEU   A O   
8287  C  CB  . LEU   A 539 ? 0.1413 0.1920 0.1629 -0.0542 -0.0592 0.0890  539 LEU   A CB  
8288  C  CG  . LEU   A 539 ? 0.1726 0.2141 0.1891 -0.0506 -0.0616 0.0852  539 LEU   A CG  
8289  C  CD1 . LEU   A 539 ? 0.1611 0.1938 0.1887 -0.0527 -0.0683 0.0876  539 LEU   A CD1 
8290  C  CD2 . LEU   A 539 ? 0.1621 0.2122 0.1721 -0.0515 -0.0599 0.0850  539 LEU   A CD2 
8302  N  N   . ALA   A 540 ? 0.1535 0.2195 0.1778 -0.0563 -0.0520 0.0928  540 ALA   A N   
8303  C  CA  . ALA   A 540 ? 0.1559 0.2322 0.1845 -0.0599 -0.0509 0.0975  540 ALA   A CA  
8304  C  C   . ALA   A 540 ? 0.1728 0.2593 0.1936 -0.0568 -0.0432 0.0954  540 ALA   A C   
8305  O  O   . ALA   A 540 ? 0.1942 0.2924 0.2136 -0.0591 -0.0409 0.0994  540 ALA   A O   
8306  C  CB  . ALA   A 540 ? 0.1887 0.2566 0.2222 -0.0608 -0.0550 0.0983  540 ALA   A CB  
8312  N  N   . ALA   A 541 ? 0.1553 0.2384 0.1757 -0.0517 -0.0392 0.0896  541 ALA   A N   
8313  C  CA  . ALA   A 541 ? 0.1731 0.2648 0.1880 -0.0482 -0.0315 0.0866  541 ALA   A CA  
8314  C  C   . ALA   A 541 ? 0.2106 0.3107 0.2108 -0.0480 -0.0267 0.0852  541 ALA   A C   
8315  O  O   . ALA   A 541 ? 0.1921 0.3009 0.1947 -0.0452 -0.0193 0.0821  541 ALA   A O   
8316  C  CB  . ALA   A 541 ? 0.1415 0.2263 0.1614 -0.0434 -0.0298 0.0815  541 ALA   A CB  
8322  N  N   . GLY   A 542 ? 0.1682 0.2686 0.1719 -0.0508 -0.0305 0.0867  542 GLY   A N   
8323  C  CA  . GLY   A 542 ? 0.2181 0.3243 0.2036 -0.0510 -0.0269 0.0842  542 GLY   A CA  
8324  C  C   . GLY   A 542 ? 0.2146 0.3162 0.1973 -0.0470 -0.0259 0.0777  542 GLY   A C   
8325  O  O   . GLY   A 542 ? 0.2551 0.3628 0.2259 -0.0464 -0.0215 0.0736  542 GLY   A O   
8329  N  N   . ILE   A 543 ? 0.1723 0.2625 0.1638 -0.0441 -0.0302 0.0756  543 ILE   A N   
8330  C  CA  . ILE   A 543 ? 0.1819 0.2659 0.1687 -0.0399 -0.0312 0.0697  543 ILE   A CA  
8331  C  C   . ILE   A 543 ? 0.2240 0.3011 0.2066 -0.0420 -0.0378 0.0705  543 ILE   A C   
8332  O  O   . ILE   A 543 ? 0.2491 0.3158 0.2412 -0.0418 -0.0432 0.0721  543 ILE   A O   
8333  C  CB  . ILE   A 543 ? 0.1495 0.2269 0.1489 -0.0349 -0.0314 0.0660  543 ILE   A CB  
8334  C  CG1 . ILE   A 543 ? 0.1504 0.2331 0.1527 -0.0331 -0.0241 0.0646  543 ILE   A CG1 
8335  C  CG2 . ILE   A 543 ? 0.1982 0.2686 0.1923 -0.0299 -0.0313 0.0575  543 ILE   A CG2 
8336  C  CD1 . ILE   A 543 ? 0.2161 0.3065 0.2081 -0.0308 -0.0153 0.0584  543 ILE   A CD1 
8348  N  N   . ASP   A 544 ? 0.1951 0.2795 0.1752 -0.0440 -0.0373 0.0694  544 ASP   A N   
8349  C  CA  . ASP   A 544 ? 0.2814 0.3584 0.2488 -0.0467 -0.0435 0.0709  544 ASP   A CA  
8350  C  C   . ASP   A 544 ? 0.2519 0.3188 0.2254 -0.0421 -0.0474 0.0661  544 ASP   A C   
8351  O  O   . ASP   A 544 ? 0.1827 0.2512 0.1641 -0.0373 -0.0444 0.0604  544 ASP   A O   
8352  C  CB  . ASP   A 544 ? 0.3009 0.3885 0.2624 -0.0502 -0.0416 0.0704  544 ASP   A CB  
8353  C  CG  . ASP   A 544 ? 0.3742 0.4586 0.3318 -0.0548 -0.0479 0.0744  544 ASP   A CG  
8354  O  OD1 . ASP   A 544 ? 0.4316 0.5182 0.3872 -0.0599 -0.0501 0.0813  544 ASP   A OD1 
8355  O  OD2 . ASP   A 544 ? 0.4136 0.4925 0.3652 -0.0536 -0.0508 0.0708  544 ASP   A OD2 
8360  N  N   . SER   A 545 ? 0.2155 0.2761 0.1992 -0.0437 -0.0535 0.0684  545 SER   A N   
8361  C  CA  . SER   A 545 ? 0.2283 0.2785 0.2098 -0.0395 -0.0570 0.0642  545 SER   A CA  
8362  C  C   . SER   A 545 ? 0.1559 0.2132 0.1388 -0.0385 -0.0556 0.0586  545 SER   A C   
8363  O  O   . SER   A 545 ? 0.1826 0.2331 0.1627 -0.0340 -0.0569 0.0536  545 SER   A O   
8364  C  CB  . SER   A 545 ? 0.2175 0.2618 0.2126 -0.0420 -0.0632 0.0687  545 SER   A CB  
8365  O  OG  . SER   A 545 ? 0.2499 0.2886 0.2499 -0.0431 -0.0647 0.0728  545 SER   A OG  
8371  N  N   . SER   A 546 ? 0.1828 0.2487 0.1473 -0.0424 -0.0527 0.0586  546 SER   A N   
8372  C  CA  . SER   A 546 ? 0.2300 0.2993 0.1794 -0.0415 -0.0504 0.0516  546 SER   A CA  
8373  C  C   . SER   A 546 ? 0.1949 0.2659 0.1504 -0.0358 -0.0456 0.0441  546 SER   A C   
8374  O  O   . SER   A 546 ? 0.1736 0.2443 0.1275 -0.0332 -0.0436 0.0360  546 SER   A O   
8375  C  CB  . SER   A 546 ? 0.2434 0.3240 0.1833 -0.0462 -0.0464 0.0519  546 SER   A CB  
8376  O  OG  . SER   A 546 ? 0.2958 0.3835 0.2293 -0.0464 -0.0398 0.0533  546 SER   A OG  
8382  N  N   . GLN   A 547 ? 0.1683 0.2391 0.1360 -0.0327 -0.0419 0.0445  547 GLN   A N   
8383  C  CA  . GLN   A 547 ? 0.1826 0.2504 0.1547 -0.0263 -0.0354 0.0367  547 GLN   A CA  
8384  C  C   . GLN   A 547 ? 0.1588 0.2176 0.1449 -0.0217 -0.0392 0.0340  547 GLN   A C   
8385  O  O   . GLN   A 547 ? 0.1513 0.2086 0.1450 -0.0168 -0.0347 0.0280  547 GLN   A O   
8386  C  CB  . GLN   A 547 ? 0.1762 0.2490 0.1542 -0.0258 -0.0296 0.0386  547 GLN   A CB  
8387  C  CG  . GLN   A 547 ? 0.1833 0.2671 0.1514 -0.0290 -0.0234 0.0399  547 GLN   A CG  
8388  C  CD  . GLN   A 547 ? 0.1907 0.2802 0.1662 -0.0268 -0.0154 0.0388  547 GLN   A CD  
8389  O  OE1 . GLN   A 547 ? 0.2079 0.2934 0.1890 -0.0215 -0.0122 0.0331  547 GLN   A OE1 
8390  N  NE2 . GLN   A 547 ? 0.2283 0.3257 0.1955 -0.0306 -0.0127 0.0448  547 GLN   A NE2 
8399  N  N   . ASP   A 548 ? 0.1440 0.1974 0.1335 -0.0235 -0.0475 0.0387  548 ASP   A N   
8400  C  CA  . ASP   A 548 ? 0.1388 0.1845 0.1400 -0.0193 -0.0513 0.0367  548 ASP   A CA  
8401  C  C   . ASP   A 548 ? 0.1686 0.2132 0.1628 -0.0183 -0.0522 0.0312  548 ASP   A C   
8402  O  O   . ASP   A 548 ? 0.1623 0.2063 0.1554 -0.0218 -0.0583 0.0343  548 ASP   A O   
8403  C  CB  . ASP   A 548 ? 0.1302 0.1675 0.1381 -0.0201 -0.0561 0.0421  548 ASP   A CB  
8404  C  CG  . ASP   A 548 ? 0.1456 0.1792 0.1564 -0.0203 -0.0550 0.0457  548 ASP   A CG  
8405  O  OD1 . ASP   A 548 ? 0.1258 0.1638 0.1395 -0.0191 -0.0510 0.0444  548 ASP   A OD1 
8406  O  OD2 . ASP   A 548 ? 0.1526 0.1805 0.1686 -0.0221 -0.0581 0.0496  548 ASP   A OD2 
8411  N  N   . THR   A 549 ? 0.1497 0.1960 0.1502 -0.0142 -0.0464 0.0232  549 THR   A N   
8412  C  CA  . THR   A 549 ? 0.1579 0.2042 0.1566 -0.0134 -0.0472 0.0173  549 THR   A CA  
8413  C  C   . THR   A 549 ? 0.1308 0.1746 0.1369 -0.0074 -0.0432 0.0107  549 THR   A C   
8414  O  O   . THR   A 549 ? 0.1083 0.1519 0.1242 -0.0043 -0.0396 0.0105  549 THR   A O   
8415  C  CB  . THR   A 549 ? 0.2518 0.3035 0.2332 -0.0166 -0.0437 0.0138  549 THR   A CB  
8416  O  OG1 . THR   A 549 ? 0.3587 0.4074 0.3297 -0.0172 -0.0469 0.0094  549 THR   A OG1 
8417  C  CG2 . THR   A 549 ? 0.2391 0.2956 0.2212 -0.0136 -0.0343 0.0088  549 THR   A CG2 
8425  N  N   . LEU   A 550 ? 0.1260 0.1687 0.1316 -0.0068 -0.0448 0.0054  550 LEU   A N   
8426  C  CA  . LEU   A 550 ? 0.1253 0.1675 0.1414 -0.0019 -0.0413 -0.0010 550 LEU   A CA  
8427  C  C   . LEU   A 550 ? 0.1273 0.1711 0.1327 -0.0026 -0.0387 -0.0083 550 LEU   A C   
8428  O  O   . LEU   A 550 ? 0.1511 0.1955 0.1428 -0.0066 -0.0410 -0.0084 550 LEU   A O   
8429  C  CB  . LEU   A 550 ? 0.1624 0.1987 0.1841 0.0003  -0.0470 0.0003  550 LEU   A CB  
8430  C  CG  . LEU   A 550 ? 0.1135 0.1496 0.1563 0.0029  -0.0477 0.0050  550 LEU   A CG  
8431  C  CD1 . LEU   A 550 ? 0.1440 0.1741 0.1877 0.0048  -0.0494 0.0061  550 LEU   A CD1 
8432  C  CD2 . LEU   A 550 ? 0.1332 0.1701 0.1763 0.0065  -0.0410 0.0030  550 LEU   A CD2 
8444  N  N   . PRO   A 551 ? 0.1059 0.1515 0.1213 0.0013  -0.0331 -0.0146 551 PRO   A N   
8445  C  CA  . PRO   A 551 ? 0.1541 0.1989 0.1581 0.0015  -0.0310 -0.0225 551 PRO   A CA  
8446  C  C   . PRO   A 551 ? 0.1607 0.2011 0.1590 -0.0009 -0.0386 -0.0241 551 PRO   A C   
8447  O  O   . PRO   A 551 ? 0.1218 0.1594 0.1320 -0.0004 -0.0447 -0.0202 551 PRO   A O   
8448  C  CB  . PRO   A 551 ? 0.1572 0.2025 0.1743 0.0064  -0.0264 -0.0267 551 PRO   A CB  
8449  C  CG  . PRO   A 551 ? 0.1279 0.1759 0.1551 0.0078  -0.0232 -0.0216 551 PRO   A CG  
8450  C  CD  . PRO   A 551 ? 0.1119 0.1577 0.1371 0.0055  -0.0287 -0.0145 551 PRO   A CD  
8458  N  N   . LYS   A 552 ? 0.1720 0.2133 0.1589 -0.0033 -0.0382 -0.0298 552 LYS   A N   
8459  C  CA  . LYS   A 552 ? 0.1920 0.2284 0.1706 -0.0064 -0.0458 -0.0322 552 LYS   A CA  
8460  C  C   . LYS   A 552 ? 0.1621 0.1936 0.1563 -0.0034 -0.0503 -0.0337 552 LYS   A C   
8461  O  O   . LYS   A 552 ? 0.1490 0.1769 0.1450 -0.0055 -0.0587 -0.0302 552 LYS   A O   
8462  C  CB  . LYS   A 552 ? 0.2312 0.2695 0.1975 -0.0085 -0.0431 -0.0406 552 LYS   A CB  
8463  C  CG  . LYS   A 552 ? 0.3477 0.3806 0.2986 -0.0129 -0.0509 -0.0436 552 LYS   A CG  
8464  C  CD  . LYS   A 552 ? 0.4736 0.5071 0.4052 -0.0145 -0.0473 -0.0532 552 LYS   A CD  
8465  C  CE  . LYS   A 552 ? 0.5682 0.5992 0.4814 -0.0213 -0.0549 -0.0537 552 LYS   A CE  
8466  N  NZ  . LYS   A 552 ? 0.6249 0.6544 0.5213 -0.0226 -0.0524 -0.0649 552 LYS   A NZ  
8480  N  N   . ARG   A 553 ? 0.1564 0.1886 0.1641 0.0015  -0.0451 -0.0380 553 ARG   A N   
8481  C  CA  . ARG   A 553 ? 0.1921 0.2195 0.2089 0.0043  -0.0488 -0.0390 553 ARG   A CA  
8482  C  C   . ARG   A 553 ? 0.1649 0.1922 0.1952 0.0045  -0.0542 -0.0304 553 ARG   A C   
8483  O  O   . ARG   A 553 ? 0.1177 0.1424 0.1581 0.0040  -0.0612 -0.0289 553 ARG   A O   
8484  C  CB  . ARG   A 553 ? 0.1665 0.1971 0.2007 0.0092  -0.0421 -0.0429 553 ARG   A CB  
8485  C  CG  . ARG   A 553 ? 0.1593 0.1883 0.2110 0.0119  -0.0450 -0.0417 553 ARG   A CG  
8486  C  CD  . ARG   A 553 ? 0.1691 0.1995 0.2296 0.0159  -0.0393 -0.0462 553 ARG   A CD  
8487  N  NE  . ARG   A 553 ? 0.1617 0.1894 0.2187 0.0158  -0.0383 -0.0555 553 ARG   A NE  
8488  C  CZ  . ARG   A 553 ? 0.1555 0.1843 0.2151 0.0189  -0.0319 -0.0610 553 ARG   A CZ  
8489  N  NH1 . ARG   A 553 ? 0.0937 0.1287 0.1692 0.0214  -0.0269 -0.0572 553 ARG   A NH1 
8490  N  NH2 . ARG   A 553 ? 0.1667 0.1926 0.2223 0.0193  -0.0312 -0.0702 553 ARG   A NH2 
8504  N  N   . LEU   A 554 ? 0.1551 0.1856 0.1889 0.0051  -0.0513 -0.0242 554 LEU   A N   
8505  C  CA  . LEU   A 554 ? 0.1212 0.1517 0.1677 0.0063  -0.0549 -0.0168 554 LEU   A CA  
8506  C  C   . LEU   A 554 ? 0.1405 0.1675 0.1778 0.0021  -0.0616 -0.0111 554 LEU   A C   
8507  O  O   . LEU   A 554 ? 0.1374 0.1620 0.1834 0.0028  -0.0607 -0.0053 554 LEU   A O   
8508  C  CB  . LEU   A 554 ? 0.0938 0.1280 0.1477 0.0085  -0.0491 -0.0137 554 LEU   A CB  
8509  C  CG  . LEU   A 554 ? 0.1259 0.1619 0.1818 0.0119  -0.0416 -0.0176 554 LEU   A CG  
8510  C  CD1 . LEU   A 554 ? 0.1195 0.1577 0.1798 0.0133  -0.0359 -0.0138 554 LEU   A CD1 
8511  C  CD2 . LEU   A 554 ? 0.1262 0.1585 0.1908 0.0137  -0.0401 -0.0185 554 LEU   A CD2 
8523  N  N   . LEU   A 555 ? 0.1254 0.1535 0.1518 -0.0023 -0.0647 -0.0123 555 LEU   A N   
8524  C  CA  . LEU   A 555 ? 0.1593 0.1847 0.1752 -0.0072 -0.0715 -0.0067 555 LEU   A CA  
8525  C  C   . LEU   A 555 ? 0.1823 0.2036 0.1925 -0.0100 -0.0766 -0.0093 555 LEU   A C   
8526  O  O   . LEU   A 555 ? 0.1856 0.2049 0.1968 -0.0126 -0.0805 -0.0037 555 LEU   A O   
8527  C  CB  . LEU   A 555 ? 0.1659 0.1939 0.1665 -0.0116 -0.0715 -0.0044 555 LEU   A CB  
8528  C  CG  . LEU   A 555 ? 0.1418 0.1746 0.1505 -0.0102 -0.0657 -0.0006 555 LEU   A CG  
8529  C  CD1 . LEU   A 555 ? 0.2183 0.2528 0.2025 -0.0150 -0.0644 0.0010  555 LEU   A CD1 
8530  C  CD2 . LEU   A 555 ? 0.1496 0.1791 0.1655 -0.0083 -0.0675 0.0065  555 LEU   A CD2 
8542  N  N   . GLU   A 556 ? 0.1717 0.1923 0.1795 -0.0095 -0.0767 -0.0182 556 GLU   A N   
8543  C  CA  . GLU   A 556 ? 0.1709 0.1875 0.1723 -0.0128 -0.0815 -0.0221 556 GLU   A CA  
8544  C  C   . GLU   A 556 ? 0.1731 0.1859 0.1847 -0.0098 -0.0817 -0.0253 556 GLU   A C   
8545  O  O   . GLU   A 556 ? 0.1832 0.1912 0.1927 -0.0120 -0.0864 -0.0254 556 GLU   A O   
8546  C  CB  . GLU   A 556 ? 0.2114 0.2282 0.1917 -0.0166 -0.0817 -0.0297 556 GLU   A CB  
8547  C  CG  . GLU   A 556 ? 0.2939 0.3152 0.2596 -0.0203 -0.0797 -0.0254 556 GLU   A CG  
8548  C  CD  . GLU   A 556 ? 0.4056 0.4276 0.3452 -0.0249 -0.0779 -0.0314 556 GLU   A CD  
8549  O  OE1 . GLU   A 556 ? 0.4506 0.4692 0.3846 -0.0247 -0.0776 -0.0407 556 GLU   A OE1 
8550  O  OE2 . GLU   A 556 ? 0.4179 0.4451 0.3482 -0.0288 -0.0768 -0.0269 556 GLU   A OE2 
8557  N  N   . GLU   A 557 ? 0.1959 0.2103 0.1906 -0.0269 -0.0860 -0.0134 557 GLU   A N   
8558  C  CA  . GLU   A 557 ? 0.1898 0.1977 0.1904 -0.0293 -0.0893 -0.0141 557 GLU   A CA  
8559  C  C   . GLU   A 557 ? 0.1897 0.1943 0.1922 -0.0321 -0.0884 -0.0094 557 GLU   A C   
8560  O  O   . GLU   A 557 ? 0.1670 0.1682 0.1737 -0.0321 -0.0846 -0.0058 557 GLU   A O   
8561  C  CB  . GLU   A 557 ? 0.2445 0.2441 0.2402 -0.0282 -0.0888 -0.0161 557 GLU   A CB  
8562  C  CG  . GLU   A 557 ? 0.2881 0.2907 0.2813 -0.0259 -0.0902 -0.0217 557 GLU   A CG  
8563  C  CD  . GLU   A 557 ? 0.3820 0.3766 0.3698 -0.0243 -0.0898 -0.0237 557 GLU   A CD  
8564  O  OE1 . GLU   A 557 ? 0.3659 0.3527 0.3619 -0.0249 -0.0899 -0.0209 557 GLU   A OE1 
8565  O  OE2 . GLU   A 557 ? 0.4241 0.4225 0.4092 -0.0222 -0.0898 -0.0281 557 GLU   A OE2 
8572  N  N   . PRO   A 558 ? 0.1857 0.1942 0.1969 -0.0346 -0.0922 -0.0096 558 PRO   A N   
8573  C  CA  . PRO   A 558 ? 0.1895 0.1978 0.2051 -0.0375 -0.0914 -0.0058 558 PRO   A CA  
8574  C  C   . PRO   A 558 ? 0.1956 0.1934 0.2068 -0.0395 -0.0905 -0.0034 558 PRO   A C   
8575  O  O   . PRO   A 558 ? 0.1770 0.1697 0.1898 -0.0396 -0.0932 -0.0061 558 PRO   A O   
8576  C  CB  . PRO   A 558 ? 0.2362 0.2491 0.2523 -0.0398 -0.0969 -0.0075 558 PRO   A CB  
8577  C  CG  . PRO   A 558 ? 0.2784 0.2944 0.2865 -0.0374 -0.1000 -0.0118 558 PRO   A CG  
8578  C  CD  . PRO   A 558 ? 0.2686 0.2792 0.2698 -0.0348 -0.0977 -0.0137 558 PRO   A CD  
8586  N  N   . ILE   A 559 ? 0.1542 0.1524 0.1737 -0.0410 -0.0869 0.0008  559 ILE   A N   
8587  C  CA  . ILE   A 559 ? 0.1601 0.1498 0.1773 -0.0432 -0.0868 0.0036  559 ILE   A CA  
8588  C  C   . ILE   A 559 ? 0.1711 0.1588 0.1903 -0.0468 -0.0922 0.0018  559 ILE   A C   
8589  O  O   . ILE   A 559 ? 0.1748 0.1695 0.1986 -0.0492 -0.0943 0.0011  559 ILE   A O   
8590  C  CB  . ILE   A 559 ? 0.1534 0.1451 0.1740 -0.0452 -0.0829 0.0081  559 ILE   A CB  
8591  C  CG1 . ILE   A 559 ? 0.1589 0.1483 0.1748 -0.0421 -0.0783 0.0102  559 ILE   A CG1 
8592  C  CG2 . ILE   A 559 ? 0.1672 0.1526 0.1859 -0.0491 -0.0840 0.0107  559 ILE   A CG2 
8593  C  CD1 . ILE   A 559 ? 0.1457 0.1377 0.1645 -0.0434 -0.0747 0.0135  559 ILE   A CD1 
8605  N  N   . PRO   A 560 ? 0.1785 0.1575 0.1975 -0.0468 -0.0952 0.0006  560 PRO   A N   
8606  C  CA  . PRO   A 560 ? 0.2094 0.1845 0.2269 -0.0497 -0.1012 -0.0014 560 PRO   A CA  
8607  C  C   . PRO   A 560 ? 0.2181 0.1944 0.2426 -0.0556 -0.1026 0.0018  560 PRO   A C   
8608  O  O   . PRO   A 560 ? 0.2328 0.2103 0.2578 -0.0588 -0.1071 -0.0001 560 PRO   A O   
8609  C  CB  . PRO   A 560 ? 0.2352 0.1992 0.2477 -0.0475 -0.1037 -0.0030 560 PRO   A CB  
8610  C  CG  . PRO   A 560 ? 0.2517 0.2116 0.2597 -0.0454 -0.0992 0.0006  560 PRO   A CG  
8611  C  CD  . PRO   A 560 ? 0.2171 0.1867 0.2285 -0.0437 -0.0940 0.0015  560 PRO   A CD  
8619  N  N   . ASP   A 561 ? 0.2588 0.2331 0.2803 -0.0573 -0.0988 0.0066  561 ASP   A N   
8620  C  CA  . ASP   A 561 ? 0.2875 0.2622 0.3104 -0.0636 -0.0998 0.0097  561 ASP   A CA  
8621  C  C   . ASP   A 561 ? 0.2545 0.2331 0.2800 -0.0649 -0.0942 0.0138  561 ASP   A C   
8622  O  O   . ASP   A 561 ? 0.2265 0.2029 0.2489 -0.0608 -0.0906 0.0149  561 ASP   A O   
8623  C  CB  . ASP   A 561 ? 0.2958 0.2613 0.3260 -0.0658 -0.1046 0.0107  561 ASP   A CB  
8624  C  CG  . ASP   A 561 ? 0.4607 0.4265 0.4907 -0.0733 -0.1074 0.0123  561 ASP   A CG  
8625  O  OD1 . ASP   A 561 ? 0.4621 0.4351 0.4966 -0.0758 -0.1095 0.0098  561 ASP   A OD1 
8626  O  OD2 . ASP   A 561 ? 0.6760 0.6329 0.6903 -0.0768 -0.1076 0.0162  561 ASP   A OD2 
8631  N  N   . GLY   A 562 ? 0.2497 0.2339 0.2803 -0.0708 -0.0934 0.0155  562 GLY   A N   
8632  C  CA  . GLY   A 562 ? 0.2412 0.2286 0.2716 -0.0726 -0.0882 0.0187  562 GLY   A CA  
8633  C  C   . GLY   A 562 ? 0.2302 0.2312 0.2687 -0.0727 -0.0840 0.0174  562 GLY   A C   
8634  O  O   . GLY   A 562 ? 0.2373 0.2460 0.2822 -0.0719 -0.0859 0.0144  562 GLY   A O   
8638  N  N   . PRO   A 563 ? 0.2133 0.2189 0.2561 -0.0740 -0.0789 0.0192  563 PRO   A N   
8639  C  CA  . PRO   A 563 ? 0.2358 0.2540 0.2834 -0.0740 -0.0748 0.0174  563 PRO   A CA  
8640  C  C   . PRO   A 563 ? 0.2521 0.2747 0.3012 -0.0676 -0.0747 0.0155  563 PRO   A C   
8641  O  O   . PRO   A 563 ? 0.2759 0.3099 0.3335 -0.0674 -0.0732 0.0137  563 PRO   A O   
8642  C  CB  . PRO   A 563 ? 0.2439 0.2612 0.2891 -0.0758 -0.0699 0.0196  563 PRO   A CB  
8643  C  CG  . PRO   A 563 ? 0.2829 0.2875 0.3148 -0.0792 -0.0719 0.0227  563 PRO   A CG  
8644  C  CD  . PRO   A 563 ? 0.2671 0.2626 0.2948 -0.0754 -0.0772 0.0227  563 PRO   A CD  
8652  N  N   . SER   A 564 ? 0.2351 0.2483 0.2741 -0.0626 -0.0759 0.0158  564 SER   A N   
8653  C  CA  . SER   A 564 ? 0.1756 0.1928 0.2193 -0.0571 -0.0755 0.0143  564 SER   A CA  
8654  C  C   . SER   A 564 ? 0.1892 0.2036 0.2276 -0.0555 -0.0803 0.0117  564 SER   A C   
8655  O  O   . SER   A 564 ? 0.1574 0.1715 0.1954 -0.0512 -0.0801 0.0104  564 SER   A O   
8656  C  CB  . SER   A 564 ? 0.1771 0.1867 0.2098 -0.0531 -0.0723 0.0163  564 SER   A CB  
8657  O  OG  . SER   A 564 ? 0.1718 0.1839 0.2053 -0.0545 -0.0685 0.0179  564 SER   A OG  
8663  N  N   . LYS   A 565 ? 0.2056 0.2197 0.2464 -0.0595 -0.0842 0.0105  565 LYS   A N   
8664  C  CA  . LYS   A 565 ? 0.1818 0.1942 0.2251 -0.0584 -0.0896 0.0074  565 LYS   A CA  
8665  C  C   . LYS   A 565 ? 0.1696 0.1909 0.2167 -0.0555 -0.0909 0.0049  565 LYS   A C   
8666  O  O   . LYS   A 565 ? 0.1872 0.2181 0.2392 -0.0567 -0.0904 0.0050  565 LYS   A O   
8667  C  CB  . LYS   A 565 ? 0.1977 0.2095 0.2445 -0.0637 -0.0943 0.0065  565 LYS   A CB  
8668  C  CG  . LYS   A 565 ? 0.2371 0.2443 0.2804 -0.0630 -0.1004 0.0031  565 LYS   A CG  
8669  C  CD  . LYS   A 565 ? 0.2553 0.2631 0.3044 -0.0686 -0.1056 0.0020  565 LYS   A CD  
8670  C  CE  . LYS   A 565 ? 0.2648 0.2700 0.3192 -0.0679 -0.1123 -0.0021 565 LYS   A CE  
8671  N  NZ  . LYS   A 565 ? 0.4113 0.4085 0.4547 -0.0733 -0.1175 -0.0023 565 LYS   A NZ  
8685  N  N   . GLY   A 566 ? 0.1902 0.2077 0.2292 -0.0517 -0.0926 0.0025  566 GLY   A N   
8686  C  CA  . GLY   A 566 ? 0.2114 0.2355 0.2487 -0.0491 -0.0951 0.0002  566 GLY   A CA  
8687  C  C   . GLY   A 566 ? 0.1903 0.2172 0.2267 -0.0448 -0.0913 0.0013  566 GLY   A C   
8688  O  O   . GLY   A 566 ? 0.2104 0.2417 0.2441 -0.0423 -0.0936 -0.0003 566 GLY   A O   
8692  N  N   . GLU   A 567 ? 0.1523 0.1760 0.1883 -0.0440 -0.0860 0.0042  567 GLU   A N   
8693  C  CA  . GLU   A 567 ? 0.1400 0.1660 0.1756 -0.0406 -0.0824 0.0060  567 GLU   A CA  
8694  C  C   . GLU   A 567 ? 0.1791 0.1979 0.1998 -0.0373 -0.0808 0.0052  567 GLU   A C   
8695  O  O   . GLU   A 567 ? 0.1412 0.1540 0.1643 -0.0376 -0.0807 0.0044  567 GLU   A O   
8696  C  CB  . GLU   A 567 ? 0.1428 0.1689 0.1823 -0.0415 -0.0779 0.0091  567 GLU   A CB  
8697  C  CG  . GLU   A 567 ? 0.2080 0.2418 0.2521 -0.0444 -0.0785 0.0093  567 GLU   A CG  
8698  C  CD  . GLU   A 567 ? 0.2424 0.2869 0.2942 -0.0426 -0.0804 0.0084  567 GLU   A CD  
8699  O  OE1 . GLU   A 567 ? 0.2315 0.2770 0.2833 -0.0393 -0.0783 0.0097  567 GLU   A OE1 
8700  O  OE2 . GLU   A 567 ? 0.2709 0.3225 0.3290 -0.0446 -0.0844 0.0068  567 GLU   A OE2 
8707  N  N   . VAL   A 568 ? 0.1628 0.1864 0.1860 -0.0344 -0.0799 0.0056  568 VAL   A N   
8708  C  CA  . VAL   A 568 ? 0.1445 0.1659 0.1649 -0.0317 -0.0779 0.0051  568 VAL   A CA  
8709  C  C   . VAL   A 568 ? 0.1695 0.1904 0.1837 -0.0302 -0.0741 0.0086  568 VAL   A C   
8710  O  O   . VAL   A 568 ? 0.1121 0.1380 0.1367 -0.0281 -0.0693 0.0093  568 VAL   A O   
8711  C  CB  . VAL   A 568 ? 0.1624 0.1879 0.1779 -0.0298 -0.0814 0.0016  568 VAL   A CB  
8712  C  CG1 . VAL   A 568 ? 0.2059 0.2277 0.2141 -0.0311 -0.0849 -0.0022 568 VAL   A CG1 
8713  C  CG2 . VAL   A 568 ? 0.1975 0.2299 0.2097 -0.0288 -0.0842 0.0021  568 VAL   A CG2 
8723  N  N   . HIS   A 569 ? 0.1581 0.1763 0.1745 -0.0288 -0.0712 0.0097  569 HIS   A N   
8724  C  CA  . HIS   A 569 ? 0.1685 0.1865 0.1815 -0.0276 -0.0683 0.0128  569 HIS   A CA  
8725  C  C   . HIS   A 569 ? 0.1488 0.1740 0.1623 -0.0255 -0.0706 0.0129  569 HIS   A C   
8726  O  O   . HIS   A 569 ? 0.1552 0.1824 0.1651 -0.0241 -0.0719 0.0108  569 HIS   A O   
8727  C  CB  . HIS   A 569 ? 0.1347 0.1471 0.1498 -0.0272 -0.0647 0.0145  569 HIS   A CB  
8728  C  CG  . HIS   A 569 ? 0.1245 0.1359 0.1409 -0.0268 -0.0624 0.0178  569 HIS   A CG  
8729  N  ND1 . HIS   A 569 ? 0.1107 0.1250 0.1277 -0.0256 -0.0621 0.0192  569 HIS   A ND1 
8730  C  CD2 . HIS   A 569 ? 0.1444 0.1529 0.1610 -0.0275 -0.0606 0.0201  569 HIS   A CD2 
8731  C  CE1 . HIS   A 569 ? 0.1450 0.1561 0.1593 -0.0255 -0.0602 0.0220  569 HIS   A CE1 
8732  N  NE2 . HIS   A 569 ? 0.1242 0.1336 0.1456 -0.0267 -0.0592 0.0223  569 HIS   A NE2 
8740  N  N   A ARG   A 570 ? 0.1189 0.1483 0.1405 -0.0248 -0.0707 0.0153  570 ARG   A N   
8741  N  N   B ARG   A 570 ? 0.1189 0.1483 0.1405 -0.0248 -0.0707 0.0153  570 ARG   A N   
8742  C  CA  A ARG   A 570 ? 0.1524 0.1867 0.1693 -0.0226 -0.0738 0.0162  570 ARG   A CA  
8743  C  CA  B ARG   A 570 ? 0.1524 0.1867 0.1693 -0.0226 -0.0738 0.0163  570 ARG   A CA  
8744  C  C   A ARG   A 570 ? 0.1564 0.1887 0.1711 -0.0214 -0.0712 0.0194  570 ARG   A C   
8745  C  C   B ARG   A 570 ? 0.1564 0.1887 0.1711 -0.0214 -0.0712 0.0194  570 ARG   A C   
8746  O  O   A ARG   A 570 ? 0.1653 0.2000 0.1821 -0.0200 -0.0725 0.0220  570 ARG   A O   
8747  O  O   B ARG   A 570 ? 0.1653 0.2000 0.1821 -0.0200 -0.0725 0.0219  570 ARG   A O   
8748  C  CB  A ARG   A 570 ? 0.1714 0.2116 0.1952 -0.0222 -0.0767 0.0167  570 ARG   A CB  
8749  C  CB  B ARG   A 570 ? 0.1714 0.2116 0.1952 -0.0222 -0.0767 0.0167  570 ARG   A CB  
8750  C  CG  A ARG   A 570 ? 0.1917 0.2347 0.2198 -0.0242 -0.0790 0.0141  570 ARG   A CG  
8751  C  CG  B ARG   A 570 ? 0.1917 0.2347 0.2198 -0.0243 -0.0791 0.0141  570 ARG   A CG  
8752  C  CD  A ARG   A 570 ? 0.2174 0.2656 0.2480 -0.0239 -0.0844 0.0116  570 ARG   A CD  
8753  C  CD  B ARG   A 570 ? 0.2174 0.2657 0.2480 -0.0239 -0.0843 0.0115  570 ARG   A CD  
8754  N  NE  A ARG   A 570 ? 0.3534 0.4044 0.3711 -0.0212 -0.0884 0.0127  570 ARG   A NE  
8755  N  NE  B ARG   A 570 ? 0.3534 0.4043 0.3711 -0.0212 -0.0884 0.0127  570 ARG   A NE  
8756  C  CZ  A ARG   A 570 ? 0.3536 0.4125 0.3865 -0.0204 -0.0917 0.0139  570 ARG   A CZ  
8757  C  CZ  B ARG   A 570 ? 0.3536 0.4125 0.3865 -0.0204 -0.0917 0.0139  570 ARG   A CZ  
8758  N  NH1 A ARG   A 570 ? 0.3250 0.3872 0.3667 -0.0223 -0.0916 0.0131  570 ARG   A NH1 
8759  N  NH1 B ARG   A 570 ? 0.3250 0.3872 0.3667 -0.0223 -0.0916 0.0131  570 ARG   A NH1 
8760  N  NH2 A ARG   A 570 ? 0.4185 0.4794 0.4444 -0.0175 -0.0951 0.0159  570 ARG   A NH2 
8761  N  NH2 B ARG   A 570 ? 0.4185 0.4793 0.4444 -0.0175 -0.0951 0.0159  570 ARG   A NH2 
8788  N  N   . LEU   A 571 ? 0.1450 0.1745 0.1570 -0.0214 -0.0690 0.0190  571 LEU   A N   
8789  C  CA  . LEU   A 571 ? 0.1489 0.1763 0.1576 -0.0210 -0.0668 0.0222  571 LEU   A CA  
8790  C  C   . LEU   A 571 ? 0.1732 0.2055 0.1769 -0.0188 -0.0698 0.0241  571 LEU   A C   
8791  O  O   . LEU   A 571 ? 0.1649 0.1963 0.1707 -0.0184 -0.0690 0.0279  571 LEU   A O   
8792  C  CB  . LEU   A 571 ? 0.1316 0.1571 0.1410 -0.0214 -0.0642 0.0209  571 LEU   A CB  
8793  C  CG  . LEU   A 571 ? 0.1886 0.2102 0.1903 -0.0218 -0.0615 0.0240  571 LEU   A CG  
8794  C  CD1 . LEU   A 571 ? 0.1601 0.1767 0.1726 -0.0235 -0.0593 0.0265  571 LEU   A CD1 
8795  C  CD2 . LEU   A 571 ? 0.1778 0.2005 0.1823 -0.0216 -0.0601 0.0220  571 LEU   A CD2 
8808  N  N   . ASP   A 572 ? 0.1849 0.2221 0.1840 -0.0171 -0.0735 0.0217  572 ASP   A N   
8809  C  CA  . ASP   A 572 ? 0.1816 0.2235 0.1770 -0.0144 -0.0775 0.0234  572 ASP   A CA  
8810  C  C   . ASP   A 572 ? 0.1914 0.2329 0.1892 -0.0139 -0.0791 0.0276  572 ASP   A C   
8811  O  O   . ASP   A 572 ? 0.2138 0.2555 0.2063 -0.0121 -0.0806 0.0314  572 ASP   A O   
8812  C  CB  . ASP   A 572 ? 0.2086 0.2548 0.1969 -0.0129 -0.0821 0.0196  572 ASP   A CB  
8813  C  CG  . ASP   A 572 ? 0.2462 0.2953 0.2468 -0.0143 -0.0849 0.0173  572 ASP   A CG  
8814  O  OD1 . ASP   A 572 ? 0.3034 0.3477 0.3028 -0.0164 -0.0820 0.0178  572 ASP   A OD1 
8815  O  OD2 . ASP   A 572 ? 0.3624 0.4130 0.3476 -0.0132 -0.0897 0.0151  572 ASP   A OD2 
8820  N  N   . VAL   A 573 ? 0.1783 0.2199 0.1861 -0.0150 -0.0791 0.0270  573 VAL   A N   
8821  C  CA  . VAL   A 573 ? 0.1888 0.2320 0.2047 -0.0136 -0.0811 0.0299  573 VAL   A CA  
8822  C  C   . VAL   A 573 ? 0.1914 0.2291 0.2094 -0.0147 -0.0769 0.0324  573 VAL   A C   
8823  O  O   . VAL   A 573 ? 0.2121 0.2491 0.2317 -0.0134 -0.0782 0.0356  573 VAL   A O   
8824  C  CB  . VAL   A 573 ? 0.2533 0.3011 0.2745 -0.0134 -0.0845 0.0275  573 VAL   A CB  
8825  C  CG1 . VAL   A 573 ? 0.3438 0.3925 0.3680 -0.0120 -0.0857 0.0296  573 VAL   A CG1 
8826  C  CG2 . VAL   A 573 ? 0.2602 0.3125 0.2750 -0.0123 -0.0899 0.0256  573 VAL   A CG2 
8836  N  N   . LEU   A 574 ? 0.1690 0.2026 0.1896 -0.0173 -0.0725 0.0307  574 LEU   A N   
8837  C  CA  . LEU   A 574 ? 0.1616 0.1898 0.1840 -0.0182 -0.0690 0.0322  574 LEU   A CA  
8838  C  C   . LEU   A 574 ? 0.1284 0.1537 0.1541 -0.0190 -0.0672 0.0353  574 LEU   A C   
8839  O  O   . LEU   A 574 ? 0.1541 0.1753 0.1781 -0.0189 -0.0666 0.0377  574 LEU   A O   
8840  C  CB  . LEU   A 574 ? 0.1521 0.1769 0.1777 -0.0204 -0.0660 0.0296  574 LEU   A CB  
8841  C  CG  . LEU   A 574 ? 0.1246 0.1548 0.1592 -0.0202 -0.0673 0.0271  574 LEU   A CG  
8842  C  CD1 . LEU   A 574 ? 0.1466 0.1717 0.1757 -0.0226 -0.0645 0.0251  574 LEU   A CD1 
8843  C  CD2 . LEU   A 574 ? 0.1521 0.1850 0.1888 -0.0185 -0.0686 0.0279  574 LEU   A CD2 
8855  N  N   . LEU   A 575 ? 0.1544 0.1790 0.1694 -0.0195 -0.0663 0.0354  575 LEU   A N   
8856  C  CA  . LEU   A 575 ? 0.1644 0.1865 0.1783 -0.0208 -0.0643 0.0383  575 LEU   A CA  
8857  C  C   . LEU   A 575 ? 0.1507 0.1744 0.1674 -0.0195 -0.0668 0.0432  575 LEU   A C   
8858  O  O   . LEU   A 575 ? 0.1539 0.1727 0.1710 -0.0208 -0.0655 0.0457  575 LEU   A O   
8859  C  CB  . LEU   A 575 ? 0.1901 0.2141 0.1960 -0.0209 -0.0633 0.0370  575 LEU   A CB  
8860  C  CG  . LEU   A 575 ? 0.1648 0.1883 0.1725 -0.0224 -0.0611 0.0398  575 LEU   A CG  
8861  C  CD1 . LEU   A 575 ? 0.1497 0.1668 0.1644 -0.0249 -0.0585 0.0406  575 LEU   A CD1 
8862  C  CD2 . LEU   A 575 ? 0.1577 0.1854 0.1606 -0.0216 -0.0603 0.0376  575 LEU   A CD2 
8874  N  N   . PRO   A 576 ? 0.2001 0.2265 0.2056 -0.0169 -0.0705 0.0444  576 PRO   A N   
8875  C  CA  . PRO   A 576 ? 0.1886 0.2151 0.1964 -0.0154 -0.0733 0.0494  576 PRO   A CA  
8876  C  C   . PRO   A 576 ? 0.1755 0.1993 0.1942 -0.0148 -0.0742 0.0505  576 PRO   A C   
8877  O  O   . PRO   A 576 ? 0.1897 0.2094 0.2069 -0.0150 -0.0745 0.0545  576 PRO   A O   
8878  C  CB  . PRO   A 576 ? 0.1959 0.2268 0.1967 -0.0123 -0.0780 0.0495  576 PRO   A CB  
8879  C  CG  . PRO   A 576 ? 0.2125 0.2460 0.2069 -0.0128 -0.0769 0.0448  576 PRO   A CG  
8880  C  CD  . PRO   A 576 ? 0.1963 0.2282 0.2005 -0.0153 -0.0732 0.0414  576 PRO   A CD  
8888  N  N   . GLU   A 577 ? 0.1973 0.2219 0.2185 -0.0139 -0.0746 0.0469  577 GLU   A N   
8889  C  CA  . GLU   A 577 ? 0.1997 0.2226 0.2290 -0.0126 -0.0752 0.0468  577 GLU   A CA  
8890  C  C   . GLU   A 577 ? 0.1718 0.1888 0.2057 -0.0151 -0.0713 0.0467  577 GLU   A C   
8891  O  O   . GLU   A 577 ? 0.1844 0.1980 0.2218 -0.0140 -0.0725 0.0485  577 GLU   A O   
8892  C  CB  . GLU   A 577 ? 0.2097 0.2381 0.2481 -0.0112 -0.0762 0.0429  577 GLU   A CB  
8893  C  CG  . GLU   A 577 ? 0.2764 0.3057 0.3252 -0.0087 -0.0772 0.0426  577 GLU   A CG  
8894  C  CD  . GLU   A 577 ? 0.4395 0.4686 0.4864 -0.0049 -0.0819 0.0460  577 GLU   A CD  
8895  O  OE1 . GLU   A 577 ? 0.5086 0.5379 0.5470 -0.0042 -0.0851 0.0488  577 GLU   A OE1 
8896  O  OE2 . GLU   A 577 ? 0.5256 0.5534 0.5759 -0.0023 -0.0826 0.0458  577 GLU   A OE2 
8903  N  N   . TYR   A 578 ? 0.1426 0.1579 0.1763 -0.0182 -0.0677 0.0451  578 TYR   A N   
8904  C  CA  . TYR   A 578 ? 0.1704 0.1783 0.2016 -0.0207 -0.0649 0.0449  578 TYR   A CA  
8905  C  C   . TYR   A 578 ? 0.1635 0.1695 0.1972 -0.0217 -0.0657 0.0493  578 TYR   A C   
8906  O  O   . TYR   A 578 ? 0.1589 0.1603 0.1969 -0.0222 -0.0663 0.0501  578 TYR   A O   
8907  C  CB  . TYR   A 578 ? 0.1657 0.1717 0.1957 -0.0233 -0.0615 0.0425  578 TYR   A CB  
8908  C  CG  . TYR   A 578 ? 0.1420 0.1409 0.1755 -0.0258 -0.0596 0.0425  578 TYR   A CG  
8909  C  CD1 . TYR   A 578 ? 0.1339 0.1281 0.1706 -0.0254 -0.0589 0.0405  578 TYR   A CD1 
8910  C  CD2 . TYR   A 578 ? 0.1431 0.1403 0.1763 -0.0282 -0.0585 0.0448  578 TYR   A CD2 
8911  C  CE1 . TYR   A 578 ? 0.1536 0.1397 0.1892 -0.0274 -0.0579 0.0404  578 TYR   A CE1 
8912  C  CE2 . TYR   A 578 ? 0.1632 0.1529 0.1971 -0.0307 -0.0574 0.0445  578 TYR   A CE2 
8913  C  CZ  . TYR   A 578 ? 0.1617 0.1453 0.1976 -0.0302 -0.0575 0.0424  578 TYR   A CZ  
8914  O  OH  . TYR   A 578 ? 0.1615 0.1408 0.1974 -0.0295 -0.0557 0.0401  578 TYR   A OH  
8924  N  N   . TYR   A 579 ? 0.1664 0.1758 0.1955 -0.0222 -0.0661 0.0521  579 TYR   A N   
8925  C  CA  . TYR   A 579 ? 0.1815 0.1894 0.2087 -0.0231 -0.0671 0.0572  579 TYR   A CA  
8926  C  C   . TYR   A 579 ? 0.1983 0.2035 0.2271 -0.0206 -0.0708 0.0598  579 TYR   A C   
8927  O  O   . TYR   A 579 ? 0.1849 0.1863 0.2203 -0.0215 -0.0715 0.0625  579 TYR   A O   
8928  C  CB  . TYR   A 579 ? 0.1657 0.1788 0.1866 -0.0230 -0.0671 0.0600  579 TYR   A CB  
8929  C  CG  . TYR   A 579 ? 0.1627 0.1788 0.1809 -0.0248 -0.0637 0.0579  579 TYR   A CG  
8930  C  CD1 . TYR   A 579 ? 0.1604 0.1735 0.1832 -0.0275 -0.0610 0.0554  579 TYR   A CD1 
8931  C  CD2 . TYR   A 579 ? 0.1860 0.2068 0.1936 -0.0232 -0.0640 0.0584  579 TYR   A CD2 
8932  C  CE1 . TYR   A 579 ? 0.1709 0.1861 0.1902 -0.0283 -0.0586 0.0534  579 TYR   A CE1 
8933  C  CE2 . TYR   A 579 ? 0.1931 0.2168 0.1975 -0.0239 -0.0613 0.0558  579 TYR   A CE2 
8934  C  CZ  . TYR   A 579 ? 0.1677 0.1898 0.1819 -0.0265 -0.0590 0.0534  579 TYR   A CZ  
8935  O  OH  . TYR   A 579 ? 0.1768 0.2016 0.1872 -0.0270 -0.0574 0.0513  579 TYR   A OH  
8945  N  N   . SER   A 580 ? 0.1819 0.1907 0.2132 -0.0170 -0.0737 0.0593  580 SER   A N   
8946  C  CA  . SER   A 580 ? 0.1894 0.1962 0.2230 -0.0136 -0.0778 0.0618  580 SER   A CA  
8947  C  C   . SER   A 580 ? 0.1855 0.1872 0.2250 -0.0128 -0.0777 0.0598  580 SER   A C   
8948  O  O   . SER   A 580 ? 0.1578 0.1552 0.2030 -0.0118 -0.0799 0.0626  580 SER   A O   
8949  C  CB  . SER   A 580 ? 0.2157 0.2275 0.2481 -0.0098 -0.0814 0.0613  580 SER   A CB  
8950  O  OG  . SER   A 580 ? 0.2649 0.2743 0.2972 -0.0060 -0.0860 0.0638  580 SER   A OG  
8956  N  N   . VAL   A 581 ? 0.1785 0.1818 0.2243 -0.0130 -0.0754 0.0546  581 VAL   A N   
8957  C  CA  . VAL   A 581 ? 0.1959 0.1946 0.2440 -0.0115 -0.0751 0.0521  581 VAL   A CA  
8958  C  C   . VAL   A 581 ? 0.1754 0.1679 0.2278 -0.0151 -0.0738 0.0526  581 VAL   A C   
8959  O  O   . VAL   A 581 ? 0.1696 0.1573 0.2258 -0.0135 -0.0751 0.0517  581 VAL   A O   
8960  C  CB  . VAL   A 581 ? 0.1830 0.1865 0.2393 -0.0106 -0.0731 0.0469  581 VAL   A CB  
8961  C  CG1 . VAL   A 581 ? 0.2339 0.2440 0.2862 -0.0070 -0.0753 0.0462  581 VAL   A CG1 
8962  C  CG2 . VAL   A 581 ? 0.1859 0.1872 0.2350 -0.0149 -0.0691 0.0449  581 VAL   A CG2 
8972  N  N   . ARG   A 582 ? 0.1781 0.1700 0.2259 -0.0195 -0.0715 0.0538  582 ARG   A N   
8973  C  CA  . ARG   A 582 ? 0.1698 0.1570 0.2194 -0.0232 -0.0710 0.0548  582 ARG   A CA  
8974  C  C   . ARG   A 582 ? 0.1727 0.1581 0.2250 -0.0233 -0.0741 0.0600  582 ARG   A C   
8975  O  O   . ARG   A 582 ? 0.1558 0.1376 0.2117 -0.0258 -0.0749 0.0607  582 ARG   A O   
8976  C  CB  . ARG   A 582 ? 0.1507 0.1400 0.1995 -0.0274 -0.0678 0.0543  582 ARG   A CB  
8977  C  CG  . ARG   A 582 ? 0.1584 0.1454 0.2041 -0.0284 -0.0649 0.0497  582 ARG   A CG  
8978  C  CD  . ARG   A 582 ? 0.1497 0.1336 0.1983 -0.0327 -0.0634 0.0489  582 ARG   A CD  
8979  N  NE  . ARG   A 582 ? 0.1639 0.1427 0.2125 -0.0325 -0.0645 0.0468  582 ARG   A NE  
8980  C  CZ  . ARG   A 582 ? 0.1433 0.1194 0.1944 -0.0298 -0.0625 0.0418  582 ARG   A CZ  
8981  N  NH1 . ARG   A 582 ? 0.1848 0.1590 0.2259 -0.0282 -0.0595 0.0388  582 ARG   A NH1 
8982  N  NH2 . ARG   A 582 ? 0.1500 0.1224 0.1994 -0.0290 -0.0644 0.0401  582 ARG   A NH2 
8996  N  N   . GLY   A 583 ? 0.2084 0.1953 0.2552 -0.0205 -0.0763 0.0640  583 GLY   A N   
8997  C  CA  . GLY   A 583 ? 0.2010 0.1859 0.2499 -0.0206 -0.0789 0.0701  583 GLY   A CA  
8998  C  C   . GLY   A 583 ? 0.2206 0.2078 0.2614 -0.0243 -0.0768 0.0742  583 GLY   A C   
8999  O  O   . GLY   A 583 ? 0.1978 0.1830 0.2437 -0.0262 -0.0779 0.0789  583 GLY   A O   
9003  N  N   . TRP   A 584 ? 0.2032 0.1967 0.2413 -0.0251 -0.0739 0.0724  584 TRP   A N   
9004  C  CA  . TRP   A 584 ? 0.1680 0.1669 0.2059 -0.0281 -0.0718 0.0761  584 TRP   A CA  
9005  C  C   . TRP   A 584 ? 0.1991 0.2000 0.2218 -0.0254 -0.0729 0.0800  584 TRP   A C   
9006  O  O   . TRP   A 584 ? 0.2105 0.2117 0.2318 -0.0213 -0.0750 0.0778  584 TRP   A O   
9007  C  CB  . TRP   A 584 ? 0.1771 0.1788 0.2135 -0.0306 -0.0682 0.0717  584 TRP   A CB  
9008  C  CG  . TRP   A 584 ? 0.1854 0.1831 0.2283 -0.0333 -0.0676 0.0679  584 TRP   A CG  
9009  C  CD1 . TRP   A 584 ? 0.1664 0.1592 0.2188 -0.0339 -0.0702 0.0678  584 TRP   A CD1 
9010  C  CD2 . TRP   A 584 ? 0.1805 0.1787 0.2260 -0.0359 -0.0648 0.0636  584 TRP   A CD2 
9011  N  NE1 . TRP   A 584 ? 0.1846 0.1745 0.2387 -0.0366 -0.0695 0.0636  584 TRP   A NE1 
9012  C  CE2 . TRP   A 584 ? 0.1682 0.1615 0.2223 -0.0379 -0.0663 0.0612  584 TRP   A CE2 
9013  C  CE3 . TRP   A 584 ? 0.1689 0.1705 0.2108 -0.0358 -0.0618 0.0614  584 TRP   A CE3 
9014  C  CZ2 . TRP   A 584 ? 0.1588 0.1499 0.2134 -0.0378 -0.0633 0.0560  584 TRP   A CZ2 
9015  C  CZ3 . TRP   A 584 ? 0.1464 0.1455 0.1941 -0.0378 -0.0599 0.0576  584 TRP   A CZ3 
9016  C  CH2 . TRP   A 584 ? 0.1897 0.1817 0.2342 -0.0373 -0.0598 0.0546  584 TRP   A CH2 
9027  N  N   . SER   A 585 ? 0.1836 0.1885 0.2045 -0.0280 -0.0718 0.0856  585 SER   A N   
9028  C  CA  . SER   A 585 ? 0.2259 0.2318 0.2281 -0.0260 -0.0729 0.0897  585 SER   A CA  
9029  C  C   . SER   A 585 ? 0.2024 0.2144 0.2029 -0.0237 -0.0718 0.0834  585 SER   A C   
9030  O  O   . SER   A 585 ? 0.1881 0.2019 0.1952 -0.0242 -0.0696 0.0768  585 SER   A O   
9031  C  CB  . SER   A 585 ? 0.2139 0.2220 0.2134 -0.0298 -0.0711 0.0977  585 SER   A CB  
9032  O  OG  . SER   A 585 ? 0.1801 0.1957 0.1809 -0.0320 -0.0676 0.0965  585 SER   A OG  
9038  N  N   . LYS   A 586 ? 0.1935 0.2081 0.1841 -0.0212 -0.0736 0.0853  586 LYS   A N   
9039  C  CA  . LYS   A 586 ? 0.2301 0.2492 0.2114 -0.0190 -0.0733 0.0796  586 LYS   A CA  
9040  C  C   . LYS   A 586 ? 0.2210 0.2460 0.2070 -0.0225 -0.0693 0.0790  586 LYS   A C   
9041  O  O   . LYS   A 586 ? 0.2832 0.3097 0.2607 -0.0214 -0.0684 0.0722  586 LYS   A O   
9042  C  CB  . LYS   A 586 ? 0.2709 0.2897 0.2380 -0.0155 -0.0772 0.0816  586 LYS   A CB  
9043  C  CG  . LYS   A 586 ? 0.2699 0.2884 0.2456 -0.0110 -0.0818 0.0798  586 LYS   A CG  
9044  C  CD  . LYS   A 586 ? 0.3872 0.4051 0.3425 -0.0072 -0.0862 0.0801  586 LYS   A CD  
9045  C  CE  . LYS   A 586 ? 0.4358 0.4502 0.3905 -0.0047 -0.0915 0.0863  586 LYS   A CE  
9046  N  NZ  . LYS   A 586 ? 0.5238 0.5376 0.4578 -0.0017 -0.0956 0.0880  586 LYS   A NZ  
9060  N  N   . GLU   A 587 ? 0.2495 0.2739 0.2295 -0.0268 -0.0670 0.0860  587 GLU   A N   
9061  C  CA  . GLU   A 587 ? 0.2539 0.2848 0.2392 -0.0303 -0.0635 0.0865  587 GLU   A CA  
9062  C  C   . GLU   A 587 ? 0.2415 0.2700 0.2356 -0.0329 -0.0623 0.0830  587 GLU   A C   
9063  O  O   . GLU   A 587 ? 0.1909 0.2257 0.1973 -0.0362 -0.0602 0.0847  587 GLU   A O   
9064  C  CB  . GLU   A 587 ? 0.3044 0.3380 0.2787 -0.0338 -0.0609 0.0963  587 GLU   A CB  
9065  C  CG  . GLU   A 587 ? 0.3417 0.3758 0.2997 -0.0319 -0.0610 0.1001  587 GLU   A CG  
9066  C  CD  . GLU   A 587 ? 0.4175 0.4417 0.3598 -0.0283 -0.0655 0.1017  587 GLU   A CD  
9067  O  OE1 . GLU   A 587 ? 0.3342 0.3554 0.2960 -0.0292 -0.0668 0.1052  587 GLU   A OE1 
9068  O  OE2 . GLU   A 587 ? 0.4184 0.4433 0.3561 -0.0246 -0.0684 0.0993  587 GLU   A OE2 
9075  N  N   . GLY   A 588 ? 0.1783 0.2025 0.1886 -0.0312 -0.0637 0.0787  588 GLY   A N   
9076  C  CA  . GLY   A 588 ? 0.1841 0.2045 0.2027 -0.0333 -0.0625 0.0748  588 GLY   A CA  
9077  C  C   . GLY   A 588 ? 0.1885 0.2076 0.2151 -0.0376 -0.0630 0.0803  588 GLY   A C   
9078  O  O   . GLY   A 588 ? 0.1861 0.2048 0.2227 -0.0402 -0.0623 0.0780  588 GLY   A O   
9082  N  N   . ILE   A 589 ? 0.1736 0.1920 0.1999 -0.0380 -0.0644 0.0876  589 ILE   A N   
9083  C  CA  . ILE   A 589 ? 0.1745 0.1914 0.2066 -0.0417 -0.0650 0.0935  589 ILE   A CA  
9084  C  C   . ILE   A 589 ? 0.1545 0.1640 0.1962 -0.0402 -0.0681 0.0917  589 ILE   A C   
9085  O  O   . ILE   A 589 ? 0.1858 0.1904 0.2165 -0.0370 -0.0698 0.0933  589 ILE   A O   
9086  C  CB  . ILE   A 589 ? 0.1783 0.1992 0.2071 -0.0436 -0.0631 0.1034  589 ILE   A CB  
9087  C  CG1 . ILE   A 589 ? 0.1869 0.2160 0.2068 -0.0443 -0.0595 0.1049  589 ILE   A CG1 
9088  C  CG2 . ILE   A 589 ? 0.2252 0.2440 0.2581 -0.0473 -0.0627 0.1092  589 ILE   A CG2 
9089  C  CD1 . ILE   A 589 ? 0.2245 0.2595 0.2501 -0.0469 -0.0578 0.1032  589 ILE   A CD1 
9101  N  N   . PRO   A 590 ? 0.1698 0.1758 0.2201 -0.0420 -0.0694 0.0883  590 PRO   A N   
9102  C  CA  . PRO   A 590 ? 0.1974 0.1952 0.2500 -0.0404 -0.0725 0.0870  590 PRO   A CA  
9103  C  C   . PRO   A 590 ? 0.2093 0.2028 0.2572 -0.0400 -0.0744 0.0949  590 PRO   A C   
9104  O  O   . PRO   A 590 ? 0.2080 0.2043 0.2579 -0.0430 -0.0734 0.1018  590 PRO   A O   
9105  C  CB  . PRO   A 590 ? 0.1957 0.1932 0.2585 -0.0433 -0.0740 0.0838  590 PRO   A CB  
9106  C  CG  . PRO   A 590 ? 0.1751 0.1791 0.2413 -0.0452 -0.0715 0.0803  590 PRO   A CG  
9107  C  CD  . PRO   A 590 ? 0.1731 0.1830 0.2310 -0.0452 -0.0687 0.0855  590 PRO   A CD  
9115  N  N   . THR   A 591 ? 0.1849 0.1731 0.2349 -0.0363 -0.0770 0.0946  591 THR   A N   
9116  C  CA  . THR   A 591 ? 0.2329 0.2140 0.2716 -0.0355 -0.0796 0.1022  591 THR   A CA  
9117  C  C   . THR   A 591 ? 0.2181 0.1935 0.2693 -0.0375 -0.0821 0.1049  591 THR   A C   
9118  O  O   . THR   A 591 ? 0.2228 0.1969 0.2806 -0.0380 -0.0830 0.0993  591 THR   A O   
9119  C  CB  . THR   A 591 ? 0.2181 0.1963 0.2576 -0.0301 -0.0824 0.1010  591 THR   A CB  
9120  O  OG1 . THR   A 591 ? 0.2192 0.1923 0.2631 -0.0276 -0.0846 0.0951  591 THR   A OG1 
9121  C  CG2 . THR   A 591 ? 0.2570 0.2404 0.2843 -0.0274 -0.0809 0.0982  591 THR   A CG2 
9129  N  N   . GLU   A 592 ? 0.2273 0.1969 0.2739 -0.0386 -0.0836 0.1132  592 GLU   A N   
9130  C  CA  . GLU   A 592 ? 0.2358 0.1977 0.2888 -0.0401 -0.0868 0.1165  592 GLU   A CA  
9131  C  C   . GLU   A 592 ? 0.2229 0.1779 0.2821 -0.0362 -0.0908 0.1099  592 GLU   A C   
9132  O  O   . GLU   A 592 ? 0.2070 0.1612 0.2732 -0.0372 -0.0906 0.1033  592 GLU   A O   
9133  C  CB  . GLU   A 592 ? 0.2686 0.2242 0.3150 -0.0417 -0.0876 0.1269  592 GLU   A CB  
9134  C  CG  . GLU   A 592 ? 0.2984 0.2425 0.3460 -0.0423 -0.0919 0.1305  592 GLU   A CG  
9135  C  CD  . GLU   A 592 ? 0.2674 0.2101 0.3131 -0.0435 -0.0896 0.1358  592 GLU   A CD  
9136  O  OE1 . GLU   A 592 ? 0.2727 0.2197 0.3107 -0.0472 -0.0849 0.1413  592 GLU   A OE1 
9137  O  OE2 . GLU   A 592 ? 0.2817 0.2141 0.3228 -0.0411 -0.0937 0.1378  592 GLU   A OE2 
9144  N  N   . GLU   A 593 ? 0.2475 0.2000 0.3009 -0.0313 -0.0925 0.1077  593 GLU   A N   
9145  C  CA  . GLU   A 593 ? 0.2602 0.2065 0.3177 -0.0270 -0.0958 0.1018  593 GLU   A CA  
9146  C  C   . GLU   A 593 ? 0.2353 0.1851 0.2985 -0.0274 -0.0939 0.0930  593 GLU   A C   
9147  O  O   . GLU   A 593 ? 0.2304 0.1748 0.3001 -0.0263 -0.0961 0.0890  593 GLU   A O   
9148  C  CB  . GLU   A 593 ? 0.2790 0.2247 0.3355 -0.0211 -0.0979 0.1017  593 GLU   A CB  
9149  C  CG  . GLU   A 593 ? 0.3530 0.2954 0.3962 -0.0201 -0.1000 0.1096  593 GLU   A CG  
9150  C  CD  . GLU   A 593 ? 0.3684 0.3124 0.4109 -0.0139 -0.1026 0.1084  593 GLU   A CD  
9151  O  OE1 . GLU   A 593 ? 0.3883 0.3265 0.4348 -0.0095 -0.1067 0.1064  593 GLU   A OE1 
9152  O  OE2 . GLU   A 593 ? 0.3673 0.3180 0.4025 -0.0135 -0.1009 0.1089  593 GLU   A OE2 
9159  N  N   . THR   A 594 ? 0.1982 0.1580 0.2638 -0.0287 -0.0898 0.0894  594 THR   A N   
9160  C  CA  . THR   A 594 ? 0.2325 0.1936 0.2940 -0.0293 -0.0878 0.0817  594 THR   A CA  
9161  C  C   . THR   A 594 ? 0.1953 0.1568 0.2694 -0.0334 -0.0889 0.0809  594 THR   A C   
9162  O  O   . THR   A 594 ? 0.1837 0.1412 0.2600 -0.0327 -0.0906 0.0754  594 THR   A O   
9163  C  CB  . THR   A 594 ? 0.2153 0.1859 0.2771 -0.0300 -0.0836 0.0787  594 THR   A CB  
9164  O  OG1 . THR   A 594 ? 0.2062 0.1779 0.2630 -0.0255 -0.0835 0.0788  594 THR   A OG1 
9165  C  CG2 . THR   A 594 ? 0.2078 0.1800 0.2729 -0.0311 -0.0818 0.0713  594 THR   A CG2 
9173  N  N   . LEU   A 595 ? 0.2116 0.1758 0.2834 -0.0373 -0.0882 0.0868  595 LEU   A N   
9174  C  CA  . LEU   A 595 ? 0.1890 0.1540 0.2705 -0.0407 -0.0899 0.0873  595 LEU   A CA  
9175  C  C   . LEU   A 595 ? 0.1993 0.1541 0.2846 -0.0394 -0.0945 0.0871  595 LEU   A C   
9176  O  O   . LEU   A 595 ? 0.2314 0.1835 0.3184 -0.0399 -0.0969 0.0823  595 LEU   A O   
9177  C  CB  . LEU   A 595 ? 0.1806 0.1516 0.2630 -0.0444 -0.0877 0.0946  595 LEU   A CB  
9178  C  CG  . LEU   A 595 ? 0.1940 0.1755 0.2751 -0.0457 -0.0834 0.0946  595 LEU   A CG  
9179  C  CD1 . LEU   A 595 ? 0.2422 0.2279 0.3188 -0.0490 -0.0807 0.1032  595 LEU   A CD1 
9180  C  CD2 . LEU   A 595 ? 0.1965 0.1822 0.2805 -0.0461 -0.0836 0.0867  595 LEU   A CD2 
9192  N  N   . LYS   A 596 ? 0.2061 0.1536 0.2902 -0.0378 -0.0965 0.0919  596 LYS   A N   
9193  C  CA  . LYS   A 596 ? 0.2638 0.1988 0.3441 -0.0360 -0.1013 0.0917  596 LYS   A CA  
9194  C  C   . LYS   A 596 ? 0.2342 0.1667 0.3217 -0.0320 -0.1030 0.0830  596 LYS   A C   
9195  O  O   . LYS   A 596 ? 0.2696 0.1953 0.3566 -0.0319 -0.1063 0.0792  596 LYS   A O   
9196  C  CB  . LYS   A 596 ? 0.2715 0.2002 0.3546 -0.0345 -0.1035 0.0991  596 LYS   A CB  
9197  C  CG  . LYS   A 596 ? 0.3181 0.2483 0.3971 -0.0386 -0.1022 0.1089  596 LYS   A CG  
9198  C  CD  . LYS   A 596 ? 0.3738 0.2984 0.4463 -0.0362 -0.1037 0.1155  596 LYS   A CD  
9199  C  CE  . LYS   A 596 ? 0.4374 0.3522 0.5117 -0.0387 -0.1072 0.1236  596 LYS   A CE  
9200  N  NZ  . LYS   A 596 ? 0.5314 0.4485 0.6005 -0.0449 -0.1043 0.1307  596 LYS   A NZ  
9214  N  N   . LYS   A 597 ? 0.2168 0.1519 0.2991 -0.0284 -0.1006 0.0793  597 LYS   A N   
9215  C  CA  . LYS   A 597 ? 0.2238 0.1555 0.3064 -0.0239 -0.1012 0.0717  597 LYS   A CA  
9216  C  C   . LYS   A 597 ? 0.2401 0.1732 0.3195 -0.0261 -0.1006 0.0655  597 LYS   A C   
9217  O  O   . LYS   A 597 ? 0.2521 0.1789 0.3345 -0.0233 -0.1030 0.0604  597 LYS   A O   
9218  C  CB  . LYS   A 597 ? 0.2494 0.1857 0.3288 -0.0201 -0.0984 0.0698  597 LYS   A CB  
9219  C  CG  . LYS   A 597 ? 0.3106 0.2447 0.3899 -0.0155 -0.0984 0.0630  597 LYS   A CG  
9220  C  CD  . LYS   A 597 ? 0.3973 0.3372 0.4674 -0.0130 -0.0951 0.0611  597 LYS   A CD  
9221  C  CE  . LYS   A 597 ? 0.3664 0.3177 0.4435 -0.0175 -0.0908 0.0618  597 LYS   A CE  
9222  N  NZ  . LYS   A 597 ? 0.4345 0.3901 0.5012 -0.0152 -0.0876 0.0587  597 LYS   A NZ  
9236  N  N   . LEU   A 598 ? 0.1838 0.1280 0.2728 -0.0303 -0.0981 0.0657  598 LEU   A N   
9237  C  CA  . LEU   A 598 ? 0.2574 0.2020 0.3336 -0.0322 -0.0981 0.0600  598 LEU   A CA  
9238  C  C   . LEU   A 598 ? 0.2200 0.1648 0.3132 -0.0347 -0.1026 0.0611  598 LEU   A C   
9239  O  O   . LEU   A 598 ? 0.2445 0.1904 0.3320 -0.0355 -0.1041 0.0569  598 LEU   A O   
9240  C  CB  . LEU   A 598 ? 0.2141 0.1710 0.2976 -0.0348 -0.0937 0.0594  598 LEU   A CB  
9241  C  CG  . LEU   A 598 ? 0.2039 0.1630 0.2830 -0.0327 -0.0896 0.0569  598 LEU   A CG  
9242  C  CD1 . LEU   A 598 ? 0.1935 0.1609 0.2698 -0.0356 -0.0856 0.0568  598 LEU   A CD1 
9243  C  CD2 . LEU   A 598 ? 0.2448 0.1979 0.3181 -0.0294 -0.0903 0.0505  598 LEU   A CD2 
9255  N  N   . GLY   A 599 ? 0.2576 0.1961 0.3469 -0.0357 -0.1051 0.0671  599 GLY   A N   
9256  C  CA  . GLY   A 599 ? 0.2417 0.1790 0.3420 -0.0384 -0.1093 0.0694  599 GLY   A CA  
9257  C  C   . GLY   A 599 ? 0.2846 0.2305 0.3807 -0.0420 -0.1074 0.0730  599 GLY   A C   
9258  O  O   . GLY   A 599 ? 0.2630 0.2108 0.3703 -0.0432 -0.1109 0.0727  599 GLY   A O   
9262  N  N   . LEU   A 600 ? 0.2353 0.1910 0.3377 -0.0431 -0.1023 0.0766  600 LEU   A N   
9263  C  CA  . LEU   A 600 ? 0.2374 0.2020 0.3396 -0.0457 -0.0992 0.0806  600 LEU   A CA  
9264  C  C   . LEU   A 600 ? 0.2554 0.2189 0.3579 -0.0485 -0.0978 0.0904  600 LEU   A C   
9265  O  O   . LEU   A 600 ? 0.2112 0.1832 0.3171 -0.0500 -0.0938 0.0952  600 LEU   A O   
9266  C  CB  . LEU   A 600 ? 0.2121 0.1862 0.3128 -0.0453 -0.0952 0.0774  600 LEU   A CB  
9267  C  CG  . LEU   A 600 ? 0.2180 0.1914 0.3109 -0.0423 -0.0938 0.0684  600 LEU   A CG  
9268  C  CD1 . LEU   A 600 ? 0.1871 0.1652 0.2755 -0.0406 -0.0872 0.0649  600 LEU   A CD1 
9269  C  CD2 . LEU   A 600 ? 0.2222 0.1963 0.3179 -0.0411 -0.0936 0.0668  600 LEU   A CD2 
9281  N  N   . ASP   A 601 ? 0.2729 0.2272 0.3783 -0.0492 -0.1012 0.0938  601 ASP   A N   
9282  C  CA  . ASP   A 601 ? 0.2614 0.2125 0.3667 -0.0520 -0.1002 0.1035  601 ASP   A CA  
9283  C  C   . ASP   A 601 ? 0.2034 0.1645 0.3217 -0.0558 -0.0967 0.1091  601 ASP   A C   
9284  O  O   . ASP   A 601 ? 0.2446 0.2043 0.3526 -0.0589 -0.0934 0.1181  601 ASP   A O   
9285  C  CB  . ASP   A 601 ? 0.2635 0.2024 0.3728 -0.0519 -0.1052 0.1050  601 ASP   A CB  
9286  C  CG  . ASP   A 601 ? 0.2813 0.2127 0.3889 -0.0474 -0.1086 0.0993  601 ASP   A CG  
9287  O  OD1 . ASP   A 601 ? 0.2962 0.2269 0.4007 -0.0453 -0.1104 0.0911  601 ASP   A OD1 
9288  O  OD2 . ASP   A 601 ? 0.3481 0.2717 0.4454 -0.0458 -0.1091 0.1027  601 ASP   A OD2 
9293  N  N   . GLU   A 602 ? 0.2301 0.1933 0.3515 -0.0565 -0.0984 0.1068  602 GLU   A N   
9294  C  CA  . GLU   A 602 ? 0.2906 0.2590 0.4139 -0.0599 -0.0953 0.1124  602 GLU   A CA  
9295  C  C   . GLU   A 602 ? 0.2505 0.2304 0.3759 -0.0606 -0.0885 0.1155  602 GLU   A C   
9296  O  O   . GLU   A 602 ? 0.2817 0.2656 0.4076 -0.0641 -0.0840 0.1217  602 GLU   A O   
9297  C  CB  . GLU   A 602 ? 0.3163 0.2864 0.4489 -0.0590 -0.0987 0.1075  602 GLU   A CB  
9298  C  CG  . GLU   A 602 ? 0.3071 0.2827 0.4427 -0.0544 -0.0999 0.0985  602 GLU   A CG  
9299  C  CD  . GLU   A 602 ? 0.3873 0.3613 0.5240 -0.0527 -0.1043 0.0940  602 GLU   A CD  
9300  O  OE1 . GLU   A 602 ? 0.4556 0.4332 0.5950 -0.0537 -0.1022 0.0968  602 GLU   A OE1 
9301  O  OE2 . GLU   A 602 ? 0.4094 0.3775 0.5425 -0.0504 -0.1102 0.0881  602 GLU   A OE2 
9308  N  N   . TYR   A 603 ? 0.2252 0.2079 0.3410 -0.0576 -0.0874 0.1111  603 TYR   A N   
9309  C  CA  . TYR   A 603 ? 0.2122 0.2045 0.3245 -0.0579 -0.0817 0.1129  603 TYR   A CA  
9310  C  C   . TYR   A 603 ? 0.2502 0.2399 0.3488 -0.0587 -0.0786 0.1190  603 TYR   A C   
9311  O  O   . TYR   A 603 ? 0.2720 0.2687 0.3653 -0.0590 -0.0740 0.1209  603 TYR   A O   
9312  C  CB  . TYR   A 603 ? 0.2065 0.2034 0.3163 -0.0545 -0.0828 0.1040  603 TYR   A CB  
9313  C  CG  . TYR   A 603 ? 0.2119 0.2097 0.3283 -0.0526 -0.0862 0.0985  603 TYR   A CG  
9314  C  CD1 . TYR   A 603 ? 0.2137 0.2166 0.3352 -0.0530 -0.0837 0.1008  603 TYR   A CD1 
9315  C  CD2 . TYR   A 603 ? 0.2225 0.2139 0.3364 -0.0501 -0.0914 0.0913  603 TYR   A CD2 
9316  C  CE1 . TYR   A 603 ? 0.2029 0.2052 0.3318 -0.0506 -0.0871 0.0964  603 TYR   A CE1 
9317  C  CE2 . TYR   A 603 ? 0.1857 0.1780 0.3096 -0.0478 -0.0949 0.0870  603 TYR   A CE2 
9318  C  CZ  . TYR   A 603 ? 0.2283 0.2232 0.3492 -0.0477 -0.0929 0.0896  603 TYR   A CZ  
9319  O  OH  . TYR   A 603 ? 0.2045 0.1963 0.3313 -0.0450 -0.0937 0.0846  603 TYR   A OH  
9329  N  N   . ILE   A 604 ? 0.2333 0.2144 0.3329 -0.0588 -0.0813 0.1220  604 ILE   A N   
9330  C  CA  . ILE   A 604 ? 0.2708 0.2473 0.3571 -0.0587 -0.0796 0.1281  604 ILE   A CA  
9331  C  C   . ILE   A 604 ? 0.2959 0.2765 0.3782 -0.0632 -0.0735 0.1383  604 ILE   A C   
9332  O  O   . ILE   A 604 ? 0.3152 0.2952 0.4044 -0.0670 -0.0722 0.1428  604 ILE   A O   
9333  C  CB  . ILE   A 604 ? 0.2809 0.2457 0.3678 -0.0573 -0.0847 0.1289  604 ILE   A CB  
9334  C  CG1 . ILE   A 604 ? 0.3123 0.2722 0.3953 -0.0526 -0.0890 0.1193  604 ILE   A CG1 
9335  C  CG2 . ILE   A 604 ? 0.3149 0.2737 0.3875 -0.0578 -0.0834 0.1373  604 ILE   A CG2 
9336  C  CD1 . ILE   A 604 ? 0.2975 0.2456 0.3837 -0.0508 -0.0941 0.1193  604 ILE   A CD1 
9348  N  N   . GLY   A 605 ? 0.2994 0.2847 0.3750 -0.0627 -0.0693 0.1418  605 GLY   A N   
9349  C  CA  . GLY   A 605 ? 0.4077 0.3941 0.4663 -0.0670 -0.0624 0.1515  605 GLY   A CA  
9350  C  C   . GLY   A 605 ? 0.4054 0.4049 0.4749 -0.0695 -0.0558 0.1518  605 GLY   A C   
9351  O  O   . GLY   A 605 ? 0.4413 0.4441 0.5031 -0.0735 -0.0484 0.1596  605 GLY   A O   
9355  N  N   . LYS   A 606 ? 0.3864 0.3916 0.4658 -0.0672 -0.0580 0.1435  606 LYS   A N   
9356  C  CA  . LYS   A 606 ? 0.3922 0.4080 0.4799 -0.0691 -0.0526 0.1427  606 LYS   A CA  
9357  C  C   . LYS   A 606 ? 0.3929 0.4163 0.4703 -0.0668 -0.0498 0.1394  606 LYS   A C   
9358  O  O   . LYS   A 606 ? 0.4232 0.4556 0.5026 -0.0686 -0.0437 0.1402  606 LYS   A O   
9359  C  CB  . LYS   A 606 ? 0.4396 0.4538 0.5385 -0.0683 -0.0572 0.1369  606 LYS   A CB  
9360  C  CG  . LYS   A 606 ? 0.4456 0.4512 0.5562 -0.0691 -0.0628 0.1376  606 LYS   A CG  
9361  C  CD  . LYS   A 606 ? 0.5101 0.5148 0.6264 -0.0741 -0.0598 0.1433  606 LYS   A CD  
9362  C  CE  . LYS   A 606 ? 0.5398 0.5384 0.6737 -0.0740 -0.0667 0.1410  606 LYS   A CE  
9363  N  NZ  . LYS   A 606 ? 0.6943 0.6864 0.8211 -0.0797 -0.0646 0.1490  606 LYS   A NZ  
9377  N  N   . PHE   A 607 ? 0.3604 0.3809 0.4301 -0.0630 -0.0539 0.1353  607 PHE   A N   
9378  C  CA  . PHE   A 607 ? 0.3683 0.3960 0.4335 -0.0606 -0.0526 0.1315  607 PHE   A CA  
9379  C  C   . PHE   A 607 ? 0.4658 0.4857 0.4947 -0.0580 -0.0513 0.1301  607 PHE   A C   
9380  O  O   . PHE   A 607 ? 0.4413 0.4694 0.4739 -0.0574 -0.0500 0.1332  607 PHE   A O   
9381  C  CB  . PHE   A 607 ? 0.4080 0.4334 0.4689 -0.0573 -0.0580 0.1212  607 PHE   A CB  
9382  C  CG  . PHE   A 607 ? 0.3233 0.3529 0.4106 -0.0578 -0.0602 0.1175  607 PHE   A CG  
9383  C  CD1 . PHE   A 607 ? 0.3912 0.4110 0.4741 -0.0577 -0.0646 0.1160  607 PHE   A CD1 
9384  C  CD2 . PHE   A 607 ? 0.2875 0.3230 0.3745 -0.0578 -0.0579 0.1154  607 PHE   A CD2 
9385  C  CE1 . PHE   A 607 ? 0.3138 0.3359 0.4172 -0.0571 -0.0669 0.1126  607 PHE   A CE1 
9386  C  CE2 . PHE   A 607 ? 0.2486 0.2844 0.3512 -0.0569 -0.0602 0.1121  607 PHE   A CE2 
9387  C  CZ  . PHE   A 607 ? 0.2874 0.3152 0.3919 -0.0563 -0.0647 0.1107  607 PHE   A CZ  
9388  O  OXT . PHE   A 607 ? 0.3672 0.3687 0.3742 -0.0006 -0.0011 0.0042  607 PHE   A OXT 
9398  N  N   . MET   B 1   ? 0.5825 0.3714 0.4858 0.0906  0.0701  -0.0122 1   MET   B N   
9399  C  CA  . MET   B 1   ? 0.5715 0.3530 0.4754 0.0848  0.0704  -0.0150 1   MET   B CA  
9400  C  C   . MET   B 1   ? 0.5189 0.3035 0.4276 0.0787  0.0644  -0.0259 1   MET   B C   
9401  O  O   . MET   B 1   ? 0.5335 0.3251 0.4354 0.0799  0.0605  -0.0295 1   MET   B O   
9402  C  CB  . MET   B 1   ? 0.5158 0.3050 0.4300 0.0856  0.0701  -0.0049 1   MET   B CB  
9403  C  CG  . MET   B 1   ? 0.5416 0.3362 0.4494 0.0925  0.0727  0.0063  1   MET   B CG  
9404  S  SD  . MET   B 1   ? 0.5438 0.3458 0.4541 0.0934  0.0727  0.0167  1   MET   B SD  
9405  C  CE  . MET   B 1   ? 0.5413 0.3454 0.4522 0.1019  0.0789  0.0276  1   MET   B CE  
9417  N  N   . TYR   B 2   ? 0.4670 0.2463 0.3800 0.0726  0.0638  -0.0305 2   TYR   B N   
9418  C  CA  . TYR   B 2   ? 0.4113 0.1942 0.3272 0.0666  0.0579  -0.0402 2   TYR   B CA  
9419  C  C   . TYR   B 2   ? 0.3885 0.1807 0.3015 0.0650  0.0535  -0.0344 2   TYR   B C   
9420  O  O   . TYR   B 2   ? 0.3710 0.1619 0.2886 0.0645  0.0558  -0.0268 2   TYR   B O   
9421  C  CB  . TYR   B 2   ? 0.4207 0.1925 0.3412 0.0605  0.0595  -0.0503 2   TYR   B CB  
9422  C  CG  . TYR   B 2   ? 0.4301 0.1924 0.3511 0.0615  0.0635  -0.0581 2   TYR   B CG  
9423  C  CD1 . TYR   B 2   ? 0.4249 0.1909 0.3399 0.0637  0.0613  -0.0655 2   TYR   B CD1 
9424  C  CD2 . TYR   B 2   ? 0.4363 0.1863 0.3654 0.0605  0.0703  -0.0579 2   TYR   B CD2 
9425  C  CE1 . TYR   B 2   ? 0.4206 0.1782 0.3363 0.0646  0.0652  -0.0730 2   TYR   B CE1 
9426  C  CE2 . TYR   B 2   ? 0.4651 0.2050 0.3904 0.0613  0.0745  -0.0650 2   TYR   B CE2 
9427  C  CZ  . TYR   B 2   ? 0.4322 0.1779 0.3613 0.0634  0.0718  -0.0732 2   TYR   B CZ  
9428  O  OH  . TYR   B 2   ? 0.5638 0.2974 0.4793 0.0643  0.0761  -0.0807 2   TYR   B OH  
9438  N  N   . GLY   B 3   ? 0.3823 0.1842 0.2899 0.0642  0.0479  -0.0374 3   GLY   B N   
9439  C  CA  . GLY   B 3   ? 0.3625 0.1737 0.2684 0.0632  0.0442  -0.0318 3   GLY   B CA  
9440  C  C   . GLY   B 3   ? 0.3136 0.1331 0.2214 0.0689  0.0453  -0.0207 3   GLY   B C   
9441  O  O   . GLY   B 3   ? 0.3013 0.1305 0.2021 0.0718  0.0425  -0.0192 3   GLY   B O   
9445  N  N   . TYR   B 4   ? 0.3423 0.1567 0.2484 0.0708  0.0495  -0.0132 4   TYR   B N   
9446  C  CA  . TYR   B 4   ? 0.3451 0.1673 0.2508 0.0768  0.0509  -0.0035 4   TYR   B CA  
9447  C  C   . TYR   B 4   ? 0.3658 0.1886 0.2669 0.0818  0.0522  -0.0042 4   TYR   B C   
9448  O  O   . TYR   B 4   ? 0.3692 0.1828 0.2710 0.0811  0.0544  -0.0106 4   TYR   B O   
9449  C  CB  . TYR   B 4   ? 0.3329 0.1506 0.2424 0.0783  0.0556  0.0041  4   TYR   B CB  
9450  C  CG  . TYR   B 4   ? 0.3410 0.1546 0.2517 0.0731  0.0557  0.0046  4   TYR   B CG  
9451  C  CD1 . TYR   B 4   ? 0.3142 0.1372 0.2269 0.0724  0.0531  0.0095  4   TYR   B CD1 
9452  C  CD2 . TYR   B 4   ? 0.3346 0.1371 0.2535 0.0684  0.0585  -0.0002 4   TYR   B CD2 
9453  C  CE1 . TYR   B 4   ? 0.3014 0.1217 0.2190 0.0674  0.0537  0.0102  4   TYR   B CE1 
9454  C  CE2 . TYR   B 4   ? 0.3451 0.1445 0.2665 0.0634  0.0588  0.0003  4   TYR   B CE2 
9455  C  CZ  . TYR   B 4   ? 0.3313 0.1393 0.2510 0.0629  0.0565  0.0059  4   TYR   B CZ  
9456  O  OH  . TYR   B 4   ? 0.3148 0.1209 0.2414 0.0578  0.0571  0.0068  4   TYR   B OH  
9466  N  N   . ASP   B 5   ? 0.3651 0.1993 0.2644 0.0863  0.0509  0.0013  5   ASP   B N   
9467  C  CA  . ASP   B 5   ? 0.3672 0.2030 0.2642 0.0912  0.0527  0.0020  5   ASP   B CA  
9468  C  C   . ASP   B 5   ? 0.3964 0.2253 0.2875 0.0957  0.0584  0.0084  5   ASP   B C   
9469  O  O   . ASP   B 5   ? 0.3457 0.1686 0.2467 0.0977  0.0623  0.0060  5   ASP   B O   
9470  C  CB  . ASP   B 5   ? 0.3436 0.1941 0.2402 0.0934  0.0493  0.0047  5   ASP   B CB  
9471  C  CG  . ASP   B 5   ? 0.3579 0.2124 0.2466 0.0905  0.0450  -0.0010 5   ASP   B CG  
9472  O  OD1 . ASP   B 5   ? 0.3270 0.1753 0.2194 0.0873  0.0442  -0.0083 5   ASP   B OD1 
9473  O  OD2 . ASP   B 5   ? 0.3249 0.1925 0.2191 0.0916  0.0428  0.0019  5   ASP   B OD2 
9478  N  N   . GLY   B 6   ? 0.3159 0.1534 0.2216 0.0974  0.0590  0.0162  6   GLY   B N   
9479  C  CA  . GLY   B 6   ? 0.3362 0.1696 0.2382 0.1023  0.0642  0.0236  6   GLY   B CA  
9480  C  C   . GLY   B 6   ? 0.3386 0.1863 0.2429 0.1078  0.0636  0.0312  6   GLY   B C   
9481  O  O   . GLY   B 6   ? 0.3461 0.1933 0.2506 0.1127  0.0679  0.0376  6   GLY   B O   
9485  N  N   . LYS   B 7   ? 0.3550 0.2145 0.2544 0.1069  0.0585  0.0304  7   LYS   B N   
9486  C  CA  . LYS   B 7   ? 0.3039 0.1787 0.2091 0.1117  0.0577  0.0358  7   LYS   B CA  
9487  C  C   . LYS   B 7   ? 0.2728 0.1618 0.1802 0.1101  0.0530  0.0374  7   LYS   B C   
9488  O  O   . LYS   B 7   ? 0.2791 0.1683 0.1840 0.1051  0.0498  0.0326  7   LYS   B O   
9489  C  CB  . LYS   B 7   ? 0.2995 0.1769 0.2033 0.1134  0.0579  0.0337  7   LYS   B CB  
9490  C  CG  . LYS   B 7   ? 0.2868 0.1574 0.1936 0.1105  0.0608  0.0311  7   LYS   B CG  
9491  C  CD  . LYS   B 7   ? 0.3319 0.1945 0.2370 0.1210  0.0679  0.0383  7   LYS   B CD  
9492  C  CE  . LYS   B 7   ? 0.3849 0.2311 0.2886 0.1220  0.0738  0.0367  7   LYS   B CE  
9493  N  NZ  . LYS   B 7   ? 0.4316 0.2763 0.3358 0.1280  0.0797  0.0435  7   LYS   B NZ  
9507  N  N   . VAL   B 8   ? 0.2612 0.1635 0.1711 0.1118  0.0522  0.0427  8   VAL   B N   
9508  C  CA  . VAL   B 8   ? 0.2575 0.1729 0.1707 0.1134  0.0488  0.0450  8   VAL   B CA  
9509  C  C   . VAL   B 8   ? 0.2609 0.1898 0.1753 0.1169  0.0476  0.0465  8   VAL   B C   
9510  O  O   . VAL   B 8   ? 0.2617 0.1921 0.1790 0.1217  0.0501  0.0504  8   VAL   B O   
9511  C  CB  . VAL   B 8   ? 0.2847 0.2018 0.1943 0.1154  0.0491  0.0502  8   VAL   B CB  
9512  C  CG1 . VAL   B 8   ? 0.2511 0.1854 0.1660 0.1153  0.0449  0.0513  8   VAL   B CG1 
9513  C  CG2 . VAL   B 8   ? 0.3166 0.2191 0.2230 0.1113  0.0509  0.0486  8   VAL   B CG2 
9523  N  N   . LEU   B 9   ? 0.2317 0.1729 0.1519 0.1128  0.0438  0.0433  9   LEU   B N   
9524  C  CA  . LEU   B 9   ? 0.2221 0.1786 0.1508 0.1135  0.0424  0.0436  9   LEU   B CA  
9525  C  C   . LEU   B 9   ? 0.2709 0.2406 0.1955 0.1184  0.0400  0.0476  9   LEU   B C   
9526  O  O   . LEU   B 9   ? 0.2702 0.2449 0.2002 0.1151  0.0374  0.0454  9   LEU   B O   
9527  C  CB  . LEU   B 9   ? 0.2301 0.1856 0.1561 0.1120  0.0419  0.0393  9   LEU   B CB  
9528  C  CG  . LEU   B 9   ? 0.2087 0.1794 0.1477 0.1118  0.0408  0.0391  9   LEU   B CG  
9529  C  CD1 . LEU   B 9   ? 0.2455 0.2155 0.1809 0.1181  0.0435  0.0428  9   LEU   B CD1 
9530  C  CD2 . LEU   B 9   ? 0.2339 0.2031 0.1697 0.1082  0.0407  0.0349  9   LEU   B CD2 
9542  N  N   . ARG   B 10  ? 0.2140 0.1969 0.1500 0.1171  0.0394  0.0503  10  ARG   B N   
9543  C  CA  . ARG   B 10  ? 0.2107 0.2113 0.1524 0.1202  0.0363  0.0534  10  ARG   B CA  
9544  C  C   . ARG   B 10  ? 0.2563 0.2706 0.1969 0.1279  0.0345  0.0548  10  ARG   B C   
9545  O  O   . ARG   B 10  ? 0.2328 0.2497 0.1840 0.1317  0.0362  0.0573  10  ARG   B O   
9546  C  CB  . ARG   B 10  ? 0.2533 0.2537 0.1847 0.1325  0.0376  0.0631  10  ARG   B CB  
9547  C  CG  . ARG   B 10  ? 0.2210 0.2425 0.1622 0.1288  0.0335  0.0632  10  ARG   B CG  
9548  C  CD  . ARG   B 10  ? 0.2722 0.2950 0.2048 0.1411  0.0347  0.0739  10  ARG   B CD  
9549  N  NE  . ARG   B 10  ? 0.2937 0.2983 0.2174 0.1399  0.0384  0.0757  10  ARG   B NE  
9550  C  CZ  . ARG   B 10  ? 0.2472 0.2522 0.1746 0.1344  0.0374  0.0738  10  ARG   B CZ  
9551  N  NH1 . ARG   B 10  ? 0.2375 0.2572 0.1623 0.1317  0.0326  0.0713  10  ARG   B NH1 
9552  N  NH2 . ARG   B 10  ? 0.3001 0.2857 0.2148 0.1363  0.0416  0.0773  10  ARG   B NH2 
9566  N  N   . ILE   B 11  ? 0.1998 0.2281 0.1545 0.1226  0.0311  0.0501  11  ILE   B N   
9567  C  CA  . ILE   B 11  ? 0.1969 0.2415 0.1624 0.1249  0.0297  0.0485  11  ILE   B CA  
9568  C  C   . ILE   B 11  ? 0.2239 0.2917 0.1933 0.1270  0.0248  0.0491  11  ILE   B C   
9569  O  O   . ILE   B 11  ? 0.2483 0.3217 0.2164 0.1243  0.0225  0.0464  11  ILE   B O   
9570  C  CB  . ILE   B 11  ? 0.2031 0.2423 0.1718 0.1185  0.0311  0.0423  11  ILE   B CB  
9571  C  CG1 . ILE   B 11  ? 0.2274 0.2462 0.1880 0.1164  0.0347  0.0414  11  ILE   B CG1 
9572  C  CG2 . ILE   B 11  ? 0.2033 0.2582 0.1845 0.1172  0.0303  0.0392  11  ILE   B CG2 
9573  C  CD1 . ILE   B 11  ? 0.2418 0.2548 0.2029 0.1100  0.0358  0.0364  11  ILE   B CD1 
9585  N  N   . ASN   B 12  ? 0.2054 0.2886 0.1835 0.1316  0.0230  0.0520  12  ASN   B N   
9586  C  CA  . ASN   B 12  ? 0.2060 0.3159 0.1917 0.1329  0.0177  0.0511  12  ASN   B CA  
9587  C  C   . ASN   B 12  ? 0.1993 0.3221 0.1999 0.1290  0.0172  0.0442  12  ASN   B C   
9588  O  O   . ASN   B 12  ? 0.2023 0.3255 0.2094 0.1310  0.0189  0.0455  12  ASN   B O   
9589  C  CB  . ASN   B 12  ? 0.2250 0.3458 0.2093 0.1396  0.0155  0.0580  12  ASN   B CB  
9590  C  CG  . ASN   B 12  ? 0.2590 0.4077 0.2449 0.1404  0.0090  0.0567  12  ASN   B CG  
9591  O  OD1 . ASN   B 12  ? 0.2153 0.3836 0.2190 0.1381  0.0062  0.0512  12  ASN   B OD1 
9592  N  ND2 . ASN   B 12  ? 0.2785 0.4318 0.2571 0.1426  0.0065  0.0608  12  ASN   B ND2 
9599  N  N   . LEU   B 13  ? 0.1910 0.3277 0.1995 0.1238  0.0152  0.0372  13  LEU   B N   
9600  C  CA  . LEU   B 13  ? 0.1830 0.3305 0.2098 0.1182  0.0164  0.0294  13  LEU   B CA  
9601  C  C   . LEU   B 13  ? 0.2067 0.3789 0.2417 0.1199  0.0123  0.0279  13  LEU   B C   
9602  O  O   . LEU   B 13  ? 0.2042 0.3842 0.2578 0.1156  0.0142  0.0220  13  LEU   B O   
9603  C  CB  . LEU   B 13  ? 0.1882 0.3379 0.2158 0.1103  0.0174  0.0217  13  LEU   B CB  
9604  C  CG  . LEU   B 13  ? 0.1825 0.3076 0.2034 0.1069  0.0220  0.0216  13  LEU   B CG  
9605  C  CD1 . LEU   B 13  ? 0.1772 0.3058 0.2025 0.0982  0.0240  0.0139  13  LEU   B CD1 
9606  C  CD2 . LEU   B 13  ? 0.2007 0.3071 0.2194 0.1065  0.0263  0.0234  13  LEU   B CD2 
9618  N  N   . LYS   B 14  ? 0.1690 0.3590 0.2092 0.1245  0.0067  0.0314  14  LYS   B N   
9619  C  CA  . LYS   B 14  ? 0.2234 0.4381 0.2649 0.1265  0.0016  0.0306  14  LYS   B CA  
9620  C  C   . LYS   B 14  ? 0.2262 0.4340 0.2735 0.1329  0.0038  0.0376  14  LYS   B C   
9621  O  O   . LYS   B 14  ? 0.2556 0.4728 0.3149 0.1316  0.0042  0.0342  14  LYS   B O   
9622  C  CB  . LYS   B 14  ? 0.2387 0.4736 0.2762 0.1287  -0.0054 0.0320  14  LYS   B CB  
9623  C  CG  . LYS   B 14  ? 0.2664 0.5291 0.3136 0.1307  -0.0113 0.0311  14  LYS   B CG  
9624  C  CD  . LYS   B 14  ? 0.3549 0.6382 0.3943 0.1309  -0.0182 0.0303  14  LYS   B CD  
9625  C  CE  . LYS   B 14  ? 0.4755 0.7875 0.5176 0.1299  -0.0246 0.0251  14  LYS   B CE  
9626  N  NZ  . LYS   B 14  ? 0.4625 0.7968 0.5202 0.1200  -0.0283 0.0116  14  LYS   B NZ  
9640  N  N   . GLU   B 15  ? 0.2333 0.4227 0.2637 0.1389  0.0060  0.0470  15  GLU   B N   
9641  C  CA  . GLU   B 15  ? 0.2160 0.3961 0.2495 0.1444  0.0095  0.0537  15  GLU   B CA  
9642  C  C   . GLU   B 15  ? 0.2260 0.3866 0.2645 0.1415  0.0157  0.0512  15  GLU   B C   
9643  O  O   . GLU   B 15  ? 0.2935 0.4489 0.3307 0.1444  0.0183  0.0542  15  GLU   B O   
9644  C  CB  . GLU   B 15  ? 0.2409 0.4077 0.2599 0.1504  0.0112  0.0630  15  GLU   B CB  
9645  C  CG  . GLU   B 15  ? 0.3263 0.5097 0.3372 0.1547  0.0063  0.0677  15  GLU   B CG  
9646  C  CD  . GLU   B 15  ? 0.4035 0.6153 0.4224 0.1566  0.0005  0.0666  15  GLU   B CD  
9647  O  OE1 . GLU   B 15  ? 0.4012 0.6158 0.4336 0.1594  0.0021  0.0685  15  GLU   B OE1 
9648  O  OE2 . GLU   B 15  ? 0.3971 0.6316 0.4208 0.1550  -0.0056 0.0633  15  GLU   B OE2 
9655  N  N   . ARG   B 16  ? 0.2316 0.3798 0.2651 0.1351  0.0181  0.0457  16  ARG   B N   
9656  C  CA  . ARG   B 16  ? 0.2419 0.3708 0.2793 0.1316  0.0239  0.0435  16  ARG   B CA  
9657  C  C   . ARG   B 16  ? 0.2439 0.3504 0.2641 0.1358  0.0277  0.0501  16  ARG   B C   
9658  O  O   . ARG   B 16  ? 0.2442 0.3427 0.2679 0.1367  0.0313  0.0512  16  ARG   B O   
9659  C  CB  . ARG   B 16  ? 0.3148 0.4523 0.3637 0.1294  0.0251  0.0389  16  ARG   B CB  
9660  C  CG  . ARG   B 16  ? 0.3187 0.4770 0.3867 0.1237  0.0229  0.0307  16  ARG   B CG  
9661  C  CD  . ARG   B 16  ? 0.3305 0.4813 0.4091 0.1163  0.0279  0.0236  16  ARG   B CD  
9662  N  NE  . ARG   B 16  ? 0.3475 0.5143 0.4388 0.1094  0.0272  0.0152  16  ARG   B NE  
9663  C  CZ  . ARG   B 16  ? 0.3402 0.5047 0.4443 0.1023  0.0321  0.0081  16  ARG   B CZ  
9664  N  NH1 . ARG   B 16  ? 0.3054 0.4529 0.4134 0.1015  0.0372  0.0089  16  ARG   B NH1 
9665  N  NH2 . ARG   B 16  ? 0.3154 0.4963 0.4365 0.0955  0.0320  0.0004  16  ARG   B NH2 
9679  N  N   . THR   B 17  ? 0.2364 0.3342 0.2437 0.1378  0.0273  0.0541  17  THR   B N   
9680  C  CA  . THR   B 17  ? 0.2414 0.3192 0.2352 0.1411  0.0315  0.0594  17  THR   B CA  
9681  C  C   . THR   B 17  ? 0.2413 0.2985 0.2242 0.1365  0.0340  0.0567  17  THR   B C   
9682  O  O   . THR   B 17  ? 0.2289 0.2888 0.2104 0.1332  0.0315  0.0539  17  THR   B O   
9683  C  CB  . THR   B 17  ? 0.2242 0.3094 0.2199 0.1473  0.0301  0.0665  17  THR   B CB  
9684  O  OG1 . THR   B 17  ? 0.2466 0.3391 0.2319 0.1464  0.0261  0.0660  17  THR   B OG1 
9685  C  CG2 . THR   B 17  ? 0.2863 0.3873 0.2834 0.1528  0.0283  0.0705  17  THR   B CG2 
9693  N  N   . CYS   B 18  ? 0.2360 0.2749 0.2130 0.1361  0.0386  0.0570  18  CYS   B N   
9694  C  CA  . CYS   B 18  ? 0.2293 0.2496 0.1970 0.1320  0.0408  0.0543  18  CYS   B CA  
9695  C  C   . CYS   B 18  ? 0.2515 0.2572 0.2093 0.1356  0.0444  0.0583  18  CYS   B C   
9696  O  O   . CYS   B 18  ? 0.2546 0.2553 0.2135 0.1381  0.0478  0.0599  18  CYS   B O   
9697  C  CB  . CYS   B 18  ? 0.2210 0.2344 0.1912 0.1271  0.0425  0.0491  18  CYS   B CB  
9698  S  SG  . CYS   B 18  ? 0.2563 0.2827 0.2332 0.1219  0.0398  0.0443  18  CYS   B SG  
9704  N  N   . LYS   B 19  ? 0.2621 0.2614 0.2141 0.1358  0.0445  0.0599  19  LYS   B N   
9705  C  CA  . LYS   B 19  ? 0.2957 0.2817 0.2386 0.1394  0.0485  0.0640  19  LYS   B CA  
9706  C  C   . LYS   B 19  ? 0.2695 0.2380 0.2070 0.1355  0.0504  0.0607  19  LYS   B C   
9707  O  O   . LYS   B 19  ? 0.2712 0.2395 0.2051 0.1310  0.0475  0.0574  19  LYS   B O   
9708  C  CB  . LYS   B 19  ? 0.3159 0.3127 0.2628 0.1447  0.0476  0.0709  19  LYS   B CB  
9709  C  CG  . LYS   B 19  ? 0.3482 0.3663 0.3020 0.1487  0.0442  0.0743  19  LYS   B CG  
9710  C  CD  . LYS   B 19  ? 0.3707 0.4011 0.3277 0.1542  0.0427  0.0809  19  LYS   B CD  
9711  C  CE  . LYS   B 19  ? 0.4354 0.4860 0.3985 0.1593  0.0401  0.0851  19  LYS   B CE  
9712  N  NZ  . LYS   B 19  ? 0.5031 0.5700 0.4630 0.1629  0.0361  0.0897  19  LYS   B NZ  
9726  N  N   . SER   B 20  ? 0.2649 0.2191 0.1976 0.1357  0.0549  0.0609  20  SER   B N   
9727  C  CA  . SER   B 20  ? 0.2780 0.2145 0.2041 0.1338  0.0573  0.0586  20  SER   B CA  
9728  C  C   . SER   B 20  ? 0.3070 0.2374 0.2263 0.1370  0.0600  0.0638  20  SER   B C   
9729  O  O   . SER   B 20  ? 0.2948 0.2285 0.2209 0.1429  0.0633  0.0700  20  SER   B O   
9730  C  CB  . SER   B 20  ? 0.2840 0.2064 0.2046 0.1326  0.0606  0.0547  20  SER   B CB  
9731  O  OG  . SER   B 20  ? 0.2715 0.1841 0.1894 0.1227  0.0603  0.0493  20  SER   B OG  
9737  N  N   . GLU   B 21  ? 0.2686 0.1984 0.1913 0.1269  0.0581  0.0598  21  GLU   B N   
9738  C  CA  . GLU   B 21  ? 0.2808 0.2035 0.2020 0.1298  0.0616  0.0645  21  GLU   B CA  
9739  C  C   . GLU   B 21  ? 0.2851 0.1900 0.2020 0.1247  0.0636  0.0595  21  GLU   B C   
9740  O  O   . GLU   B 21  ? 0.3220 0.2183 0.2318 0.1254  0.0618  0.0556  21  GLU   B O   
9741  C  CB  . GLU   B 21  ? 0.3489 0.2784 0.2626 0.1374  0.0596  0.0718  21  GLU   B CB  
9742  C  CG  . GLU   B 21  ? 0.3237 0.2749 0.2483 0.1421  0.0566  0.0761  21  GLU   B CG  
9743  C  CD  . GLU   B 21  ? 0.3408 0.3066 0.2650 0.1433  0.0525  0.0793  21  GLU   B CD  
9744  O  OE1 . GLU   B 21  ? 0.3728 0.3319 0.2902 0.1397  0.0519  0.0778  21  GLU   B OE1 
9745  O  OE2 . GLU   B 21  ? 0.3523 0.3353 0.2785 0.1477  0.0497  0.0831  21  GLU   B OE2 
9752  N  N   . ASN   B 22  ? 0.2993 0.1917 0.2128 0.1262  0.0692  0.0623  22  ASN   B N   
9753  C  CA  . ASN   B 22  ? 0.3058 0.1822 0.2219 0.1220  0.0716  0.0579  22  ASN   B CA  
9754  C  C   . ASN   B 22  ? 0.3486 0.2171 0.2533 0.1237  0.0707  0.0595  22  ASN   B C   
9755  O  O   . ASN   B 22  ? 0.3413 0.2183 0.2510 0.1268  0.0709  0.0658  22  ASN   B O   
9756  C  CB  . ASN   B 22  ? 0.3640 0.2181 0.2710 0.1306  0.0814  0.0628  22  ASN   B CB  
9757  C  CG  . ASN   B 22  ? 0.3319 0.1880 0.2471 0.1265  0.0825  0.0584  22  ASN   B CG  
9758  O  OD1 . ASN   B 22  ? 0.3326 0.1916 0.2441 0.1298  0.0801  0.0566  22  ASN   B OD1 
9759  N  ND2 . ASN   B 22  ? 0.3485 0.1908 0.2618 0.1281  0.0896  0.0594  22  ASN   B ND2 
9766  N  N   . LEU   B 23  ? 0.3118 0.1729 0.2211 0.1172  0.0686  0.0521  23  LEU   B N   
9767  C  CA  . LEU   B 23  ? 0.3196 0.1788 0.2295 0.1125  0.0668  0.0510  23  LEU   B CA  
9768  C  C   . LEU   B 23  ? 0.3819 0.2283 0.2844 0.1135  0.0731  0.0554  23  LEU   B C   
9769  O  O   . LEU   B 23  ? 0.3621 0.1978 0.2726 0.1144  0.0785  0.0543  23  LEU   B O   
9770  C  CB  . LEU   B 23  ? 0.3307 0.1825 0.2352 0.1054  0.0634  0.0419  23  LEU   B CB  
9771  C  CG  . LEU   B 23  ? 0.3165 0.1651 0.2240 0.0994  0.0616  0.0394  23  LEU   B CG  
9772  C  CD1 . LEU   B 23  ? 0.3108 0.1730 0.2159 0.0988  0.0566  0.0411  23  LEU   B CD1 
9773  C  CD2 . LEU   B 23  ? 0.3415 0.1789 0.2467 0.0931  0.0605  0.0306  23  LEU   B CD2 
9785  N  N   . ASP   B 24  ? 0.3488 0.2007 0.2586 0.1137  0.0732  0.0601  24  ASP   B N   
9786  C  CA  . ASP   B 24  ? 0.3575 0.1990 0.2703 0.1140  0.0798  0.0641  24  ASP   B CA  
9787  C  C   . ASP   B 24  ? 0.3715 0.1986 0.2809 0.1056  0.0797  0.0562  24  ASP   B C   
9788  O  O   . ASP   B 24  ? 0.3665 0.1974 0.2773 0.1011  0.0759  0.0544  24  ASP   B O   
9789  C  CB  . ASP   B 24  ? 0.4219 0.2722 0.3275 0.1177  0.0800  0.0722  24  ASP   B CB  
9790  C  CG  . ASP   B 24  ? 0.4304 0.2720 0.3419 0.1190  0.0876  0.0776  24  ASP   B CG  
9791  O  OD1 . ASP   B 24  ? 0.4160 0.2422 0.3296 0.1138  0.0914  0.0731  24  ASP   B OD1 
9792  O  OD2 . ASP   B 24  ? 0.4857 0.3349 0.3917 0.1251  0.0898  0.0859  24  ASP   B OD2 
9797  N  N   . LEU   B 25  ? 0.3490 0.1634 0.2669 0.1032  0.0835  0.0508  25  LEU   B N   
9798  C  CA  . LEU   B 25  ? 0.3997 0.2020 0.3153 0.0947  0.0825  0.0418  25  LEU   B CA  
9799  C  C   . LEU   B 25  ? 0.3838 0.1822 0.3041 0.0914  0.0852  0.0443  25  LEU   B C   
9800  O  O   . LEU   B 25  ? 0.3481 0.1459 0.2718 0.0846  0.0814  0.0388  25  LEU   B O   
9801  C  CB  . LEU   B 25  ? 0.4242 0.2135 0.3422 0.0933  0.0863  0.0349  25  LEU   B CB  
9802  C  CG  . LEU   B 25  ? 0.3896 0.1712 0.3187 0.0848  0.0844  0.0239  25  LEU   B CG  
9803  C  CD1 . LEU   B 25  ? 0.3731 0.1623 0.2953 0.0810  0.0758  0.0178  25  LEU   B CD1 
9804  C  CD2 . LEU   B 25  ? 0.4663 0.2340 0.3906 0.0841  0.0887  0.0173  25  LEU   B CD2 
9816  N  N   . ASP   B 26  ? 0.3977 0.1937 0.3203 0.0964  0.0924  0.0525  26  ASP   B N   
9817  C  CA  . ASP   B 26  ? 0.4233 0.2158 0.3517 0.0937  0.0961  0.0558  26  ASP   B CA  
9818  C  C   . ASP   B 26  ? 0.4248 0.2268 0.3422 0.0918  0.0900  0.0573  26  ASP   B C   
9819  O  O   . ASP   B 26  ? 0.3567 0.1567 0.2839 0.0855  0.0893  0.0542  26  ASP   B O   
9820  C  CB  . ASP   B 26  ? 0.5222 0.3101 0.4462 0.1005  0.1055  0.0650  26  ASP   B CB  
9821  C  CG  . ASP   B 26  ? 0.5608 0.3344 0.4951 0.1000  0.1138  0.0628  26  ASP   B CG  
9822  O  OD1 . ASP   B 26  ? 0.5553 0.3192 0.4931 0.0926  0.1128  0.0530  26  ASP   B OD1 
9823  O  OD2 . ASP   B 26  ? 0.6313 0.4020 0.5618 0.1071  0.1217  0.0704  26  ASP   B OD2 
9828  N  N   . LYS   B 27  ? 0.4161 0.2336 0.3332 0.0970  0.0856  0.0616  27  LYS   B N   
9829  C  CA  . LYS   B 27  ? 0.4397 0.2673 0.3455 0.0956  0.0798  0.0629  27  LYS   B CA  
9830  C  C   . LYS   B 27  ? 0.3383 0.1679 0.2555 0.0879  0.0733  0.0537  27  LYS   B C   
9831  O  O   . LYS   B 27  ? 0.3510 0.1812 0.2626 0.0828  0.0710  0.0524  27  LYS   B O   
9832  C  CB  . LYS   B 27  ? 0.4448 0.2907 0.3541 0.1029  0.0765  0.0688  27  LYS   B CB  
9833  C  CG  . LYS   B 27  ? 0.4984 0.3565 0.4000 0.1012  0.0701  0.0686  27  LYS   B CG  
9834  C  CD  . LYS   B 27  ? 0.5169 0.3937 0.4211 0.1075  0.0658  0.0720  27  LYS   B CD  
9835  C  CE  . LYS   B 27  ? 0.6071 0.4852 0.5046 0.1089  0.0634  0.0686  27  LYS   B CE  
9836  N  NZ  . LYS   B 27  ? 0.6095 0.5059 0.5103 0.1110  0.0574  0.0683  27  LYS   B NZ  
9850  N  N   . ALA   B 28  ? 0.3293 0.1565 0.2429 0.0871  0.0708  0.0478  28  ALA   B N   
9851  C  CA  . ALA   B 28  ? 0.3443 0.1714 0.2549 0.0809  0.0650  0.0391  28  ALA   B CA  
9852  C  C   . ALA   B 28  ? 0.3112 0.1289 0.2319 0.0728  0.0659  0.0333  28  ALA   B C   
9853  O  O   . ALA   B 28  ? 0.3161 0.1365 0.2346 0.0672  0.0617  0.0295  28  ALA   B O   
9854  C  CB  . ALA   B 28  ? 0.3444 0.1721 0.2561 0.0827  0.0633  0.0347  28  ALA   B CB  
9860  N  N   . LYS   B 29  ? 0.3249 0.1301 0.2474 0.0720  0.0714  0.0322  29  LYS   B N   
9861  C  CA  . LYS   B 29  ? 0.3228 0.1194 0.2564 0.0642  0.0728  0.0263  29  LYS   B CA  
9862  C  C   . LYS   B 29  ? 0.3458 0.1432 0.2763 0.0620  0.0743  0.0313  29  LYS   B C   
9863  O  O   . LYS   B 29  ? 0.3599 0.1569 0.2953 0.0549  0.0717  0.0265  29  LYS   B O   
9864  C  CB  . LYS   B 29  ? 0.3674 0.1502 0.3009 0.0643  0.0787  0.0234  29  LYS   B CB  
9865  C  CG  . LYS   B 29  ? 0.3689 0.1490 0.3094 0.0645  0.0773  0.0155  29  LYS   B CG  
9866  C  CD  . LYS   B 29  ? 0.4671 0.2332 0.4031 0.0657  0.0844  0.0139  29  LYS   B CD  
9867  C  CE  . LYS   B 29  ? 0.4776 0.2397 0.4212 0.0639  0.0829  0.0038  29  LYS   B CE  
9868  N  NZ  . LYS   B 29  ? 0.5339 0.2823 0.4781 0.0639  0.0905  0.0012  29  LYS   B NZ  
9882  N  N   . LYS   B 30  ? 0.3277 0.1286 0.2584 0.0682  0.0788  0.0407  30  LYS   B N   
9883  C  CA  . LYS   B 30  ? 0.3510 0.1532 0.2793 0.0671  0.0811  0.0461  30  LYS   B CA  
9884  C  C   . LYS   B 30  ? 0.3494 0.1605 0.2717 0.0634  0.0748  0.0447  30  LYS   B C   
9885  O  O   . LYS   B 30  ? 0.3030 0.1143 0.2348 0.0577  0.0749  0.0435  30  LYS   B O   
9886  C  CB  . LYS   B 30  ? 0.3641 0.1696 0.2896 0.0758  0.0868  0.0565  30  LYS   B CB  
9887  C  CG  . LYS   B 30  ? 0.3833 0.1909 0.3045 0.0764  0.0898  0.0628  30  LYS   B CG  
9888  C  CD  . LYS   B 30  ? 0.3480 0.1590 0.2699 0.0859  0.0960  0.0728  30  LYS   B CD  
9889  C  CE  . LYS   B 30  ? 0.3425 0.1606 0.2649 0.0856  0.0986  0.0773  30  LYS   B CE  
9890  N  NZ  . LYS   B 30  ? 0.3858 0.2014 0.2997 0.0974  0.1060  0.0891  30  LYS   B NZ  
9904  N  N   . PHE   B 31  ? 0.3145 0.1363 0.2361 0.0663  0.0697  0.0447  31  PHE   B N   
9905  C  CA  . PHE   B 31  ? 0.3074 0.1382 0.2233 0.0634  0.0641  0.0431  31  PHE   B CA  
9906  C  C   . PHE   B 31  ? 0.3113 0.1412 0.2282 0.0580  0.0590  0.0345  31  PHE   B C   
9907  O  O   . PHE   B 31  ? 0.2843 0.1238 0.2027 0.0569  0.0547  0.0332  31  PHE   B O   
9908  C  CB  . PHE   B 31  ? 0.2702 0.1176 0.1842 0.0691  0.0617  0.0486  31  PHE   B CB  
9909  C  CG  . PHE   B 31  ? 0.2885 0.1348 0.1969 0.0760  0.0667  0.0582  31  PHE   B CG  
9910  C  CD1 . PHE   B 31  ? 0.2949 0.1445 0.2003 0.0739  0.0671  0.0612  31  PHE   B CD1 
9911  C  CD2 . PHE   B 31  ? 0.3239 0.1690 0.2314 0.0833  0.0709  0.0637  31  PHE   B CD2 
9912  C  CE1 . PHE   B 31  ? 0.3020 0.1547 0.2052 0.0794  0.0711  0.0687  31  PHE   B CE1 
9913  C  CE2 . PHE   B 31  ? 0.3811 0.2278 0.2796 0.0889  0.0751  0.0716  31  PHE   B CE2 
9914  C  CZ  . PHE   B 31  ? 0.3230 0.1753 0.2265 0.0871  0.0750  0.0741  31  PHE   B CZ  
9924  N  N   . ILE   B 32  ? 0.2868 0.1084 0.2114 0.0552  0.0598  0.0282  32  ILE   B N   
9925  C  CA  . ILE   B 32  ? 0.2652 0.0903 0.1964 0.0496  0.0544  0.0191  32  ILE   B CA  
9926  C  C   . ILE   B 32  ? 0.2986 0.1264 0.2177 0.0552  0.0514  0.0181  32  ILE   B C   
9927  O  O   . ILE   B 32  ? 0.2930 0.1177 0.2146 0.0557  0.0507  0.0126  32  ILE   B O   
9928  C  CB  . ILE   B 32  ? 0.2872 0.1111 0.2182 0.0430  0.0522  0.0160  32  ILE   B CB  
9929  C  CG1 . ILE   B 32  ? 0.2873 0.1053 0.2242 0.0383  0.0558  0.0172  32  ILE   B CG1 
9930  C  CG2 . ILE   B 32  ? 0.3034 0.1278 0.2358 0.0390  0.0474  0.0074  32  ILE   B CG2 
9931  C  CD1 . ILE   B 32  ? 0.2649 0.0869 0.2093 0.0308  0.0533  0.0143  32  ILE   B CD1 
9943  N  N   . GLY   B 33  ? 0.2954 0.1342 0.2108 0.0583  0.0493  0.0224  33  GLY   B N   
9944  C  CA  . GLY   B 33  ? 0.2712 0.1194 0.1850 0.0624  0.0461  0.0216  33  GLY   B CA  
9945  C  C   . GLY   B 33  ? 0.2787 0.1369 0.1872 0.0615  0.0429  0.0225  33  GLY   B C   
9946  O  O   . GLY   B 33  ? 0.2681 0.1279 0.1802 0.0584  0.0438  0.0250  33  GLY   B O   
9950  N  N   . CYS   B 34  ? 0.2453 0.1132 0.1566 0.0639  0.0400  0.0206  34  CYS   B N   
9951  C  CA  . CYS   B 34  ? 0.2487 0.1268 0.1593 0.0629  0.0378  0.0207  34  CYS   B CA  
9952  C  C   . CYS   B 34  ? 0.2383 0.1203 0.1492 0.0628  0.0391  0.0263  34  CYS   B C   
9953  O  O   . CYS   B 34  ? 0.2480 0.1338 0.1539 0.0682  0.0398  0.0315  34  CYS   B O   
9954  C  CB  . CYS   B 34  ? 0.2744 0.1501 0.1847 0.0568  0.0361  0.0149  34  CYS   B CB  
9955  S  SG  . CYS   B 34  ? 0.2421 0.1330 0.1593 0.0563  0.0341  0.0134  34  CYS   B SG  
9961  N  N   . ARG   B 35  ? 0.2604 0.1406 0.1692 0.0565  0.0391  0.0255  35  ARG   B N   
9962  C  CA  . ARG   B 35  ? 0.2380 0.1251 0.1509 0.0542  0.0401  0.0297  35  ARG   B CA  
9963  C  C   . ARG   B 35  ? 0.2546 0.1356 0.1581 0.0596  0.0429  0.0365  35  ARG   B C   
9964  O  O   . ARG   B 35  ? 0.2309 0.1230 0.1337 0.0644  0.0423  0.0412  35  ARG   B O   
9965  C  CB  . ARG   B 35  ? 0.2516 0.1333 0.1642 0.0457  0.0411  0.0275  35  ARG   B CB  
9966  C  CG  . ARG   B 35  ? 0.2298 0.1190 0.1464 0.0421  0.0424  0.0302  35  ARG   B CG  
9967  C  CD  . ARG   B 35  ? 0.2550 0.1409 0.1724 0.0335  0.0434  0.0277  35  ARG   B CD  
9968  N  NE  . ARG   B 35  ? 0.2325 0.1196 0.1535 0.0301  0.0462  0.0308  35  ARG   B NE  
9969  C  CZ  . ARG   B 35  ? 0.2500 0.1324 0.1721 0.0229  0.0484  0.0297  35  ARG   B CZ  
9970  N  NH1 . ARG   B 35  ? 0.2429 0.1235 0.1744 0.0184  0.0472  0.0252  35  ARG   B NH1 
9971  N  NH2 . ARG   B 35  ? 0.2390 0.1227 0.1618 0.0206  0.0512  0.0325  35  ARG   B NH2 
9985  N  N   . GLY   B 36  ? 0.2522 0.1227 0.1609 0.0575  0.0456  0.0361  36  GLY   B N   
9986  C  CA  . GLY   B 36  ? 0.2707 0.1376 0.1735 0.0614  0.0491  0.0418  36  GLY   B CA  
9987  C  C   . GLY   B 36  ? 0.2269 0.1083 0.1371 0.0663  0.0477  0.0425  36  GLY   B C   
9988  O  O   . GLY   B 36  ? 0.2544 0.1337 0.1528 0.0750  0.0501  0.0518  36  GLY   B O   
9992  N  N   . LEU   B 37  ? 0.2409 0.1125 0.1451 0.0712  0.0479  0.0416  37  LEU   B N   
9993  C  CA  . LEU   B 37  ? 0.2519 0.1283 0.1556 0.0792  0.0484  0.0449  37  LEU   B CA  
9994  C  C   . LEU   B 37  ? 0.2820 0.1742 0.1782 0.0836  0.0448  0.0480  37  LEU   B C   
9995  O  O   . LEU   B 37  ? 0.2624 0.1637 0.1622 0.0898  0.0454  0.0534  37  LEU   B O   
9996  C  CB  . LEU   B 37  ? 0.2582 0.1290 0.1618 0.0791  0.0478  0.0397  37  LEU   B CB  
9997  C  CG  . LEU   B 37  ? 0.2554 0.1328 0.1608 0.0861  0.0479  0.0416  37  LEU   B CG  
9998  C  CD1 . LEU   B 37  ? 0.2912 0.1646 0.1924 0.0913  0.0524  0.0479  37  LEU   B CD1 
9999  C  CD2 . LEU   B 37  ? 0.2589 0.1318 0.1630 0.0850  0.0470  0.0357  37  LEU   B CD2 
10011 N  N   . GLY   B 38  ? 0.2450 0.1455 0.1476 0.0803  0.0414  0.0445  38  GLY   B N   
10012 C  CA  . GLY   B 38  ? 0.2440 0.1612 0.1436 0.0835  0.0382  0.0464  38  GLY   B CA  
10013 C  C   . GLY   B 38  ? 0.2320 0.1585 0.1300 0.0843  0.0379  0.0515  38  GLY   B C   
10014 O  O   . GLY   B 38  ? 0.2438 0.1846 0.1392 0.0895  0.0358  0.0547  38  GLY   B O   
10018 N  N   . VAL   B 39  ? 0.2387 0.1572 0.1331 0.0789  0.0397  0.0520  39  VAL   B N   
10019 C  CA  . VAL   B 39  ? 0.2445 0.1714 0.1357 0.0787  0.0400  0.0562  39  VAL   B CA  
10020 C  C   . VAL   B 39  ? 0.2740 0.2014 0.1605 0.0862  0.0418  0.0622  39  VAL   B C   
10021 O  O   . VAL   B 39  ? 0.2675 0.2113 0.1540 0.0903  0.0394  0.0655  39  VAL   B O   
10022 C  CB  . VAL   B 39  ? 0.2379 0.1552 0.1297 0.0711  0.0426  0.0550  39  VAL   B CB  
10023 C  CG1 . VAL   B 39  ? 0.2616 0.1856 0.1457 0.0714  0.0434  0.0589  39  VAL   B CG1 
10024 C  CG2 . VAL   B 39  ? 0.2509 0.1695 0.1445 0.0626  0.0412  0.0479  39  VAL   B CG2 
10034 N  N   . LYS   B 40  ? 0.2584 0.1715 0.1503 0.0873  0.0462  0.0633  40  LYS   B N   
10035 C  CA  . LYS   B 40  ? 0.2644 0.1773 0.1578 0.0947  0.0497  0.0694  40  LYS   B CA  
10036 C  C   . LYS   B 40  ? 0.3189 0.2450 0.2021 0.1014  0.0464  0.0716  40  LYS   B C   
10037 O  O   . LYS   B 40  ? 0.2831 0.2231 0.1736 0.1072  0.0458  0.0770  40  LYS   B O   
10038 C  CB  . LYS   B 40  ? 0.2770 0.1715 0.1727 0.0937  0.0552  0.0691  40  LYS   B CB  
10039 C  CG  . LYS   B 40  ? 0.3385 0.2289 0.2292 0.1006  0.0606  0.0758  40  LYS   B CG  
10040 C  CD  . LYS   B 40  ? 0.3467 0.2431 0.2400 0.1035  0.0629  0.0823  40  LYS   B CD  
10041 C  CE  . LYS   B 40  ? 0.4194 0.3107 0.3074 0.1106  0.0694  0.0896  40  LYS   B CE  
10042 N  NZ  . LYS   B 40  ? 0.4434 0.3505 0.3286 0.1179  0.0686  0.0968  40  LYS   B NZ  
10056 N  N   . THR   B 41  ? 0.2536 0.1830 0.1525 0.1010  0.0443  0.0671  41  THR   B N   
10057 C  CA  . THR   B 41  ? 0.2926 0.2343 0.1854 0.1071  0.0416  0.0680  41  THR   B CA  
10058 C  C   . THR   B 41  ? 0.2782 0.2426 0.1734 0.1085  0.0364  0.0694  41  THR   B C   
10059 O  O   . THR   B 41  ? 0.2895 0.2671 0.1844 0.1148  0.0353  0.0738  41  THR   B O   
10060 C  CB  . THR   B 41  ? 0.2785 0.2173 0.1820 0.1055  0.0410  0.0625  41  THR   B CB  
10061 O  OG1 . THR   B 41  ? 0.2797 0.1991 0.1797 0.1035  0.0452  0.0605  41  THR   B OG1 
10062 C  CG2 . THR   B 41  ? 0.3392 0.2898 0.2392 0.1113  0.0392  0.0637  41  THR   B CG2 
10070 N  N   . LEU   B 42  ? 0.2566 0.2256 0.1505 0.1024  0.0334  0.0654  42  LEU   B N   
10071 C  CA  . LEU   B 42  ? 0.2400 0.2313 0.1341 0.1022  0.0286  0.0646  42  LEU   B CA  
10072 C  C   . LEU   B 42  ? 0.2622 0.2602 0.1481 0.1049  0.0286  0.0700  42  LEU   B C   
10073 O  O   . LEU   B 42  ? 0.2610 0.2792 0.1492 0.1094  0.0250  0.0718  42  LEU   B O   
10074 C  CB  . LEU   B 42  ? 0.2374 0.2294 0.1294 0.0937  0.0273  0.0587  42  LEU   B CB  
10075 C  CG  . LEU   B 42  ? 0.2444 0.2592 0.1343 0.0908  0.0229  0.0546  42  LEU   B CG  
10076 C  CD1 . LEU   B 42  ? 0.2407 0.2714 0.1413 0.0928  0.0197  0.0508  42  LEU   B CD1 
10077 C  CD2 . LEU   B 42  ? 0.2077 0.2214 0.1036 0.0794  0.0239  0.0474  42  LEU   B CD2 
10089 N  N   . PHE   B 43  ? 0.2486 0.2330 0.1339 0.1025  0.0326  0.0725  43  PHE   B N   
10090 C  CA  . PHE   B 43  ? 0.2680 0.2572 0.1498 0.1052  0.0340  0.0780  43  PHE   B CA  
10091 C  C   . PHE   B 43  ? 0.3147 0.3085 0.1897 0.1149  0.0350  0.0844  43  PHE   B C   
10092 O  O   . PHE   B 43  ? 0.2794 0.2906 0.1578 0.1193  0.0329  0.0882  43  PHE   B O   
10093 C  CB  . PHE   B 43  ? 0.3025 0.2704 0.1755 0.1015  0.0395  0.0795  43  PHE   B CB  
10094 C  CG  . PHE   B 43  ? 0.2694 0.2429 0.1448 0.1001  0.0406  0.0817  43  PHE   B CG  
10095 C  CD1 . PHE   B 43  ? 0.2981 0.2911 0.1638 0.1046  0.0367  0.0848  43  PHE   B CD1 
10096 C  CD2 . PHE   B 43  ? 0.2804 0.2362 0.1508 0.0967  0.0458  0.0835  43  PHE   B CD2 
10097 C  CE1 . PHE   B 43  ? 0.3156 0.3118 0.1750 0.1044  0.0378  0.0875  43  PHE   B CE1 
10098 C  CE2 . PHE   B 43  ? 0.3139 0.2722 0.1764 0.0964  0.0474  0.0866  43  PHE   B CE2 
10099 C  CZ  . PHE   B 43  ? 0.3155 0.2941 0.1743 0.1005  0.0434  0.0887  43  PHE   B CZ  
10109 N  N   . ASP   B 44  ? 0.2987 0.2813 0.1826 0.1179  0.0389  0.0857  44  ASP   B N   
10110 C  CA  . ASP   B 44  ? 0.2852 0.2715 0.1732 0.1263  0.0416  0.0918  44  ASP   B CA  
10111 C  C   . ASP   B 44  ? 0.3010 0.3088 0.1887 0.1313  0.0361  0.0923  44  ASP   B C   
10112 O  O   . ASP   B 44  ? 0.3274 0.3437 0.2145 0.1389  0.0373  0.0985  44  ASP   B O   
10113 C  CB  . ASP   B 44  ? 0.2988 0.2647 0.1877 0.1275  0.0477  0.0924  44  ASP   B CB  
10114 C  CG  . ASP   B 44  ? 0.3211 0.2667 0.2105 0.1252  0.0545  0.0941  44  ASP   B CG  
10115 O  OD1 . ASP   B 44  ? 0.3599 0.3053 0.2420 0.1246  0.0557  0.0970  44  ASP   B OD1 
10116 O  OD2 . ASP   B 44  ? 0.3438 0.2726 0.2332 0.1238  0.0591  0.0924  44  ASP   B OD2 
10121 N  N   . GLU   B 45  ? 0.2828 0.3012 0.1761 0.1269  0.0307  0.0858  45  GLU   B N   
10122 C  CA  . GLU   B 45  ? 0.3124 0.3498 0.2072 0.1308  0.0262  0.0846  45  GLU   B CA  
10123 C  C   . GLU   B 45  ? 0.3259 0.3877 0.2171 0.1288  0.0191  0.0811  45  GLU   B C   
10124 O  O   . GLU   B 45  ? 0.3029 0.3855 0.2040 0.1325  0.0153  0.0807  45  GLU   B O   
10125 C  CB  . GLU   B 45  ? 0.3052 0.3353 0.2073 0.1291  0.0267  0.0802  45  GLU   B CB  
10126 C  CG  . GLU   B 45  ? 0.3094 0.3175 0.2123 0.1307  0.0332  0.0821  45  GLU   B CG  
10127 C  CD  . GLU   B 45  ? 0.3201 0.3244 0.2267 0.1311  0.0339  0.0788  45  GLU   B CD  
10128 O  OE1 . GLU   B 45  ? 0.3084 0.3273 0.2211 0.1301  0.0294  0.0749  45  GLU   B OE1 
10129 O  OE2 . GLU   B 45  ? 0.3172 0.3052 0.2253 0.1320  0.0389  0.0797  45  GLU   B OE2 
10136 N  N   . ILE   B 46  ? 0.2723 0.3363 0.1655 0.1224  0.0175  0.0777  46  ILE   B N   
10137 C  CA  . ILE   B 46  ? 0.2718 0.3594 0.1638 0.1191  0.0114  0.0727  46  ILE   B CA  
10138 C  C   . ILE   B 46  ? 0.3174 0.4070 0.1959 0.1184  0.0115  0.0751  46  ILE   B C   
10139 O  O   . ILE   B 46  ? 0.3003 0.3720 0.1780 0.1187  0.0166  0.0799  46  ILE   B O   
10140 C  CB  . ILE   B 46  ? 0.2781 0.3675 0.1705 0.1106  0.0092  0.0636  46  ILE   B CB  
10141 C  CG1 . ILE   B 46  ? 0.2702 0.3429 0.1568 0.1029  0.0124  0.0614  46  ILE   B CG1 
10142 C  CG2 . ILE   B 46  ? 0.2922 0.3756 0.1912 0.1118  0.0100  0.0617  46  ILE   B CG2 
10143 C  CD1 . ILE   B 46  ? 0.2567 0.3364 0.1450 0.0936  0.0110  0.0524  46  ILE   B CD1 
10155 N  N   . ASP   B 47  ? 0.3155 0.4298 0.1941 0.1172  0.0058  0.0716  47  ASP   B N   
10156 C  CA  . ASP   B 47  ? 0.2859 0.4079 0.1647 0.1149  0.0051  0.0711  47  ASP   B CA  
10157 C  C   . ASP   B 47  ? 0.3366 0.4510 0.1983 0.1037  0.0050  0.0626  47  ASP   B C   
10158 O  O   . ASP   B 47  ? 0.2519 0.3857 0.1312 0.0985  0.0009  0.0537  47  ASP   B O   
10159 C  CB  . ASP   B 47  ? 0.3374 0.4867 0.2087 0.1187  -0.0006 0.0704  47  ASP   B CB  
10160 C  CG  . ASP   B 47  ? 0.3922 0.5510 0.2538 0.1142  -0.0026 0.0669  47  ASP   B CG  
10161 O  OD1 . ASP   B 47  ? 0.3617 0.5034 0.2199 0.1111  0.0019  0.0692  47  ASP   B OD1 
10162 O  OD2 . ASP   B 47  ? 0.4395 0.6243 0.3015 0.1139  -0.0083 0.0618  47  ASP   B OD2 
10167 N  N   . PRO   B 48  ? 0.2872 0.3834 0.1568 0.0996  0.0102  0.0642  48  PRO   B N   
10168 C  CA  . PRO   B 48  ? 0.3032 0.3915 0.1625 0.0885  0.0113  0.0561  48  PRO   B CA  
10169 C  C   . PRO   B 48  ? 0.2652 0.3772 0.1311 0.0820  0.0073  0.0470  48  PRO   B C   
10170 O  O   . PRO   B 48  ? 0.2720 0.3831 0.1378 0.0727  0.0085  0.0385  48  PRO   B O   
10171 C  CB  . PRO   B 48  ? 0.2458 0.3113 0.1126 0.0854  0.0172  0.0597  48  PRO   B CB  
10172 C  CG  . PRO   B 48  ? 0.2565 0.3099 0.1228 0.0943  0.0203  0.0687  48  PRO   B CG  
10173 C  CD  . PRO   B 48  ? 0.3078 0.3818 0.1654 0.1044  0.0160  0.0732  48  PRO   B CD  
10181 N  N   . LYS   B 49  ? 0.2659 0.3975 0.1272 0.0864  0.0030  0.0477  49  LYS   B N   
10182 C  CA  . LYS   B 49  ? 0.2850 0.4387 0.1468 0.0803  -0.0010 0.0384  49  LYS   B CA  
10183 C  C   . LYS   B 49  ? 0.3230 0.4968 0.1865 0.0767  -0.0057 0.0279  49  LYS   B C   
10184 O  O   . LYS   B 49  ? 0.2565 0.4496 0.1317 0.0693  -0.0081 0.0175  49  LYS   B O   
10185 C  CB  . LYS   B 49  ? 0.3118 0.4781 0.1620 0.0863  -0.0036 0.0427  49  LYS   B CB  
10186 C  CG  . LYS   B 49  ? 0.3133 0.4627 0.1548 0.0888  0.0012  0.0510  49  LYS   B CG  
10187 C  CD  . LYS   B 49  ? 0.3302 0.4937 0.1616 0.0963  -0.0012 0.0562  49  LYS   B CD  
10188 C  CE  . LYS   B 49  ? 0.3040 0.4737 0.1498 0.1064  -0.0022 0.0637  49  LYS   B CE  
10189 N  NZ  . LYS   B 49  ? 0.3927 0.5386 0.2257 0.1140  0.0037  0.0752  49  LYS   B NZ  
10203 N  N   . ILE   B 50  ? 0.2898 0.4659 0.1699 0.0814  -0.0067 0.0299  50  ILE   B N   
10204 C  CA  . ILE   B 50  ? 0.2926 0.4914 0.1845 0.0794  -0.0110 0.0213  50  ILE   B CA  
10205 C  C   . ILE   B 50  ? 0.3037 0.5027 0.1947 0.0672  -0.0089 0.0084  50  ILE   B C   
10206 O  O   . ILE   B 50  ? 0.2823 0.4619 0.1761 0.0616  -0.0029 0.0080  50  ILE   B O   
10207 C  CB  . ILE   B 50  ? 0.3361 0.5306 0.2290 0.0878  -0.0115 0.0278  50  ILE   B CB  
10208 C  CG1 . ILE   B 50  ? 0.3294 0.4977 0.2265 0.0864  -0.0058 0.0308  50  ILE   B CG1 
10209 C  CG2 . ILE   B 50  ? 0.3351 0.5314 0.2277 0.0991  -0.0127 0.0387  50  ILE   B CG2 
10210 C  CD1 . ILE   B 50  ? 0.3491 0.5136 0.2507 0.0925  -0.0057 0.0342  50  ILE   B CD1 
10222 N  N   . ASP   B 51  ? 0.2424 0.4684 0.1530 0.0628  -0.0125 -0.0031 51  ASP   B N   
10223 C  CA  . ASP   B 51  ? 0.2714 0.4957 0.1914 0.0514  -0.0087 -0.0155 51  ASP   B CA  
10224 C  C   . ASP   B 51  ? 0.2244 0.4273 0.1594 0.0527  -0.0037 -0.0111 51  ASP   B C   
10225 O  O   . ASP   B 51  ? 0.2434 0.4468 0.1771 0.0608  -0.0059 -0.0054 51  ASP   B O   
10226 C  CB  . ASP   B 51  ? 0.3084 0.5634 0.2453 0.0476  -0.0131 -0.0278 51  ASP   B CB  
10227 C  CG  . ASP   B 51  ? 0.3704 0.6240 0.3218 0.0351  -0.0076 -0.0414 51  ASP   B CG  
10228 O  OD1 . ASP   B 51  ? 0.2847 0.5165 0.2451 0.0298  -0.0003 -0.0410 51  ASP   B OD1 
10229 O  OD2 . ASP   B 51  ? 0.4583 0.7350 0.4218 0.0308  -0.0101 -0.0524 51  ASP   B OD2 
10234 N  N   . ALA   B 52  ? 0.2504 0.4307 0.1806 0.0449  0.0031  -0.0134 52  ALA   B N   
10235 C  CA  . ALA   B 52  ? 0.2012 0.3617 0.1448 0.0459  0.0077  -0.0100 52  ALA   B CA  
10236 C  C   . ALA   B 52  ? 0.1906 0.3609 0.1512 0.0449  0.0081  -0.0156 52  ALA   B C   
10237 O  O   . ALA   B 52  ? 0.1937 0.3502 0.1566 0.0491  0.0103  -0.0109 52  ALA   B O   
10238 C  CB  . ALA   B 52  ? 0.2120 0.3513 0.1520 0.0377  0.0143  -0.0114 52  ALA   B CB  
10244 N  N   . LEU   B 53  ? 0.2166 0.4091 0.1852 0.0394  0.0066  -0.0263 53  LEU   B N   
10245 C  CA  . LEU   B 53  ? 0.2041 0.4085 0.1933 0.0386  0.0075  -0.0327 53  LEU   B CA  
10246 C  C   . LEU   B 53  ? 0.1870 0.4125 0.1796 0.0471  0.0004  -0.0301 53  LEU   B C   
10247 O  O   . LEU   B 53  ? 0.1884 0.4243 0.1954 0.0472  0.0010  -0.0344 53  LEU   B O   
10248 C  CB  . LEU   B 53  ? 0.2097 0.4254 0.2129 0.0266  0.0119  -0.0465 53  LEU   B CB  
10249 C  CG  . LEU   B 53  ? 0.2067 0.4037 0.2123 0.0177  0.0203  -0.0498 53  LEU   B CG  
10250 C  CD1 . LEU   B 53  ? 0.2190 0.4290 0.2398 0.0065  0.0253  -0.0638 53  LEU   B CD1 
10251 C  CD2 . LEU   B 53  ? 0.1697 0.3450 0.1804 0.0210  0.0254  -0.0427 53  LEU   B CD2 
10263 N  N   . SER   B 54  ? 0.1933 0.4251 0.1693 0.0547  -0.0059 -0.0226 54  SER   B N   
10264 C  CA  . SER   B 54  ? 0.1871 0.4391 0.1657 0.0643  -0.0125 -0.0180 54  SER   B CA  
10265 C  C   . SER   B 54  ? 0.1944 0.4304 0.1727 0.0739  -0.0108 -0.0076 54  SER   B C   
10266 O  O   . SER   B 54  ? 0.1631 0.3728 0.1363 0.0751  -0.0061 -0.0012 54  SER   B O   
10267 C  CB  . SER   B 54  ? 0.2129 0.4768 0.1734 0.0702  -0.0189 -0.0125 54  SER   B CB  
10268 O  OG  . SER   B 54  ? 0.2510 0.4922 0.1935 0.0777  -0.0172 0.0005  54  SER   B OG  
10274 N  N   . PRO   B 55  ? 0.2268 0.4785 0.2101 0.0810  -0.0146 -0.0057 55  PRO   B N   
10275 C  CA  . PRO   B 55  ? 0.2075 0.4459 0.1966 0.0909  -0.0125 0.0047  55  PRO   B CA  
10276 C  C   . PRO   B 55  ? 0.2126 0.4297 0.1793 0.0995  -0.0118 0.0181  55  PRO   B C   
10277 O  O   . PRO   B 55  ? 0.1873 0.3844 0.1572 0.1045  -0.0075 0.0247  55  PRO   B O   
10278 C  CB  . PRO   B 55  ? 0.2019 0.4673 0.2034 0.0970  -0.0178 0.0040  55  PRO   B CB  
10279 C  CG  . PRO   B 55  ? 0.2189 0.5080 0.2284 0.0869  -0.0201 -0.0099 55  PRO   B CG  
10280 C  CD  . PRO   B 55  ? 0.1825 0.4695 0.1863 0.0800  -0.0205 -0.0136 55  PRO   B CD  
10288 N  N   . GLU   B 56  ? 0.1747 0.3987 0.1349 0.1016  -0.0153 0.0224  56  GLU   B N   
10289 C  CA  . GLU   B 56  ? 0.2425 0.4471 0.1754 0.1106  -0.0141 0.0353  56  GLU   B CA  
10290 C  C   . GLU   B 56  ? 0.2079 0.3830 0.1427 0.1060  -0.0076 0.0372  56  GLU   B C   
10291 O  O   . GLU   B 56  ? 0.2399 0.3948 0.1604 0.1126  -0.0047 0.0471  56  GLU   B O   
10292 C  CB  . GLU   B 56  ? 0.2200 0.4397 0.1550 0.1127  -0.0173 0.0384  56  GLU   B CB  
10293 C  CG  . GLU   B 56  ? 0.2934 0.5362 0.2301 0.1183  -0.0215 0.0389  56  GLU   B CG  
10294 C  CD  . GLU   B 56  ? 0.3593 0.6309 0.3057 0.1123  -0.0271 0.0266  56  GLU   B CD  
10295 O  OE1 . GLU   B 56  ? 0.3243 0.6065 0.2764 0.1031  -0.0290 0.0164  56  GLU   B OE1 
10296 O  OE2 . GLU   B 56  ? 0.3788 0.6641 0.3397 0.1160  -0.0290 0.0262  56  GLU   B OE2 
10303 N  N   . ASN   B 57  ? 0.2105 0.3787 0.1469 0.0943  -0.0047 0.0274  57  ASN   B N   
10304 C  CA  . ASN   B 57  ? 0.2155 0.3557 0.1489 0.0900  0.0012  0.0281  57  ASN   B CA  
10305 C  C   . ASN   B 57  ? 0.2311 0.3545 0.1680 0.0952  0.0045  0.0326  57  ASN   B C   
10306 O  O   . ASN   B 57  ? 0.2413 0.3751 0.1880 0.0986  0.0036  0.0313  57  ASN   B O   
10307 C  CB  . ASN   B 57  ? 0.2066 0.3454 0.1446 0.0771  0.0040  0.0175  57  ASN   B CB  
10308 C  CG  . ASN   B 57  ? 0.1792 0.2937 0.1167 0.0723  0.0092  0.0185  57  ASN   B CG  
10309 O  OD1 . ASN   B 57  ? 0.2258 0.3217 0.1470 0.0774  0.0106  0.0269  57  ASN   B OD1 
10310 N  ND2 . ASN   B 57  ? 0.1933 0.3047 0.1324 0.0619  0.0124  0.0105  57  ASN   B ND2 
10317 N  N   . LYS   B 58  ? 0.2345 0.3325 0.1644 0.0955  0.0086  0.0371  58  LYS   B N   
10318 C  CA  . LYS   B 58  ? 0.2347 0.3152 0.1662 0.0997  0.0123  0.0401  58  LYS   B CA  
10319 C  C   . LYS   B 58  ? 0.2361 0.3008 0.1681 0.0911  0.0162  0.0337  58  LYS   B C   
10320 O  O   . LYS   B 58  ? 0.2197 0.2777 0.1516 0.0846  0.0175  0.0321  58  LYS   B O   
10321 C  CB  . LYS   B 58  ? 0.2223 0.2880 0.1465 0.1090  0.0139  0.0506  58  LYS   B CB  
10322 C  CG  . LYS   B 58  ? 0.2476 0.3266 0.1662 0.1174  0.0112  0.0573  58  LYS   B CG  
10323 C  CD  . LYS   B 58  ? 0.2454 0.3137 0.1673 0.1235  0.0151  0.0627  58  LYS   B CD  
10324 C  CE  . LYS   B 58  ? 0.2567 0.3404 0.1793 0.1298  0.0134  0.0679  58  LYS   B CE  
10325 N  NZ  . LYS   B 58  ? 0.2804 0.3495 0.2002 0.1351  0.0186  0.0741  58  LYS   B NZ  
10339 N  N   . PHE   B 59  ? 0.1662 0.2299 0.1147 0.0913  0.0185  0.0307  59  PHE   B N   
10340 C  CA  . PHE   B 59  ? 0.1747 0.2251 0.1248 0.0847  0.0223  0.0257  59  PHE   B CA  
10341 C  C   . PHE   B 59  ? 0.2133 0.2406 0.1508 0.0895  0.0248  0.0301  59  PHE   B C   
10342 O  O   . PHE   B 59  ? 0.2052 0.2326 0.1501 0.0961  0.0256  0.0319  59  PHE   B O   
10343 C  CB  . PHE   B 59  ? 0.1726 0.2349 0.1347 0.0817  0.0239  0.0192  59  PHE   B CB  
10344 C  CG  . PHE   B 59  ? 0.1637 0.2170 0.1319 0.0752  0.0285  0.0146  59  PHE   B CG  
10345 C  CD1 . PHE   B 59  ? 0.1353 0.1909 0.1082 0.0662  0.0300  0.0098  59  PHE   B CD1 
10346 C  CD2 . PHE   B 59  ? 0.1956 0.2384 0.1637 0.0788  0.0317  0.0153  59  PHE   B CD2 
10347 C  CE1 . PHE   B 59  ? 0.1626 0.2099 0.1371 0.0611  0.0345  0.0070  59  PHE   B CE1 
10348 C  CE2 . PHE   B 59  ? 0.1898 0.2260 0.1633 0.0740  0.0357  0.0122  59  PHE   B CE2 
10349 C  CZ  . PHE   B 59  ? 0.1799 0.2183 0.1562 0.0654  0.0372  0.0083  59  PHE   B CZ  
10359 N  N   . ILE   B 60  ? 0.1694 0.1820 0.1069 0.0866  0.0259  0.0315  60  ILE   B N   
10360 C  CA  . ILE   B 60  ? 0.2022 0.1934 0.1300 0.0907  0.0281  0.0346  60  ILE   B CA  
10361 C  C   . ILE   B 60  ? 0.2369 0.2163 0.1612 0.0851  0.0303  0.0297  60  ILE   B C   
10362 O  O   . ILE   B 60  ? 0.2150 0.1960 0.1466 0.0774  0.0305  0.0265  60  ILE   B O   
10363 C  CB  . ILE   B 60  ? 0.2150 0.1944 0.1325 0.0925  0.0286  0.0403  60  ILE   B CB  
10364 C  CG1 . ILE   B 60  ? 0.2107 0.2014 0.1276 0.0998  0.0268  0.0470  60  ILE   B CG1 
10365 C  CG2 . ILE   B 60  ? 0.2272 0.1850 0.1399 0.0946  0.0315  0.0414  60  ILE   B CG2 
10366 C  CD1 . ILE   B 60  ? 0.2599 0.2402 0.1645 0.1011  0.0282  0.0526  60  ILE   B CD1 
10378 N  N   . ILE   B 61  ? 0.1900 0.1631 0.1237 0.0895  0.0320  0.0290  61  ILE   B N   
10379 C  CA  . ILE   B 61  ? 0.2385 0.1999 0.1636 0.0851  0.0335  0.0248  61  ILE   B CA  
10380 C  C   . ILE   B 61  ? 0.2174 0.1638 0.1428 0.0847  0.0337  0.0254  61  ILE   B C   
10381 O  O   . ILE   B 61  ? 0.2400 0.1834 0.1588 0.0881  0.0340  0.0271  61  ILE   B O   
10382 C  CB  . ILE   B 61  ? 0.2244 0.1952 0.1639 0.0831  0.0339  0.0222  61  ILE   B CB  
10383 C  CG1 . ILE   B 61  ? 0.2473 0.2357 0.1958 0.0827  0.0342  0.0210  61  ILE   B CG1 
10384 C  CG2 . ILE   B 61  ? 0.2561 0.2191 0.1904 0.0776  0.0343  0.0190  61  ILE   B CG2 
10385 C  CD1 . ILE   B 61  ? 0.3242 0.3213 0.2702 0.0879  0.0334  0.0232  61  ILE   B CD1 
10397 N  N   . VAL   B 62  ? 0.2511 0.1849 0.1666 0.0806  0.0339  0.0241  62  VAL   B N   
10398 C  CA  . VAL   B 62  ? 0.2322 0.1521 0.1473 0.0797  0.0346  0.0241  62  VAL   B CA  
10399 C  C   . VAL   B 62  ? 0.2393 0.1498 0.1511 0.0747  0.0341  0.0189  62  VAL   B C   
10400 O  O   . VAL   B 62  ? 0.2442 0.1571 0.1588 0.0707  0.0336  0.0168  62  VAL   B O   
10401 C  CB  . VAL   B 62  ? 0.2502 0.1640 0.1599 0.0803  0.0356  0.0284  62  VAL   B CB  
10402 C  CG1 . VAL   B 62  ? 0.2501 0.1649 0.1605 0.0755  0.0350  0.0287  62  VAL   B CG1 
10403 C  CG2 . VAL   B 62  ? 0.2665 0.1656 0.1729 0.0795  0.0376  0.0286  62  VAL   B CG2 
10413 N  N   . THR   B 63  ? 0.2287 0.1305 0.1394 0.0752  0.0345  0.0166  63  THR   B N   
10414 C  CA  . THR   B 63  ? 0.2403 0.1344 0.1503 0.0711  0.0334  0.0111  63  THR   B CA  
10415 C  C   . THR   B 63  ? 0.2525 0.1326 0.1601 0.0682  0.0346  0.0101  63  THR   B C   
10416 O  O   . THR   B 63  ? 0.2513 0.1283 0.1586 0.0700  0.0368  0.0144  63  THR   B O   
10417 C  CB  . THR   B 63  ? 0.2682 0.1616 0.1749 0.0738  0.0331  0.0082  63  THR   B CB  
10418 O  OG1 . THR   B 63  ? 0.2860 0.1707 0.1894 0.0768  0.0350  0.0093  63  THR   B OG1 
10419 C  CG2 . THR   B 63  ? 0.2811 0.1872 0.1889 0.0764  0.0327  0.0097  63  THR   B CG2 
10427 N  N   . GLY   B 64  ? 0.2614 0.1349 0.1700 0.0638  0.0334  0.0045  64  GLY   B N   
10428 C  CA  . GLY   B 64  ? 0.2746 0.1352 0.1833 0.0601  0.0349  0.0020  64  GLY   B CA  
10429 C  C   . GLY   B 64  ? 0.2690 0.1222 0.1785 0.0613  0.0354  -0.0033 64  GLY   B C   
10430 O  O   . GLY   B 64  ? 0.2848 0.1423 0.1891 0.0644  0.0339  -0.0056 64  GLY   B O   
10434 N  N   . PRO   B 65  ? 0.2737 0.1154 0.1884 0.0588  0.0379  -0.0056 65  PRO   B N   
10435 C  CA  . PRO   B 65  ? 0.3112 0.1434 0.2194 0.0592  0.0388  -0.0123 65  PRO   B CA  
10436 C  C   . PRO   B 65  ? 0.2765 0.1125 0.1892 0.0568  0.0348  -0.0212 65  PRO   B C   
10437 O  O   . PRO   B 65  ? 0.3056 0.1390 0.2096 0.0592  0.0348  -0.0261 65  PRO   B O   
10438 C  CB  . PRO   B 65  ? 0.3311 0.1518 0.2448 0.0552  0.0424  -0.0132 65  PRO   B CB  
10439 C  CG  . PRO   B 65  ? 0.2896 0.1139 0.2127 0.0513  0.0421  -0.0091 65  PRO   B CG  
10440 C  CD  . PRO   B 65  ? 0.3163 0.1503 0.2284 0.0552  0.0407  -0.0024 65  PRO   B CD  
10448 N  N   . LEU   B 66  ? 0.2996 0.1387 0.2098 0.0525  0.0318  -0.0232 66  LEU   B N   
10449 C  CA  . LEU   B 66  ? 0.3242 0.1659 0.2286 0.0504  0.0277  -0.0313 66  LEU   B CA  
10450 C  C   . LEU   B 66  ? 0.2952 0.1507 0.1999 0.0551  0.0255  -0.0288 66  LEU   B C   
10451 O  O   . LEU   B 66  ? 0.3111 0.1704 0.2085 0.0558  0.0223  -0.0346 66  LEU   B O   
10452 C  CB  . LEU   B 66  ? 0.3044 0.1451 0.2208 0.0432  0.0262  -0.0348 66  LEU   B CB  
10453 C  CG  . LEU   B 66  ? 0.3474 0.1759 0.2655 0.0378  0.0288  -0.0366 66  LEU   B CG  
10454 C  CD1 . LEU   B 66  ? 0.3028 0.1319 0.2331 0.0301  0.0266  -0.0410 66  LEU   B CD1 
10455 C  CD2 . LEU   B 66  ? 0.3598 0.1809 0.2815 0.0387  0.0308  -0.0426 66  LEU   B CD2 
10467 N  N   . THR   B 67  ? 0.2986 0.1603 0.2004 0.0585  0.0270  -0.0203 67  THR   B N   
10468 C  CA  . THR   B 67  ? 0.2883 0.1630 0.1885 0.0628  0.0259  -0.0173 67  THR   B CA  
10469 C  C   . THR   B 67  ? 0.3009 0.1761 0.1949 0.0670  0.0254  -0.0210 67  THR   B C   
10470 O  O   . THR   B 67  ? 0.2950 0.1642 0.1889 0.0691  0.0276  -0.0209 67  THR   B O   
10471 C  CB  . THR   B 67  ? 0.2633 0.1457 0.1684 0.0652  0.0279  -0.0090 67  THR   B CB  
10472 O  OG1 . THR   B 67  ? 0.2508 0.1321 0.1583 0.0613  0.0283  -0.0060 67  THR   B OG1 
10473 C  CG2 . THR   B 67  ? 0.2883 0.1834 0.1908 0.0682  0.0275  -0.0062 67  THR   B CG2 
10481 N  N   . GLY   B 68  ? 0.3029 0.1860 0.1955 0.0684  0.0230  -0.0243 68  GLY   B N   
10482 C  CA  . GLY   B 68  ? 0.3351 0.2194 0.2195 0.0727  0.0227  -0.0276 68  GLY   B CA  
10483 C  C   . GLY   B 68  ? 0.3518 0.2277 0.2315 0.0706  0.0211  -0.0377 68  GLY   B C   
10484 O  O   . GLY   B 68  ? 0.3590 0.2369 0.2333 0.0739  0.0205  -0.0417 68  GLY   B O   
10488 N  N   . ALA   B 69  ? 0.3430 0.2105 0.2284 0.0649  0.0206  -0.0426 69  ALA   B N   
10489 C  CA  . ALA   B 69  ? 0.3639 0.2227 0.2459 0.0613  0.0194  -0.0534 69  ALA   B CA  
10490 C  C   . ALA   B 69  ? 0.3567 0.2236 0.2347 0.0597  0.0140  -0.0609 69  ALA   B C   
10491 O  O   . ALA   B 69  ? 0.3319 0.2073 0.2124 0.0599  0.0118  -0.0567 69  ALA   B O   
10492 C  CB  . ALA   B 69  ? 0.3722 0.2190 0.2622 0.0558  0.0218  -0.0547 69  ALA   B CB  
10498 N  N   . PRO   B 70  ? 0.3652 0.2315 0.2403 0.0580  0.0114  -0.0719 70  PRO   B N   
10499 C  CA  . PRO   B 70  ? 0.3870 0.2635 0.2565 0.0567  0.0050  -0.0794 70  PRO   B CA  
10500 C  C   . PRO   B 70  ? 0.3858 0.2598 0.2587 0.0494  0.0013  -0.0838 70  PRO   B C   
10501 O  O   . PRO   B 70  ? 0.3344 0.2100 0.2145 0.0442  -0.0026 -0.0947 70  PRO   B O   
10502 C  CB  . PRO   B 70  ? 0.4098 0.2853 0.2740 0.0566  0.0043  -0.0895 70  PRO   B CB  
10503 C  CG  . PRO   B 70  ? 0.4385 0.2973 0.3036 0.0536  0.0104  -0.0911 70  PRO   B CG  
10504 C  CD  . PRO   B 70  ? 0.3750 0.2320 0.2513 0.0573  0.0147  -0.0784 70  PRO   B CD  
10512 N  N   . VAL   B 71  ? 0.3585 0.2348 0.2433 0.0473  0.0028  -0.0743 71  VAL   B N   
10513 C  CA  . VAL   B 71  ? 0.3278 0.2078 0.2272 0.0387  0.0003  -0.0739 71  VAL   B CA  
10514 C  C   . VAL   B 71  ? 0.3273 0.2218 0.2263 0.0401  -0.0008 -0.0641 71  VAL   B C   
10515 O  O   . VAL   B 71  ? 0.3119 0.2104 0.2084 0.0468  0.0021  -0.0565 71  VAL   B O   
10516 C  CB  . VAL   B 71  ? 0.3449 0.2083 0.2521 0.0337  0.0055  -0.0723 71  VAL   B CB  
10517 C  CG1 . VAL   B 71  ? 0.3959 0.2431 0.2992 0.0307  0.0073  -0.0828 71  VAL   B CG1 
10518 C  CG2 . VAL   B 71  ? 0.3551 0.2129 0.2585 0.0387  0.0109  -0.0613 71  VAL   B CG2 
10528 N  N   . PRO   B 72  ? 0.3092 0.2143 0.2217 0.0342  -0.0043 -0.0636 72  PRO   B N   
10529 C  CA  . PRO   B 72  ? 0.3108 0.2290 0.2221 0.0359  -0.0043 -0.0541 72  PRO   B CA  
10530 C  C   . PRO   B 72  ? 0.2563 0.1721 0.1784 0.0363  0.0015  -0.0435 72  PRO   B C   
10531 O  O   . PRO   B 72  ? 0.2759 0.1795 0.1987 0.0315  0.0041  -0.0429 72  PRO   B O   
10532 C  CB  . PRO   B 72  ? 0.3022 0.2296 0.2262 0.0287  -0.0088 -0.0572 72  PRO   B CB  
10533 C  CG  . PRO   B 72  ? 0.2949 0.2090 0.2261 0.0215  -0.0090 -0.0654 72  PRO   B CG  
10534 C  CD  . PRO   B 72  ? 0.3364 0.2386 0.2519 0.0256  -0.0079 -0.0718 72  PRO   B CD  
10542 N  N   . THR   B 73  ? 0.2566 0.1810 0.1736 0.0417  0.0040  -0.0356 73  THR   B N   
10543 C  CA  . THR   B 73  ? 0.2579 0.1812 0.1787 0.0418  0.0093  -0.0269 73  THR   B CA  
10544 C  C   . THR   B 73  ? 0.2626 0.1736 0.1772 0.0447  0.0126  -0.0257 73  THR   B C   
10545 O  O   . THR   B 73  ? 0.2518 0.1591 0.1734 0.0422  0.0160  -0.0212 73  THR   B O   
10546 C  CB  . THR   B 73  ? 0.2337 0.1587 0.1708 0.0340  0.0099  -0.0239 73  THR   B CB  
10547 O  OG1 . THR   B 73  ? 0.2576 0.1677 0.1916 0.0288  0.0104  -0.0267 73  THR   B OG1 
10548 C  CG2 . THR   B 73  ? 0.2693 0.2048 0.2064 0.0310  0.0062  -0.0251 73  THR   B CG2 
10556 N  N   . SER   B 74  ? 0.2341 0.1421 0.1455 0.0507  0.0125  -0.0296 74  SER   B N   
10557 C  CA  . SER   B 74  ? 0.2906 0.1856 0.1896 0.0542  0.0158  -0.0286 74  SER   B CA  
10558 C  C   . SER   B 74  ? 0.2536 0.1553 0.1551 0.0606  0.0196  -0.0216 74  SER   B C   
10559 O  O   . SER   B 74  ? 0.2398 0.1375 0.1389 0.0644  0.0212  -0.0205 74  SER   B O   
10560 C  CB  . SER   B 74  ? 0.3132 0.1995 0.2062 0.0571  0.0148  -0.0365 74  SER   B CB  
10561 O  OG  . SER   B 74  ? 0.3064 0.2014 0.1939 0.0627  0.0133  -0.0389 74  SER   B OG  
10567 N  N   . GLY   B 75  ? 0.2285 0.1427 0.1370 0.0603  0.0207  -0.0161 75  GLY   B N   
10568 C  CA  . GLY   B 75  ? 0.2337 0.1546 0.1420 0.0650  0.0243  -0.0103 75  GLY   B CA  
10569 C  C   . GLY   B 75  ? 0.2208 0.1430 0.1380 0.0616  0.0269  -0.0053 75  GLY   B C   
10570 O  O   . GLY   B 75  ? 0.2371 0.1682 0.1569 0.0626  0.0288  -0.0006 75  GLY   B O   
10574 N  N   . ARG   B 76  ? 0.2192 0.1332 0.1369 0.0563  0.0260  -0.0058 76  ARG   B N   
10575 C  CA  . ARG   B 76  ? 0.2114 0.1274 0.1358 0.0528  0.0284  -0.0016 76  ARG   B CA  
10576 C  C   . ARG   B 76  ? 0.2158 0.1272 0.1381 0.0567  0.0297  0.0007  76  ARG   B C   
10577 O  O   . ARG   B 76  ? 0.2523 0.1543 0.1664 0.0584  0.0286  -0.0009 76  ARG   B O   
10578 C  CB  . ARG   B 76  ? 0.2188 0.1303 0.1462 0.0451  0.0273  -0.0022 76  ARG   B CB  
10579 C  CG  . ARG   B 76  ? 0.2126 0.1302 0.1455 0.0412  0.0259  -0.0037 76  ARG   B CG  
10580 C  CD  . ARG   B 76  ? 0.2095 0.1397 0.1457 0.0421  0.0284  -0.0004 76  ARG   B CD  
10581 N  NE  . ARG   B 76  ? 0.1633 0.0987 0.1104 0.0389  0.0320  0.0033  76  ARG   B NE  
10582 C  CZ  . ARG   B 76  ? 0.1726 0.1171 0.1268 0.0364  0.0355  0.0062  76  ARG   B CZ  
10583 N  NH1 . ARG   B 76  ? 0.1951 0.1458 0.1500 0.0374  0.0358  0.0066  76  ARG   B NH1 
10584 N  NH2 . ARG   B 76  ? 0.1895 0.1369 0.1459 0.0336  0.0390  0.0081  76  ARG   B NH2 
10598 N  N   . PHE   B 77  ? 0.2234 0.1422 0.1466 0.0569  0.0317  0.0048  77  PHE   B N   
10599 C  CA  . PHE   B 77  ? 0.2109 0.1301 0.1351 0.0601  0.0324  0.0078  77  PHE   B CA  
10600 C  C   . PHE   B 77  ? 0.2112 0.1376 0.1373 0.0568  0.0338  0.0106  77  PHE   B C   
10601 O  O   . PHE   B 77  ? 0.1859 0.1187 0.1203 0.0514  0.0348  0.0098  77  PHE   B O   
10602 C  CB  . PHE   B 77  ? 0.2236 0.1493 0.1445 0.0644  0.0321  0.0088  77  PHE   B CB  
10603 C  CG  . PHE   B 77  ? 0.1937 0.1343 0.1254 0.0639  0.0332  0.0102  77  PHE   B CG  
10604 C  CD1 . PHE   B 77  ? 0.2022 0.1473 0.1347 0.0620  0.0335  0.0090  77  PHE   B CD1 
10605 C  CD2 . PHE   B 77  ? 0.1879 0.1370 0.1226 0.0652  0.0343  0.0124  77  PHE   B CD2 
10606 C  CE1 . PHE   B 77  ? 0.1898 0.1467 0.1318 0.0604  0.0350  0.0106  77  PHE   B CE1 
10607 C  CE2 . PHE   B 77  ? 0.1815 0.1428 0.1254 0.0632  0.0358  0.0127  77  PHE   B CE2 
10608 C  CZ  . PHE   B 77  ? 0.1857 0.1500 0.1326 0.0605  0.0361  0.0121  77  PHE   B CZ  
10618 N  N   . MET   B 78  ? 0.2042 0.1327 0.1302 0.0594  0.0340  0.0136  78  MET   B N   
10619 C  CA  . MET   B 78  ? 0.1883 0.1264 0.1210 0.0552  0.0346  0.0154  78  MET   B CA  
10620 C  C   . MET   B 78  ? 0.1848 0.1341 0.1174 0.0594  0.0345  0.0172  78  MET   B C   
10621 O  O   . MET   B 78  ? 0.2138 0.1603 0.1404 0.0664  0.0339  0.0192  78  MET   B O   
10622 C  CB  . MET   B 78  ? 0.2392 0.1668 0.1629 0.0517  0.0343  0.0172  78  MET   B CB  
10623 C  CG  . MET   B 78  ? 0.2308 0.1513 0.1599 0.0455  0.0347  0.0150  78  MET   B CG  
10624 S  SD  . MET   B 78  ? 0.2468 0.1582 0.1731 0.0404  0.0359  0.0178  78  MET   B SD  
10625 C  CE  . MET   B 78  ? 0.2667 0.1912 0.1925 0.0392  0.0370  0.0198  78  MET   B CE  
10635 N  N   . VAL   B 79  ? 0.1814 0.1430 0.1185 0.0553  0.0351  0.0165  79  VAL   B N   
10636 C  CA  . VAL   B 79  ? 0.1811 0.1566 0.1218 0.0582  0.0342  0.0173  79  VAL   B CA  
10637 C  C   . VAL   B 79  ? 0.2093 0.1836 0.1398 0.0563  0.0331  0.0198  79  VAL   B C   
10638 O  O   . VAL   B 79  ? 0.2073 0.1801 0.1415 0.0496  0.0342  0.0187  79  VAL   B O   
10639 C  CB  . VAL   B 79  ? 0.1838 0.1737 0.1313 0.0548  0.0363  0.0135  79  VAL   B CB  
10640 C  CG1 . VAL   B 79  ? 0.1751 0.1809 0.1278 0.0552  0.0348  0.0127  79  VAL   B CG1 
10641 C  CG2 . VAL   B 79  ? 0.1496 0.1414 0.1061 0.0585  0.0384  0.0122  79  VAL   B CG2 
10651 N  N   . VAL   B 80  ? 0.1789 0.1555 0.1083 0.0627  0.0312  0.0242  80  VAL   B N   
10652 C  CA  . VAL   B 80  ? 0.1826 0.1599 0.1040 0.0628  0.0304  0.0281  80  VAL   B CA  
10653 C  C   . VAL   B 80  ? 0.1836 0.1800 0.1061 0.0664  0.0279  0.0286  80  VAL   B C   
10654 O  O   . VAL   B 80  ? 0.2158 0.2165 0.1378 0.0732  0.0267  0.0305  80  VAL   B O   
10655 C  CB  . VAL   B 80  ? 0.1953 0.1555 0.1083 0.0676  0.0314  0.0337  80  VAL   B CB  
10656 C  CG1 . VAL   B 80  ? 0.1989 0.1600 0.1049 0.0688  0.0317  0.0389  80  VAL   B CG1 
10657 C  CG2 . VAL   B 80  ? 0.2068 0.1500 0.1194 0.0633  0.0333  0.0315  80  VAL   B CG2 
10667 N  N   . THR   B 81  ? 0.1612 0.1697 0.0852 0.0618  0.0271  0.0268  81  THR   B N   
10668 C  CA  . THR   B 81  ? 0.1833 0.2121 0.1050 0.0642  0.0239  0.0259  81  THR   B CA  
10669 C  C   . THR   B 81  ? 0.2004 0.2362 0.1156 0.0584  0.0236  0.0239  81  THR   B C   
10670 O  O   . THR   B 81  ? 0.1714 0.1965 0.0901 0.0522  0.0267  0.0230  81  THR   B O   
10671 C  CB  . THR   B 81  ? 0.1557 0.2007 0.0970 0.0624  0.0235  0.0195  81  THR   B CB  
10672 O  OG1 . THR   B 81  ? 0.2276 0.2915 0.1615 0.0653  0.0197  0.0186  81  THR   B OG1 
10673 C  CG2 . THR   B 81  ? 0.1793 0.2237 0.1215 0.0525  0.0269  0.0124  81  THR   B CG2 
10681 N  N   . LYS   B 82  ? 0.1675 0.2243 0.0874 0.0600  0.0202  0.0228  82  LYS   B N   
10682 C  CA  . LYS   B 82  ? 0.1823 0.2469 0.0957 0.0534  0.0205  0.0191  82  LYS   B CA  
10683 C  C   . LYS   B 82  ? 0.1652 0.2347 0.0900 0.0434  0.0233  0.0091  82  LYS   B C   
10684 O  O   . LYS   B 82  ? 0.1448 0.2257 0.0823 0.0430  0.0227  0.0044  82  LYS   B O   
10685 C  CB  . LYS   B 82  ? 0.2001 0.2855 0.1067 0.0580  0.0158  0.0200  82  LYS   B CB  
10686 C  CG  . LYS   B 82  ? 0.2011 0.2937 0.1024 0.0522  0.0162  0.0170  82  LYS   B CG  
10687 C  CD  . LYS   B 82  ? 0.2192 0.3327 0.1102 0.0569  0.0113  0.0177  82  LYS   B CD  
10688 C  CE  . LYS   B 82  ? 0.2214 0.3414 0.1072 0.0503  0.0124  0.0134  82  LYS   B CE  
10689 N  NZ  . LYS   B 82  ? 0.2504 0.3883 0.1274 0.0544  0.0071  0.0141  82  LYS   B NZ  
10703 N  N   . ALA   B 83  ? 0.1499 0.2117 0.0770 0.0355  0.0273  0.0065  83  ALA   B N   
10704 C  CA  . ALA   B 83  ? 0.1726 0.2360 0.1090 0.0261  0.0315  -0.0018 83  ALA   B CA  
10705 C  C   . ALA   B 83  ? 0.1674 0.2517 0.1081 0.0206  0.0311  -0.0107 83  ALA   B C   
10706 O  O   . ALA   B 83  ? 0.1729 0.2611 0.1041 0.0189  0.0303  -0.0106 83  ALA   B O   
10707 C  CB  . ALA   B 83  ? 0.2006 0.2461 0.1344 0.0207  0.0362  -0.0004 83  ALA   B CB  
10713 N  N   . PRO   B 84  ? 0.1531 0.2512 0.1100 0.0173  0.0321  -0.0184 84  PRO   B N   
10714 C  CA  . PRO   B 84  ? 0.1640 0.2817 0.1254 0.0110  0.0322  -0.0287 84  PRO   B CA  
10715 C  C   . PRO   B 84  ? 0.1365 0.2515 0.1026 0.0006  0.0384  -0.0349 84  PRO   B C   
10716 O  O   . PRO   B 84  ? 0.1715 0.2987 0.1305 -0.0035 0.0376  -0.0414 84  PRO   B O   
10717 C  CB  . PRO   B 84  ? 0.1885 0.3159 0.1656 0.0101  0.0339  -0.0343 84  PRO   B CB  
10718 C  CG  . PRO   B 84  ? 0.1830 0.2990 0.1599 0.0187  0.0323  -0.0258 84  PRO   B CG  
10719 C  CD  . PRO   B 84  ? 0.1594 0.2539 0.1267 0.0199  0.0336  -0.0181 84  PRO   B CD  
10727 N  N   . LEU   B 85  ? 0.1289 0.2261 0.0987 -0.0030 0.0448  -0.0333 85  LEU   B N   
10728 C  CA  . LEU   B 85  ? 0.1419 0.2318 0.1142 -0.0123 0.0505  -0.0372 85  LEU   B CA  
10729 C  C   . LEU   B 85  ? 0.1650 0.2505 0.1225 -0.0131 0.0500  -0.0346 85  LEU   B C   
10730 O  O   . LEU   B 85  ? 0.1699 0.2588 0.1284 -0.0193 0.0512  -0.0401 85  LEU   B O   
10731 C  CB  . LEU   B 85  ? 0.1157 0.1856 0.1013 -0.0134 0.0540  -0.0322 85  LEU   B CB  
10732 C  CG  . LEU   B 85  ? 0.1404 0.2007 0.1317 -0.0205 0.0579  -0.0335 85  LEU   B CG  
10733 C  CD1 . LEU   B 85  ? 0.1587 0.2269 0.1590 -0.0266 0.0591  -0.0417 85  LEU   B CD1 
10734 C  CD2 . LEU   B 85  ? 0.1791 0.2225 0.1716 -0.0190 0.0590  -0.0267 85  LEU   B CD2 
10746 N  N   . THR   B 86  ? 0.1766 0.2515 0.1191 -0.0060 0.0470  -0.0251 86  THR   B N   
10747 C  CA  . THR   B 86  ? 0.1593 0.2258 0.0907 -0.0061 0.0476  -0.0199 86  THR   B CA  
10748 C  C   . THR   B 86  ? 0.1562 0.2292 0.0758 0.0013  0.0404  -0.0154 86  THR   B C   
10749 O  O   . THR   B 86  ? 0.1744 0.2460 0.0784 0.0003  0.0417  -0.0142 86  THR   B O   
10750 C  CB  . THR   B 86  ? 0.1826 0.2255 0.1075 -0.0035 0.0495  -0.0114 86  THR   B CB  
10751 O  OG1 . THR   B 86  ? 0.1671 0.2082 0.0921 0.0053  0.0444  -0.0049 86  THR   B OG1 
10752 C  CG2 . THR   B 86  ? 0.1514 0.1862 0.0938 -0.0095 0.0553  -0.0135 86  THR   B CG2 
10760 N  N   . GLY   B 87  ? 0.2045 0.2883 0.1138 0.0092  0.0353  -0.0131 87  GLY   B N   
10761 C  CA  . GLY   B 87  ? 0.1784 0.2710 0.0786 0.0179  0.0298  -0.0065 87  GLY   B CA  
10762 C  C   . GLY   B 87  ? 0.1787 0.2501 0.0725 0.0245  0.0298  0.0053  87  GLY   B C   
10763 O  O   . GLY   B 87  ? 0.2110 0.2867 0.0869 0.0335  0.0273  0.0128  87  GLY   B O   
10767 N  N   . THR   B 88  ? 0.2046 0.2565 0.0985 0.0222  0.0347  0.0080  88  THR   B N   
10768 C  CA  . THR   B 88  ? 0.2162 0.2474 0.1040 0.0278  0.0362  0.0177  88  THR   B CA  
10769 C  C   . THR   B 88  ? 0.2145 0.2405 0.1076 0.0340  0.0337  0.0215  88  THR   B C   
10770 O  O   . THR   B 88  ? 0.2030 0.2423 0.1038 0.0354  0.0306  0.0172  88  THR   B O   
10771 C  CB  . THR   B 88  ? 0.1988 0.2128 0.0950 0.0205  0.0421  0.0175  88  THR   B CB  
10772 O  OG1 . THR   B 88  ? 0.1898 0.2003 0.0959 0.0166  0.0431  0.0131  88  THR   B OG1 
10773 C  CG2 . THR   B 88  ? 0.2590 0.2744 0.1467 0.0131  0.0462  0.0135  88  THR   B CG2 
10781 N  N   . ILE   B 89  ? 0.2221 0.2287 0.1113 0.0380  0.0355  0.0287  89  ILE   B N   
10782 C  CA  . ILE   B 89  ? 0.2086 0.2079 0.1068 0.0429  0.0344  0.0310  89  ILE   B CA  
10783 C  C   . ILE   B 89  ? 0.2238 0.2205 0.1254 0.0363  0.0353  0.0240  89  ILE   B C   
10784 O  O   . ILE   B 89  ? 0.1814 0.1756 0.0943 0.0284  0.0389  0.0205  89  ILE   B O   
10785 C  CB  . ILE   B 89  ? 0.2522 0.2286 0.1384 0.0466  0.0371  0.0384  89  ILE   B CB  
10786 C  CG1 . ILE   B 89  ? 0.2569 0.2251 0.1491 0.0516  0.0360  0.0399  89  ILE   B CG1 
10787 C  CG2 . ILE   B 89  ? 0.2120 0.1761 0.1053 0.0389  0.0416  0.0374  89  ILE   B CG2 
10788 C  CD1 . ILE   B 89  ? 0.2371 0.2147 0.1288 0.0610  0.0329  0.0438  89  ILE   B CD1 
10800 N  N   . GLY   B 90  ? 0.1727 0.1757 0.0888 0.0395  0.0334  0.0222  90  GLY   B N   
10801 C  CA  . GLY   B 90  ? 0.1761 0.1759 0.0997 0.0352  0.0350  0.0173  90  GLY   B CA  
10802 C  C   . GLY   B 90  ? 0.1768 0.1600 0.1010 0.0385  0.0353  0.0205  90  GLY   B C   
10803 O  O   . GLY   B 90  ? 0.2061 0.1857 0.1240 0.0458  0.0333  0.0245  90  GLY   B O   
10807 N  N   . ILE   B 91  ? 0.1605 0.1337 0.0908 0.0330  0.0379  0.0189  91  ILE   B N   
10808 C  CA  . ILE   B 91  ? 0.1982 0.1551 0.1239 0.0349  0.0381  0.0205  91  ILE   B CA  
10809 C  C   . ILE   B 91  ? 0.1848 0.1427 0.1220 0.0300  0.0398  0.0165  91  ILE   B C   
10810 O  O   . ILE   B 91  ? 0.1995 0.1520 0.1380 0.0240  0.0420  0.0157  91  ILE   B O   
10811 C  CB  . ILE   B 91  ? 0.2105 0.1530 0.1318 0.0345  0.0394  0.0248  91  ILE   B CB  
10812 C  CG1 . ILE   B 91  ? 0.2177 0.1614 0.1384 0.0281  0.0420  0.0247  91  ILE   B CG1 
10813 C  CG2 . ILE   B 91  ? 0.2199 0.1580 0.1329 0.0425  0.0382  0.0300  91  ILE   B CG2 
10814 C  CD1 . ILE   B 91  ? 0.2244 0.1527 0.1431 0.0257  0.0446  0.0275  91  ILE   B CD1 
10826 N  N   . SER   B 92  ? 0.1685 0.1331 0.1098 0.0329  0.0393  0.0144  92  SER   B N   
10827 C  CA  . SER   B 92  ? 0.1486 0.1165 0.1019 0.0298  0.0418  0.0115  92  SER   B CA  
10828 C  C   . SER   B 92  ? 0.1806 0.1393 0.1283 0.0343  0.0404  0.0119  92  SER   B C   
10829 O  O   . SER   B 92  ? 0.1877 0.1458 0.1319 0.0406  0.0384  0.0129  92  SER   B O   
10830 C  CB  . SER   B 92  ? 0.1608 0.1430 0.1196 0.0288  0.0440  0.0083  92  SER   B CB  
10831 O  OG  . SER   B 92  ? 0.1899 0.1797 0.1473 0.0243  0.0448  0.0067  92  SER   B OG  
10837 N  N   . ASN   B 93  ? 0.1858 0.1395 0.1361 0.0309  0.0414  0.0112  93  ASN   B N   
10838 C  CA  . ASN   B 93  ? 0.1632 0.1102 0.1147 0.0346  0.0396  0.0107  93  ASN   B CA  
10839 C  C   . ASN   B 93  ? 0.1768 0.1304 0.1305 0.0365  0.0414  0.0098  93  ASN   B C   
10840 O  O   . ASN   B 93  ? 0.1659 0.1275 0.1291 0.0326  0.0452  0.0098  93  ASN   B O   
10841 C  CB  . ASN   B 93  ? 0.1767 0.1120 0.1220 0.0305  0.0383  0.0106  93  ASN   B CB  
10842 C  CG  . ASN   B 93  ? 0.1518 0.0800 0.1005 0.0338  0.0355  0.0087  93  ASN   B CG  
10843 O  OD1 . ASN   B 93  ? 0.1871 0.1178 0.1296 0.0361  0.0349  0.0073  93  ASN   B OD1 
10844 N  ND2 . ASN   B 93  ? 0.2132 0.1281 0.1480 0.0342  0.0340  0.0085  93  ASN   B ND2 
10851 N  N   . SER   B 94  ? 0.1807 0.1320 0.1306 0.0426  0.0400  0.0093  94  SER   B N   
10852 C  CA  . SER   B 94  ? 0.1639 0.1225 0.1192 0.0450  0.0415  0.0095  94  SER   B CA  
10853 C  C   . SER   B 94  ? 0.1734 0.1258 0.1220 0.0491  0.0386  0.0083  94  SER   B C   
10854 O  O   . SER   B 94  ? 0.1884 0.1306 0.1279 0.0518  0.0361  0.0066  94  SER   B O   
10855 C  CB  . SER   B 94  ? 0.1448 0.1134 0.1072 0.0462  0.0415  0.0104  94  SER   B CB  
10856 O  OG  . SER   B 94  ? 0.1590 0.1340 0.1259 0.0448  0.0421  0.0112  94  SER   B OG  
10862 N  N   . GLY   B 95  ? 0.1721 0.1304 0.1233 0.0493  0.0390  0.0089  95  GLY   B N   
10863 C  CA  . GLY   B 95  ? 0.1722 0.1270 0.1169 0.0538  0.0364  0.0071  95  GLY   B CA  
10864 C  C   . GLY   B 95  ? 0.1754 0.1374 0.1206 0.0571  0.0360  0.0093  95  GLY   B C   
10865 O  O   . GLY   B 95  ? 0.1844 0.1476 0.1296 0.0581  0.0360  0.0104  95  GLY   B O   
10869 N  N   . GLY   B 96  ? 0.1786 0.1451 0.1233 0.0598  0.0362  0.0100  96  GLY   B N   
10870 C  CA  . GLY   B 96  ? 0.1895 0.1606 0.1320 0.0634  0.0363  0.0125  96  GLY   B CA  
10871 C  C   . GLY   B 96  ? 0.1951 0.1597 0.1265 0.0687  0.0335  0.0094  96  GLY   B C   
10872 O  O   . GLY   B 96  ? 0.2034 0.1626 0.1272 0.0707  0.0308  0.0051  96  GLY   B O   
10876 N  N   . LYS   B 97  ? 0.1812 0.1469 0.1140 0.0701  0.0339  0.0112  97  LYS   B N   
10877 C  CA  . LYS   B 97  ? 0.1985 0.1580 0.1216 0.0751  0.0322  0.0091  97  LYS   B CA  
10878 C  C   . LYS   B 97  ? 0.2121 0.1674 0.1332 0.0748  0.0319  0.0090  97  LYS   B C   
10879 O  O   . LYS   B 97  ? 0.2288 0.1772 0.1434 0.0778  0.0311  0.0069  97  LYS   B O   
10880 C  CB  . LYS   B 97  ? 0.2225 0.1873 0.1449 0.0799  0.0331  0.0114  97  LYS   B CB  
10881 C  CG  . LYS   B 97  ? 0.3186 0.2878 0.2332 0.0814  0.0332  0.0125  97  LYS   B CG  
10882 C  CD  . LYS   B 97  ? 0.3406 0.3086 0.2541 0.0854  0.0297  0.0072  97  LYS   B CD  
10883 C  CE  . LYS   B 97  ? 0.4700 0.4414 0.3628 0.0918  0.0294  0.0086  97  LYS   B CE  
10884 N  NZ  . LYS   B 97  ? 0.3833 0.3668 0.2983 0.0913  0.0330  0.0160  97  LYS   B NZ  
10898 N  N   . TRP   B 98  ? 0.2124 0.1252 0.1131 0.0603  0.0011  -0.0025 98  TRP   B N   
10899 C  CA  . TRP   B 98  ? 0.2063 0.1257 0.1112 0.0624  0.0058  0.0004  98  TRP   B CA  
10900 C  C   . TRP   B 98  ? 0.2207 0.1408 0.1273 0.0641  0.0062  0.0003  98  TRP   B C   
10901 O  O   . TRP   B 98  ? 0.2160 0.1368 0.1200 0.0685  0.0094  0.0024  98  TRP   B O   
10902 C  CB  . TRP   B 98  ? 0.2136 0.1408 0.1234 0.0595  0.0077  0.0018  98  TRP   B CB  
10903 C  CG  . TRP   B 98  ? 0.1849 0.1197 0.0991 0.0648  0.0127  0.0053  98  TRP   B CG  
10904 C  CD1 . TRP   B 98  ? 0.2017 0.1373 0.1079 0.0693  0.0172  0.0081  98  TRP   B CD1 
10905 C  CD2 . TRP   B 98  ? 0.1864 0.1277 0.1052 0.0664  0.0137  0.0067  98  TRP   B CD2 
10906 N  NE1 . TRP   B 98  ? 0.1873 0.1334 0.1008 0.0737  0.0202  0.0108  98  TRP   B NE1 
10907 C  CE2 . TRP   B 98  ? 0.1922 0.1407 0.1091 0.0723  0.0180  0.0100  98  TRP   B CE2 
10908 C  CE3 . TRP   B 98  ? 0.2052 0.1463 0.1264 0.0642  0.0120  0.0058  98  TRP   B CE3 
10909 C  CZ2 . TRP   B 98  ? 0.1943 0.1515 0.1160 0.0757  0.0194  0.0122  98  TRP   B CZ2 
10910 C  CZ3 . TRP   B 98  ? 0.1721 0.1202 0.1005 0.0675  0.0143  0.0083  98  TRP   B CZ3 
10911 C  CH2 . TRP   B 98  ? 0.1936 0.1487 0.1169 0.0735  0.0173  0.0113  98  TRP   B CH2 
10922 N  N   . GLY   B 99  ? 0.2319 0.1519 0.1453 0.0610  0.0037  -0.0013 99  GLY   B N   
10923 C  CA  . GLY   B 99  ? 0.2240 0.1443 0.1437 0.0625  0.0051  -0.0010 99  GLY   B CA  
10924 C  C   . GLY   B 99  ? 0.2388 0.1521 0.1532 0.0660  0.0046  -0.0022 99  GLY   B C   
10925 O  O   . GLY   B 99  ? 0.2530 0.1659 0.1666 0.0689  0.0074  -0.0008 99  GLY   B O   
10929 N  N   . VAL   B 100 ? 0.2545 0.1610 0.1617 0.0661  0.0005  -0.0050 100 VAL   B N   
10930 C  CA  . VAL   B 100 ? 0.2597 0.1582 0.1610 0.0697  -0.0011 -0.0071 100 VAL   B CA  
10931 C  C   . VAL   B 100 ? 0.2573 0.1553 0.1489 0.0751  0.0031  -0.0042 100 VAL   B C   
10932 O  O   . VAL   B 100 ? 0.2612 0.1555 0.1502 0.0786  0.0045  -0.0043 100 VAL   B O   
10933 C  CB  . VAL   B 100 ? 0.2679 0.1594 0.1662 0.0691  -0.0078 -0.0114 100 VAL   B CB  
10934 C  CG1 . VAL   B 100 ? 0.2794 0.1619 0.1680 0.0737  -0.0104 -0.0137 100 VAL   B CG1 
10935 C  CG2 . VAL   B 100 ? 0.2776 0.1703 0.1869 0.0642  -0.0118 -0.0142 100 VAL   B CG2 
10945 N  N   . ASP   B 101 ? 0.2543 0.1557 0.1403 0.0756  0.0059  -0.0015 101 ASP   B N   
10946 C  CA  . ASP   B 101 ? 0.2446 0.1472 0.1247 0.0808  0.0115  0.0019  101 ASP   B CA  
10947 C  C   . ASP   B 101 ? 0.2528 0.1625 0.1373 0.0824  0.0156  0.0047  101 ASP   B C   
10948 O  O   . ASP   B 101 ? 0.2331 0.1422 0.1170 0.0874  0.0188  0.0063  101 ASP   B O   
10949 C  CB  . ASP   B 101 ? 0.2317 0.1366 0.1103 0.0808  0.0140  0.0041  101 ASP   B CB  
10950 C  CG  . ASP   B 101 ? 0.2933 0.1864 0.1535 0.0836  0.0130  0.0036  101 ASP   B CG  
10951 O  OD1 . ASP   B 101 ? 0.3053 0.1944 0.1579 0.0886  0.0168  0.0057  101 ASP   B OD1 
10952 O  OD2 . ASP   B 101 ? 0.3254 0.2133 0.1811 0.0810  0.0082  0.0013  101 ASP   B OD2 
10957 N  N   . LEU   B 102 ? 0.2323 0.1502 0.1288 0.0793  0.0156  0.0055  102 LEU   B N   
10958 C  CA  . LEU   B 102 ? 0.2066 0.1321 0.1129 0.0816  0.0187  0.0081  102 LEU   B CA  
10959 C  C   . LEU   B 102 ? 0.2380 0.1555 0.1375 0.0839  0.0187  0.0073  102 LEU   B C   
10960 O  O   . LEU   B 102 ? 0.2357 0.1548 0.1349 0.0886  0.0222  0.0096  102 LEU   B O   
10961 C  CB  . LEU   B 102 ? 0.2271 0.1581 0.1357 0.0780  0.0178  0.0087  102 LEU   B CB  
10962 C  CG  . LEU   B 102 ? 0.2009 0.1394 0.1187 0.0809  0.0205  0.0116  102 LEU   B CG  
10963 C  CD1 . LEU   B 102 ? 0.2198 0.1663 0.1342 0.0855  0.0235  0.0146  102 LEU   B CD1 
10964 C  CD2 . LEU   B 102 ? 0.2200 0.1618 0.1393 0.0776  0.0194  0.0118  102 LEU   B CD2 
10976 N  N   . LYS   B 103 ? 0.2453 0.1554 0.1466 0.0809  0.0151  0.0036  103 LYS   B N   
10977 C  CA  . LYS   B 103 ? 0.2281 0.1332 0.1399 0.0825  0.0147  0.0019  103 LYS   B CA  
10978 C  C   . LYS   B 103 ? 0.2968 0.1930 0.1880 0.0875  0.0154  0.0013  103 LYS   B C   
10979 O  O   . LYS   B 103 ? 0.3091 0.2030 0.2016 0.0912  0.0183  0.0022  103 LYS   B O   
10980 C  CB  . LYS   B 103 ? 0.3062 0.2046 0.2189 0.0779  0.0104  -0.0024 103 LYS   B CB  
10981 C  CG  . LYS   B 103 ? 0.3953 0.2860 0.3067 0.0782  0.0111  -0.0039 103 LYS   B CG  
10982 C  CD  . LYS   B 103 ? 0.3146 0.2110 0.2454 0.0773  0.0147  -0.0013 103 LYS   B CD  
10983 C  CE  . LYS   B 103 ? 0.3119 0.2002 0.2468 0.0774  0.0159  -0.0031 103 LYS   B CE  
10984 N  NZ  . LYS   B 103 ? 0.2917 0.1766 0.2403 0.0728  0.0121  -0.0082 103 LYS   B NZ  
10998 N  N   . LYS   B 104 ? 0.2938 0.1877 0.1806 0.0878  0.0134  0.0000  104 LYS   B N   
10999 C  CA  . LYS   B 104 ? 0.3157 0.2019 0.1893 0.0932  0.0142  -0.0002 104 LYS   B CA  
11000 C  C   . LYS   B 104 ? 0.3163 0.2083 0.1878 0.0979  0.0208  0.0046  104 LYS   B C   
11001 O  O   . LYS   B 104 ? 0.3684 0.2541 0.2289 0.1029  0.0230  0.0050  104 LYS   B O   
11002 C  CB  . LYS   B 104 ? 0.3306 0.2104 0.1946 0.0928  0.0101  -0.0026 104 LYS   B CB  
11003 C  CG  . LYS   B 104 ? 0.3313 0.2062 0.2008 0.0893  0.0028  -0.0078 104 LYS   B CG  
11004 C  CD  . LYS   B 104 ? 0.3954 0.2633 0.2556 0.0905  -0.0023 -0.0100 104 LYS   B CD  
11005 C  CE  . LYS   B 104 ? 0.5522 0.4103 0.4018 0.0896  -0.0104 -0.0157 104 LYS   B CE  
11006 N  NZ  . LYS   B 104 ? 0.5614 0.4189 0.4140 0.0878  -0.0165 -0.0178 104 LYS   B NZ  
11020 N  N   . ALA   B 105 ? 0.2799 0.1831 0.1589 0.0966  0.0236  0.0080  105 ALA   B N   
11021 C  CA  . ALA   B 105 ? 0.2728 0.1840 0.1539 0.1012  0.0292  0.0123  105 ALA   B CA  
11022 C  C   . ALA   B 105 ? 0.2869 0.1995 0.1692 0.1042  0.0313  0.0139  105 ALA   B C   
11023 O  O   . ALA   B 105 ? 0.2983 0.2170 0.1817 0.1089  0.0354  0.0174  105 ALA   B O   
11024 C  CB  . ALA   B 105 ? 0.2853 0.2070 0.1707 0.0990  0.0303  0.0146  105 ALA   B CB  
11030 N  N   . GLY   B 106 ? 0.2791 0.1866 0.1647 0.1019  0.0290  0.0118  106 GLY   B N   
11031 C  CA  . GLY   B 106 ? 0.2715 0.1785 0.1601 0.1050  0.0312  0.0136  106 GLY   B CA  
11032 C  C   . GLY   B 106 ? 0.2736 0.1878 0.1674 0.1034  0.0320  0.0159  106 GLY   B C   
11033 O  O   . GLY   B 106 ? 0.2718 0.1861 0.1676 0.1068  0.0346  0.0181  106 GLY   B O   
11037 N  N   . TRP   B 107 ? 0.2497 0.1701 0.1499 0.0987  0.0296  0.0154  107 TRP   B N   
11038 C  CA  . TRP   B 107 ? 0.2335 0.1613 0.1399 0.0977  0.0300  0.0175  107 TRP   B CA  
11039 C  C   . TRP   B 107 ? 0.2511 0.1740 0.1605 0.0919  0.0275  0.0152  107 TRP   B C   
11040 O  O   . TRP   B 107 ? 0.2643 0.1847 0.1746 0.0874  0.0242  0.0121  107 TRP   B O   
11041 C  CB  . TRP   B 107 ? 0.2235 0.1637 0.1345 0.0977  0.0298  0.0192  107 TRP   B CB  
11042 C  CG  . TRP   B 107 ? 0.2708 0.2160 0.1744 0.1028  0.0324  0.0215  107 TRP   B CG  
11043 C  CD1 . TRP   B 107 ? 0.2582 0.2056 0.1659 0.1030  0.0331  0.0211  107 TRP   B CD1 
11044 C  CD2 . TRP   B 107 ? 0.2469 0.1995 0.1563 0.1092  0.0352  0.0247  107 TRP   B CD2 
11045 N  NE1 . TRP   B 107 ? 0.2651 0.2187 0.1717 0.1095  0.0368  0.0240  107 TRP   B NE1 
11046 C  CE2 . TRP   B 107 ? 0.2614 0.2185 0.1679 0.1129  0.0375  0.0262  107 TRP   B CE2 
11047 C  CE3 . TRP   B 107 ? 0.2200 0.1743 0.1322 0.1128  0.0364  0.0271  107 TRP   B CE3 
11048 C  CZ2 . TRP   B 107 ? 0.2129 0.1810 0.1302 0.1144  0.0389  0.0287  107 TRP   B CZ2 
11049 C  CZ3 . TRP   B 107 ? 0.2718 0.2321 0.1797 0.1194  0.0386  0.0299  107 TRP   B CZ3 
11050 C  CH2 . TRP   B 107 ? 0.2829 0.2491 0.1910 0.1228  0.0404  0.0307  107 TRP   B CH2 
11061 N  N   . ASP   B 108 ? 0.2518 0.1728 0.1619 0.0926  0.0293  0.0168  108 ASP   B N   
11062 C  CA  . ASP   B 108 ? 0.2156 0.1342 0.1383 0.0875  0.0281  0.0154  108 ASP   B CA  
11063 C  C   . ASP   B 108 ? 0.2263 0.1516 0.1439 0.0855  0.0274  0.0167  108 ASP   B C   
11064 O  O   . ASP   B 108 ? 0.2259 0.1501 0.1496 0.0803  0.0253  0.0147  108 ASP   B O   
11065 C  CB  . ASP   B 108 ? 0.2807 0.1906 0.1980 0.0893  0.0315  0.0166  108 ASP   B CB  
11066 C  CG  . ASP   B 108 ? 0.3228 0.2231 0.2371 0.0911  0.0324  0.0148  108 ASP   B CG  
11067 O  OD1 . ASP   B 108 ? 0.3114 0.2069 0.2356 0.0874  0.0292  0.0104  108 ASP   B OD1 
11068 O  OD2 . ASP   B 108 ? 0.2913 0.1918 0.2062 0.0968  0.0358  0.0178  108 ASP   B OD2 
11073 N  N   . MET   B 109 ? 0.2072 0.1419 0.1248 0.0898  0.0285  0.0196  109 MET   B N   
11074 C  CA  . MET   B 109 ? 0.2120 0.1547 0.1326 0.0889  0.0276  0.0209  109 MET   B CA  
11075 C  C   . MET   B 109 ? 0.2492 0.2030 0.1652 0.0930  0.0270  0.0224  109 MET   B C   
11076 O  O   . MET   B 109 ? 0.2389 0.1956 0.1557 0.0981  0.0288  0.0242  109 MET   B O   
11077 C  CB  . MET   B 109 ? 0.2371 0.1754 0.1522 0.0910  0.0304  0.0233  109 MET   B CB  
11078 C  CG  . MET   B 109 ? 0.2535 0.1983 0.1674 0.0916  0.0297  0.0247  109 MET   B CG  
11079 S  SD  . MET   B 109 ? 0.2522 0.1890 0.1625 0.0936  0.0340  0.0276  109 MET   B SD  
11080 C  CE  . MET   B 109 ? 0.2637 0.1965 0.1671 0.1014  0.0382  0.0309  109 MET   B CE  
11090 N  N   . ILE   B 110 ? 0.2453 0.2077 0.1672 0.0905  0.0243  0.0217  110 ILE   B N   
11091 C  CA  . ILE   B 110 ? 0.2282 0.2036 0.1511 0.0958  0.0239  0.0233  110 ILE   B CA  
11092 C  C   . ILE   B 110 ? 0.2127 0.1938 0.1347 0.0985  0.0227  0.0242  110 ILE   B C   
11093 O  O   . ILE   B 110 ? 0.2002 0.1775 0.1232 0.0939  0.0215  0.0229  110 ILE   B O   
11094 C  CB  . ILE   B 110 ? 0.2074 0.1892 0.1379 0.0939  0.0225  0.0217  110 ILE   B CB  
11095 C  CG1 . ILE   B 110 ? 0.2396 0.2121 0.1629 0.0913  0.0236  0.0205  110 ILE   B CG1 
11096 C  CG2 . ILE   B 110 ? 0.2159 0.2124 0.1474 0.0997  0.0222  0.0233  110 ILE   B CG2 
11097 C  CD1 . ILE   B 110 ? 0.2169 0.1933 0.1453 0.0903  0.0235  0.0196  110 ILE   B CD1 
11109 N  N   . ILE   B 111 ? 0.1975 0.1874 0.1197 0.1058  0.0228  0.0266  111 ILE   B N   
11110 C  CA  . ILE   B 111 ? 0.2020 0.1994 0.1251 0.1098  0.0208  0.0272  111 ILE   B CA  
11111 C  C   . ILE   B 111 ? 0.2153 0.2300 0.1426 0.1134  0.0169  0.0265  111 ILE   B C   
11112 O  O   . ILE   B 111 ? 0.2400 0.2627 0.1688 0.1187  0.0168  0.0280  111 ILE   B O   
11113 C  CB  . ILE   B 111 ? 0.2709 0.2618 0.1777 0.1160  0.0230  0.0298  111 ILE   B CB  
11114 C  CG1 . ILE   B 111 ? 0.2580 0.2341 0.1667 0.1125  0.0273  0.0308  111 ILE   B CG1 
11115 C  CG2 . ILE   B 111 ? 0.2581 0.2559 0.1663 0.1209  0.0207  0.0300  111 ILE   B CG2 
11116 C  CD1 . ILE   B 111 ? 0.2858 0.2558 0.1841 0.1191  0.0308  0.0338  111 ILE   B CD1 
11128 N  N   . VAL   B 112 ? 0.2139 0.2352 0.1455 0.1103  0.0134  0.0243  112 VAL   B N   
11129 C  CA  . VAL   B 112 ? 0.2178 0.2580 0.1570 0.1129  0.0090  0.0229  112 VAL   B CA  
11130 C  C   . VAL   B 112 ? 0.2106 0.2608 0.1523 0.1180  0.0043  0.0224  112 VAL   B C   
11131 O  O   . VAL   B 112 ? 0.2248 0.2670 0.1569 0.1162  0.0034  0.0217  112 VAL   B O   
11132 C  CB  . VAL   B 112 ? 0.1909 0.2360 0.1425 0.1068  0.0077  0.0207  112 VAL   B CB  
11133 C  CG1 . VAL   B 112 ? 0.2035 0.2699 0.1647 0.1087  0.0039  0.0190  112 VAL   B CG1 
11134 C  CG2 . VAL   B 112 ? 0.2127 0.2451 0.1587 0.1025  0.0122  0.0209  112 VAL   B CG2 
11144 N  N   . GLU   B 113 ? 0.2306 0.2954 0.1744 0.1243  0.0009  0.0226  113 GLU   B N   
11145 C  CA  . GLU   B 113 ? 0.2122 0.2860 0.1574 0.1302  -0.0047 0.0218  113 GLU   B CA  
11146 C  C   . GLU   B 113 ? 0.2117 0.3084 0.1694 0.1305  -0.0126 0.0180  113 GLU   B C   
11147 O  O   . GLU   B 113 ? 0.2043 0.3132 0.1764 0.1285  -0.0123 0.0171  113 GLU   B O   
11148 C  CB  . GLU   B 113 ? 0.2224 0.2944 0.1609 0.1384  -0.0033 0.0246  113 GLU   B CB  
11149 C  CG  . GLU   B 113 ? 0.2522 0.3039 0.1783 0.1386  0.0040  0.0278  113 GLU   B CG  
11150 C  CD  . GLU   B 113 ? 0.2933 0.3431 0.2102 0.1469  0.0057  0.0308  113 GLU   B CD  
11151 O  OE1 . GLU   B 113 ? 0.2786 0.3437 0.2094 0.1509  0.0028  0.0308  113 GLU   B OE1 
11152 O  OE2 . GLU   B 113 ? 0.2718 0.3080 0.1815 0.1494  0.0100  0.0331  113 GLU   B OE2 
11159 N  N   . ASP   B 114 ? 0.2186 0.3210 0.1740 0.1327  -0.0191 0.0155  114 ASP   B N   
11160 C  CA  . ASP   B 114 ? 0.2213 0.3467 0.1902 0.1328  -0.0281 0.0108  114 ASP   B CA  
11161 C  C   . ASP   B 114 ? 0.2096 0.3460 0.1929 0.1241  -0.0293 0.0073  114 ASP   B C   
11162 O  O   . ASP   B 114 ? 0.1751 0.2992 0.1555 0.1185  -0.0252 0.0081  114 ASP   B O   
11163 C  CB  . ASP   B 114 ? 0.2105 0.3520 0.1933 0.1395  -0.0310 0.0107  114 ASP   B CB  
11164 C  CG  . ASP   B 114 ? 0.2579 0.4148 0.2403 0.1436  -0.0415 0.0064  114 ASP   B CG  
11165 O  OD1 . ASP   B 114 ? 0.2075 0.3790 0.2091 0.1363  -0.0466 0.0010  114 ASP   B OD1 
11166 O  OD2 . ASP   B 114 ? 0.2793 0.4338 0.2551 0.1522  -0.0439 0.0080  114 ASP   B OD2 
11171 N  N   . LYS   B 115 ? 0.2064 0.3663 0.2101 0.1229  -0.0343 0.0032  115 LYS   B N   
11172 C  CA  . LYS   B 115 ? 0.1786 0.3526 0.2026 0.1142  -0.0352 -0.0014 115 LYS   B CA  
11173 C  C   . LYS   B 115 ? 0.1840 0.3779 0.2272 0.1133  -0.0338 -0.0035 115 LYS   B C   
11174 O  O   . LYS   B 115 ? 0.1640 0.3606 0.2151 0.1133  -0.0363 -0.0046 115 LYS   B O   
11175 C  CB  . LYS   B 115 ? 0.1757 0.3573 0.2006 0.1103  -0.0441 -0.0072 115 LYS   B CB  
11176 C  CG  . LYS   B 115 ? 0.1926 0.3934 0.2373 0.1008  -0.0470 -0.0138 115 LYS   B CG  
11177 C  CD  . LYS   B 115 ? 0.2155 0.4233 0.2620 0.0966  -0.0565 -0.0205 115 LYS   B CD  
11178 C  CE  . LYS   B 115 ? 0.2348 0.4564 0.3002 0.0849  -0.0576 -0.0272 115 LYS   B CE  
11179 N  NZ  . LYS   B 115 ? 0.2837 0.5124 0.3488 0.0804  -0.0677 -0.0347 115 LYS   B NZ  
11193 N  N   . ALA   B 116 ? 0.1428 0.3327 0.2016 0.1013  -0.0257 -0.0043 116 ALA   B N   
11194 C  CA  . ALA   B 116 ? 0.1496 0.3693 0.2363 0.1046  -0.0237 -0.0067 116 ALA   B CA  
11195 C  C   . ALA   B 116 ? 0.1484 0.3916 0.2575 0.0980  -0.0313 -0.0146 116 ALA   B C   
11196 O  O   . ALA   B 116 ? 0.1364 0.3695 0.2373 0.0888  -0.0344 -0.0177 116 ALA   B O   
11197 C  CB  . ALA   B 116 ? 0.1722 0.3851 0.2606 0.1004  -0.0121 -0.0044 116 ALA   B CB  
11203 N  N   . ASP   B 117 ? 0.1798 0.4426 0.3097 0.0984  -0.0323 -0.0179 117 ASP   B N   
11204 C  CA  . ASP   B 117 ? 0.1609 0.4470 0.3204 0.0913  -0.0395 -0.0262 117 ASP   B CA  
11205 C  C   . ASP   B 117 ? 0.1503 0.4409 0.3228 0.0787  -0.0316 -0.0296 117 ASP   B C   
11206 O  O   . ASP   B 117 ? 0.1977 0.5029 0.3857 0.0701  -0.0363 -0.0371 117 ASP   B O   
11207 C  CB  . ASP   B 117 ? 0.2089 0.5133 0.3860 0.0955  -0.0422 -0.0282 117 ASP   B CB  
11208 C  CG  . ASP   B 117 ? 0.2392 0.5466 0.4369 0.0986  -0.0304 -0.0236 117 ASP   B CG  
11209 O  OD1 . ASP   B 117 ? 0.2900 0.5822 0.4695 0.0955  -0.0192 -0.0198 117 ASP   B OD1 
11210 O  OD2 . ASP   B 117 ? 0.4025 0.7185 0.5976 0.1042  -0.0321 -0.0237 117 ASP   B OD2 
11215 N  N   A SER   B 118 ? 0.1347 0.4136 0.3011 0.0776  -0.0192 -0.0249 118 SER   B N   
11216 N  N   B SER   B 118 ? 0.1343 0.4132 0.3007 0.0776  -0.0192 -0.0249 118 SER   B N   
11217 C  CA  A SER   B 118 ? 0.1146 0.3817 0.2873 0.0628  -0.0086 -0.0253 118 SER   B CA  
11218 C  CA  B SER   B 118 ? 0.1146 0.3816 0.2872 0.0628  -0.0085 -0.0253 118 SER   B CA  
11219 C  C   A SER   B 118 ? 0.1256 0.3831 0.2800 0.0676  -0.0004 -0.0208 118 SER   B C   
11220 C  C   B SER   B 118 ? 0.1255 0.3829 0.2797 0.0676  -0.0004 -0.0208 118 SER   B C   
11221 O  O   A SER   B 118 ? 0.1461 0.3889 0.2820 0.0774  0.0009  -0.0145 118 SER   B O   
11222 O  O   B SER   B 118 ? 0.1465 0.3893 0.2824 0.0774  0.0009  -0.0145 118 SER   B O   
11223 C  CB  A SER   B 118 ? 0.1190 0.4076 0.3213 0.0604  0.0006  -0.0277 118 SER   B CB  
11224 C  CB  B SER   B 118 ? 0.1188 0.4070 0.3192 0.0605  0.0006  -0.0274 118 SER   B CB  
11225 O  OG  A SER   B 118 ? 0.1315 0.4308 0.3512 0.0484  0.0080  -0.0329 118 SER   B OG  
11226 O  OG  B SER   B 118 ? 0.1221 0.4018 0.3185 0.0688  0.0080  -0.0212 118 SER   B OG  
11237 N  N   . PRO   B 119 ? 0.1179 0.3613 0.2714 0.0557  0.0063  -0.0215 119 PRO   B N   
11238 C  CA  . PRO   B 119 ? 0.1453 0.3570 0.2680 0.0555  0.0134  -0.0153 119 PRO   B CA  
11239 C  C   . PRO   B 119 ? 0.1376 0.3421 0.2539 0.0634  0.0236  -0.0091 119 PRO   B C   
11240 O  O   . PRO   B 119 ? 0.1078 0.3219 0.2436 0.0612  0.0319  -0.0095 119 PRO   B O   
11241 C  CB  . PRO   B 119 ? 0.1555 0.3581 0.2796 0.0414  0.0193  -0.0180 119 PRO   B CB  
11242 C  CG  . PRO   B 119 ? 0.1277 0.3498 0.2726 0.0345  0.0097  -0.0258 119 PRO   B CG  
11243 C  CD  . PRO   B 119 ? 0.1605 0.4080 0.3162 0.0430  0.0025  -0.0283 119 PRO   B CD  
11251 N  N   . VAL   B 120 ? 0.1225 0.3077 0.2179 0.0719  0.0233  -0.0037 120 VAL   B N   
11252 C  CA  . VAL   B 120 ? 0.1153 0.2845 0.2016 0.0771  0.0309  0.0016  120 VAL   B CA  
11253 C  C   . VAL   B 120 ? 0.1368 0.2814 0.1967 0.0810  0.0355  0.0056  120 VAL   B C   
11254 O  O   . VAL   B 120 ? 0.1432 0.2760 0.1913 0.0767  0.0293  0.0048  120 VAL   B O   
11255 C  CB  . VAL   B 120 ? 0.1459 0.3280 0.2325 0.0908  0.0267  0.0035  120 VAL   B CB  
11256 C  CG1 . VAL   B 120 ? 0.1368 0.3463 0.2504 0.0903  0.0234  -0.0006 120 VAL   B CG1 
11257 C  CG2 . VAL   B 120 ? 0.1568 0.3275 0.2260 0.0955  0.0167  0.0051  120 VAL   B CG2 
11267 N  N   . TYR   B 121 ? 0.1503 0.2820 0.1989 0.0864  0.0443  0.0094  121 TYR   B N   
11268 C  CA  . TYR   B 121 ? 0.1329 0.2321 0.1606 0.0848  0.0434  0.0121  121 TYR   B CA  
11269 C  C   . TYR   B 121 ? 0.1699 0.2618 0.1852 0.0948  0.0449  0.0157  121 TYR   B C   
11270 O  O   . TYR   B 121 ? 0.1726 0.2773 0.2002 0.0976  0.0483  0.0160  121 TYR   B O   
11271 C  CB  . TYR   B 121 ? 0.1419 0.2284 0.1592 0.0817  0.0537  0.0125  121 TYR   B CB  
11272 C  CG  . TYR   B 121 ? 0.1492 0.2320 0.1693 0.0802  0.0634  0.0139  121 TYR   B CG  
11273 C  CD1 . TYR   B 121 ? 0.1572 0.2188 0.1612 0.0828  0.0646  0.0167  121 TYR   B CD1 
11274 C  CD2 . TYR   B 121 ? 0.1629 0.2647 0.2026 0.0765  0.0733  0.0127  121 TYR   B CD2 
11275 C  CE1 . TYR   B 121 ? 0.1886 0.2485 0.1901 0.0864  0.0773  0.0184  121 TYR   B CE1 
11276 C  CE2 . TYR   B 121 ? 0.1908 0.2880 0.2294 0.0759  0.0843  0.0142  121 TYR   B CE2 
11277 C  CZ  . TYR   B 121 ? 0.1730 0.2488 0.1976 0.0798  0.0849  0.0169  121 TYR   B CZ  
11278 O  OH  . TYR   B 121 ? 0.2022 0.2734 0.2227 0.0810  0.0968  0.0186  121 TYR   B OH  
11288 N  N   . ILE   B 122 ? 0.1866 0.2564 0.1809 0.0966  0.0410  0.0177  122 ILE   B N   
11289 C  CA  . ILE   B 122 ? 0.1505 0.2068 0.1384 0.0964  0.0384  0.0204  122 ILE   B CA  
11290 C  C   . ILE   B 122 ? 0.1777 0.2163 0.1494 0.1008  0.0462  0.0217  122 ILE   B C   
11291 O  O   . ILE   B 122 ? 0.1820 0.2070 0.1451 0.0966  0.0450  0.0207  122 ILE   B O   
11292 C  CB  . ILE   B 122 ? 0.1546 0.2043 0.1317 0.1006  0.0326  0.0215  122 ILE   B CB  
11293 C  CG1 . ILE   B 122 ? 0.1684 0.2367 0.1532 0.1048  0.0276  0.0205  122 ILE   B CG1 
11294 C  CG2 . ILE   B 122 ? 0.1687 0.2072 0.1342 0.1067  0.0345  0.0239  122 ILE   B CG2 
11295 C  CD1 . ILE   B 122 ? 0.1733 0.2319 0.1485 0.1049  0.0221  0.0211  122 ILE   B CD1 
11307 N  N   . GLU   B 123 ? 0.1751 0.2116 0.1469 0.1033  0.0508  0.0236  123 GLU   B N   
11308 C  CA  . GLU   B 123 ? 0.1879 0.2062 0.1476 0.1047  0.0562  0.0248  123 GLU   B CA  
11309 C  C   . GLU   B 123 ? 0.1975 0.2040 0.1452 0.1089  0.0536  0.0265  123 GLU   B C   
11310 O  O   . GLU   B 123 ? 0.2091 0.2241 0.1609 0.1135  0.0555  0.0279  123 GLU   B O   
11311 C  CB  . GLU   B 123 ? 0.2278 0.2518 0.1902 0.1047  0.0662  0.0250  123 GLU   B CB  
11312 C  CG  . GLU   B 123 ? 0.2244 0.2298 0.1779 0.1061  0.0715  0.0266  123 GLU   B CG  
11313 C  CD  . GLU   B 123 ? 0.2888 0.2967 0.2411 0.1051  0.0827  0.0271  123 GLU   B CD  
11314 O  OE1 . GLU   B 123 ? 0.2650 0.2943 0.2406 0.1021  0.0870  0.0257  123 GLU   B OE1 
11315 O  OE2 . GLU   B 123 ? 0.3143 0.3057 0.2545 0.1069  0.0874  0.0288  123 GLU   B OE2 
11322 N  N   . ILE   B 124 ? 0.2317 0.2187 0.1609 0.1068  0.0496  0.0261  124 ILE   B N   
11323 C  CA  . ILE   B 124 ? 0.2390 0.2156 0.1583 0.1091  0.0474  0.0266  124 ILE   B CA  
11324 C  C   . ILE   B 124 ? 0.2325 0.1920 0.1381 0.1100  0.0494  0.0267  124 ILE   B C   
11325 O  O   . ILE   B 124 ? 0.2249 0.1740 0.1234 0.1061  0.0475  0.0250  124 ILE   B O   
11326 C  CB  . ILE   B 124 ? 0.2375 0.2103 0.1547 0.1053  0.0406  0.0249  124 ILE   B CB  
11327 C  CG1 . ILE   B 124 ? 0.2126 0.2008 0.1437 0.1052  0.0379  0.0250  124 ILE   B CG1 
11328 C  CG2 . ILE   B 124 ? 0.2416 0.2052 0.1521 0.1068  0.0396  0.0245  124 ILE   B CG2 
11329 C  CD1 . ILE   B 124 ? 0.2429 0.2252 0.1681 0.1001  0.0327  0.0230  124 ILE   B CD1 
11341 N  N   . VAL   B 125 ? 0.2311 0.1880 0.1342 0.1151  0.0531  0.0281  125 VAL   B N   
11342 C  CA  . VAL   B 125 ? 0.2742 0.2132 0.1599 0.1167  0.0541  0.0279  125 VAL   B CA  
11343 C  C   . VAL   B 125 ? 0.2820 0.2176 0.1631 0.1190  0.0521  0.0272  125 VAL   B C   
11344 O  O   . VAL   B 125 ? 0.2819 0.2244 0.1687 0.1242  0.0564  0.0295  125 VAL   B O   
11345 C  CB  . VAL   B 125 ? 0.3074 0.2428 0.1885 0.1208  0.0622  0.0301  125 VAL   B CB  
11346 C  CG1 . VAL   B 125 ? 0.3278 0.2439 0.1901 0.1231  0.0620  0.0300  125 VAL   B CG1 
11347 C  CG2 . VAL   B 125 ? 0.3170 0.2572 0.2041 0.1179  0.0659  0.0305  125 VAL   B CG2 
11357 N  N   . ASP   B 126 ? 0.2634 0.1917 0.1435 0.1151  0.0461  0.0240  126 ASP   B N   
11358 C  CA  . ASP   B 126 ? 0.3025 0.2274 0.1788 0.1164  0.0447  0.0230  126 ASP   B CA  
11359 C  C   . ASP   B 126 ? 0.2893 0.2279 0.1771 0.1188  0.0461  0.0255  126 ASP   B C   
11360 O  O   . ASP   B 126 ? 0.2607 0.2079 0.1578 0.1154  0.0437  0.0254  126 ASP   B O   
11361 C  CB  . ASP   B 126 ? 0.3465 0.2604 0.2112 0.1215  0.0474  0.0229  126 ASP   B CB  
11362 C  CG  . ASP   B 126 ? 0.3755 0.2747 0.2247 0.1194  0.0440  0.0197  126 ASP   B CG  
11363 O  OD1 . ASP   B 126 ? 0.3172 0.2150 0.1750 0.1137  0.0378  0.0157  126 ASP   B OD1 
11364 O  OD2 . ASP   B 126 ? 0.3808 0.2729 0.2229 0.1238  0.0476  0.0212  126 ASP   B OD2 
11369 N  N   . ASP   B 127 ? 0.3001 0.2412 0.1885 0.1250  0.0501  0.0279  127 ASP   B N   
11370 C  CA  . ASP   B 127 ? 0.2998 0.2535 0.1985 0.1283  0.0510  0.0302  127 ASP   B CA  
11371 C  C   . ASP   B 127 ? 0.2885 0.2587 0.2000 0.1315  0.0543  0.0326  127 ASP   B C   
11372 O  O   . ASP   B 127 ? 0.3319 0.3137 0.2482 0.1343  0.0537  0.0340  127 ASP   B O   
11373 C  CB  . ASP   B 127 ? 0.3168 0.2662 0.2136 0.1334  0.0532  0.0311  127 ASP   B CB  
11374 C  CG  . ASP   B 127 ? 0.3780 0.3241 0.2701 0.1391  0.0588  0.0326  127 ASP   B CG  
11375 O  OD1 . ASP   B 127 ? 0.4089 0.3460 0.2900 0.1378  0.0599  0.0316  127 ASP   B OD1 
11376 O  OD2 . ASP   B 127 ? 0.4523 0.4023 0.3419 0.1452  0.0623  0.0348  127 ASP   B OD2 
11381 N  N   . LYS   B 128 ? 0.2767 0.2470 0.1870 0.1312  0.0577  0.0329  128 LYS   B N   
11382 C  CA  . LYS   B 128 ? 0.2657 0.2537 0.1937 0.1331  0.0617  0.0341  128 LYS   B CA  
11383 C  C   . LYS   B 128 ? 0.2879 0.2834 0.2149 0.1279  0.0576  0.0327  128 LYS   B C   
11384 O  O   . LYS   B 128 ? 0.2233 0.2114 0.1525 0.1224  0.0555  0.0311  128 LYS   B O   
11385 C  CB  . LYS   B 128 ? 0.3164 0.3005 0.2401 0.1347  0.0693  0.0347  128 LYS   B CB  
11386 C  CG  . LYS   B 128 ? 0.3779 0.3811 0.3203 0.1358  0.0754  0.0350  128 LYS   B CG  
11387 C  CD  . LYS   B 128 ? 0.4994 0.4964 0.4343 0.1353  0.0839  0.0354  128 LYS   B CD  
11388 C  CE  . LYS   B 128 ? 0.5319 0.5497 0.4901 0.1358  0.0918  0.0350  128 LYS   B CE  
11389 N  NZ  . LYS   B 128 ? 0.5740 0.5840 0.5268 0.1356  0.1020  0.0357  128 LYS   B NZ  
11403 N  N   . VAL   B 129 ? 0.2576 0.2721 0.2041 0.1293  0.0557  0.0327  129 VAL   B N   
11404 C  CA  . VAL   B 129 ? 0.2256 0.2507 0.1824 0.1251  0.0514  0.0312  129 VAL   B CA  
11405 C  C   . VAL   B 129 ? 0.2192 0.2667 0.1935 0.1269  0.0538  0.0305  129 VAL   B C   
11406 O  O   . VAL   B 129 ? 0.2182 0.2766 0.2015 0.1322  0.0549  0.0314  129 VAL   B O   
11407 C  CB  . VAL   B 129 ? 0.2287 0.2507 0.1785 0.1242  0.0446  0.0311  129 VAL   B CB  
11408 C  CG1 . VAL   B 129 ? 0.2422 0.2727 0.1979 0.1202  0.0401  0.0296  129 VAL   B CG1 
11409 C  CG2 . VAL   B 129 ? 0.2097 0.2121 0.1463 0.1217  0.0432  0.0308  129 VAL   B CG2 
11419 N  N   . GLU   B 130 ? 0.2020 0.2579 0.1867 0.1224  0.0550  0.0286  130 GLU   B N   
11420 C  CA  . GLU   B 130 ? 0.1920 0.2716 0.2001 0.1211  0.0574  0.0266  130 GLU   B CA  
11421 C  C   . GLU   B 130 ? 0.1946 0.2862 0.2110 0.1172  0.0532  0.0240  130 GLU   B C   
11422 O  O   . GLU   B 130 ? 0.2123 0.2905 0.2162 0.1130  0.0516  0.0236  130 GLU   B O   
11423 C  CB  . GLU   B 130 ? 0.2264 0.3067 0.2380 0.1208  0.0684  0.0265  130 GLU   B CB  
11424 C  CG  . GLU   B 130 ? 0.2744 0.3406 0.2774 0.1254  0.0739  0.0289  130 GLU   B CG  
11425 C  CD  . GLU   B 130 ? 0.3875 0.4456 0.3808 0.1234  0.0843  0.0291  130 GLU   B CD  
11426 O  OE1 . GLU   B 130 ? 0.4044 0.4440 0.3847 0.1207  0.0849  0.0298  130 GLU   B OE1 
11427 O  OE2 . GLU   B 130 ? 0.3944 0.4673 0.4070 0.1245  0.0918  0.0284  130 GLU   B OE2 
11434 N  N   . ILE   B 131 ? 0.1939 0.3093 0.2290 0.1177  0.0508  0.0218  131 ILE   B N   
11435 C  CA  . ILE   B 131 ? 0.1701 0.3003 0.2198 0.1128  0.0464  0.0185  131 ILE   B CA  
11436 C  C   . ILE   B 131 ? 0.1610 0.3050 0.2305 0.1057  0.0534  0.0153  131 ILE   B C   
11437 O  O   . ILE   B 131 ? 0.1599 0.3126 0.2419 0.1043  0.0552  0.0137  131 ILE   B O   
11438 C  CB  . ILE   B 131 ? 0.1710 0.3150 0.2253 0.1162  0.0359  0.0174  131 ILE   B CB  
11439 C  CG1 . ILE   B 131 ? 0.1850 0.3114 0.2200 0.1205  0.0306  0.0205  131 ILE   B CG1 
11440 C  CG2 . ILE   B 131 ? 0.1681 0.3269 0.2337 0.1109  0.0305  0.0136  131 ILE   B CG2 
11441 C  CD1 . ILE   B 131 ? 0.2180 0.3539 0.2523 0.1262  0.0234  0.0206  131 ILE   B CD1 
11453 N  N   . LYS   B 132 ? 0.1817 0.3252 0.2521 0.1006  0.0582  0.0141  132 LYS   B N   
11454 C  CA  . LYS   B 132 ? 0.2104 0.3641 0.2921 0.0942  0.0685  0.0119  132 LYS   B CA  
11455 C  C   . LYS   B 132 ? 0.1482 0.3201 0.2542 0.0861  0.0656  0.0077  132 LYS   B C   
11456 O  O   . LYS   B 132 ? 0.1503 0.3172 0.2436 0.0856  0.0577  0.0074  132 LYS   B O   
11457 C  CB  . LYS   B 132 ? 0.2038 0.3350 0.2744 0.0924  0.0788  0.0146  132 LYS   B CB  
11458 C  CG  . LYS   B 132 ? 0.2276 0.3412 0.2802 0.0993  0.0814  0.0181  132 LYS   B CG  
11459 C  CD  . LYS   B 132 ? 0.2552 0.3513 0.2973 0.0978  0.0923  0.0201  132 LYS   B CD  
11460 C  CE  . LYS   B 132 ? 0.3246 0.4095 0.3518 0.1047  0.0956  0.0228  132 LYS   B CE  
11461 N  NZ  . LYS   B 132 ? 0.3359 0.3990 0.3480 0.1044  0.1037  0.0252  132 LYS   B NZ  
11475 N  N   . ASP   B 133 ? 0.1404 0.3211 0.2649 0.0753  0.0692  0.0030  133 ASP   B N   
11476 C  CA  . ASP   B 133 ? 0.1374 0.3437 0.2877 0.0695  0.0702  -0.0005 133 ASP   B CA  
11477 C  C   . ASP   B 133 ? 0.1631 0.3478 0.2868 0.0630  0.0742  0.0013  133 ASP   B C   
11478 O  O   . ASP   B 133 ? 0.1394 0.3000 0.2534 0.0589  0.0829  0.0033  133 ASP   B O   
11479 C  CB  . ASP   B 133 ? 0.1903 0.4202 0.3698 0.0640  0.0788  -0.0042 133 ASP   B CB  
11480 C  CG  . ASP   B 133 ? 0.2377 0.4847 0.4430 0.0518  0.0781  -0.0096 133 ASP   B CG  
11481 O  OD1 . ASP   B 133 ? 0.2404 0.4837 0.4325 0.0489  0.0655  -0.0123 133 ASP   B OD1 
11482 O  OD2 . ASP   B 133 ? 0.3862 0.6393 0.6006 0.0439  0.0891  -0.0118 133 ASP   B OD2 
11487 N  N   . ALA   B 134 ? 0.1202 0.3042 0.2462 0.0569  0.0633  -0.0019 134 ALA   B N   
11488 C  CA  . ALA   B 134 ? 0.1419 0.3018 0.2468 0.0490  0.0642  -0.0014 134 ALA   B CA  
11489 C  C   . ALA   B 134 ? 0.1666 0.3343 0.2839 0.0354  0.0656  -0.0065 134 ALA   B C   
11490 O  O   . ALA   B 134 ? 0.1496 0.3018 0.2590 0.0286  0.0634  -0.0072 134 ALA   B O   
11491 C  CB  . ALA   B 134 ? 0.1365 0.2830 0.2210 0.0529  0.0528  -0.0005 134 ALA   B CB  
11497 N  N   . SER   B 135 ? 0.1200 0.3148 0.2768 0.0315  0.0694  -0.0105 135 SER   B N   
11498 C  CA  . SER   B 135 ? 0.1851 0.3884 0.3531 0.0181  0.0702  -0.0166 135 SER   B CA  
11499 C  C   . SER   B 135 ? 0.1618 0.3423 0.3244 0.0093  0.0822  -0.0141 135 SER   B C   
11500 O  O   . SER   B 135 ? 0.1793 0.3569 0.3419 -0.0011 0.0801  -0.0181 135 SER   B O   
11501 C  CB  . SER   B 135 ? 0.1805 0.4156 0.3908 0.0160  0.0739  -0.0211 135 SER   B CB  
11502 O  OG  . SER   B 135 ? 0.2344 0.4652 0.4459 0.0175  0.0905  -0.0173 135 SER   B OG  
11508 N  N   . GLN   B 136 ? 0.1842 0.3453 0.3279 0.0142  0.0949  -0.0078 136 GLN   B N   
11509 C  CA  . GLN   B 136 ? 0.2061 0.3418 0.3320 0.0078  0.1076  -0.0046 136 GLN   B CA  
11510 C  C   . GLN   B 136 ? 0.2035 0.3120 0.3000 0.0093  0.1008  -0.0021 136 GLN   B C   
11511 O  O   . GLN   B 136 ? 0.2152 0.3010 0.2964 0.0052  0.1087  0.0004  136 GLN   B O   
11512 C  CB  . GLN   B 136 ? 0.1801 0.3093 0.3114 0.0130  0.1245  0.0007  136 GLN   B CB  
11513 C  CG  . GLN   B 136 ? 0.2377 0.3920 0.3966 0.0111  0.1317  -0.0018 136 GLN   B CG  
11514 C  CD  . GLN   B 136 ? 0.3214 0.4923 0.5063 -0.0022 0.1309  -0.0081 136 GLN   B CD  
11515 O  OE1 . GLN   B 136 ? 0.3732 0.5280 0.5517 -0.0113 0.1377  -0.0077 136 GLN   B OE1 
11516 N  NE2 . GLN   B 136 ? 0.3303 0.5322 0.5436 -0.0027 0.1213  -0.0141 136 GLN   B NE2 
11525 N  N   . LEU   B 137 ? 0.1797 0.2895 0.2668 0.0156  0.0865  -0.0026 137 LEU   B N   
11526 C  CA  . LEU   B 137 ? 0.1854 0.2717 0.2478 0.0174  0.0791  -0.0009 137 LEU   B CA  
11527 C  C   . LEU   B 137 ? 0.2239 0.3142 0.2789 0.0112  0.0667  -0.0059 137 LEU   B C   
11528 O  O   . LEU   B 137 ? 0.1612 0.2350 0.2118 0.0080  0.0635  -0.0057 137 LEU   B O   
11529 C  CB  . LEU   B 137 ? 0.2115 0.2892 0.2528 0.0300  0.0749  0.0027  137 LEU   B CB  
11530 C  CG  . LEU   B 137 ? 0.2089 0.2776 0.2431 0.0378  0.0857  0.0075  137 LEU   B CG  
11531 C  CD1 . LEU   B 137 ? 0.2171 0.2838 0.2400 0.0497  0.0800  0.0095  137 LEU   B CD1 
11532 C  CD2 . LEU   B 137 ? 0.2460 0.2856 0.2556 0.0365  0.0934  0.0103  137 LEU   B CD2 
11544 N  N   . TRP   B 138 ? 0.1488 0.2682 0.2389 0.0103  0.0592  -0.0104 138 TRP   B N   
11545 C  CA  . TRP   B 138 ? 0.2021 0.3256 0.2824 0.0058  0.0468  -0.0156 138 TRP   B CA  
11546 C  C   . TRP   B 138 ? 0.1595 0.2731 0.2460 -0.0060 0.0494  -0.0182 138 TRP   B C   
11547 O  O   . TRP   B 138 ? 0.1535 0.2724 0.2550 -0.0137 0.0586  -0.0199 138 TRP   B O   
11548 C  CB  . TRP   B 138 ? 0.1261 0.2825 0.2411 0.0066  0.0391  -0.0207 138 TRP   B CB  
11549 C  CG  . TRP   B 138 ? 0.1355 0.2984 0.2452 0.0090  0.0246  -0.0242 138 TRP   B CG  
11550 C  CD1 . TRP   B 138 ? 0.1615 0.3362 0.2789 0.0019  0.0163  -0.0312 138 TRP   B CD1 
11551 C  CD2 . TRP   B 138 ? 0.1474 0.3033 0.2374 0.0198  0.0167  -0.0209 138 TRP   B CD2 
11552 N  NE1 . TRP   B 138 ? 0.1499 0.3257 0.2581 0.0081  0.0044  -0.0322 138 TRP   B NE1 
11553 C  CE2 . TRP   B 138 ? 0.1317 0.2969 0.2262 0.0188  0.0047  -0.0257 138 TRP   B CE2 
11554 C  CE3 . TRP   B 138 ? 0.1677 0.3104 0.2404 0.0300  0.0189  -0.0145 138 TRP   B CE3 
11555 C  CZ2 . TRP   B 138 ? 0.1687 0.3273 0.2418 0.0280  -0.0034 -0.0233 138 TRP   B CZ2 
11556 C  CZ3 . TRP   B 138 ? 0.1656 0.3044 0.2266 0.0382  0.0106  -0.0129 138 TRP   B CZ3 
11557 C  CH2 . TRP   B 138 ? 0.1749 0.3209 0.2349 0.0373  0.0001  -0.0169 138 TRP   B CH2 
11568 N  N   . GLY   B 139 ? 0.1253 0.2242 0.1981 -0.0074 0.0422  -0.0188 139 GLY   B N   
11569 C  CA  . GLY   B 139 ? 0.1515 0.2377 0.2183 -0.0176 0.0439  -0.0211 139 GLY   B CA  
11570 C  C   . GLY   B 139 ? 0.2029 0.2587 0.2409 -0.0169 0.0505  -0.0165 139 GLY   B C   
11571 O  O   . GLY   B 139 ? 0.1768 0.2208 0.2153 -0.0232 0.0499  -0.0179 139 GLY   B O   
11575 N  N   . LYS   B 140 ? 0.1557 0.2039 0.1922 -0.0084 0.0557  -0.0109 140 LYS   B N   
11576 C  CA  . LYS   B 140 ? 0.2114 0.2301 0.2177 -0.0066 0.0617  -0.0066 140 LYS   B CA  
11577 C  C   . LYS   B 140 ? 0.2153 0.2194 0.2071 -0.0018 0.0520  -0.0060 140 LYS   B C   
11578 O  O   . LYS   B 140 ? 0.1970 0.2096 0.1897 0.0038  0.0442  -0.0064 140 LYS   B O   
11579 C  CB  . LYS   B 140 ? 0.1956 0.2091 0.1999 0.0005  0.0715  -0.0017 140 LYS   B CB  
11580 C  CG  . LYS   B 140 ? 0.1850 0.2066 0.2032 -0.0044 0.0848  -0.0009 140 LYS   B CG  
11581 C  CD  . LYS   B 140 ? 0.1946 0.2096 0.2071 0.0035  0.0954  0.0039  140 LYS   B CD  
11582 C  CE  . LYS   B 140 ? 0.2302 0.2519 0.2561 -0.0017 0.1105  0.0048  140 LYS   B CE  
11583 N  NZ  . LYS   B 140 ? 0.2805 0.2854 0.2996 -0.0103 0.1189  0.0052  140 LYS   B NZ  
11597 N  N   . VAL   B 141 ? 0.2469 0.2278 0.2194 -0.0038 0.0533  -0.0050 141 VAL   B N   
11598 C  CA  . VAL   B 141 ? 0.2150 0.1814 0.1768 0.0010  0.0450  -0.0048 141 VAL   B CA  
11599 C  C   . VAL   B 141 ? 0.2200 0.1780 0.1691 0.0121  0.0448  -0.0008 141 VAL   B C   
11600 O  O   . VAL   B 141 ? 0.2083 0.1692 0.1566 0.0154  0.0518  0.0011  141 VAL   B O   
11601 C  CB  . VAL   B 141 ? 0.2359 0.1810 0.1848 -0.0034 0.0460  -0.0051 141 VAL   B CB  
11602 C  CG1 . VAL   B 141 ? 0.2466 0.1982 0.2047 -0.0138 0.0451  -0.0090 141 VAL   B CG1 
11603 C  CG2 . VAL   B 141 ? 0.2646 0.1924 0.1990 -0.0017 0.0558  -0.0013 141 VAL   B CG2 
11613 N  N   . THR   B 142 ? 0.1734 0.1601 0.1970 0.0406  0.0563  0.0209  142 THR   B N   
11614 C  CA  . THR   B 142 ? 0.1866 0.1732 0.1971 0.0461  0.0534  0.0239  142 THR   B CA  
11615 C  C   . THR   B 142 ? 0.1944 0.1821 0.1978 0.0484  0.0549  0.0326  142 THR   B C   
11616 O  O   . THR   B 142 ? 0.1736 0.1673 0.1711 0.0512  0.0552  0.0328  142 THR   B O   
11617 C  CB  . THR   B 142 ? 0.1914 0.1716 0.1985 0.0478  0.0501  0.0214  142 THR   B CB  
11618 O  OG1 . THR   B 142 ? 0.1941 0.1747 0.2044 0.0457  0.0495  0.0140  142 THR   B OG1 
11619 C  CG2 . THR   B 142 ? 0.2187 0.1978 0.2106 0.0521  0.0472  0.0216  142 THR   B CG2 
11627 N  N   . SER   B 143 ? 0.1771 0.1626 0.1910 0.0476  0.0563  0.0397  143 SER   B N   
11628 C  CA  . SER   B 143 ? 0.2038 0.1931 0.2107 0.0499  0.0575  0.0496  143 SER   B CA  
11629 C  C   . SER   B 143 ? 0.2052 0.2024 0.2099 0.0497  0.0613  0.0520  143 SER   B C   
11630 O  O   . SER   B 143 ? 0.1785 0.1829 0.1755 0.0526  0.0613  0.0544  143 SER   B O   
11631 C  CB  . SER   B 143 ? 0.2096 0.1965 0.2280 0.0492  0.0591  0.0589  143 SER   B CB  
11632 O  OG  . SER   B 143 ? 0.2107 0.1956 0.2468 0.0455  0.0642  0.0610  143 SER   B OG  
11638 N  N   . GLU   B 144 ? 0.1770 0.1758 0.2001 0.0459  0.0647  0.0509  144 GLU   B N   
11639 C  CA  . GLU   B 144 ? 0.1911 0.1972 0.2141 0.0452  0.0687  0.0540  144 GLU   B CA  
11640 C  C   . GLU   B 144 ? 0.1677 0.1801 0.1824 0.0476  0.0673  0.0478  144 GLU   B C   
11641 O  O   . GLU   B 144 ? 0.1873 0.2063 0.1933 0.0502  0.0696  0.0514  144 GLU   B O   
11642 C  CB  . GLU   B 144 ? 0.1826 0.1889 0.2308 0.0397  0.0726  0.0537  144 GLU   B CB  
11643 C  CG  . GLU   B 144 ? 0.2341 0.2352 0.2947 0.0381  0.0766  0.0629  144 GLU   B CG  
11644 C  CD  . GLU   B 144 ? 0.2990 0.3066 0.3572 0.0409  0.0801  0.0769  144 GLU   B CD  
11645 O  OE1 . GLU   B 144 ? 0.3104 0.3257 0.3727 0.0400  0.0836  0.0792  144 GLU   B OE1 
11646 O  OE2 . GLU   B 144 ? 0.3153 0.3229 0.3710 0.0439  0.0795  0.0857  144 GLU   B OE2 
11653 N  N   . THR   B 145 ? 0.1511 0.1619 0.1654 0.0470  0.0642  0.0389  145 THR   B N   
11654 C  CA  . THR   B 145 ? 0.1892 0.2042 0.1909 0.0502  0.0630  0.0341  145 THR   B CA  
11655 C  C   . THR   B 145 ? 0.1989 0.2134 0.1872 0.0553  0.0629  0.0359  145 THR   B C   
11656 O  O   . THR   B 145 ? 0.1995 0.2196 0.1838 0.0573  0.0645  0.0361  145 THR   B O   
11657 C  CB  . THR   B 145 ? 0.1889 0.2030 0.1921 0.0497  0.0595  0.0267  145 THR   B CB  
11658 O  OG1 . THR   B 145 ? 0.1613 0.1785 0.1787 0.0439  0.0597  0.0233  145 THR   B OG1 
11659 C  CG2 . THR   B 145 ? 0.1950 0.2149 0.1930 0.0530  0.0585  0.0242  145 THR   B CG2 
11667 N  N   . THR   B 146 ? 0.1947 0.2027 0.1768 0.0562  0.0601  0.0362  146 THR   B N   
11668 C  CA  . THR   B 146 ? 0.1974 0.2052 0.1645 0.0599  0.0593  0.0357  146 THR   B CA  
11669 C  C   . THR   B 146 ? 0.1781 0.1943 0.1430 0.0609  0.0631  0.0420  146 THR   B C   
11670 O  O   . THR   B 146 ? 0.1873 0.2061 0.1432 0.0622  0.0626  0.0384  146 THR   B O   
11671 C  CB  . THR   B 146 ? 0.1904 0.1918 0.1548 0.0598  0.0549  0.0346  146 THR   B CB  
11672 O  OG1 . THR   B 146 ? 0.1810 0.1762 0.1505 0.0591  0.0524  0.0296  146 THR   B OG1 
11673 C  CG2 . THR   B 146 ? 0.2023 0.2043 0.1530 0.0624  0.0536  0.0316  146 THR   B CG2 
11681 N  N   . LYS   B 147 ? 0.1741 0.1927 0.1455 0.0588  0.0645  0.0506  147 LYS   B N   
11682 C  CA  . LYS   B 147 ? 0.1982 0.2259 0.1649 0.0596  0.0685  0.0594  147 LYS   B CA  
11683 C  C   . LYS   B 147 ? 0.2142 0.2470 0.1810 0.0598  0.0709  0.0567  147 LYS   B C   
11684 O  O   . LYS   B 147 ? 0.2062 0.2455 0.1677 0.0608  0.0708  0.0559  147 LYS   B O   
11685 C  CB  . LYS   B 147 ? 0.1767 0.2061 0.1587 0.0574  0.0702  0.0703  147 LYS   B CB  
11686 C  CG  . LYS   B 147 ? 0.2003 0.2291 0.1820 0.0574  0.0674  0.0774  147 LYS   B CG  
11687 C  CD  . LYS   B 147 ? 0.2636 0.2941 0.2596 0.0560  0.0707  0.0904  147 LYS   B CD  
11688 C  CE  . LYS   B 147 ? 0.3537 0.3804 0.3479 0.0559  0.0673  0.0962  147 LYS   B CE  
11689 N  NZ  . LYS   B 147 ? 0.3395 0.3767 0.3250 0.0579  0.0619  0.0962  147 LYS   B NZ  
11703 N  N   . GLU   B 148 ? 0.1853 0.2182 0.1677 0.0579  0.0727  0.0550  148 GLU   B N   
11704 C  CA  . GLU   B 148 ? 0.1904 0.2289 0.1751 0.0577  0.0748  0.0539  148 GLU   B CA  
11705 C  C   . GLU   B 148 ? 0.1790 0.2169 0.1561 0.0599  0.0720  0.0462  148 GLU   B C   
11706 O  O   . GLU   B 148 ? 0.2054 0.2480 0.1771 0.0611  0.0740  0.0464  148 GLU   B O   
11707 C  CB  . GLU   B 148 ? 0.1920 0.2324 0.1941 0.0542  0.0766  0.0536  148 GLU   B CB  
11708 C  CG  . GLU   B 148 ? 0.2167 0.2572 0.2314 0.0503  0.0805  0.0609  148 GLU   B CG  
11709 C  CD  . GLU   B 148 ? 0.2236 0.2702 0.2421 0.0507  0.0844  0.0711  148 GLU   B CD  
11710 O  OE1 . GLU   B 148 ? 0.2110 0.2636 0.2233 0.0528  0.0844  0.0710  148 GLU   B OE1 
11711 O  OE2 . GLU   B 148 ? 0.2357 0.2806 0.2643 0.0483  0.0871  0.0790  148 GLU   B OE2 
11718 N  N   . LEU   B 149 ? 0.1684 0.1995 0.1416 0.0605  0.0682  0.0394  149 LEU   B N   
11719 C  CA  . LEU   B 149 ? 0.1789 0.2072 0.1453 0.0622  0.0662  0.0326  149 LEU   B CA  
11720 C  C   . LEU   B 149 ? 0.1878 0.2168 0.1445 0.0637  0.0669  0.0302  149 LEU   B C   
11721 O  O   . LEU   B 149 ? 0.1953 0.2255 0.1489 0.0646  0.0687  0.0262  149 LEU   B O   
11722 C  CB  . LEU   B 149 ? 0.1709 0.1927 0.1409 0.0619  0.0620  0.0279  149 LEU   B CB  
11723 C  CG  . LEU   B 149 ? 0.1904 0.2154 0.1693 0.0607  0.0610  0.0274  149 LEU   B CG  
11724 C  CD1 . LEU   B 149 ? 0.2201 0.2393 0.1975 0.0600  0.0567  0.0242  149 LEU   B CD1 
11725 C  CD2 . LEU   B 149 ? 0.2022 0.2318 0.1826 0.0621  0.0625  0.0273  149 LEU   B CD2 
11737 N  N   . GLU   B 150 ? 0.2031 0.2317 0.1506 0.0635  0.0659  0.0324  150 GLU   B N   
11738 C  CA  . GLU   B 150 ? 0.1945 0.2271 0.1340 0.0639  0.0661  0.0297  150 GLU   B CA  
11739 C  C   . GLU   B 150 ? 0.2414 0.2818 0.1710 0.0641  0.0702  0.0320  150 GLU   B C   
11740 O  O   . GLU   B 150 ? 0.2137 0.2587 0.1419 0.0641  0.0715  0.0262  150 GLU   B O   
11741 C  CB  . GLU   B 150 ? 0.1900 0.2232 0.1213 0.0635  0.0635  0.0331  150 GLU   B CB  
11742 C  CG  . GLU   B 150 ? 0.1904 0.2159 0.1238 0.0637  0.0596  0.0284  150 GLU   B CG  
11743 C  CD  . GLU   B 150 ? 0.2817 0.3070 0.1959 0.0633  0.0570  0.0313  150 GLU   B CD  
11744 O  OE1 . GLU   B 150 ? 0.2762 0.3135 0.1932 0.0626  0.0572  0.0368  150 GLU   B OE1 
11745 O  OE2 . GLU   B 150 ? 0.2207 0.2411 0.1454 0.0637  0.0542  0.0288  150 GLU   B OE2 
11752 N  N   . LYS   B 151 ? 0.2011 0.2476 0.1461 0.0638  0.0726  0.0402  151 LYS   B N   
11753 C  CA  . LYS   B 151 ? 0.1953 0.2511 0.1412 0.0640  0.0768  0.0441  151 LYS   B CA  
11754 C  C   . LYS   B 151 ? 0.2428 0.2971 0.1849 0.0651  0.0793  0.0380  151 LYS   B C   
11755 O  O   . LYS   B 151 ? 0.2225 0.2843 0.1646 0.0656  0.0830  0.0372  151 LYS   B O   
11756 C  CB  . LYS   B 151 ? 0.1773 0.2343 0.1362 0.0611  0.0750  0.0528  151 LYS   B CB  
11757 C  CG  . LYS   B 151 ? 0.1936 0.2549 0.1532 0.0620  0.0782  0.0640  151 LYS   B CG  
11758 C  CD  . LYS   B 151 ? 0.2227 0.2855 0.1939 0.0602  0.0815  0.0734  151 LYS   B CD  
11759 C  CE  . LYS   B 151 ? 0.1910 0.2532 0.1767 0.0587  0.0813  0.0822  151 LYS   B CE  
11760 N  NZ  . LYS   B 151 ? 0.2104 0.2714 0.2108 0.0558  0.0854  0.0893  151 LYS   B NZ  
11774 N  N   . ILE   B 152 ? 0.2366 0.2850 0.1891 0.0653  0.0779  0.0346  152 ILE   B N   
11775 C  CA  . ILE   B 152 ? 0.2261 0.2759 0.1854 0.0667  0.0805  0.0315  152 ILE   B CA  
11776 C  C   . ILE   B 152 ? 0.2240 0.2667 0.1830 0.0677  0.0793  0.0229  152 ILE   B C   
11777 O  O   . ILE   B 152 ? 0.2314 0.2736 0.1953 0.0690  0.0809  0.0219  152 ILE   B O   
11778 C  CB  . ILE   B 152 ? 0.2289 0.2819 0.2018 0.0659  0.0806  0.0371  152 ILE   B CB  
11779 C  CG1 . ILE   B 152 ? 0.2369 0.2836 0.2114 0.0648  0.0761  0.0358  152 ILE   B CG1 
11780 C  CG2 . ILE   B 152 ? 0.2611 0.3206 0.2351 0.0645  0.0829  0.0453  152 ILE   B CG2 
11781 C  CD1 . ILE   B 152 ? 0.2038 0.2566 0.1930 0.0627  0.0759  0.0397  152 ILE   B CD1 
11793 N  N   . THR   B 153 ? 0.2549 0.2915 0.2018 0.0670  0.0771  0.0175  153 THR   B N   
11794 C  CA  . THR   B 153 ? 0.2353 0.2654 0.1836 0.0674  0.0768  0.0088  153 THR   B CA  
11795 C  C   . THR   B 153 ? 0.2402 0.2719 0.1775 0.0664  0.0792  0.0011  153 THR   B C   
11796 O  O   . THR   B 153 ? 0.2326 0.2711 0.1627 0.0653  0.0792  0.0039  153 THR   B O   
11797 C  CB  . THR   B 153 ? 0.2022 0.2253 0.1574 0.0668  0.0716  0.0089  153 THR   B CB  
11798 O  OG1 . THR   B 153 ? 0.2123 0.2340 0.1569 0.0656  0.0686  0.0101  153 THR   B OG1 
11799 C  CG2 . THR   B 153 ? 0.2225 0.2453 0.1834 0.0671  0.0697  0.0146  153 THR   B CG2 
11807 N  N   . GLU   B 154 ? 0.2341 0.2618 0.1736 0.0663  0.0813  -0.0086 154 GLU   B N   
11808 C  CA  . GLU   B 154 ? 0.2361 0.2665 0.1683 0.0642  0.0842  -0.0188 154 GLU   B CA  
11809 C  C   . GLU   B 154 ? 0.2406 0.2717 0.1629 0.0621  0.0794  -0.0185 154 GLU   B C   
11810 O  O   . GLU   B 154 ? 0.2770 0.3007 0.1976 0.0625  0.0743  -0.0150 154 GLU   B O   
11811 C  CB  . GLU   B 154 ? 0.2803 0.3057 0.2205 0.0643  0.0874  -0.0302 154 GLU   B CB  
11812 C  CG  . GLU   B 154 ? 0.4044 0.4318 0.3277 0.0617  0.0930  -0.0430 154 GLU   B CG  
11813 C  CD  . GLU   B 154 ? 0.3725 0.4003 0.3197 0.0632  0.0977  -0.0541 154 GLU   B CD  
11814 O  OE1 . GLU   B 154 ? 0.3943 0.4203 0.3461 0.0671  0.1000  -0.0498 154 GLU   B OE1 
11815 O  OE2 . GLU   B 154 ? 0.4257 0.4514 0.3642 0.0610  0.0989  -0.0667 154 GLU   B OE2 
11822 N  N   . ASN   B 155 ? 0.2805 0.3188 0.1859 0.0599  0.0807  -0.0215 155 ASN   B N   
11823 C  CA  . ASN   B 155 ? 0.3118 0.3535 0.2066 0.0579  0.0758  -0.0205 155 ASN   B CA  
11824 C  C   . ASN   B 155 ? 0.2847 0.3170 0.1820 0.0569  0.0729  -0.0283 155 ASN   B C   
11825 O  O   . ASN   B 155 ? 0.2981 0.3246 0.1998 0.0561  0.0769  -0.0387 155 ASN   B O   
11826 C  CB  . ASN   B 155 ? 0.3750 0.4285 0.2545 0.0554  0.0776  -0.0229 155 ASN   B CB  
11827 C  CG  . ASN   B 155 ? 0.4292 0.4895 0.2959 0.0537  0.0716  -0.0187 155 ASN   B CG  
11828 O  OD1 . ASN   B 155 ? 0.4243 0.4866 0.2974 0.0554  0.0672  -0.0072 155 ASN   B OD1 
11829 N  ND2 . ASN   B 155 ? 0.4344 0.5001 0.2918 0.0504  0.0713  -0.0276 155 ASN   B ND2 
11836 N  N   . LYS   B 156 ? 0.2531 0.2844 0.1509 0.0571  0.0668  -0.0234 156 LYS   B N   
11837 C  CA  . LYS   B 156 ? 0.2866 0.3075 0.1796 0.0563  0.0637  -0.0300 156 LYS   B CA  
11838 C  C   . LYS   B 156 ? 0.2021 0.2144 0.1227 0.0582  0.0620  -0.0263 156 LYS   B C   
11839 O  O   . LYS   B 156 ? 0.2708 0.2730 0.1832 0.0583  0.0598  -0.0300 156 LYS   B O   
11840 C  CB  . LYS   B 156 ? 0.3215 0.3431 0.2158 0.0529  0.0671  -0.0446 156 LYS   B CB  
11841 C  CG  . LYS   B 156 ? 0.4066 0.4386 0.2814 0.0496  0.0675  -0.0493 156 LYS   B CG  
11842 C  CD  . LYS   B 156 ? 0.4672 0.4960 0.3377 0.0458  0.0687  -0.0632 156 LYS   B CD  
11843 C  CE  . LYS   B 156 ? 0.5576 0.5905 0.4148 0.0442  0.0606  -0.0629 156 LYS   B CE  
11844 N  NZ  . LYS   B 156 ? 0.5663 0.6178 0.4157 0.0435  0.0556  -0.0536 156 LYS   B NZ  
11858 N  N   . SER   B 157 ? 0.2212 0.2314 0.1398 0.0607  0.0639  -0.0192 157 SER   B N   
11859 C  CA  . SER   B 157 ? 0.2176 0.2204 0.1492 0.0622  0.0621  -0.0147 157 SER   B CA  
11860 C  C   . SER   B 157 ? 0.2179 0.2169 0.1490 0.0624  0.0569  -0.0090 157 SER   B C   
11861 O  O   . SER   B 157 ? 0.2229 0.2271 0.1480 0.0627  0.0559  -0.0034 157 SER   B O   
11862 C  CB  . SER   B 157 ? 0.2056 0.2115 0.1448 0.0637  0.0645  -0.0090 157 SER   B CB  
11863 O  OG  . SER   B 157 ? 0.1971 0.2042 0.1409 0.0643  0.0694  -0.0142 157 SER   B OG  
11869 N  N   . LYS   B 158 ? 0.2010 0.1926 0.1402 0.0623  0.0542  -0.0097 158 LYS   B N   
11870 C  CA  . LYS   B 158 ? 0.1847 0.1731 0.1282 0.0621  0.0497  -0.0050 158 LYS   B CA  
11871 C  C   . LYS   B 158 ? 0.2029 0.1897 0.1469 0.0623  0.0490  0.0015  158 LYS   B C   
11872 O  O   . LYS   B 158 ? 0.1755 0.1651 0.1322 0.0624  0.0507  0.0015  158 LYS   B O   
11873 C  CB  . LYS   B 158 ? 0.2081 0.1892 0.1501 0.0613  0.0472  -0.0104 158 LYS   B CB  
11874 C  CG  . LYS   B 158 ? 0.2319 0.2134 0.1631 0.0605  0.0481  -0.0185 158 LYS   B CG  
11875 C  CD  . LYS   B 158 ? 0.2039 0.1941 0.1268 0.0610  0.0471  -0.0165 158 LYS   B CD  
11876 C  CE  . LYS   B 158 ? 0.2339 0.2275 0.1434 0.0593  0.0466  -0.0251 158 LYS   B CE  
11877 N  NZ  . LYS   B 158 ? 0.2542 0.2502 0.1623 0.0570  0.0511  -0.0345 158 LYS   B NZ  
11891 N  N   . VAL   B 159 ? 0.1476 0.1359 0.1008 0.0620  0.0466  0.0065  159 VAL   B N   
11892 C  CA  . VAL   B 159 ? 0.1608 0.1509 0.1186 0.0613  0.0466  0.0109  159 VAL   B CA  
11893 C  C   . VAL   B 159 ? 0.1696 0.1552 0.1292 0.0595  0.0428  0.0110  159 VAL   B C   
11894 O  O   . VAL   B 159 ? 0.1607 0.1435 0.1212 0.0593  0.0414  0.0115  159 VAL   B O   
11895 C  CB  . VAL   B 159 ? 0.1845 0.1793 0.1403 0.0617  0.0490  0.0160  159 VAL   B CB  
11896 C  CG1 . VAL   B 159 ? 0.1893 0.1873 0.1542 0.0600  0.0491  0.0182  159 VAL   B CG1 
11897 C  CG2 . VAL   B 159 ? 0.1759 0.1768 0.1294 0.0628  0.0528  0.0168  159 VAL   B CG2 
11907 N  N   . LEU   B 160 ? 0.1410 0.1298 0.1108 0.0586  0.0420  0.0113  160 LEU   B N   
11908 C  CA  . LEU   B 160 ? 0.1448 0.1329 0.1162 0.0568  0.0392  0.0116  160 LEU   B CA  
11909 C  C   . LEU   B 160 ? 0.1396 0.1364 0.1209 0.0566  0.0401  0.0136  160 LEU   B C   
11910 O  O   . LEU   B 160 ? 0.1859 0.1873 0.1633 0.0577  0.0420  0.0151  160 LEU   B O   
11911 C  CB  . LEU   B 160 ? 0.1280 0.1154 0.1059 0.0568  0.0381  0.0108  160 LEU   B CB  
11912 C  CG  . LEU   B 160 ? 0.1554 0.1447 0.1357 0.0557  0.0360  0.0120  160 LEU   B CG  
11913 C  CD1 . LEU   B 160 ? 0.1658 0.1502 0.1473 0.0552  0.0349  0.0109  160 LEU   B CD1 
11914 C  CD2 . LEU   B 160 ? 0.1767 0.1749 0.1596 0.0575  0.0372  0.0153  160 LEU   B CD2 
11926 N  N   . CYS   B 161 ? 0.1735 0.1696 0.1498 0.0548  0.0393  0.0130  161 CYS   B N   
11927 C  CA  . CYS   B 161 ? 0.1348 0.1417 0.1240 0.0540  0.0413  0.0129  161 CYS   B CA  
11928 C  C   . CYS   B 161 ? 0.1649 0.1727 0.1532 0.0519  0.0407  0.0097  161 CYS   B C   
11929 O  O   . CYS   B 161 ? 0.1662 0.1675 0.1543 0.0512  0.0384  0.0086  161 CYS   B O   
11930 C  CB  . CYS   B 161 ? 0.1452 0.1524 0.1330 0.0541  0.0449  0.0145  161 CYS   B CB  
11931 S  SG  . CYS   B 161 ? 0.1831 0.1806 0.1677 0.0534  0.0467  0.0156  161 CYS   B SG  
11937 N  N   . ILE   B 162 ? 0.1622 0.1813 0.1581 0.0507  0.0427  0.0078  162 ILE   B N   
11938 C  CA  . ILE   B 162 ? 0.1643 0.1872 0.1654 0.0480  0.0439  0.0026  162 ILE   B CA  
11939 C  C   . ILE   B 162 ? 0.1855 0.2060 0.1926 0.0440  0.0472  0.0007  162 ILE   B C   
11940 O  O   . ILE   B 162 ? 0.1664 0.1896 0.1770 0.0440  0.0490  0.0042  162 ILE   B O   
11941 C  CB  . ILE   B 162 ? 0.1470 0.1878 0.1538 0.0475  0.0429  0.0005  162 ILE   B CB  
11942 C  CG1 . ILE   B 162 ? 0.1814 0.2347 0.1852 0.0478  0.0443  0.0028  162 ILE   B CG1 
11943 C  CG2 . ILE   B 162 ? 0.1820 0.2211 0.1787 0.0498  0.0393  0.0030  162 ILE   B CG2 
11944 C  CD1 . ILE   B 162 ? 0.1630 0.2379 0.1742 0.0447  0.0430  -0.0003 162 ILE   B CD1 
11956 N  N   . GLY   B 163 ? 0.2012 0.2163 0.2128 0.0396  0.0477  -0.0041 163 GLY   B N   
11957 C  CA  . GLY   B 163 ? 0.1571 0.1710 0.1848 0.0341  0.0508  -0.0063 163 GLY   B CA  
11958 C  C   . GLY   B 163 ? 0.1663 0.1922 0.1986 0.0276  0.0513  -0.0147 163 GLY   B C   
11959 O  O   . GLY   B 163 ? 0.1568 0.1962 0.1854 0.0286  0.0487  -0.0171 163 GLY   B O   
11963 N  N   . PRO   B 164 ? 0.1649 0.1891 0.2122 0.0212  0.0549  -0.0193 164 PRO   B N   
11964 C  CA  . PRO   B 164 ? 0.1735 0.2109 0.2303 0.0135  0.0555  -0.0301 164 PRO   B CA  
11965 C  C   . PRO   B 164 ? 0.1633 0.2100 0.2164 0.0116  0.0531  -0.0392 164 PRO   B C   
11966 O  O   . PRO   B 164 ? 0.1807 0.2445 0.2310 0.0074  0.0513  -0.0457 164 PRO   B O   
11967 C  CB  . PRO   B 164 ? 0.2159 0.2424 0.2868 0.0077  0.0609  -0.0328 164 PRO   B CB  
11968 C  CG  . PRO   B 164 ? 0.2360 0.2500 0.3032 0.0129  0.0627  -0.0203 164 PRO   B CG  
11969 C  CD  . PRO   B 164 ? 0.1633 0.1747 0.2230 0.0206  0.0588  -0.0143 164 PRO   B CD  
11977 N  N   . ALA   B 165 ? 0.1855 0.2203 0.2291 0.0153  0.0531  -0.0391 165 ALA   B N   
11978 C  CA  . ALA   B 165 ? 0.1640 0.2067 0.2024 0.0138  0.0515  -0.0467 165 ALA   B CA  
11979 C  C   . ALA   B 165 ? 0.1282 0.1897 0.1598 0.0181  0.0469  -0.0430 165 ALA   B C   
11980 O  O   . ALA   B 165 ? 0.1363 0.2155 0.1634 0.0145  0.0454  -0.0499 165 ALA   B O   
11981 C  CB  . ALA   B 165 ? 0.1314 0.1592 0.1726 0.0173  0.0529  -0.0459 165 ALA   B CB  
11987 N  N   . GLY   B 166 ? 0.1346 0.1910 0.1574 0.0254  0.0450  -0.0317 166 GLY   B N   
11988 C  CA  . GLY   B 166 ? 0.1666 0.2375 0.1792 0.0304  0.0420  -0.0257 166 GLY   B CA  
11989 C  C   . GLY   B 166 ? 0.1607 0.2516 0.1764 0.0269  0.0409  -0.0265 166 GLY   B C   
11990 O  O   . GLY   B 166 ? 0.1297 0.2417 0.1460 0.0275  0.0383  -0.0259 166 GLY   B O   
11994 N  N   . GLU   B 167 ? 0.1423 0.2298 0.1678 0.0237  0.0429  -0.0268 167 GLU   B N   
11995 C  CA  . GLU   B 167 ? 0.1376 0.2440 0.1688 0.0196  0.0422  -0.0281 167 GLU   B CA  
11996 C  C   . GLU   B 167 ? 0.1222 0.2482 0.1592 0.0115  0.0407  -0.0400 167 GLU   B C   
11997 O  O   . GLU   B 167 ? 0.1459 0.2952 0.1797 0.0098  0.0377  -0.0398 167 GLU   B O   
11998 C  CB  . GLU   B 167 ? 0.1463 0.2436 0.1868 0.0168  0.0453  -0.0266 167 GLU   B CB  
11999 C  CG  . GLU   B 167 ? 0.1752 0.2563 0.2113 0.0237  0.0473  -0.0164 167 GLU   B CG  
12000 C  CD  . GLU   B 167 ? 0.1948 0.2667 0.2367 0.0208  0.0511  -0.0145 167 GLU   B CD  
12001 O  OE1 . GLU   B 167 ? 0.1628 0.2377 0.2207 0.0130  0.0528  -0.0216 167 GLU   B OE1 
12002 O  OE2 . GLU   B 167 ? 0.1792 0.2441 0.2215 0.0260  0.0527  -0.0061 167 GLU   B OE2 
12009 N  N   . ARG   B 168 ? 0.1369 0.2530 0.1740 0.0065  0.0426  -0.0505 168 ARG   B N   
12010 C  CA  . ARG   B 168 ? 0.1396 0.2724 0.1799 -0.0026 0.0424  -0.0652 168 ARG   B CA  
12011 C  C   . ARG   B 168 ? 0.1104 0.2573 0.1443 0.0002  0.0396  -0.0663 168 ARG   B C   
12012 O  O   . ARG   B 168 ? 0.1574 0.3175 0.1860 -0.0070 0.0397  -0.0790 168 ARG   B O   
12013 C  CB  . ARG   B 168 ? 0.1545 0.2714 0.2090 -0.0100 0.0475  -0.0767 168 ARG   B CB  
12014 C  CG  . ARG   B 168 ? 0.1783 0.2886 0.2476 -0.0146 0.0508  -0.0773 168 ARG   B CG  
12015 C  CD  . ARG   B 168 ? 0.2232 0.3102 0.3047 -0.0182 0.0571  -0.0816 168 ARG   B CD  
12016 N  NE  . ARG   B 168 ? 0.2523 0.3348 0.3512 -0.0223 0.0606  -0.0803 168 ARG   B NE  
12017 C  CZ  . ARG   B 168 ? 0.3096 0.4034 0.4217 -0.0322 0.0625  -0.0912 168 ARG   B CZ  
12018 N  NH1 . ARG   B 168 ? 0.2976 0.4044 0.4123 -0.0404 0.0623  -0.1078 168 ARG   B NH1 
12019 N  NH2 . ARG   B 168 ? 0.3869 0.4790 0.5061 -0.0342 0.0646  -0.0861 168 ARG   B NH2 
12033 N  N   . LEU   B 169 ? 0.1116 0.2530 0.1337 0.0098  0.0380  -0.0538 169 LEU   B N   
12034 C  CA  . LEU   B 169 ? 0.1465 0.3011 0.1562 0.0136  0.0358  -0.0517 169 LEU   B CA  
12035 C  C   . LEU   B 169 ? 0.1578 0.3020 0.1646 0.0112  0.0384  -0.0610 169 LEU   B C   
12036 O  O   . LEU   B 169 ? 0.1386 0.2983 0.1429 0.0107  0.0362  -0.0626 169 LEU   B O   
12037 C  CB  . LEU   B 169 ? 0.1382 0.3282 0.1491 0.0100  0.0321  -0.0529 169 LEU   B CB  
12038 C  CG  . LEU   B 169 ? 0.1595 0.3623 0.1694 0.0127  0.0297  -0.0427 169 LEU   B CG  
12039 C  CD1 . LEU   B 169 ? 0.1276 0.3684 0.1388 0.0115  0.0256  -0.0407 169 LEU   B CD1 
12040 C  CD2 . LEU   B 169 ? 0.1725 0.3579 0.1821 0.0234  0.0306  -0.0277 169 LEU   B CD2 
12052 N  N   . SER   B 170 ? 0.1340 0.2533 0.1511 0.0100  0.0422  -0.0649 170 SER   B N   
12053 C  CA  . SER   B 170 ? 0.1460 0.2524 0.1607 0.0090  0.0452  -0.0715 170 SER   B CA  
12054 C  C   . SER   B 170 ? 0.1120 0.2107 0.1229 0.0158  0.0400  -0.0570 170 SER   B C   
12055 O  O   . SER   B 170 ? 0.1581 0.2531 0.1588 0.0242  0.0413  -0.0487 170 SER   B O   
12056 C  CB  . SER   B 170 ? 0.1675 0.2479 0.1926 0.0078  0.0499  -0.0742 170 SER   B CB  
12057 O  OG  . SER   B 170 ? 0.1714 0.2377 0.1972 0.0091  0.0516  -0.0752 170 SER   B OG  
12063 N  N   . LEU   B 171 ? 0.1427 0.2518 0.1419 0.0154  0.0418  -0.0641 171 LEU   B N   
12064 C  CA  . LEU   B 171 ? 0.1287 0.2375 0.1254 0.0221  0.0401  -0.0541 171 LEU   B CA  
12065 C  C   . LEU   B 171 ? 0.1530 0.2338 0.1468 0.0267  0.0428  -0.0492 171 LEU   B C   
12066 O  O   . LEU   B 171 ? 0.1274 0.2055 0.1216 0.0316  0.0421  -0.0415 171 LEU   B O   
12067 C  CB  . LEU   B 171 ? 0.1389 0.2645 0.1291 0.0188  0.0388  -0.0595 171 LEU   B CB  
12068 C  CG  . LEU   B 171 ? 0.1556 0.3128 0.1438 0.0143  0.0350  -0.0627 171 LEU   B CG  
12069 C  CD1 . LEU   B 171 ? 0.1735 0.3476 0.1549 0.0127  0.0335  -0.0657 171 LEU   B CD1 
12070 C  CD2 . LEU   B 171 ? 0.1848 0.3528 0.1683 0.0202  0.0314  -0.0497 171 LEU   B CD2 
12082 N  N   . MET   B 172 ? 0.1440 0.2081 0.1483 0.0247  0.0459  -0.0533 172 MET   B N   
12083 C  CA  . MET   B 172 ? 0.1375 0.1789 0.1471 0.0293  0.0473  -0.0472 172 MET   B CA  
12084 C  C   . MET   B 172 ? 0.1754 0.2066 0.1793 0.0329  0.0467  -0.0402 172 MET   B C   
12085 O  O   . MET   B 172 ? 0.1679 0.1835 0.1800 0.0352  0.0461  -0.0356 172 MET   B O   
12086 C  CB  . MET   B 172 ? 0.1418 0.1696 0.1578 0.0251  0.0502  -0.0540 172 MET   B CB  
12087 C  CG  . MET   B 172 ? 0.1584 0.1813 0.1854 0.0192  0.0530  -0.0610 172 MET   B CG  
12088 S  SD  . MET   B 172 ? 0.1824 0.1882 0.2210 0.0152  0.0570  -0.0652 172 MET   B SD  
12089 C  CE  . MET   B 172 ? 0.1983 0.2173 0.2354 0.0100  0.0583  -0.0774 172 MET   B CE  
12099 N  N   . ALA   B 173 ? 0.1257 0.1722 0.1363 0.0333  0.0449  -0.0380 173 ALA   B N   
12100 C  CA  . ALA   B 173 ? 0.1666 0.2043 0.1713 0.0361  0.0436  -0.0304 173 ALA   B CA  
12101 C  C   . ALA   B 173 ? 0.1948 0.2210 0.1911 0.0416  0.0406  -0.0199 173 ALA   B C   
12102 O  O   . ALA   B 173 ? 0.1690 0.2020 0.1679 0.0436  0.0382  -0.0160 173 ALA   B O   
12103 C  CB  . ALA   B 173 ? 0.1531 0.2081 0.1593 0.0345  0.0422  -0.0301 173 ALA   B CB  
12109 N  N   . ALA   B 174 ? 0.1422 0.1566 0.1473 0.0425  0.0397  -0.0152 174 ALA   B N   
12110 C  CA  . ALA   B 174 ? 0.1539 0.1585 0.1546 0.0450  0.0357  -0.0075 174 ALA   B CA  
12111 C  C   . ALA   B 174 ? 0.1811 0.1852 0.1727 0.0469  0.0347  -0.0024 174 ALA   B C   
12112 O  O   . ALA   B 174 ? 0.1729 0.1841 0.1699 0.0466  0.0370  -0.0037 174 ALA   B O   
12113 C  CB  . ALA   B 174 ? 0.1867 0.1772 0.1857 0.0434  0.0349  -0.0068 174 ALA   B CB  
12119 N  N   . VAL   B 175 ? 0.1473 0.1474 0.1421 0.0484  0.0321  0.0025  175 VAL   B N   
12120 C  CA  . VAL   B 175 ? 0.1875 0.1846 0.1720 0.0499  0.0319  0.0063  175 VAL   B CA  
12121 C  C   . VAL   B 175 ? 0.1817 0.1691 0.1672 0.0487  0.0313  0.0068  175 VAL   B C   
12122 O  O   . VAL   B 175 ? 0.1640 0.1464 0.1501 0.0476  0.0290  0.0069  175 VAL   B O   
12123 C  CB  . VAL   B 175 ? 0.1584 0.1600 0.1488 0.0520  0.0311  0.0100  175 VAL   B CB  
12124 C  CG1 . VAL   B 175 ? 0.1644 0.1619 0.1493 0.0531  0.0319  0.0120  175 VAL   B CG1 
12125 C  CG2 . VAL   B 175 ? 0.1940 0.2080 0.1812 0.0543  0.0319  0.0115  175 VAL   B CG2 
12135 N  N   . MET   B 176 ? 0.1843 0.1707 0.1690 0.0492  0.0331  0.0077  176 MET   B N   
12136 C  CA  . MET   B 176 ? 0.1819 0.1608 0.1627 0.0494  0.0334  0.0095  176 MET   B CA  
12137 C  C   . MET   B 176 ? 0.1577 0.1365 0.1363 0.0516  0.0335  0.0106  176 MET   B C   
12138 O  O   . MET   B 176 ? 0.1622 0.1453 0.1382 0.0527  0.0347  0.0110  176 MET   B O   
12139 C  CB  . MET   B 176 ? 0.1672 0.1460 0.1544 0.0495  0.0368  0.0102  176 MET   B CB  
12140 C  CG  . MET   B 176 ? 0.1661 0.1461 0.1617 0.0471  0.0384  0.0070  176 MET   B CG  
12141 S  SD  . MET   B 176 ? 0.1897 0.1626 0.1873 0.0452  0.0363  0.0059  176 MET   B SD  
12142 C  CE  . MET   B 176 ? 0.2183 0.1848 0.2122 0.0466  0.0356  0.0123  176 MET   B CE  
12152 N  N   . ASN   B 177 ? 0.1750 0.1480 0.1451 0.0525  0.0326  0.0112  177 ASN   B N   
12153 C  CA  . ASN   B 177 ? 0.1476 0.1213 0.1175 0.0551  0.0337  0.0106  177 ASN   B CA  
12154 C  C   . ASN   B 177 ? 0.1565 0.1267 0.1161 0.0582  0.0349  0.0122  177 ASN   B C   
12155 O  O   . ASN   B 177 ? 0.1507 0.1177 0.1135 0.0575  0.0325  0.0139  177 ASN   B O   
12156 C  CB  . ASN   B 177 ? 0.1936 0.1645 0.1567 0.0544  0.0323  0.0075  177 ASN   B CB  
12157 C  CG  . ASN   B 177 ? 0.1582 0.1269 0.1309 0.0527  0.0294  0.0061  177 ASN   B CG  
12158 O  OD1 . ASN   B 177 ? 0.1584 0.1274 0.1324 0.0505  0.0278  0.0067  177 ASN   B OD1 
12159 N  ND2 . ASN   B 177 ? 0.1982 0.1622 0.1615 0.0545  0.0292  0.0039  177 ASN   B ND2 
12166 N  N   . ASP   B 178 ? 0.1620 0.1353 0.1147 0.0614  0.0377  0.0127  178 ASP   B N   
12167 C  CA  . ASP   B 178 ? 0.1615 0.1382 0.1111 0.0623  0.0372  0.0154  178 ASP   B CA  
12168 C  C   . ASP   B 178 ? 0.1811 0.1573 0.1340 0.0605  0.0364  0.0232  178 ASP   B C   
12169 O  O   . ASP   B 178 ? 0.1904 0.1673 0.1440 0.0595  0.0335  0.0269  178 ASP   B O   
12170 C  CB  . ASP   B 178 ? 0.2014 0.1747 0.1413 0.0622  0.0340  0.0105  178 ASP   B CB  
12171 C  CG  . ASP   B 178 ? 0.2080 0.1795 0.1451 0.0639  0.0366  0.0023  178 ASP   B CG  
12172 O  OD1 . ASP   B 178 ? 0.2053 0.1822 0.1381 0.0640  0.0391  0.0000  178 ASP   B OD1 
12173 O  OD2 . ASP   B 178 ? 0.1906 0.1573 0.1365 0.0618  0.0340  -0.0007 178 ASP   B OD2 
12178 N  N   . VAL   B 179 ? 0.1770 0.1535 0.1378 0.0597  0.0393  0.0251  179 VAL   B N   
12179 C  CA  . VAL   B 179 ? 0.1615 0.1384 0.1363 0.0575  0.0406  0.0317  179 VAL   B CA  
12180 C  C   . VAL   B 179 ? 0.1976 0.1658 0.1724 0.0564  0.0387  0.0308  179 VAL   B C   
12181 O  O   . VAL   B 179 ? 0.1712 0.1384 0.1620 0.0544  0.0411  0.0298  179 VAL   B O   
12182 C  CB  . VAL   B 179 ? 0.1826 0.1651 0.1523 0.0574  0.0410  0.0404  179 VAL   B CB  
12183 C  CG1 . VAL   B 179 ? 0.2027 0.1837 0.1847 0.0555  0.0435  0.0483  179 VAL   B CG1 
12184 C  CG2 . VAL   B 179 ? 0.1823 0.1727 0.1432 0.0585  0.0433  0.0408  179 VAL   B CG2 
12194 N  N   . ASP   B 180 ? 0.1578 0.1252 0.1373 0.0572  0.0350  0.0305  180 ASP   B N   
12195 C  CA  . ASP   B 180 ? 0.1683 0.1311 0.1539 0.0541  0.0330  0.0304  180 ASP   B CA  
12196 C  C   . ASP   B 180 ? 0.1889 0.1496 0.1697 0.0522  0.0292  0.0238  180 ASP   B C   
12197 O  O   . ASP   B 180 ? 0.1843 0.1440 0.1734 0.0496  0.0271  0.0235  180 ASP   B O   
12198 C  CB  . ASP   B 180 ? 0.1700 0.1347 0.1590 0.0545  0.0321  0.0393  180 ASP   B CB  
12199 C  CG  . ASP   B 180 ? 0.1728 0.1441 0.1529 0.0572  0.0293  0.0430  180 ASP   B CG  
12200 O  OD1 . ASP   B 180 ? 0.1922 0.1621 0.1624 0.0577  0.0260  0.0372  180 ASP   B OD1 
12201 O  OD2 . ASP   B 180 ? 0.1924 0.1709 0.1683 0.0572  0.0299  0.0507  180 ASP   B OD2 
12206 N  N   . ARG   B 181 ? 0.1734 0.1356 0.1506 0.0534  0.0286  0.0190  181 ARG   B N   
12207 C  CA  . ARG   B 181 ? 0.1852 0.1457 0.1584 0.0510  0.0256  0.0143  181 ARG   B CA  
12208 C  C   . ARG   B 181 ? 0.1633 0.1273 0.1431 0.0481  0.0260  0.0113  181 ARG   B C   
12209 O  O   . ARG   B 181 ? 0.1676 0.1340 0.1464 0.0489  0.0287  0.0116  181 ARG   B O   
12210 C  CB  . ARG   B 181 ? 0.1589 0.1191 0.1295 0.0537  0.0247  0.0119  181 ARG   B CB  
12211 C  CG  . ARG   B 181 ? 0.1635 0.1223 0.1272 0.0592  0.0242  0.0148  181 ARG   B CG  
12212 C  CD  . ARG   B 181 ? 0.1798 0.1377 0.1470 0.0578  0.0211  0.0195  181 ARG   B CD  
12213 N  NE  . ARG   B 181 ? 0.1663 0.1221 0.1388 0.0549  0.0182  0.0162  181 ARG   B NE  
12214 C  CZ  . ARG   B 181 ? 0.1334 0.0912 0.1193 0.0546  0.0151  0.0194  181 ARG   B CZ  
12215 N  NH1 . ARG   B 181 ? 0.1978 0.1566 0.1740 0.0558  0.0141  0.0270  181 ARG   B NH1 
12216 N  NH2 . ARG   B 181 ? 0.1934 0.1472 0.1738 0.0522  0.0129  0.0161  181 ARG   B NH2 
12230 N  N   . THR   B 182 ? 0.1372 0.1027 0.1228 0.0455  0.0240  0.0092  182 THR   B N   
12231 C  CA  . THR   B 182 ? 0.1497 0.1186 0.1355 0.0447  0.0248  0.0076  182 THR   B CA  
12232 C  C   . THR   B 182 ? 0.1516 0.1231 0.1398 0.0440  0.0236  0.0068  182 THR   B C   
12233 O  O   . THR   B 182 ? 0.1504 0.1199 0.1412 0.0425  0.0214  0.0066  182 THR   B O   
12234 C  CB  . THR   B 182 ? 0.1475 0.1174 0.1399 0.0438  0.0265  0.0068  182 THR   B CB  
12235 O  OG1 . THR   B 182 ? 0.1601 0.1351 0.1517 0.0439  0.0275  0.0043  182 THR   B OG1 
12236 C  CG2 . THR   B 182 ? 0.1538 0.1198 0.1491 0.0420  0.0255  0.0067  182 THR   B CG2 
12244 N  N   . ALA   B 183 ? 0.1517 0.1276 0.1390 0.0454  0.0248  0.0074  183 ALA   B N   
12245 C  CA  . ALA   B 183 ? 0.1406 0.1207 0.1316 0.0458  0.0247  0.0084  183 ALA   B CA  
12246 C  C   . ALA   B 183 ? 0.1443 0.1287 0.1355 0.0463  0.0261  0.0068  183 ALA   B C   
12247 O  O   . ALA   B 183 ? 0.1520 0.1425 0.1415 0.0481  0.0279  0.0065  183 ALA   B O   
12248 C  CB  . ALA   B 183 ? 0.1547 0.1377 0.1434 0.0481  0.0260  0.0106  183 ALA   B CB  
12254 N  N   . ALA   B 184 ? 0.1490 0.1315 0.1425 0.0449  0.0260  0.0048  184 ALA   B N   
12255 C  CA  . ALA   B 184 ? 0.1571 0.1425 0.1538 0.0447  0.0281  0.0006  184 ALA   B CA  
12256 C  C   . ALA   B 184 ? 0.1564 0.1516 0.1536 0.0456  0.0307  -0.0025 184 ALA   B C   
12257 O  O   . ALA   B 184 ? 0.1756 0.1776 0.1730 0.0452  0.0332  -0.0075 184 ALA   B O   
12258 C  CB  . ALA   B 184 ? 0.1727 0.1507 0.1721 0.0423  0.0277  -0.0008 184 ALA   B CB  
12264 N  N   . ARG   B 185 ? 0.1896 0.1870 0.1384 0.0279  0.0397  0.0010  185 ARG   B N   
12265 C  CA  . ARG   B 185 ? 0.1557 0.1607 0.1090 0.0247  0.0403  -0.0015 185 ARG   B CA  
12266 C  C   . ARG   B 185 ? 0.1778 0.1860 0.1200 0.0264  0.0381  -0.0011 185 ARG   B C   
12267 O  O   . ARG   B 185 ? 0.1743 0.1789 0.1130 0.0299  0.0365  0.0021  185 ARG   B O   
12268 C  CB  . ARG   B 185 ? 0.1787 0.1799 0.1281 0.0216  0.0410  -0.0009 185 ARG   B CB  
12269 C  CG  . ARG   B 185 ? 0.2150 0.2117 0.1650 0.0207  0.0427  -0.0004 185 ARG   B CG  
12270 C  CD  . ARG   B 185 ? 0.1631 0.1621 0.1222 0.0170  0.0448  -0.0014 185 ARG   B CD  
12271 N  NE  . ARG   B 185 ? 0.1419 0.1479 0.1090 0.0149  0.0479  -0.0059 185 ARG   B NE  
12272 C  CZ  . ARG   B 185 ? 0.1720 0.1801 0.1349 0.0117  0.0500  -0.0084 185 ARG   B CZ  
12273 N  NH1 . ARG   B 185 ? 0.1691 0.1749 0.1312 0.0106  0.0494  -0.0058 185 ARG   B NH1 
12274 N  NH2 . ARG   B 185 ? 0.1359 0.1516 0.1098 0.0100  0.0527  -0.0140 185 ARG   B NH2 
12288 N  N   . GLY   B 186 ? 0.1693 0.1865 0.1127 0.0241  0.0388  -0.0047 186 GLY   B N   
12289 C  CA  . GLY   B 186 ? 0.1352 0.1604 0.0769 0.0258  0.0365  -0.0039 186 GLY   B CA  
12290 C  C   . GLY   B 186 ? 0.1492 0.1828 0.0939 0.0270  0.0355  -0.0068 186 GLY   B C   
12291 O  O   . GLY   B 186 ? 0.1620 0.2038 0.1011 0.0282  0.0336  -0.0066 186 GLY   B O   
12295 N  N   . GLY   B 187 ? 0.1751 0.2070 0.1255 0.0271  0.0371  -0.0092 187 GLY   B N   
12296 C  CA  . GLY   B 187 ? 0.1644 0.2045 0.1226 0.0284  0.0365  -0.0114 187 GLY   B CA  
12297 C  C   . GLY   B 187 ? 0.1628 0.2001 0.1188 0.0335  0.0343  -0.0061 187 GLY   B C   
12298 O  O   . GLY   B 187 ? 0.2034 0.2480 0.1573 0.0353  0.0329  -0.0068 187 GLY   B O   
12302 N  N   . VAL   B 188 ? 0.1741 0.1998 0.1216 0.0358  0.0343  -0.0011 188 VAL   B N   
12303 C  CA  . VAL   B 188 ? 0.1824 0.2035 0.1266 0.0409  0.0329  0.0038  188 VAL   B CA  
12304 C  C   . VAL   B 188 ? 0.1900 0.2137 0.1374 0.0434  0.0338  0.0031  188 VAL   B C   
12305 O  O   . VAL   B 188 ? 0.1780 0.2045 0.1270 0.0473  0.0325  0.0058  188 VAL   B O   
12306 C  CB  . VAL   B 188 ? 0.2109 0.2185 0.1455 0.0422  0.0331  0.0073  188 VAL   B CB  
12307 C  CG1 . VAL   B 188 ? 0.1907 0.1958 0.1215 0.0407  0.0322  0.0096  188 VAL   B CG1 
12308 C  CG2 . VAL   B 188 ? 0.2213 0.2244 0.1610 0.0400  0.0350  0.0056  188 VAL   B CG2 
12318 N  N   . GLY   B 189 ? 0.1596 0.1851 0.1199 0.0411  0.0362  0.0001  189 GLY   B N   
12319 C  CA  . GLY   B 189 ? 0.1677 0.1965 0.1350 0.0433  0.0380  -0.0003 189 GLY   B CA  
12320 C  C   . GLY   B 189 ? 0.1832 0.2234 0.1534 0.0429  0.0367  -0.0030 189 GLY   B C   
12321 O  O   . GLY   B 189 ? 0.1590 0.2032 0.1373 0.0462  0.0371  -0.0014 189 GLY   B O   
12325 N  N   . ALA   B 190 ? 0.1704 0.2192 0.1444 0.0392  0.0352  -0.0072 190 ALA   B N   
12326 C  CA  . ALA   B 190 ? 0.1767 0.2390 0.1530 0.0382  0.0332  -0.0109 190 ALA   B CA  
12327 C  C   . ALA   B 190 ? 0.1809 0.2466 0.1510 0.0432  0.0300  -0.0057 190 ALA   B C   
12328 O  O   . ALA   B 190 ? 0.1660 0.2423 0.1425 0.0444  0.0286  -0.0067 190 ALA   B O   
12329 C  CB  . ALA   B 190 ? 0.1557 0.2264 0.1353 0.0334  0.0327  -0.0171 190 ALA   B CB  
12335 N  N   . VAL   B 191 ? 0.1925 0.2496 0.1507 0.0457  0.0290  -0.0002 191 VAL   B N   
12336 C  CA  . VAL   B 191 ? 0.1795 0.2383 0.1347 0.0512  0.0267  0.0060  191 VAL   B CA  
12337 C  C   . VAL   B 191 ? 0.1865 0.2415 0.1445 0.0557  0.0281  0.0086  191 VAL   B C   
12338 O  O   . VAL   B 191 ? 0.2155 0.2782 0.1738 0.0590  0.0266  0.0105  191 VAL   B O   
12339 C  CB  . VAL   B 191 ? 0.2066 0.2543 0.1445 0.0529  0.0264  0.0112  191 VAL   B CB  
12340 C  CG1 . VAL   B 191 ? 0.1766 0.2257 0.1157 0.0589  0.0249  0.0179  191 VAL   B CG1 
12341 C  CG2 . VAL   B 191 ? 0.1786 0.2311 0.1179 0.0489  0.0256  0.0092  191 VAL   B CG2 
12351 N  N   . MET   B 192 ? 0.1828 0.2264 0.1403 0.0559  0.0309  0.0089  192 MET   B N   
12352 C  CA  . MET   B 192 ? 0.1730 0.2147 0.1404 0.0602  0.0328  0.0109  192 MET   B CA  
12353 C  C   . MET   B 192 ? 0.2347 0.2860 0.2008 0.0594  0.0333  0.0083  192 MET   B C   
12354 O  O   . MET   B 192 ? 0.1773 0.2356 0.1565 0.0634  0.0330  0.0108  192 MET   B O   
12355 C  CB  . MET   B 192 ? 0.2171 0.2460 0.1750 0.0602  0.0357  0.0113  192 MET   B CB  
12356 C  CG  . MET   B 192 ? 0.2046 0.2284 0.1646 0.0657  0.0375  0.0146  192 MET   B CG  
12357 S  SD  . MET   B 192 ? 0.2201 0.2311 0.1716 0.0660  0.0394  0.0150  192 MET   B SD  
12358 C  CE  . MET   B 192 ? 0.1950 0.2083 0.1546 0.0707  0.0432  0.0169  192 MET   B CE  
12368 N  N   . GLY   B 193 ? 0.1959 0.2544 0.1792 0.0539  0.0343  0.0028  193 GLY   B N   
12369 C  CA  . GLY   B 193 ? 0.1820 0.2523 0.1771 0.0520  0.0348  -0.0011 193 GLY   B CA  
12370 C  C   . GLY   B 193 ? 0.1749 0.2591 0.1722 0.0528  0.0310  -0.0018 193 GLY   B C   
12371 O  O   . GLY   B 193 ? 0.1883 0.2806 0.1926 0.0539  0.0311  -0.0021 193 GLY   B O   
12375 N  N   . SER   B 194 ? 0.1822 0.2688 0.1684 0.0521  0.0277  -0.0016 194 SER   B N   
12376 C  CA  . SER   B 194 ? 0.1788 0.2804 0.1643 0.0533  0.0235  -0.0013 194 SER   B CA  
12377 C  C   . SER   B 194 ? 0.1901 0.2922 0.1734 0.0601  0.0229  0.0057  194 SER   B C   
12378 O  O   . SER   B 194 ? 0.1884 0.3050 0.1754 0.0616  0.0197  0.0063  194 SER   B O   
12379 C  CB  . SER   B 194 ? 0.1818 0.2855 0.1573 0.0524  0.0211  -0.0006 194 SER   B CB  
12380 O  OG  . SER   B 194 ? 0.2152 0.3078 0.1776 0.0571  0.0209  0.0071  194 SER   B OG  
12386 N  N   . LYS   B 195 ? 0.1869 0.2747 0.1675 0.0642  0.0256  0.0109  195 LYS   B N   
12387 C  CA  . LYS   B 195 ? 0.1978 0.2835 0.1752 0.0714  0.0257  0.0176  195 LYS   B CA  
12388 C  C   . LYS   B 195 ? 0.2050 0.2912 0.1908 0.0732  0.0287  0.0174  195 LYS   B C   
12389 O  O   . LYS   B 195 ? 0.1740 0.2594 0.1641 0.0792  0.0296  0.0224  195 LYS   B O   
12390 C  CB  . LYS   B 195 ? 0.1824 0.2524 0.1491 0.0751  0.0268  0.0227  195 LYS   B CB  
12391 C  CG  . LYS   B 195 ? 0.1673 0.2355 0.1266 0.0738  0.0248  0.0247  195 LYS   B CG  
12392 C  CD  . LYS   B 195 ? 0.1977 0.2504 0.1452 0.0779  0.0262  0.0301  195 LYS   B CD  
12393 C  CE  . LYS   B 195 ? 0.2148 0.2686 0.1560 0.0785  0.0243  0.0344  195 LYS   B CE  
12394 N  NZ  . LYS   B 195 ? 0.2270 0.2982 0.1696 0.0800  0.0212  0.0368  195 LYS   B NZ  
12408 N  N   . ASN   B 196 ? 0.1838 0.2733 0.1826 0.0682  0.0307  0.0120  196 ASN   B N   
12409 C  CA  . ASN   B 196 ? 0.1702 0.2608 0.1799 0.0697  0.0342  0.0123  196 ASN   B CA  
12410 C  C   . ASN   B 196 ? 0.1698 0.2452 0.1728 0.0743  0.0380  0.0167  196 ASN   B C   
12411 O  O   . ASN   B 196 ? 0.1705 0.2465 0.1784 0.0783  0.0407  0.0196  196 ASN   B O   
12412 C  CB  . ASN   B 196 ? 0.1659 0.2710 0.1878 0.0724  0.0328  0.0134  196 ASN   B CB  
12413 C  CG  . ASN   B 196 ? 0.2215 0.3391 0.2499 0.0669  0.0323  0.0073  196 ASN   B CG  
12414 O  OD1 . ASN   B 196 ? 0.1947 0.3113 0.2370 0.0620  0.0350  0.0026  196 ASN   B OD1 
12415 N  ND2 . ASN   B 196 ? 0.1856 0.3206 0.2276 0.0676  0.0290  0.0068  196 ASN   B ND2 
12422 N  N   . LEU   B 197 ? 0.1690 0.2324 0.1619 0.0734  0.0380  0.0170  197 LEU   B N   
12423 C  CA  . LEU   B 197 ? 0.1858 0.2350 0.1682 0.0772  0.0408  0.0199  197 LEU   B CA  
12424 C  C   . LEU   B 197 ? 0.1907 0.2352 0.1750 0.0738  0.0439  0.0177  197 LEU   B C   
12425 O  O   . LEU   B 197 ? 0.1501 0.1933 0.1373 0.0690  0.0426  0.0149  197 LEU   B O   
12426 C  CB  . LEU   B 197 ? 0.1595 0.1993 0.1322 0.0790  0.0390  0.0218  197 LEU   B CB  
12427 C  CG  . LEU   B 197 ? 0.1642 0.1907 0.1288 0.0825  0.0413  0.0237  197 LEU   B CG  
12428 C  CD1 . LEU   B 197 ? 0.1605 0.1867 0.1253 0.0888  0.0440  0.0266  197 LEU   B CD1 
12429 C  CD2 . LEU   B 197 ? 0.2163 0.2319 0.1660 0.0830  0.0394  0.0246  197 LEU   B CD2 
12441 N  N   . LYS   B 198 ? 0.1668 0.2113 0.1603 0.0757  0.0473  0.0196  198 LYS   B N   
12442 C  CA  . LYS   B 198 ? 0.1488 0.1899 0.1484 0.0716  0.0494  0.0190  198 LYS   B CA  
12443 C  C   . LYS   B 198 ? 0.1580 0.1876 0.1469 0.0725  0.0490  0.0205  198 LYS   B C   
12444 O  O   . LYS   B 198 ? 0.2023 0.2277 0.1857 0.0691  0.0496  0.0194  198 LYS   B O   
12445 C  CB  . LYS   B 198 ? 0.1654 0.2099 0.1735 0.0711  0.0518  0.0208  198 LYS   B CB  
12446 C  CG  . LYS   B 198 ? 0.1675 0.2086 0.1809 0.0680  0.0543  0.0217  198 LYS   B CG  
12447 C  CD  . LYS   B 198 ? 0.1558 0.1997 0.1789 0.0630  0.0553  0.0181  198 LYS   B CD  
12448 C  CE  . LYS   B 198 ? 0.1599 0.2014 0.1892 0.0603  0.0580  0.0198  198 LYS   B CE  
12449 N  NZ  . LYS   B 198 ? 0.1566 0.1983 0.1924 0.0556  0.0591  0.0164  198 LYS   B NZ  
12463 N  N   . ALA   B 199 ? 0.1903 0.2128 0.1638 0.0768  0.0482  0.0228  199 ALA   B N   
12464 C  CA  . ALA   B 199 ? 0.1732 0.1868 0.1397 0.0776  0.0478  0.0236  199 ALA   B CA  
12465 C  C   . ALA   B 199 ? 0.1827 0.1891 0.1379 0.0822  0.0470  0.0241  199 ALA   B C   
12466 O  O   . ALA   B 199 ? 0.1911 0.1999 0.1473 0.0853  0.0470  0.0256  199 ALA   B O   
12467 C  CB  . ALA   B 199 ? 0.1623 0.1767 0.1320 0.0771  0.0500  0.0256  199 ALA   B CB  
12473 N  N   . ILE   B 200 ? 0.1861 0.1842 0.1327 0.0823  0.0462  0.0230  200 ILE   B N   
12474 C  CA  . ILE   B 200 ? 0.2136 0.2027 0.1466 0.0863  0.0461  0.0225  200 ILE   B CA  
12475 C  C   . ILE   B 200 ? 0.1959 0.1828 0.1286 0.0866  0.0465  0.0217  200 ILE   B C   
12476 O  O   . ILE   B 200 ? 0.2074 0.1919 0.1355 0.0837  0.0455  0.0199  200 ILE   B O   
12477 C  CB  . ILE   B 200 ? 0.1917 0.1746 0.1236 0.0866  0.0449  0.0208  200 ILE   B CB  
12478 C  CG1 . ILE   B 200 ? 0.1935 0.1819 0.1294 0.0871  0.0443  0.0221  200 ILE   B CG1 
12479 C  CG2 . ILE   B 200 ? 0.2117 0.1849 0.1333 0.0904  0.0453  0.0201  200 ILE   B CG2 
12480 C  CD1 . ILE   B 200 ? 0.2428 0.2237 0.1690 0.0864  0.0427  0.0219  200 ILE   B CD1 
12492 N  N   . THR   B 201 ? 0.1951 0.1821 0.1252 0.0897  0.0478  0.0229  201 THR   B N   
12493 C  CA  . THR   B 201 ? 0.2023 0.1877 0.1276 0.0911  0.0483  0.0219  201 THR   B CA  
12494 C  C   . THR   B 201 ? 0.2119 0.1877 0.1253 0.0935  0.0478  0.0178  201 THR   B C   
12495 O  O   . THR   B 201 ? 0.1970 0.1698 0.1128 0.0958  0.0485  0.0182  201 THR   B O   
12496 C  CB  . THR   B 201 ? 0.2270 0.2191 0.1561 0.0933  0.0505  0.0254  201 THR   B CB  
12497 O  OG1 . THR   B 201 ? 0.2266 0.2168 0.1533 0.0971  0.0519  0.0258  201 THR   B OG1 
12498 C  CG2 . THR   B 201 ? 0.2628 0.2622 0.2001 0.0907  0.0517  0.0289  201 THR   B CG2 
12506 N  N   . VAL   B 202 ? 0.2075 0.1802 0.1165 0.0928  0.0468  0.0140  202 VAL   B N   
12507 C  CA  . VAL   B 202 ? 0.2264 0.1899 0.1272 0.0946  0.0467  0.0089  202 VAL   B CA  
12508 C  C   . VAL   B 202 ? 0.2623 0.2261 0.1527 0.0954  0.0464  0.0051  202 VAL   B C   
12509 O  O   . VAL   B 202 ? 0.2441 0.2135 0.1380 0.0931  0.0451  0.0049  202 VAL   B O   
12510 C  CB  . VAL   B 202 ? 0.2279 0.1831 0.1276 0.0922  0.0453  0.0061  202 VAL   B CB  
12511 C  CG1 . VAL   B 202 ? 0.2349 0.1902 0.1298 0.0879  0.0432  0.0040  202 VAL   B CG1 
12512 C  CG2 . VAL   B 202 ? 0.2744 0.2181 0.1646 0.0941  0.0461  0.0016  202 VAL   B CG2 
12522 N  N   . LYS   B 203 ? 0.2467 0.2081 0.1364 0.0987  0.0480  0.0019  203 LYS   B N   
12523 C  CA  . LYS   B 203 ? 0.2390 0.2022 0.1255 0.0996  0.0477  -0.0033 203 LYS   B CA  
12524 C  C   . LYS   B 203 ? 0.2780 0.2288 0.1531 0.0998  0.0481  -0.0108 203 LYS   B C   
12525 O  O   . LYS   B 203 ? 0.2859 0.2319 0.1655 0.1024  0.0502  -0.0098 203 LYS   B O   
12526 C  CB  . LYS   B 203 ? 0.2782 0.2484 0.1588 0.1034  0.0499  -0.0010 203 LYS   B CB  
12527 C  CG  . LYS   B 203 ? 0.2905 0.2623 0.1676 0.1052  0.0502  -0.0072 203 LYS   B CG  
12528 C  CD  . LYS   B 203 ? 0.3562 0.3360 0.2265 0.1094  0.0524  -0.0046 203 LYS   B CD  
12529 C  CE  . LYS   B 203 ? 0.3649 0.3496 0.2320 0.1103  0.0521  -0.0106 203 LYS   B CE  
12530 N  NZ  . LYS   B 203 ? 0.4113 0.4048 0.2732 0.1148  0.0543  -0.0071 203 LYS   B NZ  
12544 N  N   . GLY   B 204 ? 0.2604 0.2089 0.1347 0.0972  0.0463  -0.0179 204 GLY   B N   
12545 C  CA  . GLY   B 204 ? 0.2977 0.2344 0.1651 0.0968  0.0470  -0.0260 204 GLY   B CA  
12546 C  C   . GLY   B 204 ? 0.3227 0.2619 0.1836 0.0970  0.0469  -0.0342 204 GLY   B C   
12547 O  O   . GLY   B 204 ? 0.3157 0.2637 0.1738 0.0952  0.0446  -0.0351 204 GLY   B O   
12551 N  N   . THR   B 205 ? 0.3421 0.2751 0.2020 0.0992  0.0495  -0.0402 205 THR   B N   
12552 C  CA  . THR   B 205 ? 0.3589 0.2952 0.2135 0.0995  0.0500  -0.0492 205 THR   B CA  
12553 C  C   . THR   B 205 ? 0.3553 0.2796 0.2101 0.0969  0.0505  -0.0603 205 THR   B C   
12554 O  O   . THR   B 205 ? 0.3536 0.2788 0.2019 0.0966  0.0511  -0.0694 205 THR   B O   
12555 C  CB  . THR   B 205 ? 0.3948 0.3357 0.2451 0.1048  0.0534  -0.0469 205 THR   B CB  
12556 O  OG1 . THR   B 205 ? 0.3604 0.2921 0.2198 0.1073  0.0568  -0.0480 205 THR   B OG1 
12557 C  CG2 . THR   B 205 ? 0.3940 0.3463 0.2501 0.1073  0.0534  -0.0363 205 THR   B CG2 
12565 N  N   . GLY   B 206 ? 0.3930 0.3052 0.2505 0.0950  0.0503  -0.0595 206 GLY   B N   
12566 C  CA  . GLY   B 206 ? 0.4230 0.3215 0.2794 0.0923  0.0510  -0.0687 206 GLY   B CA  
12567 C  C   . GLY   B 206 ? 0.3898 0.2884 0.2498 0.0864  0.0470  -0.0741 206 GLY   B C   
12568 O  O   . GLY   B 206 ? 0.3859 0.2949 0.2389 0.0848  0.0437  -0.0708 206 GLY   B O   
12572 N  N   . LYS   B 207 ? 0.4215 0.3058 0.2791 0.0832  0.0474  -0.0818 207 LYS   B N   
12573 C  CA  . LYS   B 207 ? 0.4017 0.2857 0.2663 0.0771  0.0437  -0.0884 207 LYS   B CA  
12574 C  C   . LYS   B 207 ? 0.4247 0.2919 0.2886 0.0747  0.0441  -0.0857 207 LYS   B C   
12575 O  O   . LYS   B 207 ? 0.4320 0.2897 0.3038 0.0777  0.0478  -0.0819 207 LYS   B O   
12576 C  CB  . LYS   B 207 ? 0.4821 0.3650 0.3380 0.0738  0.0434  -0.1025 207 LYS   B CB  
12577 C  CG  . LYS   B 207 ? 0.5732 0.4693 0.4217 0.0760  0.0438  -0.1065 207 LYS   B CG  
12578 C  CD  . LYS   B 207 ? 0.6719 0.5741 0.5094 0.0711  0.0409  -0.1175 207 LYS   B CD  
12579 C  CE  . LYS   B 207 ? 0.6959 0.6021 0.5357 0.0724  0.0440  -0.1266 207 LYS   B CE  
12580 N  NZ  . LYS   B 207 ? 0.7904 0.7035 0.6197 0.0788  0.0467  -0.1194 207 LYS   B NZ  
12594 N  N   . ILE   B 208 ? 0.4073 0.2734 0.2723 0.0697  0.0406  -0.0870 208 ILE   B N   
12595 C  CA  . ILE   B 208 ? 0.3944 0.2456 0.2668 0.0665  0.0413  -0.0854 208 ILE   B CA  
12596 C  C   . ILE   B 208 ? 0.4082 0.2478 0.2840 0.0623  0.0421  -0.0977 208 ILE   B C   
12597 O  O   . ILE   B 208 ? 0.4411 0.2859 0.3119 0.0579  0.0385  -0.1076 208 ILE   B O   
12598 C  CB  . ILE   B 208 ? 0.3943 0.2494 0.2656 0.0623  0.0375  -0.0797 208 ILE   B CB  
12599 C  CG1 . ILE   B 208 ? 0.4459 0.3089 0.3108 0.0657  0.0377  -0.0669 208 ILE   B CG1 
12600 C  CG2 . ILE   B 208 ? 0.3650 0.2088 0.2456 0.0558  0.0372  -0.0800 208 ILE   B CG2 
12601 C  CD1 . ILE   B 208 ? 0.4093 0.2889 0.2731 0.0696  0.0366  -0.0650 208 ILE   B CD1 
12613 N  N   . ALA   B 209 ? 0.3750 0.2018 0.2656 0.0636  0.0464  -0.0974 209 ALA   B N   
12614 C  CA  . ALA   B 209 ? 0.4372 0.2511 0.3294 0.0599  0.0476  -0.1088 209 ALA   B CA  
12615 C  C   . ALA   B 209 ? 0.4560 0.2621 0.3494 0.0520  0.0451  -0.1121 209 ALA   B C   
12616 O  O   . ALA   B 209 ? 0.4124 0.2158 0.3145 0.0510  0.0455  -0.1017 209 ALA   B O   
12617 C  CB  . ALA   B 209 ? 0.4315 0.2341 0.3362 0.0640  0.0528  -0.1055 209 ALA   B CB  
12623 N  N   . LEU   B 210 ? 0.4185 0.2250 0.3201 0.0467  0.0424  -0.1259 210 LEU   B N   
12624 C  CA  . LEU   B 210 ? 0.4133 0.2147 0.3210 0.0380  0.0397  -0.1302 210 LEU   B CA  
12625 C  C   . LEU   B 210 ? 0.4285 0.2142 0.3453 0.0346  0.0414  -0.1361 210 LEU   B C   
12626 O  O   . LEU   B 210 ? 0.4212 0.2106 0.3403 0.0376  0.0386  -0.1417 210 LEU   B O   
12627 C  CB  . LEU   B 210 ? 0.4472 0.2624 0.3410 0.0338  0.0335  -0.1393 210 LEU   B CB  
12628 C  CG  . LEU   B 210 ? 0.4620 0.2938 0.3391 0.0379  0.0305  -0.1326 210 LEU   B CG  
12629 C  CD1 . LEU   B 210 ? 0.4624 0.3117 0.3359 0.0340  0.0242  -0.1415 210 LEU   B CD1 
12630 C  CD2 . LEU   B 210 ? 0.3833 0.2199 0.2719 0.0377  0.0300  -0.1167 210 LEU   B CD2 
12642 N  N   . ALA   B 211 ? 0.4079 0.1890 0.3432 0.0294  0.0408  -0.1287 211 ALA   B N   
12643 C  CA  . ALA   B 211 ? 0.4532 0.2150 0.3969 0.0252  0.0448  -0.1353 211 ALA   B CA  
12644 C  C   . ALA   B 211 ? 0.4634 0.2293 0.4058 0.0191  0.0401  -0.1511 211 ALA   B C   
12645 O  O   . ALA   B 211 ? 0.4521 0.2155 0.3986 0.0197  0.0384  -0.1531 211 ALA   B O   
12646 C  CB  . ALA   B 211 ? 0.4604 0.2140 0.4177 0.0206  0.0472  -0.1256 211 ALA   B CB  
12652 N  N   . ASP   B 212 ? 0.4847 0.2640 0.4203 0.0142  0.0343  -0.1560 212 ASP   B N   
12653 C  CA  . ASP   B 212 ? 0.5144 0.3006 0.4464 0.0076  0.0291  -0.1694 212 ASP   B CA  
12654 C  C   . ASP   B 212 ? 0.5075 0.3133 0.4210 0.0080  0.0234  -0.1723 212 ASP   B C   
12655 O  O   . ASP   B 212 ? 0.4677 0.2840 0.3878 0.0027  0.0195  -0.1705 212 ASP   B O   
12656 C  CB  . ASP   B 212 ? 0.5432 0.3245 0.4915 -0.0022 0.0278  -0.1720 212 ASP   B CB  
12657 C  CG  . ASP   B 212 ? 0.5963 0.3818 0.5411 -0.0093 0.0232  -0.1862 212 ASP   B CG  
12658 O  OD1 . ASP   B 212 ? 0.5913 0.3907 0.5267 -0.0077 0.0193  -0.1939 212 ASP   B OD1 
12659 O  OD2 . ASP   B 212 ? 0.5764 0.3549 0.5401 -0.0163 0.0238  -0.1891 212 ASP   B OD2 
12664 N  N   . LYS   B 213 ? 0.4774 0.2923 0.3840 0.0141  0.0233  -0.1760 213 LYS   B N   
12665 C  CA  . LYS   B 213 ? 0.5430 0.3774 0.4299 0.0155  0.0189  -0.1765 213 LYS   B CA  
12666 C  C   . LYS   B 213 ? 0.5201 0.3679 0.4081 0.0070  0.0118  -0.1836 213 LYS   B C   
12667 O  O   . LYS   B 213 ? 0.4905 0.3538 0.3762 0.0060  0.0077  -0.1789 213 LYS   B O   
12668 C  CB  . LYS   B 213 ? 0.6302 0.4698 0.5062 0.0217  0.0210  -0.1800 213 LYS   B CB  
12669 C  CG  . LYS   B 213 ? 0.7770 0.6367 0.6301 0.0215  0.0164  -0.1830 213 LYS   B CG  
12670 C  CD  . LYS   B 213 ? 0.7797 0.6448 0.6332 0.0238  0.0176  -0.1915 213 LYS   B CD  
12671 C  CE  . LYS   B 213 ? 0.8527 0.7401 0.6898 0.0238  0.0127  -0.1932 213 LYS   B CE  
12672 N  NZ  . LYS   B 213 ? 0.9000 0.7951 0.7259 0.0312  0.0166  -0.1884 213 LYS   B NZ  
12686 N  N   . GLU   B 214 ? 0.5269 0.3707 0.4210 0.0013  0.0102  -0.1947 214 GLU   B N   
12687 C  CA  . GLU   B 214 ? 0.5428 0.4001 0.4383 -0.0067 0.0032  -0.2027 214 GLU   B CA  
12688 C  C   . GLU   B 214 ? 0.4992 0.3579 0.4065 -0.0128 0.0008  -0.1967 214 GLU   B C   
12689 O  O   . GLU   B 214 ? 0.4908 0.3675 0.3951 -0.0158 -0.0052 -0.1963 214 GLU   B O   
12690 C  CB  . GLU   B 214 ? 0.5897 0.4425 0.4997 -0.0117 0.0029  -0.2158 214 GLU   B CB  
12691 C  CG  . GLU   B 214 ? 0.8302 0.6801 0.7083 -0.0064 0.0046  -0.2231 214 GLU   B CG  
12692 C  CD  . GLU   B 214 ? 0.8418 0.7161 0.7115 -0.0034 0.0002  -0.2239 214 GLU   B CD  
12693 O  OE1 . GLU   B 214 ? 0.7576 0.6504 0.6337 -0.0083 -0.0065 -0.2256 214 GLU   B OE1 
12694 O  OE2 . GLU   B 214 ? 0.8724 0.7485 0.7322 0.0039  0.0035  -0.2219 214 GLU   B OE2 
12701 N  N   . LYS   B 215 ? 0.4698 0.3109 0.3939 -0.0142 0.0057  -0.1914 215 LYS   B N   
12702 C  CA  . LYS   B 215 ? 0.5085 0.3463 0.4354 -0.0202 0.0050  -0.1848 215 LYS   B CA  
12703 C  C   . LYS   B 215 ? 0.4373 0.2888 0.3663 -0.0161 0.0038  -0.1750 215 LYS   B C   
12704 O  O   . LYS   B 215 ? 0.4316 0.2939 0.3592 -0.0209 -0.0006 -0.1729 215 LYS   B O   
12705 C  CB  . LYS   B 215 ? 0.4928 0.3108 0.4440 -0.0215 0.0114  -0.1791 215 LYS   B CB  
12706 C  CG  . LYS   B 215 ? 0.5224 0.3373 0.4872 -0.0274 0.0120  -0.1712 215 LYS   B CG  
12707 C  CD  . LYS   B 215 ? 0.6049 0.4007 0.5828 -0.0311 0.0172  -0.1677 215 LYS   B CD  
12708 C  CE  . LYS   B 215 ? 0.6446 0.4422 0.6369 -0.0399 0.0153  -0.1654 215 LYS   B CE  
12709 N  NZ  . LYS   B 215 ? 0.6688 0.4835 0.6555 -0.0423 0.0099  -0.1641 215 LYS   B NZ  
12723 N  N   . VAL   B 216 ? 0.4548 0.3022 0.3672 -0.0073 0.0078  -0.1685 216 VAL   B N   
12724 C  CA  . VAL   B 216 ? 0.4076 0.2683 0.3175 -0.0021 0.0068  -0.1545 216 VAL   B CA  
12725 C  C   . VAL   B 216 ? 0.4020 0.2853 0.3002 -0.0032 -0.0005 -0.1576 216 VAL   B C   
12726 O  O   . VAL   B 216 ? 0.4180 0.3118 0.3160 -0.0048 -0.0034 -0.1479 216 VAL   B O   
12727 C  CB  . VAL   B 216 ? 0.4303 0.2848 0.3274 0.0077  0.0119  -0.1468 216 VAL   B CB  
12728 C  CG1 . VAL   B 216 ? 0.4194 0.2884 0.3107 0.0127  0.0104  -0.1336 216 VAL   B CG1 
12729 C  CG2 . VAL   B 216 ? 0.4181 0.2523 0.3271 0.0093  0.0188  -0.1419 216 VAL   B CG2 
12739 N  N   . LYS   B 217 ? 0.3954 0.2871 0.2842 -0.0020 -0.0030 -0.1699 217 LYS   B N   
12740 C  CA  . LYS   B 217 ? 0.4004 0.3167 0.2829 -0.0020 -0.0095 -0.1717 217 LYS   B CA  
12741 C  C   . LYS   B 217 ? 0.3990 0.3235 0.2864 -0.0109 -0.0155 -0.1748 217 LYS   B C   
12742 O  O   . LYS   B 217 ? 0.3989 0.3408 0.2830 -0.0106 -0.0198 -0.1682 217 LYS   B O   
12743 C  CB  . LYS   B 217 ? 0.4899 0.4111 0.3581 0.0002  -0.0102 -0.1794 217 LYS   B CB  
12744 C  CG  . LYS   B 217 ? 0.5789 0.5252 0.4383 0.0012  -0.0160 -0.1799 217 LYS   B CG  
12745 C  CD  . LYS   B 217 ? 0.7024 0.6535 0.5491 0.0035  -0.0161 -0.1874 217 LYS   B CD  
12746 C  CE  . LYS   B 217 ? 0.7972 0.7734 0.6337 0.0049  -0.0216 -0.1869 217 LYS   B CE  
12747 N  NZ  . LYS   B 217 ? 0.8465 0.8275 0.6740 0.0072  -0.0213 -0.1946 217 LYS   B NZ  
12761 N  N   . LYS   B 218 ? 0.4007 0.3140 0.3022 -0.0184 -0.0154 -0.1827 218 LYS   B N   
12762 C  CA  . LYS   B 218 ? 0.4377 0.3584 0.3489 -0.0276 -0.0207 -0.1863 218 LYS   B CA  
12763 C  C   . LYS   B 218 ? 0.4240 0.3434 0.3414 -0.0292 -0.0198 -0.1730 218 LYS   B C   
12764 O  O   . LYS   B 218 ? 0.4290 0.3653 0.3482 -0.0320 -0.0249 -0.1686 218 LYS   B O   
12765 C  CB  . LYS   B 218 ? 0.4938 0.4024 0.4237 -0.0348 -0.0198 -0.1961 218 LYS   B CB  
12766 C  CG  . LYS   B 218 ? 0.6868 0.5952 0.6157 -0.0447 -0.0236 -0.1990 218 LYS   B CG  
12767 C  CD  . LYS   B 218 ? 0.6868 0.5871 0.6328 -0.0513 -0.0236 -0.2093 218 LYS   B CD  
12768 C  CE  . LYS   B 218 ? 0.6065 0.5186 0.5758 -0.0608 -0.0288 -0.2128 218 LYS   B CE  
12769 N  NZ  . LYS   B 218 ? 0.6796 0.6051 0.6377 -0.0616 -0.0327 -0.2049 218 LYS   B NZ  
12783 N  N   . VAL   B 219 ? 0.3828 0.2846 0.3097 -0.0268 -0.0132 -0.1632 219 VAL   B N   
12784 C  CA  . VAL   B 219 ? 0.3960 0.2945 0.3253 -0.0273 -0.0112 -0.1471 219 VAL   B CA  
12785 C  C   . VAL   B 219 ? 0.3873 0.3043 0.3095 -0.0218 -0.0138 -0.1363 219 VAL   B C   
12786 O  O   . VAL   B 219 ? 0.3890 0.3154 0.3141 -0.0248 -0.0163 -0.1290 219 VAL   B O   
12787 C  CB  . VAL   B 219 ? 0.3885 0.2672 0.3310 -0.0244 -0.0036 -0.1389 219 VAL   B CB  
12788 C  CG1 . VAL   B 219 ? 0.4114 0.2896 0.3496 -0.0226 -0.0015 -0.1222 219 VAL   B CG1 
12789 C  CG2 . VAL   B 219 ? 0.4607 0.3198 0.4080 -0.0305 -0.0004 -0.1466 219 VAL   B CG2 
12799 N  N   . SER   B 220 ? 0.4076 0.3282 0.3124 -0.0138 -0.0127 -0.1350 220 SER   B N   
12800 C  CA  . SER   B 220 ? 0.3722 0.3093 0.2713 -0.0079 -0.0139 -0.1244 220 SER   B CA  
12801 C  C   . SER   B 220 ? 0.3268 0.2874 0.2335 -0.0111 -0.0208 -0.1264 220 SER   B C   
12802 O  O   . SER   B 220 ? 0.3851 0.3524 0.2815 -0.0107 -0.0217 -0.1155 220 SER   B O   
12803 C  CB  . SER   B 220 ? 0.4071 0.3444 0.2894 0.0008  -0.0114 -0.1236 220 SER   B CB  
12804 O  OG  . SER   B 220 ? 0.3730 0.3283 0.2526 0.0057  -0.0131 -0.1153 220 SER   B OG  
12810 N  N   . VAL   B 221 ? 0.4274 0.3932 0.3162 -0.0139 -0.0252 -0.1402 221 VAL   B N   
12811 C  CA  . VAL   B 221 ? 0.4305 0.4206 0.3245 -0.0166 -0.0324 -0.1435 221 VAL   B CA  
12812 C  C   . VAL   B 221 ? 0.4103 0.4012 0.3151 -0.0238 -0.0343 -0.1378 221 VAL   B C   
12813 O  O   . VAL   B 221 ? 0.3995 0.4071 0.3061 -0.0231 -0.0372 -0.1294 221 VAL   B O   
12814 C  CB  . VAL   B 221 ? 0.4914 0.4882 0.3719 -0.0194 -0.0371 -0.1611 221 VAL   B CB  
12815 C  CG1 . VAL   B 221 ? 0.4941 0.5121 0.3846 -0.0255 -0.0447 -0.1660 221 VAL   B CG1 
12816 C  CG2 . VAL   B 221 ? 0.4316 0.4373 0.3055 -0.0113 -0.0363 -0.1639 221 VAL   B CG2 
12826 N  N   . GLU   B 222 ? 0.3820 0.3563 0.3014 -0.0302 -0.0320 -0.1417 222 GLU   B N   
12827 C  CA  . GLU   B 222 ? 0.3805 0.3542 0.3135 -0.0375 -0.0330 -0.1370 222 GLU   B CA  
12828 C  C   . GLU   B 222 ? 0.3450 0.3200 0.2792 -0.0335 -0.0300 -0.1197 222 GLU   B C   
12829 O  O   . GLU   B 222 ? 0.2895 0.2793 0.2301 -0.0354 -0.0332 -0.1138 222 GLU   B O   
12830 C  CB  . GLU   B 222 ? 0.4203 0.3733 0.3652 -0.0439 -0.0297 -0.1430 222 GLU   B CB  
12831 C  CG  . GLU   B 222 ? 0.4392 0.3896 0.4028 -0.0504 -0.0289 -0.1365 222 GLU   B CG  
12832 C  CD  . GLU   B 222 ? 0.5103 0.4409 0.4896 -0.0565 -0.0247 -0.1407 222 GLU   B CD  
12833 O  OE1 . GLU   B 222 ? 0.5814 0.5043 0.5557 -0.0600 -0.0256 -0.1548 222 GLU   B OE1 
12834 O  OE2 . GLU   B 222 ? 0.5940 0.5131 0.5737 -0.0575 -0.0203 -0.1301 222 GLU   B OE2 
12841 N  N   . LYS   B 223 ? 0.3756 0.3355 0.3019 -0.0282 -0.0239 -0.1118 223 LYS   B N   
12842 C  CA  . LYS   B 223 ? 0.3170 0.2781 0.2506 -0.0249 -0.0204 -0.0967 223 LYS   B CA  
12843 C  C   . LYS   B 223 ? 0.3262 0.3068 0.2523 -0.0198 -0.0230 -0.0900 223 LYS   B C   
12844 O  O   . LYS   B 223 ? 0.3487 0.3361 0.2770 -0.0206 -0.0231 -0.0809 223 LYS   B O   
12845 C  CB  . LYS   B 223 ? 0.2965 0.2401 0.2291 -0.0202 -0.0139 -0.0913 223 LYS   B CB  
12846 C  CG  . LYS   B 223 ? 0.3341 0.2577 0.2710 -0.0240 -0.0105 -0.0959 223 LYS   B CG  
12847 C  CD  . LYS   B 223 ? 0.3590 0.2797 0.3095 -0.0326 -0.0116 -0.0983 223 LYS   B CD  
12848 C  CE  . LYS   B 223 ? 0.3716 0.2735 0.3339 -0.0363 -0.0076 -0.1031 223 LYS   B CE  
12849 N  NZ  . LYS   B 223 ? 0.4093 0.3090 0.3825 -0.0451 -0.0087 -0.1060 223 LYS   B NZ  
12863 N  N   . ILE   B 224 ? 0.3499 0.3378 0.2606 -0.0146 -0.0247 -0.0942 224 ILE   B N   
12864 C  CA  . ILE   B 224 ? 0.3372 0.3450 0.2453 -0.0090 -0.0265 -0.0875 224 ILE   B CA  
12865 C  C   . ILE   B 224 ? 0.3643 0.3890 0.2734 -0.0135 -0.0322 -0.0877 224 ILE   B C   
12866 O  O   . ILE   B 224 ? 0.3244 0.3616 0.2394 -0.0110 -0.0321 -0.0774 224 ILE   B O   
12867 C  CB  . ILE   B 224 ? 0.3574 0.3703 0.2490 -0.0023 -0.0267 -0.0917 224 ILE   B CB  
12868 C  CG1 . ILE   B 224 ? 0.3652 0.3632 0.2508 0.0035  -0.0205 -0.0882 224 ILE   B CG1 
12869 C  CG2 . ILE   B 224 ? 0.3713 0.4064 0.2565 0.0024  -0.0295 -0.0864 224 ILE   B CG2 
12870 C  CD1 . ILE   B 224 ? 0.3621 0.3624 0.2368 0.0094  -0.0199 -0.0941 224 ILE   B CD1 
12882 N  N   . THR   B 225 ? 0.3893 0.4166 0.3019 -0.0200 -0.0369 -0.0996 225 THR   B N   
12883 C  CA  . THR   B 225 ? 0.3629 0.4094 0.2874 -0.0250 -0.0430 -0.1014 225 THR   B CA  
12884 C  C   . THR   B 225 ? 0.3459 0.3894 0.2787 -0.0283 -0.0410 -0.0906 225 THR   B C   
12885 O  O   . THR   B 225 ? 0.3255 0.3863 0.2636 -0.0270 -0.0432 -0.0830 225 THR   B O   
12886 C  CB  . THR   B 225 ? 0.4072 0.4548 0.3291 -0.0321 -0.0483 -0.1177 225 THR   B CB  
12887 O  OG1 . THR   B 225 ? 0.4565 0.5103 0.3655 -0.0280 -0.0502 -0.1270 225 THR   B OG1 
12888 C  CG2 . THR   B 225 ? 0.3595 0.4254 0.2950 -0.0384 -0.0545 -0.1196 225 THR   B CG2 
12896 N  N   . THR   B 226 ? 0.3184 0.3429 0.2626 -0.0318 -0.0365 -0.0892 226 THR   B N   
12897 C  CA  . THR   B 226 ? 0.3292 0.3495 0.2815 -0.0347 -0.0336 -0.0793 226 THR   B CA  
12898 C  C   . THR   B 226 ? 0.3046 0.3315 0.2554 -0.0279 -0.0304 -0.0660 226 THR   B C   
12899 O  O   . THR   B 226 ? 0.2969 0.3345 0.2548 -0.0289 -0.0310 -0.0588 226 THR   B O   
12900 C  CB  . THR   B 226 ? 0.3404 0.3388 0.3010 -0.0385 -0.0286 -0.0798 226 THR   B CB  
12901 O  OG1 . THR   B 226 ? 0.3524 0.3446 0.3167 -0.0444 -0.0309 -0.0923 226 THR   B OG1 
12902 C  CG2 . THR   B 226 ? 0.3257 0.3220 0.2984 -0.0417 -0.0257 -0.0707 226 THR   B CG2 
12910 N  N   . LEU   B 227 ? 0.2955 0.3158 0.2354 -0.0211 -0.0268 -0.0628 227 LEU   B N   
12911 C  CA  . LEU   B 227 ? 0.2717 0.2966 0.2101 -0.0149 -0.0231 -0.0512 227 LEU   B CA  
12912 C  C   . LEU   B 227 ? 0.2507 0.2975 0.1884 -0.0117 -0.0267 -0.0472 227 LEU   B C   
12913 O  O   . LEU   B 227 ? 0.2474 0.3012 0.1902 -0.0106 -0.0249 -0.0377 227 LEU   B O   
12914 C  CB  . LEU   B 227 ? 0.2856 0.2987 0.2120 -0.0088 -0.0189 -0.0502 227 LEU   B CB  
12915 C  CG  . LEU   B 227 ? 0.2493 0.2438 0.1850 -0.0103 -0.0145 -0.0506 227 LEU   B CG  
12916 C  CD1 . LEU   B 227 ? 0.3241 0.3082 0.2416 -0.0041 -0.0113 -0.0511 227 LEU   B CD1 
12917 C  CD2 . LEU   B 227 ? 0.2541 0.2432 0.1922 -0.0119 -0.0108 -0.0418 227 LEU   B CD2 
12929 N  N   . LYS   B 228 ? 0.2590 0.3169 0.1889 -0.0103 -0.0313 -0.0542 228 LYS   B N   
12930 C  CA  . LYS   B 228 ? 0.2928 0.3725 0.2153 -0.0062 -0.0348 -0.0504 228 LYS   B CA  
12931 C  C   . LYS   B 228 ? 0.2419 0.3363 0.1824 -0.0111 -0.0385 -0.0476 228 LYS   B C   
12932 O  O   . LYS   B 228 ? 0.2319 0.3423 0.1717 -0.0074 -0.0392 -0.0389 228 LYS   B O   
12933 C  CB  . LYS   B 228 ? 0.3113 0.4012 0.2275 -0.0038 -0.0388 -0.0594 228 LYS   B CB  
12934 C  CG  . LYS   B 228 ? 0.3853 0.4640 0.2853 0.0021  -0.0350 -0.0613 228 LYS   B CG  
12935 C  CD  . LYS   B 228 ? 0.4152 0.5091 0.3050 0.0079  -0.0374 -0.0644 228 LYS   B CD  
12936 C  CE  . LYS   B 228 ? 0.4516 0.5387 0.3340 0.0153  -0.0323 -0.0616 228 LYS   B CE  
12937 N  NZ  . LYS   B 228 ? 0.5426 0.6389 0.4056 0.0198  -0.0344 -0.0681 228 LYS   B NZ  
12951 N  N   . ASN   B 229 ? 0.2712 0.3578 0.2155 -0.0191 -0.0406 -0.0544 229 ASN   B N   
12952 C  CA  . ASN   B 229 ? 0.2735 0.3723 0.2313 -0.0248 -0.0442 -0.0530 229 ASN   B CA  
12953 C  C   . ASN   B 229 ? 0.2314 0.3232 0.2043 -0.0257 -0.0386 -0.0425 229 ASN   B C   
12954 O  O   . ASN   B 229 ? 0.2632 0.3642 0.2411 -0.0291 -0.0404 -0.0387 229 ASN   B O   
12955 C  CB  . ASN   B 229 ? 0.3120 0.4103 0.2751 -0.0332 -0.0493 -0.0660 229 ASN   B CB  
12956 C  CG  . ASN   B 229 ? 0.3706 0.4800 0.3225 -0.0329 -0.0554 -0.0777 229 ASN   B CG  
12957 O  OD1 . ASN   B 229 ? 0.3622 0.4883 0.3071 -0.0265 -0.0574 -0.0743 229 ASN   B OD1 
12958 N  ND2 . ASN   B 229 ? 0.4136 0.5150 0.3661 -0.0394 -0.0580 -0.0912 229 ASN   B ND2 
12965 N  N   . ASP   B 230 ? 0.2436 0.3174 0.2101 -0.0228 -0.0322 -0.0379 230 ASP   B N   
12966 C  CA  . ASP   B 230 ? 0.2514 0.3178 0.2232 -0.0233 -0.0266 -0.0285 230 ASP   B CA  
12967 C  C   . ASP   B 230 ? 0.2326 0.3136 0.2127 -0.0172 -0.0246 -0.0176 230 ASP   B C   
12968 O  O   . ASP   B 230 ? 0.2415 0.3264 0.2095 -0.0110 -0.0242 -0.0156 230 ASP   B O   
12969 C  CB  . ASP   B 230 ? 0.2186 0.2656 0.1955 -0.0226 -0.0208 -0.0277 230 ASP   B CB  
12970 C  CG  . ASP   B 230 ? 0.2745 0.3144 0.2531 -0.0233 -0.0153 -0.0193 230 ASP   B CG  
12971 O  OD1 . ASP   B 230 ? 0.3038 0.3398 0.2914 -0.0291 -0.0149 -0.0200 230 ASP   B OD1 
12972 O  OD2 . ASP   B 230 ? 0.2654 0.3059 0.2442 -0.0180 -0.0111 -0.0125 230 ASP   B OD2 
12977 N  N   . PRO   B 231 ? 0.2725 0.3589 0.2611 -0.0188 -0.0228 -0.0102 231 PRO   B N   
12978 C  CA  . PRO   B 231 ? 0.2758 0.3738 0.2691 -0.0130 -0.0199 0.0005  231 PRO   B CA  
12979 C  C   . PRO   B 231 ? 0.2703 0.3576 0.2558 -0.0072 -0.0133 0.0059  231 PRO   B C   
12980 O  O   . PRO   B 231 ? 0.2554 0.3523 0.2432 -0.0012 -0.0117 0.0122  231 PRO   B O   
12981 C  CB  . PRO   B 231 ? 0.2938 0.3949 0.3014 -0.0170 -0.0182 0.0051  231 PRO   B CB  
12982 C  CG  . PRO   B 231 ? 0.3392 0.4370 0.3454 -0.0249 -0.0227 -0.0030 231 PRO   B CG  
12983 C  CD  . PRO   B 231 ? 0.3061 0.3891 0.3059 -0.0260 -0.0231 -0.0115 231 PRO   B CD  
12991 N  N   . VAL   B 232 ? 0.2277 0.2980 0.2155 -0.0092 -0.0094 0.0036  232 VAL   B N   
12992 C  CA  . VAL   B 232 ? 0.2287 0.2892 0.2123 -0.0044 -0.0036 0.0073  232 VAL   B CA  
12993 C  C   . VAL   B 232 ? 0.2470 0.3025 0.2131 -0.0005 -0.0049 0.0032  232 VAL   B C   
12994 O  O   . VAL   B 232 ? 0.2194 0.2809 0.1870 0.0053  -0.0028 0.0078  232 VAL   B O   
12995 C  CB  . VAL   B 232 ? 0.2507 0.2954 0.2339 -0.0076 0.0012  0.0078  232 VAL   B CB  
12996 C  CG1 . VAL   B 232 ? 0.2099 0.2470 0.1928 -0.0032 0.0063  0.0103  232 VAL   B CG1 
12997 C  CG2 . VAL   B 232 ? 0.2672 0.3164 0.2633 -0.0109 0.0031  0.0120  232 VAL   B CG2 
13007 N  N   . ALA   B 233 ? 0.2239 0.2713 0.1882 -0.0038 -0.0076 -0.0053 233 ALA   B N   
13008 C  CA  . ALA   B 233 ? 0.2325 0.2750 0.1864 -0.0001 -0.0084 -0.0104 233 ALA   B CA  
13009 C  C   . ALA   B 233 ? 0.2587 0.3158 0.2008 0.0034  -0.0126 -0.0114 233 ALA   B C   
13010 O  O   . ALA   B 233 ? 0.2777 0.3357 0.2143 0.0087  -0.0115 -0.0113 233 ALA   B O   
13011 C  CB  . ALA   B 233 ? 0.2683 0.2962 0.2147 -0.0046 -0.0098 -0.0188 233 ALA   B CB  
13017 N  N   . GLY   B 234 ? 0.1922 0.2658 0.1486 0.0006  -0.0173 -0.0121 234 GLY   B N   
13018 C  CA  . GLY   B 234 ? 0.2580 0.3470 0.1998 0.0038  -0.0220 -0.0134 234 GLY   B CA  
13019 C  C   . GLY   B 234 ? 0.2576 0.3639 0.2046 0.0094  -0.0208 -0.0028 234 GLY   B C   
13020 O  O   . GLY   B 234 ? 0.2241 0.3456 0.1675 0.0137  -0.0237 -0.0026 234 GLY   B O   
13024 N  N   . GLN   B 235 ? 0.2646 0.3702 0.2230 0.0099  -0.0162 0.0062  235 GLN   B N   
13025 C  CA  . GLN   B 235 ? 0.2626 0.3837 0.2257 0.0153  -0.0145 0.0173  235 GLN   B CA  
13026 C  C   . GLN   B 235 ? 0.2009 0.3159 0.1789 0.0185  -0.0064 0.0260  235 GLN   B C   
13027 O  O   . GLN   B 235 ? 0.2224 0.3408 0.1927 0.0250  -0.0031 0.0326  235 GLN   B O   
13028 C  CB  . GLN   B 235 ? 0.2647 0.4013 0.2421 0.0116  -0.0184 0.0191  235 GLN   B CB  
13029 C  CG  . GLN   B 235 ? 0.3198 0.4670 0.2889 0.0080  -0.0266 0.0107  235 GLN   B CG  
13030 C  CD  . GLN   B 235 ? 0.3523 0.5164 0.3134 0.0140  -0.0300 0.0113  235 GLN   B CD  
13031 O  OE1 . GLN   B 235 ? 0.3761 0.5474 0.3356 0.0212  -0.0262 0.0212  235 GLN   B OE1 
13032 N  NE2 . GLN   B 235 ? 0.3734 0.5434 0.3248 0.0111  -0.0367 0.0008  235 GLN   B NE2 
13041 N  N   . GLY   B 236 ? 0.2310 0.3329 0.2096 0.0143  -0.0033 0.0261  236 GLY   B N   
13042 C  CA  . GLY   B 236 ? 0.2224 0.3184 0.2101 0.0167  0.0041  0.0330  236 GLY   B CA  
13043 C  C   . GLY   B 236 ? 0.2107 0.2952 0.1920 0.0202  0.0084  0.0325  236 GLY   B C   
13044 O  O   . GLY   B 236 ? 0.1581 0.2466 0.1472 0.0253  0.0134  0.0398  236 GLY   B O   
13048 N  N   A MET   B 237 ? 0.2272 0.2999 0.1991 0.0181  0.0067  0.0249  237 MET   B N   
13049 N  N   B MET   B 237 ? 0.2272 0.2998 0.1990 0.0181  0.0067  0.0249  237 MET   B N   
13050 C  CA  A MET   B 237 ? 0.2320 0.2937 0.1972 0.0212  0.0104  0.0238  237 MET   B CA  
13051 C  CA  B MET   B 237 ? 0.2320 0.2936 0.1971 0.0211  0.0104  0.0238  237 MET   B CA  
13052 C  C   A MET   B 237 ? 0.2053 0.2753 0.1654 0.0275  0.0101  0.0262  237 MET   B C   
13053 C  C   B MET   B 237 ? 0.2054 0.2754 0.1654 0.0275  0.0101  0.0262  237 MET   B C   
13054 O  O   A MET   B 237 ? 0.1910 0.2605 0.1535 0.0319  0.0151  0.0316  237 MET   B O   
13055 O  O   B MET   B 237 ? 0.1910 0.2606 0.1536 0.0319  0.0151  0.0316  237 MET   B O   
13056 C  CB  A MET   B 237 ? 0.2509 0.2975 0.2099 0.0173  0.0091  0.0160  237 MET   B CB  
13057 C  CB  B MET   B 237 ? 0.2508 0.2976 0.2097 0.0172  0.0090  0.0159  237 MET   B CB  
13058 C  CG  A MET   B 237 ? 0.2595 0.2966 0.2234 0.0121  0.0112  0.0149  237 MET   B CG  
13059 C  CG  B MET   B 237 ? 0.2601 0.2981 0.2265 0.0121  0.0109  0.0149  237 MET   B CG  
13060 S  SD  A MET   B 237 ? 0.2572 0.2773 0.2174 0.0106  0.0127  0.0099  237 MET   B SD  
13061 S  SD  B MET   B 237 ? 0.2995 0.3296 0.2666 0.0141  0.0180  0.0190  237 MET   B SD  
13062 C  CE  A MET   B 237 ? 0.2953 0.3119 0.2547 0.0145  0.0189  0.0145  237 MET   B CE  
13063 C  CE  B MET   B 237 ? 0.2917 0.3080 0.2526 0.0139  0.0181  0.0136  237 MET   B CE  
13082 N  N   . PRO   B 238 ? 0.2086 0.2885 0.1613 0.0282  0.0046  0.0230  238 PRO   B N   
13083 C  CA  . PRO   B 238 ? 0.2110 0.3008 0.1556 0.0347  0.0045  0.0259  238 PRO   B CA  
13084 C  C   . PRO   B 238 ? 0.1959 0.2983 0.1499 0.0399  0.0086  0.0377  238 PRO   B C   
13085 O  O   . PRO   B 238 ? 0.1859 0.2898 0.1406 0.0454  0.0127  0.0430  238 PRO   B O   
13086 C  CB  . PRO   B 238 ? 0.2158 0.3155 0.1538 0.0334  -0.0025 0.0190  238 PRO   B CB  
13087 C  CG  . PRO   B 238 ? 0.2449 0.3385 0.1831 0.0256  -0.0061 0.0129  238 PRO   B CG  
13088 C  CD  . PRO   B 238 ? 0.2244 0.3018 0.1707 0.0229  -0.0013 0.0136  238 PRO   B CD  
13096 N  N   . THR   B 239 ? 0.1801 0.2920 0.1467 0.0380  0.0077  0.0423  239 THR   B N   
13097 C  CA  . THR   B 239 ? 0.2077 0.3315 0.1798 0.0431  0.0117  0.0542  239 THR   B CA  
13098 C  C   . THR   B 239 ? 0.1667 0.2822 0.1572 0.0441  0.0197  0.0597  239 THR   B C   
13099 O  O   . THR   B 239 ? 0.1850 0.3042 0.1760 0.0499  0.0249  0.0679  239 THR   B O   
13100 C  CB  . THR   B 239 ? 0.1997 0.3396 0.1841 0.0412  0.0078  0.0573  239 THR   B CB  
13101 O  OG1 . THR   B 239 ? 0.2185 0.3667 0.1898 0.0396  0.0000  0.0504  239 THR   B OG1 
13102 C  CG2 . THR   B 239 ? 0.2179 0.3719 0.2103 0.0472  0.0116  0.0702  239 THR   B CG2 
13110 N  N   . TYR   B 240 ? 0.1790 0.2803 0.1691 0.0384  0.0214  0.0554  240 TYR   B N   
13111 C  CA  . TYR   B 240 ? 0.1523 0.2469 0.1596 0.0387  0.0287  0.0591  240 TYR   B CA  
13112 C  C   . TYR   B 240 ? 0.1913 0.2683 0.1882 0.0368  0.0313  0.0532  240 TYR   B C   
13113 O  O   . TYR   B 240 ? 0.2110 0.2829 0.2180 0.0378  0.0375  0.0555  240 TYR   B O   
13114 C  CB  . TYR   B 240 ? 0.1612 0.2565 0.1755 0.0346  0.0292  0.0605  240 TYR   B CB  
13115 C  CG  . TYR   B 240 ? 0.1630 0.2756 0.1840 0.0368  0.0271  0.0675  240 TYR   B CG  
13116 C  CD1 . TYR   B 240 ? 0.1393 0.2632 0.1713 0.0431  0.0316  0.0783  240 TYR   B CD1 
13117 C  CD2 . TYR   B 240 ? 0.1764 0.2960 0.1965 0.0327  0.0206  0.0645  240 TYR   B CD2 
13118 C  CE1 . TYR   B 240 ? 0.1450 0.2864 0.1836 0.0459  0.0296  0.0858  240 TYR   B CE1 
13119 C  CE2 . TYR   B 240 ? 0.1971 0.3341 0.2216 0.0347  0.0183  0.0709  240 TYR   B CE2 
13120 C  CZ  . TYR   B 240 ? 0.1938 0.3421 0.2257 0.0417  0.0225  0.0822  240 TYR   B CZ  
13121 O  OH  . TYR   B 240 ? 0.1924 0.3602 0.2329 0.0444  0.0201  0.0897  240 TYR   B OH  
13131 N  N   . GLY   B 241 ? 0.1591 0.2295 0.1479 0.0343  0.0270  0.0451  241 GLY   B N   
13132 C  CA  . GLY   B 241 ? 0.1679 0.2235 0.1492 0.0327  0.0287  0.0396  241 GLY   B CA  
13133 C  C   . GLY   B 241 ? 0.1528 0.1991 0.1414 0.0277  0.0302  0.0362  241 GLY   B C   
13134 O  O   . GLY   B 241 ? 0.1599 0.2108 0.1523 0.0244  0.0292  0.0377  241 GLY   B O   
13138 N  N   . THR   B 242 ? 0.1615 0.1577 0.1525 0.0589  0.0326  0.0285  242 THR   B N   
13139 C  CA  . THR   B 242 ? 0.1693 0.1593 0.1625 0.0570  0.0340  0.0247  242 THR   B CA  
13140 C  C   . THR   B 242 ? 0.1871 0.1784 0.1902 0.0590  0.0383  0.0280  242 THR   B C   
13141 O  O   . THR   B 242 ? 0.1793 0.1705 0.1873 0.0571  0.0393  0.0262  242 THR   B O   
13142 C  CB  . THR   B 242 ? 0.1497 0.1321 0.1423 0.0559  0.0350  0.0195  242 THR   B CB  
13143 O  OG1 . THR   B 242 ? 0.1527 0.1330 0.1463 0.0579  0.0384  0.0206  242 THR   B OG1 
13144 C  CG2 . THR   B 242 ? 0.1916 0.1705 0.1693 0.0542  0.0308  0.0154  242 THR   B CG2 
13152 N  N   . ALA   B 243 ? 0.1869 0.1797 0.1969 0.0624  0.0412  0.0330  243 ALA   B N   
13153 C  CA  . ALA   B 243 ? 0.1847 0.1772 0.2024 0.0649  0.0456  0.0368  243 ALA   B CA  
13154 C  C   . ALA   B 243 ? 0.1734 0.1747 0.2019 0.0660  0.0442  0.0395  243 ALA   B C   
13155 O  O   . ALA   B 243 ? 0.2115 0.2119 0.2440 0.0667  0.0473  0.0409  243 ALA   B O   
13156 C  CB  . ALA   B 243 ? 0.1372 0.1305 0.1618 0.0664  0.0472  0.0416  243 ALA   B CB  
13162 N  N   . ILE   B 244 ? 0.1762 0.1837 0.1965 0.0646  0.0391  0.0397  244 ILE   B N   
13163 C  CA  . ILE   B 244 ? 0.1585 0.1756 0.1858 0.0647  0.0372  0.0414  244 ILE   B CA  
13164 C  C   . ILE   B 244 ? 0.1821 0.1953 0.2112 0.0625  0.0402  0.0368  244 ILE   B C   
13165 O  O   . ILE   B 244 ? 0.1643 0.1851 0.2040 0.0635  0.0410  0.0385  244 ILE   B O   
13166 C  CB  . ILE   B 244 ? 0.1533 0.1775 0.1747 0.0623  0.0313  0.0405  244 ILE   B CB  
13167 C  CG1 . ILE   B 244 ? 0.2054 0.2404 0.2256 0.0630  0.0289  0.0439  244 ILE   B CG1 
13168 C  CG2 . ILE   B 244 ? 0.1661 0.1833 0.1751 0.0567  0.0299  0.0334  244 ILE   B CG2 
13169 C  CD1 . ILE   B 244 ? 0.1915 0.2346 0.2088 0.0600  0.0232  0.0433  244 ILE   B CD1 
13181 N  N   . LEU   B 245 ? 0.1872 0.1908 0.2115 0.0595  0.0420  0.0313  245 LEU   B N   
13182 C  CA  . LEU   B 245 ? 0.1493 0.1502 0.1797 0.0561  0.0448  0.0263  245 LEU   B CA  
13183 C  C   . LEU   B 245 ? 0.1818 0.1796 0.2171 0.0588  0.0507  0.0273  245 LEU   B C   
13184 O  O   . LEU   B 245 ? 0.1686 0.1678 0.2124 0.0568  0.0533  0.0241  245 LEU   B O   
13185 C  CB  . LEU   B 245 ? 0.1278 0.1195 0.1493 0.0522  0.0440  0.0206  245 LEU   B CB  
13186 C  CG  . LEU   B 245 ? 0.1778 0.1683 0.1843 0.0488  0.0386  0.0179  245 LEU   B CG  
13187 C  CD1 . LEU   B 245 ? 0.1944 0.1753 0.1919 0.0472  0.0375  0.0140  245 LEU   B CD1 
13188 C  CD2 . LEU   B 245 ? 0.2059 0.1989 0.2103 0.0446  0.0374  0.0156  245 LEU   B CD2 
13200 N  N   . VAL   B 246 ? 0.1465 0.1434 0.1925 0.0610  0.0523  0.0307  246 VAL   B N   
13201 C  CA  . VAL   B 246 ? 0.1723 0.1647 0.2220 0.0597  0.0558  0.0302  246 VAL   B CA  
13202 C  C   . VAL   B 246 ? 0.1983 0.1966 0.2537 0.0613  0.0570  0.0312  246 VAL   B C   
13203 O  O   . VAL   B 246 ? 0.1579 0.1548 0.2212 0.0587  0.0601  0.0266  246 VAL   B O   
13204 C  CB  . VAL   B 246 ? 0.1735 0.1635 0.2263 0.0612  0.0565  0.0344  246 VAL   B CB  
13205 C  CG1 . VAL   B 246 ? 0.1831 0.1692 0.2406 0.0609  0.0603  0.0347  246 VAL   B CG1 
13206 C  CG2 . VAL   B 246 ? 0.2065 0.1900 0.2487 0.0592  0.0560  0.0328  246 VAL   B CG2 
13216 N  N   . ASN   B 247 ? 0.1979 0.2067 0.2629 0.0655  0.0550  0.0365  247 ASN   B N   
13217 C  CA  . ASN   B 247 ? 0.2205 0.2366 0.2910 0.0675  0.0558  0.0381  247 ASN   B CA  
13218 C  C   . ASN   B 247 ? 0.1737 0.1967 0.2506 0.0655  0.0566  0.0337  247 ASN   B C   
13219 O  O   . ASN   B 247 ? 0.1985 0.2238 0.2797 0.0648  0.0592  0.0315  247 ASN   B O   
13220 C  CB  . ASN   B 247 ? 0.2199 0.2462 0.3002 0.0723  0.0529  0.0453  247 ASN   B CB  
13221 C  CG  . ASN   B 247 ? 0.2527 0.2721 0.3292 0.0742  0.0538  0.0497  247 ASN   B CG  
13222 O  OD1 . ASN   B 247 ? 0.2665 0.2771 0.3461 0.0723  0.0576  0.0472  247 ASN   B OD1 
13223 N  ND2 . ASN   B 247 ? 0.2080 0.2340 0.2891 0.0777  0.0507  0.0562  247 ASN   B ND2 
13230 N  N   . ILE   B 248 ? 0.1420 0.1658 0.2102 0.0628  0.0532  0.0319  248 ILE   B N   
13231 C  CA  . ILE   B 248 ? 0.1578 0.1846 0.2209 0.0568  0.0516  0.0268  248 ILE   B CA  
13232 C  C   . ILE   B 248 ? 0.1932 0.2103 0.2513 0.0532  0.0568  0.0207  248 ILE   B C   
13233 O  O   . ILE   B 248 ? 0.1776 0.2000 0.2444 0.0511  0.0594  0.0179  248 ILE   B O   
13234 C  CB  . ILE   B 248 ? 0.1831 0.2092 0.2331 0.0525  0.0456  0.0255  248 ILE   B CB  
13235 C  CG1 . ILE   B 248 ? 0.1999 0.2347 0.2480 0.0556  0.0407  0.0309  248 ILE   B CG1 
13236 C  CG2 . ILE   B 248 ? 0.2291 0.2548 0.2694 0.0460  0.0445  0.0204  248 ILE   B CG2 
13237 C  CD1 . ILE   B 248 ? 0.2371 0.2690 0.2703 0.0523  0.0355  0.0297  248 ILE   B CD1 
13249 N  N   . ILE   B 249 ? 0.1889 0.1950 0.2432 0.0525  0.0584  0.0183  249 ILE   B N   
13250 C  CA  . ILE   B 249 ? 0.1798 0.1772 0.2308 0.0485  0.0626  0.0126  249 ILE   B CA  
13251 C  C   . ILE   B 249 ? 0.1634 0.1626 0.2297 0.0499  0.0673  0.0122  249 ILE   B C   
13252 O  O   . ILE   B 249 ? 0.1969 0.1948 0.2600 0.0466  0.0708  0.0077  249 ILE   B O   
13253 C  CB  . ILE   B 249 ? 0.1653 0.1524 0.2094 0.0471  0.0620  0.0100  249 ILE   B CB  
13254 C  CG1 . ILE   B 249 ? 0.1796 0.1651 0.2100 0.0447  0.0556  0.0101  249 ILE   B CG1 
13255 C  CG2 . ILE   B 249 ? 0.1785 0.1572 0.2172 0.0426  0.0655  0.0043  249 ILE   B CG2 
13256 C  CD1 . ILE   B 249 ? 0.1937 0.1814 0.2171 0.0397  0.0528  0.0073  249 ILE   B CD1 
13268 N  N   . ASN   B 250 ? 0.1865 0.1844 0.2522 0.0532  0.0663  0.0165  250 ASN   B N   
13269 C  CA  . ASN   B 250 ? 0.1620 0.1597 0.2402 0.0537  0.0694  0.0165  250 ASN   B CA  
13270 C  C   . ASN   B 250 ? 0.1682 0.1760 0.2555 0.0553  0.0710  0.0162  250 ASN   B C   
13271 O  O   . ASN   B 250 ? 0.1966 0.2022 0.2847 0.0535  0.0746  0.0124  250 ASN   B O   
13272 C  CB  . ASN   B 250 ? 0.1748 0.1692 0.2529 0.0571  0.0686  0.0215  250 ASN   B CB  
13273 C  CG  . ASN   B 250 ? 0.1706 0.1616 0.2577 0.0572  0.0725  0.0206  250 ASN   B CG  
13274 O  OD1 . ASN   B 250 ? 0.1706 0.1540 0.2530 0.0531  0.0751  0.0161  250 ASN   B OD1 
13275 N  ND2 . ASN   B 250 ? 0.2073 0.2020 0.2988 0.0618  0.0727  0.0250  250 ASN   B ND2 
13282 N  N   . GLU   B 251 ? 0.1831 0.2019 0.2744 0.0586  0.0682  0.0201  251 GLU   B N   
13283 C  CA  . GLU   B 251 ? 0.2294 0.2599 0.3276 0.0601  0.0692  0.0205  251 GLU   B CA  
13284 C  C   . GLU   B 251 ? 0.2316 0.2636 0.3284 0.0547  0.0729  0.0138  251 GLU   B C   
13285 O  O   . GLU   B 251 ? 0.2065 0.2471 0.3152 0.0547  0.0752  0.0120  251 GLU   B O   
13286 C  CB  . GLU   B 251 ? 0.2404 0.2851 0.3495 0.0642  0.0648  0.0265  251 GLU   B CB  
13287 C  CG  . GLU   B 251 ? 0.3549 0.3999 0.4640 0.0696  0.0618  0.0331  251 GLU   B CG  
13288 C  CD  . GLU   B 251 ? 0.4971 0.5510 0.5973 0.0731  0.0564  0.0394  251 GLU   B CD  
13289 O  OE1 . GLU   B 251 ? 0.5051 0.5710 0.6131 0.0717  0.0548  0.0387  251 GLU   B OE1 
13290 O  OE2 . GLU   B 251 ? 0.4658 0.5203 0.5751 0.0767  0.0541  0.0451  251 GLU   B OE2 
13297 N  N   . ASN   B 252 ? 0.2127 0.2380 0.3020 0.0505  0.0734  0.0103  252 ASN   B N   
13298 C  CA  . ASN   B 252 ? 0.2148 0.2382 0.2961 0.0434  0.0762  0.0039  252 ASN   B CA  
13299 C  C   . ASN   B 252 ? 0.2034 0.2166 0.2828 0.0409  0.0805  -0.0009 252 ASN   B C   
13300 O  O   . ASN   B 252 ? 0.2035 0.2152 0.2806 0.0352  0.0838  -0.0063 252 ASN   B O   
13301 C  CB  . ASN   B 252 ? 0.2105 0.2295 0.2791 0.0376  0.0706  0.0024  252 ASN   B CB  
13302 C  CG  . ASN   B 252 ? 0.2377 0.2671 0.3051 0.0359  0.0650  0.0047  252 ASN   B CG  
13303 O  OD1 . ASN   B 252 ? 0.2837 0.3197 0.3487 0.0318  0.0657  0.0023  252 ASN   B OD1 
13304 N  ND2 . ASN   B 252 ? 0.2730 0.3023 0.3325 0.0386  0.0596  0.0090  252 ASN   B ND2 
13311 N  N   . GLY   B 253 ? 0.1598 0.1671 0.2436 0.0436  0.0798  0.0008  253 GLY   B N   
13312 C  CA  . GLY   B 253 ? 0.1517 0.1503 0.2342 0.0404  0.0828  -0.0031 253 GLY   B CA  
13313 C  C   . GLY   B 253 ? 0.1994 0.1869 0.2637 0.0351  0.0828  -0.0076 253 GLY   B C   
13314 O  O   . GLY   B 253 ? 0.1705 0.1546 0.2371 0.0307  0.0858  -0.0123 253 GLY   B O   
13318 N  N   . VAL   B 254 ? 0.2028 0.1875 0.2612 0.0354  0.0793  -0.0058 254 VAL   B N   
13319 C  CA  . VAL   B 254 ? 0.1819 0.1579 0.2305 0.0311  0.0782  -0.0094 254 VAL   B CA  
13320 C  C   . VAL   B 254 ? 0.1838 0.1541 0.2262 0.0331  0.0747  -0.0067 254 VAL   B C   
13321 O  O   . VAL   B 254 ? 0.1670 0.1328 0.2022 0.0316  0.0722  -0.0080 254 VAL   B O   
13322 C  CB  . VAL   B 254 ? 0.1859 0.1622 0.2251 0.0280  0.0782  -0.0116 254 VAL   B CB  
13323 C  CG1 . VAL   B 254 ? 0.2035 0.1813 0.2406 0.0228  0.0821  -0.0163 254 VAL   B CG1 
13324 C  CG2 . VAL   B 254 ? 0.1743 0.1586 0.2151 0.0307  0.0733  -0.0069 254 VAL   B CG2 
13334 N  N   . HIS   B 255 ? 0.1756 0.1479 0.2278 0.0366  0.0744  -0.0029 255 HIS   B N   
13335 C  CA  . HIS   B 255 ? 0.1949 0.1622 0.2407 0.0379  0.0720  -0.0002 255 HIS   B CA  
13336 C  C   . HIS   B 255 ? 0.1719 0.1341 0.2237 0.0346  0.0742  -0.0035 255 HIS   B C   
13337 O  O   . HIS   B 255 ? 0.1971 0.1581 0.2510 0.0351  0.0774  -0.0030 255 HIS   B O   
13338 C  CB  . HIS   B 255 ? 0.1661 0.1392 0.2231 0.0431  0.0708  0.0060  255 HIS   B CB  
13339 C  CG  . HIS   B 255 ? 0.1720 0.1418 0.2266 0.0440  0.0688  0.0091  255 HIS   B CG  
13340 N  ND1 . HIS   B 255 ? 0.1716 0.1416 0.2199 0.0447  0.0653  0.0103  255 HIS   B ND1 
13341 C  CD2 . HIS   B 255 ? 0.2068 0.1723 0.2603 0.0446  0.0705  0.0109  255 HIS   B CD2 
13342 C  CE1 . HIS   B 255 ? 0.2003 0.1668 0.2445 0.0454  0.0649  0.0126  255 HIS   B CE1 
13343 N  NE2 . HIS   B 255 ? 0.1852 0.1502 0.2388 0.0451  0.0681  0.0131  255 HIS   B NE2 
13351 N  N   . PRO   B 256 ? 0.1975 0.1534 0.2352 0.0311  0.0728  -0.0068 256 PRO   B N   
13352 C  CA  . PRO   B 256 ? 0.1695 0.1210 0.2102 0.0274  0.0752  -0.0103 256 PRO   B CA  
13353 C  C   . PRO   B 256 ? 0.1533 0.1040 0.2038 0.0294  0.0772  -0.0075 256 PRO   B C   
13354 O  O   . PRO   B 256 ? 0.1946 0.1447 0.2392 0.0319  0.0750  -0.0036 256 PRO   B O   
13355 C  CB  . PRO   B 256 ? 0.1841 0.1316 0.2127 0.0249  0.0720  -0.0131 256 PRO   B CB  
13356 C  CG  . PRO   B 256 ? 0.1708 0.1207 0.1976 0.0262  0.0688  -0.0123 256 PRO   B CG  
13357 C  CD  . PRO   B 256 ? 0.2063 0.1609 0.2352 0.0307  0.0689  -0.0075 256 PRO   B CD  
13365 N  N   . VAL   B 257 ? 0.1868 0.1332 0.2349 0.0274  0.0812  -0.0097 257 VAL   B N   
13366 C  CA  . VAL   B 257 ? 0.1625 0.1076 0.2242 0.0288  0.0842  -0.0075 257 VAL   B CA  
13367 C  C   . VAL   B 257 ? 0.1831 0.1220 0.2384 0.0240  0.0871  -0.0122 257 VAL   B C   
13368 O  O   . VAL   B 257 ? 0.1925 0.1308 0.2461 0.0207  0.0888  -0.0168 257 VAL   B O   
13369 C  CB  . VAL   B 257 ? 0.2077 0.1534 0.2705 0.0325  0.0869  -0.0044 257 VAL   B CB  
13370 C  CG1 . VAL   B 257 ? 0.2092 0.1513 0.2816 0.0331  0.0910  -0.0030 257 VAL   B CG1 
13371 C  CG2 . VAL   B 257 ? 0.1749 0.1277 0.2449 0.0373  0.0840  0.0007  257 VAL   B CG2 
13381 N  N   . LYS   B 258 ? 0.1846 0.1204 0.2405 0.0235  0.0880  -0.0116 258 LYS   B N   
13382 C  CA  . LYS   B 258 ? 0.1736 0.1053 0.2315 0.0189  0.0911  -0.0162 258 LYS   B CA  
13383 C  C   . LYS   B 258 ? 0.1720 0.1039 0.2218 0.0149  0.0890  -0.0214 258 LYS   B C   
13384 O  O   . LYS   B 258 ? 0.1953 0.1252 0.2418 0.0117  0.0916  -0.0257 258 LYS   B O   
13385 C  CB  . LYS   B 258 ? 0.2063 0.1341 0.2686 0.0187  0.0967  -0.0169 258 LYS   B CB  
13386 C  CG  . LYS   B 258 ? 0.2186 0.1448 0.2906 0.0223  0.0996  -0.0122 258 LYS   B CG  
13387 C  CD  . LYS   B 258 ? 0.2594 0.1828 0.3376 0.0235  0.1047  -0.0122 258 LYS   B CD  
13388 C  CE  . LYS   B 258 ? 0.2948 0.2141 0.3815 0.0255  0.1088  -0.0090 258 LYS   B CE  
13389 N  NZ  . LYS   B 258 ? 0.3629 0.2778 0.4516 0.0262  0.1141  -0.0103 258 LYS   B NZ  
13403 N  N   . ASN   B 259 ? 0.1889 0.1219 0.2290 0.0148  0.0842  -0.0215 259 ASN   B N   
13404 C  CA  . ASN   B 259 ? 0.1870 0.1202 0.2210 0.0114  0.0818  -0.0262 259 ASN   B CA  
13405 C  C   . ASN   B 259 ? 0.1969 0.1306 0.2255 0.0103  0.0821  -0.0280 259 ASN   B C   
13406 O  O   . ASN   B 259 ? 0.1866 0.1190 0.2121 0.0062  0.0829  -0.0325 259 ASN   B O   
13407 C  CB  . ASN   B 259 ? 0.1961 0.1262 0.2273 0.0069  0.0838  -0.0308 259 ASN   B CB  
13408 C  CG  . ASN   B 259 ? 0.1967 0.1271 0.2194 0.0046  0.0799  -0.0345 259 ASN   B CG  
13409 O  OD1 . ASN   B 259 ? 0.1968 0.1292 0.2157 0.0069  0.0754  -0.0329 259 ASN   B OD1 
13410 N  ND2 . ASN   B 259 ? 0.1890 0.1178 0.2097 -0.0001 0.0816  -0.0396 259 ASN   B ND2 
13417 N  N   . PHE   B 260 ? 0.1893 0.1261 0.2226 0.0137  0.0817  -0.0248 260 PHE   B N   
13418 C  CA  . PHE   B 260 ? 0.1985 0.1367 0.2292 0.0126  0.0826  -0.0264 260 PHE   B CA  
13419 C  C   . PHE   B 260 ? 0.2114 0.1485 0.2468 0.0104  0.0879  -0.0291 260 PHE   B C   
13420 O  O   . PHE   B 260 ? 0.2164 0.1547 0.2501 0.0087  0.0894  -0.0316 260 PHE   B O   
13421 C  CB  . PHE   B 260 ? 0.2017 0.1382 0.2204 0.0095  0.0795  -0.0294 260 PHE   B CB  
13422 C  CG  . PHE   B 260 ? 0.1868 0.1249 0.2027 0.0119  0.0743  -0.0271 260 PHE   B CG  
13423 C  CD1 . PHE   B 260 ? 0.1998 0.1370 0.2114 0.0137  0.0712  -0.0255 260 PHE   B CD1 
13424 C  CD2 . PHE   B 260 ? 0.2057 0.1436 0.2121 0.0124  0.0730  -0.0265 260 PHE   B CD2 
13425 C  CE1 . PHE   B 260 ? 0.1901 0.1282 0.1974 0.0162  0.0667  -0.0236 260 PHE   B CE1 
13426 C  CE2 . PHE   B 260 ? 0.1723 0.1110 0.1773 0.0148  0.0685  -0.0245 260 PHE   B CE2 
13427 C  CZ  . PHE   B 260 ? 0.1680 0.1066 0.1725 0.0168  0.0652  -0.0230 260 PHE   B CZ  
13437 N  N   . GLN   B 261 ? 0.2110 0.1460 0.2530 0.0105  0.0912  -0.0292 261 GLN   B N   
13438 C  CA  . GLN   B 261 ? 0.2071 0.1410 0.2562 0.0090  0.0964  -0.0317 261 GLN   B CA  
13439 C  C   . GLN   B 261 ? 0.2093 0.1477 0.2663 0.0132  0.0975  -0.0289 261 GLN   B C   
13440 O  O   . GLN   B 261 ? 0.2458 0.1841 0.3016 0.0118  0.1010  -0.0317 261 GLN   B O   
13441 C  CB  . GLN   B 261 ? 0.2180 0.1475 0.2705 0.0083  0.1000  -0.0326 261 GLN   B CB  
13442 C  CG  . GLN   B 261 ? 0.2244 0.1512 0.2742 0.0031  0.1004  -0.0370 261 GLN   B CG  
13443 C  CD  . GLN   B 261 ? 0.2665 0.1875 0.3142 0.0018  0.1048  -0.0382 261 GLN   B CD  
13444 O  OE1 . GLN   B 261 ? 0.2276 0.1478 0.2852 -0.0009 0.1095  -0.0420 261 GLN   B OE1 
13445 N  NE2 . GLN   B 261 ? 0.2323 0.1540 0.2893 0.0037  0.1038  -0.0349 261 GLN   B NE2 
13454 N  N   . GLU   B 262 ? 0.2211 0.1621 0.2791 0.0181  0.0947  -0.0234 262 GLU   B N   
13455 C  CA  . GLU   B 262 ? 0.2343 0.1797 0.2944 0.0225  0.0949  -0.0201 262 GLU   B CA  
13456 C  C   . GLU   B 262 ? 0.1761 0.1278 0.2408 0.0247  0.0902  -0.0171 262 GLU   B C   
13457 O  O   . GLU   B 262 ? 0.1749 0.1238 0.2282 0.0234  0.0870  -0.0170 262 GLU   B O   
13458 C  CB  . GLU   B 262 ? 0.2153 0.1616 0.2910 0.0269  0.0972  -0.0164 262 GLU   B CB  
13459 C  CG  . GLU   B 262 ? 0.2336 0.1763 0.3175 0.0255  0.1026  -0.0191 262 GLU   B CG  
13460 C  CD  . GLU   B 262 ? 0.3422 0.2800 0.4227 0.0295  0.1049  -0.0153 262 GLU   B CD  
13461 O  OE1 . GLU   B 262 ? 0.3277 0.2715 0.4223 0.0349  0.1043  -0.0112 262 GLU   B OE1 
13462 O  OE2 . GLU   B 262 ? 0.3169 0.2504 0.4060 0.0273  0.1074  -0.0164 262 GLU   B OE2 
13469 N  N   . SER   B 263 ? 0.2090 0.1655 0.2708 0.0279  0.0900  -0.0148 263 SER   B N   
13470 C  CA  . SER   B 263 ? 0.1749 0.1377 0.2401 0.0297  0.0863  -0.0126 263 SER   B CA  
13471 C  C   . SER   B 263 ? 0.1795 0.1484 0.2504 0.0356  0.0850  -0.0068 263 SER   B C   
13472 O  O   . SER   B 263 ? 0.1884 0.1627 0.2572 0.0373  0.0825  -0.0050 263 SER   B O   
13473 C  CB  . SER   B 263 ? 0.1945 0.1586 0.2518 0.0261  0.0876  -0.0167 263 SER   B CB  
13474 O  OG  . SER   B 263 ? 0.2022 0.1610 0.2542 0.0207  0.0898  -0.0219 263 SER   B OG  
13480 N  N   . TYR   B 264 ? 0.1954 0.1631 0.2724 0.0388  0.0865  -0.0038 264 TYR   B N   
13481 C  CA  . TYR   B 264 ? 0.1987 0.1732 0.2862 0.0447  0.0855  0.0019  264 TYR   B CA  
13482 C  C   . TYR   B 264 ? 0.2042 0.1729 0.2919 0.0472  0.0867  0.0055  264 TYR   B C   
13483 O  O   . TYR   B 264 ? 0.1689 0.1324 0.2615 0.0449  0.0903  0.0025  264 TYR   B O   
13484 C  CB  . TYR   B 264 ? 0.2314 0.2129 0.3244 0.0468  0.0873  0.0013  264 TYR   B CB  
13485 C  CG  . TYR   B 264 ? 0.2363 0.2254 0.3414 0.0532  0.0861  0.0072  264 TYR   B CG  
13486 C  CD1 . TYR   B 264 ? 0.2050 0.2031 0.3132 0.0561  0.0822  0.0112  264 TYR   B CD1 
13487 C  CD2 . TYR   B 264 ? 0.3063 0.2926 0.4148 0.0565  0.0886  0.0091  264 TYR   B CD2 
13488 C  CE1 . TYR   B 264 ? 0.2534 0.2575 0.3651 0.0619  0.0804  0.0169  264 TYR   B CE1 
13489 C  CE2 . TYR   B 264 ? 0.3165 0.3089 0.4339 0.0627  0.0870  0.0148  264 TYR   B CE2 
13490 C  CZ  . TYR   B 264 ? 0.2977 0.3000 0.4187 0.0654  0.0827  0.0190  264 TYR   B CZ  
13491 O  OH  . TYR   B 264 ? 0.3535 0.3617 0.4777 0.0715  0.0807  0.0248  264 TYR   B OH  
13501 N  N   . THR   B 265 ? 0.2021 0.1739 0.2951 0.0515  0.0841  0.0115  265 THR   B N   
13502 C  CA  . THR   B 265 ? 0.2258 0.1924 0.3186 0.0541  0.0858  0.0160  265 THR   B CA  
13503 C  C   . THR   B 265 ? 0.2416 0.2140 0.3381 0.0602  0.0837  0.0227  265 THR   B C   
13504 O  O   . THR   B 265 ? 0.2099 0.1898 0.3104 0.0617  0.0796  0.0253  265 THR   B O   
13505 C  CB  . THR   B 265 ? 0.1772 0.1382 0.2712 0.0513  0.0855  0.0164  265 THR   B CB  
13506 O  OG1 . THR   B 265 ? 0.2044 0.1606 0.2965 0.0544  0.0877  0.0209  265 THR   B OG1 
13507 C  CG2 . THR   B 265 ? 0.2016 0.1643 0.2823 0.0511  0.0809  0.0179  265 THR   B CG2 
13515 N  N   . ASN   B 266 ? 0.1827 0.1566 0.2988 0.0641  0.0864  0.0255  266 ASN   B N   
13516 C  CA  . ASN   B 266 ? 0.2588 0.2361 0.3697 0.0704  0.0843  0.0326  266 ASN   B CA  
13517 C  C   . ASN   B 266 ? 0.2167 0.1916 0.3302 0.0714  0.0830  0.0383  266 ASN   B C   
13518 O  O   . ASN   B 266 ? 0.2350 0.2133 0.3491 0.0764  0.0812  0.0447  266 ASN   B O   
13519 C  CB  . ASN   B 266 ? 0.2755 0.2544 0.4034 0.0742  0.0877  0.0331  266 ASN   B CB  
13520 C  CG  . ASN   B 266 ? 0.3369 0.3042 0.4627 0.0721  0.0930  0.0305  266 ASN   B CG  
13521 O  OD1 . ASN   B 266 ? 0.2962 0.2569 0.4193 0.0687  0.0940  0.0303  266 ASN   B OD1 
13522 N  ND2 . ASN   B 266 ? 0.4148 0.3808 0.5456 0.0738  0.0967  0.0281  266 ASN   B ND2 
13529 N  N   . GLN   B 267 ? 0.1984 0.1664 0.3042 0.0669  0.0836  0.0362  267 GLN   B N   
13530 C  CA  . GLN   B 267 ? 0.2195 0.1827 0.3156 0.0673  0.0832  0.0405  267 GLN   B CA  
13531 C  C   . GLN   B 267 ? 0.2192 0.1867 0.3078 0.0660  0.0787  0.0410  267 GLN   B C   
13532 O  O   . GLN   B 267 ? 0.1849 0.1513 0.2738 0.0663  0.0783  0.0447  267 GLN   B O   
13533 C  CB  . GLN   B 267 ? 0.1802 0.1352 0.2814 0.0631  0.0873  0.0378  267 GLN   B CB  
13534 C  CG  . GLN   B 267 ? 0.2172 0.1651 0.3186 0.0640  0.0927  0.0365  267 GLN   B CG  
13535 C  CD  . GLN   B 267 ? 0.1869 0.1396 0.2953 0.0652  0.0897  0.0419  267 GLN   B CD  
13536 O  OE1 . GLN   B 267 ? 0.1896 0.1407 0.2939 0.0671  0.0894  0.0473  267 GLN   B OE1 
13537 N  NE2 . GLN   B 267 ? 0.2019 0.1541 0.3195 0.0728  0.0942  0.0426  267 GLN   B NE2 
13546 N  N   . ALA   B 268 ? 0.1967 0.1706 0.2861 0.0648  0.0758  0.0379  268 ALA   B N   
13547 C  CA  . ALA   B 268 ? 0.1842 0.1609 0.2650 0.0633  0.0718  0.0375  268 ALA   B CA  
13548 C  C   . ALA   B 268 ? 0.1623 0.1450 0.2439 0.0674  0.0685  0.0443  268 ALA   B C   
13549 O  O   . ALA   B 268 ? 0.1743 0.1556 0.2467 0.0663  0.0667  0.0450  268 ALA   B O   
13550 C  CB  . ALA   B 268 ? 0.1854 0.1671 0.2652 0.0617  0.0700  0.0329  268 ALA   B CB  
13556 N  N   . ASP   B 269 ? 0.1657 0.1542 0.2526 0.0722  0.0677  0.0495  269 ASP   B N   
13557 C  CA  . ASP   B 269 ? 0.1884 0.1842 0.2773 0.0761  0.0639  0.0565  269 ASP   B CA  
13558 C  C   . ASP   B 269 ? 0.2271 0.2149 0.3013 0.0760  0.0653  0.0601  269 ASP   B C   
13559 O  O   . ASP   B 269 ? 0.2149 0.2083 0.2913 0.0777  0.0623  0.0645  269 ASP   B O   
13560 C  CB  . ASP   B 269 ? 0.2512 0.2544 0.3444 0.0811  0.0625  0.0617  269 ASP   B CB  
13561 C  CG  . ASP   B 269 ? 0.3285 0.3395 0.4155 0.0846  0.0576  0.0682  269 ASP   B CG  
13562 O  OD1 . ASP   B 269 ? 0.2723 0.2890 0.3594 0.0831  0.0544  0.0670  269 ASP   B OD1 
13563 O  OD2 . ASP   B 269 ? 0.3914 0.4050 0.4825 0.0888  0.0569  0.0744  269 ASP   B OD2 
13568 N  N   . LYS   B 270 ? 0.1567 0.1390 0.2381 0.0684  0.0669  0.0560  270 LYS   B N   
13569 C  CA  . LYS   B 270 ? 0.1998 0.1731 0.2759 0.0739  0.0723  0.0616  270 LYS   B CA  
13570 C  C   . LYS   B 270 ? 0.1815 0.1550 0.2525 0.0709  0.0708  0.0592  270 LYS   B C   
13571 O  O   . LYS   B 270 ? 0.1748 0.1468 0.2416 0.0717  0.0715  0.0631  270 LYS   B O   
13572 C  CB  . LYS   B 270 ? 0.2161 0.1801 0.2971 0.0720  0.0780  0.0597  270 LYS   B CB  
13573 C  CG  . LYS   B 270 ? 0.1967 0.1600 0.2892 0.0754  0.0805  0.0620  270 LYS   B CG  
13574 C  CD  . LYS   B 270 ? 0.2098 0.1628 0.3033 0.0732  0.0864  0.0600  270 LYS   B CD  
13575 C  CE  . LYS   B 270 ? 0.2086 0.1558 0.3018 0.0727  0.0895  0.0631  270 LYS   B CE  
13576 N  NZ  . LYS   B 270 ? 0.2285 0.1661 0.3238 0.0717  0.0956  0.0621  270 LYS   B NZ  
13590 N  N   . ILE   B 271 ? 0.1942 0.1677 0.2586 0.0674  0.0690  0.0528  271 ILE   B N   
13591 C  CA  . ILE   B 271 ? 0.1738 0.1473 0.2354 0.0647  0.0674  0.0494  271 ILE   B CA  
13592 C  C   . ILE   B 271 ? 0.1918 0.1716 0.2439 0.0656  0.0624  0.0488  271 ILE   B C   
13593 O  O   . ILE   B 271 ? 0.1751 0.1543 0.2241 0.0629  0.0609  0.0442  271 ILE   B O   
13594 C  CB  . ILE   B 271 ? 0.2047 0.1703 0.2607 0.0596  0.0699  0.0426  271 ILE   B CB  
13595 C  CG1 . ILE   B 271 ? 0.2055 0.1717 0.2643 0.0577  0.0695  0.0372  271 ILE   B CG1 
13596 C  CG2 . ILE   B 271 ? 0.2086 0.1675 0.2687 0.0586  0.0749  0.0435  271 ILE   B CG2 
13597 C  CD1 . ILE   B 271 ? 0.1996 0.1603 0.2571 0.0528  0.0712  0.0306  271 ILE   B CD1 
13609 N  N   . SER   B 272 ? 0.1882 0.1758 0.2447 0.0693  0.0600  0.0532  272 SER   B N   
13610 C  CA  . SER   B 272 ? 0.1757 0.1717 0.2307 0.0705  0.0555  0.0534  272 SER   B CA  
13611 C  C   . SER   B 272 ? 0.1739 0.1732 0.2214 0.0723  0.0526  0.0567  272 SER   B C   
13612 O  O   . SER   B 272 ? 0.1457 0.1435 0.1922 0.0726  0.0540  0.0606  272 SER   B O   
13613 C  CB  . SER   B 272 ? 0.1806 0.1848 0.2427 0.0738  0.0539  0.0567  272 SER   B CB  
13614 O  OG  . SER   B 272 ? 0.2094 0.2167 0.2712 0.0777  0.0532  0.0638  272 SER   B OG  
13620 N  N   . GLY   B 273 ? 0.2138 0.2175 0.2522 0.0722  0.0488  0.0551  273 GLY   B N   
13621 C  CA  . GLY   B 273 ? 0.1893 0.1981 0.2247 0.0743  0.0457  0.0583  273 GLY   B CA  
13622 C  C   . GLY   B 273 ? 0.1770 0.1938 0.2134 0.0779  0.0434  0.0661  273 GLY   B C   
13623 O  O   . GLY   B 273 ? 0.1769 0.1955 0.2081 0.0792  0.0423  0.0701  273 GLY   B O   
13627 N  N   . GLU   B 274 ? 0.1652 0.1878 0.2112 0.0793  0.0427  0.0682  274 GLU   B N   
13628 C  CA  . GLU   B 274 ? 0.1907 0.2205 0.2363 0.0829  0.0404  0.0755  274 GLU   B CA  
13629 C  C   . GLU   B 274 ? 0.1753 0.1993 0.2246 0.0839  0.0438  0.0800  274 GLU   B C   
13630 O  O   . GLU   B 274 ? 0.1727 0.2003 0.2169 0.0858  0.0419  0.0857  274 GLU   B O   
13631 C  CB  . GLU   B 274 ? 0.1836 0.2207 0.2414 0.0843  0.0396  0.0757  274 GLU   B CB  
13632 C  CG  . GLU   B 274 ? 0.1974 0.2439 0.2551 0.0838  0.0357  0.0730  274 GLU   B CG  
13633 C  CD  . GLU   B 274 ? 0.2222 0.2640 0.2808 0.0808  0.0383  0.0656  274 GLU   B CD  
13634 O  OE1 . GLU   B 274 ? 0.1934 0.2241 0.2524 0.0782  0.0426  0.0616  274 GLU   B OE1 
13635 O  OE2 . GLU   B 274 ? 0.2749 0.3245 0.3331 0.0805  0.0362  0.0635  274 GLU   B OE2 
13642 N  N   . THR   B 275 ? 0.1921 0.2058 0.2426 0.0824  0.0488  0.0772  275 THR   B N   
13643 C  CA  . THR   B 275 ? 0.1705 0.1776 0.2252 0.0832  0.0530  0.0807  275 THR   B CA  
13644 C  C   . THR   B 275 ? 0.1674 0.1719 0.2147 0.0820  0.0537  0.0815  275 THR   B C   
13645 O  O   . THR   B 275 ? 0.2152 0.2188 0.2561 0.0839  0.0541  0.0876  275 THR   B O   
13646 C  CB  . THR   B 275 ? 0.1797 0.1772 0.2386 0.0810  0.0582  0.0769  275 THR   B CB  
13647 O  OG1 . THR   B 275 ? 0.1875 0.1885 0.2544 0.0828  0.0575  0.0768  275 THR   B OG1 
13648 C  CG2 . THR   B 275 ? 0.1655 0.1568 0.2233 0.0765  0.0612  0.0770  275 THR   B CG2 
13656 N  N   . LEU   B 276 ? 0.1636 0.1651 0.2039 0.0790  0.0536  0.0755  276 LEU   B N   
13657 C  CA  . LEU   B 276 ? 0.1672 0.1660 0.1998 0.0782  0.0546  0.0751  276 LEU   B CA  
13658 C  C   . LEU   B 276 ? 0.1548 0.1635 0.1838 0.0772  0.0498  0.0782  276 LEU   B C   
13659 O  O   . LEU   B 276 ? 0.1807 0.1862 0.2017 0.0818  0.0520  0.0854  276 LEU   B O   
13660 C  CB  . LEU   B 276 ? 0.1897 0.1852 0.2181 0.0751  0.0545  0.0673  276 LEU   B CB  
13661 C  CG  . LEU   B 276 ? 0.2059 0.1985 0.2264 0.0747  0.0555  0.0658  276 LEU   B CG  
13662 C  CD1 . LEU   B 276 ? 0.1880 0.1734 0.2135 0.0733  0.0613  0.0663  276 LEU   B CD1 
13663 C  CD2 . LEU   B 276 ? 0.2065 0.1987 0.2240 0.0724  0.0535  0.0582  276 LEU   B CD2 
13675 N  N   . THR   B 277 ? 0.2087 0.2237 0.2304 0.0817  0.0452  0.0810  277 THR   B N   
13676 C  CA  . THR   B 277 ? 0.2134 0.2381 0.2300 0.0831  0.0403  0.0857  277 THR   B CA  
13677 C  C   . THR   B 277 ? 0.2147 0.2424 0.2346 0.0855  0.0405  0.0936  277 THR   B C   
13678 O  O   . THR   B 277 ? 0.2511 0.2819 0.2614 0.0858  0.0388  0.0976  277 THR   B O   
13679 C  CB  . THR   B 277 ? 0.1965 0.2310 0.2146 0.0833  0.0347  0.0836  277 THR   B CB  
13680 O  OG1 . THR   B 277 ? 0.1972 0.2275 0.2086 0.0805  0.0343  0.0763  277 THR   B OG1 
13681 C  CG2 . THR   B 277 ? 0.2308 0.2752 0.2389 0.0840  0.0292  0.0882  277 THR   B CG2 
13689 N  N   . ALA   B 278 ? 0.1910 0.2170 0.2219 0.0869  0.0425  0.0956  278 ALA   B N   
13690 C  CA  . ALA   B 278 ? 0.2190 0.2456 0.2490 0.0897  0.0426  0.1030  278 ALA   B CA  
13691 C  C   . ALA   B 278 ? 0.1944 0.2132 0.2300 0.0895  0.0478  0.1060  278 ALA   B C   
13692 O  O   . ALA   B 278 ? 0.2645 0.2821 0.2909 0.0916  0.0475  0.1125  278 ALA   B O   
13693 C  CB  . ALA   B 278 ? 0.2354 0.2634 0.2762 0.0919  0.0426  0.1039  278 ALA   B CB  
13699 N  N   . ASN   B 279 ? 0.2161 0.2252 0.2451 0.0869  0.0523  0.1011  279 ASN   B N   
13700 C  CA  . ASN   B 279 ? 0.2326 0.2324 0.2610 0.0864  0.0582  0.1030  279 ASN   B CA  
13701 C  C   . ASN   B 279 ? 0.2318 0.2293 0.2543 0.0842  0.0602  0.1014  279 ASN   B C   
13702 O  O   . ASN   B 279 ? 0.2615 0.2617 0.2742 0.0846  0.0590  0.1061  279 ASN   B O   
13703 C  CB  . ASN   B 279 ? 0.2296 0.2212 0.2697 0.0854  0.0632  0.1002  279 ASN   B CB  
13704 C  CG  . ASN   B 279 ? 0.2650 0.2570 0.3085 0.0883  0.0623  0.1034  279 ASN   B CG  
13705 O  OD1 . ASN   B 279 ? 0.2646 0.2540 0.3128 0.0905  0.0640  0.1093  279 ASN   B OD1 
13706 N  ND2 . ASN   B 279 ? 0.2489 0.2466 0.2998 0.0885  0.0593  0.0999  279 ASN   B ND2 
13713 N  N   . GLN   B 280 ? 0.2259 0.2177 0.2484 0.0817  0.0630  0.0945  280 GLN   B N   
13714 C  CA  . GLN   B 280 ? 0.2348 0.2226 0.2495 0.0801  0.0658  0.0924  280 GLN   B CA  
13715 C  C   . GLN   B 280 ? 0.2141 0.2087 0.2209 0.0800  0.0614  0.0903  280 GLN   B C   
13716 O  O   . GLN   B 280 ? 0.1985 0.1927 0.2003 0.0775  0.0631  0.0876  280 GLN   B O   
13717 C  CB  . GLN   B 280 ? 0.2333 0.2124 0.2549 0.0775  0.0710  0.0865  280 GLN   B CB  
13718 C  CG  . GLN   B 280 ? 0.2289 0.2014 0.2602 0.0769  0.0755  0.0875  280 GLN   B CG  
13719 C  CD  . GLN   B 280 ? 0.2541 0.2259 0.2865 0.0764  0.0739  0.0840  280 GLN   B CD  
13720 O  OE1 . GLN   B 280 ? 0.2089 0.1892 0.2471 0.0777  0.0688  0.0832  280 GLN   B OE1 
13721 N  NE2 . GLN   B 280 ? 0.2343 0.2000 0.2783 0.0748  0.0785  0.0817  280 GLN   B NE2 
13730 N  N   . LEU   B 281 ? 0.2094 0.2112 0.2134 0.0810  0.0556  0.0888  281 LEU   B N   
13731 C  CA  . LEU   B 281 ? 0.1793 0.1889 0.1813 0.0788  0.0512  0.0840  281 LEU   B CA  
13732 C  C   . LEU   B 281 ? 0.2232 0.2360 0.2058 0.0785  0.0499  0.0885  281 LEU   B C   
13733 O  O   . LEU   B 281 ? 0.2095 0.2276 0.1958 0.0811  0.0483  0.0967  281 LEU   B O   
13734 C  CB  . LEU   B 281 ? 0.2152 0.2292 0.2092 0.0794  0.0455  0.0811  281 LEU   B CB  
13735 C  CG  . LEU   B 281 ? 0.1950 0.2149 0.1863 0.0762  0.0411  0.0745  281 LEU   B CG  
13736 C  CD1 . LEU   B 281 ? 0.1962 0.2092 0.1846 0.0735  0.0428  0.0655  281 LEU   B CD1 
13737 C  CD2 . LEU   B 281 ? 0.2319 0.2585 0.2178 0.0764  0.0356  0.0744  281 LEU   B CD2 
13749 N  N   . VAL   B 282 ? 0.1957 0.2101 0.1763 0.0753  0.0508  0.0830  282 VAL   B N   
13750 C  CA  . VAL   B 282 ? 0.1912 0.2106 0.1599 0.0742  0.0502  0.0855  282 VAL   B CA  
13751 C  C   . VAL   B 282 ? 0.1878 0.2154 0.1493 0.0732  0.0441  0.0815  282 VAL   B C   
13752 O  O   . VAL   B 282 ? 0.2043 0.2386 0.1584 0.0735  0.0409  0.0862  282 VAL   B O   
13753 C  CB  . VAL   B 282 ? 0.1811 0.1975 0.1512 0.0716  0.0556  0.0824  282 VAL   B CB  
13754 C  CG1 . VAL   B 282 ? 0.2165 0.2381 0.1713 0.0698  0.0551  0.0830  282 VAL   B CG1 
13755 C  CG2 . VAL   B 282 ? 0.2022 0.2095 0.1752 0.0717  0.0618  0.0861  282 VAL   B CG2 
13765 N  N   . ARG   B 283 ? 0.1703 0.1968 0.1341 0.0714  0.0425  0.0724  283 ARG   B N   
13766 C  CA  . ARG   B 283 ? 0.1961 0.2270 0.1479 0.0698  0.0372  0.0668  283 ARG   B CA  
13767 C  C   . ARG   B 283 ? 0.1611 0.1892 0.1247 0.0686  0.0360  0.0582  283 ARG   B C   
13768 O  O   . ARG   B 283 ? 0.1964 0.2164 0.1590 0.0687  0.0392  0.0562  283 ARG   B O   
13769 C  CB  . ARG   B 283 ? 0.2015 0.2361 0.1447 0.0680  0.0378  0.0645  283 ARG   B CB  
13770 C  CG  . ARG   B 283 ? 0.1758 0.2066 0.1236 0.0667  0.0427  0.0594  283 ARG   B CG  
13771 C  CD  . ARG   B 283 ? 0.2105 0.2433 0.1452 0.0650  0.0422  0.0530  283 ARG   B CD  
13772 N  NE  . ARG   B 283 ? 0.1969 0.2280 0.1362 0.0641  0.0470  0.0487  283 ARG   B NE  
13773 C  CZ  . ARG   B 283 ? 0.2032 0.2300 0.1470 0.0640  0.0478  0.0415  283 ARG   B CZ  
13774 N  NH1 . ARG   B 283 ? 0.1940 0.2174 0.1396 0.0645  0.0440  0.0374  283 ARG   B NH1 
13775 N  NH2 . ARG   B 283 ? 0.2384 0.2641 0.1817 0.0632  0.0522  0.0381  283 ARG   B NH2 
13789 N  N   . LYS   B 284 ? 0.2216 0.2504 0.1683 0.0670  0.0313  0.0530  284 LYS   B N   
13790 C  CA  . LYS   B 284 ? 0.1838 0.2092 0.1391 0.0654  0.0299  0.0449  284 LYS   B CA  
13791 C  C   . LYS   B 284 ? 0.1984 0.2189 0.1447 0.0649  0.0325  0.0387  284 LYS   B C   
13792 O  O   . LYS   B 284 ? 0.1840 0.2085 0.1292 0.0650  0.0344  0.0406  284 LYS   B O   
13793 C  CB  . LYS   B 284 ? 0.2135 0.2411 0.1577 0.0638  0.0245  0.0418  284 LYS   B CB  
13794 C  CG  . LYS   B 284 ? 0.1985 0.2351 0.1531 0.0640  0.0214  0.0472  284 LYS   B CG  
13795 C  CD  . LYS   B 284 ? 0.3286 0.3650 0.2673 0.0615  0.0165  0.0431  284 LYS   B CD  
13796 C  CE  . LYS   B 284 ? 0.3584 0.3977 0.2912 0.0591  0.0139  0.0385  284 LYS   B CE  
13797 N  NZ  . LYS   B 284 ? 0.3875 0.4348 0.3133 0.0594  0.0131  0.0430  284 LYS   B NZ  
13811 N  N   . ASN   B 285 ? 0.1786 0.1934 0.1311 0.0645  0.0328  0.0327  285 ASN   B N   
13812 C  CA  . ASN   B 285 ? 0.1809 0.1927 0.1309 0.0644  0.0348  0.0263  285 ASN   B CA  
13813 C  C   . ASN   B 285 ? 0.1635 0.1721 0.1109 0.0637  0.0306  0.0192  285 ASN   B C   
13814 O  O   . ASN   B 285 ? 0.1793 0.1814 0.1279 0.0636  0.0306  0.0156  285 ASN   B O   
13815 C  CB  . ASN   B 285 ? 0.1964 0.2043 0.1535 0.0647  0.0393  0.0262  285 ASN   B CB  
13816 C  CG  . ASN   B 285 ? 0.1946 0.2030 0.1517 0.0648  0.0419  0.0217  285 ASN   B CG  
13817 O  OD1 . ASN   B 285 ? 0.1881 0.2011 0.1402 0.0647  0.0421  0.0206  285 ASN   B OD1 
13818 N  ND2 . ASN   B 285 ? 0.1883 0.1929 0.1520 0.0646  0.0438  0.0182  285 ASN   B ND2 
13825 N  N   . PRO   B 286 ? 0.1706 0.1821 0.1113 0.0627  0.0271  0.0172  286 PRO   B N   
13826 C  CA  . PRO   B 286 ? 0.2032 0.2094 0.1369 0.0619  0.0230  0.0108  286 PRO   B CA  
13827 C  C   . PRO   B 286 ? 0.2257 0.2258 0.1543 0.0631  0.0234  0.0038  286 PRO   B C   
13828 O  O   . PRO   B 286 ? 0.2125 0.2163 0.1432 0.0644  0.0259  0.0024  286 PRO   B O   
13829 C  CB  . PRO   B 286 ? 0.2504 0.2612 0.1759 0.0603  0.0200  0.0109  286 PRO   B CB  
13830 C  CG  . PRO   B 286 ? 0.3307 0.3474 0.2466 0.0606  0.0216  0.0182  286 PRO   B CG  
13831 C  CD  . PRO   B 286 ? 0.2242 0.2427 0.1578 0.0623  0.0266  0.0207  286 PRO   B CD  
13839 N  N   . CYS   B 287 ? 0.2176 0.2109 0.1474 0.0628  0.0207  -0.0005 287 CYS   B N   
13840 C  CA  . CYS   B 287 ? 0.2060 0.1939 0.1337 0.0646  0.0200  -0.0072 287 CYS   B CA  
13841 C  C   . CYS   B 287 ? 0.2027 0.1917 0.1242 0.0646  0.0180  -0.0112 287 CYS   B C   
13842 O  O   . CYS   B 287 ? 0.2223 0.2152 0.1360 0.0627  0.0172  -0.0088 287 CYS   B O   
13843 C  CB  . CYS   B 287 ? 0.2009 0.1800 0.1288 0.0641  0.0175  -0.0097 287 CYS   B CB  
13844 S  SG  . CYS   B 287 ? 0.1785 0.1567 0.1197 0.0625  0.0185  -0.0056 287 CYS   B SG  
13849 N  N   . TYR   B 288 ? 0.2354 0.2184 0.1484 0.0669  0.0171  -0.0176 288 TYR   B N   
13850 C  CA  . TYR   B 288 ? 0.2102 0.1939 0.1229 0.0671  0.0155  -0.0226 288 TYR   B CA  
13851 C  C   . TYR   B 288 ? 0.2536 0.2319 0.1513 0.0639  0.0119  -0.0227 288 TYR   B C   
13852 O  O   . TYR   B 288 ? 0.2493 0.2213 0.1497 0.0623  0.0094  -0.0224 288 TYR   B O   
13853 C  CB  . TYR   B 288 ? 0.2469 0.2234 0.1542 0.0692  0.0140  -0.0284 288 TYR   B CB  
13854 C  CG  . TYR   B 288 ? 0.2550 0.2306 0.1605 0.0686  0.0127  -0.0332 288 TYR   B CG  
13855 C  CD1 . TYR   B 288 ? 0.2794 0.2621 0.1825 0.0691  0.0154  -0.0348 288 TYR   B CD1 
13856 C  CD2 . TYR   B 288 ? 0.2873 0.2531 0.1846 0.0672  0.0088  -0.0362 288 TYR   B CD2 
13857 C  CE1 . TYR   B 288 ? 0.3152 0.2961 0.2125 0.0683  0.0145  -0.0394 288 TYR   B CE1 
13858 C  CE2 . TYR   B 288 ? 0.3037 0.2677 0.1982 0.0664  0.0080  -0.0405 288 TYR   B CE2 
13859 C  CZ  . TYR   B 288 ? 0.3413 0.3122 0.2321 0.0671  0.0109  -0.0425 288 TYR   B CZ  
13860 O  OH  . TYR   B 288 ? 0.3568 0.3258 0.2447 0.0661  0.0105  -0.0472 288 TYR   B OH  
13870 N  N   . SER   B 289 ? 0.2526 0.2368 0.1486 0.0621  0.0116  -0.0234 289 SER   B N   
13871 C  CA  . SER   B 289 ? 0.3092 0.2894 0.1935 0.0583  0.0080  -0.0247 289 SER   B CA  
13872 C  C   . SER   B 289 ? 0.2631 0.2434 0.1554 0.0555  0.0062  -0.0201 289 SER   B C   
13873 O  O   . SER   B 289 ? 0.2907 0.2617 0.1747 0.0533  0.0034  -0.0226 289 SER   B O   
13874 C  CB  . SER   B 289 ? 0.3848 0.3550 0.2639 0.0590  0.0059  -0.0318 289 SER   B CB  
13875 O  OG  . SER   B 289 ? 0.4735 0.4389 0.3406 0.0547  0.0028  -0.0336 289 SER   B OG  
13881 N  N   . CYS   B 290 ? 0.2613 0.2489 0.1569 0.0553  0.0078  -0.0133 290 CYS   B N   
13882 C  CA  . CYS   B 290 ? 0.2645 0.2518 0.1625 0.0531  0.0067  -0.0089 290 CYS   B CA  
13883 C  C   . CYS   B 290 ? 0.2360 0.2349 0.1394 0.0507  0.0055  -0.0039 290 CYS   B C   
13884 O  O   . CYS   B 290 ? 0.2258 0.2321 0.1291 0.0523  0.0076  0.0005  290 CYS   B O   
13885 C  CB  . CYS   B 290 ? 0.2422 0.2302 0.1536 0.0554  0.0095  -0.0054 290 CYS   B CB  
13886 S  SG  . CYS   B 290 ? 0.2481 0.2352 0.1651 0.0526  0.0085  -0.0011 290 CYS   B SG  
13891 N  N   . PRO   B 291 ? 0.2855 0.2831 0.1798 0.0468  0.0023  -0.0046 291 PRO   B N   
13892 C  CA  . PRO   B 291 ? 0.2523 0.2625 0.1540 0.0444  0.0006  0.0001  291 PRO   B CA  
13893 C  C   . PRO   B 291 ? 0.2640 0.2774 0.1700 0.0451  0.0016  0.0064  291 PRO   B C   
13894 O  O   . PRO   B 291 ? 0.2713 0.2947 0.1807 0.0441  0.0001  0.0110  291 PRO   B O   
13895 C  CB  . PRO   B 291 ? 0.2931 0.2989 0.1803 0.0398  -0.0029 -0.0046 291 PRO   B CB  
13896 C  CG  . PRO   B 291 ? 0.2735 0.2677 0.1664 0.0392  -0.0029 -0.0087 291 PRO   B CG  
13897 C  CD  . PRO   B 291 ? 0.3167 0.3042 0.2054 0.0441  0.0000  -0.0097 291 PRO   B CD  
13905 N  N   . ILE   B 292 ? 0.2320 0.2395 0.1481 0.0469  0.0039  0.0067  292 ILE   B N   
13906 C  CA  . ILE   B 292 ? 0.2370 0.2469 0.1615 0.0476  0.0054  0.0117  292 ILE   B CA  
13907 C  C   . ILE   B 292 ? 0.2393 0.2528 0.1686 0.0517  0.0090  0.0170  292 ILE   B C   
13908 O  O   . ILE   B 292 ? 0.2422 0.2638 0.1785 0.0527  0.0093  0.0230  292 ILE   B O   
13909 C  CB  . ILE   B 292 ? 0.2449 0.2457 0.1738 0.0464  0.0061  0.0085  292 ILE   B CB  
13910 C  CG1 . ILE   B 292 ? 0.2951 0.2890 0.2112 0.0421  0.0029  0.0034  292 ILE   B CG1 
13911 C  CG2 . ILE   B 292 ? 0.2426 0.2457 0.1793 0.0471  0.0081  0.0127  292 ILE   B CG2 
13912 C  CD1 . ILE   B 292 ? 0.2737 0.2581 0.1939 0.0407  0.0032  0.0003  292 ILE   B CD1 
13924 N  N   . GLY   B 293 ? 0.2060 0.2152 0.1391 0.0539  0.0116  0.0150  293 GLY   B N   
13925 C  CA  . GLY   B 293 ? 0.2226 0.2337 0.1560 0.0570  0.0155  0.0196  293 GLY   B CA  
13926 C  C   . GLY   B 293 ? 0.1830 0.1950 0.1324 0.0583  0.0182  0.0241  293 GLY   B C   
13927 O  O   . GLY   B 293 ? 0.1864 0.2029 0.1369 0.0601  0.0199  0.0301  293 GLY   B O   
13931 N  N   . CYS   B 294 ? 0.2078 0.2119 0.1567 0.0574  0.0187  0.0209  294 CYS   B N   
13932 C  CA  . CYS   B 294 ? 0.2078 0.2100 0.1639 0.0584  0.0219  0.0238  294 CYS   B CA  
13933 C  C   . CYS   B 294 ? 0.1359 0.1383 0.1068 0.0608  0.0263  0.0255  294 CYS   B C   
13934 O  O   . CYS   B 294 ? 0.1753 0.1759 0.1452 0.0620  0.0294  0.0295  294 CYS   B O   
13935 C  CB  . CYS   B 294 ? 0.2136 0.2095 0.1714 0.0562  0.0211  0.0197  294 CYS   B CB  
13936 S  SG  . CYS   B 294 ? 0.1670 0.1544 0.1299 0.0558  0.0219  0.0137  294 CYS   B SG  
13941 N  N   . GLY   B 295 ? 0.1660 0.1643 0.1226 0.0611  0.0267  0.0223  295 GLY   B N   
13942 C  CA  . GLY   B 295 ? 0.1338 0.1325 0.1031 0.0625  0.0310  0.0231  295 GLY   B CA  
13943 C  C   . GLY   B 295 ? 0.2133 0.2135 0.1740 0.0642  0.0341  0.0302  295 GLY   B C   
13944 O  O   . GLY   B 295 ? 0.1883 0.1964 0.1552 0.0644  0.0323  0.0344  295 GLY   B O   
13948 N  N   . ARG   B 296 ? 0.1492 0.1486 0.1285 0.0647  0.0387  0.0321  296 ARG   B N   
13949 C  CA  . ARG   B 296 ? 0.1612 0.1624 0.1443 0.0663  0.0423  0.0394  296 ARG   B CA  
13950 C  C   . ARG   B 296 ? 0.1931 0.1935 0.1703 0.0664  0.0462  0.0406  296 ARG   B C   
13951 O  O   . ARG   B 296 ? 0.1753 0.1733 0.1574 0.0653  0.0479  0.0357  296 ARG   B O   
13952 C  CB  . ARG   B 296 ? 0.1860 0.1820 0.1742 0.0670  0.0451  0.0413  296 ARG   B CB  
13953 C  CG  . ARG   B 296 ? 0.1779 0.1746 0.1707 0.0666  0.0423  0.0404  296 ARG   B CG  
13954 C  CD  . ARG   B 296 ? 0.1891 0.1923 0.1778 0.0680  0.0393  0.0459  296 ARG   B CD  
13955 N  NE  . ARG   B 296 ? 0.1491 0.1585 0.1367 0.0670  0.0344  0.0439  296 ARG   B NE  
13956 C  CZ  . ARG   B 296 ? 0.2093 0.2243 0.1841 0.0672  0.0308  0.0475  296 ARG   B CZ  
13957 N  NH1 . ARG   B 296 ? 0.1792 0.1998 0.1668 0.0696  0.0315  0.0541  296 ARG   B NH1 
13958 N  NH2 . ARG   B 296 ? 0.1920 0.2117 0.1645 0.0653  0.0268  0.0443  296 ARG   B NH2 
13972 N  N   . TRP   B 297 ? 0.1823 0.1875 0.1604 0.0674  0.0472  0.0472  297 TRP   B N   
13973 C  CA  . TRP   B 297 ? 0.1735 0.1798 0.1544 0.0670  0.0519  0.0496  297 TRP   B CA  
13974 C  C   . TRP   B 297 ? 0.2318 0.2330 0.2065 0.0685  0.0553  0.0579  297 TRP   B C   
13975 O  O   . TRP   B 297 ? 0.1854 0.1928 0.1690 0.0703  0.0529  0.0640  297 TRP   B O   
13976 C  CB  . TRP   B 297 ? 0.1835 0.1952 0.1515 0.0665  0.0503  0.0496  297 TRP   B CB  
13977 C  CG  . TRP   B 297 ? 0.1925 0.2051 0.1590 0.0653  0.0551  0.0498  297 TRP   B CG  
13978 C  CD1 . TRP   B 297 ? 0.1974 0.2128 0.1608 0.0652  0.0578  0.0563  297 TRP   B CD1 
13979 C  CD2 . TRP   B 297 ? 0.1998 0.2112 0.1696 0.0638  0.0578  0.0428  297 TRP   B CD2 
13980 N  NE1 . TRP   B 297 ? 0.2101 0.2253 0.1717 0.0633  0.0624  0.0539  297 TRP   B NE1 
13981 C  CE2 . TRP   B 297 ? 0.1980 0.2121 0.1674 0.0625  0.0625  0.0456  297 TRP   B CE2 
13982 C  CE3 . TRP   B 297 ? 0.2384 0.2461 0.2065 0.0634  0.0565  0.0349  297 TRP   B CE3 
13983 C  CZ2 . TRP   B 297 ? 0.2412 0.2551 0.2083 0.0608  0.0660  0.0398  297 TRP   B CZ2 
13984 C  CZ3 . TRP   B 297 ? 0.2047 0.2148 0.1819 0.0623  0.0597  0.0297  297 TRP   B CZ3 
13985 C  CH2 . TRP   B 297 ? 0.2456 0.2576 0.2162 0.0609  0.0644  0.0320  297 TRP   B CH2 
13996 N  N   . VAL   B 298 ? 0.1633 0.1615 0.1589 0.0678  0.0606  0.0582  298 VAL   B N   
13997 C  CA  . VAL   B 298 ? 0.2118 0.2032 0.2038 0.0695  0.0643  0.0657  298 VAL   B CA  
13998 C  C   . VAL   B 298 ? 0.1953 0.1854 0.1947 0.0685  0.0699  0.0701  298 VAL   B C   
13999 O  O   . VAL   B 298 ? 0.2051 0.1956 0.1983 0.0657  0.0719  0.0658  298 VAL   B O   
14000 C  CB  . VAL   B 298 ? 0.1874 0.1737 0.1940 0.0698  0.0658  0.0626  298 VAL   B CB  
14001 C  CG1 . VAL   B 298 ? 0.2059 0.1943 0.2103 0.0707  0.0607  0.0598  298 VAL   B CG1 
14002 C  CG2 . VAL   B 298 ? 0.1792 0.1606 0.1878 0.0667  0.0693  0.0558  298 VAL   B CG2 
14012 N  N   . ARG   B 299 ? 0.2335 0.2182 0.2289 0.0705  0.0726  0.0786  299 ARG   B N   
14013 C  CA  . ARG   B 299 ? 0.1893 0.1718 0.1957 0.0693  0.0786  0.0844  299 ARG   B CA  
14014 C  C   . ARG   B 299 ? 0.2291 0.1996 0.2357 0.0683  0.0843  0.0831  299 ARG   B C   
14015 O  O   . ARG   B 299 ? 0.2321 0.1988 0.2471 0.0711  0.0841  0.0858  299 ARG   B O   
14016 C  CB  . ARG   B 299 ? 0.2470 0.2289 0.2393 0.0723  0.0777  0.0951  299 ARG   B CB  
14017 C  CG  . ARG   B 299 ? 0.2444 0.2235 0.2383 0.0706  0.0830  0.1017  299 ARG   B CG  
14018 C  CD  . ARG   B 299 ? 0.2816 0.2632 0.2668 0.0729  0.0799  0.1101  299 ARG   B CD  
14019 N  NE  . ARG   B 299 ? 0.2658 0.2587 0.2460 0.0736  0.0740  0.1106  299 ARG   B NE  
14020 C  CZ  . ARG   B 299 ? 0.2723 0.2718 0.2517 0.0764  0.0674  0.1117  299 ARG   B CZ  
14021 N  NH1 . ARG   B 299 ? 0.2871 0.2841 0.2745 0.0789  0.0661  0.1121  299 ARG   B NH1 
14022 N  NH2 . ARG   B 299 ? 0.2726 0.2816 0.2429 0.0761  0.0623  0.1119  299 ARG   B NH2 
14036 N  N   . LEU   B 300 ? 0.2208 0.1887 0.2321 0.0643  0.0892  0.0789  300 LEU   B N   
14037 C  CA  . LEU   B 300 ? 0.2271 0.1852 0.2463 0.0624  0.0954  0.0779  300 LEU   B CA  
14038 C  C   . LEU   B 300 ? 0.2639 0.2148 0.2853 0.0639  0.0999  0.0882  300 LEU   B C   
14039 O  O   . LEU   B 300 ? 0.2979 0.2518 0.3091 0.0656  0.0981  0.0955  300 LEU   B O   
14040 C  CB  . LEU   B 300 ? 0.2180 0.1770 0.2391 0.0572  0.0987  0.0698  300 LEU   B CB  
14041 C  CG  . LEU   B 300 ? 0.2493 0.2148 0.2713 0.0563  0.0944  0.0597  300 LEU   B CG  
14042 C  CD1 . LEU   B 300 ? 0.2980 0.2650 0.3154 0.0517  0.0973  0.0531  300 LEU   B CD1 
14043 C  CD2 . LEU   B 300 ? 0.2915 0.2520 0.3137 0.0576  0.0924  0.0560  300 LEU   B CD2 
14055 N  N   . LYS   B 301 ? 0.3087 0.2482 0.3340 0.0631  0.1054  0.0891  301 LYS   B N   
14056 C  CA  . LYS   B 301 ? 0.3231 0.2580 0.3537 0.0640  0.1079  0.0954  301 LYS   B CA  
14057 C  C   . LYS   B 301 ? 0.2879 0.2235 0.3127 0.0614  0.1105  0.1003  301 LYS   B C   
14058 O  O   . LYS   B 301 ? 0.3309 0.2646 0.3487 0.0633  0.1092  0.1071  301 LYS   B O   
14059 C  CB  . LYS   B 301 ? 0.4027 0.3274 0.4380 0.0622  0.1128  0.0917  301 LYS   B CB  
14060 C  CG  . LYS   B 301 ? 0.4215 0.3486 0.4715 0.0636  0.1105  0.0866  301 LYS   B CG  
14061 C  CD  . LYS   B 301 ? 0.5438 0.4597 0.5881 0.0606  0.1157  0.0817  301 LYS   B CD  
14062 C  CE  . LYS   B 301 ? 0.4983 0.4100 0.5537 0.0554  0.1219  0.0775  301 LYS   B CE  
14063 N  NZ  . LYS   B 301 ? 0.4959 0.4082 0.5510 0.0525  0.1218  0.0690  301 LYS   B NZ  
14077 N  N   . ASP   B 302 ? 0.2693 0.2073 0.2915 0.0565  0.1137  0.0964  302 ASP   B N   
14078 C  CA  . ASP   B 302 ? 0.3362 0.2731 0.3405 0.0528  0.1168  0.0990  302 ASP   B CA  
14079 C  C   . ASP   B 302 ? 0.2552 0.2050 0.2614 0.0544  0.1119  0.1029  302 ASP   B C   
14080 O  O   . ASP   B 302 ? 0.2663 0.2171 0.2613 0.0512  0.1137  0.1053  302 ASP   B O   
14081 C  CB  . ASP   B 302 ? 0.3244 0.2630 0.3386 0.0463  0.1224  0.0915  302 ASP   B CB  
14082 C  CG  . ASP   B 302 ? 0.3140 0.2641 0.3271 0.0453  0.1193  0.0829  302 ASP   B CG  
14083 O  OD1 . ASP   B 302 ? 0.2780 0.2341 0.2901 0.0494  0.1126  0.0819  302 ASP   B OD1 
14084 O  OD2 . ASP   B 302 ? 0.3521 0.3055 0.3645 0.0403  0.1224  0.0760  302 ASP   B OD2 
14089 N  N   . GLY   B 303 ? 0.2577 0.2132 0.2572 0.0588  0.1057  0.1032  303 GLY   B N   
14090 C  CA  . GLY   B 303 ? 0.2725 0.2380 0.2610 0.0601  0.1007  0.1055  303 GLY   B CA  
14091 C  C   . GLY   B 303 ? 0.2662 0.2409 0.2501 0.0578  0.0990  0.0969  303 GLY   B C   
14092 O  O   . GLY   B 303 ? 0.2454 0.2294 0.2240 0.0592  0.0941  0.0970  303 GLY   B O   
14096 N  N   . THR   B 304 ? 0.2514 0.2255 0.2427 0.0544  0.1019  0.0879  304 THR   B N   
14097 C  CA  . THR   B 304 ? 0.2435 0.2262 0.2334 0.0528  0.0992  0.0776  304 THR   B CA  
14098 C  C   . THR   B 304 ? 0.2258 0.2113 0.2165 0.0565  0.0920  0.0736  304 THR   B C   
14099 O  O   . THR   B 304 ? 0.2423 0.2222 0.2364 0.0592  0.0906  0.0772  304 THR   B O   
14100 C  CB  . THR   B 304 ? 0.2521 0.2348 0.2531 0.0484  0.1040  0.0698  304 THR   B CB  
14101 O  OG1 . THR   B 304 ? 0.2768 0.2507 0.2803 0.0487  0.1046  0.0671  304 THR   B OG1 
14102 C  CG2 . THR   B 304 ? 0.3338 0.3131 0.3250 0.0439  0.1111  0.0726  304 THR   B CG2 
14110 N  N   . GLU   B 305 ? 0.1940 0.1879 0.1836 0.0564  0.0877  0.0664  305 GLU   B N   
14111 C  CA  . GLU   B 305 ? 0.2167 0.2115 0.1992 0.0593  0.0811  0.0627  305 GLU   B CA  
14112 C  C   . GLU   B 305 ? 0.2145 0.2106 0.2005 0.0581  0.0795  0.0521  305 GLU   B C   
14113 O  O   . GLU   B 305 ? 0.1989 0.1987 0.1898 0.0554  0.0823  0.0474  305 GLU   B O   
14114 C  CB  . GLU   B 305 ? 0.1721 0.1757 0.1528 0.0609  0.0765  0.0656  305 GLU   B CB  
14115 C  CG  . GLU   B 305 ? 0.2149 0.2171 0.1839 0.0621  0.0773  0.0761  305 GLU   B CG  
14116 C  CD  . GLU   B 305 ? 0.2054 0.2170 0.1707 0.0629  0.0734  0.0792  305 GLU   B CD  
14117 O  OE1 . GLU   B 305 ? 0.2402 0.2561 0.1952 0.0624  0.0700  0.0722  305 GLU   B OE1 
14118 O  OE2 . GLU   B 305 ? 0.2472 0.2579 0.2023 0.0641  0.0732  0.0882  305 GLU   B OE2 
14125 N  N   . CYS   B 306 ? 0.1549 0.1513 0.1517 0.0598  0.0749  0.0486  306 CYS   B N   
14126 C  CA  . CYS   B 306 ? 0.2058 0.2006 0.1958 0.0592  0.0726  0.0394  306 CYS   B CA  
14127 C  C   . CYS   B 306 ? 0.2108 0.2044 0.1986 0.0613  0.0668  0.0375  306 CYS   B C   
14128 O  O   . CYS   B 306 ? 0.1811 0.1758 0.1740 0.0631  0.0648  0.0432  306 CYS   B O   
14129 C  CB  . CYS   B 306 ? 0.1664 0.1583 0.1729 0.0568  0.0770  0.0363  306 CYS   B CB  
14130 S  SG  . CYS   B 306 ? 0.2190 0.2004 0.2256 0.0573  0.0787  0.0403  306 CYS   B SG  
14136 N  N   . GLY   B 307 ? 0.1422 0.1375 0.1390 0.0609  0.0636  0.0300  307 GLY   B N   
14137 C  CA  . GLY   B 307 ? 0.1565 0.1491 0.1487 0.0621  0.0589  0.0279  307 GLY   B CA  
14138 C  C   . GLY   B 307 ? 0.1753 0.1619 0.1707 0.0623  0.0602  0.0312  307 GLY   B C   
14139 O  O   . GLY   B 307 ? 0.1625 0.1456 0.1670 0.0608  0.0645  0.0304  307 GLY   B O   
14143 N  N   . GLY   B 308 ? 0.1609 0.1489 0.1591 0.0637  0.0571  0.0342  308 GLY   B N   
14144 C  CA  . GLY   B 308 ? 0.1762 0.1599 0.1789 0.0645  0.0585  0.0373  308 GLY   B CA  
14145 C  C   . GLY   B 308 ? 0.1934 0.1726 0.1952 0.0624  0.0564  0.0317  308 GLY   B C   
14146 O  O   . GLY   B 308 ? 0.1698 0.1504 0.1713 0.0613  0.0531  0.0259  308 GLY   B O   
14150 N  N   . PRO   B 309 ? 0.1772 0.1539 0.1884 0.0609  0.0573  0.0330  309 PRO   B N   
14151 C  CA  . PRO   B 309 ? 0.1910 0.1642 0.2016 0.0573  0.0552  0.0275  309 PRO   B CA  
14152 C  C   . PRO   B 309 ? 0.1877 0.1627 0.1943 0.0581  0.0511  0.0263  309 PRO   B C   
14153 O  O   . PRO   B 309 ? 0.1571 0.1364 0.1669 0.0612  0.0506  0.0311  309 PRO   B O   
14154 C  CB  . PRO   B 309 ? 0.1961 0.1655 0.2134 0.0558  0.0589  0.0296  309 PRO   B CB  
14155 C  CG  . PRO   B 309 ? 0.1825 0.1543 0.2027 0.0596  0.0609  0.0373  309 PRO   B CG  
14156 C  CD  . PRO   B 309 ? 0.1673 0.1431 0.1841 0.0626  0.0607  0.0397  309 PRO   B CD  
14164 N  N   . GLU   B 310 ? 0.1861 0.1588 0.1902 0.0555  0.0484  0.0205  310 GLU   B N   
14165 C  CA  . GLU   B 310 ? 0.1661 0.1391 0.1683 0.0558  0.0455  0.0187  310 GLU   B CA  
14166 C  C   . GLU   B 310 ? 0.1325 0.1047 0.1446 0.0539  0.0475  0.0190  310 GLU   B C   
14167 O  O   . GLU   B 310 ? 0.1678 0.1364 0.1790 0.0518  0.0504  0.0189  310 GLU   B O   
14168 C  CB  . GLU   B 310 ? 0.1815 0.1510 0.1740 0.0542  0.0421  0.0129  310 GLU   B CB  
14169 C  CG  . GLU   B 310 ? 0.1404 0.1125 0.1335 0.0557  0.0403  0.0113  310 GLU   B CG  
14170 C  CD  . GLU   B 310 ? 0.1651 0.1402 0.1498 0.0589  0.0381  0.0133  310 GLU   B CD  
14171 O  OE1 . GLU   B 310 ? 0.1585 0.1360 0.1431 0.0587  0.0368  0.0160  310 GLU   B OE1 
14172 O  OE2 . GLU   B 310 ? 0.2044 0.1807 0.1826 0.0599  0.0368  0.0120  310 GLU   B OE2 
14179 N  N   . TYR   B 311 ? 0.1499 0.1222 0.1570 0.0544  0.0462  0.0189  311 TYR   B N   
14180 C  CA  . TYR   B 311 ? 0.1578 0.1292 0.1696 0.0527  0.0484  0.0182  311 TYR   B CA  
14181 C  C   . TYR   B 311 ? 0.1504 0.1170 0.1663 0.0485  0.0498  0.0136  311 TYR   B C   
14182 O  O   . TYR   B 311 ? 0.1594 0.1245 0.1790 0.0474  0.0531  0.0141  311 TYR   B O   
14183 C  CB  . TYR   B 311 ? 0.1494 0.1227 0.1615 0.0534  0.0471  0.0173  311 TYR   B CB  
14184 C  CG  . TYR   B 311 ? 0.1566 0.1289 0.1732 0.0513  0.0497  0.0154  311 TYR   B CG  
14185 C  CD1 . TYR   B 311 ? 0.1650 0.1393 0.1888 0.0519  0.0525  0.0183  311 TYR   B CD1 
14186 C  CD2 . TYR   B 311 ? 0.1657 0.1335 0.1772 0.0486  0.0496  0.0105  311 TYR   B CD2 
14187 C  CE1 . TYR   B 311 ? 0.1524 0.1265 0.1832 0.0499  0.0551  0.0161  311 TYR   B CE1 
14188 C  CE2 . TYR   B 311 ? 0.1683 0.1355 0.1840 0.0463  0.0528  0.0085  311 TYR   B CE2 
14189 C  CZ  . TYR   B 311 ? 0.1664 0.1367 0.1908 0.0471  0.0555  0.0110  311 TYR   B CZ  
14190 O  OH  . TYR   B 311 ? 0.1598 0.1302 0.1899 0.0451  0.0586  0.0085  311 TYR   B OH  
14200 N  N   . GLU   B 312 ? 0.1705 0.1331 0.1776 0.0464  0.0478  0.0087  312 GLU   B N   
14201 C  CA  . GLU   B 312 ? 0.1731 0.1318 0.1800 0.0428  0.0486  0.0041  312 GLU   B CA  
14202 C  C   . GLU   B 312 ? 0.1595 0.1181 0.1724 0.0419  0.0512  0.0050  312 GLU   B C   
14203 O  O   . GLU   B 312 ? 0.1552 0.1113 0.1715 0.0392  0.0534  0.0025  312 GLU   B O   
14204 C  CB  . GLU   B 312 ? 0.1653 0.1212 0.1662 0.0413  0.0451  -0.0004 312 GLU   B CB  
14205 C  CG  . GLU   B 312 ? 0.1716 0.1266 0.1667 0.0428  0.0425  -0.0008 312 GLU   B CG  
14206 C  CD  . GLU   B 312 ? 0.2127 0.1653 0.2031 0.0418  0.0442  -0.0012 312 GLU   B CD  
14207 O  OE1 . GLU   B 312 ? 0.2072 0.1589 0.2033 0.0391  0.0467  -0.0029 312 GLU   B OE1 
14208 O  OE2 . GLU   B 312 ? 0.2098 0.1642 0.1996 0.0435  0.0430  0.0005  312 GLU   B OE2 
14215 N  N   . THR   B 313 ? 0.1462 0.1076 0.1628 0.0443  0.0512  0.0078  313 THR   B N   
14216 C  CA  . THR   B 313 ? 0.1958 0.1549 0.2097 0.0433  0.0544  0.0089  313 THR   B CA  
14217 C  C   . THR   B 313 ? 0.1768 0.1357 0.2008 0.0438  0.0585  0.0132  313 THR   B C   
14218 O  O   . THR   B 313 ? 0.1840 0.1393 0.2119 0.0419  0.0621  0.0123  313 THR   B O   
14219 C  CB  . THR   B 313 ? 0.1866 0.1486 0.2008 0.0454  0.0536  0.0102  313 THR   B CB  
14220 O  OG1 . THR   B 313 ? 0.1768 0.1399 0.1869 0.0451  0.0494  0.0060  313 THR   B OG1 
14221 C  CG2 . THR   B 313 ? 0.1676 0.1288 0.1878 0.0446  0.0577  0.0114  313 THR   B CG2 
14229 N  N   . LEU   B 314 ? 0.1435 0.1060 0.1721 0.0471  0.0581  0.0178  314 LEU   B N   
14230 C  CA  . LEU   B 314 ? 0.1710 0.1320 0.2006 0.0482  0.0614  0.0221  314 LEU   B CA  
14231 C  C   . LEU   B 314 ? 0.1539 0.1134 0.1944 0.0456  0.0634  0.0185  314 LEU   B C   
14232 O  O   . LEU   B 314 ? 0.2185 0.1734 0.2564 0.0449  0.0672  0.0196  314 LEU   B O   
14233 C  CB  . LEU   B 314 ? 0.1623 0.1293 0.1950 0.0523  0.0596  0.0271  314 LEU   B CB  
14234 C  CG  . LEU   B 314 ? 0.1585 0.1293 0.1907 0.0557  0.0585  0.0319  314 LEU   B CG  
14235 C  CD1 . LEU   B 314 ? 0.1727 0.1492 0.1996 0.0588  0.0550  0.0344  314 LEU   B CD1 
14236 C  CD2 . LEU   B 314 ? 0.1876 0.1563 0.2203 0.0576  0.0622  0.0375  314 LEU   B CD2 
14248 N  N   . TRP   B 315 ? 0.1717 0.1303 0.2038 0.0436  0.0610  0.0138  315 TRP   B N   
14249 C  CA  . TRP   B 315 ? 0.1883 0.1438 0.2197 0.0408  0.0630  0.0100  315 TRP   B CA  
14250 C  C   . TRP   B 315 ? 0.1670 0.1189 0.2024 0.0371  0.0649  0.0060  315 TRP   B C   
14251 O  O   . TRP   B 315 ? 0.1544 0.1034 0.1942 0.0358  0.0690  0.0056  315 TRP   B O   
14252 C  CB  . TRP   B 315 ? 0.1753 0.1323 0.2052 0.0397  0.0604  0.0064  315 TRP   B CB  
14253 C  CG  . TRP   B 315 ? 0.1664 0.1199 0.1949 0.0360  0.0624  0.0016  315 TRP   B CG  
14254 C  CD1 . TRP   B 315 ? 0.1533 0.1070 0.1894 0.0355  0.0658  0.0012  315 TRP   B CD1 
14255 C  CD2 . TRP   B 315 ? 0.1537 0.1048 0.1806 0.0327  0.0612  -0.0035 315 TRP   B CD2 
14256 N  NE1 . TRP   B 315 ? 0.1715 0.1214 0.2029 0.0315  0.0670  -0.0039 315 TRP   B NE1 
14257 C  CE2 . TRP   B 315 ? 0.1703 0.1181 0.1939 0.0298  0.0642  -0.0067 315 TRP   B CE2 
14258 C  CE3 . TRP   B 315 ? 0.1924 0.1413 0.2066 0.0319  0.0579  -0.0060 315 TRP   B CE3 
14259 C  CZ2 . TRP   B 315 ? 0.1495 0.0951 0.1711 0.0259  0.0639  -0.0118 315 TRP   B CZ2 
14260 C  CZ3 . TRP   B 315 ? 0.1688 0.1156 0.1823 0.0287  0.0573  -0.0108 315 TRP   B CZ3 
14261 C  CH2 . TRP   B 315 ? 0.1585 0.1029 0.1727 0.0257  0.0602  -0.0135 315 TRP   B CH2 
14272 N  N   . CYS   B 316 ? 0.1803 0.1310 0.2082 0.0359  0.0628  0.0030  316 CYS   B N   
14273 C  CA  . CYS   B 316 ? 0.1635 0.1123 0.1959 0.0322  0.0640  -0.0014 316 CYS   B CA  
14274 C  C   . CYS   B 316 ? 0.1902 0.1353 0.2229 0.0317  0.0685  0.0005  316 CYS   B C   
14275 O  O   . CYS   B 316 ? 0.2066 0.1487 0.2423 0.0285  0.0712  -0.0028 316 CYS   B O   
14276 C  CB  . CYS   B 316 ? 0.1919 0.1405 0.2134 0.0314  0.0601  -0.0049 316 CYS   B CB  
14277 S  SG  . CYS   B 316 ? 0.1932 0.1452 0.2145 0.0342  0.0584  -0.0028 316 CYS   B SG  
14283 N  N   . PHE   B 317 ? 0.1635 0.1103 0.2019 0.0346  0.0695  0.0056  317 PHE   B N   
14284 C  CA  . PHE   B 317 ? 0.1730 0.1164 0.2163 0.0346  0.0745  0.0085  317 PHE   B CA  
14285 C  C   . PHE   B 317 ? 0.1754 0.1175 0.2235 0.0368  0.0777  0.0133  317 PHE   B C   
14286 O  O   . PHE   B 317 ? 0.1956 0.1343 0.2460 0.0380  0.0816  0.0173  317 PHE   B O   
14287 C  CB  . PHE   B 317 ? 0.2085 0.1522 0.2454 0.0359  0.0745  0.0104  317 PHE   B CB  
14288 C  CG  . PHE   B 317 ? 0.1710 0.1173 0.2125 0.0336  0.0727  0.0053  317 PHE   B CG  
14289 C  CD1 . PHE   B 317 ? 0.1911 0.1328 0.2289 0.0297  0.0757  0.0008  317 PHE   B CD1 
14290 C  CD2 . PHE   B 317 ? 0.1952 0.1449 0.2265 0.0351  0.0682  0.0041  317 PHE   B CD2 
14291 C  CE1 . PHE   B 317 ? 0.1692 0.1142 0.2097 0.0278  0.0739  -0.0041 317 PHE   B CE1 
14292 C  CE2 . PHE   B 317 ? 0.1990 0.1507 0.2293 0.0336  0.0663  -0.0008 317 PHE   B CE2 
14293 C  CZ  . PHE   B 317 ? 0.2056 0.1543 0.2366 0.0299  0.0691  -0.0049 317 PHE   B CZ  
14303 N  N   . GLY   B 318 ? 0.1750 0.1192 0.2229 0.0379  0.0757  0.0134  318 GLY   B N   
14304 C  CA  . GLY   B 318 ? 0.1784 0.1223 0.2307 0.0407  0.0781  0.0172  318 GLY   B CA  
14305 C  C   . GLY   B 318 ? 0.1626 0.1059 0.2212 0.0387  0.0796  0.0138  318 GLY   B C   
14306 O  O   . GLY   B 318 ? 0.1954 0.1333 0.2520 0.0356  0.0831  0.0105  318 GLY   B O   
14310 N  N   . SER   B 319 ? 0.1658 0.1126 0.2222 0.0402  0.0773  0.0138  319 SER   B N   
14311 C  CA  . SER   B 319 ? 0.1743 0.1206 0.2338 0.0389  0.0792  0.0103  319 SER   B CA  
14312 C  C   . SER   B 319 ? 0.1687 0.1116 0.2267 0.0337  0.0803  0.0039  319 SER   B C   
14313 O  O   . SER   B 319 ? 0.2088 0.1478 0.2662 0.0319  0.0841  0.0012  319 SER   B O   
14314 C  CB  . SER   B 319 ? 0.2000 0.1515 0.2579 0.0409  0.0766  0.0110  319 SER   B CB  
14315 O  OG  . SER   B 319 ? 0.2038 0.1600 0.2641 0.0454  0.0746  0.0167  319 SER   B OG  
14321 N  N   . ASP   B 320 ? 0.1690 0.1120 0.2193 0.0317  0.0772  0.0009  320 ASP   B N   
14322 C  CA  . ASP   B 320 ? 0.1961 0.1357 0.2387 0.0271  0.0774  -0.0051 320 ASP   B CA  
14323 C  C   . ASP   B 320 ? 0.2008 0.1357 0.2479 0.0246  0.0819  -0.0066 320 ASP   B C   
14324 O  O   . ASP   B 320 ? 0.1794 0.1125 0.2290 0.0210  0.0841  -0.0114 320 ASP   B O   
14325 C  CB  . ASP   B 320 ? 0.1676 0.1096 0.2077 0.0262  0.0729  -0.0075 320 ASP   B CB  
14326 C  CG  . ASP   B 320 ? 0.1951 0.1347 0.2245 0.0224  0.0721  -0.0132 320 ASP   B CG  
14327 O  OD1 . ASP   B 320 ? 0.1948 0.1342 0.2280 0.0211  0.0742  -0.0150 320 ASP   B OD1 
14328 O  OD2 . ASP   B 320 ? 0.1681 0.1085 0.1964 0.0212  0.0692  -0.0157 320 ASP   B OD2 
14333 N  N   . CYS   B 321 ? 0.1840 0.1183 0.2383 0.0265  0.0840  -0.0027 321 CYS   B N   
14334 C  CA  . CYS   B 321 ? 0.1956 0.1243 0.2519 0.0238  0.0891  -0.0037 321 CYS   B CA  
14335 C  C   . CYS   B 321 ? 0.2015 0.1271 0.2647 0.0261  0.0939  -0.0003 321 CYS   B C   
14336 O  O   . CYS   B 321 ? 0.1966 0.1178 0.2655 0.0249  0.0986  0.0002  321 CYS   B O   
14337 C  CB  . CYS   B 321 ? 0.1819 0.1105 0.2388 0.0237  0.0889  -0.0029 321 CYS   B CB  
14338 S  SG  . CYS   B 321 ? 0.1913 0.1228 0.2399 0.0208  0.0843  -0.0078 321 CYS   B SG  
14344 N  N   . GLY   B 322 ? 0.1837 0.1128 0.2521 0.0295  0.0928  0.0025  322 GLY   B N   
14345 C  CA  . GLY   B 322 ? 0.1946 0.1213 0.2687 0.0326  0.0967  0.0062  322 GLY   B CA  
14346 C  C   . GLY   B 322 ? 0.2050 0.1300 0.2799 0.0361  0.0979  0.0127  322 GLY   B C   
14347 O  O   . GLY   B 322 ? 0.2107 0.1323 0.2934 0.0378  0.1026  0.0151  322 GLY   B O   
14351 N  N   . SER   B 323 ? 0.1683 0.0992 0.2430 0.0362  0.0931  0.0155  323 SER   B N   
14352 C  CA  . SER   B 323 ? 0.2015 0.1291 0.2739 0.0404  0.0956  0.0216  323 SER   B CA  
14353 C  C   . SER   B 323 ? 0.2099 0.1439 0.2816 0.0452  0.0913  0.0272  323 SER   B C   
14354 O  O   . SER   B 323 ? 0.2022 0.1415 0.2708 0.0450  0.0867  0.0250  323 SER   B O   
14355 C  CB  . SER   B 323 ? 0.2066 0.1322 0.2755 0.0377  0.0962  0.0204  323 SER   B CB  
14356 O  OG  . SER   B 323 ? 0.1818 0.1065 0.2543 0.0402  0.0985  0.0261  323 SER   B OG  
14362 N  N   . TYR   B 324 ? 0.2120 0.1462 0.2879 0.0495  0.0928  0.0339  324 TYR   B N   
14363 C  CA  . TYR   B 324 ? 0.2162 0.1568 0.2908 0.0543  0.0890  0.0395  324 TYR   B CA  
14364 C  C   . TYR   B 324 ? 0.2284 0.1684 0.3016 0.0571  0.0899  0.0462  324 TYR   B C   
14365 O  O   . TYR   B 324 ? 0.2362 0.1799 0.3125 0.0619  0.0887  0.0523  324 TYR   B O   
14366 C  CB  . TYR   B 324 ? 0.1855 0.1293 0.2682 0.0573  0.0885  0.0404  324 TYR   B CB  
14367 C  CG  . TYR   B 324 ? 0.1880 0.1319 0.2699 0.0541  0.0882  0.0336  324 TYR   B CG  
14368 C  CD1 . TYR   B 324 ? 0.1859 0.1352 0.2631 0.0533  0.0837  0.0309  324 TYR   B CD1 
14369 C  CD2 . TYR   B 324 ? 0.2008 0.1384 0.2841 0.0514  0.0926  0.0295  324 TYR   B CD2 
14370 C  CE1 . TYR   B 324 ? 0.1774 0.1272 0.2553 0.0504  0.0838  0.0248  324 TYR   B CE1 
14371 C  CE2 . TYR   B 324 ? 0.1767 0.1154 0.2627 0.0484  0.0927  0.0234  324 TYR   B CE2 
14372 C  CZ  . TYR   B 324 ? 0.1820 0.1263 0.2629 0.0479  0.0882  0.0210  324 TYR   B CZ  
14373 O  OH  . TYR   B 324 ? 0.1994 0.1435 0.2782 0.0448  0.0885  0.0152  324 TYR   B OH  
14383 N  N   . ASP   B 325 ? 0.2057 0.1425 0.2791 0.0545  0.0922  0.0450  325 ASP   B N   
14384 C  CA  . ASP   B 325 ? 0.2214 0.1568 0.2909 0.0565  0.0940  0.0507  325 ASP   B CA  
14385 C  C   . ASP   B 325 ? 0.2221 0.1633 0.2855 0.0570  0.0894  0.0508  325 ASP   B C   
14386 O  O   . ASP   B 325 ? 0.2220 0.1623 0.2816 0.0535  0.0888  0.0457  325 ASP   B O   
14387 C  CB  . ASP   B 325 ? 0.2308 0.1580 0.3017 0.0534  0.1002  0.0494  325 ASP   B CB  
14388 C  CG  . ASP   B 325 ? 0.2180 0.1433 0.2916 0.0555  0.1036  0.0554  325 ASP   B CG  
14389 O  OD1 . ASP   B 325 ? 0.2112 0.1412 0.2787 0.0584  0.1003  0.0594  325 ASP   B OD1 
14390 O  OD2 . ASP   B 325 ? 0.2629 0.1802 0.3355 0.0541  0.1095  0.0559  325 ASP   B OD2 
14395 N  N   . LEU   B 326 ? 0.2326 0.1793 0.2907 0.0612  0.0860  0.0565  326 LEU   B N   
14396 C  CA  . LEU   B 326 ? 0.1898 0.1440 0.2482 0.0620  0.0814  0.0566  326 LEU   B CA  
14397 C  C   . LEU   B 326 ? 0.2021 0.1529 0.2532 0.0615  0.0841  0.0578  326 LEU   B C   
14398 O  O   . LEU   B 326 ? 0.2014 0.1539 0.2470 0.0599  0.0819  0.0537  326 LEU   B O   
14399 C  CB  . LEU   B 326 ? 0.2223 0.1822 0.2714 0.0666  0.0774  0.0623  326 LEU   B CB  
14400 C  CG  . LEU   B 326 ? 0.1750 0.1439 0.2278 0.0678  0.0724  0.0623  326 LEU   B CG  
14401 C  CD1 . LEU   B 326 ? 0.2183 0.1857 0.2597 0.0643  0.0697  0.0545  326 LEU   B CD1 
14402 C  CD2 . LEU   B 326 ? 0.2128 0.1878 0.2575 0.0718  0.0684  0.0678  326 LEU   B CD2 
14414 N  N   . ASP   B 327 ? 0.2280 0.1743 0.2799 0.0629  0.0888  0.0632  327 ASP   B N   
14415 C  CA  . ASP   B 327 ? 0.2381 0.1808 0.2879 0.0623  0.0929  0.0644  327 ASP   B CA  
14416 C  C   . ASP   B 327 ? 0.2161 0.1558 0.2686 0.0573  0.0946  0.0563  327 ASP   B C   
14417 O  O   . ASP   B 327 ? 0.2255 0.1659 0.2718 0.0565  0.0945  0.0541  327 ASP   B O   
14418 C  CB  . ASP   B 327 ? 0.2557 0.1934 0.3093 0.0638  0.0981  0.0714  327 ASP   B CB  
14419 C  CG  . ASP   B 327 ? 0.2883 0.2306 0.3396 0.0687  0.0955  0.0800  327 ASP   B CG  
14420 O  OD1 . ASP   B 327 ? 0.2743 0.2236 0.3198 0.0706  0.0908  0.0814  327 ASP   B OD1 
14421 O  OD2 . ASP   B 327 ? 0.3505 0.2885 0.4013 0.0705  0.0976  0.0850  327 ASP   B OD2 
14426 N  N   . ALA   B 328 ? 0.2252 0.1603 0.2803 0.0538  0.0964  0.0515  328 ALA   B N   
14427 C  CA  . ALA   B 328 ? 0.2390 0.1700 0.2904 0.0486  0.0978  0.0437  328 ALA   B CA  
14428 C  C   . ALA   B 328 ? 0.1826 0.1214 0.2376 0.0473  0.0913  0.0377  328 ALA   B C   
14429 O  O   . ALA   B 328 ? 0.1978 0.1355 0.2457 0.0444  0.0908  0.0326  328 ALA   B O   
14430 C  CB  . ALA   B 328 ? 0.2261 0.1527 0.2873 0.0457  0.1009  0.0404  328 ALA   B CB  
14436 N  N   . ILE   B 329 ? 0.2095 0.1518 0.2548 0.0495  0.0860  0.0384  329 ILE   B N   
14437 C  CA  . ILE   B 329 ? 0.1873 0.1355 0.2308 0.0486  0.0798  0.0335  329 ILE   B CA  
14438 C  C   . ILE   B 329 ? 0.1894 0.1413 0.2263 0.0508  0.0783  0.0346  329 ILE   B C   
14439 O  O   . ILE   B 329 ? 0.1749 0.1290 0.2096 0.0488  0.0758  0.0292  329 ILE   B O   
14440 C  CB  . ILE   B 329 ? 0.1902 0.1426 0.2343 0.0503  0.0757  0.0337  329 ILE   B CB  
14441 C  CG1 . ILE   B 329 ? 0.2180 0.1665 0.2632 0.0480  0.0771  0.0314  329 ILE   B CG1 
14442 C  CG2 . ILE   B 329 ? 0.2155 0.1718 0.2500 0.0501  0.0699  0.0300  329 ILE   B CG2 
14443 C  CD1 . ILE   B 329 ? 0.2222 0.1746 0.2695 0.0499  0.0744  0.0322  329 ILE   B CD1 
14455 N  N   . ASN   B 330 ? 0.1989 0.1522 0.2340 0.0549  0.0798  0.0418  330 ASN   B N   
14456 C  CA  . ASN   B 330 ? 0.1768 0.1347 0.2113 0.0571  0.0795  0.0438  330 ASN   B CA  
14457 C  C   . ASN   B 330 ? 0.1883 0.1438 0.2248 0.0541  0.0833  0.0393  330 ASN   B C   
14458 O  O   . ASN   B 330 ? 0.1964 0.1563 0.2252 0.0536  0.0811  0.0354  330 ASN   B O   
14459 C  CB  . ASN   B 330 ? 0.1902 0.1493 0.2233 0.0621  0.0814  0.0531  330 ASN   B CB  
14460 C  CG  . ASN   B 330 ? 0.2328 0.1959 0.2584 0.0650  0.0765  0.0570  330 ASN   B CG  
14461 O  OD1 . ASN   B 330 ? 0.1902 0.1580 0.2201 0.0640  0.0717  0.0523  330 ASN   B OD1 
14462 N  ND2 . ASN   B 330 ? 0.2282 0.1935 0.2588 0.0686  0.0772  0.0650  330 ASN   B ND2 
14469 N  N   A GLU   B 331 ? 0.2202 0.1676 0.2551 0.0517  0.0888  0.0394  331 GLU   B N   
14470 N  N   B GLU   B 331 ? 0.2202 0.1677 0.2551 0.0517  0.0888  0.0394  331 GLU   B N   
14471 C  CA  A GLU   B 331 ? 0.1745 0.1222 0.2229 0.0480  0.0932  0.0351  331 GLU   B CA  
14472 C  CA  B GLU   B 331 ? 0.1745 0.1222 0.2229 0.0480  0.0932  0.0351  331 GLU   B CA  
14473 C  C   A GLU   B 331 ? 0.1759 0.1246 0.2166 0.0438  0.0887  0.0260  331 GLU   B C   
14474 C  C   B GLU   B 331 ? 0.1759 0.1246 0.2166 0.0438  0.0887  0.0260  331 GLU   B C   
14475 O  O   A GLU   B 331 ? 0.1706 0.1239 0.2094 0.0424  0.0875  0.0214  331 GLU   B O   
14476 O  O   B GLU   B 331 ? 0.1706 0.1239 0.2094 0.0424  0.0875  0.0214  331 GLU   B O   
14477 C  CB  A GLU   B 331 ? 0.2752 0.2117 0.3199 0.0467  0.1007  0.0380  331 GLU   B CB  
14478 C  CB  B GLU   B 331 ? 0.2752 0.2117 0.3199 0.0467  0.1007  0.0380  331 GLU   B CB  
14479 C  CG  A GLU   B 331 ? 0.3197 0.2551 0.3761 0.0415  0.1052  0.0325  331 GLU   B CG  
14480 C  CG  B GLU   B 331 ? 0.3197 0.2551 0.3761 0.0415  0.1052  0.0325  331 GLU   B CG  
14481 C  CD  A GLU   B 331 ? 0.4777 0.4140 0.5306 0.0415  0.1109  0.0344  331 GLU   B CD  
14482 C  CD  B GLU   B 331 ? 0.4777 0.4140 0.5306 0.0415  0.1110  0.0344  331 GLU   B CD  
14483 O  OE1 A GLU   B 331 ? 0.5618 0.4998 0.6052 0.0447  0.1103  0.0411  331 GLU   B OE1 
14484 O  OE1 B GLU   B 331 ? 0.5619 0.4998 0.6052 0.0447  0.1103  0.0411  331 GLU   B OE1 
14485 O  OE2 A GLU   B 331 ? 0.5846 0.5191 0.6337 0.0367  0.1145  0.0295  331 GLU   B OE2 
14486 O  OE2 B GLU   B 331 ? 0.5846 0.5190 0.6337 0.0366  0.1145  0.0295  331 GLU   B OE2 
14499 N  N   . ALA   B 332 ? 0.1954 0.1411 0.2347 0.0421  0.0863  0.0233  332 ALA   B N   
14500 C  CA  . ALA   B 332 ? 0.1968 0.1446 0.2354 0.0386  0.0821  0.0155  332 ALA   B CA  
14501 C  C   . ALA   B 332 ? 0.1679 0.1234 0.2039 0.0402  0.0758  0.0124  332 ALA   B C   
14502 O  O   . ALA   B 332 ? 0.1669 0.1251 0.2000 0.0383  0.0737  0.0068  332 ALA   B O   
14503 C  CB  . ALA   B 332 ? 0.2038 0.1489 0.2446 0.0375  0.0809  0.0144  332 ALA   B CB  
14510 N  N   . ASN   B 333 ? 0.1828 0.1404 0.2113 0.0437  0.0726  0.0162  333 ASN   B N   
14511 C  CA  . ASN   B 333 ? 0.1683 0.1317 0.1926 0.0454  0.0670  0.0140  333 ASN   B CA  
14512 C  C   . ASN   B 333 ? 0.1568 0.1248 0.1820 0.0457  0.0681  0.0121  333 ASN   B C   
14513 O  O   . ASN   B 333 ? 0.1787 0.1494 0.1986 0.0448  0.0644  0.0065  333 ASN   B O   
14514 C  CB  . ASN   B 333 ? 0.1744 0.1396 0.1940 0.0491  0.0647  0.0187  333 ASN   B CB  
14515 C  CG  . ASN   B 333 ? 0.1701 0.1408 0.1887 0.0508  0.0591  0.0160  333 ASN   B CG  
14516 O  OD1 . ASN   B 333 ? 0.2082 0.1770 0.2178 0.0490  0.0553  0.0110  333 ASN   B OD1 
14517 N  ND2 . ASN   B 333 ? 0.2288 0.2016 0.2362 0.0541  0.0591  0.0192  333 ASN   B ND2 
14524 N  N   . MET   B 334 ? 0.1689 0.1361 0.1930 0.0471  0.0732  0.0169  334 MET   B N   
14525 C  CA  . MET   B 334 ? 0.1673 0.1393 0.1917 0.0469  0.0756  0.0157  334 MET   B CA  
14526 C  C   . MET   B 334 ? 0.1600 0.1334 0.1899 0.0428  0.0761  0.0087  334 MET   B C   
14527 O  O   . MET   B 334 ? 0.1662 0.1457 0.1932 0.0428  0.0737  0.0042  334 MET   B O   
14528 C  CB  . MET   B 334 ? 0.1662 0.1378 0.1954 0.0482  0.0826  0.0224  334 MET   B CB  
14529 C  CG  . MET   B 334 ? 0.2261 0.2022 0.2490 0.0472  0.0856  0.0212  334 MET   B CG  
14530 S  SD  . MET   B 334 ? 0.2189 0.1943 0.2580 0.0419  0.0920  0.0180  334 MET   B SD  
14531 C  CE  . MET   B 334 ? 0.3315 0.2937 0.3637 0.0421  0.0987  0.0255  334 MET   B CE  
14541 N  N   . LEU   B 335 ? 0.1769 0.1436 0.2081 0.0398  0.0793  0.0078  335 LEU   B N   
14542 C  CA  . LEU   B 335 ? 0.1458 0.1151 0.1884 0.0356  0.0806  0.0013  335 LEU   B CA  
14543 C  C   . LEU   B 335 ? 0.1676 0.1403 0.2026 0.0356  0.0737  -0.0051 335 LEU   B C   
14544 O  O   . LEU   B 335 ? 0.1866 0.1649 0.2220 0.0345  0.0727  -0.0102 335 LEU   B O   
14545 C  CB  . LEU   B 335 ? 0.1939 0.1536 0.2349 0.0324  0.0857  0.0020  335 LEU   B CB  
14546 C  CG  . LEU   B 335 ? 0.2013 0.1561 0.2499 0.0319  0.0942  0.0072  335 LEU   B CG  
14547 C  CD1 . LEU   B 335 ? 0.2321 0.1770 0.2827 0.0290  0.0985  0.0075  335 LEU   B CD1 
14548 C  CD2 . LEU   B 335 ? 0.2005 0.1600 0.2503 0.0294  0.0981  0.0055  335 LEU   B CD2 
14560 N  N   . CYS   B 336 ? 0.1762 0.1462 0.2059 0.0372  0.0690  -0.0049 336 CYS   B N   
14561 C  CA  . CYS   B 336 ? 0.1663 0.1390 0.1926 0.0374  0.0626  -0.0097 336 CYS   B CA  
14562 C  C   . CYS   B 336 ? 0.1707 0.1497 0.1926 0.0404  0.0586  -0.0116 336 CYS   B C   
14563 O  O   . CYS   B 336 ? 0.1411 0.1244 0.1652 0.0409  0.0551  -0.0168 336 CYS   B O   
14564 C  CB  . CYS   B 336 ? 0.1403 0.1096 0.1676 0.0379  0.0594  -0.0086 336 CYS   B CB  
14565 S  SG  . CYS   B 336 ? 0.1929 0.1546 0.2177 0.0337  0.0627  -0.0091 336 CYS   B SG  
14571 N  N   . ASN   B 337 ? 0.1777 0.1579 0.1970 0.0430  0.0592  -0.0072 337 ASN   B N   
14572 C  CA  . ASN   B 337 ? 0.1569 0.1439 0.1768 0.0458  0.0562  -0.0085 337 ASN   B CA  
14573 C  C   . ASN   B 337 ? 0.1614 0.1540 0.1819 0.0450  0.0589  -0.0121 337 ASN   B C   
14574 O  O   . ASN   B 337 ? 0.1557 0.1540 0.1761 0.0467  0.0554  -0.0163 337 ASN   B O   
14575 C  CB  . ASN   B 337 ? 0.1900 0.1755 0.1996 0.0485  0.0569  -0.0029 337 ASN   B CB  
14576 C  CG  . ASN   B 337 ? 0.1568 0.1398 0.1678 0.0500  0.0532  -0.0004 337 ASN   B CG  
14577 O  OD1 . ASN   B 337 ? 0.1671 0.1474 0.1728 0.0492  0.0489  -0.0039 337 ASN   B OD1 
14578 N  ND2 . ASN   B 337 ? 0.1754 0.1570 0.1806 0.0521  0.0550  0.0053  337 ASN   B ND2 
14585 N  N   . GLU   B 338 ? 0.1555 0.1479 0.1831 0.0424  0.0651  -0.0105 338 GLU   B N   
14586 C  CA  . GLU   B 338 ? 0.1705 0.1690 0.2001 0.0405  0.0689  -0.0133 338 GLU   B CA  
14587 C  C   . GLU   B 338 ? 0.1567 0.1593 0.1932 0.0387  0.0671  -0.0203 338 GLU   B C   
14588 O  O   . GLU   B 338 ? 0.1373 0.1484 0.1759 0.0394  0.0659  -0.0248 338 GLU   B O   
14589 C  CB  . GLU   B 338 ? 0.1592 0.1555 0.1951 0.0379  0.0768  -0.0085 338 GLU   B CB  
14590 C  CG  . GLU   B 338 ? 0.1710 0.1664 0.2024 0.0404  0.0790  -0.0019 338 GLU   B CG  
14591 C  CD  . GLU   B 338 ? 0.1926 0.1966 0.2210 0.0414  0.0795  -0.0031 338 GLU   B CD  
14592 O  OE1 . GLU   B 338 ? 0.1564 0.1661 0.1845 0.0438  0.0739  -0.0075 338 GLU   B OE1 
14593 O  OE2 . GLU   B 338 ? 0.2420 0.2469 0.2695 0.0399  0.0855  0.0003  338 GLU   B OE2 
14600 N  N   . TYR   B 339 ? 0.1832 0.1790 0.2179 0.0362  0.0672  -0.0213 339 TYR   B N   
14601 C  CA  . TYR   B 339 ? 0.1569 0.1562 0.1985 0.0343  0.0656  -0.0276 339 TYR   B CA  
14602 C  C   . TYR   B 339 ? 0.1496 0.1506 0.1864 0.0380  0.0582  -0.0308 339 TYR   B C   
14603 O  O   . TYR   B 339 ? 0.1583 0.1638 0.1951 0.0382  0.0558  -0.0359 339 TYR   B O   
14604 C  CB  . TYR   B 339 ? 0.1667 0.1583 0.2097 0.0299  0.0689  -0.0277 339 TYR   B CB  
14605 C  CG  . TYR   B 339 ? 0.1692 0.1581 0.2218 0.0260  0.0769  -0.0254 339 TYR   B CG  
14606 C  CD1 . TYR   B 339 ? 0.2362 0.2297 0.2871 0.0234  0.0812  -0.0271 339 TYR   B CD1 
14607 C  CD2 . TYR   B 339 ? 0.1801 0.1589 0.2324 0.0243  0.0804  -0.0213 339 TYR   B CD2 
14608 C  CE1 . TYR   B 339 ? 0.2351 0.2250 0.2943 0.0194  0.0890  -0.0249 339 TYR   B CE1 
14609 C  CE2 . TYR   B 339 ? 0.2508 0.2234 0.3013 0.0210  0.0881  -0.0189 339 TYR   B CE2 
14610 C  CZ  . TYR   B 339 ? 0.2419 0.2211 0.3041 0.0183  0.0927  -0.0206 339 TYR   B CZ  
14611 O  OH  . TYR   B 339 ? 0.3057 0.2776 0.3660 0.0148  0.1007  -0.0180 339 TYR   B OH  
14621 N  N   . GLY   B 340 ? 0.1635 0.1598 0.1915 0.0410  0.0544  -0.0275 340 GLY   B N   
14622 C  CA  . GLY   B 340 ? 0.1647 0.1608 0.1877 0.0442  0.0477  -0.0302 340 GLY   B CA  
14623 C  C   . GLY   B 340 ? 0.1559 0.1467 0.1782 0.0429  0.0454  -0.0316 340 GLY   B C   
14624 O  O   . GLY   B 340 ? 0.1641 0.1564 0.1837 0.0441  0.0421  -0.0362 340 GLY   B O   
14628 N  N   . ILE   B 341 ? 0.1703 0.1536 0.1882 0.0408  0.0470  -0.0281 341 ILE   B N   
14629 C  CA  . ILE   B 341 ? 0.1496 0.1284 0.1690 0.0391  0.0454  -0.0290 341 ILE   B CA  
14630 C  C   . ILE   B 341 ? 0.1710 0.1440 0.1815 0.0398  0.0433  -0.0250 341 ILE   B C   
14631 O  O   . ILE   B 341 ? 0.1539 0.1277 0.1668 0.0404  0.0450  -0.0204 341 ILE   B O   
14632 C  CB  . ILE   B 341 ? 0.1653 0.1402 0.1855 0.0343  0.0504  -0.0301 341 ILE   B CB  
14633 C  CG1 . ILE   B 341 ? 0.1549 0.1277 0.1816 0.0327  0.0557  -0.0251 341 ILE   B CG1 
14634 C  CG2 . ILE   B 341 ? 0.1649 0.1451 0.1909 0.0325  0.0520  -0.0355 341 ILE   B CG2 
14635 C  CD1 . ILE   B 341 ? 0.1682 0.1369 0.1981 0.0283  0.0613  -0.0258 341 ILE   B CD1 
14647 N  N   . ASP   B 342 ? 0.1871 0.1558 0.1926 0.0392  0.0403  -0.0262 342 ASP   B N   
14648 C  CA  . ASP   B 342 ? 0.1747 0.1399 0.1797 0.0392  0.0391  -0.0229 342 ASP   B CA  
14649 C  C   . ASP   B 342 ? 0.1968 0.1586 0.1996 0.0368  0.0445  -0.0191 342 ASP   B C   
14650 O  O   . ASP   B 342 ? 0.1732 0.1338 0.1842 0.0339  0.0467  -0.0219 342 ASP   B O   
14651 C  CB  . ASP   B 342 ? 0.1791 0.1397 0.1763 0.0390  0.0354  -0.0254 342 ASP   B CB  
14652 C  CG  . ASP   B 342 ? 0.1911 0.1471 0.1842 0.0378  0.0356  -0.0230 342 ASP   B CG  
14653 O  OD1 . ASP   B 342 ? 0.1910 0.1477 0.1848 0.0389  0.0362  -0.0189 342 ASP   B OD1 
14654 O  OD2 . ASP   B 342 ? 0.1955 0.1475 0.1853 0.0356  0.0350  -0.0251 342 ASP   B OD2 
14659 N  N   . THR   B 343 ? 0.1486 0.1304 0.1619 0.0412  0.0662  -0.0033 343 THR   B N   
14660 C  CA  . THR   B 343 ? 0.1834 0.1604 0.1931 0.0377  0.0691  -0.0018 343 THR   B CA  
14661 C  C   . THR   B 343 ? 0.1980 0.1728 0.2092 0.0344  0.0671  -0.0039 343 THR   B C   
14662 O  O   . THR   B 343 ? 0.1902 0.1661 0.2102 0.0302  0.0698  -0.0049 343 THR   B O   
14663 C  CB  . THR   B 343 ? 0.1539 0.1255 0.1623 0.0412  0.0686  0.0012  343 THR   B CB  
14664 O  OG1 . THR   B 343 ? 0.1621 0.1296 0.1626 0.0433  0.0637  -0.0001 343 THR   B OG1 
14665 C  CG2 . THR   B 343 ? 0.1534 0.1257 0.1571 0.0445  0.0719  0.0035  343 THR   B CG2 
14673 N  N   . ILE   B 344 ? 0.1632 0.1362 0.1747 0.0356  0.0630  -0.0046 344 ILE   B N   
14674 C  CA  . ILE   B 344 ? 0.1776 0.1473 0.1856 0.0324  0.0621  -0.0062 344 ILE   B CA  
14675 C  C   . ILE   B 344 ? 0.1643 0.1393 0.1773 0.0283  0.0632  -0.0089 344 ILE   B C   
14676 O  O   . ILE   B 344 ? 0.1433 0.1177 0.1616 0.0246  0.0657  -0.0101 344 ILE   B O   
14677 C  CB  . ILE   B 344 ? 0.1771 0.1421 0.1803 0.0340  0.0584  -0.0060 344 ILE   B CB  
14678 C  CG1 . ILE   B 344 ? 0.1596 0.1202 0.1606 0.0375  0.0566  -0.0049 344 ILE   B CG1 
14679 C  CG2 . ILE   B 344 ? 0.1884 0.1508 0.1916 0.0304  0.0585  -0.0073 344 ILE   B CG2 
14680 C  CD1 . ILE   B 344 ? 0.1646 0.1196 0.1599 0.0382  0.0534  -0.0052 344 ILE   B CD1 
14692 N  N   . THR   B 345 ? 0.1645 0.1452 0.1774 0.0296  0.0613  -0.0096 345 THR   B N   
14693 C  CA  . THR   B 345 ? 0.1830 0.1695 0.1951 0.0262  0.0613  -0.0128 345 THR   B CA  
14694 C  C   . THR   B 345 ? 0.1851 0.1752 0.2049 0.0224  0.0656  -0.0147 345 THR   B C   
14695 O  O   . THR   B 345 ? 0.1479 0.1413 0.1762 0.0179  0.0666  -0.0183 345 THR   B O   
14696 C  CB  . THR   B 345 ? 0.1459 0.1398 0.1604 0.0295  0.0576  -0.0132 345 THR   B CB  
14697 O  OG1 . THR   B 345 ? 0.1670 0.1545 0.1699 0.0315  0.0545  -0.0116 345 THR   B OG1 
14698 C  CG2 . THR   B 345 ? 0.1429 0.1458 0.1592 0.0263  0.0569  -0.0167 345 THR   B CG2 
14706 N  N   . CYS   B 346 ? 0.1506 0.1422 0.1802 0.0240  0.0683  -0.0127 346 CYS   B N   
14707 C  CA  . CYS   B 346 ? 0.1696 0.1627 0.2034 0.0202  0.0733  -0.0135 346 CYS   B CA  
14708 C  C   . CYS   B 346 ? 0.1568 0.1437 0.1972 0.0171  0.0764  -0.0140 346 CYS   B C   
14709 O  O   . CYS   B 346 ? 0.1707 0.1583 0.2133 0.0123  0.0786  -0.0179 346 CYS   B O   
14710 C  CB  . CYS   B 346 ? 0.1714 0.1653 0.2088 0.0230  0.0766  -0.0104 346 CYS   B CB  
14711 S  SG  . CYS   B 346 ? 0.1739 0.1690 0.2207 0.0180  0.0838  -0.0105 346 CYS   B SG  
14717 N  N   . GLY   B 347 ? 0.1847 0.1632 0.2180 0.0200  0.0763  -0.0106 347 GLY   B N   
14718 C  CA  . GLY   B 347 ? 0.1931 0.1654 0.2299 0.0182  0.0790  -0.0103 347 GLY   B CA  
14719 C  C   . GLY   B 347 ? 0.1965 0.1678 0.2315 0.0148  0.0783  -0.0141 347 GLY   B C   
14720 O  O   . GLY   B 347 ? 0.1618 0.1315 0.2065 0.0117  0.0822  -0.0164 347 GLY   B O   
14724 N  N   . ALA   B 348 ? 0.1821 0.1559 0.2144 0.0157  0.0741  -0.0152 348 ALA   B N   
14725 C  CA  . ALA   B 348 ? 0.1832 0.1562 0.2123 0.0127  0.0740  -0.0184 348 ALA   B CA  
14726 C  C   . ALA   B 348 ? 0.1755 0.1541 0.2066 0.0084  0.0748  -0.0235 348 ALA   B C   
14727 O  O   . ALA   B 348 ? 0.1713 0.1490 0.2029 0.0052  0.0766  -0.0271 348 ALA   B O   
14728 C  CB  . ALA   B 348 ? 0.1906 0.1621 0.2122 0.0150  0.0700  -0.0171 348 ALA   B CB  
14734 N  N   . THR   B 349 ? 0.1638 0.1493 0.1979 0.0087  0.0737  -0.0242 349 THR   B N   
14735 C  CA  . THR   B 349 ? 0.1621 0.1548 0.1999 0.0041  0.0740  -0.0298 349 THR   B CA  
14736 C  C   . THR   B 349 ? 0.1722 0.1612 0.2161 -0.0003 0.0798  -0.0325 349 THR   B C   
14737 O  O   . THR   B 349 ? 0.1488 0.1401 0.1986 -0.0050 0.0810  -0.0384 349 THR   B O   
14738 C  CB  . THR   B 349 ? 0.1562 0.1590 0.1958 0.0057  0.0706  -0.0301 349 THR   B CB  
14739 O  OG1 . THR   B 349 ? 0.1676 0.1706 0.1966 0.0101  0.0656  -0.0275 349 THR   B OG1 
14740 C  CG2 . THR   B 349 ? 0.1714 0.1827 0.2141 0.0009  0.0702  -0.0363 349 THR   B CG2 
14748 N  N   . ILE   B 350 ? 0.1542 0.1394 0.2072 0.0012  0.0832  -0.0286 350 ILE   B N   
14749 C  CA  . ILE   B 350 ? 0.1656 0.1448 0.2250 -0.0021 0.0895  -0.0295 350 ILE   B CA  
14750 C  C   . ILE   B 350 ? 0.1750 0.1474 0.2341 -0.0030 0.0911  -0.0315 350 ILE   B C   
14751 O  O   . ILE   B 350 ? 0.1692 0.1393 0.2338 -0.0074 0.0950  -0.0365 350 ILE   B O   
14752 C  CB  . ILE   B 350 ? 0.1635 0.1385 0.2288 0.0009  0.0927  -0.0236 350 ILE   B CB  
14753 C  CG1 . ILE   B 350 ? 0.1754 0.1569 0.2395 0.0011  0.0927  -0.0222 350 ILE   B CG1 
14754 C  CG2 . ILE   B 350 ? 0.1957 0.1616 0.2640 -0.0015 0.0991  -0.0233 350 ILE   B CG2 
14755 C  CD1 . ILE   B 350 ? 0.1737 0.1513 0.2377 0.0053  0.0953  -0.0156 350 ILE   B CD1 
14767 N  N   . ALA   B 351 ? 0.1902 0.1593 0.2427 0.0009  0.0885  -0.0283 351 ALA   B N   
14768 C  CA  . ALA   B 351 ? 0.1910 0.1550 0.2425 0.0004  0.0902  -0.0299 351 ALA   B CA  
14769 C  C   . ALA   B 351 ? 0.1792 0.1467 0.2297 -0.0042 0.0905  -0.0367 351 ALA   B C   
14770 O  O   . ALA   B 351 ? 0.1803 0.1440 0.2349 -0.0070 0.0948  -0.0409 351 ALA   B O   
14771 C  CB  . ALA   B 351 ? 0.1771 0.1395 0.2257 0.0047  0.0872  -0.0256 351 ALA   B CB  
14777 N  N   . ALA   B 352 ? 0.1623 0.1368 0.2074 -0.0043 0.0860  -0.0381 352 ALA   B N   
14778 C  CA  . ALA   B 352 ? 0.1784 0.1565 0.2160 -0.0080 0.0854  -0.0442 352 ALA   B CA  
14779 C  C   . ALA   B 352 ? 0.1612 0.1416 0.2092 -0.0133 0.0886  -0.0510 352 ALA   B C   
14780 O  O   . ALA   B 352 ? 0.1790 0.1572 0.2234 -0.0167 0.0911  -0.0571 352 ALA   B O   
14781 C  CB  . ALA   B 352 ? 0.1897 0.1747 0.2192 -0.0063 0.0795  -0.0433 352 ALA   B CB  
14787 N  N   . ALA   B 353 ? 0.1690 0.1520 0.2221 -0.0141 0.0889  -0.0506 353 ALA   B N   
14788 C  CA  . ALA   B 353 ? 0.1712 0.1566 0.2372 -0.0199 0.0925  -0.0570 353 ALA   B CA  
14789 C  C   . ALA   B 353 ? 0.1682 0.1423 0.2389 -0.0217 0.0993  -0.0583 353 ALA   B C   
14790 O  O   . ALA   B 353 ? 0.1796 0.1522 0.2521 -0.0266 0.1026  -0.0659 353 ALA   B O   
14791 C  CB  . ALA   B 353 ? 0.2465 0.2354 0.3124 -0.0204 0.0923  -0.0553 353 ALA   B CB  
14797 N  N   . MET   B 354 ? 0.1895 0.1551 0.2581 -0.0169 0.1014  -0.0514 354 MET   B N   
14798 C  CA  . MET   B 354 ? 0.1697 0.1262 0.2505 -0.0169 0.1074  -0.0512 354 MET   B CA  
14799 C  C   . MET   B 354 ? 0.2052 0.1587 0.2774 -0.0183 0.1090  -0.0568 354 MET   B C   
14800 O  O   . MET   B 354 ? 0.1930 0.1409 0.2734 -0.0210 0.1145  -0.0617 354 MET   B O   
14801 C  CB  . MET   B 354 ? 0.1994 0.1488 0.2749 -0.0108 0.1079  -0.0422 354 MET   B CB  
14802 C  CG  . MET   B 354 ? 0.1763 0.1254 0.2593 -0.0094 0.1088  -0.0366 354 MET   B CG  
14803 S  SD  . MET   B 354 ? 0.1876 0.1299 0.2704 -0.0020 0.1094  -0.0265 354 MET   B SD  
14804 C  CE  . MET   B 354 ? 0.2351 0.1726 0.3190 -0.0027 0.1139  -0.0223 354 MET   B CE  
14814 N  N   . GLU   B 355 ? 0.2218 0.1799 0.2843 -0.0165 0.1047  -0.0563 355 GLU   B N   
14815 C  CA  . GLU   B 355 ? 0.2009 0.1587 0.2605 -0.0181 0.1065  -0.0612 355 GLU   B CA  
14816 C  C   . GLU   B 355 ? 0.1828 0.1450 0.2406 -0.0241 0.1062  -0.0703 355 GLU   B C   
14817 O  O   . GLU   B 355 ? 0.1899 0.1485 0.2467 -0.0271 0.1086  -0.0746 355 GLU   B O   
14818 C  CB  . GLU   B 355 ? 0.2131 0.1731 0.2615 -0.0150 0.1029  -0.0576 355 GLU   B CB  
14819 C  CG  . GLU   B 355 ? 0.2017 0.1613 0.2470 -0.0168 0.1058  -0.0620 355 GLU   B CG  
14820 C  CD  . GLU   B 355 ? 0.2208 0.1784 0.2568 -0.0136 0.1056  -0.0576 355 GLU   B CD  
14821 O  OE1 . GLU   B 355 ? 0.1837 0.1436 0.2222 -0.0107 0.1009  -0.0513 355 GLU   B OE1 
14822 O  OE2 . GLU   B 355 ? 0.2062 0.1622 0.2463 -0.0148 0.1102  -0.0606 355 GLU   B OE2 
14829 N  N   . LEU   B 356 ? 0.1893 0.1597 0.2421 -0.0255 0.1017  -0.0723 356 LEU   B N   
14830 C  CA  . LEU   B 356 ? 0.1922 0.1689 0.2450 -0.0311 0.1008  -0.0818 356 LEU   B CA  
14831 C  C   . LEU   B 356 ? 0.2148 0.1850 0.2768 -0.0358 0.1073  -0.0881 356 LEU   B C   
14832 O  O   . LEU   B 356 ? 0.2354 0.2049 0.2965 -0.0404 0.1096  -0.0972 356 LEU   B O   
14833 C  CB  . LEU   B 356 ? 0.1992 0.1867 0.2474 -0.0314 0.0939  -0.0812 356 LEU   B CB  
14834 C  CG  . LEU   B 356 ? 0.2097 0.2037 0.2461 -0.0272 0.0874  -0.0772 356 LEU   B CG  
14835 C  CD1 . LEU   B 356 ? 0.2146 0.2193 0.2500 -0.0266 0.0809  -0.0763 356 LEU   B CD1 
14836 C  CD2 . LEU   B 356 ? 0.2383 0.2325 0.2606 -0.0288 0.0869  -0.0822 356 LEU   B CD2 
14848 N  N   . TYR   B 357 ? 0.1951 0.1608 0.2714 -0.0349 0.1102  -0.0835 357 TYR   B N   
14849 C  CA  . TYR   B 357 ? 0.2240 0.1810 0.3103 -0.0390 0.1172  -0.0875 357 TYR   B CA  
14850 C  C   . TYR   B 357 ? 0.2179 0.1645 0.3058 -0.0378 0.1231  -0.0896 357 TYR   B C   
14851 O  O   . TYR   B 357 ? 0.2421 0.1843 0.3322 -0.0425 0.1277  -0.0985 357 TYR   B O   
14852 C  CB  . TYR   B 357 ? 0.2615 0.2132 0.3547 -0.0374 0.1198  -0.0806 357 TYR   B CB  
14853 C  CG  . TYR   B 357 ? 0.2410 0.1830 0.3503 -0.0412 0.1277  -0.0837 357 TYR   B CG  
14854 C  CD1 . TYR   B 357 ? 0.2513 0.1959 0.3683 -0.0488 0.1296  -0.0921 357 TYR   B CD1 
14855 C  CD2 . TYR   B 357 ? 0.2355 0.1648 0.3505 -0.0373 0.1334  -0.0790 357 TYR   B CD2 
14856 C  CE1 . TYR   B 357 ? 0.2865 0.2189 0.4104 -0.0527 0.1376  -0.0956 357 TYR   B CE1 
14857 C  CE2 . TYR   B 357 ? 0.2712 0.1886 0.3928 -0.0402 0.1410  -0.0816 357 TYR   B CE2 
14858 C  CZ  . TYR   B 357 ? 0.2657 0.1856 0.4018 -0.0483 0.1436  -0.0901 357 TYR   B CZ  
14859 O  OH  . TYR   B 357 ? 0.3484 0.2590 0.4849 -0.0512 0.1499  -0.0903 357 TYR   B OH  
14869 N  N   . GLN   B 358 ? 0.1982 0.1442 0.2847 -0.0324 0.1188  -0.0779 358 GLN   B N   
14870 C  CA  . GLN   B 358 ? 0.2287 0.1646 0.3129 -0.0299 0.1259  -0.0804 358 GLN   B CA  
14871 C  C   . GLN   B 358 ? 0.2276 0.1668 0.3066 -0.0340 0.1263  -0.0894 358 GLN   B C   
14872 O  O   . GLN   B 358 ? 0.2177 0.1560 0.3019 -0.0368 0.1251  -0.0873 358 GLN   B O   
14873 C  CB  . GLN   B 358 ? 0.2159 0.1524 0.3003 -0.0235 0.1232  -0.0716 358 GLN   B CB  
14874 C  CG  . GLN   B 358 ? 0.2187 0.1530 0.3024 -0.0221 0.1243  -0.0706 358 GLN   B CG  
14875 C  CD  . GLN   B 358 ? 0.2329 0.1699 0.3086 -0.0176 0.1208  -0.0650 358 GLN   B CD  
14876 O  OE1 . GLN   B 358 ? 0.2051 0.1430 0.2856 -0.0134 0.1182  -0.0578 358 GLN   B OE1 
14877 N  NE2 . GLN   B 358 ? 0.2310 0.1714 0.3027 -0.0188 0.1211  -0.0680 358 GLN   B NE2 
14886 N  N   . ARG   B 359 ? 0.2094 0.1600 0.2787 -0.0358 0.1173  -0.0883 359 ARG   B N   
14887 C  CA  . ARG   B 359 ? 0.2183 0.1721 0.2766 -0.0387 0.1170  -0.0955 359 ARG   B CA  
14888 C  C   . ARG   B 359 ? 0.2277 0.1854 0.2865 -0.0451 0.1174  -0.1067 359 ARG   B C   
14889 O  O   . ARG   B 359 ? 0.2364 0.1982 0.2855 -0.0473 0.1166  -0.1132 359 ARG   B O   
14890 C  CB  . ARG   B 359 ? 0.2176 0.1758 0.2631 -0.0355 0.1144  -0.0933 359 ARG   B CB  
14891 C  CG  . ARG   B 359 ? 0.2109 0.1661 0.2585 -0.0302 0.1147  -0.0844 359 ARG   B CG  
14892 C  CD  . ARG   B 359 ? 0.2490 0.2060 0.2804 -0.0273 0.1162  -0.0843 359 ARG   B CD  
14893 N  NE  . ARG   B 359 ? 0.2217 0.1774 0.2628 -0.0232 0.1165  -0.0767 359 ARG   B NE  
14894 C  CZ  . ARG   B 359 ? 0.2856 0.2365 0.3182 -0.0229 0.1195  -0.0761 359 ARG   B CZ  
14895 N  NH1 . ARG   B 359 ? 0.2500 0.2022 0.2859 -0.0263 0.1225  -0.0827 359 ARG   B NH1 
14896 N  NH2 . ARG   B 359 ? 0.2696 0.2201 0.3143 -0.0194 0.1195  -0.0696 359 ARG   B NH2 
14910 N  N   . GLY   B 360 ? 0.2268 0.1842 0.2962 -0.0480 0.1187  -0.1090 360 GLY   B N   
14911 C  CA  . GLY   B 360 ? 0.2367 0.1979 0.3087 -0.0549 0.1193  -0.1203 360 GLY   B CA  
14912 C  C   . GLY   B 360 ? 0.2509 0.2218 0.3143 -0.0573 0.1158  -0.1307 360 GLY   B C   
14913 O  O   . GLY   B 360 ? 0.2574 0.2330 0.3224 -0.0636 0.1151  -0.1417 360 GLY   B O   
14917 N  N   . TYR   B 361 ? 0.2416 0.2202 0.2994 -0.0526 0.1095  -0.1221 361 TYR   B N   
14918 C  CA  . TYR   B 361 ? 0.2574 0.2495 0.3049 -0.0533 0.1005  -0.1232 361 TYR   B CA  
14919 C  C   . TYR   B 361 ? 0.2455 0.2442 0.3114 -0.0566 0.0989  -0.1240 361 TYR   B C   
14920 O  O   . TYR   B 361 ? 0.2596 0.2694 0.3224 -0.0605 0.0935  -0.1308 361 TYR   B O   
14921 C  CB  . TYR   B 361 ? 0.2348 0.2320 0.2751 -0.0467 0.0952  -0.1135 361 TYR   B CB  
14922 C  CG  . TYR   B 361 ? 0.2741 0.2667 0.2933 -0.0442 0.0962  -0.1129 361 TYR   B CG  
14923 C  CD1 . TYR   B 361 ? 0.2565 0.2394 0.2808 -0.0417 0.1027  -0.1089 361 TYR   B CD1 
14924 C  CD2 . TYR   B 361 ? 0.2594 0.2613 0.2696 -0.0446 0.0911  -0.1169 361 TYR   B CD2 
14925 C  CE1 . TYR   B 361 ? 0.2553 0.2359 0.2685 -0.0401 0.1047  -0.1089 361 TYR   B CE1 
14926 C  CE2 . TYR   B 361 ? 0.3052 0.3023 0.2957 -0.0427 0.0932  -0.1164 361 TYR   B CE2 
14927 C  CZ  . TYR   B 361 ? 0.2852 0.2730 0.2832 -0.0408 0.1006  -0.1125 361 TYR   B CZ  
14928 O  OH  . TYR   B 361 ? 0.3411 0.3249 0.3217 -0.0394 0.1036  -0.1120 361 TYR   B OH  
14938 N  N   . ILE   B 362 ? 0.2749 0.2651 0.3494 -0.0549 0.1035  -0.1169 362 ILE   B N   
14939 C  CA  . ILE   B 362 ? 0.2974 0.2908 0.3857 -0.0581 0.1043  -0.1161 362 ILE   B CA  
14940 C  C   . ILE   B 362 ? 0.3393 0.3209 0.4364 -0.0638 0.1129  -0.1222 362 ILE   B C   
14941 O  O   . ILE   B 362 ? 0.3309 0.3002 0.4355 -0.0609 0.1192  -0.1178 362 ILE   B O   
14942 C  CB  . ILE   B 362 ? 0.2656 0.2582 0.3544 -0.0518 0.1033  -0.1035 362 ILE   B CB  
14943 C  CG1 . ILE   B 362 ? 0.2332 0.2353 0.3130 -0.0460 0.0953  -0.0976 362 ILE   B CG1 
14944 C  CG2 . ILE   B 362 ? 0.2317 0.2277 0.3374 -0.0551 0.1054  -0.1028 362 ILE   B CG2 
14945 C  CD1 . ILE   B 362 ? 0.2317 0.2309 0.3091 -0.0396 0.0948  -0.0861 362 ILE   B CD1 
14957 N  N   . LYS   B 363 ? 0.2853 0.2742 0.4014 -0.0715 0.1133  -0.1317 363 LYS   B N   
14958 C  CA  . LYS   B 363 ? 0.3133 0.2900 0.4383 -0.0779 0.1218  -0.1388 363 LYS   B CA  
14959 C  C   . LYS   B 363 ? 0.3015 0.2727 0.4422 -0.0786 0.1274  -0.1314 363 LYS   B C   
14960 O  O   . LYS   B 363 ? 0.2795 0.2603 0.4211 -0.0766 0.1233  -0.1252 363 LYS   B O   
14961 C  CB  . LYS   B 363 ? 0.3468 0.3319 0.4748 -0.0867 0.1198  -0.1542 363 LYS   B CB  
14962 C  CG  . LYS   B 363 ? 0.3935 0.3835 0.5146 -0.0869 0.1160  -0.1633 363 LYS   B CG  
14963 C  CD  . LYS   B 363 ? 0.5811 0.5773 0.6893 -0.0955 0.1130  -0.1790 363 LYS   B CD  
14964 C  CE  . LYS   B 363 ? 0.6333 0.6350 0.7338 -0.0949 0.1094  -0.1868 363 LYS   B CE  
14965 N  NZ  . LYS   B 363 ? 0.7045 0.7168 0.8013 -0.1019 0.1048  -0.1994 363 LYS   B NZ  
14979 N  N   . ASP   B 364 ? 0.3419 0.2968 0.4912 -0.0812 0.1368  -0.1319 364 ASP   B N   
14980 C  CA  . ASP   B 364 ? 0.3763 0.3225 0.5345 -0.0821 0.1435  -0.1251 364 ASP   B CA  
14981 C  C   . ASP   B 364 ? 0.3139 0.2750 0.4899 -0.0893 0.1414  -0.1298 364 ASP   B C   
14982 O  O   . ASP   B 364 ? 0.2689 0.2305 0.4498 -0.0880 0.1437  -0.1213 364 ASP   B O   
14983 C  CB  . ASP   B 364 ? 0.3828 0.3162 0.5490 -0.0809 0.1516  -0.1232 364 ASP   B CB  
14984 C  CG  . ASP   B 364 ? 0.3649 0.2882 0.5271 -0.0731 0.1538  -0.1160 364 ASP   B CG  
14985 O  OD1 . ASP   B 364 ? 0.3475 0.2691 0.5026 -0.0670 0.1514  -0.1076 364 ASP   B OD1 
14986 O  OD2 . ASP   B 364 ? 0.3924 0.3091 0.5537 -0.0733 0.1577  -0.1186 364 ASP   B OD2 
14991 N  N   . GLU   B 365 ? 0.3627 0.3343 0.5383 -0.0965 0.1372  -0.1434 365 GLU   B N   
14992 C  CA  . GLU   B 365 ? 0.4105 0.3959 0.5913 -0.1034 0.1346  -0.1497 365 GLU   B CA  
14993 C  C   . GLU   B 365 ? 0.3395 0.3421 0.5220 -0.0993 0.1271  -0.1430 365 GLU   B C   
14994 O  O   . GLU   B 365 ? 0.2957 0.3082 0.4942 -0.1036 0.1281  -0.1430 365 GLU   B O   
14995 C  CB  . GLU   B 365 ? 0.4169 0.4149 0.6082 -0.1098 0.1298  -0.1649 365 GLU   B CB  
14996 C  CG  . GLU   B 365 ? 0.5368 0.5412 0.7083 -0.1075 0.1214  -0.1706 365 GLU   B CG  
14997 C  CD  . GLU   B 365 ? 0.6676 0.6854 0.8287 -0.1141 0.1142  -0.1857 365 GLU   B CD  
14998 O  OE1 . GLU   B 365 ? 0.7410 0.7768 0.9155 -0.1182 0.1087  -0.1899 365 GLU   B OE1 
14999 O  OE2 . GLU   B 365 ? 0.5537 0.5710 0.7188 -0.1138 0.1138  -0.1921 365 GLU   B OE2 
15006 N  N   . GLU   B 366 ? 0.2826 0.2904 0.4524 -0.0908 0.1200  -0.1369 366 GLU   B N   
15007 C  CA  . GLU   B 366 ? 0.2710 0.2951 0.4384 -0.0855 0.1121  -0.1304 366 GLU   B CA  
15008 C  C   . GLU   B 366 ? 0.3010 0.3170 0.4622 -0.0803 0.1168  -0.1172 366 GLU   B C   
15009 O  O   . GLU   B 366 ? 0.2735 0.3035 0.4428 -0.0779 0.1129  -0.1133 366 GLU   B O   
15010 C  CB  . GLU   B 366 ? 0.3439 0.3712 0.4848 -0.0784 0.1035  -0.1292 366 GLU   B CB  
15011 C  CG  . GLU   B 366 ? 0.3551 0.3848 0.4918 -0.0821 0.1005  -0.1401 366 GLU   B CG  
15012 C  CD  . GLU   B 366 ? 0.3973 0.4276 0.5036 -0.0752 0.0935  -0.1377 366 GLU   B CD  
15013 O  OE1 . GLU   B 366 ? 0.3446 0.3882 0.4571 -0.0698 0.0865  -0.1318 366 GLU   B OE1 
15014 O  OE2 . GLU   B 366 ? 0.2888 0.3138 0.4014 -0.0752 0.0958  -0.1413 366 GLU   B OE2 
15021 N  N   . ILE   B 367 ? 0.2666 0.2653 0.4331 -0.0780 0.1249  -0.1100 367 ILE   B N   
15022 C  CA  . ILE   B 367 ? 0.2494 0.2409 0.4146 -0.0720 0.1291  -0.0966 367 ILE   B CA  
15023 C  C   . ILE   B 367 ? 0.2448 0.2251 0.4267 -0.0772 0.1402  -0.0947 367 ILE   B C   
15024 O  O   . ILE   B 367 ? 0.2781 0.2503 0.4556 -0.0726 0.1446  -0.0838 367 ILE   B O   
15025 C  CB  . ILE   B 367 ? 0.2304 0.2127 0.3836 -0.0627 0.1275  -0.0878 367 ILE   B CB  
15026 C  CG1 . ILE   B 367 ? 0.2671 0.2329 0.4159 -0.0635 0.1329  -0.0897 367 ILE   B CG1 
15027 C  CG2 . ILE   B 367 ? 0.2223 0.2157 0.3609 -0.0577 0.1177  -0.0873 367 ILE   B CG2 
15028 C  CD1 . ILE   B 367 ? 0.2794 0.2339 0.4204 -0.0550 0.1340  -0.0802 367 ILE   B CD1 
15040 N  N   . ALA   B 368 ? 0.2557 0.2323 0.4465 -0.0863 0.1446  -0.1050 368 ALA   B N   
15041 C  CA  . ALA   B 368 ? 0.2646 0.2290 0.4650 -0.0875 0.1523  -0.1033 368 ALA   B CA  
15042 C  C   . ALA   B 368 ? 0.2797 0.2504 0.4836 -0.0877 0.1538  -0.0974 368 ALA   B C   
15043 O  O   . ALA   B 368 ? 0.2647 0.2236 0.4693 -0.0834 0.1598  -0.0871 368 ALA   B O   
15044 C  CB  . ALA   B 368 ? 0.2900 0.2530 0.4942 -0.0946 0.1539  -0.1156 368 ALA   B CB  
15050 N  N   . GLY   B 369 ? 0.2875 0.2779 0.4971 -0.0921 0.1482  -0.1036 369 GLY   B N   
15051 C  CA  . GLY   B 369 ? 0.2526 0.2528 0.4723 -0.0926 0.1492  -0.0994 369 GLY   B CA  
15052 C  C   . GLY   B 369 ? 0.2511 0.2485 0.4609 -0.0840 0.1501  -0.0857 369 GLY   B C   
15053 O  O   . GLY   B 369 ? 0.2814 0.2788 0.4938 -0.0833 0.1538  -0.0799 369 GLY   B O   
15057 N  N   . ASP   B 370 ? 0.2209 0.2141 0.4147 -0.0733 0.1419  -0.0793 370 ASP   B N   
15058 C  CA  . ASP   B 370 ? 0.2666 0.2591 0.4497 -0.0685 0.1466  -0.0678 370 ASP   B CA  
15059 C  C   . ASP   B 370 ? 0.2525 0.2252 0.4367 -0.0642 0.1539  -0.0576 370 ASP   B C   
15060 O  O   . ASP   B 370 ? 0.2874 0.2569 0.4609 -0.0576 0.1549  -0.0472 370 ASP   B O   
15061 C  CB  . ASP   B 370 ? 0.2429 0.2422 0.4193 -0.0619 0.1384  -0.0669 370 ASP   B CB  
15062 C  CG  . ASP   B 370 ? 0.2491 0.2686 0.4282 -0.0628 0.1285  -0.0747 370 ASP   B CG  
15063 O  OD1 . ASP   B 370 ? 0.3274 0.3573 0.4975 -0.0592 0.1248  -0.0717 370 ASP   B OD1 
15064 O  OD2 . ASP   B 370 ? 0.2787 0.2993 0.4511 -0.0668 0.1244  -0.0839 370 ASP   B OD2 
15069 N  N   . ASN   B 371 ? 0.2416 0.1997 0.4281 -0.0663 0.1576  -0.0601 371 ASN   B N   
15070 C  CA  . ASN   B 371 ? 0.2945 0.2332 0.4771 -0.0617 0.1653  -0.0506 371 ASN   B CA  
15071 C  C   . ASN   B 371 ? 0.3221 0.2538 0.4841 -0.0529 0.1627  -0.0417 371 ASN   B C   
15072 O  O   . ASN   B 371 ? 0.3121 0.2346 0.4740 -0.0468 0.1663  -0.0310 371 ASN   B O   
15073 C  CB  . ASN   B 371 ? 0.3726 0.3071 0.5560 -0.0620 0.1711  -0.0448 371 ASN   B CB  
15074 C  CG  . ASN   B 371 ? 0.4292 0.3680 0.6257 -0.0710 0.1744  -0.0536 371 ASN   B CG  
15075 O  OD1 . ASN   B 371 ? 0.4533 0.3813 0.6554 -0.0742 0.1792  -0.0576 371 ASN   B OD1 
15076 N  ND2 . ASN   B 371 ? 0.4302 0.3858 0.6347 -0.0749 0.1715  -0.0574 371 ASN   B ND2 
15083 N  N   . LEU   B 372 ? 0.2502 0.1918 0.4167 -0.0523 0.1567  -0.0457 372 LEU   B N   
15084 C  CA  . LEU   B 372 ? 0.2597 0.1970 0.4112 -0.0436 0.1530  -0.0390 372 LEU   B CA  
15085 C  C   . LEU   B 372 ? 0.2940 0.2268 0.4366 -0.0441 0.1494  -0.0457 372 LEU   B C   
15086 O  O   . LEU   B 372 ? 0.2792 0.2203 0.4332 -0.0508 0.1478  -0.0567 372 LEU   B O   
15087 C  CB  . LEU   B 372 ? 0.2547 0.2057 0.3971 -0.0386 0.1451  -0.0359 372 LEU   B CB  
15088 C  CG  . LEU   B 372 ? 0.2602 0.2163 0.4024 -0.0374 0.1480  -0.0294 372 LEU   B CG  
15089 C  CD1 . LEU   B 372 ? 0.2364 0.2061 0.3721 -0.0321 0.1398  -0.0284 372 LEU   B CD1 
15090 C  CD2 . LEU   B 372 ? 0.2894 0.2305 0.4262 -0.0324 0.1545  -0.0184 372 LEU   B CD2 
15102 N  N   . SER   B 373 ? 0.2346 0.1605 0.3767 -0.0369 0.1479  -0.0405 373 SER   B N   
15103 C  CA  . SER   B 373 ? 0.2319 0.1551 0.3681 -0.0364 0.1449  -0.0461 373 SER   B CA  
15104 C  C   . SER   B 373 ? 0.2121 0.1460 0.3386 -0.0316 0.1357  -0.0458 373 SER   B C   
15105 O  O   . SER   B 373 ? 0.2198 0.1600 0.3383 -0.0275 0.1317  -0.0399 373 SER   B O   
15106 C  CB  . SER   B 373 ? 0.2584 0.1652 0.3921 -0.0322 0.1498  -0.0416 373 SER   B CB  
15107 O  OG  . SER   B 373 ? 0.2295 0.1368 0.3586 -0.0234 0.1451  -0.0339 373 SER   B OG  
15113 N  N   . LEU   B 374 ? 0.2261 0.1598 0.3448 -0.0317 0.1328  -0.0517 374 LEU   B N   
15114 C  CA  . LEU   B 374 ? 0.2067 0.1484 0.3185 -0.0271 0.1254  -0.0509 374 LEU   B CA  
15115 C  C   . LEU   B 374 ? 0.2306 0.1612 0.3337 -0.0225 0.1271  -0.0483 374 LEU   B C   
15116 O  O   . LEU   B 374 ? 0.1858 0.1213 0.2900 -0.0217 0.1237  -0.0517 374 LEU   B O   
15117 C  CB  . LEU   B 374 ? 0.2039 0.1565 0.3108 -0.0317 0.1206  -0.0599 374 LEU   B CB  
15118 C  CG  . LEU   B 374 ? 0.2103 0.1769 0.3189 -0.0332 0.1156  -0.0609 374 LEU   B CG  
15119 C  CD1 . LEU   B 374 ? 0.2629 0.2391 0.3622 -0.0370 0.1104  -0.0697 374 LEU   B CD1 
15120 C  CD2 . LEU   B 374 ? 0.2348 0.2034 0.3321 -0.0262 0.1113  -0.0519 374 LEU   B CD2 
15132 N  N   . LYS   B 375 ? 0.2023 0.1229 0.3160 -0.0193 0.1323  -0.0421 375 LYS   B N   
15133 C  CA  . LYS   B 375 ? 0.1967 0.1116 0.3106 -0.0156 0.1314  -0.0374 375 LYS   B CA  
15134 C  C   . LYS   B 375 ? 0.2125 0.1249 0.3186 -0.0064 0.1294  -0.0304 375 LYS   B C   
15135 O  O   . LYS   B 375 ? 0.2011 0.1135 0.3063 -0.0034 0.1287  -0.0232 375 LYS   B O   
15136 C  CB  . LYS   B 375 ? 0.2209 0.1197 0.3453 -0.0153 0.1419  -0.0384 375 LYS   B CB  
15137 C  CG  . LYS   B 375 ? 0.2751 0.1713 0.4061 -0.0232 0.1470  -0.0477 375 LYS   B CG  
15138 C  CD  . LYS   B 375 ? 0.3353 0.2230 0.4766 -0.0242 0.1537  -0.0451 375 LYS   B CD  
15139 C  CE  . LYS   B 375 ? 0.4447 0.3314 0.5884 -0.0319 0.1578  -0.0552 375 LYS   B CE  
15140 N  NZ  . LYS   B 375 ? 0.5079 0.4030 0.6505 -0.0391 0.1553  -0.0653 375 LYS   B NZ  
15154 N  N   . TRP   B 376 ? 0.2255 0.1399 0.3293 -0.0030 0.1264  -0.0310 376 TRP   B N   
15155 C  CA  . TRP   B 376 ? 0.2365 0.1520 0.3345 0.0041  0.1216  -0.0236 376 TRP   B CA  
15156 C  C   . TRP   B 376 ? 0.2338 0.1410 0.3334 0.0093  0.1240  -0.0149 376 TRP   B C   
15157 O  O   . TRP   B 376 ? 0.2200 0.1207 0.3288 0.0083  0.1285  -0.0145 376 TRP   B O   
15158 C  CB  . TRP   B 376 ? 0.2201 0.1392 0.3193 0.0051  0.1187  -0.0256 376 TRP   B CB  
15159 C  CG  . TRP   B 376 ? 0.2214 0.1469 0.3171 0.0005  0.1172  -0.0334 376 TRP   B CG  
15160 C  CD1 . TRP   B 376 ? 0.2588 0.1824 0.3511 -0.0040 0.1198  -0.0399 376 TRP   B CD1 
15161 C  CD2 . TRP   B 376 ? 0.2093 0.1424 0.2953 0.0000  0.1130  -0.0347 376 TRP   B CD2 
15162 N  NE1 . TRP   B 376 ? 0.2097 0.1412 0.3014 -0.0070 0.1175  -0.0451 376 TRP   B NE1 
15163 C  CE2 . TRP   B 376 ? 0.2039 0.1403 0.2878 -0.0045 0.1134  -0.0421 376 TRP   B CE2 
15164 C  CE3 . TRP   B 376 ? 0.1972 0.1353 0.2767 0.0029  0.1074  -0.0299 376 TRP   B CE3 
15165 C  CZ2 . TRP   B 376 ? 0.2074 0.1506 0.2806 -0.0056 0.1095  -0.0439 376 TRP   B CZ2 
15166 C  CZ3 . TRP   B 376 ? 0.1865 0.1316 0.2588 0.0011  0.1031  -0.0319 376 TRP   B CZ3 
15167 C  CH2 . TRP   B 376 ? 0.1908 0.1383 0.2603 -0.0029 0.1042  -0.0384 376 TRP   B CH2 
15178 N  N   . GLY   B 377 ? 0.1980 0.1088 0.2987 0.0145  0.1199  -0.0076 377 GLY   B N   
15179 C  CA  . GLY   B 377 ? 0.2605 0.1617 0.3521 0.0206  0.1216  0.0012  377 GLY   B CA  
15180 C  C   . GLY   B 377 ? 0.2308 0.1272 0.3269 0.0181  0.1273  0.0047  377 GLY   B C   
15181 O  O   . GLY   B 377 ? 0.2155 0.1069 0.3101 0.0229  0.1278  0.0133  377 GLY   B O   
15185 N  N   . ASP   B 378 ? 0.2025 0.1034 0.3043 0.0103  0.1295  -0.0012 378 ASP   B N   
15186 C  CA  . ASP   B 378 ? 0.2294 0.1250 0.3297 0.0070  0.1357  0.0008  378 ASP   B CA  
15187 C  C   . ASP   B 378 ? 0.2202 0.1237 0.3136 0.0096  0.1318  0.0059  378 ASP   B C   
15188 O  O   . ASP   B 378 ? 0.2031 0.1156 0.2969 0.0047  0.1307  0.0015  378 ASP   B O   
15189 C  CB  . ASP   B 378 ? 0.2335 0.1306 0.3448 -0.0021 0.1404  -0.0082 378 ASP   B CB  
15190 C  CG  . ASP   B 378 ? 0.2584 0.1500 0.3734 -0.0064 0.1478  -0.0060 378 ASP   B CG  
15191 O  OD1 . ASP   B 378 ? 0.2694 0.1571 0.3806 -0.0018 0.1494  0.0030  378 ASP   B OD1 
15192 O  OD2 . ASP   B 378 ? 0.2513 0.1434 0.3760 -0.0143 0.1518  -0.0136 378 ASP   B OD2 
15197 N  N   . THR   B 379 ? 0.2357 0.1356 0.3187 0.0173  0.1294  0.0146  379 THR   B N   
15198 C  CA  . THR   B 379 ? 0.2035 0.1118 0.2858 0.0205  0.1259  0.0193  379 THR   B CA  
15199 C  C   . THR   B 379 ? 0.2333 0.1419 0.3094 0.0155  0.1313  0.0190  379 THR   B C   
15200 O  O   . THR   B 379 ? 0.2240 0.1434 0.2988 0.0141  0.1279  0.0164  379 THR   B O   
15201 C  CB  . THR   B 379 ? 0.2800 0.1801 0.3423 0.0293  0.1240  0.0285  379 THR   B CB  
15202 O  OG1 . THR   B 379 ? 0.2647 0.1652 0.3340 0.0332  0.1192  0.0278  379 THR   B OG1 
15203 C  CG2 . THR   B 379 ? 0.2709 0.1782 0.3275 0.0332  0.1195  0.0323  379 THR   B CG2 
15211 N  N   . GLU   B 380 ? 0.2446 0.1442 0.3279 0.0129  0.1398  0.0218  380 GLU   B N   
15212 C  CA  . GLU   B 380 ? 0.2448 0.1470 0.3368 0.0075  0.1465  0.0219  380 GLU   B CA  
15213 C  C   . GLU   B 380 ? 0.2344 0.1484 0.3292 0.0000  0.1443  0.0117  380 GLU   B C   
15214 O  O   . GLU   B 380 ? 0.2486 0.1717 0.3420 -0.0015 0.1441  0.0112  380 GLU   B O   
15215 C  CB  . GLU   B 380 ? 0.3290 0.2167 0.4238 0.0048  0.1568  0.0258  380 GLU   B CB  
15216 C  CG  . GLU   B 380 ? 0.4023 0.2910 0.5041 -0.0012 0.1649  0.0267  380 GLU   B CG  
15217 C  CD  . GLU   B 380 ? 0.4892 0.3626 0.5877 -0.0018 0.1728  0.0305  380 GLU   B CD  
15218 O  OE1 . GLU   B 380 ? 0.4265 0.2912 0.5308 0.0046  0.1736  0.0370  380 GLU   B OE1 
15219 O  OE2 . GLU   B 380 ? 0.4874 0.3641 0.6011 -0.0082 0.1771  0.0263  380 GLU   B OE2 
15226 N  N   . SER   B 381 ? 0.2071 0.1228 0.3124 -0.0042 0.1427  0.0034  381 SER   B N   
15227 C  CA  . SER   B 381 ? 0.2573 0.1829 0.3592 -0.0111 0.1397  -0.0067 381 SER   B CA  
15228 C  C   . SER   B 381 ? 0.2226 0.1613 0.3206 -0.0074 0.1307  -0.0077 381 SER   B C   
15229 O  O   . SER   B 381 ? 0.1944 0.1447 0.2958 -0.0102 0.1288  -0.0113 381 SER   B O   
15230 C  CB  . SER   B 381 ? 0.2399 0.1635 0.3556 -0.0159 0.1407  -0.0148 381 SER   B CB  
15231 O  OG  . SER   B 381 ? 0.2471 0.1602 0.3707 -0.0208 0.1494  -0.0158 381 SER   B OG  
15237 N  N   . MET   B 382 ? 0.2097 0.1465 0.3005 -0.0011 0.1254  -0.0046 382 MET   B N   
15238 C  CA  . MET   B 382 ? 0.2256 0.1701 0.3019 0.0027  0.1172  -0.0047 382 MET   B CA  
15239 C  C   . MET   B 382 ? 0.1839 0.1369 0.2682 0.0047  0.1173  -0.0011 382 MET   B C   
15240 O  O   . MET   B 382 ? 0.2429 0.2041 0.3161 0.0035  0.1134  -0.0047 382 MET   B O   
15241 C  CB  . MET   B 382 ? 0.1991 0.1399 0.2727 0.0091  0.1130  -0.0007 382 MET   B CB  
15242 C  CG  . MET   B 382 ? 0.1883 0.1360 0.2540 0.0129  0.1053  -0.0005 382 MET   B CG  
15243 S  SD  . MET   B 382 ? 0.2088 0.1509 0.2658 0.0201  0.1011  0.0045  382 MET   B SD  
15244 C  CE  . MET   B 382 ? 0.2217 0.1581 0.2738 0.0252  0.1042  0.0132  382 MET   B CE  
15254 N  N   . ILE   B 383 ? 0.2403 0.1840 0.3102 0.0080  0.1218  0.0065  383 ILE   B N   
15255 C  CA  . ILE   B 383 ? 0.2167 0.1667 0.2898 0.0105  0.1234  0.0106  383 ILE   B CA  
15256 C  C   . ILE   B 383 ? 0.2285 0.1859 0.3059 0.0036  0.1272  0.0055  383 ILE   B C   
15257 O  O   . ILE   B 383 ? 0.2084 0.1769 0.2882 0.0047  0.1248  0.0038  383 ILE   B O   
15258 C  CB  . ILE   B 383 ? 0.2489 0.1890 0.3144 0.0151  0.1284  0.0198  383 ILE   B CB  
15259 C  CG1 . ILE   B 383 ? 0.2753 0.2098 0.3309 0.0225  0.1229  0.0242  383 ILE   B CG1 
15260 C  CG2 . ILE   B 383 ? 0.3054 0.2490 0.3631 0.0163  0.1321  0.0232  383 ILE   B CG2 
15261 C  CD1 . ILE   B 383 ? 0.3573 0.2967 0.3962 0.0276  0.1160  0.0246  383 ILE   B CD1 
15273 N  N   . GLY   B 384 ? 0.2055 0.1600 0.2979 -0.0028 0.1333  0.0025  384 GLY   B N   
15274 C  CA  . GLY   B 384 ? 0.2082 0.1707 0.3096 -0.0102 0.1374  -0.0030 384 GLY   B CA  
15275 C  C   . GLY   B 384 ? 0.1787 0.1565 0.2887 -0.0124 0.1285  -0.0112 384 GLY   B C   
15276 O  O   . GLY   B 384 ? 0.2236 0.2118 0.3351 -0.0158 0.1314  -0.0146 384 GLY   B O   
15280 N  N   . TRP   B 385 ? 0.2090 0.1859 0.3070 -0.0110 0.1231  -0.0149 385 TRP   B N   
15281 C  CA  . TRP   B 385 ? 0.1749 0.1656 0.2785 -0.0131 0.1161  -0.0222 385 TRP   B CA  
15282 C  C   . TRP   B 385 ? 0.1715 0.1721 0.2705 -0.0077 0.1114  -0.0203 385 TRP   B C   
15283 O  O   . TRP   B 385 ? 0.1955 0.2075 0.2943 -0.0093 0.1071  -0.0253 385 TRP   B O   
15284 C  CB  . TRP   B 385 ? 0.1889 0.1750 0.2841 -0.0124 0.1113  -0.0259 385 TRP   B CB  
15285 C  CG  . TRP   B 385 ? 0.1669 0.1487 0.2757 -0.0189 0.1150  -0.0316 385 TRP   B CG  
15286 C  CD1 . TRP   B 385 ? 0.2061 0.1744 0.3077 -0.0184 0.1179  -0.0304 385 TRP   B CD1 
15287 C  CD2 . TRP   B 385 ? 0.2038 0.1920 0.3194 -0.0267 0.1164  -0.0405 385 TRP   B CD2 
15288 N  NE1 . TRP   B 385 ? 0.2106 0.1772 0.3230 -0.0250 0.1214  -0.0374 385 TRP   B NE1 
15289 C  CE2 . TRP   B 385 ? 0.2350 0.2120 0.3496 -0.0308 0.1204  -0.0442 385 TRP   B CE2 
15290 C  CE3 . TRP   B 385 ? 0.2280 0.2300 0.3491 -0.0308 0.1143  -0.0461 385 TRP   B CE3 
15291 C  CZ2 . TRP   B 385 ? 0.2070 0.1887 0.3378 -0.0389 0.1227  -0.0537 385 TRP   B CZ2 
15292 C  CZ3 . TRP   B 385 ? 0.2255 0.2321 0.3579 -0.0389 0.1160  -0.0552 385 TRP   B CZ3 
15293 C  CH2 . TRP   B 385 ? 0.2240 0.2197 0.3584 -0.0432 0.1201  -0.0591 385 TRP   B CH2 
15304 N  N   . ILE   B 386 ? 0.2000 0.1936 0.2834 -0.0011 0.1113  -0.0130 386 ILE   B N   
15305 C  CA  . ILE   B 386 ? 0.1552 0.1574 0.2387 0.0047  0.1070  -0.0108 386 ILE   B CA  
15306 C  C   . ILE   B 386 ? 0.1720 0.1866 0.2625 0.0021  0.1092  -0.0137 386 ILE   B C   
15307 O  O   . ILE   B 386 ? 0.1605 0.1859 0.2523 0.0029  0.1034  -0.0180 386 ILE   B O   
15308 C  CB  . ILE   B 386 ? 0.1631 0.1568 0.2351 0.0113  0.1080  -0.0033 386 ILE   B CB  
15309 C  CG1 . ILE   B 386 ? 0.2115 0.1938 0.2703 0.0140  0.1046  -0.0011 386 ILE   B CG1 
15310 C  CG2 . ILE   B 386 ? 0.1918 0.1909 0.2533 0.0170  0.1047  -0.0021 386 ILE   B CG2 
15311 C  CD1 . ILE   B 386 ? 0.2188 0.1939 0.2695 0.0202  0.1047  0.0055  386 ILE   B CD1 
15323 N  N   . LYS   B 387 ? 0.2148 0.2278 0.3098 -0.0007 0.1176  -0.0116 387 LYS   B N   
15324 C  CA  . LYS   B 387 ? 0.2053 0.2324 0.3169 -0.0035 0.1211  -0.0141 387 LYS   B CA  
15325 C  C   . LYS   B 387 ? 0.1756 0.2147 0.2994 -0.0099 0.1174  -0.0232 387 LYS   B C   
15326 O  O   . LYS   B 387 ? 0.1707 0.2238 0.2979 -0.0091 0.1142  -0.0267 387 LYS   B O   
15327 C  CB  . LYS   B 387 ? 0.2734 0.2946 0.3856 -0.0066 0.1320  -0.0100 387 LYS   B CB  
15328 C  CG  . LYS   B 387 ? 0.2742 0.3093 0.4038 -0.0104 0.1357  -0.0123 387 LYS   B CG  
15329 C  CD  . LYS   B 387 ? 0.3189 0.3466 0.4541 -0.0141 0.1439  -0.0082 387 LYS   B CD  
15330 C  CE  . LYS   B 387 ? 0.4416 0.4808 0.5879 -0.0203 0.1471  -0.0123 387 LYS   B CE  
15331 N  NZ  . LYS   B 387 ? 0.5689 0.5990 0.7103 -0.0224 0.1555  -0.0071 387 LYS   B NZ  
15345 N  N   . ARG   B 388 ? 0.2117 0.2439 0.3343 -0.0156 0.1178  -0.0271 388 ARG   B N   
15346 C  CA  . ARG   B 388 ? 0.1984 0.2420 0.3346 -0.0223 0.1146  -0.0367 388 ARG   B CA  
15347 C  C   . ARG   B 388 ? 0.1861 0.2391 0.3146 -0.0182 0.1039  -0.0401 388 ARG   B C   
15348 O  O   . ARG   B 388 ? 0.1862 0.2541 0.3232 -0.0209 0.0997  -0.0465 388 ARG   B O   
15349 C  CB  . ARG   B 388 ? 0.2215 0.2542 0.3612 -0.0287 0.1182  -0.0399 388 ARG   B CB  
15350 C  CG  . ARG   B 388 ? 0.2606 0.2810 0.4062 -0.0319 0.1288  -0.0358 388 ARG   B CG  
15351 C  CD  . ARG   B 388 ? 0.3236 0.3355 0.4728 -0.0398 0.1330  -0.0413 388 ARG   B CD  
15352 N  NE  . ARG   B 388 ? 0.3008 0.3273 0.4701 -0.0479 0.1317  -0.0516 388 ARG   B NE  
15353 C  CZ  . ARG   B 388 ? 0.3260 0.3578 0.5071 -0.0545 0.1375  -0.0547 388 ARG   B CZ  
15354 N  NH1 . ARG   B 388 ? 0.3260 0.3514 0.5067 -0.0521 0.1429  -0.0466 388 ARG   B NH1 
15355 N  NH2 . ARG   B 388 ? 0.3342 0.3777 0.5285 -0.0624 0.1356  -0.0653 388 ARG   B NH2 
15369 N  N   . MET   B 389 ? 0.1678 0.2127 0.2825 -0.0119 0.0992  -0.0360 389 MET   B N   
15370 C  CA  . MET   B 389 ? 0.1640 0.2161 0.2723 -0.0073 0.0900  -0.0375 389 MET   B CA  
15371 C  C   . MET   B 389 ? 0.1792 0.2419 0.2854 -0.0021 0.0877  -0.0360 389 MET   B C   
15372 O  O   . MET   B 389 ? 0.1661 0.2423 0.2778 -0.0015 0.0818  -0.0402 389 MET   B O   
15373 C  CB  . MET   B 389 ? 0.2064 0.2448 0.2959 -0.0023 0.0870  -0.0331 389 MET   B CB  
15374 C  CG  . MET   B 389 ? 0.2186 0.2464 0.3084 -0.0063 0.0895  -0.0341 389 MET   B CG  
15375 S  SD  . MET   B 389 ? 0.2652 0.2766 0.3359 -0.0004 0.0890  -0.0275 389 MET   B SD  
15376 C  CE  . MET   B 389 ? 0.2121 0.2294 0.2796 0.0053  0.0806  -0.0266 389 MET   B CE  
15386 N  N   . VAL   B 390 ? 0.1780 0.2363 0.2819 0.0018  0.0926  -0.0299 390 VAL   B N   
15387 C  CA  . VAL   B 390 ? 0.1423 0.2110 0.2526 0.0076  0.0916  -0.0281 390 VAL   B CA  
15388 C  C   . VAL   B 390 ? 0.1708 0.2554 0.2906 0.0034  0.0927  -0.0338 390 VAL   B C   
15389 O  O   . VAL   B 390 ? 0.1445 0.2428 0.2720 0.0076  0.0872  -0.0358 390 VAL   B O   
15390 C  CB  . VAL   B 390 ? 0.1447 0.2041 0.2450 0.0117  0.0980  -0.0213 390 VAL   B CB  
15391 C  CG1 . VAL   B 390 ? 0.1453 0.2153 0.2502 0.0162  0.0994  -0.0206 390 VAL   B CG1 
15392 C  CG2 . VAL   B 390 ? 0.1446 0.1897 0.2298 0.0168  0.0953  -0.0166 390 VAL   B CG2 
15402 N  N   . TYR   B 391 ? 0.1453 0.2326 0.2839 -0.0046 0.0994  -0.0365 391 TYR   B N   
15403 C  CA  . TYR   B 391 ? 0.1638 0.2672 0.3176 -0.0099 0.1016  -0.0423 391 TYR   B CA  
15404 C  C   . TYR   B 391 ? 0.1692 0.2808 0.3305 -0.0167 0.0963  -0.0512 391 TYR   B C   
15405 O  O   . TYR   B 391 ? 0.1478 0.2741 0.3283 -0.0227 0.0978  -0.0574 391 TYR   B O   
15406 C  CB  . TYR   B 391 ? 0.1549 0.2549 0.3191 -0.0144 0.1128  -0.0392 391 TYR   B CB  
15407 C  CG  . TYR   B 391 ? 0.1763 0.2739 0.3353 -0.0077 0.1187  -0.0321 391 TYR   B CG  
15408 C  CD1 . TYR   B 391 ? 0.1990 0.3116 0.3652 -0.0044 0.1193  -0.0331 391 TYR   B CD1 
15409 C  CD2 . TYR   B 391 ? 0.1897 0.2692 0.3319 -0.0041 0.1227  -0.0244 391 TYR   B CD2 
15410 C  CE1 . TYR   B 391 ? 0.2197 0.3284 0.3759 0.0020  0.1237  -0.0270 391 TYR   B CE1 
15411 C  CE2 . TYR   B 391 ? 0.1684 0.2439 0.3029 0.0022  0.1233  -0.0180 391 TYR   B CE2 
15412 C  CZ  . TYR   B 391 ? 0.1759 0.2670 0.3194 0.0051  0.1267  -0.0196 391 TYR   B CZ  
15413 O  OH  . TYR   B 391 ? 0.1688 0.2528 0.2952 0.0107  0.1225  -0.0135 391 TYR   B OH  
15423 N  N   . SER   B 392 ? 0.1646 0.2688 0.3175 -0.0160 0.0902  -0.0524 392 SER   B N   
15424 C  CA  . SER   B 392 ? 0.1863 0.2977 0.3421 -0.0217 0.0847  -0.0611 392 SER   B CA  
15425 C  C   . SER   B 392 ? 0.2308 0.3415 0.3958 -0.0323 0.0917  -0.0670 392 SER   B C   
15426 O  O   . SER   B 392 ? 0.2077 0.3356 0.3925 -0.0376 0.0886  -0.0753 392 SER   B O   
15427 C  CB  . SER   B 392 ? 0.1618 0.2924 0.3230 -0.0180 0.0752  -0.0649 392 SER   B CB  
15428 O  OG  . SER   B 392 ? 0.2196 0.3450 0.3596 -0.0091 0.0687  -0.0600 392 SER   B OG  
15434 N  N   . GLU   B 393 ? 0.1752 0.2720 0.3508 -0.0351 0.1009  -0.0629 393 GLU   B N   
15435 C  CA  . GLU   B 393 ? 0.2158 0.3079 0.3986 -0.0452 0.1092  -0.0672 393 GLU   B CA  
15436 C  C   . GLU   B 393 ? 0.2311 0.3120 0.4073 -0.0498 0.1081  -0.0722 393 GLU   B C   
15437 O  O   . GLU   B 393 ? 0.1988 0.2654 0.3665 -0.0454 0.1084  -0.0667 393 GLU   B O   
15438 C  CB  . GLU   B 393 ? 0.2196 0.2999 0.4048 -0.0452 0.1204  -0.0592 393 GLU   B CB  
15439 C  CG  . GLU   B 393 ? 0.1952 0.2862 0.3918 -0.0404 0.1229  -0.0538 393 GLU   B CG  
15440 C  CD  . GLU   B 393 ? 0.3288 0.4024 0.5061 -0.0381 0.1319  -0.0441 393 GLU   B CD  
15441 O  OE1 . GLU   B 393 ? 0.3457 0.4034 0.5172 -0.0353 0.1340  -0.0384 393 GLU   B OE1 
15442 O  OE2 . GLU   B 393 ? 0.3086 0.3896 0.4996 -0.0385 0.1356  -0.0420 393 GLU   B OE2 
15449 N  N   . GLY   B 394 ? 0.2028 0.2928 0.3960 -0.0583 0.1070  -0.0828 394 GLY   B N   
15450 C  CA  . GLY   B 394 ? 0.2246 0.3037 0.4093 -0.0632 0.1068  -0.0888 394 GLY   B CA  
15451 C  C   . GLY   B 394 ? 0.1966 0.2733 0.3701 -0.0567 0.0988  -0.0878 394 GLY   B C   
15452 O  O   . GLY   B 394 ? 0.2126 0.3009 0.3753 -0.0520 0.0900  -0.0884 394 GLY   B O   
15456 N  N   . PHE   B 395 ? 0.2419 0.2995 0.3974 -0.0563 0.1019  -0.0858 395 PHE   B N   
15457 C  CA  . PHE   B 395 ? 0.1984 0.2528 0.3441 -0.0511 0.0958  -0.0847 395 PHE   B CA  
15458 C  C   . PHE   B 395 ? 0.2047 0.2585 0.3329 -0.0413 0.0914  -0.0753 395 PHE   B C   
15459 O  O   . PHE   B 395 ? 0.1830 0.2391 0.3029 -0.0366 0.0849  -0.0745 395 PHE   B O   
15460 C  CB  . PHE   B 395 ? 0.2041 0.2395 0.3418 -0.0524 0.1013  -0.0843 395 PHE   B CB  
15461 C  CG  . PHE   B 395 ? 0.2068 0.2375 0.3332 -0.0468 0.0968  -0.0819 395 PHE   B CG  
15462 C  CD1 . PHE   B 395 ? 0.2717 0.3075 0.3825 -0.0481 0.0905  -0.0890 395 PHE   B CD1 
15463 C  CD2 . PHE   B 395 ? 0.2322 0.2500 0.3445 -0.0402 0.0987  -0.0725 395 PHE   B CD2 
15464 C  CE1 . PHE   B 395 ? 0.2599 0.2914 0.3618 -0.0433 0.0873  -0.0866 395 PHE   B CE1 
15465 C  CE2 . PHE   B 395 ? 0.2396 0.2535 0.3416 -0.0358 0.0950  -0.0706 395 PHE   B CE2 
15466 C  CZ  . PHE   B 395 ? 0.2813 0.3003 0.3723 -0.0374 0.0898  -0.0775 395 PHE   B CZ  
15476 N  N   . GLY   B 396 ? 0.1628 0.2159 0.3017 -0.0384 0.0961  -0.0676 396 GLY   B N   
15477 C  CA  . GLY   B 396 ? 0.2124 0.2633 0.3335 -0.0295 0.0929  -0.0593 396 GLY   B CA  
15478 C  C   . GLY   B 396 ? 0.1842 0.2507 0.3064 -0.0254 0.0837  -0.0612 396 GLY   B C   
15479 O  O   . GLY   B 396 ? 0.1826 0.2461 0.2914 -0.0185 0.0793  -0.0560 396 GLY   B O   
15483 N  N   . ALA   B 397 ? 0.1875 0.2694 0.3194 -0.0302 0.0806  -0.0690 397 ALA   B N   
15484 C  CA  . ALA   B 397 ? 0.2109 0.3077 0.3376 -0.0260 0.0713  -0.0716 397 ALA   B CA  
15485 C  C   . ALA   B 397 ? 0.2043 0.2971 0.3166 -0.0224 0.0646  -0.0713 397 ALA   B C   
15486 O  O   . ALA   B 397 ? 0.1885 0.2873 0.2935 -0.0156 0.0576  -0.0687 397 ALA   B O   
15487 C  CB  . ALA   B 397 ? 0.1931 0.3083 0.3377 -0.0323 0.0691  -0.0805 397 ALA   B CB  
15493 N  N   . LYS   B 398 ? 0.2177 0.2994 0.3224 -0.0267 0.0669  -0.0743 398 LYS   B N   
15494 C  CA  . LYS   B 398 ? 0.1943 0.2722 0.2887 -0.0242 0.0621  -0.0748 398 LYS   B CA  
15495 C  C   . LYS   B 398 ? 0.2340 0.2967 0.3062 -0.0172 0.0628  -0.0652 398 LYS   B C   
15496 O  O   . LYS   B 398 ? 0.1918 0.2541 0.2597 -0.0137 0.0584  -0.0637 398 LYS   B O   
15497 C  CB  . LYS   B 398 ? 0.1967 0.2689 0.2908 -0.0315 0.0650  -0.0827 398 LYS   B CB  
15498 C  CG  . LYS   B 398 ? 0.2420 0.3269 0.3417 -0.0385 0.0622  -0.0937 398 LYS   B CG  
15499 C  CD  . LYS   B 398 ? 0.2693 0.3493 0.3688 -0.0446 0.0639  -0.1023 398 LYS   B CD  
15500 C  CE  . LYS   B 398 ? 0.3173 0.4117 0.4203 -0.0508 0.0588  -0.1141 398 LYS   B CE  
15501 N  NZ  . LYS   B 398 ? 0.3600 0.4487 0.4540 -0.0551 0.0592  -0.1223 398 LYS   B NZ  
15515 N  N   . MET   B 399 ? 0.1846 0.2413 0.2675 -0.0152 0.0685  -0.0591 399 MET   B N   
15516 C  CA  . MET   B 399 ? 0.1578 0.2033 0.2360 -0.0094 0.0696  -0.0507 399 MET   B CA  
15517 C  C   . MET   B 399 ? 0.2093 0.2568 0.2730 -0.0024 0.0663  -0.0452 399 MET   B C   
15518 O  O   . MET   B 399 ? 0.1514 0.1932 0.2149 0.0028  0.0653  -0.0396 399 MET   B O   
15519 C  CB  . MET   B 399 ? 0.1915 0.2235 0.2676 -0.0113 0.0774  -0.0480 399 MET   B CB  
15520 C  CG  . MET   B 399 ? 0.2212 0.2444 0.2980 -0.0159 0.0809  -0.0515 399 MET   B CG  
15521 S  SD  . MET   B 399 ? 0.2558 0.2623 0.3305 -0.0151 0.0886  -0.0460 399 MET   B SD  
15522 C  CE  . MET   B 399 ? 0.1996 0.2098 0.2952 -0.0203 0.0951  -0.0470 399 MET   B CE  
15532 N  N   . THR   B 400 ? 0.1930 0.2551 0.2714 -0.0027 0.0650  -0.0474 400 THR   B N   
15533 C  CA  . THR   B 400 ? 0.1648 0.2328 0.2464 0.0040  0.0631  -0.0430 400 THR   B CA  
15534 C  C   . THR   B 400 ? 0.1854 0.2491 0.2470 0.0112  0.0568  -0.0391 400 THR   B C   
15535 O  O   . THR   B 400 ? 0.1592 0.2195 0.2221 0.0169  0.0572  -0.0337 400 THR   B O   
15536 C  CB  . THR   B 400 ? 0.1641 0.2488 0.2581 0.0024  0.0622  -0.0472 400 THR   B CB  
15537 O  OG1 . THR   B 400 ? 0.1594 0.2448 0.2651 -0.0049 0.0690  -0.0505 400 THR   B OG1 
15538 C  CG2 . THR   B 400 ? 0.1841 0.2745 0.2779 0.0093  0.0612  -0.0431 400 THR   B CG2 
15546 N  N   . ASN   B 401 ? 0.1472 0.2144 0.2087 0.0108  0.0514  -0.0416 401 ASN   B N   
15547 C  CA  . ASN   B 401 ? 0.1814 0.2444 0.2227 0.0177  0.0455  -0.0378 401 ASN   B CA  
15548 C  C   . ASN   B 401 ? 0.1519 0.2021 0.1879 0.0178  0.0463  -0.0348 401 ASN   B C   
15549 O  O   . ASN   B 401 ? 0.1604 0.2072 0.1820 0.0216  0.0421  -0.0324 401 ASN   B O   
15550 C  CB  . ASN   B 401 ? 0.1601 0.2379 0.2064 0.0197  0.0382  -0.0410 401 ASN   B CB  
15551 C  CG  . ASN   B 401 ? 0.1538 0.2483 0.2176 0.0216  0.0365  -0.0429 401 ASN   B CG  
15552 O  OD1 . ASN   B 401 ? 0.1486 0.2408 0.2122 0.0245  0.0400  -0.0395 401 ASN   B OD1 
15553 N  ND2 . ASN   B 401 ? 0.2719 0.3789 0.3296 0.0201  0.0311  -0.0484 401 ASN   B ND2 
15560 N  N   . GLY   B 402 ? 0.1792 0.2190 0.2114 0.0134  0.0522  -0.0349 402 GLY   B N   
15561 C  CA  . GLY   B 402 ? 0.1675 0.1951 0.1925 0.0137  0.0534  -0.0322 402 GLY   B CA  
15562 C  C   . GLY   B 402 ? 0.1546 0.1800 0.1790 0.0085  0.0548  -0.0364 402 GLY   B C   
15563 O  O   . GLY   B 402 ? 0.1941 0.2270 0.2162 0.0051  0.0531  -0.0420 402 GLY   B O   
15567 N  N   . SER   B 403 ? 0.1605 0.1744 0.1775 0.0083  0.0576  -0.0341 403 SER   B N   
15568 C  CA  . SER   B 403 ? 0.1833 0.1924 0.1936 0.0035  0.0604  -0.0381 403 SER   B CA  
15569 C  C   . SER   B 403 ? 0.1759 0.1894 0.1785 0.0033  0.0564  -0.0404 403 SER   B C   
15570 O  O   . SER   B 403 ? 0.1713 0.1870 0.1735 -0.0011 0.0577  -0.0462 403 SER   B O   
15571 C  CB  . SER   B 403 ? 0.1562 0.1555 0.1717 0.0040  0.0643  -0.0348 403 SER   B CB  
15572 O  OG  . SER   B 403 ? 0.2123 0.2055 0.2121 0.0076  0.0621  -0.0305 403 SER   B OG  
15578 N  N   . TYR   B 404 ? 0.1693 0.1828 0.1636 0.0087  0.0522  -0.0360 404 TYR   B N   
15579 C  CA  . TYR   B 404 ? 0.1840 0.2002 0.1684 0.0094  0.0484  -0.0364 404 TYR   B CA  
15580 C  C   . TYR   B 404 ? 0.2034 0.2313 0.1843 0.0068  0.0447  -0.0432 404 TYR   B C   
15581 O  O   . TYR   B 404 ? 0.1973 0.2273 0.1752 0.0032  0.0450  -0.0483 404 TYR   B O   
15582 C  CB  . TYR   B 404 ? 0.2492 0.2612 0.2169 0.0159  0.0443  -0.0298 404 TYR   B CB  
15583 C  CG  . TYR   B 404 ? 0.2500 0.2628 0.2055 0.0175  0.0412  -0.0288 404 TYR   B CG  
15584 C  CD1 . TYR   B 404 ? 0.2644 0.2671 0.2094 0.0164  0.0446  -0.0263 404 TYR   B CD1 
15585 C  CD2 . TYR   B 404 ? 0.2260 0.2510 0.1817 0.0201  0.0345  -0.0304 404 TYR   B CD2 
15586 C  CE1 . TYR   B 404 ? 0.2755 0.2782 0.2076 0.0179  0.0425  -0.0248 404 TYR   B CE1 
15587 C  CE2 . TYR   B 404 ? 0.2819 0.3062 0.2181 0.0221  0.0311  -0.0291 404 TYR   B CE2 
15588 C  CZ  . TYR   B 404 ? 0.3213 0.3334 0.2428 0.0210  0.0354  -0.0261 404 TYR   B CZ  
15589 O  OH  . TYR   B 404 ? 0.3419 0.3538 0.2492 0.0231  0.0329  -0.0240 404 TYR   B OH  
15599 N  N   . ARG   B 405 ? 0.1798 0.2184 0.1738 0.0086  0.0414  -0.0441 405 ARG   B N   
15600 C  CA  . ARG   B 405 ? 0.1883 0.2418 0.1875 0.0063  0.0369  -0.0507 405 ARG   B CA  
15601 C  C   . ARG   B 405 ? 0.2137 0.2674 0.2180 -0.0018 0.0416  -0.0588 405 ARG   B C   
15602 O  O   . ARG   B 405 ? 0.2080 0.2702 0.2141 -0.0056 0.0390  -0.0661 405 ARG   B O   
15603 C  CB  . ARG   B 405 ? 0.1967 0.2600 0.2010 0.0109  0.0326  -0.0488 405 ARG   B CB  
15604 C  CG  . ARG   B 405 ? 0.1935 0.2581 0.1893 0.0191  0.0265  -0.0428 405 ARG   B CG  
15605 C  CD  . ARG   B 405 ? 0.1818 0.2492 0.1860 0.0248  0.0255  -0.0379 405 ARG   B CD  
15606 N  NE  . ARG   B 405 ? 0.2165 0.2820 0.2070 0.0332  0.0203  -0.0322 405 ARG   B NE  
15607 C  CZ  . ARG   B 405 ? 0.1981 0.2510 0.1834 0.0378  0.0219  -0.0251 405 ARG   B CZ  
15608 N  NH1 . ARG   B 405 ? 0.1807 0.2213 0.1664 0.0347  0.0280  -0.0235 405 ARG   B NH1 
15609 N  NH2 . ARG   B 405 ? 0.2020 0.2543 0.1800 0.0455  0.0170  -0.0200 405 ARG   B NH2 
15623 N  N   . LEU   B 406 ? 0.1844 0.2311 0.2025 -0.0042 0.0482  -0.0578 406 LEU   B N   
15624 C  CA  . LEU   B 406 ? 0.1831 0.2278 0.2101 -0.0114 0.0539  -0.0641 406 LEU   B CA  
15625 C  C   . LEU   B 406 ? 0.2066 0.2454 0.2212 -0.0146 0.0556  -0.0687 406 LEU   B C   
15626 O  O   . LEU   B 406 ? 0.1941 0.2391 0.2135 -0.0199 0.0553  -0.0772 406 LEU   B O   
15627 C  CB  . LEU   B 406 ? 0.1824 0.2167 0.2173 -0.0116 0.0607  -0.0600 406 LEU   B CB  
15628 C  CG  . LEU   B 406 ? 0.1880 0.2147 0.2290 -0.0174 0.0677  -0.0642 406 LEU   B CG  
15629 C  CD1 . LEU   B 406 ? 0.1910 0.2252 0.2456 -0.0231 0.0693  -0.0709 406 LEU   B CD1 
15630 C  CD2 . LEU   B 406 ? 0.1624 0.1775 0.2078 -0.0152 0.0731  -0.0581 406 LEU   B CD2 
15642 N  N   . CYS   B 407 ? 0.1998 0.2290 0.2065 -0.0117 0.0573  -0.0637 407 CYS   B N   
15643 C  CA  . CYS   B 407 ? 0.2056 0.2291 0.2033 -0.0146 0.0605  -0.0672 407 CYS   B CA  
15644 C  C   . CYS   B 407 ? 0.2326 0.2637 0.2153 -0.0148 0.0549  -0.0719 407 CYS   B C   
15645 O  O   . CYS   B 407 ? 0.2348 0.2665 0.2157 -0.0193 0.0570  -0.0792 407 CYS   B O   
15646 C  CB  . CYS   B 407 ? 0.2056 0.2172 0.1975 -0.0116 0.0642  -0.0606 407 CYS   B CB  
15647 S  SG  . CYS   B 407 ? 0.2152 0.2168 0.2181 -0.0122 0.0711  -0.0576 407 CYS   B SG  
15653 N  N   . GLU   B 408 ? 0.2187 0.2576 0.1975 -0.0097 0.0478  -0.0678 408 GLU   B N   
15654 C  CA  . GLU   B 408 ? 0.2295 0.2778 0.1974 -0.0087 0.0411  -0.0711 408 GLU   B CA  
15655 C  C   . GLU   B 408 ? 0.2333 0.2929 0.2070 -0.0146 0.0388  -0.0822 408 GLU   B C   
15656 O  O   . GLU   B 408 ? 0.2421 0.3053 0.2056 -0.0171 0.0369  -0.0887 408 GLU   B O   
15657 C  CB  . GLU   B 408 ? 0.2829 0.3364 0.2418 -0.0013 0.0336  -0.0643 408 GLU   B CB  
15658 C  CG  . GLU   B 408 ? 0.3484 0.4139 0.2994 0.0008  0.0254  -0.0668 408 GLU   B CG  
15659 C  CD  . GLU   B 408 ? 0.4991 0.5635 0.4321 0.0094  0.0194  -0.0582 408 GLU   B CD  
15660 O  OE1 . GLU   B 408 ? 0.4868 0.5391 0.4171 0.0128  0.0231  -0.0499 408 GLU   B OE1 
15661 O  OE2 . GLU   B 408 ? 0.6229 0.6991 0.5482 0.0129  0.0110  -0.0595 408 GLU   B OE2 
15668 N  N   . GLY   B 409 ? 0.2336 0.2992 0.2269 -0.0169 0.0394  -0.0846 409 GLY   B N   
15669 C  CA  . GLY   B 409 ? 0.2786 0.3543 0.2770 -0.0232 0.0378  -0.0953 409 GLY   B CA  
15670 C  C   . GLY   B 409 ? 0.2506 0.3210 0.2569 -0.0305 0.0441  -0.1040 409 GLY   B C   
15671 O  O   . GLY   B 409 ? 0.2741 0.3526 0.2789 -0.0358 0.0415  -0.1143 409 GLY   B O   
15675 N  N   . TYR   B 410 ? 0.2561 0.3107 0.2588 -0.0307 0.0520  -0.1003 410 TYR   B N   
15676 C  CA  . TYR   B 410 ? 0.2642 0.3110 0.2707 -0.0367 0.0593  -0.1075 410 TYR   B CA  
15677 C  C   . TYR   B 410 ? 0.3268 0.3673 0.3064 -0.0355 0.0599  -0.1087 410 TYR   B C   
15678 O  O   . TYR   B 410 ? 0.3067 0.3408 0.2927 -0.0394 0.0664  -0.1143 410 TYR   B O   
15679 C  CB  . TYR   B 410 ? 0.2602 0.2943 0.2779 -0.0375 0.0677  -0.1039 410 TYR   B CB  
15680 C  CG  . TYR   B 410 ? 0.2614 0.2979 0.2958 -0.0412 0.0697  -0.1059 410 TYR   B CG  
15681 C  CD1 . TYR   B 410 ? 0.2680 0.3046 0.3151 -0.0486 0.0737  -0.1158 410 TYR   B CD1 
15682 C  CD2 . TYR   B 410 ? 0.2289 0.2693 0.2752 -0.0375 0.0682  -0.0983 410 TYR   B CD2 
15683 C  CE1 . TYR   B 410 ? 0.2832 0.3214 0.3450 -0.0524 0.0764  -0.1174 410 TYR   B CE1 
15684 C  CE2 . TYR   B 410 ? 0.2546 0.2969 0.3134 -0.0410 0.0708  -0.0998 410 TYR   B CE2 
15685 C  CZ  . TYR   B 410 ? 0.2701 0.3119 0.3410 -0.0487 0.0751  -0.1092 410 TYR   B CZ  
15686 O  OH  . TYR   B 410 ? 0.2849 0.3283 0.3706 -0.0527 0.0787  -0.1102 410 TYR   B OH  
15696 N  N   . GLY   B 411 ? 0.2850 0.3315 0.2590 -0.0300 0.0539  -0.1032 411 GLY   B N   
15697 C  CA  . GLY   B 411 ? 0.3334 0.3734 0.2805 -0.0286 0.0551  -0.1024 411 GLY   B CA  
15698 C  C   . GLY   B 411 ? 0.2962 0.3231 0.2482 -0.0279 0.0639  -0.0974 411 GLY   B C   
15699 O  O   . GLY   B 411 ? 0.3035 0.3247 0.2435 -0.0300 0.0686  -0.1013 411 GLY   B O   
15703 N  N   . ALA   B 412 ? 0.2981 0.3179 0.2554 -0.0252 0.0662  -0.0892 412 ALA   B N   
15704 C  CA  . ALA   B 412 ? 0.2529 0.2613 0.2178 -0.0244 0.0739  -0.0843 412 ALA   B CA  
15705 C  C   . ALA   B 412 ? 0.2503 0.2544 0.2118 -0.0187 0.0722  -0.0731 412 ALA   B C   
15706 O  O   . ALA   B 412 ? 0.2439 0.2431 0.2176 -0.0179 0.0751  -0.0691 412 ALA   B O   
15707 C  CB  . ALA   B 412 ? 0.2491 0.2522 0.2275 -0.0282 0.0802  -0.0887 412 ALA   B CB  
15713 N  N   . PRO   B 413 ? 0.2528 0.2586 0.2007 -0.0145 0.0676  -0.0673 413 PRO   B N   
15714 C  CA  . PRO   B 413 ? 0.2337 0.2358 0.1836 -0.0093 0.0657  -0.0574 413 PRO   B CA  
15715 C  C   . PRO   B 413 ? 0.2691 0.2585 0.2147 -0.0094 0.0727  -0.0531 413 PRO   B C   
15716 O  O   . PRO   B 413 ? 0.2158 0.2031 0.1722 -0.0061 0.0718  -0.0465 413 PRO   B O   
15717 C  CB  . PRO   B 413 ? 0.2625 0.2654 0.1900 -0.0057 0.0610  -0.0537 413 PRO   B CB  
15718 C  CG  . PRO   B 413 ? 0.2675 0.2725 0.1868 -0.0092 0.0631  -0.0604 413 PRO   B CG  
15719 C  CD  . PRO   B 413 ? 0.2942 0.3037 0.2210 -0.0144 0.0642  -0.0700 413 PRO   B CD  
15727 N  N   . GLU   B 414 ? 0.2649 0.2507 0.2131 -0.0130 0.0794  -0.0573 414 GLU   B N   
15728 C  CA  . GLU   B 414 ? 0.2324 0.2110 0.1915 -0.0131 0.0860  -0.0542 414 GLU   B CA  
15729 C  C   . GLU   B 414 ? 0.2284 0.2036 0.1994 -0.0125 0.0872  -0.0526 414 GLU   B C   
15730 O  O   . GLU   B 414 ? 0.2623 0.2314 0.2365 -0.0117 0.0909  -0.0491 414 GLU   B O   
15731 C  CB  . GLU   B 414 ? 0.3098 0.2836 0.2556 -0.0168 0.0931  -0.0604 414 GLU   B CB  
15732 C  CG  . GLU   B 414 ? 0.2826 0.2609 0.2447 -0.0205 0.0953  -0.0694 414 GLU   B CG  
15733 C  CD  . GLU   B 414 ? 0.3314 0.3149 0.2781 -0.0231 0.0924  -0.0771 414 GLU   B CD  
15734 O  OE1 . GLU   B 414 ? 0.2838 0.2741 0.2257 -0.0210 0.0853  -0.0747 414 GLU   B OE1 
15735 O  OE2 . GLU   B 414 ? 0.3796 0.3625 0.3278 -0.0270 0.0969  -0.0856 414 GLU   B OE2 
15742 N  N   . TYR   B 415 ? 0.1965 0.1766 0.1780 -0.0130 0.0844  -0.0551 415 TYR   B N   
15743 C  CA  . TYR   B 415 ? 0.1974 0.1747 0.1922 -0.0124 0.0860  -0.0535 415 TYR   B CA  
15744 C  C   . TYR   B 415 ? 0.1778 0.1575 0.1780 -0.0085 0.0810  -0.0473 415 TYR   B C   
15745 O  O   . TYR   B 415 ? 0.1942 0.1713 0.1998 -0.0072 0.0815  -0.0449 415 TYR   B O   
15746 C  CB  . TYR   B 415 ? 0.2179 0.1962 0.2212 -0.0161 0.0891  -0.0606 415 TYR   B CB  
15747 C  CG  . TYR   B 415 ? 0.2264 0.2016 0.2299 -0.0197 0.0951  -0.0672 415 TYR   B CG  
15748 C  CD1 . TYR   B 415 ? 0.2498 0.2185 0.2537 -0.0187 0.1004  -0.0655 415 TYR   B CD1 
15749 C  CD2 . TYR   B 415 ? 0.2192 0.1982 0.2201 -0.0238 0.0956  -0.0760 415 TYR   B CD2 
15750 C  CE1 . TYR   B 415 ? 0.2488 0.2147 0.2516 -0.0214 0.1067  -0.0715 415 TYR   B CE1 
15751 C  CE2 . TYR   B 415 ? 0.2352 0.2104 0.2316 -0.0268 0.1016  -0.0824 415 TYR   B CE2 
15752 C  CZ  . TYR   B 415 ? 0.2229 0.1922 0.2244 -0.0254 0.1075  -0.0802 415 TYR   B CZ  
15753 O  OH  . TYR   B 415 ? 0.2224 0.1892 0.2215 -0.0278 0.1092  -0.0827 415 TYR   B OH  
15763 N  N   . SER   B 416 ? 0.1952 0.1713 0.2015 -0.0221 0.0888  -0.0493 416 SER   B N   
15764 C  CA  . SER   B 416 ? 0.1932 0.1719 0.1993 -0.0171 0.0835  -0.0439 416 SER   B CA  
15765 C  C   . SER   B 416 ? 0.2121 0.1883 0.2104 -0.0121 0.0801  -0.0366 416 SER   B C   
15766 O  O   . SER   B 416 ? 0.1810 0.1628 0.1769 -0.0126 0.0790  -0.0370 416 SER   B O   
15767 C  CB  . SER   B 416 ? 0.1892 0.1774 0.1883 -0.0184 0.0803  -0.0476 416 SER   B CB  
15768 O  OG  . SER   B 416 ? 0.1777 0.1678 0.1754 -0.0130 0.0756  -0.0426 416 SER   B OG  
15774 N  N   . MET   B 417 ? 0.1869 0.1582 0.1947 -0.0081 0.0796  -0.0305 417 MET   B N   
15775 C  CA  . MET   B 417 ? 0.1904 0.1600 0.1948 -0.0040 0.0770  -0.0246 417 MET   B CA  
15776 C  C   . MET   B 417 ? 0.1827 0.1563 0.1811 -0.0009 0.0718  -0.0219 417 MET   B C   
15777 O  O   . MET   B 417 ? 0.1930 0.1635 0.1929 0.0029  0.0696  -0.0173 417 MET   B O   
15778 C  CB  . MET   B 417 ? 0.1947 0.1575 0.2065 -0.0011 0.0788  -0.0200 417 MET   B CB  
15779 C  CG  . MET   B 417 ? 0.1931 0.1519 0.2114 -0.0037 0.0846  -0.0219 417 MET   B CG  
15780 S  SD  . MET   B 417 ? 0.1959 0.1580 0.2125 -0.0060 0.0866  -0.0250 417 MET   B SD  
15781 C  CE  . MET   B 417 ? 0.2198 0.1834 0.2315 -0.0125 0.0902  -0.0335 417 MET   B CE  
15791 N  N   . THR   B 418 ? 0.1669 0.1463 0.1571 -0.0024 0.0704  -0.0244 418 THR   B N   
15792 C  CA  . THR   B 418 ? 0.1469 0.1303 0.1332 0.0007  0.0663  -0.0223 418 THR   B CA  
15793 C  C   . THR   B 418 ? 0.1445 0.1298 0.1210 0.0006  0.0652  -0.0206 418 THR   B C   
15794 O  O   . THR   B 418 ? 0.1829 0.1685 0.1522 -0.0025 0.0676  -0.0225 418 THR   B O   
15795 C  CB  . THR   B 418 ? 0.1794 0.1684 0.1622 -0.0007 0.0658  -0.0270 418 THR   B CB  
15796 O  OG1 . THR   B 418 ? 0.1927 0.1861 0.1725 -0.0055 0.0682  -0.0328 418 THR   B OG1 
15797 C  CG2 . THR   B 418 ? 0.1887 0.1754 0.1796 -0.0002 0.0666  -0.0274 418 THR   B CG2 
15805 N  N   . VAL   B 419 ? 0.1569 0.1406 0.1259 0.0042  0.0623  -0.0166 419 VAL   B N   
15806 C  CA  . VAL   B 419 ? 0.1926 0.1750 0.1452 0.0046  0.0615  -0.0137 419 VAL   B CA  
15807 C  C   . VAL   B 419 ? 0.1869 0.1730 0.1355 0.0077  0.0587  -0.0134 419 VAL   B C   
15808 O  O   . VAL   B 419 ? 0.1793 0.1624 0.1324 0.0118  0.0568  -0.0116 419 VAL   B O   
15809 C  CB  . VAL   B 419 ? 0.1617 0.1380 0.1212 0.0062  0.0617  -0.0080 419 VAL   B CB  
15810 C  CG1 . VAL   B 419 ? 0.1925 0.1652 0.1328 0.0061  0.0611  -0.0040 419 VAL   B CG1 
15811 C  CG2 . VAL   B 419 ? 0.2047 0.1780 0.1660 0.0038  0.0646  -0.0086 419 VAL   B CG2 
15821 N  N   . LYS   B 420 ? 0.1924 0.1839 0.1286 0.0063  0.0578  -0.0148 420 LYS   B N   
15822 C  CA  . LYS   B 420 ? 0.1748 0.1727 0.1087 0.0099  0.0513  -0.0139 420 LYS   B CA  
15823 C  C   . LYS   B 420 ? 0.1514 0.1549 0.0988 0.0097  0.0531  -0.0198 420 LYS   B C   
15824 O  O   . LYS   B 420 ? 0.1777 0.1819 0.1235 0.0142  0.0487  -0.0178 420 LYS   B O   
15825 C  CB  . LYS   B 420 ? 0.1774 0.1686 0.1079 0.0157  0.0456  -0.0053 420 LYS   B CB  
15826 C  CG  . LYS   B 420 ? 0.2022 0.1881 0.1208 0.0156  0.0440  0.0008  420 LYS   B CG  
15827 C  CD  . LYS   B 420 ? 0.2172 0.1931 0.1340 0.0203  0.0404  0.0086  420 LYS   B CD  
15828 C  CE  . LYS   B 420 ? 0.2377 0.2068 0.1438 0.0191  0.0408  0.0144  420 LYS   B CE  
15829 N  NZ  . LYS   B 420 ? 0.2217 0.1869 0.1323 0.0142  0.0467  0.0133  420 LYS   B NZ  
15843 N  N   . LYS   B 421 ? 0.1626 0.1675 0.1155 0.0050  0.0581  -0.0262 421 LYS   B N   
15844 C  CA  . LYS   B 421 ? 0.1758 0.1846 0.1399 0.0041  0.0591  -0.0307 421 LYS   B CA  
15845 C  C   . LYS   B 421 ? 0.1816 0.1828 0.1546 0.0078  0.0585  -0.0264 421 LYS   B C   
15846 O  O   . LYS   B 421 ? 0.1928 0.1960 0.1732 0.0075  0.0593  -0.0286 421 LYS   B O   
15847 C  CB  . LYS   B 421 ? 0.1874 0.2087 0.1498 0.0034  0.0573  -0.0361 421 LYS   B CB  
15848 C  CG  . LYS   B 421 ? 0.2354 0.2672 0.1853 -0.0005 0.0542  -0.0399 421 LYS   B CG  
15849 C  CD  . LYS   B 421 ? 0.2515 0.2990 0.2037 -0.0002 0.0481  -0.0436 421 LYS   B CD  
15850 C  CE  . LYS   B 421 ? 0.2904 0.3496 0.2322 -0.0013 0.0417  -0.0438 421 LYS   B CE  
15851 N  NZ  . LYS   B 421 ? 0.3718 0.4471 0.3097 -0.0013 0.0355  -0.0481 421 LYS   B NZ  
15865 N  N   . GLN   B 422 ? 0.1713 0.1644 0.1438 0.0107  0.0573  -0.0205 422 GLN   B N   
15866 C  CA  . GLN   B 422 ? 0.1675 0.1541 0.1464 0.0137  0.0561  -0.0162 422 GLN   B CA  
15867 C  C   . GLN   B 422 ? 0.1690 0.1496 0.1516 0.0118  0.0581  -0.0145 422 GLN   B C   
15868 O  O   . GLN   B 422 ? 0.1732 0.1520 0.1539 0.0108  0.0587  -0.0135 422 GLN   B O   
15869 C  CB  . GLN   B 422 ? 0.1715 0.1533 0.1460 0.0191  0.0531  -0.0112 422 GLN   B CB  
15870 C  CG  . GLN   B 422 ? 0.1897 0.1656 0.1649 0.0216  0.0514  -0.0076 422 GLN   B CG  
15871 C  CD  . GLN   B 422 ? 0.1510 0.1255 0.1291 0.0271  0.0484  -0.0045 422 GLN   B CD  
15872 O  OE1 . GLN   B 422 ? 0.1663 0.1439 0.1398 0.0289  0.0474  -0.0061 422 GLN   B OE1 
15873 N  NE2 . GLN   B 422 ? 0.1924 0.1585 0.1594 0.0294  0.0466  -0.0004 422 GLN   B NE2 
15882 N  N   . GLU   B 423 ? 0.1379 0.1160 0.1310 0.0120  0.0590  -0.0136 423 GLU   B N   
15883 C  CA  . GLU   B 423 ? 0.1512 0.1236 0.1475 0.0107  0.0616  -0.0117 423 GLU   B CA  
15884 C  C   . GLU   B 423 ? 0.1569 0.1249 0.1516 0.0137  0.0602  -0.0067 423 GLU   B C   
15885 O  O   . GLU   B 423 ? 0.1817 0.1476 0.1727 0.0171  0.0574  -0.0032 423 GLU   B O   
15886 C  CB  . GLU   B 423 ? 0.1614 0.1303 0.1629 0.0103  0.0639  -0.0114 423 GLU   B CB  
15887 C  CG  . GLU   B 423 ? 0.1518 0.1235 0.1594 0.0061  0.0673  -0.0170 423 GLU   B CG  
15888 C  CD  . GLU   B 423 ? 0.1693 0.1480 0.1729 0.0053  0.0659  -0.0213 423 GLU   B CD  
15889 O  OE1 . GLU   B 423 ? 0.1753 0.1566 0.1760 0.0089  0.0621  -0.0191 423 GLU   B OE1 
15890 O  OE2 . GLU   B 423 ? 0.1592 0.1416 0.1669 0.0008  0.0688  -0.0272 423 GLU   B OE2 
15897 N  N   . ILE   B 424 ? 0.1415 0.1084 0.1387 0.0121  0.0625  -0.0064 424 ILE   B N   
15898 C  CA  . ILE   B 424 ? 0.1472 0.1119 0.1482 0.0145  0.0622  -0.0024 424 ILE   B CA  
15899 C  C   . ILE   B 424 ? 0.1973 0.1576 0.1960 0.0175  0.0624  0.0017  424 ILE   B C   
15900 O  O   . ILE   B 424 ? 0.2141 0.1734 0.2195 0.0163  0.0650  0.0012  424 ILE   B O   
15901 C  CB  . ILE   B 424 ? 0.1885 0.1526 0.1850 0.0116  0.0652  -0.0038 424 ILE   B CB  
15902 C  CG1 . ILE   B 424 ? 0.2131 0.1810 0.2065 0.0086  0.0654  -0.0068 424 ILE   B CG1 
15903 C  CG2 . ILE   B 424 ? 0.1666 0.1300 0.1700 0.0138  0.0662  -0.0001 424 ILE   B CG2 
15904 C  CD1 . ILE   B 424 ? 0.2746 0.2431 0.2640 0.0046  0.0689  -0.0102 424 ILE   B CD1 
15916 N  N   . PRO   B 425 ? 0.1723 0.1328 0.1745 0.0214  0.0602  0.0059  425 PRO   B N   
15917 C  CA  . PRO   B 425 ? 0.1623 0.1219 0.1685 0.0249  0.0604  0.0101  425 PRO   B CA  
15918 C  C   . PRO   B 425 ? 0.1993 0.1577 0.2058 0.0262  0.0633  0.0125  425 PRO   B C   
15919 O  O   . PRO   B 425 ? 0.1799 0.1398 0.1945 0.0234  0.0661  0.0101  425 PRO   B O   
15920 C  CB  . PRO   B 425 ? 0.1861 0.1448 0.1825 0.0286  0.0565  0.0121  425 PRO   B CB  
15921 C  CG  . PRO   B 425 ? 0.2019 0.1608 0.1954 0.0276  0.0558  0.0106  425 PRO   B CG  
15922 C  CD  . PRO   B 425 ? 0.2079 0.1672 0.2003 0.0231  0.0577  0.0068  425 PRO   B CD  
15930 N  N   . ALA   B 426 ? 0.1887 0.1485 0.1989 0.0308  0.0628  0.0170  426 ALA   B N   
15931 C  CA  . ALA   B 426 ? 0.1491 0.1118 0.1719 0.0331  0.0657  0.0203  426 ALA   B CA  
15932 C  C   . ALA   B 426 ? 0.1619 0.1284 0.1862 0.0344  0.0654  0.0203  426 ALA   B C   
15933 O  O   . ALA   B 426 ? 0.1658 0.1369 0.1952 0.0392  0.0646  0.0242  426 ALA   B O   
15934 C  CB  . ALA   B 426 ? 0.1766 0.1384 0.1932 0.0381  0.0653  0.0254  426 ALA   B CB  
15940 N  N   . TYR   B 427 ? 0.1601 0.1273 0.1860 0.0302  0.0664  0.0167  427 TYR   B N   
15941 C  CA  . TYR   B 427 ? 0.1702 0.1417 0.1996 0.0306  0.0674  0.0164  427 TYR   B CA  
15942 C  C   . TYR   B 427 ? 0.1523 0.1236 0.1885 0.0249  0.0711  0.0121  427 TYR   B C   
15943 O  O   . TYR   B 427 ? 0.1828 0.1505 0.2073 0.0214  0.0706  0.0090  427 TYR   B O   
15944 C  CB  . TYR   B 427 ? 0.1505 0.1254 0.1811 0.0324  0.0645  0.0169  427 TYR   B CB  
15945 C  CG  . TYR   B 427 ? 0.1516 0.1261 0.1776 0.0374  0.0598  0.0193  427 TYR   B CG  
15946 C  CD1 . TYR   B 427 ? 0.1720 0.1406 0.1858 0.0366  0.0576  0.0182  427 TYR   B CD1 
15947 C  CD2 . TYR   B 427 ? 0.1744 0.1541 0.2028 0.0433  0.0570  0.0229  427 TYR   B CD2 
15948 C  CE1 . TYR   B 427 ? 0.1966 0.1638 0.2023 0.0406  0.0534  0.0199  427 TYR   B CE1 
15949 C  CE2 . TYR   B 427 ? 0.1873 0.1662 0.2085 0.0480  0.0522  0.0248  427 TYR   B CE2 
15950 C  CZ  . TYR   B 427 ? 0.1795 0.1520 0.1912 0.0466  0.0506  0.0233  427 TYR   B CZ  
15951 O  OH  . TYR   B 427 ? 0.1743 0.1455 0.1778 0.0508  0.0465  0.0247  427 TYR   B OH  
15961 N  N   . ASP   B 428 ? 0.1657 0.1384 0.2075 0.0247  0.0746  0.0119  428 ASP   B N   
15962 C  CA  . ASP   B 428 ? 0.1783 0.1499 0.2210 0.0197  0.0784  0.0078  428 ASP   B CA  
15963 C  C   . ASP   B 428 ? 0.1881 0.1633 0.2286 0.0173  0.0787  0.0066  428 ASP   B C   
15964 O  O   . ASP   B 428 ? 0.1666 0.1487 0.2198 0.0190  0.0797  0.0086  428 ASP   B O   
15965 C  CB  . ASP   B 428 ? 0.1692 0.1412 0.2227 0.0205  0.0826  0.0078  428 ASP   B CB  
15966 C  CG  . ASP   B 428 ? 0.1953 0.1641 0.2449 0.0156  0.0869  0.0027  428 ASP   B CG  
15967 O  OD1 . ASP   B 428 ? 0.1747 0.1449 0.2211 0.0117  0.0864  -0.0004 428 ASP   B OD1 
15968 O  OD2 . ASP   B 428 ? 0.2065 0.1725 0.2626 0.0157  0.0910  0.0021  428 ASP   B OD2 
15973 N  N   . PRO   B 429 ? 0.1669 0.1410 0.2032 0.0130  0.0786  0.0037  429 PRO   B N   
15974 C  CA  . PRO   B 429 ? 0.1986 0.1738 0.2276 0.0100  0.0796  0.0036  429 PRO   B CA  
15975 C  C   . PRO   B 429 ? 0.1957 0.1745 0.2321 0.0069  0.0841  0.0018  429 PRO   B C   
15976 O  O   . PRO   B 429 ? 0.1758 0.1581 0.2170 0.0042  0.0854  0.0026  429 PRO   B O   
15977 C  CB  . PRO   B 429 ? 0.1776 0.1491 0.1962 0.0071  0.0782  0.0018  429 PRO   B CB  
15978 C  CG  . PRO   B 429 ? 0.1554 0.1256 0.1736 0.0064  0.0781  -0.0011 429 PRO   B CG  
15979 C  CD  . PRO   B 429 ? 0.1754 0.1445 0.1980 0.0106  0.0776  0.0007  429 PRO   B CD  
15987 N  N   . ARG   B 430 ? 0.1711 0.1499 0.2152 0.0068  0.0866  -0.0004 430 ARG   B N   
15988 C  CA  . ARG   B 430 ? 0.1866 0.1677 0.2344 0.0048  0.0913  -0.0024 430 ARG   B CA  
15989 C  C   . ARG   B 430 ? 0.1822 0.1712 0.2448 0.0068  0.0919  0.0006  430 ARG   B C   
15990 O  O   . ARG   B 430 ? 0.2026 0.1951 0.2684 0.0038  0.0954  -0.0004 430 ARG   B O   
15991 C  CB  . ARG   B 430 ? 0.1764 0.1547 0.2285 0.0049  0.0944  -0.0053 430 ARG   B CB  
15992 C  CG  . ARG   B 430 ? 0.1980 0.1715 0.2391 0.0013  0.0948  -0.0096 430 ARG   B CG  
15993 C  CD  . ARG   B 430 ? 0.2250 0.1941 0.2669 0.0009  0.0986  -0.0125 430 ARG   B CD  
15994 N  NE  . ARG   B 430 ? 0.2086 0.1754 0.2602 0.0049  0.0977  -0.0101 430 ARG   B NE  
15995 C  CZ  . ARG   B 430 ? 0.2460 0.2062 0.2933 0.0043  0.1005  -0.0119 430 ARG   B CZ  
15996 N  NH1 . ARG   B 430 ? 0.1991 0.1586 0.2513 0.0004  0.1053  -0.0173 430 ARG   B NH1 
15997 N  NH2 . ARG   B 430 ? 0.2543 0.2119 0.3072 0.0074  0.0992  -0.0087 430 ARG   B NH2 
16011 N  N   . GLY   B 431 ? 0.1698 0.1618 0.2393 0.0116  0.0887  0.0044  431 GLY   B N   
16012 C  CA  . GLY   B 431 ? 0.1725 0.1747 0.2551 0.0144  0.0880  0.0074  431 GLY   B CA  
16013 C  C   . GLY   B 431 ? 0.1841 0.1900 0.2659 0.0142  0.0848  0.0093  431 GLY   B C   
16014 O  O   . GLY   B 431 ? 0.1752 0.1915 0.2712 0.0170  0.0830  0.0117  431 GLY   B O   
16018 N  N   . ILE   B 432 ? 0.1801 0.1786 0.2484 0.0113  0.0837  0.0086  432 ILE   B N   
16019 C  CA  . ILE   B 432 ? 0.1473 0.1463 0.2148 0.0103  0.0795  0.0101  432 ILE   B CA  
16020 C  C   . ILE   B 432 ? 0.1653 0.1558 0.2170 0.0039  0.0809  0.0089  432 ILE   B C   
16021 O  O   . ILE   B 432 ? 0.1774 0.1603 0.2161 0.0045  0.0798  0.0085  432 ILE   B O   
16022 C  CB  . ILE   B 432 ? 0.1617 0.1571 0.2215 0.0164  0.0730  0.0120  432 ILE   B CB  
16023 C  CG1 . ILE   B 432 ? 0.1833 0.1810 0.2476 0.0231  0.0757  0.0137  432 ILE   B CG1 
16024 C  CG2 . ILE   B 432 ? 0.1637 0.1613 0.2213 0.0163  0.0639  0.0130  432 ILE   B CG2 
16025 C  CD1 . ILE   B 432 ? 0.1685 0.1620 0.2283 0.0285  0.0716  0.0156  432 ILE   B CD1 
16037 N  N   . GLN   B 433 ? 0.1704 0.1628 0.2245 -0.0020 0.0835  0.0084  433 GLN   B N   
16038 C  CA  . GLN   B 433 ? 0.1772 0.1622 0.2205 -0.0079 0.0868  0.0084  433 GLN   B CA  
16039 C  C   . GLN   B 433 ? 0.1849 0.1603 0.2126 -0.0083 0.0800  0.0101  433 GLN   B C   
16040 O  O   . GLN   B 433 ? 0.1982 0.1669 0.2121 -0.0090 0.0809  0.0105  433 GLN   B O   
16041 C  CB  . GLN   B 433 ? 0.2037 0.1920 0.2512 -0.0136 0.0910  0.0076  433 GLN   B CB  
16042 C  CG  . GLN   B 433 ? 0.1959 0.1914 0.2538 -0.0125 0.0941  0.0051  433 GLN   B CG  
16043 C  CD  . GLN   B 433 ? 0.1984 0.1892 0.2474 -0.0121 0.0958  0.0026  433 GLN   B CD  
16044 O  OE1 . GLN   B 433 ? 0.2067 0.1903 0.2386 -0.0141 0.0950  0.0027  433 GLN   B OE1 
16045 N  NE2 . GLN   B 433 ? 0.2378 0.2313 0.2895 -0.0100 0.0980  0.0003  433 GLN   B NE2 
16054 N  N   . GLY   B 434 ? 0.1836 0.1592 0.2135 -0.0082 0.0733  0.0107  434 GLY   B N   
16055 C  CA  . GLY   B 434 ? 0.1732 0.1394 0.1926 -0.0084 0.0673  0.0121  434 GLY   B CA  
16056 C  C   . GLY   B 434 ? 0.1724 0.1347 0.1820 -0.0025 0.0640  0.0123  434 GLY   B C   
16057 O  O   . GLY   B 434 ? 0.1735 0.1278 0.1705 -0.0023 0.0628  0.0135  434 GLY   B O   
16061 N  N   . HIS   B 435 ? 0.1750 0.1430 0.1897 0.0026  0.0628  0.0114  435 HIS   B N   
16062 C  CA  . HIS   B 435 ? 0.1654 0.1307 0.1747 0.0078  0.0605  0.0115  435 HIS   B CA  
16063 C  C   . HIS   B 435 ? 0.1694 0.1315 0.1708 0.0070  0.0653  0.0106  435 HIS   B C   
16064 O  O   . HIS   B 435 ? 0.2024 0.1598 0.1925 0.0093  0.0628  0.0107  435 HIS   B O   
16065 C  CB  . HIS   B 435 ? 0.1561 0.1277 0.1741 0.0134  0.0593  0.0116  435 HIS   B CB  
16066 C  CG  . HIS   B 435 ? 0.1698 0.1383 0.1836 0.0184  0.0561  0.0122  435 HIS   B CG  
16067 N  ND1 . HIS   B 435 ? 0.1842 0.1480 0.1892 0.0197  0.0498  0.0125  435 HIS   B ND1 
16068 C  CD2 . HIS   B 435 ? 0.2333 0.1999 0.2392 0.0224  0.0590  0.0121  435 HIS   B CD2 
16069 C  CE1 . HIS   B 435 ? 0.2359 0.1964 0.2308 0.0244  0.0490  0.0128  435 HIS   B CE1 
16070 N  NE2 . HIS   B 435 ? 0.2044 0.1690 0.2107 0.0258  0.0545  0.0127  435 HIS   B NE2 
16078 N  N   . GLY   B 436 ? 0.1568 0.1221 0.1614 0.0038  0.0722  0.0092  436 GLY   B N   
16079 C  CA  . GLY   B 436 ? 0.1611 0.1246 0.1572 0.0021  0.0764  0.0075  436 GLY   B CA  
16080 C  C   . GLY   B 436 ? 0.1782 0.1359 0.1601 -0.0001 0.0740  0.0093  436 GLY   B C   
16081 O  O   . GLY   B 436 ? 0.1759 0.1326 0.1491 0.0006  0.0734  0.0079  436 GLY   B O   
16085 N  N   . ILE   B 437 ? 0.1984 0.1522 0.1782 -0.0027 0.0718  0.0120  437 ILE   B N   
16086 C  CA  . ILE   B 437 ? 0.2179 0.1635 0.1828 -0.0037 0.0690  0.0154  437 ILE   B CA  
16087 C  C   . ILE   B 437 ? 0.1847 0.1287 0.1500 0.0015  0.0627  0.0157  437 ILE   B C   
16088 O  O   . ILE   B 437 ? 0.1991 0.1402 0.1498 0.0028  0.0612  0.0167  437 ILE   B O   
16089 C  CB  . ILE   B 437 ? 0.2162 0.1568 0.1826 -0.0075 0.0688  0.0183  437 ILE   B CB  
16090 C  CG1 . ILE   B 437 ? 0.1862 0.1323 0.1652 -0.0129 0.0756  0.0176  437 ILE   B CG1 
16091 C  CG2 . ILE   B 437 ? 0.2022 0.1339 0.1588 -0.0079 0.0669  0.0225  437 ILE   B CG2 
16092 C  CD1 . ILE   B 437 ? 0.1954 0.1371 0.1762 -0.0175 0.0760  0.0195  437 ILE   B CD1 
16104 N  N   . THR   B 438 ? 0.2171 0.1598 0.1812 0.0047  0.0585  0.0149  438 THR   B N   
16105 C  CA  . THR   B 438 ? 0.1742 0.1156 0.1419 0.0097  0.0533  0.0149  438 THR   B CA  
16106 C  C   . THR   B 438 ? 0.1783 0.1226 0.1388 0.0120  0.0547  0.0132  438 THR   B C   
16107 O  O   . THR   B 438 ? 0.1907 0.1326 0.1423 0.0141  0.0518  0.0141  438 THR   B O   
16108 C  CB  . THR   B 438 ? 0.2063 0.1480 0.1752 0.0127  0.0498  0.0138  438 THR   B CB  
16109 O  OG1 . THR   B 438 ? 0.2010 0.1399 0.1745 0.0100  0.0474  0.0144  438 THR   B OG1 
16110 C  CG2 . THR   B 438 ? 0.2090 0.1491 0.1756 0.0178  0.0459  0.0134  438 THR   B CG2 
16118 N  N   . TYR   B 439 ? 0.1830 0.1333 0.1497 0.0112  0.0592  0.0103  439 TYR   B N   
16119 C  CA  . TYR   B 439 ? 0.1962 0.1496 0.1588 0.0121  0.0619  0.0072  439 TYR   B CA  
16120 C  C   . TYR   B 439 ? 0.1967 0.1511 0.1508 0.0095  0.0618  0.0072  439 TYR   B C   
16121 O  O   . TYR   B 439 ? 0.2103 0.1663 0.1588 0.0115  0.0592  0.0061  439 TYR   B O   
16122 C  CB  . TYR   B 439 ? 0.1641 0.1233 0.1403 0.0102  0.0659  0.0041  439 TYR   B CB  
16123 C  CG  . TYR   B 439 ? 0.1627 0.1226 0.1486 0.0135  0.0654  0.0044  439 TYR   B CG  
16124 C  CD1 . TYR   B 439 ? 0.1522 0.1100 0.1378 0.0182  0.0625  0.0063  439 TYR   B CD1 
16125 C  CD2 . TYR   B 439 ? 0.1859 0.1485 0.1803 0.0123  0.0681  0.0034  439 TYR   B CD2 
16126 C  CE1 . TYR   B 439 ? 0.1575 0.1168 0.1504 0.0212  0.0617  0.0076  439 TYR   B CE1 
16127 C  CE2 . TYR   B 439 ? 0.1966 0.1602 0.1982 0.0158  0.0674  0.0052  439 TYR   B CE2 
16128 C  CZ  . TYR   B 439 ? 0.1742 0.1367 0.1759 0.0202  0.0643  0.0075  439 TYR   B CZ  
16129 O  OH  . TYR   B 439 ? 0.1698 0.1338 0.1779 0.0238  0.0636  0.0099  439 TYR   B OH  
16139 N  N   . ALA   B 440 ? 0.1872 0.1407 0.1369 0.0055  0.0647  0.0086  440 ALA   B N   
16140 C  CA  . ALA   B 440 ? 0.1730 0.1286 0.1150 0.0032  0.0653  0.0093  440 ALA   B CA  
16141 C  C   . ALA   B 440 ? 0.2040 0.1538 0.1313 0.0063  0.0590  0.0142  440 ALA   B C   
16142 O  O   . ALA   B 440 ? 0.2073 0.1613 0.1278 0.0070  0.0568  0.0139  440 ALA   B O   
16143 C  CB  . ALA   B 440 ? 0.2008 0.1559 0.1379 -0.0017 0.0692  0.0097  440 ALA   B CB  
16149 N  N   . VAL   B 441 ? 0.2021 0.1450 0.1331 0.0078  0.0560  0.0180  441 VAL   B N   
16150 C  CA  . VAL   B 441 ? 0.2216 0.1565 0.1400 0.0109  0.0512  0.0233  441 VAL   B CA  
16151 C  C   . VAL   B 441 ? 0.1943 0.1290 0.1202 0.0165  0.0459  0.0229  441 VAL   B C   
16152 O  O   . VAL   B 441 ? 0.2129 0.1419 0.1296 0.0199  0.0423  0.0268  441 VAL   B O   
16153 C  CB  . VAL   B 441 ? 0.1993 0.1267 0.1236 0.0080  0.0529  0.0278  441 VAL   B CB  
16154 C  CG1 . VAL   B 441 ? 0.2476 0.1753 0.1629 0.0024  0.0587  0.0285  441 VAL   B CG1 
16155 C  CG2 . VAL   B 441 ? 0.2050 0.1280 0.1348 0.0078  0.0517  0.0261  441 VAL   B CG2 
16165 N  N   . ASN   B 442 ? 0.1947 0.1327 0.1278 0.0176  0.0460  0.0188  442 ASN   B N   
16166 C  CA  . ASN   B 442 ? 0.2154 0.1508 0.1462 0.0230  0.0420  0.0180  442 ASN   B CA  
16167 C  C   . ASN   B 442 ? 0.2061 0.1449 0.1349 0.0267  0.0387  0.0193  442 ASN   B C   
16168 O  O   . ASN   B 442 ? 0.2005 0.1477 0.1278 0.0256  0.0398  0.0169  442 ASN   B O   
16169 C  CB  . ASN   B 442 ? 0.1697 0.1115 0.1160 0.0239  0.0435  0.0142  442 ASN   B CB  
16170 C  CG  . ASN   B 442 ? 0.1980 0.1358 0.1416 0.0285  0.0403  0.0137  442 ASN   B CG  
16171 O  OD1 . ASN   B 442 ? 0.1960 0.1317 0.1371 0.0321  0.0372  0.0148  442 ASN   B OD1 
16172 N  ND2 . ASN   B 442 ? 0.1977 0.1365 0.1485 0.0290  0.0413  0.0125  442 ASN   B ND2 
16179 N  N   . ASN   B 443 ? 0.2169 0.1489 0.1408 0.0311  0.0348  0.0226  443 ASN   B N   
16180 C  CA  . ASN   B 443 ? 0.2142 0.1491 0.1333 0.0357  0.0313  0.0246  443 ASN   B CA  
16181 C  C   . ASN   B 443 ? 0.1848 0.1308 0.1124 0.0379  0.0308  0.0200  443 ASN   B C   
16182 O  O   . ASN   B 443 ? 0.2101 0.1629 0.1321 0.0404  0.0283  0.0203  443 ASN   B O   
16183 C  CB  . ASN   B 443 ? 0.2213 0.1462 0.1387 0.0406  0.0283  0.0291  443 ASN   B CB  
16184 C  CG  . ASN   B 443 ? 0.2411 0.1545 0.1503 0.0383  0.0296  0.0342  443 ASN   B CG  
16185 O  OD1 . ASN   B 443 ? 0.2375 0.1533 0.1429 0.0356  0.0308  0.0371  443 ASN   B OD1 
16186 N  ND2 . ASN   B 443 ? 0.2234 0.1259 0.1366 0.0390  0.0294  0.0349  443 ASN   B ND2 
16193 N  N   . ARG   B 444 ? 0.1801 0.1267 0.1140 0.0371  0.0331  0.0158  444 ARG   B N   
16194 C  CA  . ARG   B 444 ? 0.1994 0.1533 0.1363 0.0388  0.0337  0.0117  444 ARG   B CA  
16195 C  C   . ARG   B 444 ? 0.2018 0.1629 0.1415 0.0340  0.0381  0.0074  444 ARG   B C   
16196 O  O   . ARG   B 444 ? 0.1654 0.1336 0.1155 0.0343  0.0401  0.0035  444 ARG   B O   
16197 C  CB  . ARG   B 444 ? 0.1843 0.1339 0.1273 0.0424  0.0337  0.0110  444 ARG   B CB  
16198 C  CG  . ARG   B 444 ? 0.1779 0.1256 0.1254 0.0401  0.0373  0.0092  444 ARG   B CG  
16199 C  CD  . ARG   B 444 ? 0.1813 0.1260 0.1298 0.0441  0.0368  0.0086  444 ARG   B CD  
16200 N  NE  . ARG   B 444 ? 0.1680 0.1153 0.1231 0.0409  0.0380  0.0082  444 ARG   B NE  
16201 C  CZ  . ARG   B 444 ? 0.1659 0.1165 0.1238 0.0406  0.0373  0.0079  444 ARG   B CZ  
16202 N  NH1 . ARG   B 444 ? 0.1643 0.1174 0.1232 0.0423  0.0362  0.0071  444 ARG   B NH1 
16203 N  NH2 . ARG   B 444 ? 0.1521 0.1041 0.1143 0.0387  0.0385  0.0085  444 ARG   B NH2 
16217 N  N   . GLY   B 445 ? 0.1801 0.1413 0.1201 0.0294  0.0405  0.0075  445 GLY   B N   
16218 C  CA  . GLY   B 445 ? 0.1514 0.1191 0.0987 0.0247  0.0456  0.0029  445 GLY   B CA  
16219 C  C   . GLY   B 445 ? 0.1899 0.1524 0.1394 0.0234  0.0499  0.0022  445 GLY   B C   
16220 O  O   . GLY   B 445 ? 0.2292 0.1850 0.1784 0.0253  0.0481  0.0054  445 GLY   B O   
16224 N  N   . GLY   B 446 ? 0.1633 0.1308 0.1233 0.0195  0.0539  -0.0018 446 GLY   B N   
16225 C  CA  . GLY   B 446 ? 0.1806 0.1452 0.1455 0.0180  0.0554  -0.0015 446 GLY   B CA  
16226 C  C   . GLY   B 446 ? 0.1642 0.1253 0.1354 0.0222  0.0533  0.0015  446 GLY   B C   
16227 O  O   . GLY   B 446 ? 0.1672 0.1301 0.1409 0.0229  0.0519  0.0006  446 GLY   B O   
16231 N  N   . CYS   B 447 ? 0.1675 0.1236 0.1373 0.0242  0.0531  0.0045  447 CYS   B N   
16232 C  CA  . CYS   B 447 ? 0.2007 0.1523 0.1654 0.0282  0.0504  0.0070  447 CYS   B CA  
16233 C  C   . CYS   B 447 ? 0.1488 0.0994 0.1246 0.0287  0.0508  0.0089  447 CYS   B C   
16234 O  O   . CYS   B 447 ? 0.1881 0.1359 0.1538 0.0256  0.0500  0.0095  447 CYS   B O   
16235 C  CB  . CYS   B 447 ? 0.1988 0.1483 0.1612 0.0319  0.0469  0.0076  447 CYS   B CB  
16236 S  SG  . CYS   B 447 ? 0.1858 0.1310 0.1473 0.0361  0.0428  0.0093  447 CYS   B SG  
16242 N  N   . HIS   B 448 ? 0.1708 0.1205 0.1449 0.0314  0.0500  0.0100  448 HIS   B N   
16243 C  CA  . HIS   B 448 ? 0.1830 0.1333 0.1601 0.0310  0.0478  0.0115  448 HIS   B CA  
16244 C  C   . HIS   B 448 ? 0.1836 0.1304 0.1572 0.0320  0.0417  0.0119  448 HIS   B C   
16245 O  O   . HIS   B 448 ? 0.2026 0.1485 0.1758 0.0294  0.0395  0.0120  448 HIS   B O   
16246 C  CB  . HIS   B 448 ? 0.1744 0.1293 0.1618 0.0340  0.0500  0.0128  448 HIS   B CB  
16247 C  CG  . HIS   B 448 ? 0.2111 0.1645 0.1882 0.0374  0.0472  0.0140  448 HIS   B CG  
16248 N  ND1 . HIS   B 448 ? 0.1666 0.1215 0.1482 0.0359  0.0469  0.0133  448 HIS   B ND1 
16249 C  CD2 . HIS   B 448 ? 0.1821 0.1379 0.1651 0.0415  0.0447  0.0158  448 HIS   B CD2 
16250 C  CE1 . HIS   B 448 ? 0.1706 0.1255 0.1481 0.0387  0.0450  0.0147  448 HIS   B CE1 
16251 N  NE2 . HIS   B 448 ? 0.1838 0.1388 0.1605 0.0421  0.0437  0.0162  448 HIS   B NE2 
16259 N  N   . ILE   B 449 ? 0.1800 0.1240 0.1482 0.0360  0.0399  0.0116  449 ILE   B N   
16260 C  CA  . ILE   B 449 ? 0.1903 0.1306 0.1522 0.0378  0.0349  0.0111  449 ILE   B CA  
16261 C  C   . ILE   B 449 ? 0.2058 0.1387 0.1603 0.0361  0.0320  0.0103  449 ILE   B C   
16262 O  O   . ILE   B 449 ? 0.1994 0.1293 0.1539 0.0361  0.0283  0.0090  449 ILE   B O   
16263 C  CB  . ILE   B 449 ? 0.1702 0.1119 0.1326 0.0431  0.0350  0.0115  449 ILE   B CB  
16264 C  CG1 . ILE   B 449 ? 0.1926 0.1328 0.1482 0.0452  0.0304  0.0107  449 ILE   B CG1 
16265 C  CG2 . ILE   B 449 ? 0.1828 0.1243 0.1395 0.0422  0.0351  0.0108  449 ILE   B CG2 
16266 C  CD1 . ILE   B 449 ? 0.2031 0.1493 0.1635 0.0440  0.0281  0.0113  449 ILE   B CD1 
16278 N  N   . LYS   B 450 ? 0.1760 0.1078 0.1329 0.0345  0.0337  0.0110  450 LYS   B N   
16279 C  CA  . LYS   B 450 ? 0.1907 0.1144 0.1403 0.0332  0.0316  0.0117  450 LYS   B CA  
16280 C  C   . LYS   B 450 ? 0.2012 0.1231 0.1537 0.0278  0.0317  0.0122  450 LYS   B C   
16281 O  O   . LYS   B 450 ? 0.2070 0.1211 0.1557 0.0261  0.0307  0.0133  450 LYS   B O   
16282 C  CB  . LYS   B 450 ? 0.1894 0.1122 0.1351 0.0344  0.0326  0.0133  450 LYS   B CB  
16283 C  CG  . LYS   B 450 ? 0.1944 0.1202 0.1388 0.0393  0.0325  0.0123  450 LYS   B CG  
16284 C  CD  . LYS   B 450 ? 0.1993 0.1212 0.1417 0.0429  0.0298  0.0110  450 LYS   B CD  
16285 C  CE  . LYS   B 450 ? 0.2117 0.1378 0.1541 0.0431  0.0295  0.0094  450 LYS   B CE  
16286 N  NZ  . LYS   B 450 ? 0.1860 0.1120 0.1289 0.0454  0.0273  0.0078  450 LYS   B NZ  
16300 N  N   . GLY   B 451 ? 0.2076 0.1365 0.1670 0.0254  0.0334  0.0119  451 GLY   B N   
16301 C  CA  . GLY   B 451 ? 0.2091 0.1388 0.1744 0.0199  0.0343  0.0120  451 GLY   B CA  
16302 C  C   . GLY   B 451 ? 0.2119 0.1512 0.1874 0.0194  0.0351  0.0111  451 GLY   B C   
16303 O  O   . GLY   B 451 ? 0.2283 0.1719 0.2075 0.0169  0.0392  0.0119  451 GLY   B O   
16307 N  N   . TYR   B 452 ? 0.2166 0.1590 0.1924 0.0220  0.0311  0.0096  452 TYR   B N   
16308 C  CA  . TYR   B 452 ? 0.2005 0.1539 0.1890 0.0235  0.0309  0.0101  452 TYR   B CA  
16309 C  C   . TYR   B 452 ? 0.2284 0.1869 0.2215 0.0186  0.0308  0.0093  452 TYR   B C   
16310 O  O   . TYR   B 452 ? 0.1880 0.1522 0.1891 0.0180  0.0259  0.0076  452 TYR   B O   
16311 C  CB  . TYR   B 452 ? 0.2190 0.1735 0.2001 0.0283  0.0264  0.0096  452 TYR   B CB  
16312 C  CG  . TYR   B 452 ? 0.2085 0.1711 0.1945 0.0333  0.0275  0.0120  452 TYR   B CG  
16313 C  CD1 . TYR   B 452 ? 0.1862 0.1491 0.1757 0.0354  0.0332  0.0142  452 TYR   B CD1 
16314 C  CD2 . TYR   B 452 ? 0.1899 0.1610 0.1816 0.0356  0.0229  0.0122  452 TYR   B CD2 
16315 C  CE1 . TYR   B 452 ? 0.1608 0.1297 0.1580 0.0404  0.0354  0.0170  452 TYR   B CE1 
16316 C  CE2 . TYR   B 452 ? 0.1937 0.1713 0.1882 0.0410  0.0242  0.0159  452 TYR   B CE2 
16317 C  CZ  . TYR   B 452 ? 0.1904 0.1659 0.1875 0.0434  0.0309  0.0186  452 TYR   B CZ  
16318 O  OH  . TYR   B 452 ? 0.2081 0.1884 0.2094 0.0491  0.0330  0.0227  452 TYR   B OH  
16328 N  N   . MET   B 453 ? 0.2451 0.2050 0.2438 0.0152  0.0361  0.0102  453 MET   B N   
16329 C  CA  . MET   B 453 ? 0.2131 0.1804 0.2252 0.0102  0.0375  0.0097  453 MET   B CA  
16330 C  C   . MET   B 453 ? 0.2007 0.1800 0.2218 0.0141  0.0365  0.0102  453 MET   B C   
16331 O  O   . MET   B 453 ? 0.1751 0.1640 0.2114 0.0108  0.0367  0.0095  453 MET   B O   
16332 C  CB  . MET   B 453 ? 0.1900 0.1554 0.2047 0.0060  0.0444  0.0105  453 MET   B CB  
16333 C  CG  . MET   B 453 ? 0.2097 0.1641 0.2145 0.0015  0.0451  0.0110  453 MET   B CG  
16334 S  SD  . MET   B 453 ? 0.2300 0.1824 0.2380 -0.0047 0.0419  0.0087  453 MET   B SD  
16335 C  CE  . MET   B 453 ? 0.2021 0.1657 0.2273 -0.0102 0.0480  0.0088  453 MET   B CE  
16345 N  N   . ILE   B 454 ? 0.1639 0.1456 0.1887 0.0206  0.0357  0.0120  454 ILE   B N   
16346 C  CA  . ILE   B 454 ? 0.1968 0.1879 0.2231 0.0257  0.0343  0.0139  454 ILE   B CA  
16347 C  C   . ILE   B 454 ? 0.1746 0.1754 0.2128 0.0249  0.0263  0.0122  454 ILE   B C   
16348 O  O   . ILE   B 454 ? 0.2035 0.2153 0.2472 0.0261  0.0245  0.0132  454 ILE   B O   
16349 C  CB  . ILE   B 454 ? 0.1797 0.1693 0.2077 0.0328  0.0357  0.0167  454 ILE   B CB  
16350 C  CG1 . ILE   B 454 ? 0.2056 0.1879 0.2275 0.0326  0.0433  0.0171  454 ILE   B CG1 
16351 C  CG2 . ILE   B 454 ? 0.1960 0.1948 0.2273 0.0390  0.0337  0.0202  454 ILE   B CG2 
16352 C  CD1 . ILE   B 454 ? 0.2059 0.1929 0.2392 0.0307  0.0499  0.0171  454 ILE   B CD1 
16364 N  N   . ASN   B 455 ? 0.2172 0.2097 0.2391 0.0225  0.0216  0.0092  455 ASN   B N   
16365 C  CA  . ASN   B 455 ? 0.2173 0.2168 0.2428 0.0205  0.0140  0.0057  455 ASN   B CA  
16366 C  C   . ASN   B 455 ? 0.1933 0.2031 0.2348 0.0144  0.0138  0.0039  455 ASN   B C   
16367 O  O   . ASN   B 455 ? 0.2050 0.2289 0.2540 0.0163  0.0095  0.0039  455 ASN   B O   
16368 C  CB  . ASN   B 455 ? 0.2507 0.2385 0.2619 0.0180  0.0107  0.0020  455 ASN   B CB  
16369 C  CG  . ASN   B 455 ? 0.2613 0.2473 0.2627 0.0242  0.0070  0.0023  455 ASN   B CG  
16370 O  OD1 . ASN   B 455 ? 0.2609 0.2501 0.2606 0.0306  0.0085  0.0063  455 ASN   B OD1 
16371 N  ND2 . ASN   B 455 ? 0.2870 0.2665 0.2780 0.0223  0.0031  -0.0023 455 ASN   B ND2 
16378 N  N   . PRO   B 456 ? 0.1916 0.1954 0.2378 0.0071  0.0185  0.0022  456 PRO   B N   
16379 C  CA  . PRO   B 456 ? 0.2437 0.2549 0.2961 0.0006  0.0195  0.0001  456 PRO   B CA  
16380 C  C   . PRO   B 456 ? 0.2002 0.2237 0.2737 0.0026  0.0248  0.0031  456 PRO   B C   
16381 O  O   . PRO   B 456 ? 0.2022 0.2394 0.2875 0.0010  0.0228  0.0019  456 PRO   B O   
16382 C  CB  . PRO   B 456 ? 0.2453 0.2437 0.2962 -0.0069 0.0241  -0.0013 456 PRO   B CB  
16383 C  CG  . PRO   B 456 ? 0.2265 0.2119 0.2650 -0.0029 0.0277  0.0017  456 PRO   B CG  
16384 C  CD  . PRO   B 456 ? 0.2170 0.2038 0.2477 0.0049  0.0228  0.0026  456 PRO   B CD  
16392 N  N   . GLU   B 457 ? 0.2050 0.2212 0.2708 0.0062  0.0314  0.0066  457 GLU   B N   
16393 C  CA  . GLU   B 457 ? 0.1758 0.2010 0.2596 0.0074  0.0384  0.0087  457 GLU   B CA  
16394 C  C   . GLU   B 457 ? 0.2159 0.2506 0.2981 0.0159  0.0361  0.0118  457 GLU   B C   
16395 O  O   . GLU   B 457 ? 0.1955 0.2420 0.2992 0.0170  0.0400  0.0128  457 GLU   B O   
16396 C  CB  . GLU   B 457 ? 0.2116 0.2237 0.2798 0.0068  0.0466  0.0099  457 GLU   B CB  
16397 C  CG  . GLU   B 457 ? 0.1905 0.1944 0.2578 -0.0009 0.0505  0.0085  457 GLU   B CG  
16398 C  CD  . GLU   B 457 ? 0.2320 0.2249 0.2813 -0.0014 0.0579  0.0097  457 GLU   B CD  
16399 O  OE1 . GLU   B 457 ? 0.2029 0.1891 0.2473 0.0019  0.0566  0.0105  457 GLU   B OE1 
16400 O  OE2 . GLU   B 457 ? 0.1820 0.1787 0.2447 -0.0052 0.0650  0.0095  457 GLU   B OE2 
16407 N  N   . ILE   B 458 ? 0.1527 0.1882 0.2374 0.0220  0.0308  0.0136  458 ILE   B N   
16408 C  CA  . ILE   B 458 ? 0.1891 0.2327 0.2715 0.0311  0.0285  0.0179  458 ILE   B CA  
16409 C  C   . ILE   B 458 ? 0.1783 0.2327 0.2623 0.0338  0.0179  0.0176  458 ILE   B C   
16410 O  O   . ILE   B 458 ? 0.1423 0.2122 0.2404 0.0380  0.0144  0.0199  458 ILE   B O   
16411 C  CB  . ILE   B 458 ? 0.1903 0.2240 0.2687 0.0372  0.0333  0.0215  458 ILE   B CB  
16412 C  CG1 . ILE   B 458 ? 0.2078 0.2312 0.2820 0.0341  0.0431  0.0206  458 ILE   B CG1 
16413 C  CG2 . ILE   B 458 ? 0.2303 0.2706 0.3091 0.0467  0.0325  0.0269  458 ILE   B CG2 
16414 C  CD1 . ILE   B 458 ? 0.2127 0.2416 0.3001 0.0372  0.0506  0.0225  458 ILE   B CD1 
16426 N  N   . LEU   B 459 ? 0.1931 0.2402 0.2640 0.0314  0.0124  0.0147  459 LEU   B N   
16427 C  CA  . LEU   B 459 ? 0.2159 0.2707 0.2781 0.0345  0.0026  0.0137  459 LEU   B CA  
16428 C  C   . LEU   B 459 ? 0.1890 0.2548 0.2625 0.0270  -0.0044 0.0074  459 LEU   B C   
16429 O  O   . LEU   B 459 ? 0.2086 0.2849 0.2787 0.0293  -0.0128 0.0063  459 LEU   B O   
16430 C  CB  . LEU   B 459 ? 0.2063 0.2484 0.2550 0.0366  0.0019  0.0136  459 LEU   B CB  
16431 C  CG  . LEU   B 459 ? 0.2415 0.2723 0.2761 0.0431  0.0084  0.0189  459 LEU   B CG  
16432 C  CD1 . LEU   B 459 ? 0.2129 0.2327 0.2367 0.0444  0.0077  0.0179  459 LEU   B CD1 
16433 C  CD2 . LEU   B 459 ? 0.2136 0.2553 0.2607 0.0518  0.0088  0.0254  459 LEU   B CD2 
16445 N  N   . GLY   B 460 ? 0.1768 0.2374 0.2548 0.0181  -0.0007 0.0032  460 GLY   B N   
16446 C  CA  . GLY   B 460 ? 0.1834 0.2519 0.2693 0.0096  -0.0056 -0.0035 460 GLY   B CA  
16447 C  C   . GLY   B 460 ? 0.2309 0.2871 0.2996 0.0046  -0.0097 -0.0093 460 GLY   B C   
16448 O  O   . GLY   B 460 ? 0.2229 0.2872 0.2984 -0.0014 -0.0157 -0.0157 460 GLY   B O   
16452 N  N   . TYR   B 461 ? 0.2436 0.2820 0.2973 0.0068  -0.0062 -0.0080 461 TYR   B N   
16453 C  CA  . TYR   B 461 ? 0.2398 0.2651 0.2799 0.0031  -0.0086 -0.0131 461 TYR   B CA  
16454 C  C   . TYR   B 461 ? 0.2517 0.2603 0.2904 -0.0031 -0.0015 -0.0138 461 TYR   B C   
16455 O  O   . TYR   B 461 ? 0.2464 0.2471 0.2810 0.0001  0.0048  -0.0088 461 TYR   B O   
16456 C  CB  . TYR   B 461 ? 0.2204 0.2400 0.2467 0.0109  -0.0108 -0.0111 461 TYR   B CB  
16457 C  CG  . TYR   B 461 ? 0.2250 0.2580 0.2468 0.0163  -0.0189 -0.0113 461 TYR   B CG  
16458 C  CD1 . TYR   B 461 ? 0.1945 0.2426 0.2279 0.0232  -0.0199 -0.0052 461 TYR   B CD1 
16459 C  CD2 . TYR   B 461 ? 0.2536 0.2860 0.2651 0.0149  -0.0253 -0.0173 461 TYR   B CD2 
16460 C  CE1 . TYR   B 461 ? 0.2433 0.3035 0.2682 0.0289  -0.0274 -0.0044 461 TYR   B CE1 
16461 C  CE2 . TYR   B 461 ? 0.2717 0.3176 0.2783 0.0198  -0.0330 -0.0174 461 TYR   B CE2 
16462 C  CZ  . TYR   B 461 ? 0.2562 0.3173 0.2727 0.0272  -0.0345 -0.0103 461 TYR   B CZ  
16463 O  OH  . TYR   B 461 ? 0.2855 0.3599 0.2944 0.0329  -0.0422 -0.0093 461 TYR   B OH  
16473 N  N   . PRO   B 462 ? 0.2871 0.2888 0.3247 -0.0117 -0.0020 -0.0197 462 PRO   B N   
16474 C  CA  . PRO   B 462 ? 0.2775 0.2905 0.3273 -0.0174 -0.0089 -0.0274 462 PRO   B CA  
16475 C  C   . PRO   B 462 ? 0.3088 0.3391 0.3723 -0.0220 -0.0098 -0.0284 462 PRO   B C   
16476 O  O   . PRO   B 462 ? 0.3080 0.3516 0.3808 -0.0263 -0.0164 -0.0345 462 PRO   B O   
16477 C  CB  . PRO   B 462 ? 0.3215 0.3153 0.3577 -0.0252 -0.0062 -0.0323 462 PRO   B CB  
16478 C  CG  . PRO   B 462 ? 0.2842 0.2673 0.3267 -0.0263 0.0029  -0.0266 462 PRO   B CG  
16479 C  CD  . PRO   B 462 ? 0.3070 0.2908 0.3395 -0.0168 0.0045  -0.0195 462 PRO   B CD  
16487 N  N   . GLU   B 463 ? 0.3019 0.3336 0.3745 -0.0218 -0.0027 -0.0231 463 GLU   B N   
16488 C  CA  . GLU   B 463 ? 0.2455 0.2969 0.3463 -0.0250 -0.0016 -0.0230 463 GLU   B CA  
16489 C  C   . GLU   B 463 ? 0.2648 0.3183 0.3613 -0.0174 0.0038  -0.0154 463 GLU   B C   
16490 O  O   . GLU   B 463 ? 0.2553 0.2956 0.3415 -0.0124 0.0078  -0.0112 463 GLU   B O   
16491 C  CB  . GLU   B 463 ? 0.2955 0.3394 0.3972 -0.0363 0.0043  -0.0263 463 GLU   B CB  
16492 C  CG  . GLU   B 463 ? 0.3161 0.3436 0.4186 -0.0374 0.0145  -0.0216 463 GLU   B CG  
16493 C  CD  . GLU   B 463 ? 0.4538 0.4716 0.5492 -0.0481 0.0215  -0.0235 463 GLU   B CD  
16494 O  OE1 . GLU   B 463 ? 0.4326 0.4675 0.5553 -0.0537 0.0222  -0.0262 463 GLU   B OE1 
16495 O  OE2 . GLU   B 463 ? 0.4370 0.4370 0.5302 -0.0506 0.0265  -0.0219 463 GLU   B OE2 
16502 N  N   . LYS   B 464 ? 0.2471 0.3192 0.3641 -0.0165 0.0043  -0.0139 464 LYS   B N   
16503 C  CA  . LYS   B 464 ? 0.2389 0.3142 0.3629 -0.0099 0.0109  -0.0075 464 LYS   B CA  
16504 C  C   . LYS   B 464 ? 0.2259 0.2946 0.3545 -0.0164 0.0215  -0.0070 464 LYS   B C   
16505 O  O   . LYS   B 464 ? 0.2234 0.3000 0.3652 -0.0244 0.0225  -0.0106 464 LYS   B O   
16506 C  CB  . LYS   B 464 ? 0.2647 0.3613 0.3995 -0.0035 0.0068  -0.0052 464 LYS   B CB  
16507 C  CG  . LYS   B 464 ? 0.2171 0.3171 0.3638 0.0039  0.0140  0.0011  464 LYS   B CG  
16508 C  CD  . LYS   B 464 ? 0.2249 0.3123 0.3566 0.0124  0.0158  0.0061  464 LYS   B CD  
16509 C  CE  . LYS   B 464 ? 0.2667 0.3561 0.3999 0.0201  0.0227  0.0116  464 LYS   B CE  
16510 N  NZ  . LYS   B 464 ? 0.2263 0.3095 0.3691 0.0156  0.0337  0.0112  464 LYS   B NZ  
16524 N  N   . LEU   B 465 ? 0.2198 0.2755 0.3408 -0.0136 0.0291  -0.0030 465 LEU   B N   
16525 C  CA  . LEU   B 465 ? 0.2553 0.3044 0.3738 -0.0190 0.0397  -0.0019 465 LEU   B CA  
16526 C  C   . LEU   B 465 ? 0.2537 0.3117 0.3827 -0.0132 0.0457  0.0014  465 LEU   B C   
16527 O  O   . LEU   B 465 ? 0.2160 0.2795 0.3498 -0.0044 0.0426  0.0042  465 LEU   B O   
16528 C  CB  . LEU   B 465 ? 0.2266 0.2562 0.3328 -0.0206 0.0438  -0.0005 465 LEU   B CB  
16529 C  CG  . LEU   B 465 ? 0.2686 0.2845 0.3569 -0.0248 0.0392  -0.0030 465 LEU   B CG  
16530 C  CD1 . LEU   B 465 ? 0.2586 0.2565 0.3317 -0.0238 0.0427  -0.0003 465 LEU   B CD1 
16531 C  CD2 . LEU   B 465 ? 0.2719 0.2905 0.3723 -0.0350 0.0402  -0.0070 465 LEU   B CD2 
16543 N  N   . ASP   B 466 ? 0.2120 0.2736 0.3567 -0.0179 0.0549  0.0014  466 ASP   B N   
16544 C  CA  . ASP   B 466 ? 0.2195 0.2857 0.3679 -0.0128 0.0627  0.0038  466 ASP   B CA  
16545 C  C   . ASP   B 466 ? 0.2024 0.2527 0.3355 -0.0098 0.0676  0.0059  466 ASP   B C   
16546 O  O   . ASP   B 466 ? 0.1956 0.2342 0.3179 -0.0157 0.0728  0.0054  466 ASP   B O   
16547 C  CB  . ASP   B 466 ? 0.1984 0.2747 0.3701 -0.0191 0.0712  0.0022  466 ASP   B CB  
16548 C  CG  . ASP   B 466 ? 0.2743 0.3509 0.4452 -0.0153 0.0817  0.0036  466 ASP   B CG  
16549 O  OD1 . ASP   B 466 ? 0.2663 0.3405 0.4355 -0.0071 0.0818  0.0059  466 ASP   B OD1 
16550 O  OD2 . ASP   B 466 ? 0.3047 0.3851 0.4854 -0.0207 0.0897  0.0022  466 ASP   B OD2 
16555 N  N   . ARG   B 467 ? 0.2056 0.2547 0.3326 -0.0012 0.0662  0.0083  467 ARG   B N   
16556 C  CA  . ARG   B 467 ? 0.1880 0.2230 0.3010 0.0012  0.0697  0.0094  467 ARG   B CA  
16557 C  C   . ARG   B 467 ? 0.2191 0.2482 0.3241 -0.0019 0.0809  0.0085  467 ARG   B C   
16558 O  O   . ARG   B 467 ? 0.1929 0.2118 0.2897 -0.0027 0.0837  0.0084  467 ARG   B O   
16559 C  CB  . ARG   B 467 ? 0.1617 0.1974 0.2745 0.0106  0.0667  0.0120  467 ARG   B CB  
16560 C  CG  . ARG   B 467 ? 0.1874 0.2339 0.3133 0.0168  0.0702  0.0139  467 ARG   B CG  
16561 C  CD  . ARG   B 467 ? 0.2177 0.2663 0.3464 0.0262  0.0654  0.0178  467 ARG   B CD  
16562 N  NE  . ARG   B 467 ? 0.2997 0.3566 0.4333 0.0333  0.0684  0.0207  467 ARG   B NE  
16563 C  CZ  . ARG   B 467 ? 0.2143 0.2667 0.3599 0.0355  0.0743  0.0211  467 ARG   B CZ  
16564 N  NH1 . ARG   B 467 ? 0.2168 0.2528 0.3418 0.0317  0.0783  0.0186  467 ARG   B NH1 
16565 N  NH2 . ARG   B 467 ? 0.2458 0.3034 0.3942 0.0406  0.0741  0.0235  467 ARG   B NH2 
16579 N  N   . PHE   B 468 ? 0.1648 0.2064 0.2964 -0.0034 0.0874  0.0076  468 PHE   B N   
16580 C  CA  . PHE   B 468 ? 0.2307 0.2636 0.3460 -0.0062 0.0940  0.0057  468 PHE   B CA  
16581 C  C   . PHE   B 468 ? 0.2159 0.2444 0.3275 -0.0151 0.0971  0.0046  468 PHE   B C   
16582 O  O   . PHE   B 468 ? 0.2134 0.2347 0.3146 -0.0172 0.1008  0.0034  468 PHE   B O   
16583 C  CB  . PHE   B 468 ? 0.2086 0.2522 0.3443 -0.0031 0.0963  0.0050  468 PHE   B CB  
16584 C  CG  . PHE   B 468 ? 0.2332 0.2800 0.3743 0.0058  0.0937  0.0070  468 PHE   B CG  
16585 C  CD1 . PHE   B 468 ? 0.2294 0.2645 0.3575 0.0094  0.0939  0.0072  468 PHE   B CD1 
16586 C  CD2 . PHE   B 468 ? 0.2857 0.3472 0.4432 0.0105  0.0904  0.0092  468 PHE   B CD2 
16587 C  CE1 . PHE   B 468 ? 0.2339 0.2699 0.3653 0.0168  0.0920  0.0096  468 PHE   B CE1 
16588 C  CE2 . PHE   B 468 ? 0.3221 0.3843 0.4780 0.0192  0.0879  0.0121  468 PHE   B CE2 
16589 C  CZ  . PHE   B 468 ? 0.2318 0.2823 0.3844 0.0222  0.0891  0.0125  468 PHE   B CZ  
16599 N  N   . ALA   B 469 ? 0.1860 0.2189 0.3065 -0.0201 0.0953  0.0050  469 ALA   B N   
16600 C  CA  . ALA   B 469 ? 0.1943 0.2206 0.3070 -0.0287 0.0980  0.0048  469 ALA   B CA  
16601 C  C   . ALA   B 469 ? 0.1569 0.1680 0.2528 -0.0306 0.0981  0.0066  469 ALA   B C   
16602 O  O   . ALA   B 469 ? 0.1801 0.1843 0.2605 -0.0262 0.0947  0.0076  469 ALA   B O   
16603 C  CB  . ALA   B 469 ? 0.2335 0.2675 0.3592 -0.0344 0.0952  0.0038  469 ALA   B CB  
16609 N  N   . LEU   B 470 ? 0.2162 0.2183 0.2932 -0.0360 0.1012  0.0071  470 LEU   B N   
16610 C  CA  . LEU   B 470 ? 0.2142 0.2031 0.2753 -0.0370 0.1009  0.0096  470 LEU   B CA  
16611 C  C   . LEU   B 470 ? 0.2353 0.2151 0.2886 -0.0431 0.0997  0.0118  470 LEU   B C   
16612 O  O   . LEU   B 470 ? 0.2137 0.1827 0.2573 -0.0425 0.0970  0.0144  470 LEU   B O   
16613 C  CB  . LEU   B 470 ? 0.2302 0.2166 0.2786 -0.0377 0.1054  0.0091  470 LEU   B CB  
16614 C  CG  . LEU   B 470 ? 0.2209 0.2138 0.2763 -0.0329 0.1069  0.0062  470 LEU   B CG  
16615 C  CD1 . LEU   B 470 ? 0.3230 0.3103 0.3567 -0.0346 0.1110  0.0055  470 LEU   B CD1 
16616 C  CD2 . LEU   B 470 ? 0.2360 0.2250 0.2805 -0.0272 0.1025  0.0058  470 LEU   B CD2 
16628 N  N   . ASP   B 471 ? 0.2193 0.2059 0.2909 -0.0486 0.1018  0.0107  471 ASP   B N   
16629 C  CA  . ASP   B 471 ? 0.2661 0.2434 0.3341 -0.0552 0.1013  0.0119  471 ASP   B CA  
16630 C  C   . ASP   B 471 ? 0.2632 0.2351 0.3296 -0.0549 0.0948  0.0113  471 ASP   B C   
16631 O  O   . ASP   B 471 ? 0.2368 0.2208 0.3175 -0.0513 0.0887  0.0082  471 ASP   B O   
16632 C  CB  . ASP   B 471 ? 0.3088 0.2961 0.3970 -0.0615 0.1046  0.0097  471 ASP   B CB  
16633 C  CG  . ASP   B 471 ? 0.4583 0.4440 0.5348 -0.0629 0.1112  0.0109  471 ASP   B CG  
16634 O  OD1 . ASP   B 471 ? 0.4922 0.4667 0.5520 -0.0622 0.1130  0.0145  471 ASP   B OD1 
16635 O  OD2 . ASP   B 471 ? 0.5144 0.5125 0.6055 -0.0643 0.1144  0.0084  471 ASP   B OD2 
16640 N  N   . GLY   B 472 ? 0.2518 0.2082 0.3070 -0.0558 0.0930  0.0142  472 GLY   B N   
16641 C  CA  . GLY   B 472 ? 0.2768 0.2265 0.3238 -0.0535 0.0836  0.0127  472 GLY   B CA  
16642 C  C   . GLY   B 472 ? 0.2561 0.2040 0.2920 -0.0443 0.0770  0.0131  472 GLY   B C   
16643 O  O   . GLY   B 472 ? 0.2259 0.1682 0.2605 -0.0421 0.0701  0.0119  472 GLY   B O   
16647 N  N   . LYS   B 473 ? 0.2172 0.1717 0.2548 -0.0397 0.0796  0.0141  473 LYS   B N   
16648 C  CA  . LYS   B 473 ? 0.2394 0.1919 0.2601 -0.0315 0.0742  0.0143  473 LYS   B CA  
16649 C  C   . LYS   B 473 ? 0.1827 0.1236 0.1980 -0.0290 0.0720  0.0176  473 LYS   B C   
16650 O  O   . LYS   B 473 ? 0.2382 0.1740 0.2387 -0.0239 0.0653  0.0168  473 LYS   B O   
16651 C  CB  . LYS   B 473 ? 0.2051 0.1683 0.2369 -0.0280 0.0785  0.0136  473 LYS   B CB  
16652 C  CG  . LYS   B 473 ? 0.1995 0.1775 0.2481 -0.0273 0.0789  0.0108  473 LYS   B CG  
16653 C  CD  . LYS   B 473 ? 0.2002 0.1843 0.2585 -0.0245 0.0702  0.0088  473 LYS   B CD  
16654 C  CE  . LYS   B 473 ? 0.2168 0.2170 0.2931 -0.0237 0.0699  0.0069  473 LYS   B CE  
16655 N  NZ  . LYS   B 473 ? 0.2343 0.2407 0.3149 -0.0184 0.0744  0.0075  473 LYS   B NZ  
16669 N  N   . ALA   B 474 ? 0.2213 0.1522 0.2185 -0.0321 0.0777  0.0215  474 ALA   B N   
16670 C  CA  . ALA   B 474 ? 0.2574 0.1754 0.2372 -0.0290 0.0760  0.0259  474 ALA   B CA  
16671 C  C   . ALA   B 474 ? 0.2379 0.1460 0.2180 -0.0292 0.0707  0.0258  474 ALA   B C   
16672 O  O   . ALA   B 474 ? 0.2338 0.1364 0.2053 -0.0234 0.0654  0.0264  474 ALA   B O   
16673 C  CB  . ALA   B 474 ? 0.2989 0.2110 0.2671 -0.0323 0.0827  0.0306  474 ALA   B CB  
16679 N  N   . ALA   B 475 ? 0.2373 0.1432 0.2280 -0.0358 0.0727  0.0245  475 ALA   B N   
16680 C  CA  . ALA   B 475 ? 0.2879 0.1820 0.2736 -0.0373 0.0689  0.0231  475 ALA   B CA  
16681 C  C   . ALA   B 475 ? 0.2573 0.1587 0.2514 -0.0326 0.0604  0.0179  475 ALA   B C   
16682 O  O   . ALA   B 475 ? 0.2777 0.1690 0.2631 -0.0292 0.0563  0.0172  475 ALA   B O   
16683 C  CB  . ALA   B 475 ? 0.2910 0.1838 0.2902 -0.0464 0.0735  0.0217  475 ALA   B CB  
16689 N  N   . TYR   B 476 ? 0.2246 0.1419 0.2304 -0.0317 0.0585  0.0138  476 TYR   B N   
16690 C  CA  . TYR   B 476 ? 0.2279 0.1539 0.2426 -0.0272 0.0508  0.0096  476 TYR   B CA  
16691 C  C   . TYR   B 476 ? 0.2800 0.1991 0.2675 -0.0189 0.0476  0.0115  476 TYR   B C   
16692 O  O   . TYR   B 476 ? 0.2243 0.1430 0.2193 -0.0152 0.0422  0.0092  476 TYR   B O   
16693 C  CB  . TYR   B 476 ? 0.3102 0.2516 0.3298 -0.0276 0.0497  0.0065  476 TYR   B CB  
16694 C  CG  . TYR   B 476 ? 0.3155 0.2656 0.3490 -0.0289 0.0430  0.0012  476 TYR   B CG  
16695 C  CD1 . TYR   B 476 ? 0.3374 0.2877 0.3649 -0.0231 0.0359  -0.0009 476 TYR   B CD1 
16696 C  CD2 . TYR   B 476 ? 0.3149 0.2729 0.3636 -0.0364 0.0434  -0.0025 476 TYR   B CD2 
16697 C  CE1 . TYR   B 476 ? 0.3588 0.3163 0.3906 -0.0243 0.0293  -0.0061 476 TYR   B CE1 
16698 C  CE2 . TYR   B 476 ? 0.3511 0.3172 0.4037 -0.0379 0.0365  -0.0080 476 TYR   B CE2 
16699 C  CZ  . TYR   B 476 ? 0.3411 0.3091 0.3950 -0.0318 0.0290  -0.0100 476 TYR   B CZ  
16700 O  OH  . TYR   B 476 ? 0.4436 0.4186 0.4923 -0.0333 0.0216  -0.0158 476 TYR   B OH  
16710 N  N   . ALA   B 477 ? 0.2066 0.1295 0.2012 -0.0163 0.0516  0.0150  477 ALA   B N   
16711 C  CA  . ALA   B 477 ? 0.2258 0.1459 0.2060 -0.0094 0.0493  0.0166  477 ALA   B CA  
16712 C  C   . ALA   B 477 ? 0.2324 0.1391 0.2030 -0.0073 0.0470  0.0187  477 ALA   B C   
16713 O  O   . ALA   B 477 ? 0.2508 0.1557 0.2148 -0.0016 0.0424  0.0174  477 ALA   B O   
16714 C  CB  . ALA   B 477 ? 0.2447 0.1687 0.2205 -0.0086 0.0542  0.0188  477 ALA   B CB  
16720 N  N   . LYS   B 478 ? 0.2545 0.1505 0.2186 -0.0112 0.0504  0.0219  478 LYS   B N   
16721 C  CA  . LYS   B 478 ? 0.2715 0.1529 0.2259 -0.0087 0.0492  0.0248  478 LYS   B CA  
16722 C  C   . LYS   B 478 ? 0.2595 0.1378 0.2201 -0.0080 0.0442  0.0198  478 LYS   B C   
16723 O  O   . LYS   B 478 ? 0.2729 0.1451 0.2243 -0.0021 0.0409  0.0198  478 LYS   B O   
16724 C  CB  . LYS   B 478 ? 0.2839 0.1534 0.2340 -0.0136 0.0546  0.0297  478 LYS   B CB  
16725 C  CG  . LYS   B 478 ? 0.2872 0.1407 0.2307 -0.0106 0.0540  0.0336  478 LYS   B CG  
16726 C  CD  . LYS   B 478 ? 0.3194 0.1628 0.2568 -0.0142 0.0588  0.0389  478 LYS   B CD  
16727 C  CE  . LYS   B 478 ? 0.3305 0.1638 0.2635 -0.0092 0.0565  0.0420  478 LYS   B CE  
16728 N  NZ  . LYS   B 478 ? 0.3497 0.1748 0.2851 -0.0088 0.0537  0.0371  478 LYS   B NZ  
16742 N  N   . LEU   B 479 ? 0.2832 0.1650 0.2519 -0.0137 0.0438  0.0151  479 LEU   B N   
16743 C  CA  . LEU   B 479 ? 0.3133 0.1921 0.2826 -0.0141 0.0389  0.0091  479 LEU   B CA  
16744 C  C   . LEU   B 479 ? 0.2893 0.1763 0.2596 -0.0066 0.0337  0.0070  479 LEU   B C   
16745 O  O   . LEU   B 479 ? 0.2893 0.1686 0.2521 -0.0030 0.0308  0.0049  479 LEU   B O   
16746 C  CB  . LEU   B 479 ? 0.3164 0.2046 0.3051 -0.0216 0.0384  0.0039  479 LEU   B CB  
16747 C  CG  . LEU   B 479 ? 0.4152 0.3082 0.4037 -0.0213 0.0319  -0.0034 479 LEU   B CG  
16748 C  CD1 . LEU   B 479 ? 0.4694 0.3464 0.4494 -0.0220 0.0308  -0.0066 479 LEU   B CD1 
16749 C  CD2 . LEU   B 479 ? 0.4556 0.3620 0.4560 -0.0278 0.0304  -0.0080 479 LEU   B CD2 
16761 N  N   . PHE   B 480 ? 0.3010 0.2006 0.2702 -0.0044 0.0333  0.0074  480 PHE   B N   
16762 C  CA  . PHE   B 480 ? 0.2494 0.1578 0.2250 0.0022  0.0294  0.0062  480 PHE   B CA  
16763 C  C   . PHE   B 480 ? 0.2554 0.1553 0.2154 0.0083  0.0296  0.0089  480 PHE   B C   
16764 O  O   . PHE   B 480 ? 0.2707 0.1693 0.2257 0.0131  0.0266  0.0071  480 PHE   B O   
16765 C  CB  . PHE   B 480 ? 0.3013 0.2225 0.2765 0.0032  0.0302  0.0065  480 PHE   B CB  
16766 C  CG  . PHE   B 480 ? 0.2954 0.2289 0.2853 0.0031  0.0259  0.0029  480 PHE   B CG  
16767 C  CD1 . PHE   B 480 ? 0.3052 0.2417 0.2885 0.0090  0.0220  0.0017  480 PHE   B CD1 
16768 C  CD2 . PHE   B 480 ? 0.3595 0.2983 0.3533 -0.0028 0.0257  0.0006  480 PHE   B CD2 
16769 C  CE1 . PHE   B 480 ? 0.3233 0.2702 0.3118 0.0096  0.0175  -0.0009 480 PHE   B CE1 
16770 C  CE2 . PHE   B 480 ? 0.3592 0.3102 0.3623 -0.0024 0.0207  -0.0025 480 PHE   B CE2 
16771 C  CZ  . PHE   B 480 ? 0.3419 0.2969 0.3409 0.0039  0.0164  -0.0030 480 PHE   B CZ  
16781 N  N   . HIS   B 481 ? 0.2508 0.1468 0.2057 0.0083  0.0332  0.0136  481 HIS   B N   
16782 C  CA  . HIS   B 481 ? 0.2379 0.1293 0.1863 0.0138  0.0331  0.0167  481 HIS   B CA  
16783 C  C   . HIS   B 481 ? 0.2585 0.1369 0.1999 0.0162  0.0312  0.0159  481 HIS   B C   
16784 O  O   . HIS   B 481 ? 0.2559 0.1335 0.1937 0.0222  0.0291  0.0150  481 HIS   B O   
16785 C  CB  . HIS   B 481 ? 0.2439 0.1344 0.1858 0.0128  0.0369  0.0215  481 HIS   B CB  
16786 C  CG  . HIS   B 481 ? 0.2310 0.1335 0.1786 0.0109  0.0396  0.0213  481 HIS   B CG  
16787 N  ND1 . HIS   B 481 ? 0.2314 0.1355 0.1768 0.0077  0.0438  0.0242  481 HIS   B ND1 
16788 C  CD2 . HIS   B 481 ? 0.2367 0.1488 0.1887 0.0118  0.0393  0.0182  481 HIS   B CD2 
16789 C  CE1 . HIS   B 481 ? 0.2468 0.1604 0.1945 0.0066  0.0462  0.0222  481 HIS   B CE1 
16790 N  NE2 . HIS   B 481 ? 0.2225 0.1420 0.1795 0.0095  0.0435  0.0190  481 HIS   B NE2 
16798 N  N   . ASP   B 482 ? 0.2780 0.1462 0.2190 0.0113  0.0327  0.0158  482 ASP   B N   
16799 C  CA  . ASP   B 482 ? 0.2686 0.1228 0.2082 0.0131  0.0321  0.0148  482 ASP   B CA  
16800 C  C   . ASP   B 482 ? 0.2693 0.1248 0.2101 0.0144  0.0283  0.0079  482 ASP   B C   
16801 O  O   . ASP   B 482 ? 0.2820 0.1301 0.2166 0.0198  0.0274  0.0067  482 ASP   B O   
16802 C  CB  . ASP   B 482 ? 0.2776 0.1192 0.2172 0.0071  0.0360  0.0170  482 ASP   B CB  
16803 C  CG  . ASP   B 482 ? 0.2985 0.1364 0.2324 0.0069  0.0402  0.0250  482 ASP   B CG  
16804 O  OD1 . ASP   B 482 ? 0.2994 0.1439 0.2292 0.0121  0.0392  0.0287  482 ASP   B OD1 
16805 O  OD2 . ASP   B 482 ? 0.3001 0.1305 0.2363 0.0010  0.0442  0.0272  482 ASP   B OD2 
16810 N  N   . LEU   B 483 ? 0.2756 0.1408 0.2228 0.0099  0.0263  0.0030  483 LEU   B N   
16811 C  CA  . LEU   B 483 ? 0.3004 0.1677 0.2429 0.0107  0.0222  -0.0037 483 LEU   B CA  
16812 C  C   . LEU   B 483 ? 0.2581 0.1328 0.2005 0.0185  0.0203  -0.0034 483 LEU   B C   
16813 O  O   . LEU   B 483 ? 0.2456 0.1163 0.1836 0.0217  0.0185  -0.0073 483 LEU   B O   
16814 C  CB  . LEU   B 483 ? 0.2769 0.1571 0.2343 0.0048  0.0198  -0.0080 483 LEU   B CB  
16815 C  CG  . LEU   B 483 ? 0.3039 0.1889 0.2577 0.0051  0.0147  -0.0149 483 LEU   B CG  
16816 C  CD1 . LEU   B 483 ? 0.3066 0.1784 0.2577 0.0025  0.0145  -0.0207 483 LEU   B CD1 
16817 C  CD2 . LEU   B 483 ? 0.2987 0.1994 0.2629 0.0008  0.0117  -0.0173 483 LEU   B CD2 
16829 N  N   . THR   B 484 ? 0.2358 0.1204 0.1809 0.0208  0.0213  0.0008  484 THR   B N   
16830 C  CA  . THR   B 484 ? 0.2500 0.1400 0.1891 0.0276  0.0207  0.0016  484 THR   B CA  
16831 C  C   . THR   B 484 ? 0.2507 0.1316 0.1838 0.0327  0.0217  0.0029  484 THR   B C   
16832 O  O   . THR   B 484 ? 0.2396 0.1215 0.1707 0.0376  0.0209  0.0008  484 THR   B O   
16833 C  CB  . THR   B 484 ? 0.2388 0.1399 0.1813 0.0280  0.0226  0.0049  484 THR   B CB  
16834 O  OG1 . THR   B 484 ? 0.2092 0.1188 0.1619 0.0240  0.0217  0.0037  484 THR   B OG1 
16835 C  CG2 . THR   B 484 ? 0.2150 0.1221 0.1585 0.0337  0.0226  0.0054  484 THR   B CG2 
16843 N  N   . ALA   B 485 ? 0.2460 0.1192 0.1784 0.0321  0.0236  0.0068  485 ALA   B N   
16844 C  CA  . ALA   B 485 ? 0.2434 0.1123 0.1763 0.0369  0.0238  0.0087  485 ALA   B CA  
16845 C  C   . ALA   B 485 ? 0.2635 0.1236 0.1892 0.0377  0.0227  0.0038  485 ALA   B C   
16846 O  O   . ALA   B 485 ? 0.2512 0.1154 0.1789 0.0421  0.0221  0.0029  485 ALA   B O   
16847 C  CB  . ALA   B 485 ? 0.3007 0.1637 0.2262 0.0356  0.0254  0.0140  485 ALA   B CB  
16853 N  N   . VAL   B 486 ? 0.2585 0.1090 0.1868 0.0331  0.0229  -0.0002 486 VAL   B N   
16854 C  CA  . VAL   B 486 ? 0.2830 0.1243 0.2051 0.0329  0.0223  -0.0069 486 VAL   B CA  
16855 C  C   . VAL   B 486 ? 0.2615 0.1115 0.1849 0.0368  0.0201  -0.0113 486 VAL   B C   
16856 O  O   . VAL   B 486 ? 0.2834 0.1339 0.2029 0.0404  0.0202  -0.0130 486 VAL   B O   
16857 C  CB  . VAL   B 486 ? 0.2699 0.1048 0.2024 0.0249  0.0225  -0.0115 486 VAL   B CB  
16858 C  CG1 . VAL   B 486 ? 0.3485 0.1757 0.2693 0.0236  0.0211  -0.0203 486 VAL   B CG1 
16859 C  CG2 . VAL   B 486 ? 0.2905 0.1122 0.2187 0.0214  0.0260  -0.0070 486 VAL   B CG2 
16869 N  N   . ILE   B 487 ? 0.2530 0.1150 0.1773 0.0346  0.0178  -0.0125 487 ILE   B N   
16870 C  CA  . ILE   B 487 ? 0.2662 0.1362 0.1849 0.0379  0.0157  -0.0157 487 ILE   B CA  
16871 C  C   . ILE   B 487 ? 0.2533 0.1259 0.1713 0.0451  0.0179  -0.0128 487 ILE   B C   
16872 O  O   . ILE   B 487 ? 0.2566 0.1305 0.1702 0.0479  0.0180  -0.0157 487 ILE   B O   
16873 C  CB  . ILE   B 487 ? 0.2652 0.1493 0.1887 0.0347  0.0130  -0.0158 487 ILE   B CB  
16874 C  CG1 . ILE   B 487 ? 0.2589 0.1434 0.1881 0.0270  0.0104  -0.0196 487 ILE   B CG1 
16875 C  CG2 . ILE   B 487 ? 0.2661 0.1586 0.1852 0.0391  0.0114  -0.0172 487 ILE   B CG2 
16876 C  CD1 . ILE   B 487 ? 0.2648 0.1623 0.2006 0.0237  0.0087  -0.0176 487 ILE   B CD1 
16888 N  N   . ASP   B 488 ? 0.2556 0.1350 0.1760 0.0456  0.0192  -0.0067 488 ASP   B N   
16889 C  CA  . ASP   B 488 ? 0.2226 0.1125 0.1500 0.0485  0.0202  -0.0034 488 ASP   B CA  
16890 C  C   . ASP   B 488 ? 0.2536 0.1380 0.1764 0.0505  0.0206  -0.0047 488 ASP   B C   
16891 O  O   . ASP   B 488 ? 0.2472 0.1371 0.1715 0.0531  0.0212  -0.0057 488 ASP   B O   
16892 C  CB  . ASP   B 488 ? 0.2159 0.1115 0.1457 0.0477  0.0213  0.0014  488 ASP   B CB  
16893 C  CG  . ASP   B 488 ? 0.2270 0.1314 0.1579 0.0471  0.0222  0.0031  488 ASP   B CG  
16894 O  OD1 . ASP   B 488 ? 0.2246 0.1328 0.1554 0.0483  0.0221  0.0013  488 ASP   B OD1 
16895 O  OD2 . ASP   B 488 ? 0.2292 0.1369 0.1632 0.0458  0.0235  0.0059  488 ASP   B OD2 
16900 N  N   . SER   B 489 ? 0.2618 0.1364 0.1850 0.0491  0.0208  -0.0043 489 SER   B N   
16901 C  CA  . SER   B 489 ? 0.2398 0.1105 0.1689 0.0516  0.0217  -0.0046 489 SER   B CA  
16902 C  C   . SER   B 489 ? 0.2453 0.1093 0.1685 0.0522  0.0220  -0.0112 489 SER   B C   
16903 O  O   . SER   B 489 ? 0.2617 0.1248 0.1850 0.0555  0.0233  -0.0119 489 SER   B O   
16904 C  CB  . SER   B 489 ? 0.2791 0.1398 0.2036 0.0504  0.0223  -0.0011 489 SER   B CB  
16905 O  OG  . SER   B 489 ? 0.2540 0.1216 0.1840 0.0504  0.0221  0.0046  489 SER   B OG  
16911 N  N   . LEU   B 490 ? 0.2474 0.1082 0.1680 0.0495  0.0210  -0.0163 490 LEU   B N   
16912 C  CA  . LEU   B 490 ? 0.3037 0.1575 0.2115 0.0495  0.0211  -0.0240 490 LEU   B CA  
16913 C  C   . LEU   B 490 ? 0.2720 0.1368 0.1831 0.0534  0.0216  -0.0248 490 LEU   B C   
16914 O  O   . LEU   B 490 ? 0.2612 0.1229 0.1689 0.0548  0.0227  -0.0293 490 LEU   B O   
16915 C  CB  . LEU   B 490 ? 0.2903 0.1397 0.1994 0.0449  0.0189  -0.0300 490 LEU   B CB  
16916 C  CG  . LEU   B 490 ? 0.2973 0.1342 0.2078 0.0391  0.0192  -0.0319 490 LEU   B CG  
16917 C  CD1 . LEU   B 490 ? 0.3142 0.1505 0.2210 0.0333  0.0161  -0.0375 490 LEU   B CD1 
16918 C  CD2 . LEU   B 490 ? 0.2932 0.1201 0.2053 0.0387  0.0215  -0.0358 490 LEU   B CD2 
16930 N  N   . GLY   B 491 ? 0.2786 0.1538 0.1884 0.0545  0.0209  -0.0206 491 GLY   B N   
16931 C  CA  . GLY   B 491 ? 0.2799 0.1634 0.1862 0.0574  0.0218  -0.0206 491 GLY   B CA  
16932 C  C   . GLY   B 491 ? 0.2699 0.1555 0.1696 0.0576  0.0201  -0.0237 491 GLY   B C   
16933 O  O   . GLY   B 491 ? 0.2807 0.1700 0.1735 0.0599  0.0208  -0.0252 491 GLY   B O   
16937 N  N   . LEU   B 492 ? 0.2656 0.1484 0.1627 0.0551  0.0176  -0.0246 492 LEU   B N   
16938 C  CA  . LEU   B 492 ? 0.2483 0.1356 0.1413 0.0549  0.0146  -0.0272 492 LEU   B CA  
16939 C  C   . LEU   B 492 ? 0.2465 0.1444 0.1440 0.0546  0.0143  -0.0203 492 LEU   B C   
16940 O  O   . LEU   B 492 ? 0.2522 0.1494 0.1559 0.0555  0.0169  -0.0158 492 LEU   B O   
16941 C  CB  . LEU   B 492 ? 0.2628 0.1467 0.1561 0.0482  0.0106  -0.0333 492 LEU   B CB  
16942 C  CG  . LEU   B 492 ? 0.3226 0.1942 0.2036 0.0472  0.0109  -0.0419 492 LEU   B CG  
16943 C  CD1 . LEU   B 492 ? 0.3224 0.1935 0.2087 0.0394  0.0068  -0.0482 492 LEU   B CD1 
16944 C  CD2 . LEU   B 492 ? 0.3096 0.1844 0.1841 0.0520  0.0120  -0.0454 492 LEU   B CD2 
16956 N  N   . CYS   B 493 ? 0.2357 0.1439 0.1343 0.0538  0.0111  -0.0196 493 CYS   B N   
16957 C  CA  . CYS   B 493 ? 0.2576 0.1745 0.1573 0.0543  0.0114  -0.0132 493 CYS   B CA  
16958 C  C   . CYS   B 493 ? 0.2097 0.1318 0.1273 0.0484  0.0086  -0.0126 493 CYS   B C   
16959 O  O   . CYS   B 493 ? 0.2457 0.1669 0.1562 0.0442  0.0043  -0.0174 493 CYS   B O   
16960 C  CB  . CYS   B 493 ? 0.2516 0.1783 0.1494 0.0579  0.0103  -0.0109 493 CYS   B CB  
16961 S  SG  . CYS   B 493 ? 0.2257 0.1631 0.1361 0.0592  0.0121  -0.0031 493 CYS   B SG  
16966 N  N   . ILE   B 494 ? 0.2262 0.1499 0.1468 0.0477  0.0111  -0.0074 494 ILE   B N   
16967 C  CA  . ILE   B 494 ? 0.2307 0.1584 0.1618 0.0423  0.0098  -0.0064 494 ILE   B CA  
16968 C  C   . ILE   B 494 ? 0.2488 0.1875 0.1811 0.0414  0.0053  -0.0069 494 ILE   B C   
16969 O  O   . ILE   B 494 ? 0.2365 0.1790 0.1775 0.0361  0.0029  -0.0086 494 ILE   B O   
16970 C  CB  . ILE   B 494 ? 0.2263 0.1550 0.1624 0.0427  0.0144  -0.0012 494 ILE   B CB  
16971 C  CG1 . ILE   B 494 ? 0.1927 0.1234 0.1419 0.0367  0.0143  -0.0007 494 ILE   B CG1 
16972 C  CG2 . ILE   B 494 ? 0.2251 0.1616 0.1642 0.0469  0.0166  0.0027  494 ILE   B CG2 
16973 C  CD1 . ILE   B 494 ? 0.2414 0.1613 0.1836 0.0324  0.0136  -0.0036 494 ILE   B CD1 
16985 N  N   . PHE   B 495 ? 0.2520 0.1970 0.1796 0.0465  0.0044  -0.0050 495 PHE   B N   
16986 C  CA  . PHE   B 495 ? 0.2281 0.1863 0.1598 0.0473  -0.0002 -0.0040 495 PHE   B CA  
16987 C  C   . PHE   B 495 ? 0.2271 0.1881 0.1567 0.0431  -0.0069 -0.0111 495 PHE   B C   
16988 O  O   . PHE   B 495 ? 0.2238 0.1969 0.1551 0.0427  -0.0121 -0.0113 495 PHE   B O   
16989 C  CB  . PHE   B 495 ? 0.2311 0.1939 0.1567 0.0545  0.0014  0.0015  495 PHE   B CB  
16990 C  CG  . PHE   B 495 ? 0.2204 0.1834 0.1564 0.0575  0.0080  0.0079  495 PHE   B CG  
16991 C  CD1 . PHE   B 495 ? 0.2624 0.2252 0.2027 0.0541  0.0103  0.0097  495 PHE   B CD1 
16992 C  CD2 . PHE   B 495 ? 0.2425 0.2016 0.1667 0.0631  0.0128  0.0122  495 PHE   B CD2 
16993 C  CE1 . PHE   B 495 ? 0.2298 0.1927 0.1807 0.0562  0.0165  0.0142  495 PHE   B CE1 
16994 C  CE2 . PHE   B 495 ? 0.2016 0.1610 0.1384 0.0649  0.0192  0.0167  495 PHE   B CE2 
16995 C  CZ  . PHE   B 495 ? 0.2279 0.1876 0.1713 0.0613  0.0209  0.0176  495 PHE   B CZ  
17005 N  N   . THR   B 496 ? 0.2713 0.2203 0.1903 0.0401  -0.0067 -0.0174 496 THR   B N   
17006 C  CA  . THR   B 496 ? 0.2587 0.2091 0.1802 0.0347  -0.0121 -0.0259 496 THR   B CA  
17007 C  C   . THR   B 496 ? 0.2674 0.2214 0.1998 0.0273  -0.0139 -0.0273 496 THR   B C   
17008 O  O   . THR   B 496 ? 0.2743 0.2325 0.2083 0.0217  -0.0187 -0.0342 496 THR   B O   
17009 C  CB  . THR   B 496 ? 0.2788 0.2136 0.1869 0.0336  -0.0100 -0.0321 496 THR   B CB  
17010 O  OG1 . THR   B 496 ? 0.2658 0.1896 0.1813 0.0329  -0.0046 -0.0295 496 THR   B OG1 
17011 C  CG2 . THR   B 496 ? 0.2680 0.2012 0.1660 0.0402  -0.0087 -0.0326 496 THR   B CG2 
17019 N  N   . THR   B 497 ? 0.2650 0.2180 0.2076 0.0268  -0.0095 -0.0216 497 THR   B N   
17020 C  CA  . THR   B 497 ? 0.2709 0.2277 0.2255 0.0198  -0.0096 -0.0218 497 THR   B CA  
17021 C  C   . THR   B 497 ? 0.2506 0.2266 0.2165 0.0194  -0.0154 -0.0221 497 THR   B C   
17022 O  O   . THR   B 497 ? 0.2615 0.2428 0.2355 0.0131  -0.0166 -0.0244 497 THR   B O   
17023 C  CB  . THR   B 497 ? 0.2808 0.2332 0.2416 0.0201  -0.0032 -0.0156 497 THR   B CB  
17024 O  OG1 . THR   B 497 ? 0.2707 0.2289 0.2323 0.0268  -0.0012 -0.0097 497 THR   B OG1 
17025 C  CG2 . THR   B 497 ? 0.2940 0.2300 0.2496 0.0192  0.0013  -0.0158 497 THR   B CG2 
17033 N  N   . PHE   B 498 ? 0.2768 0.2609 0.2328 0.0263  -0.0183 -0.0192 498 PHE   B N   
17034 C  CA  . PHE   B 498 ? 0.2554 0.2592 0.2208 0.0274  -0.0246 -0.0185 498 PHE   B CA  
17035 C  C   . PHE   B 498 ? 0.2559 0.2647 0.2168 0.0228  -0.0322 -0.0278 498 PHE   B C   
17036 O  O   . PHE   B 498 ? 0.2577 0.2738 0.2074 0.0274  -0.0373 -0.0283 498 PHE   B O   
17037 C  CB  . PHE   B 498 ? 0.2707 0.2800 0.2281 0.0369  -0.0240 -0.0103 498 PHE   B CB  
17038 C  CG  . PHE   B 498 ? 0.2138 0.2218 0.1872 0.0400  -0.0167 -0.0027 498 PHE   B CG  
17039 C  CD1 . PHE   B 498 ? 0.2238 0.2375 0.2081 0.0370  -0.0150 -0.0008 498 PHE   B CD1 
17040 C  CD2 . PHE   B 498 ? 0.2566 0.2533 0.2158 0.0456  -0.0106 0.0020  498 PHE   B CD2 
17041 C  CE1 . PHE   B 498 ? 0.2479 0.2578 0.2366 0.0394  -0.0077 0.0049  498 PHE   B CE1 
17042 C  CE2 . PHE   B 498 ? 0.2639 0.2580 0.2309 0.0474  -0.0038 0.0074  498 PHE   B CE2 
17043 C  CZ  . PHE   B 498 ? 0.2521 0.2527 0.2343 0.0443  -0.0025 0.0088  498 PHE   B CZ  
17053 N  N   . GLY   B 499 ? 0.2892 0.2922 0.2516 0.0137  -0.0326 -0.0353 499 GLY   B N   
17054 C  CA  . GLY   B 499 ? 0.2739 0.2812 0.2380 0.0075  -0.0389 -0.0458 499 GLY   B CA  
17055 C  C   . GLY   B 499 ? 0.3072 0.2947 0.2625 0.0004  -0.0350 -0.0532 499 GLY   B C   
17056 O  O   . GLY   B 499 ? 0.3162 0.3065 0.2786 -0.0080 -0.0385 -0.0623 499 GLY   B O   
17060 N  N   . LEU   B 500 ? 0.2621 0.2329 0.2171 0.0038  -0.0279 -0.0496 500 LEU   B N   
17061 C  CA  . LEU   B 500 ? 0.2807 0.2313 0.2292 -0.0013 -0.0237 -0.0552 500 LEU   B CA  
17062 C  C   . LEU   B 500 ? 0.2893 0.2302 0.2503 -0.0056 -0.0172 -0.0515 500 LEU   B C   
17063 O  O   . LEU   B 500 ? 0.2996 0.2435 0.2616 -0.0020 -0.0143 -0.0429 500 LEU   B O   
17064 C  CB  . LEU   B 500 ? 0.3111 0.2486 0.2406 0.0058  -0.0208 -0.0548 500 LEU   B CB  
17065 C  CG  . LEU   B 500 ? 0.2786 0.2243 0.1998 0.0098  -0.0256 -0.0594 500 LEU   B CG  
17066 C  CD1 . LEU   B 500 ? 0.3028 0.2330 0.2082 0.0150  -0.0211 -0.0604 500 LEU   B CD1 
17067 C  CD2 . LEU   B 500 ? 0.2589 0.2125 0.1799 0.0024  -0.0324 -0.0698 500 LEU   B CD2 
17079 N  N   . GLY   B 501 ? 0.3599 0.2854 0.3149 -0.0129 -0.0145 -0.0570 501 GLY   B N   
17080 C  CA  . GLY   B 501 ? 0.3333 0.2480 0.3010 -0.0168 -0.0078 -0.0532 501 GLY   B CA  
17081 C  C   . GLY   B 501 ? 0.3434 0.2342 0.2993 -0.0166 -0.0026 -0.0546 501 GLY   B C   
17082 O  O   . GLY   B 501 ? 0.3373 0.2234 0.2865 -0.0134 -0.0040 -0.0597 501 GLY   B O   
17086 N  N   . ILE   B 502 ? 0.3032 0.1824 0.2692 -0.0196 0.0037  -0.0504 502 ILE   B N   
17087 C  CA  . ILE   B 502 ? 0.3369 0.1926 0.2920 -0.0180 0.0093  -0.0496 502 ILE   B CA  
17088 C  C   . ILE   B 502 ? 0.3488 0.1949 0.3016 -0.0213 0.0082  -0.0606 502 ILE   B C   
17089 O  O   . ILE   B 502 ? 0.3890 0.2221 0.3295 -0.0153 0.0104  -0.0612 502 ILE   B O   
17090 C  CB  . ILE   B 502 ? 0.3296 0.1752 0.2964 -0.0226 0.0158  -0.0439 502 ILE   B CB  
17091 C  CG1 . ILE   B 502 ? 0.4008 0.2221 0.3510 -0.0187 0.0215  -0.0403 502 ILE   B CG1 
17092 C  CG2 . ILE   B 502 ? 0.3449 0.1923 0.3176 -0.0340 0.0160  -0.0495 502 ILE   B CG2 
17093 C  CD1 . ILE   B 502 ? 0.3700 0.1914 0.3179 -0.0078 0.0216  -0.0341 502 ILE   B CD1 
17105 N  N   . GLN   B 503 ? 0.3471 0.1985 0.3053 -0.0308 0.0054  -0.0698 503 GLN   B N   
17106 C  CA  . GLN   B 503 ? 0.3516 0.1922 0.3055 -0.0355 0.0049  -0.0821 503 GLN   B CA  
17107 C  C   . GLN   B 503 ? 0.3486 0.1951 0.2916 -0.0283 0.0004  -0.0864 503 GLN   B C   
17108 O  O   . GLN   B 503 ? 0.3698 0.2009 0.3025 -0.0268 0.0031  -0.0923 503 GLN   B O   
17109 C  CB  . GLN   B 503 ? 0.3493 0.1974 0.3145 -0.0478 0.0022  -0.0922 503 GLN   B CB  
17110 C  CG  . GLN   B 503 ? 0.3618 0.1981 0.3265 -0.0542 0.0028  -0.1054 503 GLN   B CG  
17111 C  CD  . GLN   B 503 ? 0.4335 0.2397 0.3893 -0.0535 0.0120  -0.1044 503 GLN   B CD  
17112 O  OE1 . GLN   B 503 ? 0.4578 0.2532 0.4225 -0.0565 0.0183  -0.0979 503 GLN   B OE1 
17113 N  NE2 . GLN   B 503 ? 0.4199 0.2162 0.3692 -0.0484 0.0129  -0.1092 503 GLN   B NE2 
17122 N  N   . ASP   B 504 ? 0.3509 0.2178 0.2909 -0.0237 -0.0055 -0.0834 504 ASP   B N   
17123 C  CA  . ASP   B 504 ? 0.3686 0.2417 0.2924 -0.0166 -0.0094 -0.0857 504 ASP   B CA  
17124 C  C   . ASP   B 504 ? 0.3517 0.2105 0.2716 -0.0075 -0.0037 -0.0808 504 ASP   B C   
17125 O  O   . ASP   B 504 ? 0.3704 0.2226 0.2768 -0.0042 -0.0033 -0.0866 504 ASP   B O   
17126 C  CB  . ASP   B 504 ? 0.3351 0.2327 0.2655 -0.0128 -0.0158 -0.0811 504 ASP   B CB  
17127 C  CG  . ASP   B 504 ? 0.3382 0.2527 0.2768 -0.0210 -0.0222 -0.0861 504 ASP   B CG  
17128 O  OD1 . ASP   B 504 ? 0.3561 0.2749 0.2910 -0.0262 -0.0269 -0.0970 504 ASP   B OD1 
17129 O  OD2 . ASP   B 504 ? 0.3205 0.2448 0.2714 -0.0224 -0.0221 -0.0795 504 ASP   B OD2 
17134 N  N   . TYR   B 505 ? 0.3606 0.2135 0.2798 -0.0035 0.0008  -0.0700 505 TYR   B N   
17135 C  CA  . TYR   B 505 ? 0.3251 0.1670 0.2427 0.0052  0.0059  -0.0640 505 TYR   B CA  
17136 C  C   . TYR   B 505 ? 0.3437 0.1635 0.2581 0.0038  0.0110  -0.0695 505 TYR   B C   
17137 O  O   . TYR   B 505 ? 0.3476 0.1581 0.2531 0.0104  0.0138  -0.0706 505 TYR   B O   
17138 C  CB  . TYR   B 505 ? 0.3116 0.1566 0.2313 0.0091  0.0081  -0.0522 505 TYR   B CB  
17139 C  CG  . TYR   B 505 ? 0.2864 0.1517 0.2118 0.0109  0.0042  -0.0474 505 TYR   B CG  
17140 C  CD1 . TYR   B 505 ? 0.3031 0.1763 0.2155 0.0177  0.0020  -0.0467 505 TYR   B CD1 
17141 C  CD2 . TYR   B 505 ? 0.2978 0.1720 0.2303 0.0064  0.0032  -0.0436 505 TYR   B CD2 
17142 C  CE1 . TYR   B 505 ? 0.2503 0.1414 0.1724 0.0199  -0.0007 -0.0421 505 TYR   B CE1 
17143 C  CE2 . TYR   B 505 ? 0.3085 0.1995 0.2422 0.0086  0.0001  -0.0395 505 TYR   B CE2 
17144 C  CZ  . TYR   B 505 ? 0.2809 0.1802 0.2100 0.0157  -0.0019 -0.0384 505 TYR   B CZ  
17145 O  OH  . TYR   B 505 ? 0.2979 0.2122 0.2288 0.0186  -0.0042 -0.0336 505 TYR   B OH  
17155 N  N   . VAL   B 506 ? 0.3846 0.1942 0.3014 -0.0048 0.0129  -0.0725 506 VAL   B N   
17156 C  CA  . VAL   B 506 ? 0.3535 0.1434 0.2808 -0.0071 0.0185  -0.0778 506 VAL   B CA  
17157 C  C   . VAL   B 506 ? 0.3968 0.1862 0.3097 -0.0078 0.0162  -0.0898 506 VAL   B C   
17158 O  O   . VAL   B 506 ? 0.4193 0.2025 0.3318 -0.0022 0.0191  -0.0898 506 VAL   B O   
17159 C  CB  . VAL   B 506 ? 0.4177 0.1978 0.3428 -0.0172 0.0210  -0.0782 506 VAL   B CB  
17160 C  CG1 . VAL   B 506 ? 0.3841 0.1533 0.3213 -0.0192 0.0241  -0.0822 506 VAL   B CG1 
17161 C  CG2 . VAL   B 506 ? 0.3847 0.1656 0.3230 -0.0163 0.0241  -0.0662 506 VAL   B CG2 
17171 N  N   . ASP   B 507 ? 0.3889 0.1909 0.3009 -0.0142 0.0103  -0.0991 507 ASP   B N   
17172 C  CA  . ASP   B 507 ? 0.3969 0.2007 0.2994 -0.0160 0.0074  -0.1121 507 ASP   B CA  
17173 C  C   . ASP   B 507 ? 0.3902 0.1953 0.2826 -0.0046 0.0088  -0.1092 507 ASP   B C   
17174 O  O   . ASP   B 507 ? 0.3849 0.1842 0.2777 -0.0024 0.0115  -0.1140 507 ASP   B O   
17175 C  CB  . ASP   B 507 ? 0.4105 0.2359 0.3141 -0.0225 -0.0012 -0.1189 507 ASP   B CB  
17176 C  CG  . ASP   B 507 ? 0.4169 0.2455 0.3334 -0.0344 -0.0029 -0.1228 507 ASP   B CG  
17177 O  OD1 . ASP   B 507 ? 0.4368 0.2463 0.3591 -0.0396 0.0035  -0.1247 507 ASP   B OD1 
17178 O  OD2 . ASP   B 507 ? 0.3924 0.2429 0.3157 -0.0382 -0.0100 -0.1234 507 ASP   B OD2 
17183 N  N   . MET   B 508 ? 0.3750 0.1902 0.2626 0.0028  0.0071  -0.1004 508 MET   B N   
17184 C  CA  . MET   B 508 ? 0.3624 0.1813 0.2420 0.0126  0.0088  -0.0967 508 MET   B CA  
17185 C  C   . MET   B 508 ? 0.3330 0.1444 0.2264 0.0183  0.0157  -0.0904 508 MET   B C   
17186 O  O   . MET   B 508 ? 0.3921 0.2004 0.2751 0.0220  0.0184  -0.0939 508 MET   B O   
17187 C  CB  . MET   B 508 ? 0.3701 0.2045 0.2459 0.0186  0.0054  -0.0881 508 MET   B CB  
17188 C  CG  . MET   B 508 ? 0.3655 0.2198 0.2397 0.0149  -0.0023 -0.0905 508 MET   B CG  
17189 S  SD  . MET   B 508 ? 0.3594 0.2323 0.2314 0.0220  -0.0051 -0.0780 508 MET   B SD  
17190 C  CE  . MET   B 508 ? 0.2910 0.1680 0.1840 0.0181  -0.0051 -0.0700 508 MET   B CE  
17200 N  N   . TYR   B 509 ? 0.3555 0.1596 0.2520 0.0191  0.0181  -0.0809 509 TYR   B N   
17201 C  CA  . TYR   B 509 ? 0.3738 0.1713 0.2768 0.0249  0.0230  -0.0734 509 TYR   B CA  
17202 C  C   . TYR   B 509 ? 0.3700 0.1569 0.2806 0.0229  0.0259  -0.0811 509 TYR   B C   
17203 O  O   . TYR   B 509 ? 0.3976 0.1824 0.3040 0.0287  0.0286  -0.0808 509 TYR   B O   
17204 C  CB  . TYR   B 509 ? 0.3698 0.1640 0.2817 0.0247  0.0243  -0.0629 509 TYR   B CB  
17205 C  CG  . TYR   B 509 ? 0.3698 0.1597 0.2885 0.0307  0.0279  -0.0547 509 TYR   B CG  
17206 C  CD1 . TYR   B 509 ? 0.3742 0.1505 0.2970 0.0291  0.0309  -0.0554 509 TYR   B CD1 
17207 C  CD2 . TYR   B 509 ? 0.3792 0.1786 0.2980 0.0379  0.0280  -0.0462 509 TYR   B CD2 
17208 C  CE1 . TYR   B 509 ? 0.3662 0.1390 0.2937 0.0352  0.0335  -0.0481 509 TYR   B CE1 
17209 C  CE2 . TYR   B 509 ? 0.3881 0.1848 0.3097 0.0432  0.0303  -0.0396 509 TYR   B CE2 
17210 C  CZ  . TYR   B 509 ? 0.3499 0.1343 0.2815 0.0422  0.0331  -0.0402 509 TYR   B CZ  
17211 O  OH  . TYR   B 509 ? 0.3608 0.1420 0.2929 0.0482  0.0348  -0.0334 509 TYR   B OH  
17221 N  N   . ASN   B 510 ? 0.4036 0.1808 0.3120 0.0145  0.0253  -0.0878 510 ASN   B N   
17222 C  CA  . ASN   B 510 ? 0.3996 0.1645 0.3145 0.0122  0.0279  -0.0949 510 ASN   B CA  
17223 C  C   . ASN   B 510 ? 0.4276 0.1947 0.3312 0.0135  0.0271  -0.1061 510 ASN   B C   
17224 O  O   . ASN   B 510 ? 0.4301 0.1893 0.3380 0.0173  0.0306  -0.1083 510 ASN   B O   
17225 C  CB  . ASN   B 510 ? 0.3975 0.1536 0.3189 0.0022  0.0277  -0.0982 510 ASN   B CB  
17226 C  CG  . ASN   B 510 ? 0.4411 0.1882 0.3645 0.0021  0.0309  -0.0869 510 ASN   B CG  
17227 O  OD1 . ASN   B 510 ? 0.4146 0.1630 0.3447 0.0100  0.0331  -0.0764 510 ASN   B OD1 
17228 N  ND2 . ASN   B 510 ? 0.4337 0.1764 0.3663 -0.0071 0.0312  -0.0884 510 ASN   B ND2 
17235 N  N   . ALA   B 511 ? 0.3961 0.1764 0.2964 0.0108  0.0227  -0.1132 511 ALA   B N   
17236 C  CA  . ALA   B 511 ? 0.4223 0.2076 0.3107 0.0120  0.0216  -0.1235 511 ALA   B CA  
17237 C  C   . ALA   B 511 ? 0.4329 0.2198 0.3182 0.0216  0.0261  -0.1182 511 ALA   B C   
17238 O  O   . ALA   B 511 ? 0.4316 0.2151 0.3176 0.0237  0.0286  -0.1252 511 ALA   B O   
17239 C  CB  . ALA   B 511 ? 0.4356 0.2355 0.3138 0.0080  0.0156  -0.1295 511 ALA   B CB  
17245 N  N   . VAL   B 512 ? 0.3906 0.1857 0.2840 0.0271  0.0271  -0.1061 512 VAL   B N   
17246 C  CA  . VAL   B 512 ? 0.4322 0.2302 0.3165 0.0356  0.0306  -0.0999 512 VAL   B CA  
17247 C  C   . VAL   B 512 ? 0.4108 0.1998 0.3115 0.0402  0.0349  -0.0944 512 VAL   B C   
17248 O  O   . VAL   B 512 ? 0.4081 0.1956 0.3088 0.0450  0.0384  -0.0966 512 VAL   B O   
17249 C  CB  . VAL   B 512 ? 0.3826 0.1958 0.2746 0.0395  0.0289  -0.0900 512 VAL   B CB  
17250 C  CG1 . VAL   B 512 ? 0.4106 0.2273 0.2983 0.0472  0.0324  -0.0831 512 VAL   B CG1 
17251 C  CG2 . VAL   B 512 ? 0.4267 0.2487 0.2995 0.0367  0.0247  -0.0942 512 VAL   B CG2 
17261 N  N   . VAL   B 513 ? 0.4109 0.1929 0.3185 0.0390  0.0348  -0.0870 513 VAL   B N   
17262 C  CA  . VAL   B 513 ? 0.4110 0.1845 0.3260 0.0441  0.0381  -0.0793 513 VAL   B CA  
17263 C  C   . VAL   B 513 ? 0.4353 0.1916 0.3517 0.0416  0.0407  -0.0855 513 VAL   B C   
17264 O  O   . VAL   B 513 ? 0.4048 0.1558 0.3300 0.0472  0.0440  -0.0842 513 VAL   B O   
17265 C  CB  . VAL   B 513 ? 0.3590 0.1370 0.2875 0.0450  0.0370  -0.0667 513 VAL   B CB  
17266 C  CG1 . VAL   B 513 ? 0.4488 0.2162 0.3731 0.0496  0.0396  -0.0592 513 VAL   B CG1 
17267 C  CG2 . VAL   B 513 ? 0.3695 0.1615 0.2873 0.0482  0.0348  -0.0606 513 VAL   B CG2 
17277 N  N   . GLY   B 514 ? 0.4198 0.1703 0.3411 0.0335  0.0391  -0.0920 514 GLY   B N   
17278 C  CA  . GLY   B 514 ? 0.4573 0.1893 0.3765 0.0300  0.0417  -0.0970 514 GLY   B CA  
17279 C  C   . GLY   B 514 ? 0.4407 0.1676 0.3667 0.0202  0.0401  -0.0995 514 GLY   B C   
17280 O  O   . GLY   B 514 ? 0.4285 0.1593 0.3552 0.0186  0.0387  -0.0911 514 GLY   B O   
17284 N  N   . GLU   B 515 ? 0.4890 0.2049 0.4091 0.0135  0.0405  -0.1105 515 GLU   B N   
17285 C  CA  . GLU   B 515 ? 0.4980 0.2108 0.4273 0.0025  0.0391  -0.1146 515 GLU   B CA  
17286 C  C   . GLU   B 515 ? 0.5116 0.2148 0.4438 0.0014  0.0423  -0.1030 515 GLU   B C   
17287 O  O   . GLU   B 515 ? 0.5172 0.2099 0.4531 0.0074  0.0468  -0.0962 515 GLU   B O   
17288 C  CB  . GLU   B 515 ? 0.5998 0.3012 0.5218 -0.0041 0.0399  -0.1280 515 GLU   B CB  
17289 C  CG  . GLU   B 515 ? 0.6986 0.3967 0.6220 -0.0166 0.0386  -0.1340 515 GLU   B CG  
17290 C  CD  . GLU   B 515 ? 0.7605 0.4460 0.6826 -0.0238 0.0409  -0.1461 515 GLU   B CD  
17291 O  OE1 . GLU   B 515 ? 0.7004 0.3763 0.6265 -0.0183 0.0450  -0.1486 515 GLU   B OE1 
17292 O  OE2 . GLU   B 515 ? 0.8185 0.5058 0.7432 -0.0351 0.0387  -0.1533 515 GLU   B OE2 
17299 N  N   . SER   B 516 ? 0.5141 0.2226 0.4506 -0.0055 0.0403  -0.1001 516 SER   B N   
17300 C  CA  . SER   B 516 ? 0.5369 0.2365 0.4760 -0.0079 0.0437  -0.0897 516 SER   B CA  
17301 C  C   . SER   B 516 ? 0.5064 0.2080 0.4514 0.0024  0.0456  -0.0752 516 SER   B C   
17302 O  O   . SER   B 516 ? 0.5301 0.2219 0.4769 0.0022  0.0493  -0.0664 516 SER   B O   
17303 C  CB  . SER   B 516 ? 0.5192 0.2036 0.4719 -0.0139 0.0484  -0.0942 516 SER   B CB  
17304 O  OG  . SER   B 516 ? 0.6230 0.3048 0.5635 -0.0222 0.0465  -0.1084 516 SER   B OG  
17310 N  N   . THR   B 517 ? 0.4809 0.1939 0.4205 0.0105  0.0432  -0.0721 517 THR   B N   
17311 C  CA  . THR   B 517 ? 0.4538 0.1717 0.3980 0.0193  0.0440  -0.0589 517 THR   B CA  
17312 C  C   . THR   B 517 ? 0.4900 0.2108 0.4297 0.0160  0.0433  -0.0499 517 THR   B C   
17313 O  O   . THR   B 517 ? 0.4557 0.1725 0.4028 0.0190  0.0457  -0.0396 517 THR   B O   
17314 C  CB  . THR   B 517 ? 0.4588 0.1896 0.3995 0.0276  0.0419  -0.0581 517 THR   B CB  
17315 O  OG1 . THR   B 517 ? 0.5003 0.2255 0.4344 0.0301  0.0434  -0.0667 517 THR   B OG1 
17316 C  CG2 . THR   B 517 ? 0.4890 0.2244 0.4271 0.0358  0.0423  -0.0457 517 THR   B CG2 
17324 N  N   . TYR   B 518 ? 0.4945 0.2250 0.4344 0.0100  0.0400  -0.0537 518 TYR   B N   
17325 C  CA  . TYR   B 518 ? 0.4692 0.2055 0.4126 0.0063  0.0394  -0.0466 518 TYR   B CA  
17326 C  C   . TYR   B 518 ? 0.4783 0.2134 0.4229 -0.0054 0.0387  -0.0543 518 TYR   B C   
17327 O  O   . TYR   B 518 ? 0.4570 0.1922 0.4026 -0.0099 0.0368  -0.0662 518 TYR   B O   
17328 C  CB  . TYR   B 518 ? 0.4476 0.1991 0.3857 0.0113  0.0361  -0.0416 518 TYR   B CB  
17329 C  CG  . TYR   B 518 ? 0.4084 0.1650 0.3487 0.0196  0.0367  -0.0295 518 TYR   B CG  
17330 C  CD1 . TYR   B 518 ? 0.3977 0.1523 0.3384 0.0185  0.0384  -0.0198 518 TYR   B CD1 
17331 C  CD2 . TYR   B 518 ? 0.4192 0.1825 0.3543 0.0282  0.0355  -0.0274 518 TYR   B CD2 
17332 C  CE1 . TYR   B 518 ? 0.3931 0.1532 0.3327 0.0256  0.0383  -0.0097 518 TYR   B CE1 
17333 C  CE2 . TYR   B 518 ? 0.4054 0.1750 0.3422 0.0349  0.0354  -0.0175 518 TYR   B CE2 
17334 C  CZ  . TYR   B 518 ? 0.3925 0.1606 0.3310 0.0338  0.0365  -0.0085 518 TYR   B CZ  
17335 O  OH  . TYR   B 518 ? 0.3943 0.1690 0.3317 0.0400  0.0358  0.0004  518 TYR   B OH  
17345 N  N   . ASP   B 519 ? 0.4847 0.2205 0.4324 -0.0106 0.0400  -0.0485 519 ASP   B N   
17346 C  CA  . ASP   B 519 ? 0.4461 0.1867 0.4046 -0.0223 0.0390  -0.0551 519 ASP   B CA  
17347 C  C   . ASP   B 519 ? 0.4445 0.1963 0.3978 -0.0223 0.0369  -0.0501 519 ASP   B C   
17348 O  O   . ASP   B 519 ? 0.4190 0.1747 0.3711 -0.0143 0.0374  -0.0396 519 ASP   B O   
17349 C  CB  . ASP   B 519 ? 0.4861 0.2138 0.4478 -0.0305 0.0436  -0.0561 519 ASP   B CB  
17350 C  CG  . ASP   B 519 ? 0.5263 0.2478 0.4881 -0.0297 0.0485  -0.0435 519 ASP   B CG  
17351 O  OD1 . ASP   B 519 ? 0.4802 0.2102 0.4441 -0.0239 0.0477  -0.0342 519 ASP   B OD1 
17352 O  OD2 . ASP   B 519 ? 0.5507 0.2613 0.5190 -0.0349 0.0531  -0.0430 519 ASP   B OD2 
17357 N  N   . ALA   B 520 ? 0.3970 0.1797 0.3951 -0.0086 0.0148  -0.0806 520 ALA   B N   
17358 C  CA  . ALA   B 520 ? 0.4021 0.2079 0.4044 -0.0116 0.0150  -0.0727 520 ALA   B CA  
17359 C  C   . ALA   B 520 ? 0.3769 0.1762 0.3868 -0.0148 0.0277  -0.0557 520 ALA   B C   
17360 O  O   . ALA   B 520 ? 0.3999 0.2121 0.3993 -0.0092 0.0300  -0.0441 520 ALA   B O   
17361 C  CB  . ALA   B 520 ? 0.3357 0.1581 0.3669 -0.0233 0.0087  -0.0838 520 ALA   B CB  
17367 N  N   . ASP   B 521 ? 0.3769 0.1537 0.3940 -0.0231 0.0360  -0.0542 521 ASP   B N   
17368 C  CA  . ASP   B 521 ? 0.4061 0.1752 0.4249 -0.0260 0.0486  -0.0383 521 ASP   B CA  
17369 C  C   . ASP   B 521 ? 0.4144 0.1761 0.4048 -0.0123 0.0528  -0.0255 521 ASP   B C   
17370 O  O   . ASP   B 521 ? 0.3741 0.1490 0.3656 -0.0096 0.0568  -0.0134 521 ASP   B O   
17371 C  CB  . ASP   B 521 ? 0.4710 0.2194 0.5024 -0.0369 0.0562  -0.0387 521 ASP   B CB  
17372 C  CG  . ASP   B 521 ? 0.5356 0.2976 0.5902 -0.0512 0.0568  -0.0419 521 ASP   B CG  
17373 O  OD1 . ASP   B 521 ? 0.5411 0.3208 0.6079 -0.0551 0.0492  -0.0522 521 ASP   B OD1 
17374 O  OD2 . ASP   B 521 ? 0.5712 0.3288 0.6329 -0.0574 0.0645  -0.0339 521 ASP   B OD2 
17379 N  N   . SER   B 522 ? 0.3828 0.1287 0.3673 -0.0037 0.0519  -0.0286 522 SER   B N   
17380 C  CA  . SER   B 522 ? 0.4410 0.1783 0.3937 0.0100  0.0560  -0.0172 522 SER   B CA  
17381 C  C   . SER   B 522 ? 0.3781 0.1436 0.3306 0.0187  0.0502  -0.0128 522 SER   B C   
17382 O  O   . SER   B 522 ? 0.3775 0.1477 0.3186 0.0254  0.0546  -0.0003 522 SER   B O   
17383 C  CB  . SER   B 522 ? 0.4095 0.1271 0.3618 0.0174  0.0557  -0.0228 522 SER   B CB  
17384 O  OG  . SER   B 522 ? 0.4247 0.1432 0.3730 0.0184  0.0463  -0.0389 522 SER   B OG  
17390 N  N   . LEU   B 523 ? 0.3574 0.1389 0.3108 0.0190  0.0407  -0.0231 523 LEU   B N   
17391 C  CA  . LEU   B 523 ? 0.3542 0.1583 0.2977 0.0276  0.0359  -0.0195 523 LEU   B CA  
17392 C  C   . LEU   B 523 ? 0.3426 0.1639 0.2942 0.0219  0.0390  -0.0102 523 LEU   B C   
17393 O  O   . LEU   B 523 ? 0.3274 0.1590 0.2732 0.0281  0.0411  -0.0003 523 LEU   B O   
17394 C  CB  . LEU   B 523 ? 0.3252 0.1418 0.2705 0.0302  0.0259  -0.0319 523 LEU   B CB  
17395 C  CG  . LEU   B 523 ? 0.3288 0.1640 0.2626 0.0415  0.0221  -0.0284 523 LEU   B CG  
17396 C  CD1 . LEU   B 523 ? 0.3432 0.1705 0.2596 0.0533  0.0263  -0.0206 523 LEU   B CD1 
17397 C  CD2 . LEU   B 523 ? 0.3476 0.1923 0.2772 0.0451  0.0126  -0.0402 523 LEU   B CD2 
17409 N  N   . LEU   B 524 ? 0.3208 0.1467 0.2928 0.0101  0.0392  -0.0138 524 LEU   B N   
17410 C  CA  . LEU   B 524 ? 0.3577 0.1971 0.3329 0.0046  0.0428  -0.0064 524 LEU   B CA  
17411 C  C   . LEU   B 524 ? 0.3084 0.1405 0.2858 0.0056  0.0521  0.0065  524 LEU   B C   
17412 O  O   . LEU   B 524 ? 0.3237 0.1673 0.2914 0.0076  0.0543  0.0143  524 LEU   B O   
17413 C  CB  . LEU   B 524 ? 0.3812 0.2271 0.3798 -0.0076 0.0415  -0.0135 524 LEU   B CB  
17414 C  CG  . LEU   B 524 ? 0.4218 0.2894 0.4264 -0.0078 0.0337  -0.0198 524 LEU   B CG  
17415 C  CD1 . LEU   B 524 ? 0.4645 0.3383 0.4894 -0.0195 0.0327  -0.0271 524 LEU   B CD1 
17416 C  CD2 . LEU   B 524 ? 0.3823 0.2664 0.3848 -0.0028 0.0350  -0.0109 524 LEU   B CD2 
17428 N  N   . GLU   B 525 ? 0.3675 0.1753 0.3316 0.0054  0.0578  0.0086  525 GLU   B N   
17429 C  CA  . GLU   B 525 ? 0.3469 0.1467 0.3088 0.0088  0.0668  0.0215  525 GLU   B CA  
17430 C  C   . GLU   B 525 ? 0.3446 0.1517 0.2851 0.0214  0.0648  0.0283  525 GLU   B C   
17431 O  O   . GLU   B 525 ? 0.3229 0.1371 0.2609 0.0244  0.0688  0.0383  525 GLU   B O   
17432 C  CB  . GLU   B 525 ? 0.3914 0.1648 0.3507 0.0070  0.0736  0.0231  525 GLU   B CB  
17433 C  CG  . GLU   B 525 ? 0.4463 0.2195 0.3962 0.0128  0.0794  0.0353  525 GLU   B CG  
17434 C  CD  . GLU   B 525 ? 0.4997 0.2556 0.4499 0.0103  0.0848  0.0369  525 GLU   B CD  
17435 O  OE1 . GLU   B 525 ? 0.4921 0.2347 0.4379 0.0166  0.0838  0.0347  525 GLU   B OE1 
17436 O  OE2 . GLU   B 525 ? 0.5159 0.2726 0.4767 0.0024  0.0903  0.0403  525 GLU   B OE2 
17443 N  N   . ALA   B 526 ? 0.3169 0.1258 0.2534 0.0291  0.0585  0.0226  526 ALA   B N   
17444 C  CA  . ALA   B 526 ? 0.3115 0.1301 0.2348 0.0412  0.0568  0.0281  526 ALA   B CA  
17445 C  C   . ALA   B 526 ? 0.2784 0.1219 0.2076 0.0396  0.0542  0.0313  526 ALA   B C   
17446 O  O   . ALA   B 526 ? 0.2964 0.1485 0.2158 0.0451  0.0558  0.0393  526 ALA   B O   
17447 C  CB  . ALA   B 526 ? 0.3432 0.1574 0.2574 0.0494  0.0519  0.0212  526 ALA   B CB  
17453 N  N   . GLY   B 527 ? 0.2854 0.1382 0.2203 0.0324  0.0505  0.0247  527 GLY   B N   
17454 C  CA  . GLY   B 527 ? 0.2504 0.1243 0.1946 0.0304  0.0492  0.0275  527 GLY   B CA  
17455 C  C   . GLY   B 527 ? 0.2677 0.1426 0.2082 0.0263  0.0548  0.0351  527 GLY   B C   
17456 O  O   . GLY   B 527 ? 0.2530 0.1417 0.1939 0.0289  0.0550  0.0400  527 GLY   B O   
17460 N  N   . ASP   B 528 ? 0.2498 0.1131 0.1993 0.0201  0.0601  0.0363  528 ASP   B N   
17461 C  CA  . ASP   B 528 ? 0.2918 0.1541 0.2363 0.0175  0.0669  0.0444  528 ASP   B CA  
17462 C  C   . ASP   B 528 ? 0.3020 0.1630 0.2291 0.0272  0.0685  0.0527  528 ASP   B C   
17463 O  O   . ASP   B 528 ? 0.2844 0.1611 0.2136 0.0282  0.0683  0.0562  528 ASP   B O   
17464 C  CB  . ASP   B 528 ? 0.3130 0.1599 0.2645 0.0099  0.0734  0.0449  528 ASP   B CB  
17465 C  CG  . ASP   B 528 ? 0.3210 0.1729 0.2723 0.0066  0.0795  0.0510  528 ASP   B CG  
17466 O  OD1 . ASP   B 528 ? 0.2849 0.1503 0.2318 0.0115  0.0783  0.0550  528 ASP   B OD1 
17467 O  OD2 . ASP   B 528 ? 0.3285 0.1752 0.2904 -0.0007 0.0838  0.0500  528 ASP   B OD2 
17472 N  N   A ARG   B 529 ? 0.2821 0.1315 0.2078 0.0342  0.0685  0.0536  529 ARG   B N   
17473 N  N   B ARG   B 529 ? 0.2821 0.1315 0.2078 0.0341  0.0685  0.0536  529 ARG   B N   
17474 C  CA  A ARG   B 529 ? 0.3175 0.1727 0.2296 0.0439  0.0675  0.0585  529 ARG   B CA  
17475 C  CA  B ARG   B 529 ? 0.3175 0.1727 0.2296 0.0438  0.0675  0.0585  529 ARG   B CA  
17476 C  C   A ARG   B 529 ? 0.2965 0.1728 0.2074 0.0481  0.0625  0.0591  529 ARG   B C   
17477 C  C   B ARG   B 529 ? 0.2965 0.1728 0.2074 0.0481  0.0625  0.0591  529 ARG   B C   
17478 O  O   A ARG   B 529 ? 0.2843 0.1749 0.1947 0.0511  0.0615  0.0624  529 ARG   B O   
17479 O  O   B ARG   B 529 ? 0.2843 0.1748 0.1947 0.0511  0.0616  0.0624  529 ARG   B O   
17480 C  CB  A ARG   B 529 ? 0.3510 0.1907 0.2563 0.0509  0.0676  0.0575  529 ARG   B CB  
17481 C  CB  B ARG   B 529 ? 0.3510 0.1907 0.2563 0.0509  0.0677  0.0576  529 ARG   B CB  
17482 C  CG  A ARG   B 529 ? 0.3517 0.2011 0.2508 0.0619  0.0659  0.0612  529 ARG   B CG  
17483 C  CG  B ARG   B 529 ? 0.3517 0.2011 0.2508 0.0619  0.0659  0.0612  529 ARG   B CG  
17484 C  CD  A ARG   B 529 ? 0.3637 0.1971 0.2595 0.0686  0.0677  0.0606  529 ARG   B CD  
17485 C  CD  B ARG   B 529 ? 0.3637 0.1971 0.2595 0.0686  0.0677  0.0606  529 ARG   B CD  
17486 N  NE  A ARG   B 529 ? 0.4468 0.2634 0.3319 0.0681  0.0658  0.0530  529 ARG   B NE  
17487 N  NE  B ARG   B 529 ? 0.4468 0.2634 0.3319 0.0680  0.0658  0.0530  529 ARG   B NE  
17488 C  CZ  A ARG   B 529 ? 0.3648 0.1632 0.2678 0.0624  0.0679  0.0477  529 ARG   B CZ  
17489 C  CZ  B ARG   B 529 ? 0.3648 0.1632 0.2678 0.0624  0.0679  0.0477  529 ARG   B CZ  
17490 N  NH1 A ARG   B 529 ? 0.4141 0.2024 0.3134 0.0553  0.0731  0.0508  529 ARG   B NH1 
17491 N  NH1 B ARG   B 529 ? 0.4141 0.2023 0.3133 0.0553  0.0731  0.0508  529 ARG   B NH1 
17492 N  NH2 A ARG   B 529 ? 0.3617 0.1475 0.2581 0.0637  0.0647  0.0386  529 ARG   B NH2 
17493 N  NH2 B ARG   B 529 ? 0.3617 0.1475 0.2581 0.0637  0.0648  0.0387  529 ARG   B NH2 
17520 N  N   . ILE   B 530 ? 0.2656 0.1455 0.1814 0.0481  0.0592  0.0550  530 ILE   B N   
17521 C  CA  . ILE   B 530 ? 0.2327 0.1329 0.1514 0.0516  0.0552  0.0551  530 ILE   B CA  
17522 C  C   . ILE   B 530 ? 0.2320 0.1468 0.1559 0.0450  0.0554  0.0561  530 ILE   B C   
17523 O  O   . ILE   B 530 ? 0.2511 0.1807 0.1724 0.0473  0.0534  0.0577  530 ILE   B O   
17524 C  CB  . ILE   B 530 ? 0.2557 0.1587 0.1753 0.0528  0.0510  0.0487  530 ILE   B CB  
17525 C  CG1 . ILE   B 530 ? 0.2743 0.1656 0.1862 0.0616  0.0502  0.0469  530 ILE   B CG1 
17526 C  CG2 . ILE   B 530 ? 0.2724 0.1946 0.1952 0.0537  0.0488  0.0497  530 ILE   B CG2 
17527 C  CD1 . ILE   B 530 ? 0.2970 0.1849 0.2086 0.0618  0.0465  0.0387  530 ILE   B CD1 
17540 N  N   . TRP   B 531 ? 0.2561 0.1675 0.1827 0.0362  0.0568  0.0529  531 TRP   B N   
17541 C  CA  . TRP   B 531 ? 0.2298 0.1536 0.1656 0.0303  0.0580  0.0530  531 TRP   B CA  
17542 C  C   . TRP   B 531 ? 0.2308 0.1576 0.1587 0.0320  0.0591  0.0567  531 TRP   B C   
17543 O  O   . TRP   B 531 ? 0.2230 0.1641 0.1522 0.0318  0.0572  0.0568  531 TRP   B O   
17544 C  CB  . TRP   B 531 ? 0.2392 0.1594 0.1819 0.0215  0.0597  0.0485  531 TRP   B CB  
17545 C  CG  . TRP   B 531 ? 0.2320 0.1629 0.1809 0.0163  0.0614  0.0479  531 TRP   B CG  
17546 C  CD1 . TRP   B 531 ? 0.2540 0.1859 0.1988 0.0140  0.0647  0.0499  531 TRP   B CD1 
17547 C  CD2 . TRP   B 531 ? 0.2078 0.1505 0.1677 0.0136  0.0591  0.0439  531 TRP   B CD2 
17548 N  NE1 . TRP   B 531 ? 0.2472 0.1897 0.1987 0.0099  0.0649  0.0471  531 TRP   B NE1 
17549 C  CE2 . TRP   B 531 ? 0.2408 0.1880 0.1968 0.0094  0.0622  0.0439  531 TRP   B CE2 
17550 C  CE3 . TRP   B 531 ? 0.2073 0.1548 0.1703 0.0151  0.0554  0.0408  531 TRP   B CE3 
17551 C  CZ2 . TRP   B 531 ? 0.2173 0.1740 0.1840 0.0062  0.0619  0.0404  531 TRP   B CZ2 
17552 C  CZ3 . TRP   B 531 ? 0.2054 0.1621 0.1759 0.0123  0.0554  0.0387  531 TRP   B CZ3 
17553 C  CH2 . TRP   B 531 ? 0.2019 0.1625 0.1752 0.0079  0.0586  0.0381  531 TRP   B CH2 
17564 N  N   . THR   B 532 ? 0.2316 0.1463 0.1560 0.0336  0.0621  0.0595  532 THR   B N   
17565 C  CA  . THR   B 532 ? 0.2538 0.1710 0.1719 0.0366  0.0634  0.0636  532 THR   B CA  
17566 C  C   . THR   B 532 ? 0.2496 0.1778 0.1602 0.0450  0.0592  0.0657  532 THR   B C   
17567 O  O   . THR   B 532 ? 0.2166 0.1574 0.1276 0.0462  0.0574  0.0669  532 THR   B O   
17568 C  CB  . THR   B 532 ? 0.2998 0.1988 0.2105 0.0362  0.0689  0.0664  532 THR   B CB  
17569 O  OG1 . THR   B 532 ? 0.2874 0.1801 0.2112 0.0274  0.0724  0.0636  532 THR   B OG1 
17570 C  CG2 . THR   B 532 ? 0.2683 0.1708 0.1776 0.0400  0.0711  0.0714  532 THR   B CG2 
17578 N  N   . LEU   B 533 ? 0.2535 0.1804 0.1642 0.0505  0.0572  0.0656  533 LEU   B N   
17579 C  CA  . LEU   B 533 ? 0.2468 0.1872 0.1567 0.0585  0.0535  0.0673  533 LEU   B CA  
17580 C  C   . LEU   B 533 ? 0.2502 0.2094 0.1618 0.0556  0.0499  0.0657  533 LEU   B C   
17581 O  O   . LEU   B 533 ? 0.2368 0.2098 0.1492 0.0592  0.0477  0.0677  533 LEU   B O   
17582 C  CB  . LEU   B 533 ? 0.2485 0.1839 0.1573 0.0645  0.0528  0.0665  533 LEU   B CB  
17583 C  CG  . LEU   B 533 ? 0.2561 0.2057 0.1663 0.0733  0.0502  0.0683  533 LEU   B CG  
17584 C  CD1 . LEU   B 533 ? 0.2956 0.2424 0.1951 0.0801  0.0516  0.0728  533 LEU   B CD1 
17585 C  CD2 . LEU   B 533 ? 0.2713 0.2179 0.1792 0.0779  0.0499  0.0664  533 LEU   B CD2 
17597 N  N   . GLU   B 534 ? 0.2170 0.1790 0.1403 0.0493  0.0497  0.0622  534 GLU   B N   
17598 C  CA  . GLU   B 534 ? 0.2314 0.2086 0.1568 0.0454  0.0480  0.0604  534 GLU   B CA  
17599 C  C   . GLU   B 534 ? 0.2180 0.2013 0.1422 0.0416  0.0487  0.0603  534 GLU   B C   
17600 O  O   . GLU   B 534 ? 0.2187 0.2174 0.1414 0.0423  0.0466  0.0605  534 GLU   B O   
17601 C  CB  . GLU   B 534 ? 0.2314 0.2070 0.1663 0.0398  0.0491  0.0570  534 GLU   B CB  
17602 C  CG  . GLU   B 534 ? 0.2384 0.2100 0.1722 0.0445  0.0482  0.0568  534 GLU   B CG  
17603 C  CD  . GLU   B 534 ? 0.1858 0.1554 0.1335 0.0407  0.0493  0.0539  534 GLU   B CD  
17604 O  OE1 . GLU   B 534 ? 0.2298 0.1949 0.1736 0.0337  0.0503  0.0513  534 GLU   B OE1 
17605 O  OE2 . GLU   B 534 ? 0.2116 0.1804 0.1528 0.0451  0.0482  0.0541  534 GLU   B OE2 
17612 N  N   . LYS   B 535 ? 0.2282 0.1995 0.1475 0.0380  0.0519  0.0600  535 LYS   B N   
17613 C  CA  . LYS   B 535 ? 0.2185 0.1947 0.1373 0.0353  0.0535  0.0599  535 LYS   B CA  
17614 C  C   . LYS   B 535 ? 0.2594 0.2425 0.1611 0.0429  0.0507  0.0637  535 LYS   B C   
17615 O  O   . LYS   B 535 ? 0.2009 0.1993 0.1061 0.0426  0.0489  0.0619  535 LYS   B O   
17616 C  CB  . LYS   B 535 ? 0.2482 0.2095 0.1619 0.0313  0.0583  0.0602  535 LYS   B CB  
17617 C  CG  . LYS   B 535 ? 0.2651 0.2283 0.1698 0.0305  0.0606  0.0612  535 LYS   B CG  
17618 C  CD  . LYS   B 535 ? 0.2184 0.1935 0.1305 0.0253  0.0610  0.0565  535 LYS   B CD  
17619 C  CE  . LYS   B 535 ? 0.2475 0.2251 0.1477 0.0254  0.0635  0.0566  535 LYS   B CE  
17620 N  NZ  . LYS   B 535 ? 0.2769 0.2636 0.1754 0.0211  0.0645  0.0508  535 LYS   B NZ  
17634 N  N   . LEU   B 536 ? 0.2726 0.2491 0.1727 0.0499  0.0507  0.0677  536 LEU   B N   
17635 C  CA  . LEU   B 536 ? 0.2423 0.2280 0.1403 0.0587  0.0484  0.0719  536 LEU   B CA  
17636 C  C   . LEU   B 536 ? 0.2516 0.2574 0.1477 0.0619  0.0429  0.0708  536 LEU   B C   
17637 O  O   . LEU   B 536 ? 0.2676 0.2884 0.1586 0.0655  0.0396  0.0713  536 LEU   B O   
17638 C  CB  . LEU   B 536 ? 0.2714 0.2422 0.1622 0.0655  0.0509  0.0762  536 LEU   B CB  
17639 C  CG  . LEU   B 536 ? 0.2861 0.2382 0.1789 0.0630  0.0571  0.0783  536 LEU   B CG  
17640 C  CD1 . LEU   B 536 ? 0.3395 0.2754 0.2239 0.0688  0.0599  0.0811  536 LEU   B CD1 
17641 C  CD2 . LEU   B 536 ? 0.3357 0.2879 0.2144 0.0639  0.0593  0.0814  536 LEU   B CD2 
17653 N  N   . PHE   B 537 ? 0.2247 0.2337 0.1314 0.0608  0.0418  0.0691  537 PHE   B N   
17654 C  CA  . PHE   B 537 ? 0.2163 0.2471 0.1291 0.0626  0.0379  0.0686  537 PHE   B CA  
17655 C  C   . PHE   B 537 ? 0.2004 0.2460 0.1122 0.0566  0.0366  0.0647  537 PHE   B C   
17656 O  O   . PHE   B 537 ? 0.2115 0.2769 0.1218 0.0589  0.0315  0.0631  537 PHE   B O   
17657 C  CB  . PHE   B 537 ? 0.2533 0.2824 0.1691 0.0616  0.0386  0.0678  537 PHE   B CB  
17658 C  CG  . PHE   B 537 ? 0.1743 0.2285 0.1102 0.0619  0.0357  0.0676  537 PHE   B CG  
17659 C  CD1 . PHE   B 537 ? 0.1703 0.2339 0.1142 0.0518  0.0343  0.0607  537 PHE   B CD1 
17660 C  CD2 . PHE   B 537 ? 0.2075 0.2720 0.1398 0.0710  0.0340  0.0718  537 PHE   B CD2 
17661 C  CE1 . PHE   B 537 ? 0.1923 0.2753 0.1476 0.0495  0.0315  0.0579  537 PHE   B CE1 
17662 C  CE2 . PHE   B 537 ? 0.2252 0.3112 0.1697 0.0691  0.0312  0.0694  537 PHE   B CE2 
17663 C  CZ  . PHE   B 537 ? 0.1858 0.2819 0.1476 0.0579  0.0299  0.0624  537 PHE   B CZ  
17673 N  N   . ASN   B 538 ? 0.1983 0.2342 0.1136 0.0474  0.0398  0.0601  538 ASN   B N   
17674 C  CA  . ASN   B 538 ? 0.2212 0.2666 0.1386 0.0391  0.0381  0.0521  538 ASN   B CA  
17675 C  C   . ASN   B 538 ? 0.2107 0.2644 0.1164 0.0431  0.0361  0.0521  538 ASN   B C   
17676 O  O   . ASN   B 538 ? 0.2096 0.2811 0.1178 0.0410  0.0310  0.0455  538 ASN   B O   
17677 C  CB  . ASN   B 538 ? 0.2220 0.2541 0.1458 0.0305  0.0425  0.0478  538 ASN   B CB  
17678 C  CG  . ASN   B 538 ? 0.1764 0.2092 0.1201 0.0255  0.0428  0.0451  538 ASN   B CG  
17679 O  OD1 . ASN   B 538 ? 0.1683 0.2096 0.1160 0.0283  0.0403  0.0464  538 ASN   B OD1 
17680 N  ND2 . ASN   B 538 ? 0.1956 0.2179 0.1412 0.0193  0.0462  0.0418  538 ASN   B ND2 
17687 N  N   . LEU   B 539 ? 0.2035 0.2432 0.0990 0.0474  0.0395  0.0573  539 LEU   B N   
17688 C  CA  . LEU   B 539 ? 0.2319 0.2774 0.1112 0.0532  0.0386  0.0595  539 LEU   B CA  
17689 C  C   . LEU   B 539 ? 0.2374 0.3038 0.1135 0.0616  0.0314  0.0606  539 LEU   B C   
17690 O  O   . LEU   B 539 ? 0.2392 0.3238 0.1087 0.0632  0.0266  0.0562  539 LEU   B O   
17691 C  CB  . LEU   B 539 ? 0.2706 0.2949 0.1428 0.0554  0.0435  0.0650  539 LEU   B CB  
17692 C  CG  . LEU   B 539 ? 0.2835 0.2920 0.1602 0.0473  0.0502  0.0637  539 LEU   B CG  
17693 C  CD1 . LEU   B 539 ? 0.3184 0.3081 0.1914 0.0494  0.0550  0.0694  539 LEU   B CD1 
17694 C  CD2 . LEU   B 539 ? 0.2873 0.3024 0.1567 0.0437  0.0516  0.0589  539 LEU   B CD2 
17706 N  N   . ALA   B 540 ? 0.2456 0.3104 0.1261 0.0671  0.0301  0.0654  540 ALA   B N   
17707 C  CA  . ALA   B 540 ? 0.2288 0.3148 0.1145 0.0756  0.0236  0.0667  540 ALA   B CA  
17708 C  C   . ALA   B 540 ? 0.2387 0.3521 0.1303 0.0713  0.0173  0.0600  540 ALA   B C   
17709 O  O   . ALA   B 540 ? 0.2698 0.4064 0.1584 0.0766  0.0100  0.0582  540 ALA   B O   
17710 C  CB  . ALA   B 540 ? 0.2382 0.3155 0.1262 0.0819  0.0254  0.0725  540 ALA   B CB  
17716 N  N   . ALA   B 541 ? 0.2289 0.3370 0.1336 0.0593  0.0192  0.0528  541 ALA   B N   
17717 C  CA  . ALA   B 541 ? 0.1883 0.3169 0.1173 0.0506  0.0140  0.0426  541 ALA   B CA  
17718 C  C   . ALA   B 541 ? 0.2399 0.3742 0.1563 0.0436  0.0109  0.0320  541 ALA   B C   
17719 O  O   . ALA   B 541 ? 0.2014 0.3529 0.1405 0.0355  0.0063  0.0224  541 ALA   B O   
17720 C  CB  . ALA   B 541 ? 0.1858 0.3040 0.1267 0.0427  0.0182  0.0414  541 ALA   B CB  
17726 N  N   . GLY   B 542 ? 0.2050 0.3293 0.1115 0.0462  0.0139  0.0335  542 GLY   B N   
17727 C  CA  . GLY   B 542 ? 0.2101 0.3398 0.1104 0.0409  0.0119  0.0236  542 GLY   B CA  
17728 C  C   . GLY   B 542 ? 0.2350 0.3462 0.1366 0.0305  0.0183  0.0182  542 GLY   B C   
17729 O  O   . GLY   B 542 ? 0.2345 0.3513 0.1397 0.0246  0.0167  0.0077  542 GLY   B O   
17733 N  N   . ILE   B 543 ? 0.1941 0.2880 0.1093 0.0287  0.0251  0.0246  543 ILE   B N   
17734 C  CA  . ILE   B 543 ? 0.2599 0.3354 0.1730 0.0205  0.0316  0.0214  543 ILE   B CA  
17735 C  C   . ILE   B 543 ? 0.3210 0.3838 0.2198 0.0243  0.0376  0.0262  543 ILE   B C   
17736 O  O   . ILE   B 543 ? 0.3549 0.4037 0.2475 0.0285  0.0421  0.0356  543 ILE   B O   
17737 C  CB  . ILE   B 543 ? 0.2232 0.2889 0.1559 0.0167  0.0349  0.0243  543 ILE   B CB  
17738 C  CG1 . ILE   B 543 ? 0.2054 0.2847 0.1530 0.0143  0.0306  0.0215  543 ILE   B CG1 
17739 C  CG2 . ILE   B 543 ? 0.2416 0.2927 0.1771 0.0094  0.0407  0.0208  543 ILE   B CG2 
17740 C  CD1 . ILE   B 543 ? 0.2064 0.2955 0.1651 0.0054  0.0281  0.0106  543 ILE   B CD1 
17752 N  N   . ASP   B 544 ? 0.3558 0.4219 0.2454 0.0230  0.0381  0.0200  544 ASP   B N   
17753 C  CA  . ASP   B 544 ? 0.4100 0.4642 0.2781 0.0269  0.0450  0.0246  544 ASP   B CA  
17754 C  C   . ASP   B 544 ? 0.3737 0.4102 0.2510 0.0205  0.0532  0.0258  544 ASP   B C   
17755 O  O   . ASP   B 544 ? 0.2902 0.3271 0.1903 0.0130  0.0528  0.0195  544 ASP   B O   
17756 C  CB  . ASP   B 544 ? 0.4054 0.4734 0.2719 0.0286  0.0429  0.0174  544 ASP   B CB  
17757 C  CG  . ASP   B 544 ? 0.5788 0.6351 0.4118 0.0345  0.0505  0.0234  544 ASP   B CG  
17758 O  OD1 . ASP   B 544 ? 0.5811 0.6273 0.4223 0.0296  0.0580  0.0218  544 ASP   B OD1 
17759 O  OD2 . ASP   B 544 ? 0.6216 0.6813 0.4467 0.0425  0.0481  0.0297  544 ASP   B OD2 
17764 N  N   . SER   B 545 ? 0.3526 0.3774 0.2247 0.0236  0.0610  0.0336  545 SER   B N   
17765 C  CA  . SER   B 545 ? 0.3385 0.3489 0.2168 0.0176  0.0687  0.0341  545 SER   B CA  
17766 C  C   . SER   B 545 ? 0.2939 0.3080 0.1783 0.0119  0.0700  0.0233  545 SER   B C   
17767 O  O   . SER   B 545 ? 0.2857 0.2920 0.1826 0.0064  0.0743  0.0216  545 SER   B O   
17768 C  CB  . SER   B 545 ? 0.3411 0.3406 0.2168 0.0193  0.0729  0.0417  545 SER   B CB  
17769 O  OG  . SER   B 545 ? 0.3219 0.3162 0.1998 0.0234  0.0702  0.0489  545 SER   B OG  
17775 N  N   . SER   B 546 ? 0.2545 0.2818 0.1348 0.0137  0.0661  0.0157  546 SER   B N   
17776 C  CA  . SER   B 546 ? 0.3210 0.3487 0.1940 0.0086  0.0667  0.0037  546 SER   B CA  
17777 C  C   . SER   B 546 ? 0.2743 0.3016 0.1737 0.0008  0.0641  -0.0030 546 SER   B C   
17778 O  O   . SER   B 546 ? 0.2427 0.2666 0.1494 -0.0038 0.0673  -0.0109 546 SER   B O   
17779 C  CB  . SER   B 546 ? 0.3325 0.3754 0.1977 0.0122  0.0615  -0.0043 546 SER   B CB  
17780 O  OG  . SER   B 546 ? 0.3748 0.4301 0.2409 0.0115  0.0515  -0.0087 546 SER   B OG  
17786 N  N   . GLN   B 547 ? 0.2683 0.2975 0.1766 0.0001  0.0593  0.0005  547 GLN   B N   
17787 C  CA  . GLN   B 547 ? 0.2324 0.2610 0.1641 -0.0063 0.0577  -0.0032 547 GLN   B CA  
17788 C  C   . GLN   B 547 ? 0.2352 0.2489 0.1702 -0.0079 0.0638  0.0020  547 GLN   B C   
17789 O  O   . GLN   B 547 ? 0.1770 0.1891 0.1322 -0.0117 0.0638  0.0001  547 GLN   B O   
17790 C  CB  . GLN   B 547 ? 0.2533 0.2911 0.1883 -0.0054 0.0508  -0.0015 547 GLN   B CB  
17791 C  CG  . GLN   B 547 ? 0.2787 0.3327 0.2058 -0.0036 0.0436  -0.0071 547 GLN   B CG  
17792 C  CD  . GLN   B 547 ? 0.2554 0.3221 0.2013 -0.0069 0.0375  -0.0103 547 GLN   B CD  
17793 O  OE1 . GLN   B 547 ? 0.2801 0.3405 0.2382 -0.0122 0.0398  -0.0107 547 GLN   B OE1 
17794 N  NE2 . GLN   B 547 ? 0.2555 0.3388 0.1947 -0.0036 0.0303  -0.0121 547 GLN   B NE2 
17803 N  N   . ASP   B 548 ? 0.2291 0.2362 0.1599 -0.0048 0.0692  0.0086  548 ASP   B N   
17804 C  CA  . ASP   B 548 ? 0.2137 0.2111 0.1562 -0.0067 0.0747  0.0125  548 ASP   B CA  
17805 C  C   . ASP   B 548 ? 0.2405 0.2346 0.1832 -0.0098 0.0798  0.0060  548 ASP   B C   
17806 O  O   . ASP   B 548 ? 0.2633 0.2558 0.1980 -0.0080 0.0854  0.0070  548 ASP   B O   
17807 C  CB  . ASP   B 548 ? 0.2290 0.2188 0.1621 -0.0037 0.0782  0.0217  548 ASP   B CB  
17808 C  CG  . ASP   B 548 ? 0.2242 0.2135 0.1585 -0.0003 0.0741  0.0283  548 ASP   B CG  
17809 O  OD1 . ASP   B 548 ? 0.2230 0.2175 0.1600 -0.0002 0.0683  0.0263  548 ASP   B OD1 
17810 O  OD2 . ASP   B 548 ? 0.2624 0.2445 0.1887 0.0020  0.0754  0.0345  548 ASP   B OD2 
17815 N  N   . THR   B 549 ? 0.2208 0.2151 0.1784 -0.0131 0.0791  -0.0004 549 THR   B N   
17816 C  CA  . THR   B 549 ? 0.2431 0.2335 0.2015 -0.0151 0.0842  -0.0073 549 THR   B CA  
17817 C  C   . THR   B 549 ? 0.2055 0.1919 0.1834 -0.0178 0.0851  -0.0094 549 THR   B C   
17818 O  O   . THR   B 549 ? 0.1829 0.1694 0.1678 -0.0177 0.0815  -0.0048 549 THR   B O   
17819 C  CB  . THR   B 549 ? 0.2792 0.2754 0.2295 -0.0154 0.0832  -0.0168 549 THR   B CB  
17820 O  OG1 . THR   B 549 ? 0.3284 0.3191 0.2752 -0.0158 0.0894  -0.0227 549 THR   B OG1 
17821 C  CG2 . THR   B 549 ? 0.2838 0.2849 0.2380 -0.0189 0.0765  -0.0234 549 THR   B CG2 
17829 N  N   . LEU   B 550 ? 0.2298 0.2108 0.2078 -0.0185 0.0900  -0.0154 550 LEU   B N   
17830 C  CA  . LEU   B 550 ? 0.1854 0.1625 0.1859 -0.0199 0.0918  -0.0172 550 LEU   B CA  
17831 C  C   . LEU   B 550 ? 0.2007 0.1744 0.2000 -0.0226 0.0937  -0.0282 550 LEU   B C   
17832 O  O   . LEU   B 550 ? 0.2448 0.2198 0.2275 -0.0224 0.0943  -0.0344 550 LEU   B O   
17833 C  CB  . LEU   B 550 ? 0.2280 0.1999 0.2287 -0.0171 0.0970  -0.0125 550 LEU   B CB  
17834 C  CG  . LEU   B 550 ? 0.2108 0.1855 0.2192 -0.0152 0.0947  -0.0035 550 LEU   B CG  
17835 C  CD1 . LEU   B 550 ? 0.2074 0.1812 0.2236 -0.0125 0.0969  -0.0010 550 LEU   B CD1 
17836 C  CD2 . LEU   B 550 ? 0.2076 0.1823 0.2204 -0.0152 0.0897  0.0002  550 LEU   B CD2 
17848 N  N   . PRO   B 551 ? 0.2357 0.2014 0.2394 -0.0250 0.0944  -0.0312 551 PRO   B N   
17849 C  CA  . PRO   B 551 ? 0.2066 0.1680 0.2200 -0.0281 0.0971  -0.0426 551 PRO   B CA  
17850 C  C   . PRO   B 551 ? 0.2143 0.1713 0.2213 -0.0246 0.1038  -0.0470 551 PRO   B C   
17851 O  O   . PRO   B 551 ? 0.2261 0.1817 0.2335 -0.0205 0.1078  -0.0399 551 PRO   B O   
17852 C  CB  . PRO   B 551 ? 0.2120 0.1641 0.2373 -0.0296 0.0995  -0.0403 551 PRO   B CB  
17853 C  CG  . PRO   B 551 ? 0.1808 0.1395 0.2135 -0.0288 0.0952  -0.0300 551 PRO   B CG  
17854 C  CD  . PRO   B 551 ? 0.1914 0.1566 0.2139 -0.0247 0.0933  -0.0238 551 PRO   B CD  
17862 N  N   . LYS   B 552 ? 0.2441 0.1985 0.2408 -0.0262 0.1051  -0.0591 552 LYS   B N   
17863 C  CA  . LYS   B 552 ? 0.2459 0.1978 0.2432 -0.0221 0.1124  -0.0643 552 LYS   B CA  
17864 C  C   . LYS   B 552 ? 0.2663 0.2070 0.2682 -0.0186 0.1199  -0.0600 552 LYS   B C   
17865 O  O   . LYS   B 552 ? 0.2430 0.1863 0.2472 -0.0136 0.1255  -0.0561 552 LYS   B O   
17866 C  CB  . LYS   B 552 ? 0.3453 0.2931 0.3247 -0.0246 0.1119  -0.0798 552 LYS   B CB  
17867 C  CG  . LYS   B 552 ? 0.3930 0.3545 0.3666 -0.0263 0.1043  -0.0857 552 LYS   B CG  
17868 C  CD  . LYS   B 552 ? 0.5807 0.5395 0.5297 -0.0265 0.1043  -0.1014 552 LYS   B CD  
17869 C  CE  . LYS   B 552 ? 0.6649 0.6337 0.6112 -0.0313 0.0944  -0.1118 552 LYS   B CE  
17870 N  NZ  . LYS   B 552 ? 0.6913 0.6525 0.6519 -0.0389 0.0927  -0.1244 552 LYS   B NZ  
17884 N  N   . ARG   B 553 ? 0.2495 0.1816 0.2677 -0.0206 0.1205  -0.0601 553 ARG   B N   
17885 C  CA  . ARG   B 553 ? 0.2203 0.1437 0.2533 -0.0159 0.1268  -0.0549 553 ARG   B CA  
17886 C  C   . ARG   B 553 ? 0.2057 0.1384 0.2426 -0.0110 0.1249  -0.0421 553 ARG   B C   
17887 O  O   . ARG   B 553 ? 0.2335 0.1635 0.2701 -0.0050 0.1335  -0.0417 553 ARG   B O   
17888 C  CB  . ARG   B 553 ? 0.2314 0.1452 0.2763 -0.0182 0.1274  -0.0524 553 ARG   B CB  
17889 C  CG  . ARG   B 553 ? 0.2294 0.1365 0.2873 -0.0114 0.1330  -0.0437 553 ARG   B CG  
17890 C  CD  . ARG   B 553 ? 0.2306 0.1257 0.3005 -0.0132 0.1353  -0.0420 553 ARG   B CD  
17891 N  NE  . ARG   B 553 ? 0.2395 0.1255 0.3130 -0.0178 0.1370  -0.0510 553 ARG   B NE  
17892 C  CZ  . ARG   B 553 ? 0.2796 0.1481 0.3577 -0.0227 0.1418  -0.0572 553 ARG   B CZ  
17893 N  NH1 . ARG   B 553 ? 0.2396 0.1188 0.3298 -0.0241 0.1369  -0.0452 553 ARG   B NH1 
17894 N  NH2 . ARG   B 553 ? 0.2742 0.1401 0.3569 -0.0275 0.1413  -0.0667 553 ARG   B NH2 
17908 N  N   . LEU   B 554 ? 0.2359 0.1760 0.2669 -0.0121 0.1214  -0.0354 554 LEU   B N   
17909 C  CA  . LEU   B 554 ? 0.2340 0.1816 0.2680 -0.0081 0.1209  -0.0252 554 LEU   B CA  
17910 C  C   . LEU   B 554 ? 0.2266 0.1824 0.2561 -0.0072 0.1212  -0.0244 554 LEU   B C   
17911 O  O   . LEU   B 554 ? 0.2457 0.2066 0.2782 -0.0044 0.1190  -0.0177 554 LEU   B O   
17912 C  CB  . LEU   B 554 ? 0.1923 0.1451 0.2328 -0.0101 0.1136  -0.0181 554 LEU   B CB  
17913 C  CG  . LEU   B 554 ? 0.1970 0.1432 0.2446 -0.0107 0.1123  -0.0163 554 LEU   B CG  
17914 C  CD1 . LEU   B 554 ? 0.2011 0.1526 0.2468 -0.0118 0.1058  -0.0093 554 LEU   B CD1 
17915 C  CD2 . LEU   B 554 ? 0.2228 0.1618 0.2786 -0.0051 0.1178  -0.0133 554 LEU   B CD2 
17927 N  N   . LEU   B 555 ? 0.2277 0.1842 0.2441 -0.0091 0.1229  -0.0315 555 LEU   B N   
17928 C  CA  . LEU   B 555 ? 0.2557 0.2177 0.2583 -0.0075 0.1237  -0.0300 555 LEU   B CA  
17929 C  C   . LEU   B 555 ? 0.2542 0.2140 0.2582 -0.0039 0.1298  -0.0355 555 LEU   B C   
17930 O  O   . LEU   B 555 ? 0.2594 0.2252 0.2619 -0.0014 0.1317  -0.0316 555 LEU   B O   
17931 C  CB  . LEU   B 555 ? 0.2343 0.2013 0.2246 -0.0099 0.1213  -0.0321 555 LEU   B CB  
17932 C  CG  . LEU   B 555 ? 0.2275 0.1985 0.2173 -0.0126 0.1154  -0.0262 555 LEU   B CG  
17933 C  CD1 . LEU   B 555 ? 0.2527 0.2274 0.2231 -0.0137 0.1113  -0.0290 555 LEU   B CD1 
17934 C  CD2 . LEU   B 555 ? 0.2452 0.2190 0.2385 -0.0113 0.1121  -0.0156 555 LEU   B CD2 
17946 N  N   . GLU   B 556 ? 0.2426 0.1937 0.2505 -0.0039 0.1330  -0.0444 556 GLU   B N   
17947 C  CA  . GLU   B 556 ? 0.2729 0.2200 0.2767 -0.0001 0.1384  -0.0515 556 GLU   B CA  
17948 C  C   . GLU   B 556 ? 0.3164 0.2531 0.3265 0.0033  0.1422  -0.0517 556 GLU   B C   
17949 O  O   . GLU   B 556 ? 0.2692 0.2070 0.2871 0.0079  0.1467  -0.0539 556 GLU   B O   
17950 C  CB  . GLU   B 556 ? 0.2873 0.2311 0.2762 -0.0024 0.1382  -0.0641 556 GLU   B CB  
17951 C  CG  . GLU   B 556 ? 0.3402 0.2932 0.3163 -0.0048 0.1340  -0.0648 556 GLU   B CG  
17952 C  CD  . GLU   B 556 ? 0.4895 0.4389 0.4409 -0.0069 0.1319  -0.0787 556 GLU   B CD  
17953 O  OE1 . GLU   B 556 ? 0.5242 0.4648 0.4830 -0.0082 0.1330  -0.0894 556 GLU   B OE1 
17954 O  OE2 . GLU   B 556 ? 0.4957 0.4547 0.4367 -0.0070 0.1283  -0.0792 556 GLU   B OE2 
17961 N  N   . GLU   B 557 ? 0.2842 0.2153 0.3116 0.0020  0.1410  -0.0492 557 GLU   B N   
17962 C  CA  . GLU   B 557 ? 0.2467 0.1699 0.2915 0.0057  0.1428  -0.0476 557 GLU   B CA  
17963 C  C   . GLU   B 557 ? 0.2624 0.1904 0.3117 0.0110  0.1436  -0.0365 557 GLU   B C   
17964 O  O   . GLU   B 557 ? 0.2347 0.1664 0.2923 0.0097  0.1394  -0.0300 557 GLU   B O   
17965 C  CB  . GLU   B 557 ? 0.3095 0.2178 0.3541 0.0024  0.1454  -0.0540 557 GLU   B CB  
17966 C  CG  . GLU   B 557 ? 0.3938 0.2970 0.4292 -0.0039 0.1445  -0.0672 557 GLU   B CG  
17967 C  CD  . GLU   B 557 ? 0.4911 0.3801 0.5264 -0.0094 0.1444  -0.0730 557 GLU   B CD  
17968 O  OE1 . GLU   B 557 ? 0.4094 0.2937 0.4677 -0.0074 0.1465  -0.0653 557 GLU   B OE1 
17969 O  OE2 . GLU   B 557 ? 0.5349 0.4229 0.5686 -0.0158 0.1417  -0.0847 557 GLU   B OE2 
17976 N  N   . PRO   B 558 ? 0.2623 0.1950 0.3191 0.0170  0.1467  -0.0338 558 PRO   B N   
17977 C  CA  . PRO   B 558 ? 0.2668 0.2084 0.3351 0.0220  0.1446  -0.0241 558 PRO   B CA  
17978 C  C   . PRO   B 558 ? 0.2234 0.1583 0.3013 0.0234  0.1399  -0.0177 558 PRO   B C   
17979 O  O   . PRO   B 558 ? 0.2533 0.1733 0.3288 0.0251  0.1479  -0.0228 558 PRO   B O   
17980 C  CB  . PRO   B 558 ? 0.3246 0.2705 0.3933 0.0278  0.1494  -0.0249 558 PRO   B CB  
17981 C  CG  . PRO   B 558 ? 0.3568 0.2981 0.4089 0.0254  0.1532  -0.0337 558 PRO   B CG  
17982 C  CD  . PRO   B 558 ? 0.2716 0.2027 0.3261 0.0199  0.1521  -0.0405 558 PRO   B CD  
17990 N  N   . ILE   B 559 ? 0.2147 0.1576 0.2981 0.0267  0.1372  -0.0099 559 ILE   B N   
17991 C  CA  . ILE   B 559 ? 0.2094 0.1473 0.2978 0.0302  0.1336  -0.0024 559 ILE   B CA  
17992 C  C   . ILE   B 559 ? 0.2227 0.1544 0.3150 0.0359  0.1382  -0.0027 559 ILE   B C   
17993 O  O   . ILE   B 559 ? 0.2323 0.1730 0.3297 0.0427  0.1432  -0.0031 559 ILE   B O   
17994 C  CB  . ILE   B 559 ? 0.1928 0.1441 0.2878 0.0329  0.1256  0.0057  559 ILE   B CB  
17995 C  CG1 . ILE   B 559 ? 0.2076 0.1619 0.3004 0.0299  0.1264  0.0057  559 ILE   B CG1 
17996 C  CG2 . ILE   B 559 ? 0.2100 0.1588 0.3128 0.0443  0.1321  0.0120  559 ILE   B CG2 
17997 C  CD1 . ILE   B 559 ? 0.2139 0.1824 0.3111 0.0324  0.1196  0.0114  559 ILE   B CD1 
18009 N  N   . PRO   B 560 ? 0.2392 0.1550 0.3339 0.0373  0.1448  -0.0039 560 PRO   B N   
18010 C  CA  . PRO   B 560 ? 0.2684 0.1744 0.3699 0.0461  0.1557  -0.0060 560 PRO   B CA  
18011 C  C   . PRO   B 560 ? 0.2988 0.2122 0.4040 0.0566  0.1551  0.0031  560 PRO   B C   
18012 O  O   . PRO   B 560 ? 0.3061 0.2213 0.4154 0.0625  0.1588  0.0017  560 PRO   B O   
18013 C  CB  . PRO   B 560 ? 0.3048 0.1907 0.4009 0.0425  0.1599  -0.0081 560 PRO   B CB  
18014 C  CG  . PRO   B 560 ? 0.2734 0.1623 0.3737 0.0386  0.1555  -0.0030 560 PRO   B CG  
18015 C  CD  . PRO   B 560 ? 0.2495 0.1529 0.3458 0.0346  0.1494  -0.0049 560 PRO   B CD  
18023 N  N   . ASP   B 561 ? 0.2767 0.1975 0.3910 0.0598  0.1502  0.0122  561 ASP   B N   
18024 C  CA  . ASP   B 561 ? 0.3238 0.2512 0.4358 0.0708  0.1491  0.0208  561 ASP   B CA  
18025 C  C   . ASP   B 561 ? 0.2868 0.2308 0.4065 0.0731  0.1406  0.0278  561 ASP   B C   
18026 O  O   . ASP   B 561 ? 0.2532 0.1958 0.3700 0.0666  0.1373  0.0280  561 ASP   B O   
18027 C  CB  . ASP   B 561 ? 0.3052 0.2196 0.4327 0.0763  0.1554  0.0251  561 ASP   B CB  
18028 C  CG  . ASP   B 561 ? 0.4897 0.3912 0.6043 0.0796  0.1630  0.0201  561 ASP   B CG  
18029 O  OD1 . ASP   B 561 ? 0.5438 0.4562 0.6644 0.0881  0.1629  0.0221  561 ASP   B OD1 
18030 O  OD2 . ASP   B 561 ? 0.5331 0.4178 0.6466 0.0737  0.1686  0.0135  561 ASP   B OD2 
18035 N  N   . GLY   B 562 ? 0.2972 0.2562 0.4219 0.0823  0.1371  0.0329  562 GLY   B N   
18036 C  CA  . GLY   B 562 ? 0.3012 0.2745 0.4245 0.0859  0.1287  0.0386  562 GLY   B CA  
18037 C  C   . GLY   B 562 ? 0.2285 0.2260 0.3659 0.0844  0.1221  0.0354  562 GLY   B C   
18038 O  O   . GLY   B 562 ? 0.2457 0.2471 0.3822 0.0809  0.1247  0.0297  562 GLY   B O   
18042 N  N   . PRO   B 563 ? 0.2213 0.2332 0.3604 0.0867  0.1138  0.0387  563 PRO   B N   
18043 C  CA  . PRO   B 563 ? 0.2338 0.2679 0.3805 0.0846  0.1075  0.0350  563 PRO   B CA  
18044 C  C   . PRO   B 563 ? 0.2798 0.3123 0.4188 0.0727  0.1092  0.0284  563 PRO   B C   
18045 O  O   . PRO   B 563 ? 0.2465 0.2974 0.4017 0.0704  0.1070  0.0252  563 PRO   B O   
18046 C  CB  . PRO   B 563 ? 0.2554 0.2977 0.3996 0.0878  0.0992  0.0392  563 PRO   B CB  
18047 C  CG  . PRO   B 563 ? 0.3174 0.3459 0.4472 0.0962  0.1011  0.0466  563 PRO   B CG  
18048 C  CD  . PRO   B 563 ? 0.2792 0.2855 0.4075 0.0912  0.1106  0.0458  563 PRO   B CD  
18056 N  N   . SER   B 564 ? 0.2478 0.2635 0.3820 0.0652  0.1128  0.0262  564 SER   B N   
18057 C  CA  . SER   B 564 ? 0.2171 0.2308 0.3456 0.0547  0.1140  0.0205  564 SER   B CA  
18058 C  C   . SER   B 564 ? 0.1950 0.1960 0.3230 0.0517  0.1220  0.0158  564 SER   B C   
18059 O  O   . SER   B 564 ? 0.2164 0.2102 0.3323 0.0435  0.1233  0.0114  564 SER   B O   
18060 C  CB  . SER   B 564 ? 0.1860 0.1958 0.3109 0.0486  0.1100  0.0211  564 SER   B CB  
18061 O  OG  . SER   B 564 ? 0.1890 0.2114 0.3162 0.0520  0.1030  0.0244  564 SER   B OG  
18067 N  N   . LYS   B 565 ? 0.2263 0.2219 0.3520 0.0587  0.1268  0.0163  565 LYS   B N   
18068 C  CA  . LYS   B 565 ? 0.2343 0.2166 0.3573 0.0572  0.1346  0.0112  565 LYS   B CA  
18069 C  C   . LYS   B 565 ? 0.2320 0.2205 0.3505 0.0510  0.1366  0.0053  565 LYS   B C   
18070 O  O   . LYS   B 565 ? 0.2038 0.2096 0.3308 0.0509  0.1326  0.0065  565 LYS   B O   
18071 C  CB  . LYS   B 565 ? 0.2597 0.2392 0.3839 0.0668  0.1392  0.0128  565 LYS   B CB  
18072 C  CG  . LYS   B 565 ? 0.2377 0.2052 0.3615 0.0640  0.1426  0.0078  565 LYS   B CG  
18073 C  CD  . LYS   B 565 ? 0.3219 0.2863 0.4437 0.0774  0.1520  0.0093  565 LYS   B CD  
18074 C  CE  . LYS   B 565 ? 0.2812 0.2395 0.4129 0.0782  0.1599  0.0025  565 LYS   B CE  
18075 N  NZ  . LYS   B 565 ? 0.3875 0.3213 0.4978 0.0724  0.1640  -0.0033 565 LYS   B NZ  
18089 N  N   . GLY   B 566 ? 0.2373 0.2136 0.3470 0.0455  0.1405  -0.0008 566 GLY   B N   
18090 C  CA  . GLY   B 566 ? 0.2558 0.2368 0.3578 0.0411  0.1433  -0.0055 566 GLY   B CA  
18091 C  C   . GLY   B 566 ? 0.2346 0.2208 0.3329 0.0329  0.1391  -0.0058 566 GLY   B C   
18092 O  O   . GLY   B 566 ? 0.2541 0.2423 0.3444 0.0295  0.1417  -0.0090 566 GLY   B O   
18096 N  N   . GLU   B 567 ? 0.2029 0.1898 0.3026 0.0304  0.1328  -0.0022 567 GLU   B N   
18097 C  CA  . GLU   B 567 ? 0.1956 0.1875 0.2906 0.0234  0.1282  -0.0016 567 GLU   B CA  
18098 C  C   . GLU   B 567 ? 0.1905 0.1708 0.2726 0.0178  0.1281  -0.0055 567 GLU   B C   
18099 O  O   . GLU   B 567 ? 0.1855 0.1529 0.2605 0.0175  0.1242  -0.0067 567 GLU   B O   
18100 C  CB  . GLU   B 567 ? 0.2203 0.2212 0.3223 0.0239  0.1215  0.0037  567 GLU   B CB  
18101 C  CG  . GLU   B 567 ? 0.2301 0.2473 0.3463 0.0279  0.1206  0.0063  567 GLU   B CG  
18102 C  CD  . GLU   B 567 ? 0.2328 0.2617 0.3569 0.0237  0.1223  0.0053  567 GLU   B CD  
18103 O  OE1 . GLU   B 567 ? 0.2615 0.2896 0.3764 0.0168  0.1199  0.0055  567 GLU   B OE1 
18104 O  OE2 . GLU   B 567 ? 0.2756 0.3111 0.4018 0.0271  0.1265  0.0049  567 GLU   B OE2 
18111 N  N   . VAL   B 568 ? 0.2340 0.2161 0.3017 0.0123  0.1268  -0.0065 568 VAL   B N   
18112 C  CA  . VAL   B 568 ? 0.2041 0.1801 0.2641 0.0073  0.1254  -0.0098 568 VAL   B CA  
18113 C  C   . VAL   B 568 ? 0.1842 0.1665 0.2405 0.0032  0.1197  -0.0054 568 VAL   B C   
18114 O  O   . VAL   B 568 ? 0.1837 0.1745 0.2457 0.0033  0.1190  -0.0018 568 VAL   B O   
18115 C  CB  . VAL   B 568 ? 0.2388 0.2107 0.2888 0.0065  0.1308  -0.0166 568 VAL   B CB  
18116 C  CG1 . VAL   B 568 ? 0.3081 0.2705 0.3527 0.0104  0.1365  -0.0221 568 VAL   B CG1 
18117 C  CG2 . VAL   B 568 ? 0.2819 0.2614 0.3219 0.0060  0.1327  -0.0147 568 VAL   B CG2 
18127 N  N   . HIS   B 569 ? 0.1846 0.1627 0.2314 -0.0003 0.1162  -0.0058 569 HIS   B N   
18128 C  CA  . HIS   B 569 ? 0.1888 0.1715 0.2329 -0.0038 0.1108  -0.0016 569 HIS   B CA  
18129 C  C   . HIS   B 569 ? 0.2127 0.1964 0.2417 -0.0057 0.1134  -0.0017 569 HIS   B C   
18130 O  O   . HIS   B 569 ? 0.2010 0.1824 0.2237 -0.0056 0.1168  -0.0063 569 HIS   B O   
18131 C  CB  . HIS   B 569 ? 0.2074 0.1851 0.2417 -0.0058 0.1059  -0.0006 569 HIS   B CB  
18132 C  CG  . HIS   B 569 ? 0.1598 0.1433 0.2023 -0.0078 0.1005  0.0040  569 HIS   B CG  
18133 N  ND1 . HIS   B 569 ? 0.2201 0.2006 0.2403 -0.0102 0.0993  0.0050  569 HIS   B ND1 
18134 C  CD2 . HIS   B 569 ? 0.1997 0.1849 0.2409 -0.0072 0.0967  0.0078  569 HIS   B CD2 
18135 C  CE1 . HIS   B 569 ? 0.1929 0.1762 0.2203 -0.0113 0.0951  0.0092  569 HIS   B CE1 
18136 N  NE2 . HIS   B 569 ? 0.2008 0.1865 0.2376 -0.0098 0.0935  0.0104  569 HIS   B NE2 
18144 N  N   . ARG   B 570 ? 0.1726 0.1630 0.2108 -0.0072 0.1121  0.0028  570 ARG   B N   
18145 C  CA  . ARG   B 570 ? 0.1967 0.1885 0.2240 -0.0084 0.1158  0.0048  570 ARG   B CA  
18146 C  C   . ARG   B 570 ? 0.2043 0.1931 0.2207 -0.0110 0.1111  0.0068  570 ARG   B C   
18147 O  O   . ARG   B 570 ? 0.2259 0.2163 0.2424 -0.0123 0.1123  0.0125  570 ARG   B O   
18148 C  CB  . ARG   B 570 ? 0.2109 0.2099 0.2520 -0.0085 0.1188  0.0075  570 ARG   B CB  
18149 C  CG  . ARG   B 570 ? 0.2567 0.2592 0.3059 -0.0053 0.1219  0.0051  570 ARG   B CG  
18150 C  CD  . ARG   B 570 ? 0.2663 0.2700 0.3180 -0.0022 0.1289  0.0019  570 ARG   B CD  
18151 N  NE  . ARG   B 570 ? 0.4171 0.4213 0.4487 -0.0032 0.1335  0.0045  570 ARG   B NE  
18152 C  CZ  . ARG   B 570 ? 0.3845 0.3990 0.4376 -0.0038 0.1373  0.0079  570 ARG   B CZ  
18153 N  NH1 . ARG   B 570 ? 0.3986 0.4194 0.4655 -0.0027 0.1367  0.0076  570 ARG   B NH1 
18154 N  NH2 . ARG   B 570 ? 0.3794 0.3956 0.4255 -0.0053 0.1417  0.0116  570 ARG   B NH2 
18168 N  N   . LEU   B 571 ? 0.1954 0.1628 0.2009 -0.0414 0.0659  -0.0323 571 LEU   B N   
18169 C  CA  . LEU   B 571 ? 0.2265 0.1962 0.2099 -0.0402 0.0626  -0.0282 571 LEU   B CA  
18170 C  C   . LEU   B 571 ? 0.2393 0.2047 0.2059 -0.0300 0.0800  -0.0208 571 LEU   B C   
18171 O  O   . LEU   B 571 ? 0.2435 0.2098 0.2065 -0.0285 0.0832  -0.0125 571 LEU   B O   
18172 C  CB  . LEU   B 571 ? 0.2386 0.2124 0.2014 -0.0424 0.0467  -0.0338 571 LEU   B CB  
18173 C  CG  . LEU   B 571 ? 0.2380 0.2180 0.1913 -0.0417 0.0415  -0.0280 571 LEU   B CG  
18174 C  CD1 . LEU   B 571 ? 0.2018 0.1823 0.1735 -0.0469 0.0395  -0.0241 571 LEU   B CD1 
18175 C  CD2 . LEU   B 571 ? 0.2826 0.2678 0.2194 -0.0431 0.0272  -0.0318 571 LEU   B CD2 
18187 N  N   . ASP   B 572 ? 0.2731 0.2295 0.2211 -0.0222 0.0919  -0.0232 572 ASP   B N   
18188 C  CA  . ASP   B 572 ? 0.3080 0.2533 0.2268 -0.0104 0.1101  -0.0162 572 ASP   B CA  
18189 C  C   . ASP   B 572 ? 0.3076 0.2550 0.2532 -0.0092 0.1277  -0.0029 572 ASP   B C   
18190 O  O   . ASP   B 572 ? 0.3373 0.2784 0.2614 -0.0019 0.1387  0.0059  572 ASP   B O   
18191 C  CB  . ASP   B 572 ? 0.3142 0.2441 0.2104 -0.0008 0.1225  -0.0219 572 ASP   B CB  
18192 C  CG  . ASP   B 572 ? 0.3377 0.2687 0.2723 -0.0003 0.1385  -0.0218 572 ASP   B CG  
18193 O  OD1 . ASP   B 572 ? 0.3672 0.3092 0.3367 -0.0106 0.1287  -0.0226 572 ASP   B OD1 
18194 O  OD2 . ASP   B 572 ? 0.4559 0.3695 0.3638 0.0113  0.1606  -0.0203 572 ASP   B OD2 
18199 N  N   . VAL   B 573 ? 0.2652 0.2196 0.2595 -0.0165 0.1284  -0.0006 573 VAL   B N   
18200 C  CA  . VAL   B 573 ? 0.2478 0.2039 0.2816 -0.0173 0.1419  0.0122  573 VAL   B CA  
18201 C  C   . VAL   B 573 ? 0.2578 0.2168 0.2985 -0.0262 0.1247  0.0143  573 VAL   B C   
18202 O  O   . VAL   B 573 ? 0.2741 0.2310 0.3234 -0.0247 0.1327  0.0247  573 VAL   B O   
18203 C  CB  . VAL   B 573 ? 0.2817 0.2400 0.3644 -0.0193 0.1525  0.0150  573 VAL   B CB  
18204 C  CG1 . VAL   B 573 ? 0.3546 0.3134 0.4746 -0.0238 0.1525  0.0260  573 VAL   B CG1 
18205 C  CG2 . VAL   B 573 ? 0.3511 0.2999 0.4137 -0.0070 0.1775  0.0162  573 VAL   B CG2 
18215 N  N   . LEU   B 574 ? 0.2079 0.1708 0.2531 -0.0342 0.1027  0.0049  574 LEU   B N   
18216 C  CA  . LEU   B 574 ? 0.2063 0.1663 0.2559 -0.0414 0.0876  0.0054  574 LEU   B CA  
18217 C  C   . LEU   B 574 ? 0.1963 0.1576 0.2175 -0.0373 0.0851  0.0080  574 LEU   B C   
18218 O  O   . LEU   B 574 ? 0.2085 0.1641 0.2334 -0.0384 0.0836  0.0137  574 LEU   B O   
18219 C  CB  . LEU   B 574 ? 0.2048 0.1632 0.2644 -0.0497 0.0685  -0.0041 574 LEU   B CB  
18220 C  CG  . LEU   B 574 ? 0.1693 0.1280 0.2705 -0.0544 0.0661  -0.0065 574 LEU   B CG  
18221 C  CD1 . LEU   B 574 ? 0.2222 0.1770 0.3113 -0.0606 0.0484  -0.0166 574 LEU   B CD1 
18222 C  CD2 . LEU   B 574 ? 0.2065 0.1585 0.3320 -0.0562 0.0617  0.0011  574 LEU   B CD2 
18234 N  N   . LEU   B 575 ? 0.1962 0.1629 0.1874 -0.0327 0.0831  0.0039  575 LEU   B N   
18235 C  CA  . LEU   B 575 ? 0.2385 0.2076 0.2026 -0.0291 0.0779  0.0068  575 LEU   B CA  
18236 C  C   . LEU   B 575 ? 0.2443 0.2089 0.2034 -0.0224 0.0906  0.0185  575 LEU   B C   
18237 O  O   . LEU   B 575 ? 0.2358 0.1993 0.1967 -0.0222 0.0870  0.0229  575 LEU   B O   
18238 C  CB  . LEU   B 575 ? 0.2506 0.2254 0.1904 -0.0261 0.0700  0.0012  575 LEU   B CB  
18239 C  CG  . LEU   B 575 ? 0.2587 0.2394 0.1840 -0.0233 0.0612  0.0044  575 LEU   B CG  
18240 C  CD1 . LEU   B 575 ? 0.2208 0.2053 0.1628 -0.0284 0.0544  0.0046  575 LEU   B CD1 
18241 C  CD2 . LEU   B 575 ? 0.3029 0.2870 0.2070 -0.0217 0.0493  -0.0007 575 LEU   B CD2 
18253 N  N   . PRO   B 576 ? 0.2394 0.1996 0.1938 -0.0157 0.1071  0.0245  576 PRO   B N   
18254 C  CA  . PRO   B 576 ? 0.2688 0.2225 0.2182 -0.0093 0.1206  0.0372  576 PRO   B CA  
18255 C  C   . PRO   B 576 ? 0.2601 0.2102 0.2399 -0.0151 0.1209  0.0433  576 PRO   B C   
18256 O  O   . PRO   B 576 ? 0.2626 0.2094 0.2382 -0.0125 0.1210  0.0504  576 PRO   B O   
18257 C  CB  . PRO   B 576 ? 0.3243 0.2706 0.2632 -0.0023 0.1404  0.0415  576 PRO   B CB  
18258 C  CG  . PRO   B 576 ? 0.3675 0.3126 0.2833 -0.0016 0.1350  0.0299  576 PRO   B CG  
18259 C  CD  . PRO   B 576 ? 0.2555 0.2135 0.2047 -0.0125 0.1160  0.0202  576 PRO   B CD  
18267 N  N   . GLU   B 577 ? 0.2346 0.1846 0.2526 -0.0226 0.1191  0.0405  577 GLU   B N   
18268 C  CA  . GLU   B 577 ? 0.2707 0.2112 0.3139 -0.0294 0.1141  0.0447  577 GLU   B CA  
18269 C  C   . GLU   B 577 ? 0.2143 0.1513 0.2543 -0.0326 0.0967  0.0392  577 GLU   B C   
18270 O  O   . GLU   B 577 ? 0.2645 0.1886 0.3038 -0.0332 0.0943  0.0442  577 GLU   B O   
18271 C  CB  . GLU   B 577 ? 0.2669 0.2085 0.3576 -0.0364 0.1107  0.0429  577 GLU   B CB  
18272 C  CG  . GLU   B 577 ? 0.3234 0.2570 0.4442 -0.0410 0.0968  0.0451  577 GLU   B CG  
18273 C  CD  . GLU   B 577 ? 0.4589 0.3889 0.5836 -0.0359 0.1066  0.0564  577 GLU   B CD  
18274 O  OE1 . GLU   B 577 ? 0.4830 0.4191 0.6037 -0.0274 0.1260  0.0634  577 GLU   B OE1 
18275 O  OE2 . GLU   B 577 ? 0.4037 0.3283 0.5582 -0.0399 0.0940  0.0579  577 GLU   B OE2 
18282 N  N   . TYR   B 578 ? 0.2063 0.1481 0.2234 -0.0334 0.0858  0.0291  578 TYR   B N   
18283 C  CA  . TYR   B 578 ? 0.2067 0.1426 0.2078 -0.0344 0.0740  0.0249  578 TYR   B CA  
18284 C  C   . TYR   B 578 ? 0.2203 0.1565 0.2045 -0.0263 0.0798  0.0327  578 TYR   B C   
18285 O  O   . TYR   B 578 ? 0.2165 0.1398 0.2014 -0.0255 0.0773  0.0350  578 TYR   B O   
18286 C  CB  . TYR   B 578 ? 0.1852 0.1295 0.1779 -0.0365 0.0645  0.0153  578 TYR   B CB  
18287 C  CG  . TYR   B 578 ? 0.2277 0.1640 0.2022 -0.0360 0.0573  0.0127  578 TYR   B CG  
18288 C  CD1 . TYR   B 578 ? 0.2344 0.1513 0.2116 -0.0405 0.0486  0.0087  578 TYR   B CD1 
18289 C  CD2 . TYR   B 578 ? 0.2246 0.1718 0.1859 -0.0299 0.0592  0.0155  578 TYR   B CD2 
18290 C  CE1 . TYR   B 578 ? 0.2519 0.1569 0.2101 -0.0376 0.0461  0.0072  578 TYR   B CE1 
18291 C  CE2 . TYR   B 578 ? 0.2010 0.1427 0.1576 -0.0276 0.0573  0.0152  578 TYR   B CE2 
18292 C  CZ  . TYR   B 578 ? 0.2419 0.1600 0.1887 -0.0307 0.0527  0.0111  578 TYR   B CZ  
18293 O  OH  . TYR   B 578 ? 0.2287 0.1364 0.1643 -0.0262 0.0547  0.0113  578 TYR   B OH  
18303 N  N   . TYR   B 579 ? 0.2186 0.1674 0.1896 -0.0197 0.0863  0.0365  579 TYR   B N   
18304 C  CA  . TYR   B 579 ? 0.2554 0.2039 0.2065 -0.0114 0.0903  0.0452  579 TYR   B CA  
18305 C  C   . TYR   B 579 ? 0.2487 0.1848 0.2142 -0.0103 0.0994  0.0548  579 TYR   B C   
18306 O  O   . TYR   B 579 ? 0.2505 0.1794 0.2127 -0.0065 0.0985  0.0595  579 TYR   B O   
18307 C  CB  . TYR   B 579 ? 0.2362 0.1948 0.1705 -0.0051 0.0928  0.0477  579 TYR   B CB  
18308 C  CG  . TYR   B 579 ? 0.2535 0.2231 0.1737 -0.0059 0.0808  0.0399  579 TYR   B CG  
18309 C  CD1 . TYR   B 579 ? 0.2365 0.2127 0.1685 -0.0101 0.0709  0.0340  579 TYR   B CD1 
18310 C  CD2 . TYR   B 579 ? 0.2722 0.2439 0.1713 -0.0020 0.0790  0.0384  579 TYR   B CD2 
18311 C  CE1 . TYR   B 579 ? 0.2626 0.2492 0.1865 -0.0117 0.0600  0.0287  579 TYR   B CE1 
18312 C  CE2 . TYR   B 579 ? 0.2729 0.2531 0.1645 -0.0038 0.0649  0.0314  579 TYR   B CE2 
18313 C  CZ  . TYR   B 579 ? 0.2411 0.2321 0.1546 -0.0093 0.0552  0.0269  579 TYR   B CZ  
18314 O  OH  . TYR   B 579 ? 0.2666 0.2657 0.1740 -0.0118 0.0414  0.0216  579 TYR   B OH  
18324 N  N   . SER   B 580 ? 0.2354 0.1685 0.2197 -0.0130 0.1082  0.0584  580 SER   B N   
18325 C  CA  . SER   B 580 ? 0.2577 0.1786 0.2600 -0.0129 0.1179  0.0696  580 SER   B CA  
18326 C  C   . SER   B 580 ? 0.2469 0.1539 0.2645 -0.0181 0.1047  0.0659  580 SER   B C   
18327 O  O   . SER   B 580 ? 0.2902 0.1836 0.3021 -0.0150 0.1080  0.0738  580 SER   B O   
18328 C  CB  . SER   B 580 ? 0.3056 0.2292 0.3261 -0.0135 0.1268  0.0728  580 SER   B CB  
18329 O  OG  . SER   B 580 ? 0.3026 0.2208 0.3428 -0.0113 0.1324  0.0817  580 SER   B OG  
18335 N  N   . VAL   B 581 ? 0.2322 0.1346 0.2630 -0.0261 0.0919  0.0559  581 VAL   B N   
18336 C  CA  . VAL   B 581 ? 0.2732 0.1499 0.3086 -0.0321 0.0796  0.0529  581 VAL   B CA  
18337 C  C   . VAL   B 581 ? 0.2708 0.1391 0.2775 -0.0252 0.0763  0.0502  581 VAL   B C   
18338 O  O   . VAL   B 581 ? 0.2990 0.1429 0.3012 -0.0251 0.0700  0.0502  581 VAL   B O   
18339 C  CB  . VAL   B 581 ? 0.3131 0.1825 0.3599 -0.0413 0.0647  0.0431  581 VAL   B CB  
18340 C  CG1 . VAL   B 581 ? 0.3268 0.2115 0.4087 -0.0447 0.0652  0.0452  581 VAL   B CG1 
18341 C  CG2 . VAL   B 581 ? 0.2630 0.1429 0.2933 -0.0405 0.0596  0.0328  581 VAL   B CG2 
18351 N  N   . ARG   B 582 ? 0.2412 0.1275 0.2285 -0.0193 0.0802  0.0481  582 ARG   B N   
18352 C  CA  . ARG   B 582 ? 0.2450 0.1273 0.2096 -0.0120 0.0797  0.0474  582 ARG   B CA  
18353 C  C   . ARG   B 582 ? 0.2610 0.1428 0.2232 -0.0035 0.0885  0.0582  582 ARG   B C   
18354 O  O   . ARG   B 582 ? 0.3000 0.1746 0.2472 0.0039  0.0896  0.0595  582 ARG   B O   
18355 C  CB  . ARG   B 582 ? 0.2330 0.1361 0.1884 -0.0100 0.0786  0.0426  582 ARG   B CB  
18356 C  CG  . ARG   B 582 ? 0.2506 0.1494 0.2000 -0.0163 0.0701  0.0323  582 ARG   B CG  
18357 C  CD  . ARG   B 582 ? 0.2386 0.1444 0.1805 -0.0117 0.0707  0.0302  582 ARG   B CD  
18358 N  NE  . ARG   B 582 ? 0.2948 0.1778 0.2166 -0.0050 0.0743  0.0313  582 ARG   B NE  
18359 C  CZ  . ARG   B 582 ? 0.2809 0.1395 0.1926 -0.0055 0.0710  0.0250  582 ARG   B CZ  
18360 N  NH1 . ARG   B 582 ? 0.3013 0.1566 0.2078 -0.0132 0.0630  0.0175  582 ARG   B NH1 
18361 N  NH2 . ARG   B 582 ? 0.3001 0.1320 0.1916 0.0023  0.0759  0.0262  582 ARG   B NH2 
18375 N  N   . GLY   B 583 ? 0.2654 0.1525 0.2366 -0.0033 0.0964  0.0676  583 GLY   B N   
18376 C  CA  . GLY   B 583 ? 0.2888 0.1757 0.2542 0.0055  0.1046  0.0793  583 GLY   B CA  
18377 C  C   . GLY   B 583 ? 0.3351 0.2401 0.2760 0.0131  0.1057  0.0821  583 GLY   B C   
18378 O  O   . GLY   B 583 ? 0.3036 0.2099 0.2461 0.0216  0.1074  0.0891  583 GLY   B O   
18382 N  N   . TRP   B 584 ? 0.2636 0.1871 0.2104 0.0102  0.1029  0.0766  584 TRP   B N   
18383 C  CA  . TRP   B 584 ? 0.2744 0.2142 0.2037 0.0159  0.0989  0.0779  584 TRP   B CA  
18384 C  C   . TRP   B 584 ? 0.3181 0.2585 0.2282 0.0187  0.1051  0.0838  584 TRP   B C   
18385 O  O   . TRP   B 584 ? 0.3206 0.2545 0.2414 0.0150  0.1143  0.0847  584 TRP   B O   
18386 C  CB  . TRP   B 584 ? 0.2676 0.2194 0.1971 0.0115  0.0893  0.0672  584 TRP   B CB  
18387 C  CG  . TRP   B 584 ? 0.2576 0.2059 0.1963 0.0111  0.0863  0.0627  584 TRP   B CG  
18388 C  CD1 . TRP   B 584 ? 0.2882 0.2199 0.2242 0.0153  0.0907  0.0659  584 TRP   B CD1 
18389 C  CD2 . TRP   B 584 ? 0.2565 0.2127 0.1966 0.0075  0.0802  0.0547  584 TRP   B CD2 
18390 N  NE1 . TRP   B 584 ? 0.2663 0.1942 0.2054 0.0157  0.0894  0.0605  584 TRP   B NE1 
18391 C  CE2 . TRP   B 584 ? 0.2566 0.1999 0.1966 0.0108  0.0837  0.0544  584 TRP   B CE2 
18392 C  CE3 . TRP   B 584 ? 0.2532 0.2239 0.1945 0.0023  0.0730  0.0483  584 TRP   B CE3 
18393 C  CZ2 . TRP   B 584 ? 0.2301 0.1755 0.1730 0.0095  0.0824  0.0490  584 TRP   B CZ2 
18394 C  CZ3 . TRP   B 584 ? 0.2444 0.2185 0.1902 -0.0003 0.0698  0.0432  584 TRP   B CZ3 
18395 C  CH2 . TRP   B 584 ? 0.2185 0.1810 0.1671 0.0035  0.0756  0.0442  584 TRP   B CH2 
18406 N  N   . SER   B 585 ? 0.2892 0.2385 0.1872 0.0254  0.0993  0.0877  585 SER   B N   
18407 C  CA  . SER   B 585 ? 0.3647 0.3061 0.2250 0.0303  0.1041  0.0924  585 SER   B CA  
18408 C  C   . SER   B 585 ? 0.3426 0.2883 0.2076 0.0250  0.1050  0.0821  585 SER   B C   
18409 O  O   . SER   B 585 ? 0.3427 0.2966 0.2214 0.0174  0.0979  0.0718  585 SER   B O   
18410 C  CB  . SER   B 585 ? 0.3341 0.2802 0.1812 0.0382  0.0909  0.0967  585 SER   B CB  
18411 O  OG  . SER   B 585 ? 0.3341 0.2906 0.1739 0.0356  0.0757  0.0885  585 SER   B OG  
18417 N  N   . LYS   B 586 ? 0.3880 0.3234 0.2239 0.0292  0.1111  0.0827  586 LYS   B N   
18418 C  CA  . LYS   B 586 ? 0.3419 0.2805 0.1825 0.0263  0.1113  0.0726  586 LYS   B CA  
18419 C  C   . LYS   B 586 ? 0.4069 0.3488 0.2184 0.0263  0.0936  0.0652  586 LYS   B C   
18420 O  O   . LYS   B 586 ? 0.4528 0.3964 0.2623 0.0220  0.0903  0.0544  586 LYS   B O   
18421 C  CB  . LYS   B 586 ? 0.4299 0.3512 0.2400 0.0332  0.1242  0.0760  586 LYS   B CB  
18422 C  CG  . LYS   B 586 ? 0.4574 0.3771 0.3009 0.0324  0.1413  0.0818  586 LYS   B CG  
18423 C  CD  . LYS   B 586 ? 0.6109 0.5146 0.4303 0.0398  0.1561  0.0849  586 LYS   B CD  
18424 C  CE  . LYS   B 586 ? 0.6444 0.5476 0.5035 0.0399  0.1734  0.0931  586 LYS   B CE  
18425 N  NZ  . LYS   B 586 ? 0.7915 0.6772 0.6242 0.0491  0.1905  0.0976  586 LYS   B NZ  
18439 N  N   . GLU   B 587 ? 0.3933 0.3406 0.2001 0.0298  0.0782  0.0692  587 GLU   B N   
18440 C  CA  . GLU   B 587 ? 0.3732 0.3312 0.1795 0.0275  0.0550  0.0627  587 GLU   B CA  
18441 C  C   . GLU   B 587 ? 0.3320 0.3086 0.1760 0.0201  0.0493  0.0590  587 GLU   B C   
18442 O  O   . GLU   B 587 ? 0.3207 0.3096 0.1759 0.0181  0.0324  0.0565  587 GLU   B O   
18443 C  CB  . GLU   B 587 ? 0.3962 0.3490 0.1807 0.0360  0.0398  0.0703  587 GLU   B CB  
18444 C  CG  . GLU   B 587 ? 0.5374 0.4623 0.2629 0.0450  0.0438  0.0738  587 GLU   B CG  
18445 C  CD  . GLU   B 587 ? 0.5753 0.4880 0.2983 0.0515  0.0683  0.0850  587 GLU   B CD  
18446 O  OE1 . GLU   B 587 ? 0.6010 0.5195 0.3394 0.0517  0.0736  0.0941  587 GLU   B OE1 
18447 O  OE2 . GLU   B 587 ? 0.7020 0.5977 0.3953 0.0536  0.0797  0.0819  587 GLU   B OE2 
18454 N  N   . GLY   B 588 ? 0.2783 0.2561 0.1494 0.0166  0.0627  0.0596  588 GLY   B N   
18455 C  CA  . GLY   B 588 ? 0.2877 0.2751 0.1843 0.0112  0.0602  0.0563  588 GLY   B CA  
18456 C  C   . GLY   B 588 ? 0.3199 0.3123 0.2236 0.0168  0.0572  0.0647  588 GLY   B C   
18457 O  O   . GLY   B 588 ? 0.3184 0.3215 0.2445 0.0148  0.0533  0.0627  588 GLY   B O   
18461 N  N   . ILE   B 589 ? 0.2729 0.2599 0.1733 0.0249  0.0606  0.0754  589 ILE   B N   
18462 C  CA  . ILE   B 589 ? 0.2710 0.2623 0.1817 0.0320  0.0589  0.0853  589 ILE   B CA  
18463 C  C   . ILE   B 589 ? 0.2708 0.2480 0.1870 0.0341  0.0737  0.0894  589 ILE   B C   
18464 O  O   . ILE   B 589 ? 0.2842 0.2486 0.1879 0.0354  0.0820  0.0939  589 ILE   B O   
18465 C  CB  . ILE   B 589 ? 0.3047 0.2968 0.2006 0.0400  0.0471  0.0947  589 ILE   B CB  
18466 C  CG1 . ILE   B 589 ? 0.3319 0.3290 0.2135 0.0371  0.0296  0.0889  589 ILE   B CG1 
18467 C  CG2 . ILE   B 589 ? 0.3155 0.3157 0.2301 0.0473  0.0433  0.1050  589 ILE   B CG2 
18468 C  CD1 . ILE   B 589 ? 0.3295 0.3455 0.2381 0.0318  0.0178  0.0840  589 ILE   B CD1 
18480 N  N   . PRO   B 590 ? 0.2603 0.2367 0.1945 0.0350  0.0781  0.0885  590 PRO   B N   
18481 C  CA  . PRO   B 590 ? 0.2672 0.2251 0.2041 0.0378  0.0891  0.0918  590 PRO   B CA  
18482 C  C   . PRO   B 590 ? 0.3061 0.2569 0.2325 0.0460  0.0920  0.1044  590 PRO   B C   
18483 O  O   . PRO   B 590 ? 0.2942 0.2563 0.2245 0.0531  0.0854  0.1120  590 PRO   B O   
18484 C  CB  . PRO   B 590 ? 0.2694 0.2260 0.2155 0.0418  0.0919  0.0902  590 PRO   B CB  
18485 C  CG  . PRO   B 590 ? 0.2470 0.2201 0.2027 0.0362  0.0857  0.0831  590 PRO   B CG  
18486 C  CD  . PRO   B 590 ? 0.2570 0.2455 0.2065 0.0341  0.0744  0.0847  590 PRO   B CD  
18494 N  N   . THR   B 591 ? 0.3140 0.2476 0.2375 0.0445  0.1006  0.1076  591 THR   B N   
18495 C  CA  . THR   B 591 ? 0.3177 0.2437 0.2387 0.0515  0.1039  0.1188  591 THR   B CA  
18496 C  C   . THR   B 591 ? 0.3329 0.2493 0.2579 0.0607  0.1077  0.1269  591 THR   B C   
18497 O  O   . THR   B 591 ? 0.3177 0.2292 0.2535 0.0597  0.1089  0.1191  591 THR   B O   
18498 C  CB  . THR   B 591 ? 0.3552 0.2653 0.2724 0.0467  0.1138  0.1211  591 THR   B CB  
18499 O  OG1 . THR   B 591 ? 0.3778 0.2722 0.3076 0.0422  0.1166  0.1167  591 THR   B OG1 
18500 C  CG2 . THR   B 591 ? 0.3641 0.2806 0.2755 0.0395  0.1145  0.1151  591 THR   B CG2 
18508 N  N   . GLU   B 592 ? 0.3428 0.2589 0.2681 0.0682  0.1055  0.1353  592 GLU   B N   
18509 C  CA  . GLU   B 592 ? 0.3537 0.2610 0.2900 0.0776  0.1092  0.1424  592 GLU   B CA  
18510 C  C   . GLU   B 592 ? 0.3900 0.2690 0.3235 0.0751  0.1194  0.1400  592 GLU   B C   
18511 O  O   . GLU   B 592 ? 0.3967 0.2652 0.3373 0.0806  0.1231  0.1378  592 GLU   B O   
18512 C  CB  . GLU   B 592 ? 0.3793 0.2839 0.3078 0.0854  0.1074  0.1555  592 GLU   B CB  
18513 C  CG  . GLU   B 592 ? 0.3885 0.2817 0.3282 0.0925  0.1114  0.1590  592 GLU   B CG  
18514 C  CD  . GLU   B 592 ? 0.4118 0.3031 0.3466 0.0998  0.1081  0.1715  592 GLU   B CD  
18515 O  OE1 . GLU   B 592 ? 0.4218 0.3177 0.3401 0.0983  0.1024  0.1757  592 GLU   B OE1 
18516 O  OE2 . GLU   B 592 ? 0.4283 0.3097 0.3709 0.1080  0.1117  0.1780  592 GLU   B OE2 
18523 N  N   . GLU   B 593 ? 0.3581 0.2346 0.3012 0.0650  0.1178  0.1320  593 GLU   B N   
18524 C  CA  . GLU   B 593 ? 0.4172 0.2628 0.3530 0.0609  0.1227  0.1304  593 GLU   B CA  
18525 C  C   . GLU   B 593 ? 0.3717 0.2091 0.3134 0.0562  0.1207  0.1187  593 GLU   B C   
18526 O  O   . GLU   B 593 ? 0.3669 0.1887 0.3088 0.0560  0.1162  0.1079  593 GLU   B O   
18527 C  CB  . GLU   B 593 ? 0.3673 0.2188 0.3251 0.0512  0.1210  0.1278  593 GLU   B CB  
18528 C  CG  . GLU   B 593 ? 0.4239 0.2693 0.3766 0.0574  0.1283  0.1439  593 GLU   B CG  
18529 C  CD  . GLU   B 593 ? 0.5215 0.3477 0.4644 0.0640  0.1287  0.1487  593 GLU   B CD  
18530 O  OE1 . GLU   B 593 ? 0.4916 0.3008 0.4554 0.0594  0.1264  0.1434  593 GLU   B OE1 
18531 O  OE2 . GLU   B 593 ? 0.4232 0.2599 0.3760 0.0733  0.1282  0.1556  593 GLU   B OE2 
18538 N  N   . THR   B 594 ? 0.3422 0.1995 0.2831 0.0503  0.1164  0.1107  594 THR   B N   
18539 C  CA  . THR   B 594 ? 0.3285 0.1799 0.2673 0.0455  0.1128  0.0982  594 THR   B CA  
18540 C  C   . THR   B 594 ? 0.3567 0.2009 0.2843 0.0568  0.1180  0.0991  594 THR   B C   
18541 O  O   . THR   B 594 ? 0.3569 0.1755 0.2769 0.0582  0.1191  0.0916  594 THR   B O   
18542 C  CB  . THR   B 594 ? 0.3299 0.1992 0.2668 0.0373  0.1098  0.0932  594 THR   B CB  
18543 O  OG1 . THR   B 594 ? 0.3282 0.1937 0.2729 0.0283  0.1098  0.0938  594 THR   B OG1 
18544 C  CG2 . THR   B 594 ? 0.3238 0.1908 0.2570 0.0337  0.1056  0.0813  594 THR   B CG2 
18552 N  N   . LEU   B 595 ? 0.3318 0.2003 0.2698 0.0651  0.1198  0.1073  595 LEU   B N   
18553 C  CA  . LEU   B 595 ? 0.3385 0.2087 0.2811 0.0768  0.1260  0.1103  595 LEU   B CA  
18554 C  C   . LEU   B 595 ? 0.3783 0.2157 0.3126 0.0859  0.1339  0.1124  595 LEU   B C   
18555 O  O   . LEU   B 595 ? 0.4093 0.2284 0.3336 0.0932  0.1418  0.1075  595 LEU   B O   
18556 C  CB  . LEU   B 595 ? 0.3301 0.2309 0.2863 0.0831  0.1224  0.1208  595 LEU   B CB  
18557 C  CG  . LEU   B 595 ? 0.3094 0.2394 0.2761 0.0752  0.1123  0.1183  595 LEU   B CG  
18558 C  CD1 . LEU   B 595 ? 0.3543 0.3073 0.3288 0.0816  0.1036  0.1294  595 LEU   B CD1 
18559 C  CD2 . LEU   B 595 ? 0.3176 0.2503 0.2828 0.0710  0.1144  0.1082  595 LEU   B CD2 
18571 N  N   . LYS   B 596 ? 0.4040 0.2305 0.3381 0.0864  0.1329  0.1197  596 LYS   B N   
18572 C  CA  . LYS   B 596 ? 0.4387 0.2378 0.3681 0.0930  0.1363  0.1188  596 LYS   B CA  
18573 C  C   . LYS   B 596 ? 0.4584 0.2242 0.3683 0.0866  0.1330  0.1040  596 LYS   B C   
18574 O  O   . LYS   B 596 ? 0.4684 0.2117 0.3674 0.0947  0.1379  0.0982  596 LYS   B O   
18575 C  CB  . LYS   B 596 ? 0.4605 0.2613 0.3979 0.0908  0.1328  0.1273  596 LYS   B CB  
18576 C  CG  . LYS   B 596 ? 0.4932 0.3172 0.4416 0.0992  0.1335  0.1416  596 LYS   B CG  
18577 C  CD  . LYS   B 596 ? 0.5682 0.3820 0.5118 0.1015  0.1330  0.1494  596 LYS   B CD  
18578 C  CE  . LYS   B 596 ? 0.5229 0.3551 0.4784 0.0980  0.1292  0.1589  596 LYS   B CE  
18579 N  NZ  . LYS   B 596 ? 0.6026 0.4181 0.5495 0.0943  0.1299  0.1629  596 LYS   B NZ  
18593 N  N   . LYS   B 597 ? 0.4133 0.1821 0.3313 0.0717  0.1224  0.0959  597 LYS   B N   
18594 C  CA  . LYS   B 597 ? 0.4706 0.2028 0.3671 0.0646  0.1141  0.0841  597 LYS   B CA  
18595 C  C   . LYS   B 597 ? 0.4522 0.1729 0.3308 0.0697  0.1182  0.0744  597 LYS   B C   
18596 O  O   . LYS   B 597 ? 0.4804 0.1693 0.3354 0.0708  0.1134  0.0641  597 LYS   B O   
18597 C  CB  . LYS   B 597 ? 0.4867 0.2247 0.3984 0.0488  0.1033  0.0814  597 LYS   B CB  
18598 C  CG  . LYS   B 597 ? 0.5140 0.2277 0.4197 0.0394  0.0887  0.0680  597 LYS   B CG  
18599 C  CD  . LYS   B 597 ? 0.5675 0.2938 0.4847 0.0258  0.0809  0.0659  597 LYS   B CD  
18600 C  CE  . LYS   B 597 ? 0.5762 0.3291 0.4974 0.0262  0.0898  0.0679  597 LYS   B CE  
18601 N  NZ  . LYS   B 597 ? 0.6104 0.3771 0.5460 0.0139  0.0844  0.0668  597 LYS   B NZ  
18615 N  N   . LEU   B 598 ? 0.4351 0.1795 0.3169 0.0729  0.1262  0.0782  598 LEU   B N   
18616 C  CA  . LEU   B 598 ? 0.4532 0.1879 0.3140 0.0771  0.1322  0.0712  598 LEU   B CA  
18617 C  C   . LEU   B 598 ? 0.4357 0.1777 0.2992 0.0916  0.1460  0.0722  598 LEU   B C   
18618 O  O   . LEU   B 598 ? 0.4643 0.1861 0.3057 0.0997  0.1575  0.0700  598 LEU   B O   
18619 C  CB  . LEU   B 598 ? 0.4124 0.1868 0.2917 0.0688  0.1290  0.0706  598 LEU   B CB  
18620 C  CG  . LEU   B 598 ? 0.3946 0.1738 0.2779 0.0526  0.1149  0.0637  598 LEU   B CG  
18621 C  CD1 . LEU   B 598 ? 0.3508 0.1651 0.2467 0.0463  0.1129  0.0623  598 LEU   B CD1 
18622 C  CD2 . LEU   B 598 ? 0.4506 0.1864 0.3080 0.0474  0.1058  0.0523  598 LEU   B CD2 
18634 N  N   . GLY   B 599 ? 0.4392 0.1893 0.3153 0.0997  0.1509  0.0815  599 GLY   B N   
18635 C  CA  . GLY   B 599 ? 0.4576 0.2075 0.3365 0.1158  0.1673  0.0882  599 GLY   B CA  
18636 C  C   . GLY   B 599 ? 0.4615 0.2366 0.3632 0.1269  0.1797  0.1040  599 GLY   B C   
18637 O  O   . GLY   B 599 ? 0.4478 0.2346 0.3602 0.1350  0.1932  0.1048  599 GLY   B O   
18641 N  N   . LEU   B 600 ? 0.4025 0.2168 0.3324 0.1154  0.1670  0.1073  600 LEU   B N   
18642 C  CA  . LEU   B 600 ? 0.4069 0.2631 0.3613 0.1167  0.1666  0.1164  600 LEU   B CA  
18643 C  C   . LEU   B 600 ? 0.3870 0.2672 0.3714 0.1215  0.1601  0.1305  600 LEU   B C   
18644 O  O   . LEU   B 600 ? 0.3865 0.2996 0.3876 0.1159  0.1483  0.1355  600 LEU   B O   
18645 C  CB  . LEU   B 600 ? 0.3500 0.2279 0.3127 0.1013  0.1549  0.1086  600 LEU   B CB  
18646 C  CG  . LEU   B 600 ? 0.3998 0.2564 0.3350 0.0970  0.1599  0.0966  600 LEU   B CG  
18647 C  CD1 . LEU   B 600 ? 0.3697 0.2437 0.3078 0.0810  0.1461  0.0887  600 LEU   B CD1 
18648 C  CD2 . LEU   B 600 ? 0.4189 0.2777 0.3635 0.1088  0.1777  0.1011  600 LEU   B CD2 
18660 N  N   . ASP   B 601 ? 0.4120 0.2710 0.3911 0.1322  0.1663  0.1369  601 ASP   B N   
18661 C  CA  . ASP   B 601 ? 0.4111 0.2854 0.4114 0.1376  0.1597  0.1509  601 ASP   B CA  
18662 C  C   . ASP   B 601 ? 0.3809 0.2925 0.4164 0.1443  0.1565  0.1631  601 ASP   B C   
18663 O  O   . ASP   B 601 ? 0.3744 0.3055 0.4204 0.1429  0.1416  0.1726  601 ASP   B O   
18664 C  CB  . ASP   B 601 ? 0.4961 0.3416 0.4824 0.1464  0.1674  0.1513  601 ASP   B CB  
18665 C  CG  . ASP   B 601 ? 0.5640 0.3724 0.5131 0.1376  0.1665  0.1370  601 ASP   B CG  
18666 O  OD1 . ASP   B 601 ? 0.5209 0.3090 0.4612 0.1384  0.1742  0.1257  601 ASP   B OD1 
18667 O  OD2 . ASP   B 601 ? 0.5179 0.3230 0.4715 0.1296  0.1571  0.1376  601 ASP   B OD2 
18672 N  N   . GLU   B 602 ? 0.3811 0.3005 0.4355 0.1516  0.1695  0.1640  602 GLU   B N   
18673 C  CA  . GLU   B 602 ? 0.3715 0.3278 0.4767 0.1586  0.1669  0.1778  602 GLU   B CA  
18674 C  C   . GLU   B 602 ? 0.3741 0.3605 0.4840 0.1454  0.1444  0.1781  602 GLU   B C   
18675 O  O   . GLU   B 602 ? 0.3608 0.3770 0.5113 0.1486  0.1332  0.1899  602 GLU   B O   
18676 C  CB  . GLU   B 602 ? 0.4657 0.4189 0.5781 0.1697  0.1899  0.1801  602 GLU   B CB  
18677 C  CG  . GLU   B 602 ? 0.4065 0.3695 0.5318 0.1603  0.1936  0.1714  602 GLU   B CG  
18678 C  CD  . GLU   B 602 ? 0.5268 0.4838 0.6474 0.1664  0.2162  0.1738  602 GLU   B CD  
18679 O  OE1 . GLU   B 602 ? 0.5098 0.4310 0.6005 0.1686  0.2322  0.1648  602 GLU   B OE1 
18680 O  OE2 . GLU   B 602 ? 0.5047 0.4961 0.6789 0.1660  0.2145  0.1852  602 GLU   B OE2 
18687 N  N   . TYR   B 603 ? 0.3337 0.3143 0.4180 0.1306  0.1365  0.1647  603 TYR   B N   
18688 C  CA  . TYR   B 603 ? 0.3242 0.3289 0.4086 0.1178  0.1162  0.1615  603 TYR   B CA  
18689 C  C   . TYR   B 603 ? 0.3557 0.3556 0.4152 0.1123  0.0999  0.1625  603 TYR   B C   
18690 O  O   . TYR   B 603 ? 0.3486 0.3626 0.4042 0.1034  0.0828  0.1600  603 TYR   B O   
18691 C  CB  . TYR   B 603 ? 0.3065 0.3079 0.3793 0.1067  0.1207  0.1477  603 TYR   B CB  
18692 C  CG  . TYR   B 603 ? 0.3002 0.3035 0.3917 0.1127  0.1385  0.1480  603 TYR   B CG  
18693 C  CD1 . TYR   B 603 ? 0.2907 0.3242 0.4255 0.1152  0.1364  0.1579  603 TYR   B CD1 
18694 C  CD2 . TYR   B 603 ? 0.3349 0.3061 0.3985 0.1167  0.1581  0.1400  603 TYR   B CD2 
18695 C  CE1 . TYR   B 603 ? 0.3086 0.3433 0.4614 0.1218  0.1568  0.1610  603 TYR   B CE1 
18696 C  CE2 . TYR   B 603 ? 0.3256 0.2937 0.4025 0.1243  0.1778  0.1417  603 TYR   B CE2 
18697 C  CZ  . TYR   B 603 ? 0.3319 0.3322 0.4517 0.1273  0.1797  0.1531  603 TYR   B CZ  
18698 O  OH  . TYR   B 603 ? 0.3267 0.3204 0.4562 0.1325  0.1988  0.1557  603 TYR   B OH  
18708 N  N   . ILE   B 604 ? 0.3668 0.3457 0.4123 0.1183  0.1059  0.1666  604 ILE   B N   
18709 C  CA  . ILE   B 604 ? 0.4050 0.3742 0.4218 0.1147  0.0957  0.1699  604 ILE   B CA  
18710 C  C   . ILE   B 604 ? 0.3865 0.3760 0.4215 0.1189  0.0760  0.1821  604 ILE   B C   
18711 O  O   . ILE   B 604 ? 0.4283 0.4275 0.4869 0.1295  0.0741  0.1931  604 ILE   B O   
18712 C  CB  . ILE   B 604 ? 0.3925 0.3336 0.3967 0.1198  0.1076  0.1724  604 ILE   B CB  
18713 C  CG1 . ILE   B 604 ? 0.4012 0.3190 0.3907 0.1125  0.1195  0.1592  604 ILE   B CG1 
18714 C  CG2 . ILE   B 604 ? 0.4012 0.3355 0.3872 0.1201  0.0994  0.1818  604 ILE   B CG2 
18715 C  CD1 . ILE   B 604 ? 0.4751 0.3606 0.4478 0.1172  0.1290  0.1611  604 ILE   B CD1 
18727 N  N   . GLY   B 605 ? 0.4234 0.4130 0.4284 0.1118  0.0609  0.1808  605 GLY   B N   
18728 C  CA  . GLY   B 605 ? 0.4242 0.4235 0.4322 0.1160  0.0382  0.1913  605 GLY   B CA  
18729 C  C   . GLY   B 605 ? 0.4607 0.4848 0.4929 0.1124  0.0190  0.1905  605 GLY   B C   
18730 O  O   . GLY   B 605 ? 0.5049 0.5335 0.5339 0.1153  -0.0049 0.1989  605 GLY   B O   
18734 N  N   . LYS   B 606 ? 0.4839 0.5203 0.5344 0.1060  0.0271  0.1809  606 LYS   B N   
18735 C  CA  . LYS   B 606 ? 0.4754 0.5370 0.5586 0.1022  0.0106  0.1813  606 LYS   B CA  
18736 C  C   . LYS   B 606 ? 0.4427 0.5060 0.5077 0.0891  0.0002  0.1676  606 LYS   B C   
18737 O  O   . LYS   B 606 ? 0.4313 0.5114 0.5157 0.0847  -0.0193 0.1680  606 LYS   B O   
18738 C  CB  . LYS   B 606 ? 0.4546 0.5319 0.5880 0.1073  0.0277  0.1854  606 LYS   B CB  
18739 C  CG  . LYS   B 606 ? 0.4530 0.5311 0.6173 0.1221  0.0378  0.1995  606 LYS   B CG  
18740 C  CD  . LYS   B 606 ? 0.5092 0.5820 0.6889 0.1293  0.0679  0.1993  606 LYS   B CD  
18741 C  CE  . LYS   B 606 ? 0.5368 0.6125 0.7544 0.1458  0.0783  0.2143  606 LYS   B CE  
18742 N  NZ  . LYS   B 606 ? 0.6198 0.6992 0.8631 0.1541  0.1039  0.2172  606 LYS   B NZ  
18756 N  N   . PHE   B 607 ? 0.4726 0.5172 0.4963 0.0830  0.0125  0.1560  607 PHE   B N   
18757 C  CA  . PHE   B 607 ? 0.5134 0.5568 0.5140 0.0715  0.0071  0.1422  607 PHE   B CA  
18758 C  C   . PHE   B 607 ? 0.5613 0.5800 0.5034 0.0696  0.0049  0.1346  607 PHE   B C   
18759 O  O   . PHE   B 607 ? 0.5407 0.5599 0.4713 0.0654  -0.0093 0.1326  607 PHE   B O   
18760 C  CB  . PHE   B 607 ? 0.5172 0.5617 0.5271 0.0649  0.0256  0.1315  607 PHE   B CB  
18761 C  CG  . PHE   B 607 ? 0.4804 0.5414 0.5305 0.0672  0.0327  0.1348  607 PHE   B CG  
18762 C  CD1 . PHE   B 607 ? 0.4512 0.5085 0.5215 0.0770  0.0506  0.1421  607 PHE   B CD1 
18763 C  CD2 . PHE   B 607 ? 0.4036 0.4830 0.4796 0.0605  0.0236  0.1319  607 PHE   B CD2 
18764 C  CE1 . PHE   B 607 ? 0.4103 0.4801 0.5166 0.0814  0.0615  0.1466  607 PHE   B CE1 
18765 C  CE2 . PHE   B 607 ? 0.2705 0.3676 0.3995 0.0636  0.0340  0.1375  607 PHE   B CE2 
18766 C  CZ  . PHE   B 607 ? 0.3667 0.4554 0.4950 0.0747  0.0542  0.1450  607 PHE   B CZ  
18767 O  OXT . PHE   B 607 ? 0.3679 0.3703 0.3745 0.0007  0.0001  0.0043  607 PHE   B OXT 
18777 FE FE1 . SF4   C .   ? 0.1477 0.1496 0.1484 -0.0026 -0.0006 -0.0004 701 SF4   A FE1 
18778 FE FE2 . SF4   C .   ? 0.1532 0.1555 0.1532 -0.0025 -0.0013 0.0016  701 SF4   A FE2 
18779 FE FE3 . SF4   C .   ? 0.1639 0.1659 0.1642 -0.0022 -0.0013 0.0004  701 SF4   A FE3 
18780 FE FE4 . SF4   C .   ? 0.1480 0.1501 0.1496 -0.0020 -0.0013 0.0013  701 SF4   A FE4 
18781 S  S1  . SF4   C .   ? 0.1753 0.1750 0.1724 -0.0003 -0.0002 0.0003  701 SF4   A S1  
18782 S  S2  . SF4   C .   ? 0.1685 0.1685 0.1660 -0.0001 -0.0005 0.0001  701 SF4   A S2  
18783 S  S3  . SF4   C .   ? 0.1476 0.1483 0.1476 -0.0007 -0.0002 0.0003  701 SF4   A S3  
18784 S  S4  . SF4   C .   ? 0.1409 0.1423 0.1427 -0.0010 -0.0002 0.0000  701 SF4   A S4  
18785 C  C1  . A1IJH D .   ? 0.1162 0.1158 0.1138 -0.0001 0.0001  0.0000  702 A1IJH A C1  
18786 C  C2  . A1IJH D .   ? 0.0888 0.0895 0.0921 0.0000  0.0000  0.0001  702 A1IJH A C2  
18787 C  C3  . A1IJH D .   ? 0.1046 0.1046 0.1045 0.0002  0.0000  0.0000  702 A1IJH A C3  
18788 S  S3  . A1IJH D .   ? 0.1157 0.1161 0.1153 -0.0002 0.0000  0.0007  702 A1IJH A S3  
18789 C  C4  . A1IJH D .   ? 0.1093 0.1096 0.1104 -0.0002 0.0002  0.0001  702 A1IJH A C4  
18790 S  S4  . A1IJH D .   ? 0.1272 0.1275 0.1270 -0.0004 -0.0001 0.0002  702 A1IJH A S4  
18791 C  C5  . A1IJH D .   ? 0.1178 0.1179 0.1182 0.0000  0.0000  0.0000  702 A1IJH A C5  
18792 N  N6  . A1IJH D .   ? 0.1533 0.1523 0.1493 0.0001  0.0001  0.0000  702 A1IJH A N6  
18793 C  C7  . A1IJH D .   ? 0.1062 0.1067 0.1078 -0.0001 0.0000  0.0001  702 A1IJH A C7  
18794 C  C8  . A1IJH D .   ? 0.0950 0.0952 0.0963 0.0000  0.0000  -0.0001 702 A1IJH A C8  
18795 O  O8  . A1IJH D .   ? 0.0903 0.0904 0.0905 -0.0002 -0.0002 0.0001  702 A1IJH A O8  
18796 N  N9  . A1IJH D .   ? 0.1157 0.1150 0.1126 -0.0001 -0.0001 0.0000  702 A1IJH A N9  
18797 C  C10 . A1IJH D .   ? 0.0720 0.0733 0.0782 0.0000  0.0000  0.0000  702 A1IJH A C10 
18798 N  N10 . A1IJH D .   ? 0.1284 0.1278 0.1257 -0.0002 -0.0001 -0.0001 702 A1IJH A N10 
18799 N  N11 . A1IJH D .   ? 0.1002 0.0999 0.0989 -0.0001 0.0000  0.0001  702 A1IJH A N11 
18800 C  C12 . A1IJH D .   ? 0.1028 0.1031 0.1036 0.0000  -0.0001 -0.0001 702 A1IJH A C12 
18801 N  N13 . A1IJH D .   ? 0.1180 0.1177 0.1164 0.0000  0.0000  0.0001  702 A1IJH A N13 
18802 C  C14 . A1IJH D .   ? 0.0977 0.0984 0.1004 0.0000  0.0001  0.0001  702 A1IJH A C14 
18803 O  O2  . A1IJH D .   ? 0.1131 0.1129 0.1113 0.0002  0.0000  0.0001  702 A1IJH A O2  
18804 C  C21 . A1IJH D .   ? 0.1644 0.1638 0.1613 0.0000  -0.0001 0.0000  702 A1IJH A C21 
18805 C  C22 . A1IJH D .   ? 0.1214 0.1222 0.1247 0.0000  -0.0001 0.0000  702 A1IJH A C22 
18806 C  C23 . A1IJH D .   ? 0.1363 0.1362 0.1364 0.0001  0.0000  0.0000  702 A1IJH A C23 
18807 S  S23 . A1IJH D .   ? 0.1348 0.1350 0.1348 -0.0005 -0.0002 -0.0005 702 A1IJH A S23 
18808 C  C24 . A1IJH D .   ? 0.1529 0.1525 0.1511 -0.0001 0.0000  -0.0001 702 A1IJH A C24 
18809 S  S24 . A1IJH D .   ? 0.1328 0.1332 0.1336 0.0008  -0.0004 -0.0002 702 A1IJH A S24 
18810 C  C25 . A1IJH D .   ? 0.1521 0.1520 0.1523 -0.0001 0.0002  0.0000  702 A1IJH A C25 
18811 N  N26 . A1IJH D .   ? 0.1514 0.1511 0.1503 0.0001  0.0000  0.0001  702 A1IJH A N26 
18812 C  C27 . A1IJH D .   ? 0.1289 0.1296 0.1319 -0.0002 0.0000  0.0000  702 A1IJH A C27 
18813 C  C28 . A1IJH D .   ? 0.1465 0.1458 0.1436 -0.0001 0.0000  -0.0002 702 A1IJH A C28 
18814 O  O28 . A1IJH D .   ? 0.1204 0.1206 0.1215 -0.0002 0.0001  0.0000  702 A1IJH A O28 
18815 N  N29 . A1IJH D .   ? 0.1290 0.1289 0.1285 0.0000  0.0001  0.0000  702 A1IJH A N29 
18816 C  C30 . A1IJH D .   ? 0.1009 0.1021 0.1066 -0.0002 -0.0001 0.0000  702 A1IJH A C30 
18817 N  N30 . A1IJH D .   ? 0.1417 0.1413 0.1397 0.0000  0.0000  -0.0001 702 A1IJH A N30 
18818 N  N31 . A1IJH D .   ? 0.1501 0.1497 0.1479 0.0000  0.0000  0.0000  702 A1IJH A N31 
18819 C  C32 . A1IJH D .   ? 0.1530 0.1529 0.1522 -0.0001 0.0001  -0.0001 702 A1IJH A C32 
18820 N  N33 . A1IJH D .   ? 0.1621 0.1619 0.1614 0.0000  -0.0001 0.0002  702 A1IJH A N33 
18821 C  C34 . A1IJH D .   ? 0.1564 0.1562 0.1553 0.0000  -0.0001 -0.0001 702 A1IJH A C34 
18822 O  O22 . A1IJH D .   ? 0.1326 0.1327 0.1333 0.0001  0.0000  -0.0002 702 A1IJH A O22 
18823 P  P1  . A1IJH D .   ? 0.1174 0.1166 0.1138 0.0000  0.0001  0.0002  702 A1IJH A P1  
18824 O  O1P . A1IJH D .   ? 0.0941 0.0945 0.0955 -0.0002 -0.0002 -0.0002 702 A1IJH A O1P 
18825 O  O2P . A1IJH D .   ? 0.1024 0.1027 0.1033 -0.0002 -0.0001 0.0002  702 A1IJH A O2P 
18826 O  O3P . A1IJH D .   ? 0.1024 0.1028 0.1032 -0.0001 0.0000  0.0000  702 A1IJH A O3P 
18827 O  O4P . A1IJH D .   ? 0.0958 0.0961 0.0980 -0.0002 -0.0003 0.0000  702 A1IJH A O4P 
18828 P  P2  . A1IJH D .   ? 0.1240 0.1248 0.1258 0.0002  -0.0002 -0.0004 702 A1IJH A P2  
18829 O  O5P . A1IJH D .   ? 0.1127 0.1129 0.1137 -0.0002 -0.0001 -0.0001 702 A1IJH A O5P 
18830 O  O6P . A1IJH D .   ? 0.1298 0.1296 0.1296 -0.0001 -0.0001 0.0000  702 A1IJH A O6P 
18831 O  O7P . A1IJH D .   ? 0.1486 0.1484 0.1473 -0.0002 -0.0001 0.0001  702 A1IJH A O7P 
18832 O  O8P . A1IJH D .   ? 0.1420 0.1422 0.1423 -0.0001 -0.0002 0.0001  702 A1IJH A O8P 
18833 MG MG  . A1IJH D .   ? 0.0958 0.0959 0.0961 -0.0006 -0.0002 0.0002  702 A1IJH A MG  
18834 W  W   . A1IJH D .   ? 0.2279 0.2302 0.2289 -0.0039 -0.0028 0.0016  702 A1IJH A W   
18855 CL CL  . CL    E .   ? 0.2645 0.2646 0.2645 -0.0003 -0.0002 0.0000  703 CL    A CL  
18856 MG MG  . MG    F .   ? 0.3664 0.3664 0.3664 -0.0001 0.0001  0.0000  704 MG    A MG  
18857 FE FE1 . SF4   G .   ? 0.1747 0.1740 0.1718 0.0026  0.0000  0.0002  701 SF4   B FE1 
18858 FE FE2 . SF4   G .   ? 0.1648 0.1659 0.1628 0.0024  0.0008  0.0015  701 SF4   B FE2 
18859 FE FE3 . SF4   G .   ? 0.1745 0.1757 0.1729 0.0013  0.0006  0.0002  701 SF4   B FE3 
18860 FE FE4 . SF4   G .   ? 0.1658 0.1658 0.1625 0.0032  0.0007  0.0003  701 SF4   B FE4 
18861 S  S1  . SF4   G .   ? 0.1578 0.1588 0.1593 0.0004  -0.0002 -0.0003 701 SF4   B S1  
18862 S  S2  . SF4   G .   ? 0.1816 0.1813 0.1797 -0.0001 0.0000  -0.0004 701 SF4   B S2  
18863 S  S3  . SF4   G .   ? 0.1574 0.1579 0.1587 0.0002  0.0003  0.0004  701 SF4   B S3  
18864 S  S4  . SF4   G .   ? 0.1780 0.1784 0.1773 0.0004  0.0002  -0.0003 701 SF4   B S4  
18865 C  C1  . A1IJH H .   ? 0.1131 0.1135 0.1150 0.0002  0.0000  -0.0001 702 A1IJH B C1  
18866 C  C2  . A1IJH H .   ? 0.1333 0.1331 0.1322 -0.0001 0.0001  0.0001  702 A1IJH B C2  
18867 C  C3  . A1IJH H .   ? 0.1216 0.1221 0.1237 0.0000  0.0001  0.0000  702 A1IJH B C3  
18868 S  S3  . A1IJH H .   ? 0.1428 0.1426 0.1420 0.0005  0.0007  0.0003  702 A1IJH B S3  
18869 C  C4  . A1IJH H .   ? 0.1314 0.1315 0.1319 0.0001  -0.0002 -0.0001 702 A1IJH B C4  
18870 S  S4  . A1IJH H .   ? 0.1444 0.1449 0.1437 0.0012  0.0005  -0.0001 702 A1IJH B S4  
18871 C  C5  . A1IJH H .   ? 0.1395 0.1396 0.1402 0.0002  0.0001  0.0001  702 A1IJH B C5  
18872 N  N6  . A1IJH H .   ? 0.1470 0.1465 0.1454 0.0002  -0.0001 0.0000  702 A1IJH B N6  
18873 C  C7  . A1IJH H .   ? 0.1200 0.1202 0.1211 0.0001  0.0001  0.0001  702 A1IJH B C7  
18874 C  C8  . A1IJH H .   ? 0.1139 0.1144 0.1163 0.0001  -0.0001 -0.0001 702 A1IJH B C8  
18875 O  O8  . A1IJH H .   ? 0.1442 0.1437 0.1427 0.0001  0.0002  0.0001  702 A1IJH B O8  
18876 N  N9  . A1IJH H .   ? 0.1250 0.1247 0.1239 0.0002  0.0000  0.0000  702 A1IJH B N9  
18877 C  C10 . A1IJH H .   ? 0.1098 0.1105 0.1130 0.0001  0.0000  0.0000  702 A1IJH B C10 
18878 N  N10 . A1IJH H .   ? 0.1481 0.1477 0.1464 0.0001  0.0000  0.0000  702 A1IJH B N10 
18879 N  N11 . A1IJH H .   ? 0.1242 0.1239 0.1234 0.0002  0.0002  0.0001  702 A1IJH B N11 
18880 C  C12 . A1IJH H .   ? 0.1211 0.1213 0.1217 0.0001  0.0000  -0.0001 702 A1IJH B C12 
18881 N  N13 . A1IJH H .   ? 0.1297 0.1299 0.1306 0.0001  0.0001  0.0000  702 A1IJH B N13 
18882 C  C14 . A1IJH H .   ? 0.1563 0.1557 0.1536 -0.0001 0.0000  0.0000  702 A1IJH B C14 
18883 O  O2  . A1IJH H .   ? 0.1422 0.1422 0.1425 0.0000  0.0001  0.0002  702 A1IJH B O2  
18884 C  C21 . A1IJH H .   ? 0.1717 0.1714 0.1703 0.0001  0.0000  0.0000  702 A1IJH B C21 
18885 C  C22 . A1IJH H .   ? 0.1639 0.1636 0.1623 0.0000  0.0000  0.0001  702 A1IJH B C22 
18886 C  C23 . A1IJH H .   ? 0.1596 0.1592 0.1584 0.0000  0.0001  0.0000  702 A1IJH B C23 
18887 S  S23 . A1IJH H .   ? 0.1114 0.1122 0.1136 0.0008  0.0003  -0.0003 702 A1IJH B S23 
18888 C  C24 . A1IJH H .   ? 0.1786 0.1780 0.1761 0.0000  0.0000  -0.0001 702 A1IJH B C24 
18889 S  S24 . A1IJH H .   ? 0.1537 0.1540 0.1548 0.0000  0.0001  -0.0001 702 A1IJH B S24 
18890 C  C25 . A1IJH H .   ? 0.1705 0.1704 0.1700 0.0002  -0.0001 0.0000  702 A1IJH B C25 
18891 N  N26 . A1IJH H .   ? 0.1735 0.1732 0.1723 -0.0001 0.0000  -0.0001 702 A1IJH B N26 
18892 C  C27 . A1IJH H .   ? 0.1529 0.1533 0.1547 0.0001  0.0001  0.0001  702 A1IJH B C27 
18893 C  C28 . A1IJH H .   ? 0.1714 0.1705 0.1678 0.0001  0.0000  -0.0001 702 A1IJH B C28 
18894 O  O28 . A1IJH H .   ? 0.1397 0.1399 0.1411 0.0003  -0.0001 0.0001  702 A1IJH B O28 
18895 N  N29 . A1IJH H .   ? 0.1485 0.1487 0.1494 0.0000  0.0000  0.0000  702 A1IJH B N29 
18896 C  C30 . A1IJH H .   ? 0.1447 0.1450 0.1459 0.0001  -0.0001 0.0000  702 A1IJH B C30 
18897 N  N30 . A1IJH H .   ? 0.1593 0.1590 0.1585 0.0001  0.0000  0.0000  702 A1IJH B N30 
18898 N  N31 . A1IJH H .   ? 0.1523 0.1521 0.1518 0.0001  0.0001  0.0001  702 A1IJH B N31 
18899 C  C32 . A1IJH H .   ? 0.1517 0.1520 0.1531 0.0001  -0.0001 -0.0001 702 A1IJH B C32 
18900 N  N33 . A1IJH H .   ? 0.1782 0.1776 0.1754 0.0000  0.0001  0.0001  702 A1IJH B N33 
18901 C  C34 . A1IJH H .   ? 0.1468 0.1472 0.1484 0.0000  0.0001  -0.0001 702 A1IJH B C34 
18902 O  O22 . A1IJH H .   ? 0.1269 0.1275 0.1295 0.0000  -0.0001 -0.0001 702 A1IJH B O22 
18903 P  P1  . A1IJH H .   ? 0.1470 0.1466 0.1448 0.0004  -0.0002 0.0001  702 A1IJH B P1  
18904 O  O1P . A1IJH H .   ? 0.1639 0.1636 0.1634 0.0003  0.0002  0.0000  702 A1IJH B O1P 
18905 O  O2P . A1IJH H .   ? 0.1215 0.1219 0.1228 0.0003  0.0000  0.0000  702 A1IJH B O2P 
18906 O  O3P . A1IJH H .   ? 0.1239 0.1244 0.1249 0.0003  -0.0001 0.0001  702 A1IJH B O3P 
18907 O  O4P . A1IJH H .   ? 0.1323 0.1323 0.1320 0.0003  0.0001  -0.0001 702 A1IJH B O4P 
18908 P  P2  . A1IJH H .   ? 0.1435 0.1432 0.1429 0.0000  0.0003  -0.0003 702 A1IJH B P2  
18909 O  O5P . A1IJH H .   ? 0.1124 0.1129 0.1140 0.0001  0.0001  -0.0002 702 A1IJH B O5P 
18910 O  O6P . A1IJH H .   ? 0.1412 0.1412 0.1413 0.0003  0.0001  0.0001  702 A1IJH B O6P 
18911 O  O7P . A1IJH H .   ? 0.1561 0.1559 0.1554 0.0000  0.0001  0.0001  702 A1IJH B O7P 
18912 O  O8P . A1IJH H .   ? 0.1509 0.1510 0.1516 0.0000  0.0000  0.0001  702 A1IJH B O8P 
18913 MG MG  . A1IJH H .   ? 0.1107 0.1109 0.1108 0.0008  0.0001  0.0002  702 A1IJH B MG  
18914 W  W   . A1IJH H .   ? 0.2474 0.2484 0.2470 0.0049  0.0019  0.0022  702 A1IJH B W   
18935 C  C1  . EDO   I .   ? 0.3838 0.3839 0.3846 0.0000  0.0000  0.0000  703 EDO   B C1  
18936 O  O1  . EDO   I .   ? 0.3330 0.3335 0.3354 0.0000  0.0000  0.0000  703 EDO   B O1  
18937 C  C2  . EDO   I .   ? 0.4518 0.4516 0.4505 0.0000  0.0000  0.0000  703 EDO   B C2  
18938 O  O2  . EDO   I .   ? 0.4921 0.4916 0.4902 0.0000  0.0000  0.0000  703 EDO   B O2  
18945 C  C1  . EDO   J .   ? 0.2399 0.2399 0.2398 0.0000  0.0000  0.0000  704 EDO   B C1  
18946 O  O1  . EDO   J .   ? 0.2400 0.2401 0.2400 0.0000  0.0000  0.0000  704 EDO   B O1  
18947 C  C2  . EDO   J .   ? 0.2399 0.2399 0.2398 0.0000  0.0001  -0.0001 704 EDO   B C2  
18948 O  O2  . EDO   J .   ? 0.2400 0.2402 0.2400 -0.0001 0.0001  -0.0001 704 EDO   B O2  
18955 CL CL  . CL    K .   ? 0.2114 0.2116 0.2115 0.0000  0.0001  0.0002  705 CL    B CL  
18956 CL CL  . CL    L .   ? 0.3664 0.3665 0.3664 0.0001  0.0001  -0.0001 706 CL    B CL  
# 
