data_8Z0O
# 
_entry.id   8Z0O 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8Z0O         pdb_00008z0o 10.2210/pdb8z0o/pdb 
WWPDB D_1300046775 ?            ?                   
EMDB  EMD-39709    ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-12-04 
# 
_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                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8Z0O 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'Cryo-EM structure of chitin synthase' 
_pdbx_database_related.db_id          EMD-39709 
_pdbx_database_related.content_type   'associated EM volume' 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 zhangxiaoyue@qdio.ac.cn Xiaoyue Zhang ? 'principal investigator/group leader' 0009-0004-0701-2925 
3 niusuhao@qdio.ac.cn     Suhao   Niu   ? 'principal investigator/group leader' 0009-0001-2316-0221 
4 lipengwei@qdio.ac.cn    Pengwei Li    ? 'principal investigator/group leader' 0000-0003-4536-6578 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Zhang, X.' 1 ? 
'Niu, S.'   2 ? 
'Li, P.'    3 ? 
'Bi, Y.'    4 ? 
# 
_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                   CH 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Int J Mol Sci' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1422-0067 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            25 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Chitin Translocation Is Functionally Coupled with Synthesis in Chitin Synthase.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.3390/ijms252111667 
_citation.pdbx_database_id_PubMed   39519219 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Niu, S.'   1 ?                   
primary 'Qi, L.'    2 ?                   
primary 'Zhang, X.' 3 ?                   
primary 'He, D.'    4 ?                   
primary 'Li, P.'    5 ?                   
primary 'Wang, H.'  6 0000-0003-0214-7615 
primary 'Bi, Y.'    7 ?                   
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'chitin synthase'        104586.328 2 2.4.1.16 ? ? ? 
2 non-polymer syn "URIDINE-5'-DIPHOSPHATE" 404.161    2 ?        ? ? ? 
3 non-polymer syn 'MANGANESE (II) ION'     54.938     2 ?        ? ? ? 
# 
_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       
;MSGAPPPSSGFAPRSYGQQPLSHAPRSSMMSVEYDGIPLPPPSIRSCGSQQYVTSYIPTGAAFPPSSVQDMISSMKSYAS
ATDLVRTYSEIPSVEEALSTLDRAAAALNARRYRDALKLYLEGGYAMANVAERQANPKICNLLTSKGFETLNWCARLCDW
IEGRIKEKHPRPGVHKVGIPVSNWDEDWVGPFMDEEEARRMWYTPVYCPHPIDFSNLGYRLRCVETGRRPRLMICITMYN
EGPQQLKATLKKLANNLAYLKEQMPGDEKSLTGAFAGDDVWQNVLVCIVADGREQVHPKTLDYLEAIGLYDEDLLTINSA
GIGAQCHLFEHTLQLSVNGKCLLPIQTVFALKENKASKLDSHHWYFNAFAEQIQPEYTAVMDVGTMLTKSALYHLLFAFE
RNHQIGGACGQLTVDNPFENLSNWVISAQHFEYKISNILDKSLESCFGFISVLPGAFSAYRYEAIRGAPLDAYFQTLNIE
LDVLGPFIGNMYLAEDRILSFEVVARKNCNWTMHYVKDAVARTDVPHDLVGLISQRKRWLNGAFFATLFSIWNWGRIYSE
SKHTFVRKMAFLVFYVYHLLYTAFGFFLPANLYLALFFIVFQGFQQNRLEFIDTSEYSQTVLDCAVYIYNFSYLFGLLML
IIIGLGNNPKHMKLTYYFVGAVFGLMMMLSSLVGAGIFFSTPATVHSIVVSILTVGVYFIASALHGEVHHIFMTFTHYTA
LIPSFVNIFTIYSFCNLQDLSWGTKGLHDDPLLAASLDETEKGDFKDVIAKRRALEELRREEKERVENRKKNFEAFRTNV
LLTWAFSNLIFALFVVYFASSSTYMPVLYIFVASLNTCRLLGSIGHWVYIHTEGLRGRVIDKSECGNGTGRYPQNSYVQL
EEHYAALAEDQRTYASGRTNASVRTVNDVSSAALVPRGSHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSGAPPPSSGFAPRSYGQQPLSHAPRSSMMSVEYDGIPLPPPSIRSCGSQQYVTSYIPTGAAFPPSSVQDMISSMKSYAS
ATDLVRTYSEIPSVEEALSTLDRAAAALNARRYRDALKLYLEGGYAMANVAERQANPKICNLLTSKGFETLNWCARLCDW
IEGRIKEKHPRPGVHKVGIPVSNWDEDWVGPFMDEEEARRMWYTPVYCPHPIDFSNLGYRLRCVETGRRPRLMICITMYN
EGPQQLKATLKKLANNLAYLKEQMPGDEKSLTGAFAGDDVWQNVLVCIVADGREQVHPKTLDYLEAIGLYDEDLLTINSA
GIGAQCHLFEHTLQLSVNGKCLLPIQTVFALKENKASKLDSHHWYFNAFAEQIQPEYTAVMDVGTMLTKSALYHLLFAFE
RNHQIGGACGQLTVDNPFENLSNWVISAQHFEYKISNILDKSLESCFGFISVLPGAFSAYRYEAIRGAPLDAYFQTLNIE
LDVLGPFIGNMYLAEDRILSFEVVARKNCNWTMHYVKDAVARTDVPHDLVGLISQRKRWLNGAFFATLFSIWNWGRIYSE
SKHTFVRKMAFLVFYVYHLLYTAFGFFLPANLYLALFFIVFQGFQQNRLEFIDTSEYSQTVLDCAVYIYNFSYLFGLLML
IIIGLGNNPKHMKLTYYFVGAVFGLMMMLSSLVGAGIFFSTPATVHSIVVSILTVGVYFIASALHGEVHHIFMTFTHYTA
LIPSFVNIFTIYSFCNLQDLSWGTKGLHDDPLLAASLDETEKGDFKDVIAKRRALEELRREEKERVENRKKNFEAFRTNV
LLTWAFSNLIFALFVVYFASSSTYMPVLYIFVASLNTCRLLGSIGHWVYIHTEGLRGRVIDKSECGNGTGRYPQNSYVQL
EEHYAALAEDQRTYASGRTNASVRTVNDVSSAALVPRGSHHHHHH
;
_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 "URIDINE-5'-DIPHOSPHATE" UDP 
3 'MANGANESE (II) ION'     MN  
# 
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   SER n 
1 3   GLY n 
1 4   ALA n 
1 5   PRO n 
1 6   PRO n 
1 7   PRO n 
1 8   SER n 
1 9   SER n 
1 10  GLY n 
1 11  PHE n 
1 12  ALA n 
1 13  PRO n 
1 14  ARG n 
1 15  SER n 
1 16  TYR n 
1 17  GLY n 
1 18  GLN n 
1 19  GLN n 
1 20  PRO n 
1 21  LEU n 
1 22  SER n 
1 23  HIS n 
1 24  ALA n 
1 25  PRO n 
1 26  ARG n 
1 27  SER n 
1 28  SER n 
1 29  MET n 
1 30  MET n 
1 31  SER n 
1 32  VAL n 
1 33  GLU n 
1 34  TYR n 
1 35  ASP n 
1 36  GLY n 
1 37  ILE n 
1 38  PRO n 
1 39  LEU n 
1 40  PRO n 
1 41  PRO n 
1 42  PRO n 
1 43  SER n 
1 44  ILE n 
1 45  ARG n 
1 46  SER n 
1 47  CYS n 
1 48  GLY n 
1 49  SER n 
1 50  GLN n 
1 51  GLN n 
1 52  TYR n 
1 53  VAL n 
1 54  THR n 
1 55  SER n 
1 56  TYR n 
1 57  ILE n 
1 58  PRO n 
1 59  THR n 
1 60  GLY n 
1 61  ALA n 
1 62  ALA n 
1 63  PHE n 
1 64  PRO n 
1 65  PRO n 
1 66  SER n 
1 67  SER n 
1 68  VAL n 
1 69  GLN n 
1 70  ASP n 
1 71  MET n 
1 72  ILE n 
1 73  SER n 
1 74  SER n 
1 75  MET n 
1 76  LYS n 
1 77  SER n 
1 78  TYR n 
1 79  ALA n 
1 80  SER n 
1 81  ALA n 
1 82  THR n 
1 83  ASP n 
1 84  LEU n 
1 85  VAL n 
1 86  ARG n 
1 87  THR n 
1 88  TYR n 
1 89  SER n 
1 90  GLU n 
1 91  ILE n 
1 92  PRO n 
1 93  SER n 
1 94  VAL n 
1 95  GLU n 
1 96  GLU n 
1 97  ALA n 
1 98  LEU n 
1 99  SER n 
1 100 THR n 
1 101 LEU n 
1 102 ASP n 
1 103 ARG n 
1 104 ALA n 
1 105 ALA n 
1 106 ALA n 
1 107 ALA n 
1 108 LEU n 
1 109 ASN n 
1 110 ALA n 
1 111 ARG n 
1 112 ARG n 
1 113 TYR n 
1 114 ARG n 
1 115 ASP n 
1 116 ALA n 
1 117 LEU n 
1 118 LYS n 
1 119 LEU n 
1 120 TYR n 
1 121 LEU n 
1 122 GLU n 
1 123 GLY n 
1 124 GLY n 
1 125 TYR n 
1 126 ALA n 
1 127 MET n 
1 128 ALA n 
1 129 ASN n 
1 130 VAL n 
1 131 ALA n 
1 132 GLU n 
1 133 ARG n 
1 134 GLN n 
1 135 ALA n 
1 136 ASN n 
1 137 PRO n 
1 138 LYS n 
1 139 ILE n 
1 140 CYS n 
1 141 ASN n 
1 142 LEU n 
1 143 LEU n 
1 144 THR n 
1 145 SER n 
1 146 LYS n 
1 147 GLY n 
1 148 PHE n 
1 149 GLU n 
1 150 THR n 
1 151 LEU n 
1 152 ASN n 
1 153 TRP n 
1 154 CYS n 
1 155 ALA n 
1 156 ARG n 
1 157 LEU n 
1 158 CYS n 
1 159 ASP n 
1 160 TRP n 
1 161 ILE n 
1 162 GLU n 
1 163 GLY n 
1 164 ARG n 
1 165 ILE n 
1 166 LYS n 
1 167 GLU n 
1 168 LYS n 
1 169 HIS n 
1 170 PRO n 
1 171 ARG n 
1 172 PRO n 
1 173 GLY n 
1 174 VAL n 
1 175 HIS n 
1 176 LYS n 
1 177 VAL n 
1 178 GLY n 
1 179 ILE n 
1 180 PRO n 
1 181 VAL n 
1 182 SER n 
1 183 ASN n 
1 184 TRP n 
1 185 ASP n 
1 186 GLU n 
1 187 ASP n 
1 188 TRP n 
1 189 VAL n 
1 190 GLY n 
1 191 PRO n 
1 192 PHE n 
1 193 MET n 
1 194 ASP n 
1 195 GLU n 
1 196 GLU n 
1 197 GLU n 
1 198 ALA n 
1 199 ARG n 
1 200 ARG n 
1 201 MET n 
1 202 TRP n 
1 203 TYR n 
1 204 THR n 
1 205 PRO n 
1 206 VAL n 
1 207 TYR n 
1 208 CYS n 
1 209 PRO n 
1 210 HIS n 
1 211 PRO n 
1 212 ILE n 
1 213 ASP n 
1 214 PHE n 
1 215 SER n 
1 216 ASN n 
1 217 LEU n 
1 218 GLY n 
1 219 TYR n 
1 220 ARG n 
1 221 LEU n 
1 222 ARG n 
1 223 CYS n 
1 224 VAL n 
1 225 GLU n 
1 226 THR n 
1 227 GLY n 
1 228 ARG n 
1 229 ARG n 
1 230 PRO n 
1 231 ARG n 
1 232 LEU n 
1 233 MET n 
1 234 ILE n 
1 235 CYS n 
1 236 ILE n 
1 237 THR n 
1 238 MET n 
1 239 TYR n 
1 240 ASN n 
1 241 GLU n 
1 242 GLY n 
1 243 PRO n 
1 244 GLN n 
1 245 GLN n 
1 246 LEU n 
1 247 LYS n 
1 248 ALA n 
1 249 THR n 
1 250 LEU n 
1 251 LYS n 
1 252 LYS n 
1 253 LEU n 
1 254 ALA n 
1 255 ASN n 
1 256 ASN n 
1 257 LEU n 
1 258 ALA n 
1 259 TYR n 
1 260 LEU n 
1 261 LYS n 
1 262 GLU n 
1 263 GLN n 
1 264 MET n 
1 265 PRO n 
1 266 GLY n 
1 267 ASP n 
1 268 GLU n 
1 269 LYS n 
1 270 SER n 
1 271 LEU n 
1 272 THR n 
1 273 GLY n 
1 274 ALA n 
1 275 PHE n 
1 276 ALA n 
1 277 GLY n 
1 278 ASP n 
1 279 ASP n 
1 280 VAL n 
1 281 TRP n 
1 282 GLN n 
1 283 ASN n 
1 284 VAL n 
1 285 LEU n 
1 286 VAL n 
1 287 CYS n 
1 288 ILE n 
1 289 VAL n 
1 290 ALA n 
1 291 ASP n 
1 292 GLY n 
1 293 ARG n 
1 294 GLU n 
1 295 GLN n 
1 296 VAL n 
1 297 HIS n 
1 298 PRO n 
1 299 LYS n 
1 300 THR n 
1 301 LEU n 
1 302 ASP n 
1 303 TYR n 
1 304 LEU n 
1 305 GLU n 
1 306 ALA n 
1 307 ILE n 
1 308 GLY n 
1 309 LEU n 
1 310 TYR n 
1 311 ASP n 
1 312 GLU n 
1 313 ASP n 
1 314 LEU n 
1 315 LEU n 
1 316 THR n 
1 317 ILE n 
1 318 ASN n 
1 319 SER n 
1 320 ALA n 
1 321 GLY n 
1 322 ILE n 
1 323 GLY n 
1 324 ALA n 
1 325 GLN n 
1 326 CYS n 
1 327 HIS n 
1 328 LEU n 
1 329 PHE n 
1 330 GLU n 
1 331 HIS n 
1 332 THR n 
1 333 LEU n 
1 334 GLN n 
1 335 LEU n 
1 336 SER n 
1 337 VAL n 
1 338 ASN n 
1 339 GLY n 
1 340 LYS n 
1 341 CYS n 
1 342 LEU n 
1 343 LEU n 
1 344 PRO n 
1 345 ILE n 
1 346 GLN n 
1 347 THR n 
1 348 VAL n 
1 349 PHE n 
1 350 ALA n 
1 351 LEU n 
1 352 LYS n 
1 353 GLU n 
1 354 ASN n 
1 355 LYS n 
1 356 ALA n 
1 357 SER n 
1 358 LYS n 
1 359 LEU n 
1 360 ASP n 
1 361 SER n 
1 362 HIS n 
1 363 HIS n 
1 364 TRP n 
1 365 TYR n 
1 366 PHE n 
1 367 ASN n 
1 368 ALA n 
1 369 PHE n 
1 370 ALA n 
1 371 GLU n 
1 372 GLN n 
1 373 ILE n 
1 374 GLN n 
1 375 PRO n 
1 376 GLU n 
1 377 TYR n 
1 378 THR n 
1 379 ALA n 
1 380 VAL n 
1 381 MET n 
1 382 ASP n 
1 383 VAL n 
1 384 GLY n 
1 385 THR n 
1 386 MET n 
1 387 LEU n 
1 388 THR n 
1 389 LYS n 
1 390 SER n 
1 391 ALA n 
1 392 LEU n 
1 393 TYR n 
1 394 HIS n 
1 395 LEU n 
1 396 LEU n 
1 397 PHE n 
1 398 ALA n 
1 399 PHE n 
1 400 GLU n 
1 401 ARG n 
1 402 ASN n 
1 403 HIS n 
1 404 GLN n 
1 405 ILE n 
1 406 GLY n 
1 407 GLY n 
1 408 ALA n 
1 409 CYS n 
1 410 GLY n 
1 411 GLN n 
1 412 LEU n 
1 413 THR n 
1 414 VAL n 
1 415 ASP n 
1 416 ASN n 
1 417 PRO n 
1 418 PHE n 
1 419 GLU n 
1 420 ASN n 
1 421 LEU n 
1 422 SER n 
1 423 ASN n 
1 424 TRP n 
1 425 VAL n 
1 426 ILE n 
1 427 SER n 
1 428 ALA n 
1 429 GLN n 
1 430 HIS n 
1 431 PHE n 
1 432 GLU n 
1 433 TYR n 
1 434 LYS n 
1 435 ILE n 
1 436 SER n 
1 437 ASN n 
1 438 ILE n 
1 439 LEU n 
1 440 ASP n 
1 441 LYS n 
1 442 SER n 
1 443 LEU n 
1 444 GLU n 
1 445 SER n 
1 446 CYS n 
1 447 PHE n 
1 448 GLY n 
1 449 PHE n 
1 450 ILE n 
1 451 SER n 
1 452 VAL n 
1 453 LEU n 
1 454 PRO n 
1 455 GLY n 
1 456 ALA n 
1 457 PHE n 
1 458 SER n 
1 459 ALA n 
1 460 TYR n 
1 461 ARG n 
1 462 TYR n 
1 463 GLU n 
1 464 ALA n 
1 465 ILE n 
1 466 ARG n 
1 467 GLY n 
1 468 ALA n 
1 469 PRO n 
1 470 LEU n 
1 471 ASP n 
1 472 ALA n 
1 473 TYR n 
1 474 PHE n 
1 475 GLN n 
1 476 THR n 
1 477 LEU n 
1 478 ASN n 
1 479 ILE n 
1 480 GLU n 
1 481 LEU n 
1 482 ASP n 
1 483 VAL n 
1 484 LEU n 
1 485 GLY n 
1 486 PRO n 
1 487 PHE n 
1 488 ILE n 
1 489 GLY n 
1 490 ASN n 
1 491 MET n 
1 492 TYR n 
1 493 LEU n 
1 494 ALA n 
1 495 GLU n 
1 496 ASP n 
1 497 ARG n 
1 498 ILE n 
1 499 LEU n 
1 500 SER n 
1 501 PHE n 
1 502 GLU n 
1 503 VAL n 
1 504 VAL n 
1 505 ALA n 
1 506 ARG n 
1 507 LYS n 
1 508 ASN n 
1 509 CYS n 
1 510 ASN n 
1 511 TRP n 
1 512 THR n 
1 513 MET n 
1 514 HIS n 
1 515 TYR n 
1 516 VAL n 
1 517 LYS n 
1 518 ASP n 
1 519 ALA n 
1 520 VAL n 
1 521 ALA n 
1 522 ARG n 
1 523 THR n 
1 524 ASP n 
1 525 VAL n 
1 526 PRO n 
1 527 HIS n 
1 528 ASP n 
1 529 LEU n 
1 530 VAL n 
1 531 GLY n 
1 532 LEU n 
1 533 ILE n 
1 534 SER n 
1 535 GLN n 
1 536 ARG n 
1 537 LYS n 
1 538 ARG n 
1 539 TRP n 
1 540 LEU n 
1 541 ASN n 
1 542 GLY n 
1 543 ALA n 
1 544 PHE n 
1 545 PHE n 
1 546 ALA n 
1 547 THR n 
1 548 LEU n 
1 549 PHE n 
1 550 SER n 
1 551 ILE n 
1 552 TRP n 
1 553 ASN n 
1 554 TRP n 
1 555 GLY n 
1 556 ARG n 
1 557 ILE n 
1 558 TYR n 
1 559 SER n 
1 560 GLU n 
1 561 SER n 
1 562 LYS n 
1 563 HIS n 
1 564 THR n 
1 565 PHE n 
1 566 VAL n 
1 567 ARG n 
1 568 LYS n 
1 569 MET n 
1 570 ALA n 
1 571 PHE n 
1 572 LEU n 
1 573 VAL n 
1 574 PHE n 
1 575 TYR n 
1 576 VAL n 
1 577 TYR n 
1 578 HIS n 
1 579 LEU n 
1 580 LEU n 
1 581 TYR n 
1 582 THR n 
1 583 ALA n 
1 584 PHE n 
1 585 GLY n 
1 586 PHE n 
1 587 PHE n 
1 588 LEU n 
1 589 PRO n 
1 590 ALA n 
1 591 ASN n 
1 592 LEU n 
1 593 TYR n 
1 594 LEU n 
1 595 ALA n 
1 596 LEU n 
1 597 PHE n 
1 598 PHE n 
1 599 ILE n 
1 600 VAL n 
1 601 PHE n 
1 602 GLN n 
1 603 GLY n 
1 604 PHE n 
1 605 GLN n 
1 606 GLN n 
1 607 ASN n 
1 608 ARG n 
1 609 LEU n 
1 610 GLU n 
1 611 PHE n 
1 612 ILE n 
1 613 ASP n 
1 614 THR n 
1 615 SER n 
1 616 GLU n 
1 617 TYR n 
1 618 SER n 
1 619 GLN n 
1 620 THR n 
1 621 VAL n 
1 622 LEU n 
1 623 ASP n 
1 624 CYS n 
1 625 ALA n 
1 626 VAL n 
1 627 TYR n 
1 628 ILE n 
1 629 TYR n 
1 630 ASN n 
1 631 PHE n 
1 632 SER n 
1 633 TYR n 
1 634 LEU n 
1 635 PHE n 
1 636 GLY n 
1 637 LEU n 
1 638 LEU n 
1 639 MET n 
1 640 LEU n 
1 641 ILE n 
1 642 ILE n 
1 643 ILE n 
1 644 GLY n 
1 645 LEU n 
1 646 GLY n 
1 647 ASN n 
1 648 ASN n 
1 649 PRO n 
1 650 LYS n 
1 651 HIS n 
1 652 MET n 
1 653 LYS n 
1 654 LEU n 
1 655 THR n 
1 656 TYR n 
1 657 TYR n 
1 658 PHE n 
1 659 VAL n 
1 660 GLY n 
1 661 ALA n 
1 662 VAL n 
1 663 PHE n 
1 664 GLY n 
1 665 LEU n 
1 666 MET n 
1 667 MET n 
1 668 MET n 
1 669 LEU n 
1 670 SER n 
1 671 SER n 
1 672 LEU n 
1 673 VAL n 
1 674 GLY n 
1 675 ALA n 
1 676 GLY n 
1 677 ILE n 
1 678 PHE n 
1 679 PHE n 
1 680 SER n 
1 681 THR n 
1 682 PRO n 
1 683 ALA n 
1 684 THR n 
1 685 VAL n 
1 686 HIS n 
1 687 SER n 
1 688 ILE n 
1 689 VAL n 
1 690 VAL n 
1 691 SER n 
1 692 ILE n 
1 693 LEU n 
1 694 THR n 
1 695 VAL n 
1 696 GLY n 
1 697 VAL n 
1 698 TYR n 
1 699 PHE n 
1 700 ILE n 
1 701 ALA n 
1 702 SER n 
1 703 ALA n 
1 704 LEU n 
1 705 HIS n 
1 706 GLY n 
1 707 GLU n 
1 708 VAL n 
1 709 HIS n 
1 710 HIS n 
1 711 ILE n 
1 712 PHE n 
1 713 MET n 
1 714 THR n 
1 715 PHE n 
1 716 THR n 
1 717 HIS n 
1 718 TYR n 
1 719 THR n 
1 720 ALA n 
1 721 LEU n 
1 722 ILE n 
1 723 PRO n 
1 724 SER n 
1 725 PHE n 
1 726 VAL n 
1 727 ASN n 
1 728 ILE n 
1 729 PHE n 
1 730 THR n 
1 731 ILE n 
1 732 TYR n 
1 733 SER n 
1 734 PHE n 
1 735 CYS n 
1 736 ASN n 
1 737 LEU n 
1 738 GLN n 
1 739 ASP n 
1 740 LEU n 
1 741 SER n 
1 742 TRP n 
1 743 GLY n 
1 744 THR n 
1 745 LYS n 
1 746 GLY n 
1 747 LEU n 
1 748 HIS n 
1 749 ASP n 
1 750 ASP n 
1 751 PRO n 
1 752 LEU n 
1 753 LEU n 
1 754 ALA n 
1 755 ALA n 
1 756 SER n 
1 757 LEU n 
1 758 ASP n 
1 759 GLU n 
1 760 THR n 
1 761 GLU n 
1 762 LYS n 
1 763 GLY n 
1 764 ASP n 
1 765 PHE n 
1 766 LYS n 
1 767 ASP n 
1 768 VAL n 
1 769 ILE n 
1 770 ALA n 
1 771 LYS n 
1 772 ARG n 
1 773 ARG n 
1 774 ALA n 
1 775 LEU n 
1 776 GLU n 
1 777 GLU n 
1 778 LEU n 
1 779 ARG n 
1 780 ARG n 
1 781 GLU n 
1 782 GLU n 
1 783 LYS n 
1 784 GLU n 
1 785 ARG n 
1 786 VAL n 
1 787 GLU n 
1 788 ASN n 
1 789 ARG n 
1 790 LYS n 
1 791 LYS n 
1 792 ASN n 
1 793 PHE n 
1 794 GLU n 
1 795 ALA n 
1 796 PHE n 
1 797 ARG n 
1 798 THR n 
1 799 ASN n 
1 800 VAL n 
1 801 LEU n 
1 802 LEU n 
1 803 THR n 
1 804 TRP n 
1 805 ALA n 
1 806 PHE n 
1 807 SER n 
1 808 ASN n 
1 809 LEU n 
1 810 ILE n 
1 811 PHE n 
1 812 ALA n 
1 813 LEU n 
1 814 PHE n 
1 815 VAL n 
1 816 VAL n 
1 817 TYR n 
1 818 PHE n 
1 819 ALA n 
1 820 SER n 
1 821 SER n 
1 822 SER n 
1 823 THR n 
1 824 TYR n 
1 825 MET n 
1 826 PRO n 
1 827 VAL n 
1 828 LEU n 
1 829 TYR n 
1 830 ILE n 
1 831 PHE n 
1 832 VAL n 
1 833 ALA n 
1 834 SER n 
1 835 LEU n 
1 836 ASN n 
1 837 THR n 
1 838 CYS n 
1 839 ARG n 
1 840 LEU n 
1 841 LEU n 
1 842 GLY n 
1 843 SER n 
1 844 ILE n 
1 845 GLY n 
1 846 HIS n 
1 847 TRP n 
1 848 VAL n 
1 849 TYR n 
1 850 ILE n 
1 851 HIS n 
1 852 THR n 
1 853 GLU n 
1 854 GLY n 
1 855 LEU n 
1 856 ARG n 
1 857 GLY n 
1 858 ARG n 
1 859 VAL n 
1 860 ILE n 
1 861 ASP n 
1 862 LYS n 
1 863 SER n 
1 864 GLU n 
1 865 CYS n 
1 866 GLY n 
1 867 ASN n 
1 868 GLY n 
1 869 THR n 
1 870 GLY n 
1 871 ARG n 
1 872 TYR n 
1 873 PRO n 
1 874 GLN n 
1 875 ASN n 
1 876 SER n 
1 877 TYR n 
1 878 VAL n 
1 879 GLN n 
1 880 LEU n 
1 881 GLU n 
1 882 GLU n 
1 883 HIS n 
1 884 TYR n 
1 885 ALA n 
1 886 ALA n 
1 887 LEU n 
1 888 ALA n 
1 889 GLU n 
1 890 ASP n 
1 891 GLN n 
1 892 ARG n 
1 893 THR n 
1 894 TYR n 
1 895 ALA n 
1 896 SER n 
1 897 GLY n 
1 898 ARG n 
1 899 THR n 
1 900 ASN n 
1 901 ALA n 
1 902 SER n 
1 903 VAL n 
1 904 ARG n 
1 905 THR n 
1 906 VAL n 
1 907 ASN n 
1 908 ASP n 
1 909 VAL n 
1 910 SER n 
1 911 SER n 
1 912 ALA n 
1 913 ALA n 
1 914 LEU n 
1 915 VAL n 
1 916 PRO n 
1 917 ARG n 
1 918 GLY n 
1 919 SER n 
1 920 HIS n 
1 921 HIS n 
1 922 HIS n 
1 923 HIS n 
1 924 HIS n 
1 925 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   925 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 PHYSODRAFT_557500 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Phytophthora sojae strain P6497' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1094619 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               human 
_entity_src_gen.pdbx_host_org_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                  ? 'C3 H7 N O2'       89.093  
ARG 'L-peptide linking' y ARGININE                 ? 'C6 H15 N4 O2 1'   175.209 
ASN 'L-peptide linking' y ASPARAGINE               ? 'C4 H8 N2 O3'      132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'          ? 'C4 H7 N O4'       133.103 
CYS 'L-peptide linking' y CYSTEINE                 ? 'C3 H7 N O2 S'     121.158 
GLN 'L-peptide linking' y GLUTAMINE                ? 'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'          ? 'C5 H9 N O4'       147.129 
GLY 'peptide linking'   y GLYCINE                  ? 'C2 H5 N O2'       75.067  
HIS 'L-peptide linking' y HISTIDINE                ? 'C6 H10 N3 O2 1'   156.162 
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 
MN  non-polymer         . 'MANGANESE (II) ION'     ? 'Mn 2'             54.938  
PHE 'L-peptide linking' y PHENYLALANINE            ? 'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE                  ? 'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE                   ? 'C3 H7 N O3'       105.093 
THR 'L-peptide linking' y THREONINE                ? 'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN               ? 'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE                 ? 'C9 H11 N O3'      181.189 
UDP 'RNA linking'       . "URIDINE-5'-DIPHOSPHATE" ? 'C9 H14 N2 O12 P2' 404.161 
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   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   GLY 3   3   ?   ?   ?   A . n 
A 1 4   ALA 4   4   ?   ?   ?   A . n 
A 1 5   PRO 5   5   ?   ?   ?   A . n 
A 1 6   PRO 6   6   ?   ?   ?   A . n 
A 1 7   PRO 7   7   ?   ?   ?   A . n 
A 1 8   SER 8   8   ?   ?   ?   A . n 
A 1 9   SER 9   9   ?   ?   ?   A . n 
A 1 10  GLY 10  10  ?   ?   ?   A . n 
A 1 11  PHE 11  11  ?   ?   ?   A . n 
A 1 12  ALA 12  12  ?   ?   ?   A . n 
A 1 13  PRO 13  13  ?   ?   ?   A . n 
A 1 14  ARG 14  14  ?   ?   ?   A . n 
A 1 15  SER 15  15  ?   ?   ?   A . n 
A 1 16  TYR 16  16  ?   ?   ?   A . n 
A 1 17  GLY 17  17  ?   ?   ?   A . n 
A 1 18  GLN 18  18  ?   ?   ?   A . n 
A 1 19  GLN 19  19  ?   ?   ?   A . n 
A 1 20  PRO 20  20  ?   ?   ?   A . n 
A 1 21  LEU 21  21  ?   ?   ?   A . n 
A 1 22  SER 22  22  ?   ?   ?   A . n 
A 1 23  HIS 23  23  23  HIS HIS A . n 
A 1 24  ALA 24  24  24  ALA ALA A . n 
A 1 25  PRO 25  25  25  PRO PRO A . n 
A 1 26  ARG 26  26  26  ARG ARG A . n 
A 1 27  SER 27  27  27  SER SER A . n 
A 1 28  SER 28  28  28  SER SER A . n 
A 1 29  MET 29  29  29  MET MET A . n 
A 1 30  MET 30  30  30  MET MET A . n 
A 1 31  SER 31  31  31  SER SER A . n 
A 1 32  VAL 32  32  32  VAL VAL A . n 
A 1 33  GLU 33  33  33  GLU GLU A . n 
A 1 34  TYR 34  34  34  TYR TYR A . n 
A 1 35  ASP 35  35  35  ASP ASP A . n 
A 1 36  GLY 36  36  36  GLY GLY A . n 
A 1 37  ILE 37  37  37  ILE ILE A . n 
A 1 38  PRO 38  38  38  PRO PRO A . n 
A 1 39  LEU 39  39  39  LEU LEU A . n 
A 1 40  PRO 40  40  ?   ?   ?   A . n 
A 1 41  PRO 41  41  ?   ?   ?   A . n 
A 1 42  PRO 42  42  ?   ?   ?   A . n 
A 1 43  SER 43  43  ?   ?   ?   A . n 
A 1 44  ILE 44  44  ?   ?   ?   A . n 
A 1 45  ARG 45  45  ?   ?   ?   A . n 
A 1 46  SER 46  46  ?   ?   ?   A . n 
A 1 47  CYS 47  47  ?   ?   ?   A . n 
A 1 48  GLY 48  48  ?   ?   ?   A . n 
A 1 49  SER 49  49  ?   ?   ?   A . n 
A 1 50  GLN 50  50  ?   ?   ?   A . n 
A 1 51  GLN 51  51  ?   ?   ?   A . n 
A 1 52  TYR 52  52  ?   ?   ?   A . n 
A 1 53  VAL 53  53  ?   ?   ?   A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  SER 55  55  55  SER SER A . n 
A 1 56  TYR 56  56  ?   ?   ?   A . n 
A 1 57  ILE 57  57  ?   ?   ?   A . n 
A 1 58  PRO 58  58  ?   ?   ?   A . n 
A 1 59  THR 59  59  ?   ?   ?   A . n 
A 1 60  GLY 60  60  ?   ?   ?   A . n 
A 1 61  ALA 61  61  ?   ?   ?   A . n 
A 1 62  ALA 62  62  ?   ?   ?   A . n 
A 1 63  PHE 63  63  ?   ?   ?   A . n 
A 1 64  PRO 64  64  ?   ?   ?   A . n 
A 1 65  PRO 65  65  ?   ?   ?   A . n 
A 1 66  SER 66  66  ?   ?   ?   A . n 
A 1 67  SER 67  67  ?   ?   ?   A . n 
A 1 68  VAL 68  68  ?   ?   ?   A . n 
A 1 69  GLN 69  69  ?   ?   ?   A . n 
A 1 70  ASP 70  70  ?   ?   ?   A . n 
A 1 71  MET 71  71  ?   ?   ?   A . n 
A 1 72  ILE 72  72  ?   ?   ?   A . n 
A 1 73  SER 73  73  ?   ?   ?   A . n 
A 1 74  SER 74  74  ?   ?   ?   A . n 
A 1 75  MET 75  75  ?   ?   ?   A . n 
A 1 76  LYS 76  76  ?   ?   ?   A . n 
A 1 77  SER 77  77  ?   ?   ?   A . n 
A 1 78  TYR 78  78  ?   ?   ?   A . n 
A 1 79  ALA 79  79  ?   ?   ?   A . n 
A 1 80  SER 80  80  ?   ?   ?   A . n 
A 1 81  ALA 81  81  ?   ?   ?   A . n 
A 1 82  THR 82  82  ?   ?   ?   A . n 
A 1 83  ASP 83  83  ?   ?   ?   A . n 
A 1 84  LEU 84  84  ?   ?   ?   A . n 
A 1 85  VAL 85  85  ?   ?   ?   A . n 
A 1 86  ARG 86  86  ?   ?   ?   A . n 
A 1 87  THR 87  87  ?   ?   ?   A . n 
A 1 88  TYR 88  88  ?   ?   ?   A . n 
A 1 89  SER 89  89  ?   ?   ?   A . n 
A 1 90  GLU 90  90  ?   ?   ?   A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  PRO 92  92  92  PRO PRO A . n 
A 1 93  SER 93  93  93  SER SER A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  GLU 95  95  95  GLU GLU A . n 
A 1 96  GLU 96  96  96  GLU GLU A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 THR 100 100 100 THR THR A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 ASP 102 102 102 ASP ASP A . n 
A 1 103 ARG 103 103 103 ARG ARG A . n 
A 1 104 ALA 104 104 104 ALA ALA A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 ALA 106 106 106 ALA ALA A . n 
A 1 107 ALA 107 107 107 ALA ALA A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 ASN 109 109 109 ASN ASN A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 ARG 111 111 111 ARG ARG A . n 
A 1 112 ARG 112 112 112 ARG ARG A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 ARG 114 114 114 ARG ARG A . n 
A 1 115 ASP 115 115 115 ASP ASP A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 LYS 118 118 118 LYS LYS A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 TYR 120 120 120 TYR TYR A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 GLU 122 122 122 GLU GLU A . n 
A 1 123 GLY 123 123 123 GLY GLY A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 TYR 125 125 125 TYR TYR A . n 
A 1 126 ALA 126 126 126 ALA ALA A . n 
A 1 127 MET 127 127 127 MET MET A . n 
A 1 128 ALA 128 128 128 ALA ALA A . n 
A 1 129 ASN 129 129 129 ASN ASN A . n 
A 1 130 VAL 130 130 130 VAL VAL A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 ARG 133 133 133 ARG ARG A . n 
A 1 134 GLN 134 134 134 GLN GLN A . n 
A 1 135 ALA 135 135 135 ALA ALA A . n 
A 1 136 ASN 136 136 136 ASN ASN A . n 
A 1 137 PRO 137 137 137 PRO PRO A . n 
A 1 138 LYS 138 138 138 LYS LYS A . n 
A 1 139 ILE 139 139 139 ILE ILE A . n 
A 1 140 CYS 140 140 140 CYS CYS A . n 
A 1 141 ASN 141 141 141 ASN ASN A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 THR 144 144 144 THR THR A . n 
A 1 145 SER 145 145 145 SER SER A . n 
A 1 146 LYS 146 146 146 LYS LYS A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 PHE 148 148 ?   ?   ?   A . n 
A 1 149 GLU 149 149 149 GLU GLU A . n 
A 1 150 THR 150 150 150 THR THR A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 ASN 152 152 152 ASN ASN A . n 
A 1 153 TRP 153 153 153 TRP TRP A . n 
A 1 154 CYS 154 154 154 CYS CYS A . n 
A 1 155 ALA 155 155 155 ALA ALA A . n 
A 1 156 ARG 156 156 156 ARG ARG A . n 
A 1 157 LEU 157 157 157 LEU LEU A . n 
A 1 158 CYS 158 158 158 CYS CYS A . n 
A 1 159 ASP 159 159 159 ASP ASP A . n 
A 1 160 TRP 160 160 160 TRP TRP A . n 
A 1 161 ILE 161 161 161 ILE ILE A . n 
A 1 162 GLU 162 162 ?   ?   ?   A . n 
A 1 163 GLY 163 163 163 GLY GLY A . n 
A 1 164 ARG 164 164 164 ARG ARG A . n 
A 1 165 ILE 165 165 165 ILE ILE A . n 
A 1 166 LYS 166 166 166 LYS LYS A . n 
A 1 167 GLU 167 167 167 GLU GLU A . n 
A 1 168 LYS 168 168 168 LYS LYS A . n 
A 1 169 HIS 169 169 169 HIS HIS A . n 
A 1 170 PRO 170 170 170 PRO PRO A . n 
A 1 171 ARG 171 171 171 ARG ARG A . n 
A 1 172 PRO 172 172 172 PRO PRO A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 VAL 174 174 174 VAL VAL A . n 
A 1 175 HIS 175 175 175 HIS HIS A . n 
A 1 176 LYS 176 176 176 LYS LYS A . n 
A 1 177 VAL 177 177 177 VAL VAL A . n 
A 1 178 GLY 178 178 178 GLY GLY A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 PRO 180 180 180 PRO PRO A . n 
A 1 181 VAL 181 181 181 VAL VAL A . n 
A 1 182 SER 182 182 182 SER SER A . n 
A 1 183 ASN 183 183 183 ASN ASN A . n 
A 1 184 TRP 184 184 184 TRP TRP A . n 
A 1 185 ASP 185 185 185 ASP ASP A . n 
A 1 186 GLU 186 186 186 GLU GLU A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 TRP 188 188 188 TRP TRP A . n 
A 1 189 VAL 189 189 189 VAL VAL A . n 
A 1 190 GLY 190 190 190 GLY GLY A . n 
A 1 191 PRO 191 191 191 PRO PRO A . n 
A 1 192 PHE 192 192 192 PHE PHE A . n 
A 1 193 MET 193 193 193 MET MET A . n 
A 1 194 ASP 194 194 194 ASP ASP A . n 
A 1 195 GLU 195 195 195 GLU GLU A . n 
A 1 196 GLU 196 196 196 GLU GLU A . n 
A 1 197 GLU 197 197 197 GLU GLU A . n 
A 1 198 ALA 198 198 198 ALA ALA A . n 
A 1 199 ARG 199 199 199 ARG ARG A . n 
A 1 200 ARG 200 200 200 ARG ARG A . n 
A 1 201 MET 201 201 201 MET MET A . n 
A 1 202 TRP 202 202 202 TRP TRP A . n 
A 1 203 TYR 203 203 203 TYR TYR A . n 
A 1 204 THR 204 204 204 THR THR A . n 
A 1 205 PRO 205 205 205 PRO PRO A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 TYR 207 207 207 TYR TYR A . n 
A 1 208 CYS 208 208 208 CYS CYS A . n 
A 1 209 PRO 209 209 209 PRO PRO A . n 
A 1 210 HIS 210 210 210 HIS HIS A . n 
A 1 211 PRO 211 211 211 PRO PRO A . n 
A 1 212 ILE 212 212 212 ILE ILE A . n 
A 1 213 ASP 213 213 213 ASP ASP A . n 
A 1 214 PHE 214 214 214 PHE PHE A . n 
A 1 215 SER 215 215 215 SER SER A . n 
A 1 216 ASN 216 216 216 ASN ASN A . n 
A 1 217 LEU 217 217 217 LEU LEU A . n 
A 1 218 GLY 218 218 218 GLY GLY A . n 
A 1 219 TYR 219 219 219 TYR TYR A . n 
A 1 220 ARG 220 220 220 ARG ARG A . n 
A 1 221 LEU 221 221 221 LEU LEU A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 CYS 223 223 223 CYS CYS A . n 
A 1 224 VAL 224 224 224 VAL VAL A . n 
A 1 225 GLU 225 225 225 GLU GLU A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 GLY 227 227 227 GLY GLY A . n 
A 1 228 ARG 228 228 228 ARG ARG A . n 
A 1 229 ARG 229 229 229 ARG ARG A . n 
A 1 230 PRO 230 230 230 PRO PRO A . n 
A 1 231 ARG 231 231 231 ARG ARG A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 MET 233 233 233 MET MET A . n 
A 1 234 ILE 234 234 234 ILE ILE A . n 
A 1 235 CYS 235 235 235 CYS CYS A . n 
A 1 236 ILE 236 236 236 ILE ILE A . n 
A 1 237 THR 237 237 237 THR THR A . n 
A 1 238 MET 238 238 238 MET MET A . n 
A 1 239 TYR 239 239 239 TYR TYR A . n 
A 1 240 ASN 240 240 240 ASN ASN A . n 
A 1 241 GLU 241 241 241 GLU GLU A . n 
A 1 242 GLY 242 242 242 GLY GLY A . n 
A 1 243 PRO 243 243 243 PRO PRO A . n 
A 1 244 GLN 244 244 244 GLN GLN A . n 
A 1 245 GLN 245 245 245 GLN GLN A . n 
A 1 246 LEU 246 246 246 LEU LEU A . n 
A 1 247 LYS 247 247 247 LYS LYS A . n 
A 1 248 ALA 248 248 248 ALA ALA A . n 
A 1 249 THR 249 249 249 THR THR A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 LYS 251 251 251 LYS LYS A . n 
A 1 252 LYS 252 252 252 LYS LYS A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 ALA 254 254 254 ALA ALA A . n 
A 1 255 ASN 255 255 255 ASN ASN A . n 
A 1 256 ASN 256 256 256 ASN ASN A . n 
A 1 257 LEU 257 257 257 LEU LEU A . n 
A 1 258 ALA 258 258 258 ALA ALA A . n 
A 1 259 TYR 259 259 259 TYR TYR A . n 
A 1 260 LEU 260 260 260 LEU LEU A . n 
A 1 261 LYS 261 261 261 LYS LYS A . n 
A 1 262 GLU 262 262 262 GLU GLU A . n 
A 1 263 GLN 263 263 263 GLN GLN A . n 
A 1 264 MET 264 264 264 MET MET A . n 
A 1 265 PRO 265 265 265 PRO PRO A . n 
A 1 266 GLY 266 266 266 GLY GLY A . n 
A 1 267 ASP 267 267 267 ASP ASP A . n 
A 1 268 GLU 268 268 268 GLU GLU A . n 
A 1 269 LYS 269 269 269 LYS LYS A . n 
A 1 270 SER 270 270 270 SER SER A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 THR 272 272 272 THR THR A . n 
A 1 273 GLY 273 273 273 GLY GLY A . n 
A 1 274 ALA 274 274 274 ALA ALA A . n 
A 1 275 PHE 275 275 275 PHE PHE A . n 
A 1 276 ALA 276 276 276 ALA ALA A . n 
A 1 277 GLY 277 277 277 GLY GLY A . n 
A 1 278 ASP 278 278 278 ASP ASP A . n 
A 1 279 ASP 279 279 279 ASP ASP A . n 
A 1 280 VAL 280 280 280 VAL VAL A . n 
A 1 281 TRP 281 281 281 TRP TRP A . n 
A 1 282 GLN 282 282 282 GLN GLN A . n 
A 1 283 ASN 283 283 283 ASN ASN A . n 
A 1 284 VAL 284 284 284 VAL VAL A . n 
A 1 285 LEU 285 285 285 LEU LEU A . n 
A 1 286 VAL 286 286 286 VAL VAL A . n 
A 1 287 CYS 287 287 287 CYS CYS A . n 
A 1 288 ILE 288 288 288 ILE ILE A . n 
A 1 289 VAL 289 289 289 VAL VAL A . n 
A 1 290 ALA 290 290 290 ALA ALA A . n 
A 1 291 ASP 291 291 291 ASP ASP A . n 
A 1 292 GLY 292 292 292 GLY GLY A . n 
A 1 293 ARG 293 293 293 ARG ARG A . n 
A 1 294 GLU 294 294 294 GLU GLU A . n 
A 1 295 GLN 295 295 295 GLN GLN A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 HIS 297 297 297 HIS HIS A . n 
A 1 298 PRO 298 298 298 PRO PRO A . n 
A 1 299 LYS 299 299 299 LYS LYS A . n 
A 1 300 THR 300 300 300 THR THR A . n 
A 1 301 LEU 301 301 301 LEU LEU A . n 
A 1 302 ASP 302 302 302 ASP ASP A . n 
A 1 303 TYR 303 303 303 TYR TYR A . n 
A 1 304 LEU 304 304 304 LEU LEU A . n 
A 1 305 GLU 305 305 305 GLU GLU A . n 
A 1 306 ALA 306 306 306 ALA ALA A . n 
A 1 307 ILE 307 307 307 ILE ILE A . n 
A 1 308 GLY 308 308 308 GLY GLY A . n 
A 1 309 LEU 309 309 309 LEU LEU A . n 
A 1 310 TYR 310 310 310 TYR TYR A . n 
A 1 311 ASP 311 311 311 ASP ASP A . n 
A 1 312 GLU 312 312 312 GLU GLU A . n 
A 1 313 ASP 313 313 313 ASP ASP A . n 
A 1 314 LEU 314 314 314 LEU LEU A . n 
A 1 315 LEU 315 315 315 LEU LEU A . n 
A 1 316 THR 316 316 316 THR THR A . n 
A 1 317 ILE 317 317 317 ILE ILE A . n 
A 1 318 ASN 318 318 318 ASN ASN A . n 
A 1 319 SER 319 319 319 SER SER A . n 
A 1 320 ALA 320 320 320 ALA ALA A . n 
A 1 321 GLY 321 321 321 GLY GLY A . n 
A 1 322 ILE 322 322 322 ILE ILE A . n 
A 1 323 GLY 323 323 323 GLY GLY A . n 
A 1 324 ALA 324 324 324 ALA ALA A . n 
A 1 325 GLN 325 325 325 GLN GLN A . n 
A 1 326 CYS 326 326 326 CYS CYS A . n 
A 1 327 HIS 327 327 327 HIS HIS A . n 
A 1 328 LEU 328 328 328 LEU LEU A . n 
A 1 329 PHE 329 329 329 PHE PHE A . n 
A 1 330 GLU 330 330 330 GLU GLU A . n 
A 1 331 HIS 331 331 331 HIS HIS A . n 
A 1 332 THR 332 332 332 THR THR A . n 
A 1 333 LEU 333 333 333 LEU LEU A . n 
A 1 334 GLN 334 334 334 GLN GLN A . n 
A 1 335 LEU 335 335 335 LEU LEU A . n 
A 1 336 SER 336 336 336 SER SER A . n 
A 1 337 VAL 337 337 337 VAL VAL A . n 
A 1 338 ASN 338 338 338 ASN ASN A . n 
A 1 339 GLY 339 339 339 GLY GLY A . n 
A 1 340 LYS 340 340 340 LYS LYS A . n 
A 1 341 CYS 341 341 341 CYS CYS A . n 
A 1 342 LEU 342 342 342 LEU LEU A . n 
A 1 343 LEU 343 343 343 LEU LEU A . n 
A 1 344 PRO 344 344 344 PRO PRO A . n 
A 1 345 ILE 345 345 345 ILE ILE A . n 
A 1 346 GLN 346 346 346 GLN GLN A . n 
A 1 347 THR 347 347 347 THR THR A . n 
A 1 348 VAL 348 348 348 VAL VAL A . n 
A 1 349 PHE 349 349 349 PHE PHE A . n 
A 1 350 ALA 350 350 350 ALA ALA A . n 
A 1 351 LEU 351 351 351 LEU LEU A . n 
A 1 352 LYS 352 352 352 LYS LYS A . n 
A 1 353 GLU 353 353 353 GLU GLU A . n 
A 1 354 ASN 354 354 354 ASN ASN A . n 
A 1 355 LYS 355 355 355 LYS LYS A . n 
A 1 356 ALA 356 356 356 ALA ALA A . n 
A 1 357 SER 357 357 357 SER SER A . n 
A 1 358 LYS 358 358 358 LYS LYS A . n 
A 1 359 LEU 359 359 359 LEU LEU A . n 
A 1 360 ASP 360 360 360 ASP ASP A . n 
A 1 361 SER 361 361 361 SER SER A . n 
A 1 362 HIS 362 362 362 HIS HIS A . n 
A 1 363 HIS 363 363 363 HIS HIS A . n 
A 1 364 TRP 364 364 364 TRP TRP A . n 
A 1 365 TYR 365 365 365 TYR TYR A . n 
A 1 366 PHE 366 366 366 PHE PHE A . n 
A 1 367 ASN 367 367 367 ASN ASN A . n 
A 1 368 ALA 368 368 368 ALA ALA A . n 
A 1 369 PHE 369 369 369 PHE PHE A . n 
A 1 370 ALA 370 370 370 ALA ALA A . n 
A 1 371 GLU 371 371 371 GLU GLU A . n 
A 1 372 GLN 372 372 372 GLN GLN A . n 
A 1 373 ILE 373 373 373 ILE ILE A . n 
A 1 374 GLN 374 374 374 GLN GLN A . n 
A 1 375 PRO 375 375 375 PRO PRO A . n 
A 1 376 GLU 376 376 376 GLU GLU A . n 
A 1 377 TYR 377 377 377 TYR TYR A . n 
A 1 378 THR 378 378 378 THR THR A . n 
A 1 379 ALA 379 379 379 ALA ALA A . n 
A 1 380 VAL 380 380 380 VAL VAL A . n 
A 1 381 MET 381 381 381 MET MET A . n 
A 1 382 ASP 382 382 382 ASP ASP A . n 
A 1 383 VAL 383 383 383 VAL VAL A . n 
A 1 384 GLY 384 384 384 GLY GLY A . n 
A 1 385 THR 385 385 385 THR THR A . n 
A 1 386 MET 386 386 386 MET MET A . n 
A 1 387 LEU 387 387 387 LEU LEU A . n 
A 1 388 THR 388 388 388 THR THR A . n 
A 1 389 LYS 389 389 389 LYS LYS A . n 
A 1 390 SER 390 390 390 SER SER A . n 
A 1 391 ALA 391 391 391 ALA ALA A . n 
A 1 392 LEU 392 392 392 LEU LEU A . n 
A 1 393 TYR 393 393 393 TYR TYR A . n 
A 1 394 HIS 394 394 394 HIS HIS A . n 
A 1 395 LEU 395 395 395 LEU LEU A . n 
A 1 396 LEU 396 396 396 LEU LEU A . n 
A 1 397 PHE 397 397 397 PHE PHE A . n 
A 1 398 ALA 398 398 398 ALA ALA A . n 
A 1 399 PHE 399 399 399 PHE PHE A . n 
A 1 400 GLU 400 400 400 GLU GLU A . n 
A 1 401 ARG 401 401 401 ARG ARG A . n 
A 1 402 ASN 402 402 402 ASN ASN A . n 
A 1 403 HIS 403 403 403 HIS HIS A . n 
A 1 404 GLN 404 404 404 GLN GLN A . n 
A 1 405 ILE 405 405 405 ILE ILE A . n 
A 1 406 GLY 406 406 406 GLY GLY A . n 
A 1 407 GLY 407 407 407 GLY GLY A . n 
A 1 408 ALA 408 408 408 ALA ALA A . n 
A 1 409 CYS 409 409 409 CYS CYS A . n 
A 1 410 GLY 410 410 410 GLY GLY A . n 
A 1 411 GLN 411 411 411 GLN GLN A . n 
A 1 412 LEU 412 412 412 LEU LEU A . n 
A 1 413 THR 413 413 413 THR THR A . n 
A 1 414 VAL 414 414 414 VAL VAL A . n 
A 1 415 ASP 415 415 415 ASP ASP A . n 
A 1 416 ASN 416 416 416 ASN ASN A . n 
A 1 417 PRO 417 417 417 PRO PRO A . n 
A 1 418 PHE 418 418 418 PHE PHE A . n 
A 1 419 GLU 419 419 419 GLU GLU A . n 
A 1 420 ASN 420 420 420 ASN ASN A . n 
A 1 421 LEU 421 421 421 LEU LEU A . n 
A 1 422 SER 422 422 422 SER SER A . n 
A 1 423 ASN 423 423 423 ASN ASN A . n 
A 1 424 TRP 424 424 424 TRP TRP A . n 
A 1 425 VAL 425 425 425 VAL VAL A . n 
A 1 426 ILE 426 426 426 ILE ILE A . n 
A 1 427 SER 427 427 427 SER SER A . n 
A 1 428 ALA 428 428 428 ALA ALA A . n 
A 1 429 GLN 429 429 429 GLN GLN A . n 
A 1 430 HIS 430 430 430 HIS HIS A . n 
A 1 431 PHE 431 431 431 PHE PHE A . n 
A 1 432 GLU 432 432 432 GLU GLU A . n 
A 1 433 TYR 433 433 433 TYR TYR A . n 
A 1 434 LYS 434 434 434 LYS LYS A . n 
A 1 435 ILE 435 435 435 ILE ILE A . n 
A 1 436 SER 436 436 436 SER SER A . n 
A 1 437 ASN 437 437 437 ASN ASN A . n 
A 1 438 ILE 438 438 438 ILE ILE A . n 
A 1 439 LEU 439 439 439 LEU LEU A . n 
A 1 440 ASP 440 440 440 ASP ASP A . n 
A 1 441 LYS 441 441 441 LYS LYS A . n 
A 1 442 SER 442 442 442 SER SER A . n 
A 1 443 LEU 443 443 443 LEU LEU A . n 
A 1 444 GLU 444 444 444 GLU GLU A . n 
A 1 445 SER 445 445 445 SER SER A . n 
A 1 446 CYS 446 446 446 CYS CYS A . n 
A 1 447 PHE 447 447 447 PHE PHE A . n 
A 1 448 GLY 448 448 448 GLY GLY A . n 
A 1 449 PHE 449 449 449 PHE PHE A . n 
A 1 450 ILE 450 450 450 ILE ILE A . n 
A 1 451 SER 451 451 451 SER SER A . n 
A 1 452 VAL 452 452 452 VAL VAL A . n 
A 1 453 LEU 453 453 453 LEU LEU A . n 
A 1 454 PRO 454 454 454 PRO PRO A . n 
A 1 455 GLY 455 455 455 GLY GLY A . n 
A 1 456 ALA 456 456 456 ALA ALA A . n 
A 1 457 PHE 457 457 457 PHE PHE A . n 
A 1 458 SER 458 458 458 SER SER A . n 
A 1 459 ALA 459 459 459 ALA ALA A . n 
A 1 460 TYR 460 460 460 TYR TYR A . n 
A 1 461 ARG 461 461 461 ARG ARG A . n 
A 1 462 TYR 462 462 462 TYR TYR A . n 
A 1 463 GLU 463 463 463 GLU GLU A . n 
A 1 464 ALA 464 464 464 ALA ALA A . n 
A 1 465 ILE 465 465 465 ILE ILE A . n 
A 1 466 ARG 466 466 466 ARG ARG A . n 
A 1 467 GLY 467 467 467 GLY GLY A . n 
A 1 468 ALA 468 468 468 ALA ALA A . n 
A 1 469 PRO 469 469 469 PRO PRO 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 ALA 472 472 472 ALA ALA A . n 
A 1 473 TYR 473 473 473 TYR TYR A . n 
A 1 474 PHE 474 474 474 PHE PHE A . n 
A 1 475 GLN 475 475 475 GLN GLN A . n 
A 1 476 THR 476 476 476 THR THR A . n 
A 1 477 LEU 477 477 477 LEU LEU A . n 
A 1 478 ASN 478 478 478 ASN ASN A . n 
A 1 479 ILE 479 479 479 ILE ILE A . n 
A 1 480 GLU 480 480 480 GLU GLU A . n 
A 1 481 LEU 481 481 481 LEU LEU A . n 
A 1 482 ASP 482 482 482 ASP ASP A . n 
A 1 483 VAL 483 483 483 VAL VAL A . n 
A 1 484 LEU 484 484 484 LEU LEU A . n 
A 1 485 GLY 485 485 485 GLY GLY A . n 
A 1 486 PRO 486 486 486 PRO PRO A . n 
A 1 487 PHE 487 487 487 PHE PHE A . n 
A 1 488 ILE 488 488 488 ILE ILE A . n 
A 1 489 GLY 489 489 489 GLY GLY A . n 
A 1 490 ASN 490 490 ?   ?   ?   A . n 
A 1 491 MET 491 491 491 MET MET A . n 
A 1 492 TYR 492 492 492 TYR TYR A . n 
A 1 493 LEU 493 493 493 LEU LEU A . n 
A 1 494 ALA 494 494 494 ALA ALA A . n 
A 1 495 GLU 495 495 495 GLU ALA A . n 
A 1 496 ASP 496 496 496 ASP ASP A . n 
A 1 497 ARG 497 497 497 ARG ARG A . n 
A 1 498 ILE 498 498 498 ILE ILE A . n 
A 1 499 LEU 499 499 499 LEU LEU A . n 
A 1 500 SER 500 500 500 SER SER A . n 
A 1 501 PHE 501 501 501 PHE PHE A . n 
A 1 502 GLU 502 502 502 GLU GLU A . n 
A 1 503 VAL 503 503 503 VAL VAL A . n 
A 1 504 VAL 504 504 504 VAL VAL A . n 
A 1 505 ALA 505 505 505 ALA ALA A . n 
A 1 506 ARG 506 506 506 ARG ARG A . n 
A 1 507 LYS 507 507 507 LYS LYS A . n 
A 1 508 ASN 508 508 508 ASN ASN A . n 
A 1 509 CYS 509 509 509 CYS CYS A . n 
A 1 510 ASN 510 510 510 ASN ASN A . n 
A 1 511 TRP 511 511 511 TRP TRP A . n 
A 1 512 THR 512 512 512 THR THR A . n 
A 1 513 MET 513 513 513 MET MET A . n 
A 1 514 HIS 514 514 514 HIS HIS A . n 
A 1 515 TYR 515 515 515 TYR TYR A . n 
A 1 516 VAL 516 516 516 VAL VAL A . n 
A 1 517 LYS 517 517 517 LYS LYS A . n 
A 1 518 ASP 518 518 518 ASP ASP A . n 
A 1 519 ALA 519 519 519 ALA ALA A . n 
A 1 520 VAL 520 520 520 VAL VAL A . n 
A 1 521 ALA 521 521 521 ALA ALA A . n 
A 1 522 ARG 522 522 522 ARG ARG A . n 
A 1 523 THR 523 523 523 THR THR A . n 
A 1 524 ASP 524 524 524 ASP ASP A . n 
A 1 525 VAL 525 525 525 VAL VAL A . n 
A 1 526 PRO 526 526 526 PRO PRO A . n 
A 1 527 HIS 527 527 527 HIS HIS A . n 
A 1 528 ASP 528 528 528 ASP ASP A . n 
A 1 529 LEU 529 529 529 LEU LEU A . n 
A 1 530 VAL 530 530 530 VAL VAL A . n 
A 1 531 GLY 531 531 531 GLY GLY A . n 
A 1 532 LEU 532 532 532 LEU LEU A . n 
A 1 533 ILE 533 533 533 ILE ILE A . n 
A 1 534 SER 534 534 534 SER SER A . n 
A 1 535 GLN 535 535 535 GLN GLN A . n 
A 1 536 ARG 536 536 536 ARG ARG A . n 
A 1 537 LYS 537 537 537 LYS LYS A . n 
A 1 538 ARG 538 538 538 ARG ARG A . n 
A 1 539 TRP 539 539 539 TRP TRP A . n 
A 1 540 LEU 540 540 540 LEU LEU A . n 
A 1 541 ASN 541 541 541 ASN ASN A . n 
A 1 542 GLY 542 542 542 GLY GLY A . n 
A 1 543 ALA 543 543 543 ALA ALA A . n 
A 1 544 PHE 544 544 544 PHE PHE A . n 
A 1 545 PHE 545 545 545 PHE PHE A . n 
A 1 546 ALA 546 546 546 ALA ALA A . n 
A 1 547 THR 547 547 547 THR THR A . n 
A 1 548 LEU 548 548 548 LEU LEU A . n 
A 1 549 PHE 549 549 549 PHE PHE A . n 
A 1 550 SER 550 550 550 SER SER A . n 
A 1 551 ILE 551 551 551 ILE ILE A . n 
A 1 552 TRP 552 552 552 TRP TRP A . n 
A 1 553 ASN 553 553 553 ASN ASN A . n 
A 1 554 TRP 554 554 554 TRP TRP A . n 
A 1 555 GLY 555 555 555 GLY GLY A . n 
A 1 556 ARG 556 556 556 ARG ARG A . n 
A 1 557 ILE 557 557 557 ILE ILE A . n 
A 1 558 TYR 558 558 558 TYR TYR A . n 
A 1 559 SER 559 559 559 SER SER A . n 
A 1 560 GLU 560 560 560 GLU GLU A . n 
A 1 561 SER 561 561 561 SER SER A . n 
A 1 562 LYS 562 562 562 LYS LYS A . n 
A 1 563 HIS 563 563 563 HIS HIS A . n 
A 1 564 THR 564 564 564 THR THR A . n 
A 1 565 PHE 565 565 565 PHE PHE A . n 
A 1 566 VAL 566 566 566 VAL VAL A . n 
A 1 567 ARG 567 567 567 ARG ARG A . n 
A 1 568 LYS 568 568 568 LYS LYS A . n 
A 1 569 MET 569 569 569 MET MET A . n 
A 1 570 ALA 570 570 570 ALA ALA A . n 
A 1 571 PHE 571 571 571 PHE PHE A . n 
A 1 572 LEU 572 572 572 LEU LEU A . n 
A 1 573 VAL 573 573 573 VAL VAL A . n 
A 1 574 PHE 574 574 574 PHE PHE A . n 
A 1 575 TYR 575 575 575 TYR TYR A . n 
A 1 576 VAL 576 576 576 VAL VAL A . n 
A 1 577 TYR 577 577 577 TYR TYR A . n 
A 1 578 HIS 578 578 578 HIS HIS A . n 
A 1 579 LEU 579 579 579 LEU LEU A . n 
A 1 580 LEU 580 580 580 LEU LEU A . n 
A 1 581 TYR 581 581 581 TYR TYR A . n 
A 1 582 THR 582 582 582 THR THR A . n 
A 1 583 ALA 583 583 583 ALA ALA A . n 
A 1 584 PHE 584 584 584 PHE PHE A . n 
A 1 585 GLY 585 585 585 GLY GLY A . n 
A 1 586 PHE 586 586 586 PHE PHE A . n 
A 1 587 PHE 587 587 587 PHE PHE A . n 
A 1 588 LEU 588 588 588 LEU LEU A . n 
A 1 589 PRO 589 589 589 PRO PRO A . n 
A 1 590 ALA 590 590 590 ALA ALA A . n 
A 1 591 ASN 591 591 591 ASN ASN A . n 
A 1 592 LEU 592 592 592 LEU LEU A . n 
A 1 593 TYR 593 593 593 TYR TYR A . n 
A 1 594 LEU 594 594 594 LEU LEU A . n 
A 1 595 ALA 595 595 595 ALA ALA A . n 
A 1 596 LEU 596 596 596 LEU LEU A . n 
A 1 597 PHE 597 597 597 PHE PHE A . n 
A 1 598 PHE 598 598 598 PHE PHE A . n 
A 1 599 ILE 599 599 599 ILE ILE A . n 
A 1 600 VAL 600 600 600 VAL VAL A . n 
A 1 601 PHE 601 601 601 PHE PHE A . n 
A 1 602 GLN 602 602 602 GLN GLN A . n 
A 1 603 GLY 603 603 603 GLY GLY A . n 
A 1 604 PHE 604 604 604 PHE PHE A . n 
A 1 605 GLN 605 605 605 GLN GLN A . n 
A 1 606 GLN 606 606 606 GLN GLN A . n 
A 1 607 ASN 607 607 607 ASN ASN A . n 
A 1 608 ARG 608 608 608 ARG ARG A . n 
A 1 609 LEU 609 609 609 LEU LEU A . n 
A 1 610 GLU 610 610 610 GLU GLU A . n 
A 1 611 PHE 611 611 611 PHE PHE A . n 
A 1 612 ILE 612 612 612 ILE ILE A . n 
A 1 613 ASP 613 613 613 ASP ASP A . n 
A 1 614 THR 614 614 614 THR THR A . n 
A 1 615 SER 615 615 615 SER SER A . n 
A 1 616 GLU 616 616 616 GLU GLU A . n 
A 1 617 TYR 617 617 617 TYR TYR A . n 
A 1 618 SER 618 618 618 SER SER A . n 
A 1 619 GLN 619 619 619 GLN GLN A . n 
A 1 620 THR 620 620 620 THR THR A . n 
A 1 621 VAL 621 621 621 VAL VAL A . n 
A 1 622 LEU 622 622 622 LEU LEU A . n 
A 1 623 ASP 623 623 623 ASP ASP A . n 
A 1 624 CYS 624 624 624 CYS CYS A . n 
A 1 625 ALA 625 625 625 ALA ALA A . n 
A 1 626 VAL 626 626 626 VAL VAL A . n 
A 1 627 TYR 627 627 627 TYR TYR A . n 
A 1 628 ILE 628 628 628 ILE ILE A . n 
A 1 629 TYR 629 629 629 TYR TYR A . n 
A 1 630 ASN 630 630 630 ASN ASN A . n 
A 1 631 PHE 631 631 631 PHE PHE A . n 
A 1 632 SER 632 632 632 SER SER A . n 
A 1 633 TYR 633 633 633 TYR TYR A . n 
A 1 634 LEU 634 634 634 LEU LEU A . n 
A 1 635 PHE 635 635 635 PHE PHE A . n 
A 1 636 GLY 636 636 636 GLY GLY A . n 
A 1 637 LEU 637 637 637 LEU LEU A . n 
A 1 638 LEU 638 638 638 LEU LEU A . n 
A 1 639 MET 639 639 639 MET MET A . n 
A 1 640 LEU 640 640 640 LEU LEU A . n 
A 1 641 ILE 641 641 641 ILE ILE A . n 
A 1 642 ILE 642 642 642 ILE ILE A . n 
A 1 643 ILE 643 643 643 ILE ILE A . n 
A 1 644 GLY 644 644 644 GLY GLY A . n 
A 1 645 LEU 645 645 645 LEU LEU A . n 
A 1 646 GLY 646 646 646 GLY GLY A . n 
A 1 647 ASN 647 647 647 ASN ASN A . n 
A 1 648 ASN 648 648 648 ASN ASN A . n 
A 1 649 PRO 649 649 649 PRO PRO A . n 
A 1 650 LYS 650 650 650 LYS LYS A . n 
A 1 651 HIS 651 651 651 HIS HIS A . n 
A 1 652 MET 652 652 652 MET MET A . n 
A 1 653 LYS 653 653 653 LYS LYS A . n 
A 1 654 LEU 654 654 654 LEU LEU A . n 
A 1 655 THR 655 655 655 THR THR A . n 
A 1 656 TYR 656 656 656 TYR TYR A . n 
A 1 657 TYR 657 657 657 TYR TYR A . n 
A 1 658 PHE 658 658 658 PHE PHE A . n 
A 1 659 VAL 659 659 659 VAL VAL A . n 
A 1 660 GLY 660 660 660 GLY GLY A . n 
A 1 661 ALA 661 661 661 ALA ALA A . n 
A 1 662 VAL 662 662 662 VAL VAL A . n 
A 1 663 PHE 663 663 663 PHE PHE A . n 
A 1 664 GLY 664 664 664 GLY GLY A . n 
A 1 665 LEU 665 665 665 LEU LEU A . n 
A 1 666 MET 666 666 666 MET MET A . n 
A 1 667 MET 667 667 667 MET MET A . n 
A 1 668 MET 668 668 668 MET MET A . n 
A 1 669 LEU 669 669 669 LEU LEU A . n 
A 1 670 SER 670 670 670 SER SER A . n 
A 1 671 SER 671 671 671 SER SER A . n 
A 1 672 LEU 672 672 672 LEU LEU A . n 
A 1 673 VAL 673 673 673 VAL VAL A . n 
A 1 674 GLY 674 674 674 GLY GLY A . n 
A 1 675 ALA 675 675 675 ALA ALA A . n 
A 1 676 GLY 676 676 676 GLY GLY A . n 
A 1 677 ILE 677 677 677 ILE ILE A . n 
A 1 678 PHE 678 678 678 PHE PHE A . n 
A 1 679 PHE 679 679 679 PHE PHE A . n 
A 1 680 SER 680 680 680 SER SER A . n 
A 1 681 THR 681 681 681 THR THR A . n 
A 1 682 PRO 682 682 682 PRO PRO A . n 
A 1 683 ALA 683 683 683 ALA ALA A . n 
A 1 684 THR 684 684 684 THR THR A . n 
A 1 685 VAL 685 685 685 VAL VAL A . n 
A 1 686 HIS 686 686 686 HIS HIS A . n 
A 1 687 SER 687 687 687 SER SER A . n 
A 1 688 ILE 688 688 688 ILE ILE A . n 
A 1 689 VAL 689 689 689 VAL VAL A . n 
A 1 690 VAL 690 690 690 VAL VAL A . n 
A 1 691 SER 691 691 691 SER SER A . n 
A 1 692 ILE 692 692 692 ILE ILE A . n 
A 1 693 LEU 693 693 693 LEU LEU A . n 
A 1 694 THR 694 694 694 THR THR A . n 
A 1 695 VAL 695 695 695 VAL VAL A . n 
A 1 696 GLY 696 696 696 GLY GLY A . n 
A 1 697 VAL 697 697 697 VAL VAL A . n 
A 1 698 TYR 698 698 698 TYR TYR A . n 
A 1 699 PHE 699 699 699 PHE PHE A . n 
A 1 700 ILE 700 700 700 ILE ILE A . n 
A 1 701 ALA 701 701 701 ALA ALA A . n 
A 1 702 SER 702 702 702 SER SER A . n 
A 1 703 ALA 703 703 703 ALA ALA A . n 
A 1 704 LEU 704 704 704 LEU LEU A . n 
A 1 705 HIS 705 705 705 HIS HIS A . n 
A 1 706 GLY 706 706 706 GLY GLY A . n 
A 1 707 GLU 707 707 707 GLU GLU A . n 
A 1 708 VAL 708 708 708 VAL VAL A . n 
A 1 709 HIS 709 709 709 HIS HIS A . n 
A 1 710 HIS 710 710 710 HIS HIS A . n 
A 1 711 ILE 711 711 711 ILE ILE A . n 
A 1 712 PHE 712 712 712 PHE PHE A . n 
A 1 713 MET 713 713 713 MET MET A . n 
A 1 714 THR 714 714 714 THR THR A . n 
A 1 715 PHE 715 715 715 PHE PHE A . n 
A 1 716 THR 716 716 716 THR THR A . n 
A 1 717 HIS 717 717 717 HIS HIS A . n 
A 1 718 TYR 718 718 718 TYR TYR A . n 
A 1 719 THR 719 719 719 THR THR A . n 
A 1 720 ALA 720 720 720 ALA ALA A . n 
A 1 721 LEU 721 721 721 LEU LEU A . n 
A 1 722 ILE 722 722 722 ILE ILE A . n 
A 1 723 PRO 723 723 723 PRO PRO A . n 
A 1 724 SER 724 724 724 SER SER A . n 
A 1 725 PHE 725 725 725 PHE PHE A . n 
A 1 726 VAL 726 726 726 VAL VAL A . n 
A 1 727 ASN 727 727 727 ASN ASN A . n 
A 1 728 ILE 728 728 728 ILE ILE A . n 
A 1 729 PHE 729 729 729 PHE PHE A . n 
A 1 730 THR 730 730 730 THR THR A . n 
A 1 731 ILE 731 731 731 ILE ILE A . n 
A 1 732 TYR 732 732 732 TYR TYR A . n 
A 1 733 SER 733 733 733 SER SER A . n 
A 1 734 PHE 734 734 734 PHE PHE A . n 
A 1 735 CYS 735 735 735 CYS CYS A . n 
A 1 736 ASN 736 736 736 ASN ASN A . n 
A 1 737 LEU 737 737 737 LEU LEU A . n 
A 1 738 GLN 738 738 ?   ?   ?   A . n 
A 1 739 ASP 739 739 ?   ?   ?   A . n 
A 1 740 LEU 740 740 ?   ?   ?   A . n 
A 1 741 SER 741 741 ?   ?   ?   A . n 
A 1 742 TRP 742 742 ?   ?   ?   A . n 
A 1 743 GLY 743 743 ?   ?   ?   A . n 
A 1 744 THR 744 744 ?   ?   ?   A . n 
A 1 745 LYS 745 745 ?   ?   ?   A . n 
A 1 746 GLY 746 746 ?   ?   ?   A . n 
A 1 747 LEU 747 747 ?   ?   ?   A . n 
A 1 748 HIS 748 748 ?   ?   ?   A . n 
A 1 749 ASP 749 749 ?   ?   ?   A . n 
A 1 750 ASP 750 750 ?   ?   ?   A . n 
A 1 751 PRO 751 751 ?   ?   ?   A . n 
A 1 752 LEU 752 752 ?   ?   ?   A . n 
A 1 753 LEU 753 753 ?   ?   ?   A . n 
A 1 754 ALA 754 754 ?   ?   ?   A . n 
A 1 755 ALA 755 755 ?   ?   ?   A . n 
A 1 756 SER 756 756 ?   ?   ?   A . n 
A 1 757 LEU 757 757 ?   ?   ?   A . n 
A 1 758 ASP 758 758 ?   ?   ?   A . n 
A 1 759 GLU 759 759 ?   ?   ?   A . n 
A 1 760 THR 760 760 ?   ?   ?   A . n 
A 1 761 GLU 761 761 ?   ?   ?   A . n 
A 1 762 LYS 762 762 762 LYS LYS A . n 
A 1 763 GLY 763 763 763 GLY GLY A . n 
A 1 764 ASP 764 764 764 ASP ASP A . n 
A 1 765 PHE 765 765 765 PHE PHE A . n 
A 1 766 LYS 766 766 766 LYS LYS A . n 
A 1 767 ASP 767 767 767 ASP ASP A . n 
A 1 768 VAL 768 768 768 VAL VAL A . n 
A 1 769 ILE 769 769 769 ILE ILE A . n 
A 1 770 ALA 770 770 770 ALA ALA A . n 
A 1 771 LYS 771 771 771 LYS LYS A . n 
A 1 772 ARG 772 772 772 ARG ARG A . n 
A 1 773 ARG 773 773 773 ARG ARG A . n 
A 1 774 ALA 774 774 774 ALA ALA A . n 
A 1 775 LEU 775 775 775 LEU LEU A . n 
A 1 776 GLU 776 776 776 GLU GLU A . n 
A 1 777 GLU 777 777 777 GLU GLU A . n 
A 1 778 LEU 778 778 778 LEU LEU A . n 
A 1 779 ARG 779 779 779 ARG ARG A . n 
A 1 780 ARG 780 780 780 ARG ARG A . n 
A 1 781 GLU 781 781 781 GLU GLU A . n 
A 1 782 GLU 782 782 782 GLU GLU A . n 
A 1 783 LYS 783 783 783 LYS LYS A . n 
A 1 784 GLU 784 784 784 GLU GLU A . n 
A 1 785 ARG 785 785 785 ARG ARG A . n 
A 1 786 VAL 786 786 786 VAL VAL A . n 
A 1 787 GLU 787 787 787 GLU GLU A . n 
A 1 788 ASN 788 788 788 ASN ASN A . n 
A 1 789 ARG 789 789 789 ARG ARG A . n 
A 1 790 LYS 790 790 790 LYS LYS A . n 
A 1 791 LYS 791 791 791 LYS LYS A . n 
A 1 792 ASN 792 792 792 ASN ASN A . n 
A 1 793 PHE 793 793 793 PHE PHE A . n 
A 1 794 GLU 794 794 794 GLU GLU A . n 
A 1 795 ALA 795 795 795 ALA ALA A . n 
A 1 796 PHE 796 796 796 PHE PHE A . n 
A 1 797 ARG 797 797 797 ARG ARG A . n 
A 1 798 THR 798 798 798 THR THR A . n 
A 1 799 ASN 799 799 799 ASN ASN A . n 
A 1 800 VAL 800 800 800 VAL VAL A . n 
A 1 801 LEU 801 801 801 LEU LEU A . n 
A 1 802 LEU 802 802 802 LEU LEU A . n 
A 1 803 THR 803 803 803 THR THR A . n 
A 1 804 TRP 804 804 804 TRP TRP A . n 
A 1 805 ALA 805 805 805 ALA ALA A . n 
A 1 806 PHE 806 806 806 PHE PHE A . n 
A 1 807 SER 807 807 807 SER SER A . n 
A 1 808 ASN 808 808 808 ASN ASN A . n 
A 1 809 LEU 809 809 809 LEU LEU A . n 
A 1 810 ILE 810 810 810 ILE ILE A . n 
A 1 811 PHE 811 811 811 PHE PHE A . n 
A 1 812 ALA 812 812 812 ALA ALA A . n 
A 1 813 LEU 813 813 813 LEU LEU A . n 
A 1 814 PHE 814 814 814 PHE PHE A . n 
A 1 815 VAL 815 815 815 VAL VAL A . n 
A 1 816 VAL 816 816 816 VAL VAL A . n 
A 1 817 TYR 817 817 817 TYR TYR A . n 
A 1 818 PHE 818 818 818 PHE PHE A . n 
A 1 819 ALA 819 819 819 ALA ALA A . n 
A 1 820 SER 820 820 820 SER SER A . n 
A 1 821 SER 821 821 821 SER SER A . n 
A 1 822 SER 822 822 822 SER SER A . n 
A 1 823 THR 823 823 823 THR THR A . n 
A 1 824 TYR 824 824 824 TYR TYR A . n 
A 1 825 MET 825 825 825 MET MET A . n 
A 1 826 PRO 826 826 826 PRO PRO A . n 
A 1 827 VAL 827 827 827 VAL VAL A . n 
A 1 828 LEU 828 828 828 LEU LEU A . n 
A 1 829 TYR 829 829 829 TYR TYR A . n 
A 1 830 ILE 830 830 830 ILE ILE A . n 
A 1 831 PHE 831 831 831 PHE PHE A . n 
A 1 832 VAL 832 832 832 VAL VAL A . n 
A 1 833 ALA 833 833 833 ALA ALA A . n 
A 1 834 SER 834 834 834 SER SER A . n 
A 1 835 LEU 835 835 835 LEU LEU A . n 
A 1 836 ASN 836 836 836 ASN ASN A . n 
A 1 837 THR 837 837 837 THR THR A . n 
A 1 838 CYS 838 838 838 CYS CYS A . n 
A 1 839 ARG 839 839 839 ARG ARG A . n 
A 1 840 LEU 840 840 840 LEU LEU A . n 
A 1 841 LEU 841 841 841 LEU LEU A . n 
A 1 842 GLY 842 842 842 GLY GLY A . n 
A 1 843 SER 843 843 843 SER SER A . n 
A 1 844 ILE 844 844 844 ILE ILE A . n 
A 1 845 GLY 845 845 845 GLY GLY A . n 
A 1 846 HIS 846 846 846 HIS HIS A . n 
A 1 847 TRP 847 847 847 TRP TRP A . n 
A 1 848 VAL 848 848 848 VAL VAL A . n 
A 1 849 TYR 849 849 849 TYR TYR A . n 
A 1 850 ILE 850 850 850 ILE ILE A . n 
A 1 851 HIS 851 851 851 HIS HIS A . n 
A 1 852 THR 852 852 852 THR THR A . n 
A 1 853 GLU 853 853 853 GLU GLU A . n 
A 1 854 GLY 854 854 854 GLY GLY A . n 
A 1 855 LEU 855 855 855 LEU LEU A . n 
A 1 856 ARG 856 856 856 ARG ARG A . n 
A 1 857 GLY 857 857 857 GLY GLY A . n 
A 1 858 ARG 858 858 858 ARG ARG A . n 
A 1 859 VAL 859 859 859 VAL VAL A . n 
A 1 860 ILE 860 860 ?   ?   ?   A . n 
A 1 861 ASP 861 861 ?   ?   ?   A . n 
A 1 862 LYS 862 862 ?   ?   ?   A . n 
A 1 863 SER 863 863 ?   ?   ?   A . n 
A 1 864 GLU 864 864 ?   ?   ?   A . n 
A 1 865 CYS 865 865 ?   ?   ?   A . n 
A 1 866 GLY 866 866 ?   ?   ?   A . n 
A 1 867 ASN 867 867 ?   ?   ?   A . n 
A 1 868 GLY 868 868 ?   ?   ?   A . n 
A 1 869 THR 869 869 ?   ?   ?   A . n 
A 1 870 GLY 870 870 ?   ?   ?   A . n 
A 1 871 ARG 871 871 ?   ?   ?   A . n 
A 1 872 TYR 872 872 ?   ?   ?   A . n 
A 1 873 PRO 873 873 ?   ?   ?   A . n 
A 1 874 GLN 874 874 ?   ?   ?   A . n 
A 1 875 ASN 875 875 ?   ?   ?   A . n 
A 1 876 SER 876 876 ?   ?   ?   A . n 
A 1 877 TYR 877 877 ?   ?   ?   A . n 
A 1 878 VAL 878 878 ?   ?   ?   A . n 
A 1 879 GLN 879 879 ?   ?   ?   A . n 
A 1 880 LEU 880 880 ?   ?   ?   A . n 
A 1 881 GLU 881 881 ?   ?   ?   A . n 
A 1 882 GLU 882 882 ?   ?   ?   A . n 
A 1 883 HIS 883 883 ?   ?   ?   A . n 
A 1 884 TYR 884 884 ?   ?   ?   A . n 
A 1 885 ALA 885 885 ?   ?   ?   A . n 
A 1 886 ALA 886 886 ?   ?   ?   A . n 
A 1 887 LEU 887 887 ?   ?   ?   A . n 
A 1 888 ALA 888 888 ?   ?   ?   A . n 
A 1 889 GLU 889 889 ?   ?   ?   A . n 
A 1 890 ASP 890 890 ?   ?   ?   A . n 
A 1 891 GLN 891 891 ?   ?   ?   A . n 
A 1 892 ARG 892 892 ?   ?   ?   A . n 
A 1 893 THR 893 893 ?   ?   ?   A . n 
A 1 894 TYR 894 894 ?   ?   ?   A . n 
A 1 895 ALA 895 895 ?   ?   ?   A . n 
A 1 896 SER 896 896 ?   ?   ?   A . n 
A 1 897 GLY 897 897 ?   ?   ?   A . n 
A 1 898 ARG 898 898 ?   ?   ?   A . n 
A 1 899 THR 899 899 ?   ?   ?   A . n 
A 1 900 ASN 900 900 ?   ?   ?   A . n 
A 1 901 ALA 901 901 ?   ?   ?   A . n 
A 1 902 SER 902 902 ?   ?   ?   A . n 
A 1 903 VAL 903 903 ?   ?   ?   A . n 
A 1 904 ARG 904 904 ?   ?   ?   A . n 
A 1 905 THR 905 905 ?   ?   ?   A . n 
A 1 906 VAL 906 906 ?   ?   ?   A . n 
A 1 907 ASN 907 907 ?   ?   ?   A . n 
A 1 908 ASP 908 908 ?   ?   ?   A . n 
A 1 909 VAL 909 909 ?   ?   ?   A . n 
A 1 910 SER 910 910 ?   ?   ?   A . n 
A 1 911 SER 911 911 ?   ?   ?   A . n 
A 1 912 ALA 912 912 ?   ?   ?   A . n 
A 1 913 ALA 913 913 ?   ?   ?   A . n 
A 1 914 LEU 914 914 ?   ?   ?   A . n 
A 1 915 VAL 915 915 ?   ?   ?   A . n 
A 1 916 PRO 916 916 ?   ?   ?   A . n 
A 1 917 ARG 917 917 ?   ?   ?   A . n 
A 1 918 GLY 918 918 ?   ?   ?   A . n 
A 1 919 SER 919 919 ?   ?   ?   A . n 
A 1 920 HIS 920 920 ?   ?   ?   A . n 
A 1 921 HIS 921 921 ?   ?   ?   A . n 
A 1 922 HIS 922 922 ?   ?   ?   A . n 
A 1 923 HIS 923 923 ?   ?   ?   A . n 
A 1 924 HIS 924 924 ?   ?   ?   A . n 
A 1 925 HIS 925 925 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   GLY 3   3   ?   ?   ?   B . n 
B 1 4   ALA 4   4   ?   ?   ?   B . n 
B 1 5   PRO 5   5   ?   ?   ?   B . n 
B 1 6   PRO 6   6   ?   ?   ?   B . n 
B 1 7   PRO 7   7   ?   ?   ?   B . n 
B 1 8   SER 8   8   ?   ?   ?   B . n 
B 1 9   SER 9   9   ?   ?   ?   B . n 
B 1 10  GLY 10  10  ?   ?   ?   B . n 
B 1 11  PHE 11  11  ?   ?   ?   B . n 
B 1 12  ALA 12  12  ?   ?   ?   B . n 
B 1 13  PRO 13  13  ?   ?   ?   B . n 
B 1 14  ARG 14  14  ?   ?   ?   B . n 
B 1 15  SER 15  15  ?   ?   ?   B . n 
B 1 16  TYR 16  16  ?   ?   ?   B . n 
B 1 17  GLY 17  17  ?   ?   ?   B . n 
B 1 18  GLN 18  18  ?   ?   ?   B . n 
B 1 19  GLN 19  19  ?   ?   ?   B . n 
B 1 20  PRO 20  20  ?   ?   ?   B . n 
B 1 21  LEU 21  21  ?   ?   ?   B . n 
B 1 22  SER 22  22  ?   ?   ?   B . n 
B 1 23  HIS 23  23  23  HIS HIS B . n 
B 1 24  ALA 24  24  24  ALA ALA B . n 
B 1 25  PRO 25  25  25  PRO PRO B . n 
B 1 26  ARG 26  26  26  ARG ARG B . n 
B 1 27  SER 27  27  27  SER SER B . n 
B 1 28  SER 28  28  28  SER SER B . n 
B 1 29  MET 29  29  29  MET MET B . n 
B 1 30  MET 30  30  30  MET MET B . n 
B 1 31  SER 31  31  31  SER SER B . n 
B 1 32  VAL 32  32  32  VAL VAL B . n 
B 1 33  GLU 33  33  33  GLU GLU B . n 
B 1 34  TYR 34  34  34  TYR TYR B . n 
B 1 35  ASP 35  35  35  ASP ASP B . n 
B 1 36  GLY 36  36  36  GLY GLY B . n 
B 1 37  ILE 37  37  37  ILE ILE B . n 
B 1 38  PRO 38  38  38  PRO PRO B . n 
B 1 39  LEU 39  39  39  LEU LEU B . n 
B 1 40  PRO 40  40  ?   ?   ?   B . n 
B 1 41  PRO 41  41  ?   ?   ?   B . n 
B 1 42  PRO 42  42  ?   ?   ?   B . n 
B 1 43  SER 43  43  ?   ?   ?   B . n 
B 1 44  ILE 44  44  ?   ?   ?   B . n 
B 1 45  ARG 45  45  ?   ?   ?   B . n 
B 1 46  SER 46  46  ?   ?   ?   B . n 
B 1 47  CYS 47  47  ?   ?   ?   B . n 
B 1 48  GLY 48  48  ?   ?   ?   B . n 
B 1 49  SER 49  49  ?   ?   ?   B . n 
B 1 50  GLN 50  50  ?   ?   ?   B . n 
B 1 51  GLN 51  51  ?   ?   ?   B . n 
B 1 52  TYR 52  52  ?   ?   ?   B . n 
B 1 53  VAL 53  53  ?   ?   ?   B . n 
B 1 54  THR 54  54  ?   ?   ?   B . n 
B 1 55  SER 55  55  ?   ?   ?   B . n 
B 1 56  TYR 56  56  ?   ?   ?   B . n 
B 1 57  ILE 57  57  ?   ?   ?   B . n 
B 1 58  PRO 58  58  ?   ?   ?   B . n 
B 1 59  THR 59  59  ?   ?   ?   B . n 
B 1 60  GLY 60  60  ?   ?   ?   B . n 
B 1 61  ALA 61  61  ?   ?   ?   B . n 
B 1 62  ALA 62  62  ?   ?   ?   B . n 
B 1 63  PHE 63  63  ?   ?   ?   B . n 
B 1 64  PRO 64  64  ?   ?   ?   B . n 
B 1 65  PRO 65  65  ?   ?   ?   B . n 
B 1 66  SER 66  66  ?   ?   ?   B . n 
B 1 67  SER 67  67  ?   ?   ?   B . n 
B 1 68  VAL 68  68  ?   ?   ?   B . n 
B 1 69  GLN 69  69  ?   ?   ?   B . n 
B 1 70  ASP 70  70  ?   ?   ?   B . n 
B 1 71  MET 71  71  ?   ?   ?   B . n 
B 1 72  ILE 72  72  ?   ?   ?   B . n 
B 1 73  SER 73  73  ?   ?   ?   B . n 
B 1 74  SER 74  74  ?   ?   ?   B . n 
B 1 75  MET 75  75  ?   ?   ?   B . n 
B 1 76  LYS 76  76  ?   ?   ?   B . n 
B 1 77  SER 77  77  ?   ?   ?   B . n 
B 1 78  TYR 78  78  ?   ?   ?   B . n 
B 1 79  ALA 79  79  ?   ?   ?   B . n 
B 1 80  SER 80  80  ?   ?   ?   B . n 
B 1 81  ALA 81  81  ?   ?   ?   B . n 
B 1 82  THR 82  82  ?   ?   ?   B . n 
B 1 83  ASP 83  83  ?   ?   ?   B . n 
B 1 84  LEU 84  84  ?   ?   ?   B . n 
B 1 85  VAL 85  85  ?   ?   ?   B . n 
B 1 86  ARG 86  86  ?   ?   ?   B . n 
B 1 87  THR 87  87  ?   ?   ?   B . n 
B 1 88  TYR 88  88  ?   ?   ?   B . n 
B 1 89  SER 89  89  ?   ?   ?   B . n 
B 1 90  GLU 90  90  ?   ?   ?   B . n 
B 1 91  ILE 91  91  91  ILE ILE B . n 
B 1 92  PRO 92  92  92  PRO PRO B . n 
B 1 93  SER 93  93  93  SER SER B . n 
B 1 94  VAL 94  94  94  VAL VAL B . n 
B 1 95  GLU 95  95  95  GLU GLU B . n 
B 1 96  GLU 96  96  96  GLU GLU B . n 
B 1 97  ALA 97  97  97  ALA ALA B . n 
B 1 98  LEU 98  98  98  LEU LEU B . n 
B 1 99  SER 99  99  99  SER SER B . n 
B 1 100 THR 100 100 100 THR THR B . n 
B 1 101 LEU 101 101 101 LEU LEU B . n 
B 1 102 ASP 102 102 102 ASP ASP B . n 
B 1 103 ARG 103 103 103 ARG ARG B . n 
B 1 104 ALA 104 104 104 ALA ALA B . n 
B 1 105 ALA 105 105 105 ALA ALA B . n 
B 1 106 ALA 106 106 106 ALA ALA B . n 
B 1 107 ALA 107 107 107 ALA ALA B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 ASN 109 109 109 ASN ASN B . n 
B 1 110 ALA 110 110 110 ALA ALA B . n 
B 1 111 ARG 111 111 111 ARG ARG B . n 
B 1 112 ARG 112 112 112 ARG ARG B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 ARG 114 114 114 ARG ARG B . n 
B 1 115 ASP 115 115 115 ASP ASP B . n 
B 1 116 ALA 116 116 116 ALA ALA B . n 
B 1 117 LEU 117 117 117 LEU LEU B . n 
B 1 118 LYS 118 118 118 LYS LYS B . n 
B 1 119 LEU 119 119 119 LEU LEU B . n 
B 1 120 TYR 120 120 120 TYR TYR B . n 
B 1 121 LEU 121 121 121 LEU LEU B . n 
B 1 122 GLU 122 122 ?   ?   ?   B . n 
B 1 123 GLY 123 123 123 GLY GLY B . n 
B 1 124 GLY 124 124 124 GLY GLY B . n 
B 1 125 TYR 125 125 ?   ?   ?   B . n 
B 1 126 ALA 126 126 ?   ?   ?   B . n 
B 1 127 MET 127 127 ?   ?   ?   B . n 
B 1 128 ALA 128 128 128 ALA ALA B . n 
B 1 129 ASN 129 129 129 ASN ASN B . n 
B 1 130 VAL 130 130 130 VAL VAL B . n 
B 1 131 ALA 131 131 131 ALA ALA B . n 
B 1 132 GLU 132 132 ?   ?   ?   B . n 
B 1 133 ARG 133 133 133 ARG ARG B . n 
B 1 134 GLN 134 134 134 GLN GLN B . n 
B 1 135 ALA 135 135 135 ALA ALA B . n 
B 1 136 ASN 136 136 136 ASN ASN B . n 
B 1 137 PRO 137 137 137 PRO PRO B . n 
B 1 138 LYS 138 138 138 LYS LYS B . n 
B 1 139 ILE 139 139 139 ILE ILE B . n 
B 1 140 CYS 140 140 140 CYS CYS B . n 
B 1 141 ASN 141 141 141 ASN ASN B . n 
B 1 142 LEU 142 142 142 LEU LEU B . n 
B 1 143 LEU 143 143 143 LEU LEU B . n 
B 1 144 THR 144 144 144 THR THR B . n 
B 1 145 SER 145 145 145 SER SER B . n 
B 1 146 LYS 146 146 146 LYS LYS B . n 
B 1 147 GLY 147 147 147 GLY GLY B . n 
B 1 148 PHE 148 148 148 PHE PHE B . n 
B 1 149 GLU 149 149 149 GLU GLU B . n 
B 1 150 THR 150 150 150 THR THR B . n 
B 1 151 LEU 151 151 151 LEU LEU B . n 
B 1 152 ASN 152 152 152 ASN ASN B . n 
B 1 153 TRP 153 153 153 TRP TRP B . n 
B 1 154 CYS 154 154 154 CYS CYS B . n 
B 1 155 ALA 155 155 155 ALA ALA B . n 
B 1 156 ARG 156 156 156 ARG ARG B . n 
B 1 157 LEU 157 157 157 LEU LEU B . n 
B 1 158 CYS 158 158 158 CYS CYS B . n 
B 1 159 ASP 159 159 159 ASP ASP B . n 
B 1 160 TRP 160 160 160 TRP TRP B . n 
B 1 161 ILE 161 161 161 ILE ILE B . n 
B 1 162 GLU 162 162 162 GLU GLU B . n 
B 1 163 GLY 163 163 163 GLY GLY B . n 
B 1 164 ARG 164 164 164 ARG ARG B . n 
B 1 165 ILE 165 165 165 ILE ILE B . n 
B 1 166 LYS 166 166 166 LYS LYS B . n 
B 1 167 GLU 167 167 167 GLU GLU B . n 
B 1 168 LYS 168 168 168 LYS LYS B . n 
B 1 169 HIS 169 169 169 HIS HIS B . n 
B 1 170 PRO 170 170 170 PRO PRO B . n 
B 1 171 ARG 171 171 171 ARG ARG B . n 
B 1 172 PRO 172 172 172 PRO PRO B . n 
B 1 173 GLY 173 173 173 GLY GLY B . n 
B 1 174 VAL 174 174 174 VAL VAL B . n 
B 1 175 HIS 175 175 175 HIS HIS B . n 
B 1 176 LYS 176 176 176 LYS LYS B . n 
B 1 177 VAL 177 177 177 VAL VAL B . n 
B 1 178 GLY 178 178 178 GLY GLY B . n 
B 1 179 ILE 179 179 179 ILE ILE B . n 
B 1 180 PRO 180 180 180 PRO PRO B . n 
B 1 181 VAL 181 181 181 VAL VAL B . n 
B 1 182 SER 182 182 182 SER SER B . n 
B 1 183 ASN 183 183 183 ASN ASN B . n 
B 1 184 TRP 184 184 184 TRP TRP B . n 
B 1 185 ASP 185 185 185 ASP ASP B . n 
B 1 186 GLU 186 186 186 GLU GLU B . n 
B 1 187 ASP 187 187 187 ASP ASP B . n 
B 1 188 TRP 188 188 188 TRP TRP B . n 
B 1 189 VAL 189 189 189 VAL VAL B . n 
B 1 190 GLY 190 190 190 GLY GLY B . n 
B 1 191 PRO 191 191 191 PRO PRO B . n 
B 1 192 PHE 192 192 192 PHE PHE B . n 
B 1 193 MET 193 193 193 MET MET B . n 
B 1 194 ASP 194 194 194 ASP ASP B . n 
B 1 195 GLU 195 195 195 GLU GLU B . n 
B 1 196 GLU 196 196 196 GLU GLU B . n 
B 1 197 GLU 197 197 197 GLU GLU B . n 
B 1 198 ALA 198 198 198 ALA ALA B . n 
B 1 199 ARG 199 199 199 ARG ARG B . n 
B 1 200 ARG 200 200 200 ARG ARG B . n 
B 1 201 MET 201 201 201 MET MET B . n 
B 1 202 TRP 202 202 202 TRP TRP B . n 
B 1 203 TYR 203 203 203 TYR TYR B . n 
B 1 204 THR 204 204 204 THR THR B . n 
B 1 205 PRO 205 205 205 PRO PRO B . n 
B 1 206 VAL 206 206 206 VAL VAL B . n 
B 1 207 TYR 207 207 207 TYR TYR B . n 
B 1 208 CYS 208 208 208 CYS CYS B . n 
B 1 209 PRO 209 209 209 PRO PRO B . n 
B 1 210 HIS 210 210 210 HIS HIS B . n 
B 1 211 PRO 211 211 211 PRO PRO B . n 
B 1 212 ILE 212 212 212 ILE ILE B . n 
B 1 213 ASP 213 213 213 ASP ASP B . n 
B 1 214 PHE 214 214 214 PHE PHE B . n 
B 1 215 SER 215 215 215 SER SER B . n 
B 1 216 ASN 216 216 216 ASN ASN B . n 
B 1 217 LEU 217 217 217 LEU LEU B . n 
B 1 218 GLY 218 218 218 GLY GLY B . n 
B 1 219 TYR 219 219 219 TYR TYR B . n 
B 1 220 ARG 220 220 220 ARG ARG B . n 
B 1 221 LEU 221 221 221 LEU LEU B . n 
B 1 222 ARG 222 222 222 ARG ARG B . n 
B 1 223 CYS 223 223 223 CYS CYS B . n 
B 1 224 VAL 224 224 224 VAL VAL B . n 
B 1 225 GLU 225 225 225 GLU GLU B . n 
B 1 226 THR 226 226 226 THR THR B . n 
B 1 227 GLY 227 227 227 GLY GLY B . n 
B 1 228 ARG 228 228 228 ARG ARG B . n 
B 1 229 ARG 229 229 229 ARG ARG B . n 
B 1 230 PRO 230 230 230 PRO PRO B . n 
B 1 231 ARG 231 231 231 ARG ARG B . n 
B 1 232 LEU 232 232 232 LEU LEU B . n 
B 1 233 MET 233 233 233 MET MET B . n 
B 1 234 ILE 234 234 234 ILE ILE B . n 
B 1 235 CYS 235 235 235 CYS CYS B . n 
B 1 236 ILE 236 236 236 ILE ILE B . n 
B 1 237 THR 237 237 237 THR THR B . n 
B 1 238 MET 238 238 238 MET MET B . n 
B 1 239 TYR 239 239 239 TYR TYR B . n 
B 1 240 ASN 240 240 240 ASN ASN B . n 
B 1 241 GLU 241 241 241 GLU GLU B . n 
B 1 242 GLY 242 242 242 GLY GLY B . n 
B 1 243 PRO 243 243 243 PRO PRO B . n 
B 1 244 GLN 244 244 244 GLN GLN B . n 
B 1 245 GLN 245 245 245 GLN GLN B . n 
B 1 246 LEU 246 246 246 LEU LEU B . n 
B 1 247 LYS 247 247 247 LYS LYS B . n 
B 1 248 ALA 248 248 248 ALA ALA B . n 
B 1 249 THR 249 249 249 THR THR B . n 
B 1 250 LEU 250 250 250 LEU LEU B . n 
B 1 251 LYS 251 251 251 LYS LYS B . n 
B 1 252 LYS 252 252 252 LYS LYS B . n 
B 1 253 LEU 253 253 253 LEU LEU B . n 
B 1 254 ALA 254 254 254 ALA ALA B . n 
B 1 255 ASN 255 255 255 ASN ASN B . n 
B 1 256 ASN 256 256 256 ASN ASN B . n 
B 1 257 LEU 257 257 257 LEU LEU B . n 
B 1 258 ALA 258 258 258 ALA ALA B . n 
B 1 259 TYR 259 259 259 TYR TYR B . n 
B 1 260 LEU 260 260 260 LEU LEU B . n 
B 1 261 LYS 261 261 261 LYS LYS B . n 
B 1 262 GLU 262 262 262 GLU GLU B . n 
B 1 263 GLN 263 263 263 GLN GLN B . n 
B 1 264 MET 264 264 264 MET MET B . n 
B 1 265 PRO 265 265 265 PRO PRO B . n 
B 1 266 GLY 266 266 266 GLY GLY B . n 
B 1 267 ASP 267 267 267 ASP ASP B . n 
B 1 268 GLU 268 268 268 GLU GLU B . n 
B 1 269 LYS 269 269 269 LYS LYS B . n 
B 1 270 SER 270 270 270 SER SER B . n 
B 1 271 LEU 271 271 271 LEU LEU B . n 
B 1 272 THR 272 272 272 THR THR B . n 
B 1 273 GLY 273 273 273 GLY GLY B . n 
B 1 274 ALA 274 274 274 ALA ALA B . n 
B 1 275 PHE 275 275 275 PHE PHE B . n 
B 1 276 ALA 276 276 276 ALA ALA B . n 
B 1 277 GLY 277 277 277 GLY GLY B . n 
B 1 278 ASP 278 278 278 ASP ASP B . n 
B 1 279 ASP 279 279 279 ASP ASP B . n 
B 1 280 VAL 280 280 280 VAL VAL B . n 
B 1 281 TRP 281 281 281 TRP TRP B . n 
B 1 282 GLN 282 282 282 GLN GLN B . n 
B 1 283 ASN 283 283 283 ASN ASN B . n 
B 1 284 VAL 284 284 284 VAL VAL B . n 
B 1 285 LEU 285 285 285 LEU LEU B . n 
B 1 286 VAL 286 286 286 VAL VAL B . n 
B 1 287 CYS 287 287 287 CYS CYS B . n 
B 1 288 ILE 288 288 288 ILE ILE B . n 
B 1 289 VAL 289 289 289 VAL VAL B . n 
B 1 290 ALA 290 290 290 ALA ALA B . n 
B 1 291 ASP 291 291 291 ASP ASP B . n 
B 1 292 GLY 292 292 292 GLY GLY B . n 
B 1 293 ARG 293 293 293 ARG ARG B . n 
B 1 294 GLU 294 294 294 GLU GLU B . n 
B 1 295 GLN 295 295 295 GLN GLN B . n 
B 1 296 VAL 296 296 296 VAL VAL B . n 
B 1 297 HIS 297 297 297 HIS HIS B . n 
B 1 298 PRO 298 298 298 PRO PRO B . n 
B 1 299 LYS 299 299 299 LYS LYS B . n 
B 1 300 THR 300 300 300 THR THR B . n 
B 1 301 LEU 301 301 301 LEU LEU B . n 
B 1 302 ASP 302 302 302 ASP ASP B . n 
B 1 303 TYR 303 303 303 TYR TYR B . n 
B 1 304 LEU 304 304 304 LEU LEU B . n 
B 1 305 GLU 305 305 305 GLU GLU B . n 
B 1 306 ALA 306 306 306 ALA ALA B . n 
B 1 307 ILE 307 307 307 ILE ILE B . n 
B 1 308 GLY 308 308 308 GLY GLY B . n 
B 1 309 LEU 309 309 309 LEU LEU B . n 
B 1 310 TYR 310 310 310 TYR TYR B . n 
B 1 311 ASP 311 311 311 ASP ASP B . n 
B 1 312 GLU 312 312 312 GLU GLU B . n 
B 1 313 ASP 313 313 313 ASP ASP B . n 
B 1 314 LEU 314 314 314 LEU LEU B . n 
B 1 315 LEU 315 315 315 LEU LEU B . n 
B 1 316 THR 316 316 316 THR THR B . n 
B 1 317 ILE 317 317 317 ILE ILE B . n 
B 1 318 ASN 318 318 318 ASN ASN B . n 
B 1 319 SER 319 319 319 SER SER B . n 
B 1 320 ALA 320 320 320 ALA ALA B . n 
B 1 321 GLY 321 321 321 GLY GLY B . n 
B 1 322 ILE 322 322 322 ILE ILE B . n 
B 1 323 GLY 323 323 323 GLY GLY B . n 
B 1 324 ALA 324 324 324 ALA ALA B . n 
B 1 325 GLN 325 325 325 GLN GLN B . n 
B 1 326 CYS 326 326 326 CYS CYS B . n 
B 1 327 HIS 327 327 327 HIS HIS B . n 
B 1 328 LEU 328 328 328 LEU LEU B . n 
B 1 329 PHE 329 329 329 PHE PHE B . n 
B 1 330 GLU 330 330 330 GLU GLU B . n 
B 1 331 HIS 331 331 331 HIS HIS B . n 
B 1 332 THR 332 332 332 THR THR B . n 
B 1 333 LEU 333 333 333 LEU LEU B . n 
B 1 334 GLN 334 334 334 GLN GLN B . n 
B 1 335 LEU 335 335 335 LEU LEU B . n 
B 1 336 SER 336 336 336 SER SER B . n 
B 1 337 VAL 337 337 337 VAL VAL B . n 
B 1 338 ASN 338 338 338 ASN ASN B . n 
B 1 339 GLY 339 339 339 GLY GLY B . n 
B 1 340 LYS 340 340 340 LYS LYS B . n 
B 1 341 CYS 341 341 341 CYS CYS B . n 
B 1 342 LEU 342 342 342 LEU LEU B . n 
B 1 343 LEU 343 343 343 LEU LEU B . n 
B 1 344 PRO 344 344 344 PRO PRO B . n 
B 1 345 ILE 345 345 345 ILE ILE B . n 
B 1 346 GLN 346 346 346 GLN GLN B . n 
B 1 347 THR 347 347 347 THR THR B . n 
B 1 348 VAL 348 348 348 VAL VAL B . n 
B 1 349 PHE 349 349 349 PHE PHE B . n 
B 1 350 ALA 350 350 350 ALA ALA B . n 
B 1 351 LEU 351 351 351 LEU LEU B . n 
B 1 352 LYS 352 352 352 LYS LYS B . n 
B 1 353 GLU 353 353 353 GLU GLU B . n 
B 1 354 ASN 354 354 354 ASN ASN B . n 
B 1 355 LYS 355 355 355 LYS LYS B . n 
B 1 356 ALA 356 356 356 ALA ALA B . n 
B 1 357 SER 357 357 357 SER SER B . n 
B 1 358 LYS 358 358 358 LYS LYS B . n 
B 1 359 LEU 359 359 359 LEU LEU B . n 
B 1 360 ASP 360 360 360 ASP ASP B . n 
B 1 361 SER 361 361 361 SER SER B . n 
B 1 362 HIS 362 362 362 HIS HIS B . n 
B 1 363 HIS 363 363 363 HIS HIS B . n 
B 1 364 TRP 364 364 364 TRP TRP B . n 
B 1 365 TYR 365 365 365 TYR TYR B . n 
B 1 366 PHE 366 366 366 PHE PHE B . n 
B 1 367 ASN 367 367 367 ASN ASN B . n 
B 1 368 ALA 368 368 368 ALA ALA B . n 
B 1 369 PHE 369 369 369 PHE PHE B . n 
B 1 370 ALA 370 370 370 ALA ALA B . n 
B 1 371 GLU 371 371 371 GLU GLU B . n 
B 1 372 GLN 372 372 372 GLN GLN B . n 
B 1 373 ILE 373 373 373 ILE ILE B . n 
B 1 374 GLN 374 374 374 GLN GLN B . n 
B 1 375 PRO 375 375 375 PRO PRO B . n 
B 1 376 GLU 376 376 376 GLU GLU B . n 
B 1 377 TYR 377 377 377 TYR TYR B . n 
B 1 378 THR 378 378 378 THR THR B . n 
B 1 379 ALA 379 379 379 ALA ALA B . n 
B 1 380 VAL 380 380 380 VAL VAL B . n 
B 1 381 MET 381 381 381 MET MET B . n 
B 1 382 ASP 382 382 382 ASP ASP B . n 
B 1 383 VAL 383 383 383 VAL VAL B . n 
B 1 384 GLY 384 384 384 GLY GLY B . n 
B 1 385 THR 385 385 385 THR THR B . n 
B 1 386 MET 386 386 386 MET MET B . n 
B 1 387 LEU 387 387 387 LEU LEU B . n 
B 1 388 THR 388 388 388 THR THR B . n 
B 1 389 LYS 389 389 389 LYS LYS B . n 
B 1 390 SER 390 390 390 SER SER B . n 
B 1 391 ALA 391 391 391 ALA ALA B . n 
B 1 392 LEU 392 392 392 LEU LEU B . n 
B 1 393 TYR 393 393 393 TYR TYR B . n 
B 1 394 HIS 394 394 394 HIS HIS B . n 
B 1 395 LEU 395 395 395 LEU LEU B . n 
B 1 396 LEU 396 396 396 LEU LEU B . n 
B 1 397 PHE 397 397 397 PHE PHE B . n 
B 1 398 ALA 398 398 398 ALA ALA B . n 
B 1 399 PHE 399 399 399 PHE PHE B . n 
B 1 400 GLU 400 400 400 GLU GLU B . n 
B 1 401 ARG 401 401 401 ARG ARG B . n 
B 1 402 ASN 402 402 402 ASN ASN B . n 
B 1 403 HIS 403 403 403 HIS HIS B . n 
B 1 404 GLN 404 404 404 GLN GLN B . n 
B 1 405 ILE 405 405 405 ILE ILE B . n 
B 1 406 GLY 406 406 406 GLY GLY B . n 
B 1 407 GLY 407 407 407 GLY GLY B . n 
B 1 408 ALA 408 408 408 ALA ALA B . n 
B 1 409 CYS 409 409 409 CYS CYS B . n 
B 1 410 GLY 410 410 410 GLY GLY B . n 
B 1 411 GLN 411 411 411 GLN GLN B . n 
B 1 412 LEU 412 412 412 LEU LEU B . n 
B 1 413 THR 413 413 413 THR THR B . n 
B 1 414 VAL 414 414 414 VAL VAL B . n 
B 1 415 ASP 415 415 415 ASP ASP B . n 
B 1 416 ASN 416 416 416 ASN ASN B . n 
B 1 417 PRO 417 417 417 PRO PRO B . n 
B 1 418 PHE 418 418 418 PHE PHE B . n 
B 1 419 GLU 419 419 419 GLU GLU B . n 
B 1 420 ASN 420 420 420 ASN ASN B . n 
B 1 421 LEU 421 421 421 LEU LEU B . n 
B 1 422 SER 422 422 422 SER SER B . n 
B 1 423 ASN 423 423 423 ASN ASN B . n 
B 1 424 TRP 424 424 424 TRP TRP B . n 
B 1 425 VAL 425 425 425 VAL VAL B . n 
B 1 426 ILE 426 426 426 ILE ILE B . n 
B 1 427 SER 427 427 427 SER SER B . n 
B 1 428 ALA 428 428 428 ALA ALA B . n 
B 1 429 GLN 429 429 429 GLN GLN B . n 
B 1 430 HIS 430 430 430 HIS HIS B . n 
B 1 431 PHE 431 431 431 PHE PHE B . n 
B 1 432 GLU 432 432 432 GLU GLU B . n 
B 1 433 TYR 433 433 433 TYR TYR B . n 
B 1 434 LYS 434 434 434 LYS LYS B . n 
B 1 435 ILE 435 435 435 ILE ILE B . n 
B 1 436 SER 436 436 436 SER SER B . n 
B 1 437 ASN 437 437 437 ASN ASN B . n 
B 1 438 ILE 438 438 438 ILE ILE B . n 
B 1 439 LEU 439 439 439 LEU LEU B . n 
B 1 440 ASP 440 440 440 ASP ASP B . n 
B 1 441 LYS 441 441 441 LYS LYS B . n 
B 1 442 SER 442 442 442 SER SER B . n 
B 1 443 LEU 443 443 443 LEU LEU B . n 
B 1 444 GLU 444 444 444 GLU GLU B . n 
B 1 445 SER 445 445 445 SER SER B . n 
B 1 446 CYS 446 446 446 CYS CYS B . n 
B 1 447 PHE 447 447 447 PHE PHE B . n 
B 1 448 GLY 448 448 448 GLY GLY B . n 
B 1 449 PHE 449 449 449 PHE PHE B . n 
B 1 450 ILE 450 450 450 ILE ILE B . n 
B 1 451 SER 451 451 451 SER SER B . n 
B 1 452 VAL 452 452 452 VAL VAL B . n 
B 1 453 LEU 453 453 453 LEU LEU B . n 
B 1 454 PRO 454 454 454 PRO PRO B . n 
B 1 455 GLY 455 455 455 GLY GLY B . n 
B 1 456 ALA 456 456 456 ALA ALA B . n 
B 1 457 PHE 457 457 457 PHE PHE B . n 
B 1 458 SER 458 458 458 SER SER B . n 
B 1 459 ALA 459 459 459 ALA ALA B . n 
B 1 460 TYR 460 460 460 TYR TYR B . n 
B 1 461 ARG 461 461 461 ARG ARG B . n 
B 1 462 TYR 462 462 462 TYR TYR B . n 
B 1 463 GLU 463 463 463 GLU GLU B . n 
B 1 464 ALA 464 464 464 ALA ALA B . n 
B 1 465 ILE 465 465 465 ILE ILE B . n 
B 1 466 ARG 466 466 466 ARG ARG B . n 
B 1 467 GLY 467 467 467 GLY GLY B . n 
B 1 468 ALA 468 468 468 ALA ALA B . n 
B 1 469 PRO 469 469 469 PRO PRO 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 ALA 472 472 472 ALA ALA B . n 
B 1 473 TYR 473 473 473 TYR TYR B . n 
B 1 474 PHE 474 474 474 PHE PHE B . n 
B 1 475 GLN 475 475 475 GLN GLN B . n 
B 1 476 THR 476 476 476 THR THR B . n 
B 1 477 LEU 477 477 477 LEU LEU B . n 
B 1 478 ASN 478 478 478 ASN ASN B . n 
B 1 479 ILE 479 479 479 ILE ILE B . n 
B 1 480 GLU 480 480 480 GLU GLU B . n 
B 1 481 LEU 481 481 481 LEU LEU B . n 
B 1 482 ASP 482 482 482 ASP ASP B . n 
B 1 483 VAL 483 483 483 VAL VAL B . n 
B 1 484 LEU 484 484 484 LEU LEU B . n 
B 1 485 GLY 485 485 485 GLY GLY B . n 
B 1 486 PRO 486 486 486 PRO PRO B . n 
B 1 487 PHE 487 487 487 PHE PHE B . n 
B 1 488 ILE 488 488 488 ILE ILE B . n 
B 1 489 GLY 489 489 489 GLY GLY B . n 
B 1 490 ASN 490 490 490 ASN ASN B . n 
B 1 491 MET 491 491 491 MET MET B . n 
B 1 492 TYR 492 492 492 TYR TYR B . n 
B 1 493 LEU 493 493 493 LEU LEU B . n 
B 1 494 ALA 494 494 494 ALA ALA B . n 
B 1 495 GLU 495 495 495 GLU ALA B . n 
B 1 496 ASP 496 496 496 ASP ASP B . n 
B 1 497 ARG 497 497 497 ARG ARG B . n 
B 1 498 ILE 498 498 498 ILE ILE B . n 
B 1 499 LEU 499 499 499 LEU LEU B . n 
B 1 500 SER 500 500 500 SER SER B . n 
B 1 501 PHE 501 501 501 PHE PHE B . n 
B 1 502 GLU 502 502 502 GLU GLU B . n 
B 1 503 VAL 503 503 503 VAL VAL B . n 
B 1 504 VAL 504 504 504 VAL VAL B . n 
B 1 505 ALA 505 505 505 ALA ALA B . n 
B 1 506 ARG 506 506 506 ARG ARG B . n 
B 1 507 LYS 507 507 507 LYS LYS B . n 
B 1 508 ASN 508 508 508 ASN ASN B . n 
B 1 509 CYS 509 509 509 CYS CYS B . n 
B 1 510 ASN 510 510 510 ASN ASN B . n 
B 1 511 TRP 511 511 511 TRP TRP B . n 
B 1 512 THR 512 512 512 THR THR B . n 
B 1 513 MET 513 513 513 MET MET B . n 
B 1 514 HIS 514 514 514 HIS HIS B . n 
B 1 515 TYR 515 515 515 TYR TYR B . n 
B 1 516 VAL 516 516 516 VAL VAL B . n 
B 1 517 LYS 517 517 517 LYS LYS B . n 
B 1 518 ASP 518 518 518 ASP ASP B . n 
B 1 519 ALA 519 519 519 ALA ALA B . n 
B 1 520 VAL 520 520 520 VAL VAL B . n 
B 1 521 ALA 521 521 521 ALA ALA B . n 
B 1 522 ARG 522 522 522 ARG ARG B . n 
B 1 523 THR 523 523 523 THR THR B . n 
B 1 524 ASP 524 524 524 ASP ASP B . n 
B 1 525 VAL 525 525 525 VAL VAL B . n 
B 1 526 PRO 526 526 526 PRO PRO B . n 
B 1 527 HIS 527 527 527 HIS HIS B . n 
B 1 528 ASP 528 528 528 ASP ASP B . n 
B 1 529 LEU 529 529 529 LEU LEU B . n 
B 1 530 VAL 530 530 530 VAL VAL B . n 
B 1 531 GLY 531 531 531 GLY GLY B . n 
B 1 532 LEU 532 532 532 LEU LEU B . n 
B 1 533 ILE 533 533 533 ILE ILE B . n 
B 1 534 SER 534 534 534 SER SER B . n 
B 1 535 GLN 535 535 535 GLN GLN B . n 
B 1 536 ARG 536 536 536 ARG ARG B . n 
B 1 537 LYS 537 537 537 LYS LYS B . n 
B 1 538 ARG 538 538 538 ARG ARG B . n 
B 1 539 TRP 539 539 539 TRP TRP B . n 
B 1 540 LEU 540 540 540 LEU LEU B . n 
B 1 541 ASN 541 541 541 ASN ASN B . n 
B 1 542 GLY 542 542 542 GLY GLY B . n 
B 1 543 ALA 543 543 543 ALA ALA B . n 
B 1 544 PHE 544 544 544 PHE PHE B . n 
B 1 545 PHE 545 545 545 PHE PHE B . n 
B 1 546 ALA 546 546 546 ALA ALA B . n 
B 1 547 THR 547 547 547 THR THR B . n 
B 1 548 LEU 548 548 548 LEU LEU B . n 
B 1 549 PHE 549 549 549 PHE PHE B . n 
B 1 550 SER 550 550 550 SER SER B . n 
B 1 551 ILE 551 551 551 ILE ILE B . n 
B 1 552 TRP 552 552 552 TRP TRP B . n 
B 1 553 ASN 553 553 553 ASN ASN B . n 
B 1 554 TRP 554 554 554 TRP TRP B . n 
B 1 555 GLY 555 555 555 GLY GLY B . n 
B 1 556 ARG 556 556 556 ARG ARG B . n 
B 1 557 ILE 557 557 557 ILE ILE B . n 
B 1 558 TYR 558 558 558 TYR TYR B . n 
B 1 559 SER 559 559 559 SER SER B . n 
B 1 560 GLU 560 560 560 GLU GLU B . n 
B 1 561 SER 561 561 561 SER SER B . n 
B 1 562 LYS 562 562 562 LYS LYS B . n 
B 1 563 HIS 563 563 563 HIS HIS B . n 
B 1 564 THR 564 564 564 THR THR B . n 
B 1 565 PHE 565 565 565 PHE PHE B . n 
B 1 566 VAL 566 566 566 VAL VAL B . n 
B 1 567 ARG 567 567 567 ARG ARG B . n 
B 1 568 LYS 568 568 568 LYS LYS B . n 
B 1 569 MET 569 569 569 MET MET B . n 
B 1 570 ALA 570 570 570 ALA ALA B . n 
B 1 571 PHE 571 571 571 PHE PHE B . n 
B 1 572 LEU 572 572 572 LEU LEU B . n 
B 1 573 VAL 573 573 573 VAL VAL B . n 
B 1 574 PHE 574 574 574 PHE PHE B . n 
B 1 575 TYR 575 575 575 TYR TYR B . n 
B 1 576 VAL 576 576 576 VAL VAL B . n 
B 1 577 TYR 577 577 577 TYR TYR B . n 
B 1 578 HIS 578 578 578 HIS HIS B . n 
B 1 579 LEU 579 579 579 LEU LEU B . n 
B 1 580 LEU 580 580 580 LEU LEU B . n 
B 1 581 TYR 581 581 581 TYR TYR B . n 
B 1 582 THR 582 582 582 THR THR B . n 
B 1 583 ALA 583 583 583 ALA ALA B . n 
B 1 584 PHE 584 584 584 PHE PHE B . n 
B 1 585 GLY 585 585 585 GLY GLY B . n 
B 1 586 PHE 586 586 586 PHE PHE B . n 
B 1 587 PHE 587 587 587 PHE PHE B . n 
B 1 588 LEU 588 588 588 LEU LEU B . n 
B 1 589 PRO 589 589 589 PRO PRO B . n 
B 1 590 ALA 590 590 590 ALA ALA B . n 
B 1 591 ASN 591 591 591 ASN ASN B . n 
B 1 592 LEU 592 592 592 LEU LEU B . n 
B 1 593 TYR 593 593 593 TYR TYR B . n 
B 1 594 LEU 594 594 594 LEU LEU B . n 
B 1 595 ALA 595 595 595 ALA ALA B . n 
B 1 596 LEU 596 596 596 LEU LEU B . n 
B 1 597 PHE 597 597 597 PHE PHE B . n 
B 1 598 PHE 598 598 598 PHE PHE B . n 
B 1 599 ILE 599 599 599 ILE ILE B . n 
B 1 600 VAL 600 600 600 VAL VAL B . n 
B 1 601 PHE 601 601 601 PHE PHE B . n 
B 1 602 GLN 602 602 602 GLN GLN B . n 
B 1 603 GLY 603 603 603 GLY GLY B . n 
B 1 604 PHE 604 604 604 PHE PHE B . n 
B 1 605 GLN 605 605 605 GLN GLN B . n 
B 1 606 GLN 606 606 606 GLN GLN B . n 
B 1 607 ASN 607 607 607 ASN ASN B . n 
B 1 608 ARG 608 608 608 ARG ARG B . n 
B 1 609 LEU 609 609 609 LEU LEU B . n 
B 1 610 GLU 610 610 610 GLU GLU B . n 
B 1 611 PHE 611 611 611 PHE PHE B . n 
B 1 612 ILE 612 612 612 ILE ILE B . n 
B 1 613 ASP 613 613 613 ASP ASP B . n 
B 1 614 THR 614 614 614 THR THR B . n 
B 1 615 SER 615 615 615 SER SER B . n 
B 1 616 GLU 616 616 616 GLU GLU B . n 
B 1 617 TYR 617 617 617 TYR TYR B . n 
B 1 618 SER 618 618 618 SER SER B . n 
B 1 619 GLN 619 619 619 GLN GLN B . n 
B 1 620 THR 620 620 620 THR THR B . n 
B 1 621 VAL 621 621 621 VAL VAL B . n 
B 1 622 LEU 622 622 622 LEU LEU B . n 
B 1 623 ASP 623 623 623 ASP ASP B . n 
B 1 624 CYS 624 624 624 CYS CYS B . n 
B 1 625 ALA 625 625 625 ALA ALA B . n 
B 1 626 VAL 626 626 626 VAL VAL B . n 
B 1 627 TYR 627 627 627 TYR TYR B . n 
B 1 628 ILE 628 628 628 ILE ILE B . n 
B 1 629 TYR 629 629 629 TYR TYR B . n 
B 1 630 ASN 630 630 630 ASN ASN B . n 
B 1 631 PHE 631 631 631 PHE PHE B . n 
B 1 632 SER 632 632 632 SER SER B . n 
B 1 633 TYR 633 633 633 TYR TYR B . n 
B 1 634 LEU 634 634 634 LEU LEU B . n 
B 1 635 PHE 635 635 635 PHE PHE B . n 
B 1 636 GLY 636 636 636 GLY GLY B . n 
B 1 637 LEU 637 637 637 LEU LEU B . n 
B 1 638 LEU 638 638 638 LEU LEU B . n 
B 1 639 MET 639 639 639 MET MET B . n 
B 1 640 LEU 640 640 640 LEU LEU B . n 
B 1 641 ILE 641 641 641 ILE ILE B . n 
B 1 642 ILE 642 642 642 ILE ILE B . n 
B 1 643 ILE 643 643 643 ILE ILE B . n 
B 1 644 GLY 644 644 644 GLY GLY B . n 
B 1 645 LEU 645 645 645 LEU LEU B . n 
B 1 646 GLY 646 646 646 GLY GLY B . n 
B 1 647 ASN 647 647 647 ASN ASN B . n 
B 1 648 ASN 648 648 648 ASN ASN B . n 
B 1 649 PRO 649 649 649 PRO PRO B . n 
B 1 650 LYS 650 650 650 LYS LYS B . n 
B 1 651 HIS 651 651 651 HIS HIS B . n 
B 1 652 MET 652 652 652 MET MET B . n 
B 1 653 LYS 653 653 653 LYS LYS B . n 
B 1 654 LEU 654 654 654 LEU LEU B . n 
B 1 655 THR 655 655 655 THR THR B . n 
B 1 656 TYR 656 656 656 TYR TYR B . n 
B 1 657 TYR 657 657 657 TYR TYR B . n 
B 1 658 PHE 658 658 658 PHE PHE B . n 
B 1 659 VAL 659 659 659 VAL VAL B . n 
B 1 660 GLY 660 660 660 GLY GLY B . n 
B 1 661 ALA 661 661 661 ALA ALA B . n 
B 1 662 VAL 662 662 662 VAL VAL B . n 
B 1 663 PHE 663 663 663 PHE PHE B . n 
B 1 664 GLY 664 664 664 GLY GLY B . n 
B 1 665 LEU 665 665 665 LEU LEU B . n 
B 1 666 MET 666 666 666 MET MET B . n 
B 1 667 MET 667 667 667 MET MET B . n 
B 1 668 MET 668 668 668 MET MET B . n 
B 1 669 LEU 669 669 669 LEU LEU B . n 
B 1 670 SER 670 670 670 SER SER B . n 
B 1 671 SER 671 671 671 SER SER B . n 
B 1 672 LEU 672 672 672 LEU LEU B . n 
B 1 673 VAL 673 673 673 VAL VAL B . n 
B 1 674 GLY 674 674 674 GLY GLY B . n 
B 1 675 ALA 675 675 675 ALA ALA B . n 
B 1 676 GLY 676 676 676 GLY GLY B . n 
B 1 677 ILE 677 677 677 ILE ILE B . n 
B 1 678 PHE 678 678 678 PHE PHE B . n 
B 1 679 PHE 679 679 679 PHE PHE B . n 
B 1 680 SER 680 680 680 SER SER B . n 
B 1 681 THR 681 681 681 THR THR B . n 
B 1 682 PRO 682 682 682 PRO PRO B . n 
B 1 683 ALA 683 683 683 ALA ALA B . n 
B 1 684 THR 684 684 684 THR THR B . n 
B 1 685 VAL 685 685 685 VAL VAL B . n 
B 1 686 HIS 686 686 686 HIS HIS B . n 
B 1 687 SER 687 687 687 SER SER B . n 
B 1 688 ILE 688 688 688 ILE ILE B . n 
B 1 689 VAL 689 689 689 VAL VAL B . n 
B 1 690 VAL 690 690 690 VAL VAL B . n 
B 1 691 SER 691 691 691 SER SER B . n 
B 1 692 ILE 692 692 692 ILE ILE B . n 
B 1 693 LEU 693 693 693 LEU LEU B . n 
B 1 694 THR 694 694 694 THR THR B . n 
B 1 695 VAL 695 695 695 VAL VAL B . n 
B 1 696 GLY 696 696 696 GLY GLY B . n 
B 1 697 VAL 697 697 697 VAL VAL B . n 
B 1 698 TYR 698 698 698 TYR TYR B . n 
B 1 699 PHE 699 699 699 PHE PHE B . n 
B 1 700 ILE 700 700 700 ILE ILE B . n 
B 1 701 ALA 701 701 701 ALA ALA B . n 
B 1 702 SER 702 702 702 SER SER B . n 
B 1 703 ALA 703 703 703 ALA ALA B . n 
B 1 704 LEU 704 704 704 LEU LEU B . n 
B 1 705 HIS 705 705 705 HIS HIS B . n 
B 1 706 GLY 706 706 706 GLY GLY B . n 
B 1 707 GLU 707 707 707 GLU GLU B . n 
B 1 708 VAL 708 708 708 VAL VAL B . n 
B 1 709 HIS 709 709 709 HIS HIS B . n 
B 1 710 HIS 710 710 710 HIS HIS B . n 
B 1 711 ILE 711 711 711 ILE ILE B . n 
B 1 712 PHE 712 712 712 PHE PHE B . n 
B 1 713 MET 713 713 713 MET MET B . n 
B 1 714 THR 714 714 714 THR THR B . n 
B 1 715 PHE 715 715 715 PHE PHE B . n 
B 1 716 THR 716 716 716 THR THR B . n 
B 1 717 HIS 717 717 717 HIS HIS B . n 
B 1 718 TYR 718 718 718 TYR TYR B . n 
B 1 719 THR 719 719 719 THR THR B . n 
B 1 720 ALA 720 720 720 ALA ALA B . n 
B 1 721 LEU 721 721 721 LEU LEU B . n 
B 1 722 ILE 722 722 722 ILE ILE B . n 
B 1 723 PRO 723 723 723 PRO PRO B . n 
B 1 724 SER 724 724 724 SER SER B . n 
B 1 725 PHE 725 725 725 PHE PHE B . n 
B 1 726 VAL 726 726 726 VAL VAL B . n 
B 1 727 ASN 727 727 727 ASN ASN B . n 
B 1 728 ILE 728 728 728 ILE ILE B . n 
B 1 729 PHE 729 729 729 PHE PHE B . n 
B 1 730 THR 730 730 730 THR THR B . n 
B 1 731 ILE 731 731 731 ILE ILE B . n 
B 1 732 TYR 732 732 732 TYR TYR B . n 
B 1 733 SER 733 733 733 SER SER B . n 
B 1 734 PHE 734 734 734 PHE PHE B . n 
B 1 735 CYS 735 735 735 CYS CYS B . n 
B 1 736 ASN 736 736 736 ASN ASN B . n 
B 1 737 LEU 737 737 737 LEU LEU B . n 
B 1 738 GLN 738 738 738 GLN GLN B . n 
B 1 739 ASP 739 739 739 ASP ASP B . n 
B 1 740 LEU 740 740 740 LEU LEU B . n 
B 1 741 SER 741 741 741 SER SER B . n 
B 1 742 TRP 742 742 ?   ?   ?   B . n 
B 1 743 GLY 743 743 ?   ?   ?   B . n 
B 1 744 THR 744 744 ?   ?   ?   B . n 
B 1 745 LYS 745 745 ?   ?   ?   B . n 
B 1 746 GLY 746 746 ?   ?   ?   B . n 
B 1 747 LEU 747 747 ?   ?   ?   B . n 
B 1 748 HIS 748 748 ?   ?   ?   B . n 
B 1 749 ASP 749 749 ?   ?   ?   B . n 
B 1 750 ASP 750 750 ?   ?   ?   B . n 
B 1 751 PRO 751 751 ?   ?   ?   B . n 
B 1 752 LEU 752 752 ?   ?   ?   B . n 
B 1 753 LEU 753 753 ?   ?   ?   B . n 
B 1 754 ALA 754 754 ?   ?   ?   B . n 
B 1 755 ALA 755 755 ?   ?   ?   B . n 
B 1 756 SER 756 756 ?   ?   ?   B . n 
B 1 757 LEU 757 757 ?   ?   ?   B . n 
B 1 758 ASP 758 758 ?   ?   ?   B . n 
B 1 759 GLU 759 759 ?   ?   ?   B . n 
B 1 760 THR 760 760 ?   ?   ?   B . n 
B 1 761 GLU 761 761 ?   ?   ?   B . n 
B 1 762 LYS 762 762 762 LYS LYS B . n 
B 1 763 GLY 763 763 763 GLY GLY B . n 
B 1 764 ASP 764 764 764 ASP ASP B . n 
B 1 765 PHE 765 765 765 PHE PHE B . n 
B 1 766 LYS 766 766 766 LYS LYS B . n 
B 1 767 ASP 767 767 767 ASP ASP B . n 
B 1 768 VAL 768 768 768 VAL VAL B . n 
B 1 769 ILE 769 769 769 ILE ILE B . n 
B 1 770 ALA 770 770 770 ALA ALA B . n 
B 1 771 LYS 771 771 771 LYS LYS B . n 
B 1 772 ARG 772 772 772 ARG ARG B . n 
B 1 773 ARG 773 773 773 ARG ARG B . n 
B 1 774 ALA 774 774 774 ALA ALA B . n 
B 1 775 LEU 775 775 775 LEU LEU B . n 
B 1 776 GLU 776 776 776 GLU GLU B . n 
B 1 777 GLU 777 777 777 GLU GLU B . n 
B 1 778 LEU 778 778 778 LEU LEU B . n 
B 1 779 ARG 779 779 779 ARG ARG B . n 
B 1 780 ARG 780 780 780 ARG ARG B . n 
B 1 781 GLU 781 781 781 GLU GLU B . n 
B 1 782 GLU 782 782 782 GLU GLU B . n 
B 1 783 LYS 783 783 783 LYS LYS B . n 
B 1 784 GLU 784 784 784 GLU GLU B . n 
B 1 785 ARG 785 785 785 ARG ARG B . n 
B 1 786 VAL 786 786 786 VAL VAL B . n 
B 1 787 GLU 787 787 787 GLU GLU B . n 
B 1 788 ASN 788 788 788 ASN ASN B . n 
B 1 789 ARG 789 789 789 ARG ARG B . n 
B 1 790 LYS 790 790 790 LYS LYS B . n 
B 1 791 LYS 791 791 791 LYS LYS B . n 
B 1 792 ASN 792 792 792 ASN ASN B . n 
B 1 793 PHE 793 793 793 PHE PHE B . n 
B 1 794 GLU 794 794 794 GLU GLU B . n 
B 1 795 ALA 795 795 795 ALA ALA B . n 
B 1 796 PHE 796 796 796 PHE PHE B . n 
B 1 797 ARG 797 797 797 ARG ARG B . n 
B 1 798 THR 798 798 798 THR THR B . n 
B 1 799 ASN 799 799 799 ASN ASN B . n 
B 1 800 VAL 800 800 800 VAL VAL B . n 
B 1 801 LEU 801 801 801 LEU LEU B . n 
B 1 802 LEU 802 802 802 LEU LEU B . n 
B 1 803 THR 803 803 803 THR THR B . n 
B 1 804 TRP 804 804 804 TRP TRP B . n 
B 1 805 ALA 805 805 805 ALA ALA B . n 
B 1 806 PHE 806 806 806 PHE PHE B . n 
B 1 807 SER 807 807 807 SER SER B . n 
B 1 808 ASN 808 808 808 ASN ASN B . n 
B 1 809 LEU 809 809 809 LEU LEU B . n 
B 1 810 ILE 810 810 810 ILE ILE B . n 
B 1 811 PHE 811 811 811 PHE PHE B . n 
B 1 812 ALA 812 812 812 ALA ALA B . n 
B 1 813 LEU 813 813 813 LEU LEU B . n 
B 1 814 PHE 814 814 814 PHE PHE B . n 
B 1 815 VAL 815 815 815 VAL VAL B . n 
B 1 816 VAL 816 816 816 VAL VAL B . n 
B 1 817 TYR 817 817 817 TYR TYR B . n 
B 1 818 PHE 818 818 818 PHE PHE B . n 
B 1 819 ALA 819 819 819 ALA ALA B . n 
B 1 820 SER 820 820 820 SER SER B . n 
B 1 821 SER 821 821 821 SER SER B . n 
B 1 822 SER 822 822 822 SER SER B . n 
B 1 823 THR 823 823 823 THR THR B . n 
B 1 824 TYR 824 824 824 TYR TYR B . n 
B 1 825 MET 825 825 825 MET MET B . n 
B 1 826 PRO 826 826 826 PRO PRO B . n 
B 1 827 VAL 827 827 827 VAL VAL B . n 
B 1 828 LEU 828 828 828 LEU LEU B . n 
B 1 829 TYR 829 829 829 TYR TYR B . n 
B 1 830 ILE 830 830 830 ILE ILE B . n 
B 1 831 PHE 831 831 831 PHE PHE B . n 
B 1 832 VAL 832 832 832 VAL VAL B . n 
B 1 833 ALA 833 833 833 ALA ALA B . n 
B 1 834 SER 834 834 834 SER SER B . n 
B 1 835 LEU 835 835 835 LEU LEU B . n 
B 1 836 ASN 836 836 836 ASN ASN B . n 
B 1 837 THR 837 837 837 THR THR B . n 
B 1 838 CYS 838 838 838 CYS CYS B . n 
B 1 839 ARG 839 839 839 ARG ARG B . n 
B 1 840 LEU 840 840 840 LEU LEU B . n 
B 1 841 LEU 841 841 841 LEU LEU B . n 
B 1 842 GLY 842 842 842 GLY GLY B . n 
B 1 843 SER 843 843 843 SER SER B . n 
B 1 844 ILE 844 844 844 ILE ILE B . n 
B 1 845 GLY 845 845 845 GLY GLY B . n 
B 1 846 HIS 846 846 846 HIS HIS B . n 
B 1 847 TRP 847 847 847 TRP TRP B . n 
B 1 848 VAL 848 848 848 VAL VAL B . n 
B 1 849 TYR 849 849 849 TYR TYR B . n 
B 1 850 ILE 850 850 850 ILE ILE B . n 
B 1 851 HIS 851 851 851 HIS HIS B . n 
B 1 852 THR 852 852 852 THR THR B . n 
B 1 853 GLU 853 853 853 GLU GLU B . n 
B 1 854 GLY 854 854 854 GLY GLY B . n 
B 1 855 LEU 855 855 855 LEU LEU B . n 
B 1 856 ARG 856 856 856 ARG ARG B . n 
B 1 857 GLY 857 857 857 GLY GLY B . n 
B 1 858 ARG 858 858 858 ARG ARG B . n 
B 1 859 VAL 859 859 859 VAL VAL B . n 
B 1 860 ILE 860 860 ?   ?   ?   B . n 
B 1 861 ASP 861 861 ?   ?   ?   B . n 
B 1 862 LYS 862 862 ?   ?   ?   B . n 
B 1 863 SER 863 863 ?   ?   ?   B . n 
B 1 864 GLU 864 864 ?   ?   ?   B . n 
B 1 865 CYS 865 865 ?   ?   ?   B . n 
B 1 866 GLY 866 866 ?   ?   ?   B . n 
B 1 867 ASN 867 867 ?   ?   ?   B . n 
B 1 868 GLY 868 868 ?   ?   ?   B . n 
B 1 869 THR 869 869 ?   ?   ?   B . n 
B 1 870 GLY 870 870 ?   ?   ?   B . n 
B 1 871 ARG 871 871 ?   ?   ?   B . n 
B 1 872 TYR 872 872 ?   ?   ?   B . n 
B 1 873 PRO 873 873 ?   ?   ?   B . n 
B 1 874 GLN 874 874 ?   ?   ?   B . n 
B 1 875 ASN 875 875 ?   ?   ?   B . n 
B 1 876 SER 876 876 ?   ?   ?   B . n 
B 1 877 TYR 877 877 ?   ?   ?   B . n 
B 1 878 VAL 878 878 ?   ?   ?   B . n 
B 1 879 GLN 879 879 ?   ?   ?   B . n 
B 1 880 LEU 880 880 ?   ?   ?   B . n 
B 1 881 GLU 881 881 ?   ?   ?   B . n 
B 1 882 GLU 882 882 ?   ?   ?   B . n 
B 1 883 HIS 883 883 ?   ?   ?   B . n 
B 1 884 TYR 884 884 ?   ?   ?   B . n 
B 1 885 ALA 885 885 ?   ?   ?   B . n 
B 1 886 ALA 886 886 ?   ?   ?   B . n 
B 1 887 LEU 887 887 ?   ?   ?   B . n 
B 1 888 ALA 888 888 ?   ?   ?   B . n 
B 1 889 GLU 889 889 ?   ?   ?   B . n 
B 1 890 ASP 890 890 ?   ?   ?   B . n 
B 1 891 GLN 891 891 ?   ?   ?   B . n 
B 1 892 ARG 892 892 ?   ?   ?   B . n 
B 1 893 THR 893 893 ?   ?   ?   B . n 
B 1 894 TYR 894 894 ?   ?   ?   B . n 
B 1 895 ALA 895 895 ?   ?   ?   B . n 
B 1 896 SER 896 896 ?   ?   ?   B . n 
B 1 897 GLY 897 897 ?   ?   ?   B . n 
B 1 898 ARG 898 898 ?   ?   ?   B . n 
B 1 899 THR 899 899 ?   ?   ?   B . n 
B 1 900 ASN 900 900 ?   ?   ?   B . n 
B 1 901 ALA 901 901 ?   ?   ?   B . n 
B 1 902 SER 902 902 ?   ?   ?   B . n 
B 1 903 VAL 903 903 ?   ?   ?   B . n 
B 1 904 ARG 904 904 ?   ?   ?   B . n 
B 1 905 THR 905 905 ?   ?   ?   B . n 
B 1 906 VAL 906 906 ?   ?   ?   B . n 
B 1 907 ASN 907 907 ?   ?   ?   B . n 
B 1 908 ASP 908 908 ?   ?   ?   B . n 
B 1 909 VAL 909 909 ?   ?   ?   B . n 
B 1 910 SER 910 910 ?   ?   ?   B . n 
B 1 911 SER 911 911 ?   ?   ?   B . n 
B 1 912 ALA 912 912 ?   ?   ?   B . n 
B 1 913 ALA 913 913 ?   ?   ?   B . n 
B 1 914 LEU 914 914 ?   ?   ?   B . n 
B 1 915 VAL 915 915 ?   ?   ?   B . n 
B 1 916 PRO 916 916 ?   ?   ?   B . n 
B 1 917 ARG 917 917 ?   ?   ?   B . n 
B 1 918 GLY 918 918 ?   ?   ?   B . n 
B 1 919 SER 919 919 ?   ?   ?   B . n 
B 1 920 HIS 920 920 ?   ?   ?   B . n 
B 1 921 HIS 921 921 ?   ?   ?   B . n 
B 1 922 HIS 922 922 ?   ?   ?   B . n 
B 1 923 HIS 923 923 ?   ?   ?   B . n 
B 1 924 HIS 924 924 ?   ?   ?   B . n 
B 1 925 HIS 925 925 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 UDP 1 1001 1001 UDP UD1 A . 
D 3 MN  1 1002 1002 MN  MN  A . 
E 2 UDP 1 1001 1001 UDP UD1 B . 
F 3 MN  1 1002 1002 MN  MN  B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU 495 ? CG  ? A GLU 495 CG  
2  1 Y 1 A GLU 495 ? CD  ? A GLU 495 CD  
3  1 Y 1 A GLU 495 ? OE1 ? A GLU 495 OE1 
4  1 Y 1 A GLU 495 ? OE2 ? A GLU 495 OE2 
5  1 Y 1 B GLU 495 ? CG  ? B GLU 495 CG  
6  1 Y 1 B GLU 495 ? CD  ? B GLU 495 CD  
7  1 Y 1 B GLU 495 ? OE1 ? B GLU 495 OE1 
8  1 Y 1 B GLU 495 ? OE2 ? B GLU 495 OE2 
9  1 Y 1 B LYS 650 ? CD  ? B LYS 650 CD  
10 1 Y 1 B LYS 650 ? CE  ? B LYS 650 CE  
11 1 Y 1 B LYS 650 ? NZ  ? B LYS 650 NZ  
# 
_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                     8Z0O 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_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                         8Z0O 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8Z0O 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8Z0O 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_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                            . 
_refine.ls_d_res_low                             ? 
_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                     ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
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 
'ELECTRON MICROSCOPY' ? 0.004 ? 13404 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.608 ? 18206 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 6.372 ? 1888  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.040 ? 2002  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.005 ? 2292  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     8Z0O 
_struct.title                        'Cryo-EM structure of chitin synthase' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8Z0O 
_struct_keywords.text            'chitin synthase, membrane-integrated glycosyltransferase, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    G4Z2L3_PHYSP 
_struct_ref.pdbx_db_accession          G4Z2L3 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSGAPPPSSGFAPRSYGQQPLSHAPRSSMMSVEYDGIPLPPPSIRSCGSQQYVTSYIPTGAAFPPSSVQDMISSMKSYAS
ATDLVRTYSEIPSVEEALSTLDRAAAALNARRYRDALKLYLEGGYAMANVAERQANPKICNLLTSKGFETLNWCARLCDW
IEGRIKEKHPRPGVHKVGIPVSNWDEDWVGPFMDEEEARRMWYTPVYCPHPIDFSNLGYRLRCVETGRRPRLMICITMYN
EGPQQLKATLKKLANNLAYLKEQMPGDEKSLTGAFAGDDVWQNVLVCIVADGREQVHPKTLDYLEAIGLYDEDLLTINSA
GIGAQCHLFEHTLQLSVNGKCLLPIQTVFALKENKASKLDSHHWYFNAFAEQIQPEYTAVMDVGTMLTKSALYHLLFAFE
RNHQIGGACGQLTVDNPFENLSNWVISAQHFEYKISNILDKSLESCFGFISVLPGAFSAYRYEAIRGAPLDAYFQTLNIE
LDVLGPFIGNMYLAEDRILSFEVVARKNCNWTMHYVKDAVARTDVPHDLVGLISQRKRWLNGAFFATLFSIWNWGRIYSE
SKHTFVRKMAFLVFYVYHLLYTAFGFFLPANLYLALFFIVFQGFQQNRLEFIDTSEYSQTVLDCAVYIYNFSYLFGLLML
IIIGLGNNPKHMKLTYYFVGAVFGLMMMLSSLVGAGIFFSTPATVHSIVVSILTVGVYFIASALHGEVHHIFMTFTHYTA
LIPSFVNIFTIYSFCNLQDLSWGTKGLHDDPLLAASLDETEKGDFKDVIAKRRALEELRREEKERVENRKKNFEAFRTNV
LLTWAFSNLIFALFVVYFASSSTYMPVLYIFVASLNTCRLLGSIGHWVYIHTEGLRGRVIDKSECGNGTGRYPQNSYVQL
EEHYAALAEDQRTYASGRTNASVRTVNDVSSAA
;
_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 8Z0O A 1 ? 913 ? G4Z2L3 1 ? 913 ? 1 913 
2 1 8Z0O B 1 ? 913 ? G4Z2L3 1 ? 913 ? 1 913 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8Z0O LEU A 914 ? UNP G4Z2L3 ? ? 'expression tag' 914 1  
1 8Z0O VAL A 915 ? UNP G4Z2L3 ? ? 'expression tag' 915 2  
1 8Z0O PRO A 916 ? UNP G4Z2L3 ? ? 'expression tag' 916 3  
1 8Z0O ARG A 917 ? UNP G4Z2L3 ? ? 'expression tag' 917 4  
1 8Z0O GLY A 918 ? UNP G4Z2L3 ? ? 'expression tag' 918 5  
1 8Z0O SER A 919 ? UNP G4Z2L3 ? ? 'expression tag' 919 6  
1 8Z0O HIS A 920 ? UNP G4Z2L3 ? ? 'expression tag' 920 7  
1 8Z0O HIS A 921 ? UNP G4Z2L3 ? ? 'expression tag' 921 8  
1 8Z0O HIS A 922 ? UNP G4Z2L3 ? ? 'expression tag' 922 9  
1 8Z0O HIS A 923 ? UNP G4Z2L3 ? ? 'expression tag' 923 10 
1 8Z0O HIS A 924 ? UNP G4Z2L3 ? ? 'expression tag' 924 11 
1 8Z0O HIS A 925 ? UNP G4Z2L3 ? ? 'expression tag' 925 12 
2 8Z0O LEU B 914 ? UNP G4Z2L3 ? ? 'expression tag' 914 13 
2 8Z0O VAL B 915 ? UNP G4Z2L3 ? ? 'expression tag' 915 14 
2 8Z0O PRO B 916 ? UNP G4Z2L3 ? ? 'expression tag' 916 15 
2 8Z0O ARG B 917 ? UNP G4Z2L3 ? ? 'expression tag' 917 16 
2 8Z0O GLY B 918 ? UNP G4Z2L3 ? ? 'expression tag' 918 17 
2 8Z0O SER B 919 ? UNP G4Z2L3 ? ? 'expression tag' 919 18 
2 8Z0O HIS B 920 ? UNP G4Z2L3 ? ? 'expression tag' 920 19 
2 8Z0O HIS B 921 ? UNP G4Z2L3 ? ? 'expression tag' 921 20 
2 8Z0O HIS B 922 ? UNP G4Z2L3 ? ? 'expression tag' 922 21 
2 8Z0O HIS B 923 ? UNP G4Z2L3 ? ? 'expression tag' 923 22 
2 8Z0O HIS B 924 ? UNP G4Z2L3 ? ? 'expression tag' 924 23 
2 8Z0O HIS B 925 ? UNP G4Z2L3 ? ? 'expression tag' 925 24 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_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   ? 
_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 HIS A 23  ? ILE A 37  ? HIS A 23  ILE A 37  1 ? 15 
HELX_P HELX_P2  AA2 SER A 93  ? ALA A 110 ? SER A 93  ALA A 110 1 ? 18 
HELX_P HELX_P3  AA3 ARG A 112 ? GLN A 134 ? ARG A 112 GLN A 134 1 ? 23 
HELX_P HELX_P4  AA4 ASN A 136 ? GLY A 147 ? ASN A 136 GLY A 147 1 ? 12 
HELX_P HELX_P5  AA5 THR A 150 ? ILE A 161 ? THR A 150 ILE A 161 1 ? 12 
HELX_P HELX_P6  AA6 ASP A 194 ? ARG A 199 ? ASP A 194 ARG A 199 1 ? 6  
HELX_P HELX_P7  AA7 HIS A 210 ? SER A 215 ? HIS A 210 SER A 215 5 ? 6  
HELX_P HELX_P8  AA8 LEU A 221 ? GLY A 227 ? LEU A 221 GLY A 227 1 ? 7  
HELX_P HELX_P9  AA9 GLY A 242 ? GLU A 262 ? GLY A 242 GLU A 262 1 ? 21 
HELX_P HELX_P10 AB1 ASP A 279 ? GLN A 282 ? ASP A 279 GLN A 282 5 ? 4  
HELX_P HELX_P11 AB2 HIS A 297 ? ILE A 307 ? HIS A 297 ILE A 307 1 ? 11 
HELX_P HELX_P12 AB3 ASP A 311 ? SER A 319 ? ASP A 311 SER A 319 1 ? 9  
HELX_P HELX_P13 AB4 SER A 357 ? GLN A 374 ? SER A 357 GLN A 374 1 ? 18 
HELX_P HELX_P14 AB5 SER A 390 ? HIS A 403 ? SER A 390 HIS A 403 1 ? 14 
HELX_P HELX_P15 AB6 ASN A 423 ? PHE A 447 ? ASN A 423 PHE A 447 1 ? 25 
HELX_P HELX_P16 AB7 GLY A 467 ? PHE A 474 ? GLY A 467 PHE A 474 1 ? 8  
HELX_P HELX_P17 AB8 PHE A 474 ? ILE A 479 ? PHE A 474 ILE A 479 1 ? 6  
HELX_P HELX_P18 AB9 GLU A 480 ? GLY A 485 ? GLU A 480 GLY A 485 1 ? 6  
HELX_P HELX_P19 AC1 ILE A 488 ? GLY A 489 ? ILE A 488 GLY A 489 5 ? 2  
HELX_P HELX_P20 AC2 MET A 491 ? ALA A 494 ? MET A 491 ALA A 494 5 ? 4  
HELX_P HELX_P21 AC3 GLU A 495 ? ALA A 505 ? GLU A 495 ALA A 505 1 ? 11 
HELX_P HELX_P22 AC4 ASP A 528 ? TRP A 554 ? ASP A 528 TRP A 554 1 ? 27 
HELX_P HELX_P23 AC5 GLY A 555 ? GLU A 560 ? GLY A 555 GLU A 560 1 ? 6  
HELX_P HELX_P24 AC6 THR A 564 ? PHE A 587 ? THR A 564 PHE A 587 1 ? 24 
HELX_P HELX_P25 AC7 PHE A 587 ? GLN A 605 ? PHE A 587 GLN A 605 1 ? 19 
HELX_P HELX_P26 AC8 THR A 620 ? GLY A 646 ? THR A 620 GLY A 646 1 ? 27 
HELX_P HELX_P27 AC9 MET A 652 ? THR A 681 ? MET A 652 THR A 681 1 ? 30 
HELX_P HELX_P28 AD1 THR A 684 ? GLY A 696 ? THR A 684 GLY A 696 1 ? 13 
HELX_P HELX_P29 AD2 GLY A 696 ? GLY A 706 ? GLY A 696 GLY A 706 1 ? 11 
HELX_P HELX_P30 AD3 VAL A 708 ? ALA A 720 ? VAL A 708 ALA A 720 1 ? 13 
HELX_P HELX_P31 AD4 LEU A 721 ? ASN A 736 ? LEU A 721 ASN A 736 1 ? 16 
HELX_P HELX_P32 AD5 ASP A 764 ? ALA A 819 ? ASP A 764 ALA A 819 1 ? 56 
HELX_P HELX_P33 AD6 SER A 820 ? GLU A 853 ? SER A 820 GLU A 853 1 ? 34 
HELX_P HELX_P34 AD7 GLY A 854 ? ARG A 858 ? GLY A 854 ARG A 858 5 ? 5  
HELX_P HELX_P35 AD8 ALA B 24  ? ILE B 37  ? ALA B 24  ILE B 37  1 ? 14 
HELX_P HELX_P36 AD9 SER B 93  ? ALA B 110 ? SER B 93  ALA B 110 1 ? 18 
HELX_P HELX_P37 AE1 ARG B 112 ? LEU B 121 ? ARG B 112 LEU B 121 1 ? 10 
HELX_P HELX_P38 AE2 ASN B 136 ? GLY B 163 ? ASN B 136 GLY B 163 1 ? 28 
HELX_P HELX_P39 AE3 ASP B 194 ? ARG B 199 ? ASP B 194 ARG B 199 1 ? 6  
HELX_P HELX_P40 AE4 HIS B 210 ? SER B 215 ? HIS B 210 SER B 215 5 ? 6  
HELX_P HELX_P41 AE5 LEU B 221 ? GLY B 227 ? LEU B 221 GLY B 227 1 ? 7  
HELX_P HELX_P42 AE6 GLY B 242 ? GLU B 262 ? GLY B 242 GLU B 262 1 ? 21 
HELX_P HELX_P43 AE7 ASP B 279 ? GLN B 282 ? ASP B 279 GLN B 282 5 ? 4  
HELX_P HELX_P44 AE8 HIS B 297 ? ILE B 307 ? HIS B 297 ILE B 307 1 ? 11 
HELX_P HELX_P45 AE9 ASP B 311 ? SER B 319 ? ASP B 311 SER B 319 1 ? 9  
HELX_P HELX_P46 AF1 SER B 357 ? GLN B 374 ? SER B 357 GLN B 374 1 ? 18 
HELX_P HELX_P47 AF2 SER B 390 ? HIS B 403 ? SER B 390 HIS B 403 1 ? 14 
HELX_P HELX_P48 AF3 ASN B 423 ? PHE B 447 ? ASN B 423 PHE B 447 1 ? 25 
HELX_P HELX_P49 AF4 GLY B 467 ? PHE B 474 ? GLY B 467 PHE B 474 1 ? 8  
HELX_P HELX_P50 AF5 PHE B 474 ? ILE B 479 ? PHE B 474 ILE B 479 1 ? 6  
HELX_P HELX_P51 AF6 GLU B 480 ? GLY B 485 ? GLU B 480 GLY B 485 1 ? 6  
HELX_P HELX_P52 AF7 GLY B 485 ? TYR B 492 ? GLY B 485 TYR B 492 1 ? 8  
HELX_P HELX_P53 AF8 GLU B 495 ? ALA B 505 ? GLU B 495 ALA B 505 1 ? 11 
HELX_P HELX_P54 AF9 ASP B 528 ? TRP B 554 ? ASP B 528 TRP B 554 1 ? 27 
HELX_P HELX_P55 AG1 TRP B 554 ? GLU B 560 ? TRP B 554 GLU B 560 1 ? 7  
HELX_P HELX_P56 AG2 THR B 564 ? PHE B 587 ? THR B 564 PHE B 587 1 ? 24 
HELX_P HELX_P57 AG3 PHE B 587 ? GLN B 605 ? PHE B 587 GLN B 605 1 ? 19 
HELX_P HELX_P58 AG4 GLN B 619 ? GLY B 646 ? GLN B 619 GLY B 646 1 ? 28 
HELX_P HELX_P59 AG5 MET B 652 ? THR B 681 ? MET B 652 THR B 681 1 ? 30 
HELX_P HELX_P60 AG6 THR B 684 ? VAL B 695 ? THR B 684 VAL B 695 1 ? 12 
HELX_P HELX_P61 AG7 GLY B 696 ? GLY B 706 ? GLY B 696 GLY B 706 1 ? 11 
HELX_P HELX_P62 AG8 VAL B 708 ? ALA B 720 ? VAL B 708 ALA B 720 1 ? 13 
HELX_P HELX_P63 AG9 LEU B 721 ? ASN B 736 ? LEU B 721 ASN B 736 1 ? 16 
HELX_P HELX_P64 AH1 ASP B 764 ? ALA B 819 ? ASP B 764 ALA B 819 1 ? 56 
HELX_P HELX_P65 AH2 SER B 820 ? GLU B 853 ? SER B 820 GLU B 853 1 ? 34 
HELX_P HELX_P66 AH3 GLY B 854 ? ARG B 858 ? GLY B 854 ARG B 858 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 ? ? C UDP . O2B ? ? ? 1_555 D MN . MN ? ? A UDP 1001 A MN 1002 1_555 ? ? ? ? ? ? ? 2.152 ? ? 
metalc2 metalc ? ? E UDP . O2A ? ? ? 1_555 F MN . MN ? ? B UDP 1001 B MN 1002 1_555 ? ? ? ? ? ? ? 2.552 ? ? 
metalc3 metalc ? ? E UDP . O2B ? ? ? 1_555 F MN . MN ? ? B UDP 1001 B MN 1002 1_555 ? ? ? ? ? ? ? 2.307 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_struct_conn_angle.id                    1 
_pdbx_struct_conn_angle.ptnr1_label_atom_id   O2A 
_pdbx_struct_conn_angle.ptnr1_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr1_label_asym_id   E 
_pdbx_struct_conn_angle.ptnr1_label_comp_id   UDP 
_pdbx_struct_conn_angle.ptnr1_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id    B 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id    UDP 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id     1001 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr1_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr2_label_atom_id   MN 
_pdbx_struct_conn_angle.ptnr2_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr2_label_asym_id   F 
_pdbx_struct_conn_angle.ptnr2_label_comp_id   MN 
_pdbx_struct_conn_angle.ptnr2_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id    B 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id    MN 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id     1002 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr2_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr3_label_atom_id   O2B 
_pdbx_struct_conn_angle.ptnr3_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr3_label_asym_id   E 
_pdbx_struct_conn_angle.ptnr3_label_comp_id   UDP 
_pdbx_struct_conn_angle.ptnr3_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id    B 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id    UDP 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id     1001 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr3_symmetry        1_555 
_pdbx_struct_conn_angle.value                 76.5 
_pdbx_struct_conn_angle.value_esd             ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 11 ? 
AA2 ? 2  ? 
AA3 ? 11 ? 
AA4 ? 2  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1  2  ? anti-parallel 
AA1 2  3  ? anti-parallel 
AA1 3  4  ? anti-parallel 
AA1 4  5  ? parallel      
AA1 5  6  ? parallel      
AA1 6  7  ? parallel      
AA1 7  8  ? anti-parallel 
AA1 8  9  ? anti-parallel 
AA1 9  10 ? parallel      
AA1 10 11 ? anti-parallel 
AA2 1  2  ? anti-parallel 
AA3 1  2  ? anti-parallel 
AA3 2  3  ? anti-parallel 
AA3 3  4  ? anti-parallel 
AA3 4  5  ? parallel      
AA3 5  6  ? parallel      
AA3 6  7  ? parallel      
AA3 7  8  ? anti-parallel 
AA3 8  9  ? anti-parallel 
AA3 9  10 ? parallel      
AA3 10 11 ? anti-parallel 
AA4 1  2  ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  VAL A 177 ? PRO A 180 ? VAL A 177 PRO A 180 
AA1 2  ARG A 200 ? VAL A 206 ? ARG A 200 VAL A 206 
AA1 3  CYS A 326 ? LEU A 333 ? CYS A 326 LEU A 333 
AA1 4  ILE A 345 ? LYS A 352 ? ILE A 345 LYS A 352 
AA1 5  VAL A 284 ? ALA A 290 ? VAL A 284 ALA A 290 
AA1 6  LEU A 232 ? MET A 238 ? LEU A 232 MET A 238 
AA1 7  TYR A 377 ? ASP A 382 ? TYR A 377 ASP A 382 
AA1 8  SER A 458 ? ARG A 461 ? SER A 458 ARG A 461 
AA1 9  ILE A 405 ? VAL A 414 ? ILE A 405 VAL A 414 
AA1 10 THR A 512 ? THR A 523 ? THR A 512 THR A 523 
AA1 11 MET A 386 ? LEU A 387 ? MET A 386 LEU A 387 
AA2 1  SER A 336 ? VAL A 337 ? SER A 336 VAL A 337 
AA2 2  LYS A 340 ? CYS A 341 ? LYS A 340 CYS A 341 
AA3 1  VAL B 177 ? PRO B 180 ? VAL B 177 PRO B 180 
AA3 2  ARG B 200 ? VAL B 206 ? ARG B 200 VAL B 206 
AA3 3  CYS B 326 ? LEU B 333 ? CYS B 326 LEU B 333 
AA3 4  ILE B 345 ? LYS B 352 ? ILE B 345 LYS B 352 
AA3 5  VAL B 284 ? ALA B 290 ? VAL B 284 ALA B 290 
AA3 6  LEU B 232 ? MET B 238 ? LEU B 232 MET B 238 
AA3 7  TYR B 377 ? ASP B 382 ? TYR B 377 ASP B 382 
AA3 8  SER B 458 ? ARG B 461 ? SER B 458 ARG B 461 
AA3 9  ILE B 405 ? VAL B 414 ? ILE B 405 VAL B 414 
AA3 10 THR B 512 ? THR B 523 ? THR B 512 THR B 523 
AA3 11 MET B 386 ? LEU B 387 ? MET B 386 LEU B 387 
AA4 1  SER B 336 ? VAL B 337 ? SER B 336 VAL B 337 
AA4 2  LYS B 340 ? CYS B 341 ? LYS B 340 CYS B 341 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1  2  N ILE A 179 ? N ILE A 179 O MET A 201 ? O MET A 201 
AA1 2  3  N TRP A 202 ? N TRP A 202 O GLU A 330 ? O GLU A 330 
AA1 3  4  N HIS A 327 ? N HIS A 327 O LEU A 351 ? O LEU A 351 
AA1 4  5  O GLN A 346 ? O GLN A 346 N VAL A 286 ? N VAL A 286 
AA1 5  6  O CYS A 287 ? O CYS A 287 N ILE A 234 ? N ILE A 234 
AA1 6  7  N MET A 233 ? N MET A 233 O ALA A 379 ? O ALA A 379 
AA1 7  8  N THR A 378 ? N THR A 378 O TYR A 460 ? O TYR A 460 
AA1 8  9  O ALA A 459 ? O ALA A 459 N ALA A 408 ? N ALA A 408 
AA1 9  10 N GLY A 406 ? N GLY A 406 O THR A 512 ? O THR A 512 
AA1 10 11 O ARG A 522 ? O ARG A 522 N MET A 386 ? N MET A 386 
AA2 1  2  N VAL A 337 ? N VAL A 337 O LYS A 340 ? O LYS A 340 
AA3 1  2  N ILE B 179 ? N ILE B 179 O MET B 201 ? O MET B 201 
AA3 2  3  N TRP B 202 ? N TRP B 202 O GLU B 330 ? O GLU B 330 
AA3 3  4  N HIS B 327 ? N HIS B 327 O LEU B 351 ? O LEU B 351 
AA3 4  5  O GLN B 346 ? O GLN B 346 N VAL B 286 ? N VAL B 286 
AA3 5  6  O CYS B 287 ? O CYS B 287 N ILE B 234 ? N ILE B 234 
AA3 6  7  N MET B 233 ? N MET B 233 O ALA B 379 ? O ALA B 379 
AA3 7  8  N THR B 378 ? N THR B 378 O TYR B 460 ? O TYR B 460 
AA3 8  9  O ALA B 459 ? O ALA B 459 N ALA B 408 ? N ALA B 408 
AA3 9  10 N GLY B 406 ? N GLY B 406 O THR B 512 ? O THR B 512 
AA3 10 11 O ARG B 522 ? O ARG B 522 N MET B 386 ? N MET B 386 
AA4 1  2  N VAL B 337 ? N VAL B 337 O LYS B 340 ? O LYS B 340 
# 
_pdbx_entry_details.entry_id                   8Z0O 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 PHE A 192 ? ? -171.90 141.34  
2  1 CYS A 208 ? ? -45.42  107.74  
3  1 PRO A 211 ? ? -60.86  6.21    
4  1 ASP A 213 ? ? -90.10  30.75   
5  1 ASN A 240 ? ? 55.02   70.72   
6  1 ASP A 278 ? ? 72.45   -2.91   
7  1 ASN A 338 ? ? 58.16   -133.62 
8  1 GLN A 374 ? ? 56.28   73.16   
9  1 ASN A 607 ? ? 56.41   71.66   
10 1 GLU A 616 ? ? -95.98  -63.21  
11 1 TYR A 617 ? ? 49.71   -159.77 
12 1 GLN A 619 ? ? 73.52   -5.88   
13 1 MET A 652 ? ? -99.36  35.40   
14 1 PRO A 682 ? ? -66.29  8.03    
15 1 PHE A 725 ? ? -48.63  -72.89  
16 1 ARG A 856 ? ? -95.18  30.42   
17 1 HIS B 169 ? ? 58.42   70.41   
18 1 CYS B 208 ? ? -43.82  108.95  
19 1 PRO B 211 ? ? -62.67  3.12    
20 1 ASP B 213 ? ? -90.62  30.25   
21 1 ASP B 278 ? ? 69.11   -1.73   
22 1 ASN B 338 ? ? 58.32   -132.90 
23 1 GLN B 374 ? ? 56.52   71.89   
24 1 GLU B 616 ? ? -96.31  -63.08  
25 1 TYR B 617 ? ? 49.56   -159.85 
26 1 GLN B 619 ? ? 73.25   -8.57   
27 1 PRO B 649 ? ? -69.96  60.91   
28 1 MET B 652 ? ? -94.81  32.01   
29 1 PRO B 682 ? ? -69.05  10.35   
30 1 PHE B 725 ? ? -48.93  -71.61  
31 1 ARG B 856 ? ? -95.54  30.51   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          8Z0O 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    8Z0O 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.2 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               561823 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            8.0 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 
'a membrane-integrated glycosyltransferase that transfers GlcNAc from UDP-GlcNAc to a growing chitin chain' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        8Z0O 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             1200 
_em_imaging.nominal_defocus_max             5000 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_vitrification.entry_id              8Z0O 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                8Z0O 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET 1   ? A MET 1   
2   1 Y 1 A SER 2   ? A SER 2   
3   1 Y 1 A GLY 3   ? A GLY 3   
4   1 Y 1 A ALA 4   ? A ALA 4   
5   1 Y 1 A PRO 5   ? A PRO 5   
6   1 Y 1 A PRO 6   ? A PRO 6   
7   1 Y 1 A PRO 7   ? A PRO 7   
8   1 Y 1 A SER 8   ? A SER 8   
9   1 Y 1 A SER 9   ? A SER 9   
10  1 Y 1 A GLY 10  ? A GLY 10  
11  1 Y 1 A PHE 11  ? A PHE 11  
12  1 Y 1 A ALA 12  ? A ALA 12  
13  1 Y 1 A PRO 13  ? A PRO 13  
14  1 Y 1 A ARG 14  ? A ARG 14  
15  1 Y 1 A SER 15  ? A SER 15  
16  1 Y 1 A TYR 16  ? A TYR 16  
17  1 Y 1 A GLY 17  ? A GLY 17  
18  1 Y 1 A GLN 18  ? A GLN 18  
19  1 Y 1 A GLN 19  ? A GLN 19  
20  1 Y 1 A PRO 20  ? A PRO 20  
21  1 Y 1 A LEU 21  ? A LEU 21  
22  1 Y 1 A SER 22  ? A SER 22  
23  1 Y 1 A PRO 40  ? A PRO 40  
24  1 Y 1 A PRO 41  ? A PRO 41  
25  1 Y 1 A PRO 42  ? A PRO 42  
26  1 Y 1 A SER 43  ? A SER 43  
27  1 Y 1 A ILE 44  ? A ILE 44  
28  1 Y 1 A ARG 45  ? A ARG 45  
29  1 Y 1 A SER 46  ? A SER 46  
30  1 Y 1 A CYS 47  ? A CYS 47  
31  1 Y 1 A GLY 48  ? A GLY 48  
32  1 Y 1 A SER 49  ? A SER 49  
33  1 Y 1 A GLN 50  ? A GLN 50  
34  1 Y 1 A GLN 51  ? A GLN 51  
35  1 Y 1 A TYR 52  ? A TYR 52  
36  1 Y 1 A VAL 53  ? A VAL 53  
37  1 Y 1 A TYR 56  ? A TYR 56  
38  1 Y 1 A ILE 57  ? A ILE 57  
39  1 Y 1 A PRO 58  ? A PRO 58  
40  1 Y 1 A THR 59  ? A THR 59  
41  1 Y 1 A GLY 60  ? A GLY 60  
42  1 Y 1 A ALA 61  ? A ALA 61  
43  1 Y 1 A ALA 62  ? A ALA 62  
44  1 Y 1 A PHE 63  ? A PHE 63  
45  1 Y 1 A PRO 64  ? A PRO 64  
46  1 Y 1 A PRO 65  ? A PRO 65  
47  1 Y 1 A SER 66  ? A SER 66  
48  1 Y 1 A SER 67  ? A SER 67  
49  1 Y 1 A VAL 68  ? A VAL 68  
50  1 Y 1 A GLN 69  ? A GLN 69  
51  1 Y 1 A ASP 70  ? A ASP 70  
52  1 Y 1 A MET 71  ? A MET 71  
53  1 Y 1 A ILE 72  ? A ILE 72  
54  1 Y 1 A SER 73  ? A SER 73  
55  1 Y 1 A SER 74  ? A SER 74  
56  1 Y 1 A MET 75  ? A MET 75  
57  1 Y 1 A LYS 76  ? A LYS 76  
58  1 Y 1 A SER 77  ? A SER 77  
59  1 Y 1 A TYR 78  ? A TYR 78  
60  1 Y 1 A ALA 79  ? A ALA 79  
61  1 Y 1 A SER 80  ? A SER 80  
62  1 Y 1 A ALA 81  ? A ALA 81  
63  1 Y 1 A THR 82  ? A THR 82  
64  1 Y 1 A ASP 83  ? A ASP 83  
65  1 Y 1 A LEU 84  ? A LEU 84  
66  1 Y 1 A VAL 85  ? A VAL 85  
67  1 Y 1 A ARG 86  ? A ARG 86  
68  1 Y 1 A THR 87  ? A THR 87  
69  1 Y 1 A TYR 88  ? A TYR 88  
70  1 Y 1 A SER 89  ? A SER 89  
71  1 Y 1 A GLU 90  ? A GLU 90  
72  1 Y 1 A PHE 148 ? A PHE 148 
73  1 Y 1 A GLU 162 ? A GLU 162 
74  1 Y 1 A ASN 490 ? A ASN 490 
75  1 Y 1 A GLN 738 ? A GLN 738 
76  1 Y 1 A ASP 739 ? A ASP 739 
77  1 Y 1 A LEU 740 ? A LEU 740 
78  1 Y 1 A SER 741 ? A SER 741 
79  1 Y 1 A TRP 742 ? A TRP 742 
80  1 Y 1 A GLY 743 ? A GLY 743 
81  1 Y 1 A THR 744 ? A THR 744 
82  1 Y 1 A LYS 745 ? A LYS 745 
83  1 Y 1 A GLY 746 ? A GLY 746 
84  1 Y 1 A LEU 747 ? A LEU 747 
85  1 Y 1 A HIS 748 ? A HIS 748 
86  1 Y 1 A ASP 749 ? A ASP 749 
87  1 Y 1 A ASP 750 ? A ASP 750 
88  1 Y 1 A PRO 751 ? A PRO 751 
89  1 Y 1 A LEU 752 ? A LEU 752 
90  1 Y 1 A LEU 753 ? A LEU 753 
91  1 Y 1 A ALA 754 ? A ALA 754 
92  1 Y 1 A ALA 755 ? A ALA 755 
93  1 Y 1 A SER 756 ? A SER 756 
94  1 Y 1 A LEU 757 ? A LEU 757 
95  1 Y 1 A ASP 758 ? A ASP 758 
96  1 Y 1 A GLU 759 ? A GLU 759 
97  1 Y 1 A THR 760 ? A THR 760 
98  1 Y 1 A GLU 761 ? A GLU 761 
99  1 Y 1 A ILE 860 ? A ILE 860 
100 1 Y 1 A ASP 861 ? A ASP 861 
101 1 Y 1 A LYS 862 ? A LYS 862 
102 1 Y 1 A SER 863 ? A SER 863 
103 1 Y 1 A GLU 864 ? A GLU 864 
104 1 Y 1 A CYS 865 ? A CYS 865 
105 1 Y 1 A GLY 866 ? A GLY 866 
106 1 Y 1 A ASN 867 ? A ASN 867 
107 1 Y 1 A GLY 868 ? A GLY 868 
108 1 Y 1 A THR 869 ? A THR 869 
109 1 Y 1 A GLY 870 ? A GLY 870 
110 1 Y 1 A ARG 871 ? A ARG 871 
111 1 Y 1 A TYR 872 ? A TYR 872 
112 1 Y 1 A PRO 873 ? A PRO 873 
113 1 Y 1 A GLN 874 ? A GLN 874 
114 1 Y 1 A ASN 875 ? A ASN 875 
115 1 Y 1 A SER 876 ? A SER 876 
116 1 Y 1 A TYR 877 ? A TYR 877 
117 1 Y 1 A VAL 878 ? A VAL 878 
118 1 Y 1 A GLN 879 ? A GLN 879 
119 1 Y 1 A LEU 880 ? A LEU 880 
120 1 Y 1 A GLU 881 ? A GLU 881 
121 1 Y 1 A GLU 882 ? A GLU 882 
122 1 Y 1 A HIS 883 ? A HIS 883 
123 1 Y 1 A TYR 884 ? A TYR 884 
124 1 Y 1 A ALA 885 ? A ALA 885 
125 1 Y 1 A ALA 886 ? A ALA 886 
126 1 Y 1 A LEU 887 ? A LEU 887 
127 1 Y 1 A ALA 888 ? A ALA 888 
128 1 Y 1 A GLU 889 ? A GLU 889 
129 1 Y 1 A ASP 890 ? A ASP 890 
130 1 Y 1 A GLN 891 ? A GLN 891 
131 1 Y 1 A ARG 892 ? A ARG 892 
132 1 Y 1 A THR 893 ? A THR 893 
133 1 Y 1 A TYR 894 ? A TYR 894 
134 1 Y 1 A ALA 895 ? A ALA 895 
135 1 Y 1 A SER 896 ? A SER 896 
136 1 Y 1 A GLY 897 ? A GLY 897 
137 1 Y 1 A ARG 898 ? A ARG 898 
138 1 Y 1 A THR 899 ? A THR 899 
139 1 Y 1 A ASN 900 ? A ASN 900 
140 1 Y 1 A ALA 901 ? A ALA 901 
141 1 Y 1 A SER 902 ? A SER 902 
142 1 Y 1 A VAL 903 ? A VAL 903 
143 1 Y 1 A ARG 904 ? A ARG 904 
144 1 Y 1 A THR 905 ? A THR 905 
145 1 Y 1 A VAL 906 ? A VAL 906 
146 1 Y 1 A ASN 907 ? A ASN 907 
147 1 Y 1 A ASP 908 ? A ASP 908 
148 1 Y 1 A VAL 909 ? A VAL 909 
149 1 Y 1 A SER 910 ? A SER 910 
150 1 Y 1 A SER 911 ? A SER 911 
151 1 Y 1 A ALA 912 ? A ALA 912 
152 1 Y 1 A ALA 913 ? A ALA 913 
153 1 Y 1 A LEU 914 ? A LEU 914 
154 1 Y 1 A VAL 915 ? A VAL 915 
155 1 Y 1 A PRO 916 ? A PRO 916 
156 1 Y 1 A ARG 917 ? A ARG 917 
157 1 Y 1 A GLY 918 ? A GLY 918 
158 1 Y 1 A SER 919 ? A SER 919 
159 1 Y 1 A HIS 920 ? A HIS 920 
160 1 Y 1 A HIS 921 ? A HIS 921 
161 1 Y 1 A HIS 922 ? A HIS 922 
162 1 Y 1 A HIS 923 ? A HIS 923 
163 1 Y 1 A HIS 924 ? A HIS 924 
164 1 Y 1 A HIS 925 ? A HIS 925 
165 1 Y 1 B MET 1   ? B MET 1   
166 1 Y 1 B SER 2   ? B SER 2   
167 1 Y 1 B GLY 3   ? B GLY 3   
168 1 Y 1 B ALA 4   ? B ALA 4   
169 1 Y 1 B PRO 5   ? B PRO 5   
170 1 Y 1 B PRO 6   ? B PRO 6   
171 1 Y 1 B PRO 7   ? B PRO 7   
172 1 Y 1 B SER 8   ? B SER 8   
173 1 Y 1 B SER 9   ? B SER 9   
174 1 Y 1 B GLY 10  ? B GLY 10  
175 1 Y 1 B PHE 11  ? B PHE 11  
176 1 Y 1 B ALA 12  ? B ALA 12  
177 1 Y 1 B PRO 13  ? B PRO 13  
178 1 Y 1 B ARG 14  ? B ARG 14  
179 1 Y 1 B SER 15  ? B SER 15  
180 1 Y 1 B TYR 16  ? B TYR 16  
181 1 Y 1 B GLY 17  ? B GLY 17  
182 1 Y 1 B GLN 18  ? B GLN 18  
183 1 Y 1 B GLN 19  ? B GLN 19  
184 1 Y 1 B PRO 20  ? B PRO 20  
185 1 Y 1 B LEU 21  ? B LEU 21  
186 1 Y 1 B SER 22  ? B SER 22  
187 1 Y 1 B PRO 40  ? B PRO 40  
188 1 Y 1 B PRO 41  ? B PRO 41  
189 1 Y 1 B PRO 42  ? B PRO 42  
190 1 Y 1 B SER 43  ? B SER 43  
191 1 Y 1 B ILE 44  ? B ILE 44  
192 1 Y 1 B ARG 45  ? B ARG 45  
193 1 Y 1 B SER 46  ? B SER 46  
194 1 Y 1 B CYS 47  ? B CYS 47  
195 1 Y 1 B GLY 48  ? B GLY 48  
196 1 Y 1 B SER 49  ? B SER 49  
197 1 Y 1 B GLN 50  ? B GLN 50  
198 1 Y 1 B GLN 51  ? B GLN 51  
199 1 Y 1 B TYR 52  ? B TYR 52  
200 1 Y 1 B VAL 53  ? B VAL 53  
201 1 Y 1 B THR 54  ? B THR 54  
202 1 Y 1 B SER 55  ? B SER 55  
203 1 Y 1 B TYR 56  ? B TYR 56  
204 1 Y 1 B ILE 57  ? B ILE 57  
205 1 Y 1 B PRO 58  ? B PRO 58  
206 1 Y 1 B THR 59  ? B THR 59  
207 1 Y 1 B GLY 60  ? B GLY 60  
208 1 Y 1 B ALA 61  ? B ALA 61  
209 1 Y 1 B ALA 62  ? B ALA 62  
210 1 Y 1 B PHE 63  ? B PHE 63  
211 1 Y 1 B PRO 64  ? B PRO 64  
212 1 Y 1 B PRO 65  ? B PRO 65  
213 1 Y 1 B SER 66  ? B SER 66  
214 1 Y 1 B SER 67  ? B SER 67  
215 1 Y 1 B VAL 68  ? B VAL 68  
216 1 Y 1 B GLN 69  ? B GLN 69  
217 1 Y 1 B ASP 70  ? B ASP 70  
218 1 Y 1 B MET 71  ? B MET 71  
219 1 Y 1 B ILE 72  ? B ILE 72  
220 1 Y 1 B SER 73  ? B SER 73  
221 1 Y 1 B SER 74  ? B SER 74  
222 1 Y 1 B MET 75  ? B MET 75  
223 1 Y 1 B LYS 76  ? B LYS 76  
224 1 Y 1 B SER 77  ? B SER 77  
225 1 Y 1 B TYR 78  ? B TYR 78  
226 1 Y 1 B ALA 79  ? B ALA 79  
227 1 Y 1 B SER 80  ? B SER 80  
228 1 Y 1 B ALA 81  ? B ALA 81  
229 1 Y 1 B THR 82  ? B THR 82  
230 1 Y 1 B ASP 83  ? B ASP 83  
231 1 Y 1 B LEU 84  ? B LEU 84  
232 1 Y 1 B VAL 85  ? B VAL 85  
233 1 Y 1 B ARG 86  ? B ARG 86  
234 1 Y 1 B THR 87  ? B THR 87  
235 1 Y 1 B TYR 88  ? B TYR 88  
236 1 Y 1 B SER 89  ? B SER 89  
237 1 Y 1 B GLU 90  ? B GLU 90  
238 1 Y 1 B GLU 122 ? B GLU 122 
239 1 Y 1 B TYR 125 ? B TYR 125 
240 1 Y 1 B ALA 126 ? B ALA 126 
241 1 Y 1 B MET 127 ? B MET 127 
242 1 Y 1 B GLU 132 ? B GLU 132 
243 1 Y 1 B TRP 742 ? B TRP 742 
244 1 Y 1 B GLY 743 ? B GLY 743 
245 1 Y 1 B THR 744 ? B THR 744 
246 1 Y 1 B LYS 745 ? B LYS 745 
247 1 Y 1 B GLY 746 ? B GLY 746 
248 1 Y 1 B LEU 747 ? B LEU 747 
249 1 Y 1 B HIS 748 ? B HIS 748 
250 1 Y 1 B ASP 749 ? B ASP 749 
251 1 Y 1 B ASP 750 ? B ASP 750 
252 1 Y 1 B PRO 751 ? B PRO 751 
253 1 Y 1 B LEU 752 ? B LEU 752 
254 1 Y 1 B LEU 753 ? B LEU 753 
255 1 Y 1 B ALA 754 ? B ALA 754 
256 1 Y 1 B ALA 755 ? B ALA 755 
257 1 Y 1 B SER 756 ? B SER 756 
258 1 Y 1 B LEU 757 ? B LEU 757 
259 1 Y 1 B ASP 758 ? B ASP 758 
260 1 Y 1 B GLU 759 ? B GLU 759 
261 1 Y 1 B THR 760 ? B THR 760 
262 1 Y 1 B GLU 761 ? B GLU 761 
263 1 Y 1 B ILE 860 ? B ILE 860 
264 1 Y 1 B ASP 861 ? B ASP 861 
265 1 Y 1 B LYS 862 ? B LYS 862 
266 1 Y 1 B SER 863 ? B SER 863 
267 1 Y 1 B GLU 864 ? B GLU 864 
268 1 Y 1 B CYS 865 ? B CYS 865 
269 1 Y 1 B GLY 866 ? B GLY 866 
270 1 Y 1 B ASN 867 ? B ASN 867 
271 1 Y 1 B GLY 868 ? B GLY 868 
272 1 Y 1 B THR 869 ? B THR 869 
273 1 Y 1 B GLY 870 ? B GLY 870 
274 1 Y 1 B ARG 871 ? B ARG 871 
275 1 Y 1 B TYR 872 ? B TYR 872 
276 1 Y 1 B PRO 873 ? B PRO 873 
277 1 Y 1 B GLN 874 ? B GLN 874 
278 1 Y 1 B ASN 875 ? B ASN 875 
279 1 Y 1 B SER 876 ? B SER 876 
280 1 Y 1 B TYR 877 ? B TYR 877 
281 1 Y 1 B VAL 878 ? B VAL 878 
282 1 Y 1 B GLN 879 ? B GLN 879 
283 1 Y 1 B LEU 880 ? B LEU 880 
284 1 Y 1 B GLU 881 ? B GLU 881 
285 1 Y 1 B GLU 882 ? B GLU 882 
286 1 Y 1 B HIS 883 ? B HIS 883 
287 1 Y 1 B TYR 884 ? B TYR 884 
288 1 Y 1 B ALA 885 ? B ALA 885 
289 1 Y 1 B ALA 886 ? B ALA 886 
290 1 Y 1 B LEU 887 ? B LEU 887 
291 1 Y 1 B ALA 888 ? B ALA 888 
292 1 Y 1 B GLU 889 ? B GLU 889 
293 1 Y 1 B ASP 890 ? B ASP 890 
294 1 Y 1 B GLN 891 ? B GLN 891 
295 1 Y 1 B ARG 892 ? B ARG 892 
296 1 Y 1 B THR 893 ? B THR 893 
297 1 Y 1 B TYR 894 ? B TYR 894 
298 1 Y 1 B ALA 895 ? B ALA 895 
299 1 Y 1 B SER 896 ? B SER 896 
300 1 Y 1 B GLY 897 ? B GLY 897 
301 1 Y 1 B ARG 898 ? B ARG 898 
302 1 Y 1 B THR 899 ? B THR 899 
303 1 Y 1 B ASN 900 ? B ASN 900 
304 1 Y 1 B ALA 901 ? B ALA 901 
305 1 Y 1 B SER 902 ? B SER 902 
306 1 Y 1 B VAL 903 ? B VAL 903 
307 1 Y 1 B ARG 904 ? B ARG 904 
308 1 Y 1 B THR 905 ? B THR 905 
309 1 Y 1 B VAL 906 ? B VAL 906 
310 1 Y 1 B ASN 907 ? B ASN 907 
311 1 Y 1 B ASP 908 ? B ASP 908 
312 1 Y 1 B VAL 909 ? B VAL 909 
313 1 Y 1 B SER 910 ? B SER 910 
314 1 Y 1 B SER 911 ? B SER 911 
315 1 Y 1 B ALA 912 ? B ALA 912 
316 1 Y 1 B ALA 913 ? B ALA 913 
317 1 Y 1 B LEU 914 ? B LEU 914 
318 1 Y 1 B VAL 915 ? B VAL 915 
319 1 Y 1 B PRO 916 ? B PRO 916 
320 1 Y 1 B ARG 917 ? B ARG 917 
321 1 Y 1 B GLY 918 ? B GLY 918 
322 1 Y 1 B SER 919 ? B SER 919 
323 1 Y 1 B HIS 920 ? B HIS 920 
324 1 Y 1 B HIS 921 ? B HIS 921 
325 1 Y 1 B HIS 922 ? B HIS 922 
326 1 Y 1 B HIS 923 ? B HIS 923 
327 1 Y 1 B HIS 924 ? B HIS 924 
328 1 Y 1 B HIS 925 ? B HIS 925 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
CYS N      N  N N 74  
CYS CA     C  N R 75  
CYS C      C  N N 76  
CYS O      O  N N 77  
CYS CB     C  N N 78  
CYS SG     S  N N 79  
CYS OXT    O  N N 80  
CYS H      H  N N 81  
CYS H2     H  N N 82  
CYS HA     H  N N 83  
CYS HB2    H  N N 84  
CYS HB3    H  N N 85  
CYS HG     H  N N 86  
CYS HXT    H  N N 87  
GLN N      N  N N 88  
GLN CA     C  N S 89  
GLN C      C  N N 90  
GLN O      O  N N 91  
GLN CB     C  N N 92  
GLN CG     C  N N 93  
GLN CD     C  N N 94  
GLN OE1    O  N N 95  
GLN NE2    N  N N 96  
GLN OXT    O  N N 97  
GLN H      H  N N 98  
GLN H2     H  N N 99  
GLN HA     H  N N 100 
GLN HB2    H  N N 101 
GLN HB3    H  N N 102 
GLN HG2    H  N N 103 
GLN HG3    H  N N 104 
GLN HE21   H  N N 105 
GLN HE22   H  N N 106 
GLN HXT    H  N N 107 
GLU N      N  N N 108 
GLU CA     C  N S 109 
GLU C      C  N N 110 
GLU O      O  N N 111 
GLU CB     C  N N 112 
GLU CG     C  N N 113 
GLU CD     C  N N 114 
GLU OE1    O  N N 115 
GLU OE2    O  N N 116 
GLU OXT    O  N N 117 
GLU H      H  N N 118 
GLU H2     H  N N 119 
GLU HA     H  N N 120 
GLU HB2    H  N N 121 
GLU HB3    H  N N 122 
GLU HG2    H  N N 123 
GLU HG3    H  N N 124 
GLU HE2    H  N N 125 
GLU HXT    H  N N 126 
GLY N      N  N N 127 
GLY CA     C  N N 128 
GLY C      C  N N 129 
GLY O      O  N N 130 
GLY OXT    O  N N 131 
GLY H      H  N N 132 
GLY H2     H  N N 133 
GLY HA2    H  N N 134 
GLY HA3    H  N N 135 
GLY HXT    H  N N 136 
HIS N      N  N N 137 
HIS CA     C  N S 138 
HIS C      C  N N 139 
HIS O      O  N N 140 
HIS CB     C  N N 141 
HIS CG     C  Y N 142 
HIS ND1    N  Y N 143 
HIS CD2    C  Y N 144 
HIS CE1    C  Y N 145 
HIS NE2    N  Y N 146 
HIS OXT    O  N N 147 
HIS H      H  N N 148 
HIS H2     H  N N 149 
HIS HA     H  N N 150 
HIS HB2    H  N N 151 
HIS HB3    H  N N 152 
HIS HD1    H  N N 153 
HIS HD2    H  N N 154 
HIS HE1    H  N N 155 
HIS HE2    H  N N 156 
HIS HXT    H  N N 157 
ILE N      N  N N 158 
ILE CA     C  N S 159 
ILE C      C  N N 160 
ILE O      O  N N 161 
ILE CB     C  N S 162 
ILE CG1    C  N N 163 
ILE CG2    C  N N 164 
ILE CD1    C  N N 165 
ILE OXT    O  N N 166 
ILE H      H  N N 167 
ILE H2     H  N N 168 
ILE HA     H  N N 169 
ILE HB     H  N N 170 
ILE HG12   H  N N 171 
ILE HG13   H  N N 172 
ILE HG21   H  N N 173 
ILE HG22   H  N N 174 
ILE HG23   H  N N 175 
ILE HD11   H  N N 176 
ILE HD12   H  N N 177 
ILE HD13   H  N N 178 
ILE HXT    H  N N 179 
LEU N      N  N N 180 
LEU CA     C  N S 181 
LEU C      C  N N 182 
LEU O      O  N N 183 
LEU CB     C  N N 184 
LEU CG     C  N N 185 
LEU CD1    C  N N 186 
LEU CD2    C  N N 187 
LEU OXT    O  N N 188 
LEU H      H  N N 189 
LEU H2     H  N N 190 
LEU HA     H  N N 191 
LEU HB2    H  N N 192 
LEU HB3    H  N N 193 
LEU HG     H  N N 194 
LEU HD11   H  N N 195 
LEU HD12   H  N N 196 
LEU HD13   H  N N 197 
LEU HD21   H  N N 198 
LEU HD22   H  N N 199 
LEU HD23   H  N N 200 
LEU HXT    H  N N 201 
LYS N      N  N N 202 
LYS CA     C  N S 203 
LYS C      C  N N 204 
LYS O      O  N N 205 
LYS CB     C  N N 206 
LYS CG     C  N N 207 
LYS CD     C  N N 208 
LYS CE     C  N N 209 
LYS NZ     N  N N 210 
LYS OXT    O  N N 211 
LYS H      H  N N 212 
LYS H2     H  N N 213 
LYS HA     H  N N 214 
LYS HB2    H  N N 215 
LYS HB3    H  N N 216 
LYS HG2    H  N N 217 
LYS HG3    H  N N 218 
LYS HD2    H  N N 219 
LYS HD3    H  N N 220 
LYS HE2    H  N N 221 
LYS HE3    H  N N 222 
LYS HZ1    H  N N 223 
LYS HZ2    H  N N 224 
LYS HZ3    H  N N 225 
LYS HXT    H  N N 226 
MET N      N  N N 227 
MET CA     C  N S 228 
MET C      C  N N 229 
MET O      O  N N 230 
MET CB     C  N N 231 
MET CG     C  N N 232 
MET SD     S  N N 233 
MET CE     C  N N 234 
MET OXT    O  N N 235 
MET H      H  N N 236 
MET H2     H  N N 237 
MET HA     H  N N 238 
MET HB2    H  N N 239 
MET HB3    H  N N 240 
MET HG2    H  N N 241 
MET HG3    H  N N 242 
MET HE1    H  N N 243 
MET HE2    H  N N 244 
MET HE3    H  N N 245 
MET HXT    H  N N 246 
MN  MN     MN N N 247 
PHE N      N  N N 248 
PHE CA     C  N S 249 
PHE C      C  N N 250 
PHE O      O  N N 251 
PHE CB     C  N N 252 
PHE CG     C  Y N 253 
PHE CD1    C  Y N 254 
PHE CD2    C  Y N 255 
PHE CE1    C  Y N 256 
PHE CE2    C  Y N 257 
PHE CZ     C  Y N 258 
PHE OXT    O  N N 259 
PHE H      H  N N 260 
PHE H2     H  N N 261 
PHE HA     H  N N 262 
PHE HB2    H  N N 263 
PHE HB3    H  N N 264 
PHE HD1    H  N N 265 
PHE HD2    H  N N 266 
PHE HE1    H  N N 267 
PHE HE2    H  N N 268 
PHE HZ     H  N N 269 
PHE HXT    H  N N 270 
PRO N      N  N N 271 
PRO CA     C  N S 272 
PRO C      C  N N 273 
PRO O      O  N N 274 
PRO CB     C  N N 275 
PRO CG     C  N N 276 
PRO CD     C  N N 277 
PRO OXT    O  N N 278 
PRO H      H  N N 279 
PRO HA     H  N N 280 
PRO HB2    H  N N 281 
PRO HB3    H  N N 282 
PRO HG2    H  N N 283 
PRO HG3    H  N N 284 
PRO HD2    H  N N 285 
PRO HD3    H  N N 286 
PRO HXT    H  N N 287 
SER N      N  N N 288 
SER CA     C  N S 289 
SER C      C  N N 290 
SER O      O  N N 291 
SER CB     C  N N 292 
SER OG     O  N N 293 
SER OXT    O  N N 294 
SER H      H  N N 295 
SER H2     H  N N 296 
SER HA     H  N N 297 
SER HB2    H  N N 298 
SER HB3    H  N N 299 
SER HG     H  N N 300 
SER HXT    H  N N 301 
THR N      N  N N 302 
THR CA     C  N S 303 
THR C      C  N N 304 
THR O      O  N N 305 
THR CB     C  N R 306 
THR OG1    O  N N 307 
THR CG2    C  N N 308 
THR OXT    O  N N 309 
THR H      H  N N 310 
THR H2     H  N N 311 
THR HA     H  N N 312 
THR HB     H  N N 313 
THR HG1    H  N N 314 
THR HG21   H  N N 315 
THR HG22   H  N N 316 
THR HG23   H  N N 317 
THR HXT    H  N N 318 
TRP N      N  N N 319 
TRP CA     C  N S 320 
TRP C      C  N N 321 
TRP O      O  N N 322 
TRP CB     C  N N 323 
TRP CG     C  Y N 324 
TRP CD1    C  Y N 325 
TRP CD2    C  Y N 326 
TRP NE1    N  Y N 327 
TRP CE2    C  Y N 328 
TRP CE3    C  Y N 329 
TRP CZ2    C  Y N 330 
TRP CZ3    C  Y N 331 
TRP CH2    C  Y N 332 
TRP OXT    O  N N 333 
TRP H      H  N N 334 
TRP H2     H  N N 335 
TRP HA     H  N N 336 
TRP HB2    H  N N 337 
TRP HB3    H  N N 338 
TRP HD1    H  N N 339 
TRP HE1    H  N N 340 
TRP HE3    H  N N 341 
TRP HZ2    H  N N 342 
TRP HZ3    H  N N 343 
TRP HH2    H  N N 344 
TRP HXT    H  N N 345 
TYR N      N  N N 346 
TYR CA     C  N S 347 
TYR C      C  N N 348 
TYR O      O  N N 349 
TYR CB     C  N N 350 
TYR CG     C  Y N 351 
TYR CD1    C  Y N 352 
TYR CD2    C  Y N 353 
TYR CE1    C  Y N 354 
TYR CE2    C  Y N 355 
TYR CZ     C  Y N 356 
TYR OH     O  N N 357 
TYR OXT    O  N N 358 
TYR H      H  N N 359 
TYR H2     H  N N 360 
TYR HA     H  N N 361 
TYR HB2    H  N N 362 
TYR HB3    H  N N 363 
TYR HD1    H  N N 364 
TYR HD2    H  N N 365 
TYR HE1    H  N N 366 
TYR HE2    H  N N 367 
TYR HH     H  N N 368 
TYR HXT    H  N N 369 
UDP N1     N  N N 370 
UDP C2     C  N N 371 
UDP N3     N  N N 372 
UDP C4     C  N N 373 
UDP C5     C  N N 374 
UDP C6     C  N N 375 
UDP O2     O  N N 376 
UDP O4     O  N N 377 
UDP "C1'"  C  N R 378 
UDP "C2'"  C  N R 379 
UDP "O2'"  O  N N 380 
UDP "C3'"  C  N S 381 
UDP "C4'"  C  N R 382 
UDP "O4'"  O  N N 383 
UDP "O3'"  O  N N 384 
UDP "C5'"  C  N N 385 
UDP "O5'"  O  N N 386 
UDP PA     P  N N 387 
UDP O1A    O  N N 388 
UDP O2A    O  N N 389 
UDP O3A    O  N N 390 
UDP PB     P  N N 391 
UDP O1B    O  N N 392 
UDP O2B    O  N N 393 
UDP O3B    O  N N 394 
UDP HN3    H  N N 395 
UDP H5     H  N N 396 
UDP H6     H  N N 397 
UDP "H1'"  H  N N 398 
UDP "H2'"  H  N N 399 
UDP "HO2'" H  N N 400 
UDP "H3'"  H  N N 401 
UDP "H4'"  H  N N 402 
UDP "HO3'" H  N N 403 
UDP "H5'1" H  N N 404 
UDP "H5'2" H  N N 405 
UDP HOA2   H  N N 406 
UDP HOB2   H  N N 407 
UDP HOB3   H  N N 408 
VAL N      N  N N 409 
VAL CA     C  N S 410 
VAL C      C  N N 411 
VAL O      O  N N 412 
VAL CB     C  N N 413 
VAL CG1    C  N N 414 
VAL CG2    C  N N 415 
VAL OXT    O  N N 416 
VAL H      H  N N 417 
VAL H2     H  N N 418 
VAL HA     H  N N 419 
VAL HB     H  N N 420 
VAL HG11   H  N N 421 
VAL HG12   H  N N 422 
VAL HG13   H  N N 423 
VAL HG21   H  N N 424 
VAL HG22   H  N N 425 
VAL HG23   H  N N 426 
VAL HXT    H  N N 427 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
GLN N     CA     sing N N 83  
GLN N     H      sing N N 84  
GLN N     H2     sing N N 85  
GLN CA    C      sing N N 86  
GLN CA    CB     sing N N 87  
GLN CA    HA     sing N N 88  
GLN C     O      doub N N 89  
GLN C     OXT    sing N N 90  
GLN CB    CG     sing N N 91  
GLN CB    HB2    sing N N 92  
GLN CB    HB3    sing N N 93  
GLN CG    CD     sing N N 94  
GLN CG    HG2    sing N N 95  
GLN CG    HG3    sing N N 96  
GLN CD    OE1    doub N N 97  
GLN CD    NE2    sing N N 98  
GLN NE2   HE21   sing N N 99  
GLN NE2   HE22   sing N N 100 
GLN OXT   HXT    sing N N 101 
GLU N     CA     sing N N 102 
GLU N     H      sing N N 103 
GLU N     H2     sing N N 104 
GLU CA    C      sing N N 105 
GLU CA    CB     sing N N 106 
GLU CA    HA     sing N N 107 
GLU C     O      doub N N 108 
GLU C     OXT    sing N N 109 
GLU CB    CG     sing N N 110 
GLU CB    HB2    sing N N 111 
GLU CB    HB3    sing N N 112 
GLU CG    CD     sing N N 113 
GLU CG    HG2    sing N N 114 
GLU CG    HG3    sing N N 115 
GLU CD    OE1    doub N N 116 
GLU CD    OE2    sing N N 117 
GLU OE2   HE2    sing N N 118 
GLU OXT   HXT    sing N N 119 
GLY N     CA     sing N N 120 
GLY N     H      sing N N 121 
GLY N     H2     sing N N 122 
GLY CA    C      sing N N 123 
GLY CA    HA2    sing N N 124 
GLY CA    HA3    sing N N 125 
GLY C     O      doub N N 126 
GLY C     OXT    sing N N 127 
GLY OXT   HXT    sing N N 128 
HIS N     CA     sing N N 129 
HIS N     H      sing N N 130 
HIS N     H2     sing N N 131 
HIS CA    C      sing N N 132 
HIS CA    CB     sing N N 133 
HIS CA    HA     sing N N 134 
HIS C     O      doub N N 135 
HIS C     OXT    sing N N 136 
HIS CB    CG     sing N N 137 
HIS CB    HB2    sing N N 138 
HIS CB    HB3    sing N N 139 
HIS CG    ND1    sing Y N 140 
HIS CG    CD2    doub Y N 141 
HIS ND1   CE1    doub Y N 142 
HIS ND1   HD1    sing N N 143 
HIS CD2   NE2    sing Y N 144 
HIS CD2   HD2    sing N N 145 
HIS CE1   NE2    sing Y N 146 
HIS CE1   HE1    sing N N 147 
HIS NE2   HE2    sing N N 148 
HIS OXT   HXT    sing N N 149 
ILE N     CA     sing N N 150 
ILE N     H      sing N N 151 
ILE N     H2     sing N N 152 
ILE CA    C      sing N N 153 
ILE CA    CB     sing N N 154 
ILE CA    HA     sing N N 155 
ILE C     O      doub N N 156 
ILE C     OXT    sing N N 157 
ILE CB    CG1    sing N N 158 
ILE CB    CG2    sing N N 159 
ILE CB    HB     sing N N 160 
ILE CG1   CD1    sing N N 161 
ILE CG1   HG12   sing N N 162 
ILE CG1   HG13   sing N N 163 
ILE CG2   HG21   sing N N 164 
ILE CG2   HG22   sing N N 165 
ILE CG2   HG23   sing N N 166 
ILE CD1   HD11   sing N N 167 
ILE CD1   HD12   sing N N 168 
ILE CD1   HD13   sing N N 169 
ILE OXT   HXT    sing N N 170 
LEU N     CA     sing N N 171 
LEU N     H      sing N N 172 
LEU N     H2     sing N N 173 
LEU CA    C      sing N N 174 
LEU CA    CB     sing N N 175 
LEU CA    HA     sing N N 176 
LEU C     O      doub N N 177 
LEU C     OXT    sing N N 178 
LEU CB    CG     sing N N 179 
LEU CB    HB2    sing N N 180 
LEU CB    HB3    sing N N 181 
LEU CG    CD1    sing N N 182 
LEU CG    CD2    sing N N 183 
LEU CG    HG     sing N N 184 
LEU CD1   HD11   sing N N 185 
LEU CD1   HD12   sing N N 186 
LEU CD1   HD13   sing N N 187 
LEU CD2   HD21   sing N N 188 
LEU CD2   HD22   sing N N 189 
LEU CD2   HD23   sing N N 190 
LEU OXT   HXT    sing N N 191 
LYS N     CA     sing N N 192 
LYS N     H      sing N N 193 
LYS N     H2     sing N N 194 
LYS CA    C      sing N N 195 
LYS CA    CB     sing N N 196 
LYS CA    HA     sing N N 197 
LYS C     O      doub N N 198 
LYS C     OXT    sing N N 199 
LYS CB    CG     sing N N 200 
LYS CB    HB2    sing N N 201 
LYS CB    HB3    sing N N 202 
LYS CG    CD     sing N N 203 
LYS CG    HG2    sing N N 204 
LYS CG    HG3    sing N N 205 
LYS CD    CE     sing N N 206 
LYS CD    HD2    sing N N 207 
LYS CD    HD3    sing N N 208 
LYS CE    NZ     sing N N 209 
LYS CE    HE2    sing N N 210 
LYS CE    HE3    sing N N 211 
LYS NZ    HZ1    sing N N 212 
LYS NZ    HZ2    sing N N 213 
LYS NZ    HZ3    sing N N 214 
LYS OXT   HXT    sing N N 215 
MET N     CA     sing N N 216 
MET N     H      sing N N 217 
MET N     H2     sing N N 218 
MET CA    C      sing N N 219 
MET CA    CB     sing N N 220 
MET CA    HA     sing N N 221 
MET C     O      doub N N 222 
MET C     OXT    sing N N 223 
MET CB    CG     sing N N 224 
MET CB    HB2    sing N N 225 
MET CB    HB3    sing N N 226 
MET CG    SD     sing N N 227 
MET CG    HG2    sing N N 228 
MET CG    HG3    sing N N 229 
MET SD    CE     sing N N 230 
MET CE    HE1    sing N N 231 
MET CE    HE2    sing N N 232 
MET CE    HE3    sing N N 233 
MET OXT   HXT    sing N N 234 
PHE N     CA     sing N N 235 
PHE N     H      sing N N 236 
PHE N     H2     sing N N 237 
PHE CA    C      sing N N 238 
PHE CA    CB     sing N N 239 
PHE CA    HA     sing N N 240 
PHE C     O      doub N N 241 
PHE C     OXT    sing N N 242 
PHE CB    CG     sing N N 243 
PHE CB    HB2    sing N N 244 
PHE CB    HB3    sing N N 245 
PHE CG    CD1    doub Y N 246 
PHE CG    CD2    sing Y N 247 
PHE CD1   CE1    sing Y N 248 
PHE CD1   HD1    sing N N 249 
PHE CD2   CE2    doub Y N 250 
PHE CD2   HD2    sing N N 251 
PHE CE1   CZ     doub Y N 252 
PHE CE1   HE1    sing N N 253 
PHE CE2   CZ     sing Y N 254 
PHE CE2   HE2    sing N N 255 
PHE CZ    HZ     sing N N 256 
PHE OXT   HXT    sing N N 257 
PRO N     CA     sing N N 258 
PRO N     CD     sing N N 259 
PRO N     H      sing N N 260 
PRO CA    C      sing N N 261 
PRO CA    CB     sing N N 262 
PRO CA    HA     sing N N 263 
PRO C     O      doub N N 264 
PRO C     OXT    sing N N 265 
PRO CB    CG     sing N N 266 
PRO CB    HB2    sing N N 267 
PRO CB    HB3    sing N N 268 
PRO CG    CD     sing N N 269 
PRO CG    HG2    sing N N 270 
PRO CG    HG3    sing N N 271 
PRO CD    HD2    sing N N 272 
PRO CD    HD3    sing N N 273 
PRO OXT   HXT    sing N N 274 
SER N     CA     sing N N 275 
SER N     H      sing N N 276 
SER N     H2     sing N N 277 
SER CA    C      sing N N 278 
SER CA    CB     sing N N 279 
SER CA    HA     sing N N 280 
SER C     O      doub N N 281 
SER C     OXT    sing N N 282 
SER CB    OG     sing N N 283 
SER CB    HB2    sing N N 284 
SER CB    HB3    sing N N 285 
SER OG    HG     sing N N 286 
SER OXT   HXT    sing N N 287 
THR N     CA     sing N N 288 
THR N     H      sing N N 289 
THR N     H2     sing N N 290 
THR CA    C      sing N N 291 
THR CA    CB     sing N N 292 
THR CA    HA     sing N N 293 
THR C     O      doub N N 294 
THR C     OXT    sing N N 295 
THR CB    OG1    sing N N 296 
THR CB    CG2    sing N N 297 
THR CB    HB     sing N N 298 
THR OG1   HG1    sing N N 299 
THR CG2   HG21   sing N N 300 
THR CG2   HG22   sing N N 301 
THR CG2   HG23   sing N N 302 
THR OXT   HXT    sing N N 303 
TRP N     CA     sing N N 304 
TRP N     H      sing N N 305 
TRP N     H2     sing N N 306 
TRP CA    C      sing N N 307 
TRP CA    CB     sing N N 308 
TRP CA    HA     sing N N 309 
TRP C     O      doub N N 310 
TRP C     OXT    sing N N 311 
TRP CB    CG     sing N N 312 
TRP CB    HB2    sing N N 313 
TRP CB    HB3    sing N N 314 
TRP CG    CD1    doub Y N 315 
TRP CG    CD2    sing Y N 316 
TRP CD1   NE1    sing Y N 317 
TRP CD1   HD1    sing N N 318 
TRP CD2   CE2    doub Y N 319 
TRP CD2   CE3    sing Y N 320 
TRP NE1   CE2    sing Y N 321 
TRP NE1   HE1    sing N N 322 
TRP CE2   CZ2    sing Y N 323 
TRP CE3   CZ3    doub Y N 324 
TRP CE3   HE3    sing N N 325 
TRP CZ2   CH2    doub Y N 326 
TRP CZ2   HZ2    sing N N 327 
TRP CZ3   CH2    sing Y N 328 
TRP CZ3   HZ3    sing N N 329 
TRP CH2   HH2    sing N N 330 
TRP OXT   HXT    sing N N 331 
TYR N     CA     sing N N 332 
TYR N     H      sing N N 333 
TYR N     H2     sing N N 334 
TYR CA    C      sing N N 335 
TYR CA    CB     sing N N 336 
TYR CA    HA     sing N N 337 
TYR C     O      doub N N 338 
TYR C     OXT    sing N N 339 
TYR CB    CG     sing N N 340 
TYR CB    HB2    sing N N 341 
TYR CB    HB3    sing N N 342 
TYR CG    CD1    doub Y N 343 
TYR CG    CD2    sing Y N 344 
TYR CD1   CE1    sing Y N 345 
TYR CD1   HD1    sing N N 346 
TYR CD2   CE2    doub Y N 347 
TYR CD2   HD2    sing N N 348 
TYR CE1   CZ     doub Y N 349 
TYR CE1   HE1    sing N N 350 
TYR CE2   CZ     sing Y N 351 
TYR CE2   HE2    sing N N 352 
TYR CZ    OH     sing N N 353 
TYR OH    HH     sing N N 354 
TYR OXT   HXT    sing N N 355 
UDP N1    C2     sing N N 356 
UDP N1    C6     sing N N 357 
UDP N1    "C1'"  sing N N 358 
UDP C2    N3     sing N N 359 
UDP C2    O2     doub N N 360 
UDP N3    C4     sing N N 361 
UDP N3    HN3    sing N N 362 
UDP C4    C5     sing N N 363 
UDP C4    O4     doub N N 364 
UDP C5    C6     doub N N 365 
UDP C5    H5     sing N N 366 
UDP C6    H6     sing N N 367 
UDP "C1'" "C2'"  sing N N 368 
UDP "C1'" "O4'"  sing N N 369 
UDP "C1'" "H1'"  sing N N 370 
UDP "C2'" "O2'"  sing N N 371 
UDP "C2'" "C3'"  sing N N 372 
UDP "C2'" "H2'"  sing N N 373 
UDP "O2'" "HO2'" sing N N 374 
UDP "C3'" "C4'"  sing N N 375 
UDP "C3'" "O3'"  sing N N 376 
UDP "C3'" "H3'"  sing N N 377 
UDP "C4'" "O4'"  sing N N 378 
UDP "C4'" "C5'"  sing N N 379 
UDP "C4'" "H4'"  sing N N 380 
UDP "O3'" "HO3'" sing N N 381 
UDP "C5'" "O5'"  sing N N 382 
UDP "C5'" "H5'1" sing N N 383 
UDP "C5'" "H5'2" sing N N 384 
UDP "O5'" PA     sing N N 385 
UDP PA    O1A    doub N N 386 
UDP PA    O2A    sing N N 387 
UDP PA    O3A    sing N N 388 
UDP O2A   HOA2   sing N N 389 
UDP O3A   PB     sing N N 390 
UDP PB    O1B    doub N N 391 
UDP PB    O2B    sing N N 392 
UDP PB    O3B    sing N N 393 
UDP O2B   HOB2   sing N N 394 
UDP O3B   HOB3   sing N N 395 
VAL N     CA     sing N N 396 
VAL N     H      sing N N 397 
VAL N     H2     sing N N 398 
VAL CA    C      sing N N 399 
VAL CA    CB     sing N N 400 
VAL CA    HA     sing N N 401 
VAL C     O      doub N N 402 
VAL C     OXT    sing N N 403 
VAL CB    CG1    sing N N 404 
VAL CB    CG2    sing N N 405 
VAL CB    HB     sing N N 406 
VAL CG1   HG11   sing N N 407 
VAL CG1   HG12   sing N N 408 
VAL CG1   HG13   sing N N 409 
VAL CG2   HG21   sing N N 410 
VAL CG2   HG22   sing N N 411 
VAL CG2   HG23   sing N N 412 
VAL OXT   HXT    sing N N 413 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-04-10 
_em_admin.deposition_site    PDBJ 
_em_admin.entry_id           8Z0O 
_em_admin.last_update        2024-12-04 
_em_admin.map_release_date   2024-12-04 
_em_admin.title              'Cryo-EM structure of chitin synthase' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    YES 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                KILODALTONS/NANOMETER 
_em_entity_assembly_molwt.value                103 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          1094619 
_em_entity_assembly_naturalsource.organism             'Phytophthora sojae strain P6497' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          9606 
_em_entity_assembly_recombinant.organism             'Homo sapiens' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         60 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'FEI FALCON IV (4k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'            ? 1  1 ? ? ? ? 
'IMAGE ACQUISITION'             ? 2  ? ? 1 ? ? 
MASKING                         ? 3  ? ? ? ? ? 
'CTF CORRECTION'                ? 4  1 ? ? ? ? 
'LAYERLINE INDEXING'            ? 5  ? ? ? ? ? 
'DIFFRACTION INDEXING'          ? 6  ? ? ? ? ? 
'MODEL FITTING'                 ? 7  ? ? ? ? ? 
'MODEL REFINEMENT'              ? 8  ? ? ? ? ? 
OTHER                           ? 9  ? ? ? ? ? 
'INITIAL EULER ASSIGNMENT'      ? 10 1 ? ? ? ? 
'FINAL EULER ASSIGNMENT'        ? 11 1 ? ? ? ? 
CLASSIFICATION                  ? 12 1 ? ? ? ? 
RECONSTRUCTION                  ? 13 1 ? ? ? ? 
'VOLUME SELECTION'              ? 14 1 1 1 ? ? 
'SERIES ALIGNMENT'              ? 15 1 1 1 ? ? 
'MOLECULAR REPLACEMENT'         ? 16 1 1 1 ? ? 
'LATTICE DISTORTION CORRECTION' ? 17 1 1 1 ? ? 
'SYMMETRY DETERMINATION'        ? 18 1 1 1 ? ? 
'CRYSTALLOGRAPHY MERGING'       ? 19 1 1 1 ? ? 
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   'Other government' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    8Z0O 
_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]   1.000000 
_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]   1.000000 
_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]   1.000000 
_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  
MN 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N     . HIS A 1 23  ? 188.679 145.703 164.551 1.00 186.62 ? 23   HIS A N     1 
ATOM   2     C  CA    . HIS A 1 23  ? 188.524 145.047 165.844 1.00 188.41 ? 23   HIS A CA    1 
ATOM   3     C  C     . HIS A 1 23  ? 188.280 146.068 166.949 1.00 185.74 ? 23   HIS A C     1 
ATOM   4     O  O     . HIS A 1 23  ? 187.613 145.774 167.941 1.00 182.74 ? 23   HIS A O     1 
ATOM   5     C  CB    . HIS A 1 23  ? 189.760 144.206 166.170 1.00 194.66 ? 23   HIS A CB    1 
ATOM   6     C  CG    . HIS A 1 23  ? 190.238 143.367 165.027 1.00 199.40 ? 23   HIS A CG    1 
ATOM   7     N  ND1   . HIS A 1 23  ? 189.773 142.091 164.794 1.00 201.21 ? 23   HIS A ND1   1 
ATOM   8     C  CD2   . HIS A 1 23  ? 191.140 143.623 164.050 1.00 199.03 ? 23   HIS A CD2   1 
ATOM   9     C  CE1   . HIS A 1 23  ? 190.368 141.597 163.723 1.00 199.52 ? 23   HIS A CE1   1 
ATOM   10    N  NE2   . HIS A 1 23  ? 191.203 142.507 163.253 1.00 198.93 ? 23   HIS A NE2   1 
ATOM   11    N  N     . ALA A 1 24  ? 188.841 147.265 166.777 1.00 188.34 ? 24   ALA A N     1 
ATOM   12    C  CA    . ALA A 1 24  ? 188.619 148.333 167.751 1.00 183.44 ? 24   ALA A CA    1 
ATOM   13    C  C     . ALA A 1 24  ? 187.153 148.737 167.861 1.00 181.72 ? 24   ALA A C     1 
ATOM   14    O  O     . ALA A 1 24  ? 186.645 148.814 168.993 1.00 181.01 ? 24   ALA A O     1 
ATOM   15    C  CB    . ALA A 1 24  ? 189.512 149.533 167.415 1.00 178.23 ? 24   ALA A CB    1 
ATOM   16    N  N     . PRO A 1 25  ? 186.419 149.013 166.772 1.00 181.39 ? 25   PRO A N     1 
ATOM   17    C  CA    . PRO A 1 25  ? 184.987 149.325 166.941 1.00 180.37 ? 25   PRO A CA    1 
ATOM   18    C  C     . PRO A 1 25  ? 184.169 148.154 167.459 1.00 178.22 ? 25   PRO A C     1 
ATOM   19    O  O     . PRO A 1 25  ? 183.190 148.366 168.186 1.00 178.25 ? 25   PRO A O     1 
ATOM   20    C  CB    . PRO A 1 25  ? 184.554 149.750 165.532 1.00 177.86 ? 25   PRO A CB    1 
ATOM   21    C  CG    . PRO A 1 25  ? 185.482 149.051 164.633 1.00 178.94 ? 25   PRO A CG    1 
ATOM   22    C  CD    . PRO A 1 25  ? 186.802 149.002 165.347 1.00 179.45 ? 25   PRO A CD    1 
ATOM   23    N  N     . ARG A 1 26  ? 184.537 146.918 167.102 1.00 173.52 ? 26   ARG A N     1 
ATOM   24    C  CA    . ARG A 1 26  ? 183.859 145.747 167.656 1.00 167.74 ? 26   ARG A CA    1 
ATOM   25    C  C     . ARG A 1 26  ? 184.033 145.672 169.166 1.00 171.31 ? 26   ARG A C     1 
ATOM   26    O  O     . ARG A 1 26  ? 183.062 145.458 169.904 1.00 169.32 ? 26   ARG A O     1 
ATOM   27    C  CB    . ARG A 1 26  ? 184.379 144.473 166.980 1.00 163.56 ? 26   ARG A CB    1 
ATOM   28    C  CG    . ARG A 1 26  ? 183.563 143.182 167.202 1.00 154.94 ? 26   ARG A CG    1 
ATOM   29    C  CD    . ARG A 1 26  ? 182.060 143.361 167.391 1.00 150.90 ? 26   ARG A CD    1 
ATOM   30    N  NE    . ARG A 1 26  ? 181.439 144.347 166.511 1.00 148.78 ? 26   ARG A NE    1 
ATOM   31    C  CZ    . ARG A 1 26  ? 181.094 144.114 165.254 1.00 142.05 ? 26   ARG A CZ    1 
ATOM   32    N  NH1   . ARG A 1 26  ? 181.325 142.946 164.679 1.00 135.42 ? 26   ARG A NH1   1 
ATOM   33    N  NH2   . ARG A 1 26  ? 180.482 145.071 164.564 1.00 141.23 ? 26   ARG A NH2   1 
ATOM   34    N  N     . SER A 1 27  ? 185.266 145.846 169.641 1.00 174.16 ? 27   SER A N     1 
ATOM   35    C  CA    . SER A 1 27  ? 185.507 145.871 171.078 1.00 173.07 ? 27   SER A CA    1 
ATOM   36    C  C     . SER A 1 27  ? 184.763 147.023 171.736 1.00 175.16 ? 27   SER A C     1 
ATOM   37    O  O     . SER A 1 27  ? 184.230 146.874 172.840 1.00 178.10 ? 27   SER A O     1 
ATOM   38    C  CB    . SER A 1 27  ? 187.004 145.971 171.362 1.00 177.53 ? 27   SER A CB    1 
ATOM   39    O  OG    . SER A 1 27  ? 187.248 146.090 172.752 1.00 180.28 ? 27   SER A OG    1 
ATOM   40    N  N     . SER A 1 28  ? 184.716 148.180 171.072 1.00 175.33 ? 28   SER A N     1 
ATOM   41    C  CA    . SER A 1 28  ? 183.997 149.321 171.628 1.00 175.41 ? 28   SER A CA    1 
ATOM   42    C  C     . SER A 1 28  ? 182.517 149.008 171.809 1.00 176.39 ? 28   SER A C     1 
ATOM   43    O  O     . SER A 1 28  ? 181.945 149.272 172.872 1.00 179.26 ? 28   SER A O     1 
ATOM   44    C  CB    . SER A 1 28  ? 184.181 150.542 170.727 1.00 175.43 ? 28   SER A CB    1 
ATOM   45    O  OG    . SER A 1 28  ? 183.594 151.696 171.301 1.00 179.31 ? 28   SER A OG    1 
ATOM   46    N  N     . MET A 1 29  ? 181.885 148.427 170.787 1.00 174.32 ? 29   MET A N     1 
ATOM   47    C  CA    . MET A 1 29  ? 180.461 148.116 170.886 1.00 172.92 ? 29   MET A CA    1 
ATOM   48    C  C     . MET A 1 29  ? 180.193 147.033 171.924 1.00 174.14 ? 29   MET A C     1 
ATOM   49    O  O     . MET A 1 29  ? 179.224 147.125 172.690 1.00 174.55 ? 29   MET A O     1 
ATOM   50    C  CB    . MET A 1 29  ? 179.907 147.685 169.533 1.00 162.97 ? 29   MET A CB    1 
ATOM   51    C  CG    . MET A 1 29  ? 178.466 147.218 169.624 1.00 155.16 ? 29   MET A CG    1 
ATOM   52    S  SD    . MET A 1 29  ? 177.883 146.301 168.194 1.00 144.35 ? 29   MET A SD    1 
ATOM   53    C  CE    . MET A 1 29  ? 176.123 146.289 168.520 1.00 123.51 ? 29   MET A CE    1 
ATOM   54    N  N     . MET A 1 30  ? 181.028 145.994 171.965 1.00 173.01 ? 30   MET A N     1 
ATOM   55    C  CA    . MET A 1 30  ? 180.788 144.928 172.930 1.00 170.38 ? 30   MET A CA    1 
ATOM   56    C  C     . MET A 1 30  ? 181.028 145.418 174.353 1.00 176.52 ? 30   MET A C     1 
ATOM   57    O  O     . MET A 1 30  ? 180.340 144.994 175.287 1.00 179.00 ? 30   MET A O     1 
ATOM   58    C  CB    . MET A 1 30  ? 181.658 143.716 172.606 1.00 168.67 ? 30   MET A CB    1 
ATOM   59    C  CG    . MET A 1 30  ? 181.110 142.874 171.461 1.00 164.30 ? 30   MET A CG    1 
ATOM   60    S  SD    . MET A 1 30  ? 179.334 142.596 171.607 1.00 158.16 ? 30   MET A SD    1 
ATOM   61    C  CE    . MET A 1 30  ? 178.994 141.665 170.116 1.00 124.53 ? 30   MET A CE    1 
ATOM   62    N  N     . SER A 1 31  ? 181.979 146.337 174.538 1.00 179.32 ? 31   SER A N     1 
ATOM   63    C  CA    . SER A 1 31  ? 182.171 146.940 175.852 1.00 181.54 ? 31   SER A CA    1 
ATOM   64    C  C     . SER A 1 31  ? 180.998 147.840 176.218 1.00 184.28 ? 31   SER A C     1 
ATOM   65    O  O     . SER A 1 31  ? 180.622 147.934 177.391 1.00 188.82 ? 31   SER A O     1 
ATOM   66    C  CB    . SER A 1 31  ? 183.483 147.721 175.885 1.00 182.58 ? 31   SER A CB    1 
ATOM   67    O  OG    . SER A 1 31  ? 184.593 146.859 175.704 1.00 182.16 ? 31   SER A OG    1 
ATOM   68    N  N     . VAL A 1 32  ? 180.413 148.519 175.228 1.00 183.31 ? 32   VAL A N     1 
ATOM   69    C  CA    . VAL A 1 32  ? 179.206 149.301 175.483 1.00 187.03 ? 32   VAL A CA    1 
ATOM   70    C  C     . VAL A 1 32  ? 178.079 148.392 175.954 1.00 188.53 ? 32   VAL A C     1 
ATOM   71    O  O     . VAL A 1 32  ? 177.357 148.709 176.907 1.00 191.73 ? 32   VAL A O     1 
ATOM   72    C  CB    . VAL A 1 32  ? 178.808 150.097 174.226 1.00 184.81 ? 32   VAL A CB    1 
ATOM   73    C  CG1   . VAL A 1 32  ? 177.342 150.498 174.288 1.00 181.99 ? 32   VAL A CG1   1 
ATOM   74    C  CG2   . VAL A 1 32  ? 179.695 151.323 174.075 1.00 184.49 ? 32   VAL A CG2   1 
ATOM   75    N  N     . GLU A 1 33  ? 177.914 147.243 175.297 1.00 183.80 ? 33   GLU A N     1 
ATOM   76    C  CA    . GLU A 1 33  ? 176.899 146.286 175.730 1.00 180.26 ? 33   GLU A CA    1 
ATOM   77    C  C     . GLU A 1 33  ? 177.204 145.749 177.124 1.00 187.65 ? 33   GLU A C     1 
ATOM   78    O  O     . GLU A 1 33  ? 176.291 145.551 177.934 1.00 188.48 ? 33   GLU A O     1 
ATOM   79    C  CB    . GLU A 1 33  ? 176.791 145.140 174.725 1.00 170.52 ? 33   GLU A CB    1 
ATOM   80    C  CG    . GLU A 1 33  ? 176.223 145.552 173.382 1.00 164.65 ? 33   GLU A CG    1 
ATOM   81    C  CD    . GLU A 1 33  ? 175.282 144.514 172.813 1.00 149.51 ? 33   GLU A CD    1 
ATOM   82    O  OE1   . GLU A 1 33  ? 174.721 144.750 171.724 1.00 141.57 ? 33   GLU A OE1   1 
ATOM   83    O  OE2   . GLU A 1 33  ? 175.104 143.460 173.455 1.00 146.46 ? 33   GLU A OE2   1 
ATOM   84    N  N     . TYR A 1 34  ? 178.482 145.504 177.420 1.00 191.72 ? 34   TYR A N     1 
ATOM   85    C  CA    . TYR A 1 34  ? 178.865 145.043 178.751 1.00 197.32 ? 34   TYR A CA    1 
ATOM   86    C  C     . TYR A 1 34  ? 178.529 146.082 179.814 1.00 200.00 ? 34   TYR A C     1 
ATOM   87    O  O     . TYR A 1 34  ? 178.052 145.738 180.901 1.00 201.22 ? 34   TYR A O     1 
ATOM   88    C  CB    . TYR A 1 34  ? 180.357 144.706 178.778 1.00 198.92 ? 34   TYR A CB    1 
ATOM   89    C  CG    . TYR A 1 34  ? 180.851 144.179 180.108 1.00 206.97 ? 34   TYR A CG    1 
ATOM   90    C  CD1   . TYR A 1 34  ? 180.650 142.854 180.471 1.00 210.17 ? 34   TYR A CD1   1 
ATOM   91    C  CD2   . TYR A 1 34  ? 181.527 145.006 180.997 1.00 209.22 ? 34   TYR A CD2   1 
ATOM   92    C  CE1   . TYR A 1 34  ? 181.102 142.368 181.685 1.00 213.43 ? 34   TYR A CE1   1 
ATOM   93    C  CE2   . TYR A 1 34  ? 181.983 144.530 182.212 1.00 213.90 ? 34   TYR A CE2   1 
ATOM   94    C  CZ    . TYR A 1 34  ? 181.767 143.210 182.551 1.00 216.95 ? 34   TYR A CZ    1 
ATOM   95    O  OH    . TYR A 1 34  ? 182.219 142.731 183.760 1.00 222.01 ? 34   TYR A OH    1 
ATOM   96    N  N     . ASP A 1 35  ? 178.778 147.360 179.520 1.00 199.13 ? 35   ASP A N     1 
ATOM   97    C  CA    . ASP A 1 35  ? 178.447 148.418 180.468 1.00 200.36 ? 35   ASP A CA    1 
ATOM   98    C  C     . ASP A 1 35  ? 176.942 148.607 180.591 1.00 199.50 ? 35   ASP A C     1 
ATOM   99    O  O     . ASP A 1 35  ? 176.456 149.038 181.643 1.00 201.26 ? 35   ASP A O     1 
ATOM   100   C  CB    . ASP A 1 35  ? 179.114 149.729 180.053 1.00 200.70 ? 35   ASP A CB    1 
ATOM   101   C  CG    . ASP A 1 35  ? 179.260 150.700 181.208 1.00 205.11 ? 35   ASP A CG    1 
ATOM   102   O  OD1   . ASP A 1 35  ? 179.023 150.289 182.364 1.00 205.97 ? 35   ASP A OD1   1 
ATOM   103   O  OD2   . ASP A 1 35  ? 179.611 151.873 180.962 1.00 206.66 ? 35   ASP A OD2   1 
ATOM   104   N  N     . GLY A 1 36  ? 176.192 148.305 179.531 1.00 195.01 ? 36   GLY A N     1 
ATOM   105   C  CA    . GLY A 1 36  ? 174.744 148.330 179.608 1.00 194.91 ? 36   GLY A CA    1 
ATOM   106   C  C     . GLY A 1 36  ? 174.118 147.094 180.215 1.00 198.69 ? 36   GLY A C     1 
ATOM   107   O  O     . GLY A 1 36  ? 172.911 147.089 180.477 1.00 196.91 ? 36   GLY A O     1 
ATOM   108   N  N     . ILE A 1 37  ? 174.911 146.043 180.431 1.00 199.70 ? 37   ILE A N     1 
ATOM   109   C  CA    . ILE A 1 37  ? 174.382 144.826 181.054 1.00 199.01 ? 37   ILE A CA    1 
ATOM   110   C  C     . ILE A 1 37  ? 173.882 145.070 182.472 1.00 199.15 ? 37   ILE A C     1 
ATOM   111   O  O     . ILE A 1 37  ? 172.751 144.653 182.783 1.00 199.17 ? 37   ILE A O     1 
ATOM   112   C  CB    . ILE A 1 37  ? 175.427 143.699 180.978 1.00 199.35 ? 37   ILE A CB    1 
ATOM   113   C  CG1   . ILE A 1 37  ? 175.296 142.934 179.660 1.00 197.09 ? 37   ILE A CG1   1 
ATOM   114   C  CG2   . ILE A 1 37  ? 175.285 142.743 182.157 1.00 198.61 ? 37   ILE A CG2   1 
ATOM   115   C  CD1   . ILE A 1 37  ? 174.017 142.129 179.546 1.00 184.28 ? 37   ILE A CD1   1 
ATOM   116   N  N     . PRO A 1 38  ? 174.635 145.707 183.378 1.00 201.89 ? 38   PRO A N     1 
ATOM   117   C  CA    . PRO A 1 38  ? 174.145 145.856 184.753 1.00 201.71 ? 38   PRO A CA    1 
ATOM   118   C  C     . PRO A 1 38  ? 172.868 146.682 184.816 1.00 199.99 ? 38   PRO A C     1 
ATOM   119   O  O     . PRO A 1 38  ? 172.697 147.654 184.077 1.00 192.50 ? 38   PRO A O     1 
ATOM   120   C  CB    . PRO A 1 38  ? 175.304 146.557 185.474 1.00 201.36 ? 38   PRO A CB    1 
ATOM   121   C  CG    . PRO A 1 38  ? 176.092 147.198 184.397 1.00 201.63 ? 38   PRO A CG    1 
ATOM   122   C  CD    . PRO A 1 38  ? 175.997 146.259 183.242 1.00 202.40 ? 38   PRO A CD    1 
ATOM   123   N  N     . LEU A 1 39  ? 171.977 146.279 185.719 1.00 202.36 ? 39   LEU A N     1 
ATOM   124   C  CA    . LEU A 1 39  ? 170.691 146.939 185.940 1.00 199.31 ? 39   LEU A CA    1 
ATOM   125   C  C     . LEU A 1 39  ? 169.904 147.115 184.645 1.00 194.35 ? 39   LEU A C     1 
ATOM   126   O  O     . LEU A 1 39  ? 169.940 148.176 184.021 1.00 190.87 ? 39   LEU A O     1 
ATOM   127   C  CB    . LEU A 1 39  ? 170.895 148.295 186.619 1.00 197.71 ? 39   LEU A CB    1 
ATOM   128   C  CG    . LEU A 1 39  ? 169.660 148.881 187.306 1.00 191.72 ? 39   LEU A CG    1 
ATOM   129   C  CD1   . LEU A 1 39  ? 169.170 147.955 188.407 1.00 186.16 ? 39   LEU A CD1   1 
ATOM   130   C  CD2   . LEU A 1 39  ? 169.963 150.264 187.859 1.00 190.06 ? 39   LEU A CD2   1 
ATOM   131   N  N     . THR A 1 54  ? 169.356 135.843 184.396 1.00 171.43 ? 54   THR A N     1 
ATOM   132   C  CA    . THR A 1 54  ? 169.511 134.541 183.757 1.00 166.77 ? 54   THR A CA    1 
ATOM   133   C  C     . THR A 1 54  ? 169.657 133.487 184.845 1.00 170.07 ? 54   THR A C     1 
ATOM   134   O  O     . THR A 1 54  ? 170.529 133.604 185.713 1.00 172.81 ? 54   THR A O     1 
ATOM   135   C  CB    . THR A 1 54  ? 170.720 134.523 182.823 1.00 164.33 ? 54   THR A CB    1 
ATOM   136   O  OG1   . THR A 1 54  ? 170.507 135.444 181.746 1.00 160.86 ? 54   THR A OG1   1 
ATOM   137   C  CG2   . THR A 1 54  ? 170.932 133.128 182.251 1.00 160.09 ? 54   THR A CG2   1 
ATOM   138   N  N     . SER A 1 55  ? 168.811 132.460 184.796 1.00 167.61 ? 55   SER A N     1 
ATOM   139   C  CA    . SER A 1 55  ? 168.760 131.450 185.840 1.00 171.59 ? 55   SER A CA    1 
ATOM   140   C  C     . SER A 1 55  ? 168.743 130.058 185.228 1.00 168.47 ? 55   SER A C     1 
ATOM   141   O  O     . SER A 1 55  ? 168.296 129.860 184.096 1.00 160.78 ? 55   SER A O     1 
ATOM   142   C  CB    . SER A 1 55  ? 167.526 131.631 186.736 1.00 169.96 ? 55   SER A CB    1 
ATOM   143   O  OG    . SER A 1 55  ? 167.503 132.921 187.322 1.00 169.74 ? 55   SER A OG    1 
ATOM   144   N  N     . ILE A 1 91  ? 135.782 149.857 195.964 1.00 201.90 ? 91   ILE A N     1 
ATOM   145   C  CA    . ILE A 1 91  ? 134.693 150.459 195.199 1.00 194.47 ? 91   ILE A CA    1 
ATOM   146   C  C     . ILE A 1 91  ? 134.635 149.785 193.832 1.00 189.81 ? 91   ILE A C     1 
ATOM   147   O  O     . ILE A 1 91  ? 135.581 149.932 193.043 1.00 190.92 ? 91   ILE A O     1 
ATOM   148   C  CB    . ILE A 1 91  ? 134.875 151.977 195.057 1.00 193.28 ? 91   ILE A CB    1 
ATOM   149   C  CG1   . ILE A 1 91  ? 136.357 152.330 194.903 1.00 197.64 ? 91   ILE A CG1   1 
ATOM   150   C  CG2   . ILE A 1 91  ? 134.280 152.696 196.258 1.00 190.35 ? 91   ILE A CG2   1 
ATOM   151   C  CD1   . ILE A 1 91  ? 136.617 153.810 194.740 1.00 196.20 ? 91   ILE A CD1   1 
ATOM   152   N  N     . PRO A 1 92  ? 133.576 149.052 193.513 1.00 185.00 ? 92   PRO A N     1 
ATOM   153   C  CA    . PRO A 1 92  ? 133.436 148.459 192.180 1.00 176.81 ? 92   PRO A CA    1 
ATOM   154   C  C     . PRO A 1 92  ? 133.151 149.533 191.135 1.00 173.54 ? 92   PRO A C     1 
ATOM   155   O  O     . PRO A 1 92  ? 133.044 150.721 191.435 1.00 175.10 ? 92   PRO A O     1 
ATOM   156   C  CB    . PRO A 1 92  ? 132.245 147.509 192.341 1.00 171.93 ? 92   PRO A CB    1 
ATOM   157   C  CG    . PRO A 1 92  ? 132.157 147.246 193.811 1.00 177.80 ? 92   PRO A CG    1 
ATOM   158   C  CD    . PRO A 1 92  ? 132.571 148.533 194.454 1.00 183.68 ? 92   PRO A CD    1 
ATOM   159   N  N     . SER A 1 93  ? 133.022 149.090 189.885 1.00 167.21 ? 93   SER A N     1 
ATOM   160   C  CA    . SER A 1 93  ? 132.730 149.982 188.773 1.00 162.43 ? 93   SER A CA    1 
ATOM   161   C  C     . SER A 1 93  ? 131.657 149.360 187.892 1.00 162.79 ? 93   SER A C     1 
ATOM   162   O  O     . SER A 1 93  ? 131.541 148.136 187.789 1.00 165.76 ? 93   SER A O     1 
ATOM   163   C  CB    . SER A 1 93  ? 133.984 150.281 187.942 1.00 158.31 ? 93   SER A CB    1 
ATOM   164   O  OG    . SER A 1 93  ? 133.675 151.123 186.846 1.00 156.59 ? 93   SER A OG    1 
ATOM   165   N  N     . VAL A 1 94  ? 130.866 150.224 187.251 1.00 158.76 ? 94   VAL A N     1 
ATOM   166   C  CA    . VAL A 1 94  ? 129.794 149.740 186.384 1.00 153.78 ? 94   VAL A CA    1 
ATOM   167   C  C     . VAL A 1 94  ? 130.371 149.051 185.153 1.00 154.12 ? 94   VAL A C     1 
ATOM   168   O  O     . VAL A 1 94  ? 129.812 148.065 184.657 1.00 156.05 ? 94   VAL A O     1 
ATOM   169   C  CB    . VAL A 1 94  ? 128.832 150.889 186.018 1.00 149.40 ? 94   VAL A CB    1 
ATOM   170   C  CG1   . VAL A 1 94  ? 129.386 151.749 184.895 1.00 153.10 ? 94   VAL A CG1   1 
ATOM   171   C  CG2   . VAL A 1 94  ? 127.470 150.333 185.641 1.00 146.81 ? 94   VAL A CG2   1 
ATOM   172   N  N     . GLU A 1 95  ? 131.503 149.547 184.645 1.00 152.85 ? 95   GLU A N     1 
ATOM   173   C  CA    . GLU A 1 95  ? 132.154 148.879 183.524 1.00 152.60 ? 95   GLU A CA    1 
ATOM   174   C  C     . GLU A 1 95  ? 132.657 147.501 183.929 1.00 155.00 ? 95   GLU A C     1 
ATOM   175   O  O     . GLU A 1 95  ? 132.537 146.536 183.164 1.00 152.49 ? 95   GLU A O     1 
ATOM   176   C  CB    . GLU A 1 95  ? 133.302 149.738 182.992 1.00 150.97 ? 95   GLU A CB    1 
ATOM   177   C  CG    . GLU A 1 95  ? 134.235 149.083 181.953 1.00 155.71 ? 95   GLU A CG    1 
ATOM   178   C  CD    . GLU A 1 95  ? 133.541 148.364 180.789 1.00 159.22 ? 95   GLU A CD    1 
ATOM   179   O  OE1   . GLU A 1 95  ? 132.297 148.341 180.693 1.00 158.49 ? 95   GLU A OE1   1 
ATOM   180   O  OE2   . GLU A 1 95  ? 134.273 147.805 179.944 1.00 161.17 ? 95   GLU A OE2   1 
ATOM   181   N  N     . GLU A 1 96  ? 133.219 147.390 185.134 1.00 156.35 ? 96   GLU A N     1 
ATOM   182   C  CA    . GLU A 1 96  ? 133.638 146.089 185.642 1.00 156.02 ? 96   GLU A CA    1 
ATOM   183   C  C     . GLU A 1 96  ? 132.449 145.149 185.782 1.00 151.67 ? 96   GLU A C     1 
ATOM   184   O  O     . GLU A 1 96  ? 132.545 143.962 185.449 1.00 152.50 ? 96   GLU A O     1 
ATOM   185   C  CB    . GLU A 1 96  ? 134.351 146.256 186.984 1.00 160.47 ? 96   GLU A CB    1 
ATOM   186   C  CG    . GLU A 1 96  ? 134.851 144.956 187.591 1.00 161.21 ? 96   GLU A CG    1 
ATOM   187   C  CD    . GLU A 1 96  ? 134.733 144.937 189.104 1.00 165.37 ? 96   GLU A CD    1 
ATOM   188   O  OE1   . GLU A 1 96  ? 134.825 146.019 189.723 1.00 166.28 ? 96   GLU A OE1   1 
ATOM   189   O  OE2   . GLU A 1 96  ? 134.545 143.842 189.673 1.00 163.99 ? 96   GLU A OE2   1 
ATOM   190   N  N     . ALA A 1 97  ? 131.319 145.661 186.274 1.00 146.72 ? 97   ALA A N     1 
ATOM   191   C  CA    . ALA A 1 97  ? 130.129 144.827 186.408 1.00 145.17 ? 97   ALA A CA    1 
ATOM   192   C  C     . ALA A 1 97  ? 129.646 144.332 185.051 1.00 147.97 ? 97   ALA A C     1 
ATOM   193   O  O     . ALA A 1 97  ? 129.319 143.149 184.893 1.00 151.38 ? 97   ALA A O     1 
ATOM   194   C  CB    . ALA A 1 97  ? 129.023 145.601 187.122 1.00 144.31 ? 97   ALA A CB    1 
ATOM   195   N  N     . LEU A 1 98  ? 129.601 145.222 184.057 1.00 148.12 ? 98   LEU A N     1 
ATOM   196   C  CA    . LEU A 1 98  ? 129.174 144.817 182.721 1.00 145.95 ? 98   LEU A CA    1 
ATOM   197   C  C     . LEU A 1 98  ? 130.121 143.784 182.124 1.00 147.24 ? 98   LEU A C     1 
ATOM   198   O  O     . LEU A 1 98  ? 129.675 142.799 181.523 1.00 148.85 ? 98   LEU A O     1 
ATOM   199   C  CB    . LEU A 1 98  ? 129.070 146.039 181.808 1.00 143.48 ? 98   LEU A CB    1 
ATOM   200   C  CG    . LEU A 1 98  ? 127.913 147.003 182.067 1.00 140.59 ? 98   LEU A CG    1 
ATOM   201   C  CD1   . LEU A 1 98  ? 127.964 148.171 181.100 1.00 145.37 ? 98   LEU A CD1   1 
ATOM   202   C  CD2   . LEU A 1 98  ? 126.594 146.275 181.939 1.00 132.97 ? 98   LEU A CD2   1 
ATOM   203   N  N     . SER A 1 99  ? 131.431 143.987 182.282 1.00 146.69 ? 99   SER A N     1 
ATOM   204   C  CA    . SER A 1 99  ? 132.393 143.031 181.743 1.00 147.94 ? 99   SER A CA    1 
ATOM   205   C  C     . SER A 1 99  ? 132.269 141.674 182.425 1.00 147.51 ? 99   SER A C     1 
ATOM   206   O  O     . SER A 1 99  ? 132.333 140.631 181.764 1.00 147.30 ? 99   SER A O     1 
ATOM   207   C  CB    . SER A 1 99  ? 133.812 143.577 181.888 1.00 149.11 ? 99   SER A CB    1 
ATOM   208   O  OG    . SER A 1 99  ? 134.643 143.114 180.839 1.00 149.56 ? 99   SER A OG    1 
ATOM   209   N  N     . THR A 1 100 ? 132.093 141.666 183.749 1.00 146.04 ? 100  THR A N     1 
ATOM   210   C  CA    . THR A 1 100 ? 131.944 140.402 184.460 1.00 144.68 ? 100  THR A CA    1 
ATOM   211   C  C     . THR A 1 100 ? 130.668 139.684 184.045 1.00 145.09 ? 100  THR A C     1 
ATOM   212   O  O     . THR A 1 100 ? 130.659 138.458 183.898 1.00 146.62 ? 100  THR A O     1 
ATOM   213   C  CB    . THR A 1 100 ? 131.959 140.634 185.970 1.00 146.16 ? 100  THR A CB    1 
ATOM   214   O  OG1   . THR A 1 100 ? 131.099 141.732 186.296 1.00 149.50 ? 100  THR A OG1   1 
ATOM   215   C  CG2   . THR A 1 100 ? 133.369 140.941 186.444 1.00 147.52 ? 100  THR A CG2   1 
ATOM   216   N  N     . LEU A 1 101 ? 129.577 140.428 183.849 1.00 143.81 ? 101  LEU A N     1 
ATOM   217   C  CA    . LEU A 1 101 ? 128.340 139.798 183.397 1.00 138.58 ? 101  LEU A CA    1 
ATOM   218   C  C     . LEU A 1 101 ? 128.490 139.235 181.989 1.00 141.35 ? 101  LEU A C     1 
ATOM   219   O  O     . LEU A 1 101 ? 127.958 138.162 181.682 1.00 143.20 ? 101  LEU A O     1 
ATOM   220   C  CB    . LEU A 1 101 ? 127.186 140.793 183.468 1.00 132.83 ? 101  LEU A CB    1 
ATOM   221   C  CG    . LEU A 1 101 ? 126.636 141.019 184.876 1.00 133.02 ? 101  LEU A CG    1 
ATOM   222   C  CD1   . LEU A 1 101 ? 125.372 141.849 184.831 1.00 136.50 ? 101  LEU A CD1   1 
ATOM   223   C  CD2   . LEU A 1 101 ? 126.379 139.693 185.562 1.00 134.90 ? 101  LEU A CD2   1 
ATOM   224   N  N     . ASP A 1 102 ? 129.208 139.945 181.116 1.00 143.36 ? 102  ASP A N     1 
ATOM   225   C  CA    . ASP A 1 102 ? 129.448 139.435 179.769 1.00 145.40 ? 102  ASP A CA    1 
ATOM   226   C  C     . ASP A 1 102 ? 130.274 138.153 179.827 1.00 146.79 ? 102  ASP A C     1 
ATOM   227   O  O     . ASP A 1 102 ? 129.980 137.177 179.122 1.00 147.20 ? 102  ASP A O     1 
ATOM   228   C  CB    . ASP A 1 102 ? 130.124 140.535 178.935 1.00 145.36 ? 102  ASP A CB    1 
ATOM   229   C  CG    . ASP A 1 102 ? 130.665 140.062 177.576 1.00 154.09 ? 102  ASP A CG    1 
ATOM   230   O  OD1   . ASP A 1 102 ? 130.986 138.877 177.359 1.00 156.71 ? 102  ASP A OD1   1 
ATOM   231   O  OD2   . ASP A 1 102 ? 130.770 140.930 176.685 1.00 157.44 ? 102  ASP A OD2   1 
ATOM   232   N  N     . ARG A 1 103 ? 131.304 138.132 180.675 1.00 145.25 ? 103  ARG A N     1 
ATOM   233   C  CA    . ARG A 1 103 ? 132.106 136.923 180.840 1.00 145.32 ? 103  ARG A CA    1 
ATOM   234   C  C     . ARG A 1 103 ? 131.265 135.777 181.388 1.00 143.22 ? 103  ARG A C     1 
ATOM   235   O  O     . ARG A 1 103 ? 131.440 134.621 180.988 1.00 144.07 ? 103  ARG A O     1 
ATOM   236   C  CB    . ARG A 1 103 ? 133.291 137.203 181.760 1.00 147.77 ? 103  ARG A CB    1 
ATOM   237   C  CG    . ARG A 1 103 ? 134.354 138.105 181.159 1.00 147.82 ? 103  ARG A CG    1 
ATOM   238   C  CD    . ARG A 1 103 ? 135.364 138.505 182.215 1.00 148.11 ? 103  ARG A CD    1 
ATOM   239   N  NE    . ARG A 1 103 ? 135.812 137.356 182.989 1.00 149.95 ? 103  ARG A NE    1 
ATOM   240   C  CZ    . ARG A 1 103 ? 136.365 137.433 184.192 1.00 150.46 ? 103  ARG A CZ    1 
ATOM   241   N  NH1   . ARG A 1 103 ? 136.541 138.595 184.798 1.00 148.55 ? 103  ARG A NH1   1 
ATOM   242   N  NH2   . ARG A 1 103 ? 136.747 136.315 184.803 1.00 152.66 ? 103  ARG A NH2   1 
ATOM   243   N  N     . ALA A 1 104 ? 130.357 136.079 182.317 1.00 141.40 ? 104  ALA A N     1 
ATOM   244   C  CA    . ALA A 1 104 ? 129.461 135.055 182.842 1.00 141.21 ? 104  ALA A CA    1 
ATOM   245   C  C     . ALA A 1 104 ? 128.560 134.501 181.750 1.00 140.93 ? 104  ALA A C     1 
ATOM   246   O  O     . ALA A 1 104 ? 128.308 133.293 181.695 1.00 145.47 ? 104  ALA A O     1 
ATOM   247   C  CB    . ALA A 1 104 ? 128.622 135.625 183.983 1.00 140.54 ? 104  ALA A CB    1 
ATOM   248   N  N     . ALA A 1 105 ? 128.052 135.375 180.880 1.00 138.80 ? 105  ALA A N     1 
ATOM   249   C  CA    . ALA A 1 105 ? 127.229 134.914 179.768 1.00 139.52 ? 105  ALA A CA    1 
ATOM   250   C  C     . ALA A 1 105 ? 128.026 134.009 178.838 1.00 142.33 ? 105  ALA A C     1 
ATOM   251   O  O     . ALA A 1 105 ? 127.521 132.979 178.379 1.00 144.73 ? 105  ALA A O     1 
ATOM   252   C  CB    . ALA A 1 105 ? 126.664 136.107 179.000 1.00 137.92 ? 105  ALA A CB    1 
ATOM   253   N  N     . ALA A 1 106 ? 129.277 134.376 178.555 1.00 142.05 ? 106  ALA A N     1 
ATOM   254   C  CA    . ALA A 1 106 ? 130.115 133.529 177.710 1.00 143.71 ? 106  ALA A CA    1 
ATOM   255   C  C     . ALA A 1 106 ? 130.369 132.173 178.362 1.00 143.26 ? 106  ALA A C     1 
ATOM   256   O  O     . ALA A 1 106 ? 130.295 131.130 177.699 1.00 144.05 ? 106  ALA A O     1 
ATOM   257   C  CB    . ALA A 1 106 ? 131.436 134.234 177.404 1.00 145.69 ? 106  ALA A CB    1 
ATOM   258   N  N     . ALA A 1 107 ? 130.662 132.169 179.664 1.00 141.04 ? 107  ALA A N     1 
ATOM   259   C  CA    . ALA A 1 107 ? 130.902 130.914 180.367 1.00 142.19 ? 107  ALA A CA    1 
ATOM   260   C  C     . ALA A 1 107 ? 129.658 130.036 180.369 1.00 142.34 ? 107  ALA A C     1 
ATOM   261   O  O     . ALA A 1 107 ? 129.748 128.817 180.186 1.00 146.24 ? 107  ALA A O     1 
ATOM   262   C  CB    . ALA A 1 107 ? 131.366 131.192 181.795 1.00 144.23 ? 107  ALA A CB    1 
ATOM   263   N  N     . LEU A 1 108 ? 128.486 130.639 180.579 1.00 139.00 ? 108  LEU A N     1 
ATOM   264   C  CA    . LEU A 1 108 ? 127.245 129.876 180.547 1.00 136.21 ? 108  LEU A CA    1 
ATOM   265   C  C     . LEU A 1 108 ? 126.971 129.335 179.150 1.00 140.29 ? 108  LEU A C     1 
ATOM   266   O  O     . LEU A 1 108 ? 126.443 128.227 179.008 1.00 143.62 ? 108  LEU A O     1 
ATOM   267   C  CB    . LEU A 1 108 ? 126.089 130.754 181.029 1.00 134.87 ? 108  LEU A CB    1 
ATOM   268   C  CG    . LEU A 1 108 ? 124.651 130.237 181.003 1.00 136.35 ? 108  LEU A CG    1 
ATOM   269   C  CD1   . LEU A 1 108 ? 124.566 128.782 181.437 1.00 138.50 ? 108  LEU A CD1   1 
ATOM   270   C  CD2   . LEU A 1 108 ? 123.772 131.110 181.875 1.00 138.06 ? 108  LEU A CD2   1 
ATOM   271   N  N     . ASN A 1 109 ? 127.328 130.095 178.113 1.00 142.18 ? 109  ASN A N     1 
ATOM   272   C  CA    . ASN A 1 109 ? 127.240 129.573 176.754 1.00 143.38 ? 109  ASN A CA    1 
ATOM   273   C  C     . ASN A 1 109 ? 128.174 128.388 176.557 1.00 144.06 ? 109  ASN A C     1 
ATOM   274   O  O     . ASN A 1 109 ? 127.855 127.464 175.801 1.00 144.95 ? 109  ASN A O     1 
ATOM   275   C  CB    . ASN A 1 109 ? 127.563 130.671 175.740 1.00 144.13 ? 109  ASN A CB    1 
ATOM   276   C  CG    . ASN A 1 109 ? 126.408 131.623 175.524 1.00 145.18 ? 109  ASN A CG    1 
ATOM   277   O  OD1   . ASN A 1 109 ? 125.252 131.278 175.757 1.00 145.09 ? 109  ASN A OD1   1 
ATOM   278   N  ND2   . ASN A 1 109 ? 126.717 132.831 175.068 1.00 145.40 ? 109  ASN A ND2   1 
ATOM   279   N  N     . ALA A 1 110 ? 129.323 128.395 177.226 1.00 143.54 ? 110  ALA A N     1 
ATOM   280   C  CA    . ALA A 1 110 ? 130.266 127.287 177.152 1.00 142.43 ? 110  ALA A CA    1 
ATOM   281   C  C     . ALA A 1 110 ? 129.918 126.146 178.099 1.00 145.56 ? 110  ALA A C     1 
ATOM   282   O  O     . ALA A 1 110 ? 130.649 125.151 178.138 1.00 145.25 ? 110  ALA A O     1 
ATOM   283   C  CB    . ALA A 1 110 ? 131.686 127.781 177.443 1.00 143.64 ? 110  ALA A CB    1 
ATOM   284   N  N     . ARG A 1 111 ? 128.828 126.269 178.859 1.00 150.62 ? 111  ARG A N     1 
ATOM   285   C  CA    . ARG A 1 111 ? 128.408 125.258 179.833 1.00 151.71 ? 111  ARG A CA    1 
ATOM   286   C  C     . ARG A 1 111 ? 129.504 124.980 180.860 1.00 150.40 ? 111  ARG A C     1 
ATOM   287   O  O     . ARG A 1 111 ? 129.967 123.850 181.026 1.00 153.11 ? 111  ARG A O     1 
ATOM   288   C  CB    . ARG A 1 111 ? 127.961 123.967 179.144 1.00 151.80 ? 111  ARG A CB    1 
ATOM   289   C  CG    . ARG A 1 111 ? 126.943 124.167 178.037 1.00 152.59 ? 111  ARG A CG    1 
ATOM   290   C  CD    . ARG A 1 111 ? 126.988 123.022 177.042 1.00 158.24 ? 111  ARG A CD    1 
ATOM   291   N  NE    . ARG A 1 111 ? 125.742 122.901 176.295 1.00 168.83 ? 111  ARG A NE    1 
ATOM   292   C  CZ    . ARG A 1 111 ? 124.689 122.206 176.705 1.00 169.23 ? 111  ARG A CZ    1 
ATOM   293   N  NH1   . ARG A 1 111 ? 124.692 121.566 177.863 1.00 165.84 ? 111  ARG A NH1   1 
ATOM   294   N  NH2   . ARG A 1 111 ? 123.607 122.153 175.935 1.00 169.38 ? 111  ARG A NH2   1 
ATOM   295   N  N     . ARG A 1 112 ? 129.922 126.035 181.553 1.00 148.59 ? 112  ARG A N     1 
ATOM   296   C  CA    . ARG A 1 112 ? 130.817 125.948 182.704 1.00 151.01 ? 112  ARG A CA    1 
ATOM   297   C  C     . ARG A 1 112 ? 130.058 126.587 183.860 1.00 152.66 ? 112  ARG A C     1 
ATOM   298   O  O     . ARG A 1 112 ? 130.213 127.778 184.134 1.00 154.51 ? 112  ARG A O     1 
ATOM   299   C  CB    . ARG A 1 112 ? 132.143 126.644 182.438 1.00 150.40 ? 112  ARG A CB    1 
ATOM   300   C  CG    . ARG A 1 112 ? 132.638 126.509 181.011 1.00 147.63 ? 112  ARG A CG    1 
ATOM   301   C  CD    . ARG A 1 112 ? 134.152 126.501 180.959 1.00 151.59 ? 112  ARG A CD    1 
ATOM   302   N  NE    . ARG A 1 112 ? 134.696 127.852 181.028 1.00 155.60 ? 112  ARG A NE    1 
ATOM   303   C  CZ    . ARG A 1 112 ? 135.111 128.545 179.978 1.00 155.04 ? 112  ARG A CZ    1 
ATOM   304   N  NH1   . ARG A 1 112 ? 135.066 128.042 178.755 1.00 152.01 ? 112  ARG A NH1   1 
ATOM   305   N  NH2   . ARG A 1 112 ? 135.583 129.775 180.158 1.00 155.21 ? 112  ARG A NH2   1 
ATOM   306   N  N     . TYR A 1 113 ? 129.238 125.785 184.537 1.00 148.48 ? 113  TYR A N     1 
ATOM   307   C  CA    . TYR A 1 113 ? 128.254 126.340 185.457 1.00 151.80 ? 113  TYR A CA    1 
ATOM   308   C  C     . TYR A 1 113 ? 128.873 126.890 186.735 1.00 153.52 ? 113  TYR A C     1 
ATOM   309   O  O     . TYR A 1 113 ? 128.366 127.876 187.273 1.00 155.00 ? 113  TYR A O     1 
ATOM   310   C  CB    . TYR A 1 113 ? 127.193 125.289 185.776 1.00 153.70 ? 113  TYR A CB    1 
ATOM   311   C  CG    . TYR A 1 113 ? 126.374 124.911 184.566 1.00 153.99 ? 113  TYR A CG    1 
ATOM   312   C  CD1   . TYR A 1 113 ? 125.335 125.721 184.132 1.00 153.80 ? 113  TYR A CD1   1 
ATOM   313   C  CD2   . TYR A 1 113 ? 126.650 123.759 183.847 1.00 155.41 ? 113  TYR A CD2   1 
ATOM   314   C  CE1   . TYR A 1 113 ? 124.586 125.388 183.022 1.00 154.87 ? 113  TYR A CE1   1 
ATOM   315   C  CE2   . TYR A 1 113 ? 125.906 123.417 182.735 1.00 155.76 ? 113  TYR A CE2   1 
ATOM   316   C  CZ    . TYR A 1 113 ? 124.876 124.236 182.328 1.00 154.82 ? 113  TYR A CZ    1 
ATOM   317   O  OH    . TYR A 1 113 ? 124.131 123.901 181.222 1.00 155.30 ? 113  TYR A OH    1 
ATOM   318   N  N     . ARG A 1 114 ? 129.957 126.297 187.235 1.00 153.90 ? 114  ARG A N     1 
ATOM   319   C  CA    . ARG A 1 114 ? 130.603 126.854 188.421 1.00 156.70 ? 114  ARG A CA    1 
ATOM   320   C  C     . ARG A 1 114 ? 131.145 128.253 188.147 1.00 154.95 ? 114  ARG A C     1 
ATOM   321   O  O     . ARG A 1 114 ? 130.877 129.198 188.904 1.00 155.32 ? 114  ARG A O     1 
ATOM   322   C  CB    . ARG A 1 114 ? 131.719 125.925 188.900 1.00 167.63 ? 114  ARG A CB    1 
ATOM   323   C  CG    . ARG A 1 114 ? 131.324 125.032 190.065 1.00 171.21 ? 114  ARG A CG    1 
ATOM   324   C  CD    . ARG A 1 114 ? 130.329 123.966 189.646 1.00 166.18 ? 114  ARG A CD    1 
ATOM   325   N  NE    . ARG A 1 114 ? 129.855 123.194 190.788 1.00 170.93 ? 114  ARG A NE    1 
ATOM   326   C  CZ    . ARG A 1 114 ? 130.458 122.114 191.265 1.00 174.20 ? 114  ARG A CZ    1 
ATOM   327   N  NH1   . ARG A 1 114 ? 131.569 121.647 190.720 1.00 176.24 ? 114  ARG A NH1   1 
ATOM   328   N  NH2   . ARG A 1 114 ? 129.934 121.488 192.315 1.00 172.01 ? 114  ARG A NH2   1 
ATOM   329   N  N     . ASP A 1 115 ? 131.902 128.406 187.058 1.00 153.15 ? 115  ASP A N     1 
ATOM   330   C  CA    . ASP A 1 115 ? 132.428 129.718 186.700 1.00 154.53 ? 115  ASP A CA    1 
ATOM   331   C  C     . ASP A 1 115 ? 131.304 130.692 186.377 1.00 152.63 ? 115  ASP A C     1 
ATOM   332   O  O     . ASP A 1 115 ? 131.376 131.875 186.731 1.00 151.94 ? 115  ASP A O     1 
ATOM   333   C  CB    . ASP A 1 115 ? 133.384 129.595 185.515 1.00 154.79 ? 115  ASP A CB    1 
ATOM   334   C  CG    . ASP A 1 115 ? 134.233 128.346 185.585 1.00 160.08 ? 115  ASP A CG    1 
ATOM   335   O  OD1   . ASP A 1 115 ? 133.669 127.238 185.474 1.00 160.57 ? 115  ASP A OD1   1 
ATOM   336   O  OD2   . ASP A 1 115 ? 135.464 128.470 185.756 1.00 165.52 ? 115  ASP A OD2   1 
ATOM   337   N  N     . ALA A 1 116 ? 130.262 130.215 185.693 1.00 148.84 ? 116  ALA A N     1 
ATOM   338   C  CA    . ALA A 1 116 ? 129.131 131.078 185.379 1.00 143.59 ? 116  ALA A CA    1 
ATOM   339   C  C     . ALA A 1 116 ? 128.459 131.584 186.646 1.00 142.90 ? 116  ALA A C     1 
ATOM   340   O  O     . ALA A 1 116 ? 128.141 132.772 186.753 1.00 145.66 ? 116  ALA A O     1 
ATOM   341   C  CB    . ALA A 1 116 ? 128.129 130.333 184.500 1.00 144.33 ? 116  ALA A CB    1 
ATOM   342   N  N     . LEU A 1 117 ? 128.248 130.701 187.624 1.00 141.34 ? 117  LEU A N     1 
ATOM   343   C  CA    . LEU A 1 117 ? 127.648 131.116 188.885 1.00 140.70 ? 117  LEU A CA    1 
ATOM   344   C  C     . LEU A 1 117 ? 128.530 132.123 189.607 1.00 145.20 ? 117  LEU A C     1 
ATOM   345   O  O     . LEU A 1 117 ? 128.034 133.132 190.124 1.00 151.20 ? 117  LEU A O     1 
ATOM   346   C  CB    . LEU A 1 117 ? 127.394 129.898 189.771 1.00 143.11 ? 117  LEU A CB    1 
ATOM   347   C  CG    . LEU A 1 117 ? 126.913 130.192 191.191 1.00 147.35 ? 117  LEU A CG    1 
ATOM   348   C  CD1   . LEU A 1 117 ? 125.614 130.977 191.162 1.00 147.51 ? 117  LEU A CD1   1 
ATOM   349   C  CD2   . LEU A 1 117 ? 126.746 128.904 191.976 1.00 155.67 ? 117  LEU A CD2   1 
ATOM   350   N  N     . LYS A 1 118 ? 129.841 131.877 189.642 1.00 145.72 ? 118  LYS A N     1 
ATOM   351   C  CA    . LYS A 1 118 ? 130.739 132.800 190.332 1.00 147.63 ? 118  LYS A CA    1 
ATOM   352   C  C     . LYS A 1 118 ? 130.713 134.180 189.684 1.00 144.70 ? 118  LYS A C     1 
ATOM   353   O  O     . LYS A 1 118 ? 130.557 135.202 190.368 1.00 145.68 ? 118  LYS A O     1 
ATOM   354   C  CB    . LYS A 1 118 ? 132.160 132.241 190.345 1.00 149.03 ? 118  LYS A CB    1 
ATOM   355   C  CG    . LYS A 1 118 ? 133.154 133.121 191.084 1.00 152.67 ? 118  LYS A CG    1 
ATOM   356   C  CD    . LYS A 1 118 ? 134.519 132.464 191.174 1.00 156.02 ? 118  LYS A CD    1 
ATOM   357   C  CE    . LYS A 1 118 ? 135.120 132.259 189.795 1.00 152.68 ? 118  LYS A CE    1 
ATOM   358   N  NZ    . LYS A 1 118 ? 136.467 131.634 189.867 1.00 155.92 ? 118  LYS A NZ    1 
ATOM   359   N  N     . LEU A 1 119 ? 130.851 134.229 188.357 1.00 141.95 ? 119  LEU A N     1 
ATOM   360   C  CA    . LEU A 1 119 ? 130.890 135.513 187.667 1.00 140.99 ? 119  LEU A CA    1 
ATOM   361   C  C     . LEU A 1 119 ? 129.546 136.228 187.740 1.00 142.42 ? 119  LEU A C     1 
ATOM   362   O  O     . LEU A 1 119 ? 129.501 137.455 187.878 1.00 145.74 ? 119  LEU A O     1 
ATOM   363   C  CB    . LEU A 1 119 ? 131.323 135.320 186.216 1.00 137.94 ? 119  LEU A CB    1 
ATOM   364   C  CG    . LEU A 1 119 ? 132.718 134.735 186.012 1.00 140.46 ? 119  LEU A CG    1 
ATOM   365   C  CD1   . LEU A 1 119 ? 132.812 134.021 184.676 1.00 140.24 ? 119  LEU A CD1   1 
ATOM   366   C  CD2   . LEU A 1 119 ? 133.766 135.826 186.116 1.00 145.54 ? 119  LEU A CD2   1 
ATOM   367   N  N     . TYR A 1 120 ? 128.441 135.484 187.652 1.00 140.45 ? 120  TYR A N     1 
ATOM   368   C  CA    . TYR A 1 120 ? 127.128 136.105 187.768 1.00 138.02 ? 120  TYR A CA    1 
ATOM   369   C  C     . TYR A 1 120 ? 126.907 136.674 189.162 1.00 140.77 ? 120  TYR A C     1 
ATOM   370   O  O     . TYR A 1 120 ? 126.336 137.759 189.309 1.00 147.91 ? 120  TYR A O     1 
ATOM   371   C  CB    . TYR A 1 120 ? 126.040 135.093 187.414 1.00 136.72 ? 120  TYR A CB    1 
ATOM   372   C  CG    . TYR A 1 120 ? 125.680 135.062 185.949 1.00 135.11 ? 120  TYR A CG    1 
ATOM   373   C  CD1   . TYR A 1 120 ? 125.413 136.232 185.258 1.00 138.55 ? 120  TYR A CD1   1 
ATOM   374   C  CD2   . TYR A 1 120 ? 125.610 133.864 185.257 1.00 134.56 ? 120  TYR A CD2   1 
ATOM   375   C  CE1   . TYR A 1 120 ? 125.083 136.210 183.921 1.00 140.36 ? 120  TYR A CE1   1 
ATOM   376   C  CE2   . TYR A 1 120 ? 125.282 133.831 183.920 1.00 133.82 ? 120  TYR A CE2   1 
ATOM   377   C  CZ    . TYR A 1 120 ? 125.021 135.007 183.257 1.00 135.92 ? 120  TYR A CZ    1 
ATOM   378   O  OH    . TYR A 1 120 ? 124.693 134.981 181.922 1.00 133.14 ? 120  TYR A OH    1 
ATOM   379   N  N     . LEU A 1 121 ? 127.346 135.958 190.200 1.00 139.48 ? 121  LEU A N     1 
ATOM   380   C  CA    . LEU A 1 121 ? 127.238 136.487 191.556 1.00 141.40 ? 121  LEU A CA    1 
ATOM   381   C  C     . LEU A 1 121 ? 128.061 137.759 191.709 1.00 145.93 ? 121  LEU A C     1 
ATOM   382   O  O     . LEU A 1 121 ? 127.599 138.751 192.291 1.00 149.55 ? 121  LEU A O     1 
ATOM   383   C  CB    . LEU A 1 121 ? 127.683 135.431 192.566 1.00 140.69 ? 121  LEU A CB    1 
ATOM   384   C  CG    . LEU A 1 121 ? 126.578 134.528 193.114 1.00 144.29 ? 121  LEU A CG    1 
ATOM   385   C  CD1   . LEU A 1 121 ? 127.165 133.255 193.696 1.00 159.87 ? 121  LEU A CD1   1 
ATOM   386   C  CD2   . LEU A 1 121 ? 125.748 135.263 194.150 1.00 149.05 ? 121  LEU A CD2   1 
ATOM   387   N  N     . GLU A 1 122 ? 129.289 137.749 191.182 1.00 144.58 ? 122  GLU A N     1 
ATOM   388   C  CA    . GLU A 1 122 ? 130.126 138.942 191.257 1.00 144.71 ? 122  GLU A CA    1 
ATOM   389   C  C     . GLU A 1 122 ? 129.473 140.116 190.540 1.00 146.62 ? 122  GLU A C     1 
ATOM   390   O  O     . GLU A 1 122 ? 129.438 141.232 191.069 1.00 147.71 ? 122  GLU A O     1 
ATOM   391   C  CB    . GLU A 1 122 ? 131.507 138.659 190.669 1.00 146.20 ? 122  GLU A CB    1 
ATOM   392   C  CG    . GLU A 1 122 ? 132.343 137.695 191.487 1.00 152.64 ? 122  GLU A CG    1 
ATOM   393   C  CD    . GLU A 1 122 ? 133.686 137.408 190.848 1.00 160.34 ? 122  GLU A CD    1 
ATOM   394   O  OE1   . GLU A 1 122 ? 134.058 138.129 189.899 1.00 161.89 ? 122  GLU A OE1   1 
ATOM   395   O  OE2   . GLU A 1 122 ? 134.369 136.463 191.294 1.00 163.12 ? 122  GLU A OE2   1 
ATOM   396   N  N     . GLY A 1 123 ? 128.934 139.878 189.343 1.00 146.57 ? 123  GLY A N     1 
ATOM   397   C  CA    . GLY A 1 123 ? 128.280 140.948 188.609 1.00 144.33 ? 123  GLY A CA    1 
ATOM   398   C  C     . GLY A 1 123 ? 127.045 141.476 189.312 1.00 144.10 ? 123  GLY A C     1 
ATOM   399   O  O     . GLY A 1 123 ? 126.810 142.687 189.346 1.00 148.33 ? 123  GLY A O     1 
ATOM   400   N  N     . GLY A 1 124 ? 126.237 140.579 189.879 1.00 142.49 ? 124  GLY A N     1 
ATOM   401   C  CA    . GLY A 1 124 ? 125.048 141.017 190.589 1.00 142.98 ? 124  GLY A CA    1 
ATOM   402   C  C     . GLY A 1 124 ? 125.379 141.871 191.795 1.00 148.41 ? 124  GLY A C     1 
ATOM   403   O  O     . GLY A 1 124 ? 124.782 142.932 192.004 1.00 151.57 ? 124  GLY A O     1 
ATOM   404   N  N     . TYR A 1 125 ? 126.344 141.427 192.605 1.00 147.17 ? 125  TYR A N     1 
ATOM   405   C  CA    . TYR A 1 125 ? 126.735 142.226 193.762 1.00 149.13 ? 125  TYR A CA    1 
ATOM   406   C  C     . TYR A 1 125 ? 127.368 143.545 193.337 1.00 150.36 ? 125  TYR A C     1 
ATOM   407   O  O     . TYR A 1 125 ? 127.141 144.583 193.973 1.00 152.17 ? 125  TYR A O     1 
ATOM   408   C  CB    . TYR A 1 125 ? 127.674 141.431 194.668 1.00 149.18 ? 125  TYR A CB    1 
ATOM   409   C  CG    . TYR A 1 125 ? 126.959 140.408 195.522 1.00 152.42 ? 125  TYR A CG    1 
ATOM   410   C  CD1   . TYR A 1 125 ? 126.125 140.807 196.558 1.00 156.46 ? 125  TYR A CD1   1 
ATOM   411   C  CD2   . TYR A 1 125 ? 127.119 139.049 195.298 1.00 153.74 ? 125  TYR A CD2   1 
ATOM   412   C  CE1   . TYR A 1 125 ? 125.468 139.880 197.343 1.00 161.89 ? 125  TYR A CE1   1 
ATOM   413   C  CE2   . TYR A 1 125 ? 126.467 138.115 196.079 1.00 157.93 ? 125  TYR A CE2   1 
ATOM   414   C  CZ    . TYR A 1 125 ? 125.643 138.536 197.099 1.00 165.97 ? 125  TYR A CZ    1 
ATOM   415   O  OH    . TYR A 1 125 ? 124.991 137.608 197.878 1.00 176.28 ? 125  TYR A OH    1 
ATOM   416   N  N     . ALA A 1 126 ? 128.152 143.533 192.256 1.00 146.96 ? 126  ALA A N     1 
ATOM   417   C  CA    . ALA A 1 126 ? 128.754 144.768 191.769 1.00 147.90 ? 126  ALA A CA    1 
ATOM   418   C  C     . ALA A 1 126 ? 127.690 145.767 191.335 1.00 148.83 ? 126  ALA A C     1 
ATOM   419   O  O     . ALA A 1 126 ? 127.774 146.953 191.668 1.00 150.62 ? 126  ALA A O     1 
ATOM   420   C  CB    . ALA A 1 126 ? 129.711 144.467 190.617 1.00 144.90 ? 126  ALA A CB    1 
ATOM   421   N  N     . MET A 1 127 ? 126.678 145.306 190.597 1.00 146.13 ? 127  MET A N     1 
ATOM   422   C  CA    . MET A 1 127 ? 125.598 146.200 190.190 1.00 143.26 ? 127  MET A CA    1 
ATOM   423   C  C     . MET A 1 127 ? 124.808 146.703 191.390 1.00 146.59 ? 127  MET A C     1 
ATOM   424   O  O     . MET A 1 127 ? 124.424 147.878 191.437 1.00 149.89 ? 127  MET A O     1 
ATOM   425   C  CB    . MET A 1 127 ? 124.674 145.501 189.197 1.00 138.48 ? 127  MET A CB    1 
ATOM   426   C  CG    . MET A 1 127 ? 125.303 145.239 187.850 1.00 140.11 ? 127  MET A CG    1 
ATOM   427   S  SD    . MET A 1 127 ? 124.098 145.407 186.526 1.00 152.74 ? 127  MET A SD    1 
ATOM   428   C  CE    . MET A 1 127 ? 125.172 145.421 185.101 1.00 134.73 ? 127  MET A CE    1 
ATOM   429   N  N     . ALA A 1 128 ? 124.548 145.829 192.365 1.00 146.24 ? 128  ALA A N     1 
ATOM   430   C  CA    . ALA A 1 128 ? 123.814 146.257 193.550 1.00 149.39 ? 128  ALA A CA    1 
ATOM   431   C  C     . ALA A 1 128 ? 124.573 147.342 194.304 1.00 152.80 ? 128  ALA A C     1 
ATOM   432   O  O     . ALA A 1 128 ? 123.972 148.306 194.792 1.00 154.51 ? 128  ALA A O     1 
ATOM   433   C  CB    . ALA A 1 128 ? 123.538 145.060 194.459 1.00 152.88 ? 128  ALA A CB    1 
ATOM   434   N  N     . ASN A 1 129 ? 125.897 147.202 194.410 1.00 153.70 ? 129  ASN A N     1 
ATOM   435   C  CA    . ASN A 1 129 ? 126.690 148.224 195.087 1.00 154.99 ? 129  ASN A CA    1 
ATOM   436   C  C     . ASN A 1 129 ? 126.782 149.502 194.261 1.00 154.78 ? 129  ASN A C     1 
ATOM   437   O  O     . ASN A 1 129 ? 126.778 150.607 194.817 1.00 155.82 ? 129  ASN A O     1 
ATOM   438   C  CB    . ASN A 1 129 ? 128.084 147.683 195.401 1.00 154.74 ? 129  ASN A CB    1 
ATOM   439   C  CG    . ASN A 1 129 ? 128.043 146.412 196.225 1.00 157.70 ? 129  ASN A CG    1 
ATOM   440   O  OD1   . ASN A 1 129 ? 126.973 145.951 196.623 1.00 156.35 ? 129  ASN A OD1   1 
ATOM   441   N  ND2   . ASN A 1 129 ? 129.211 145.837 196.486 1.00 159.84 ? 129  ASN A ND2   1 
ATOM   442   N  N     . VAL A 1 130 ? 126.871 149.375 192.935 1.00 152.12 ? 130  VAL A N     1 
ATOM   443   C  CA    . VAL A 1 130 ? 127.046 150.543 192.076 1.00 149.97 ? 130  VAL A CA    1 
ATOM   444   C  C     . VAL A 1 130 ? 125.775 151.384 192.027 1.00 152.67 ? 130  VAL A C     1 
ATOM   445   O  O     . VAL A 1 130 ? 125.835 152.620 192.010 1.00 154.34 ? 130  VAL A O     1 
ATOM   446   C  CB    . VAL A 1 130 ? 127.493 150.098 190.670 1.00 143.72 ? 130  VAL A CB    1 
ATOM   447   C  CG1   . VAL A 1 130 ? 127.155 151.155 189.633 1.00 141.90 ? 130  VAL A CG1   1 
ATOM   448   C  CG2   . VAL A 1 130 ? 128.981 149.806 190.661 1.00 148.84 ? 130  VAL A CG2   1 
ATOM   449   N  N     . ALA A 1 131 ? 124.607 150.733 192.014 1.00 151.58 ? 131  ALA A N     1 
ATOM   450   C  CA    . ALA A 1 131 ? 123.355 151.447 191.779 1.00 150.47 ? 131  ALA A CA    1 
ATOM   451   C  C     . ALA A 1 131 ? 123.119 152.562 192.791 1.00 156.90 ? 131  ALA A C     1 
ATOM   452   O  O     . ALA A 1 131 ? 122.475 153.565 192.464 1.00 160.30 ? 131  ALA A O     1 
ATOM   453   C  CB    . ALA A 1 131 ? 122.184 150.466 191.800 1.00 148.08 ? 131  ALA A CB    1 
ATOM   454   N  N     . GLU A 1 132 ? 123.624 152.414 194.017 1.00 158.86 ? 132  GLU A N     1 
ATOM   455   C  CA    . GLU A 1 132 ? 123.409 153.447 195.027 1.00 160.43 ? 132  GLU A CA    1 
ATOM   456   C  C     . GLU A 1 132 ? 124.124 154.742 194.663 1.00 161.71 ? 132  GLU A C     1 
ATOM   457   O  O     . GLU A 1 132 ? 123.608 155.836 194.921 1.00 163.32 ? 132  GLU A O     1 
ATOM   458   C  CB    . GLU A 1 132 ? 123.869 152.952 196.399 1.00 161.78 ? 132  GLU A CB    1 
ATOM   459   C  CG    . GLU A 1 132 ? 123.376 151.563 196.766 1.00 163.37 ? 132  GLU A CG    1 
ATOM   460   C  CD    . GLU A 1 132 ? 124.059 151.014 198.005 1.00 166.08 ? 132  GLU A CD    1 
ATOM   461   O  OE1   . GLU A 1 132 ? 124.837 151.761 198.635 1.00 167.43 ? 132  GLU A OE1   1 
ATOM   462   O  OE2   . GLU A 1 132 ? 123.815 149.839 198.351 1.00 163.57 ? 132  GLU A OE2   1 
ATOM   463   N  N     . ARG A 1 133 ? 125.312 154.642 194.065 1.00 159.79 ? 133  ARG A N     1 
ATOM   464   C  CA    . ARG A 1 133 ? 126.120 155.829 193.814 1.00 161.40 ? 133  ARG A CA    1 
ATOM   465   C  C     . ARG A 1 133 ? 125.640 156.623 192.604 1.00 161.88 ? 133  ARG A C     1 
ATOM   466   O  O     . ARG A 1 133 ? 126.026 157.786 192.442 1.00 164.84 ? 133  ARG A O     1 
ATOM   467   C  CB    . ARG A 1 133 ? 127.586 155.429 193.641 1.00 162.39 ? 133  ARG A CB    1 
ATOM   468   C  CG    . ARG A 1 133 ? 128.074 155.386 192.205 1.00 162.88 ? 133  ARG A CG    1 
ATOM   469   C  CD    . ARG A 1 133 ? 129.584 155.152 192.097 1.00 167.77 ? 133  ARG A CD    1 
ATOM   470   N  NE    . ARG A 1 133 ? 130.057 154.001 192.862 1.00 170.78 ? 133  ARG A NE    1 
ATOM   471   C  CZ    . ARG A 1 133 ? 130.502 154.049 194.112 1.00 173.16 ? 133  ARG A CZ    1 
ATOM   472   N  NH1   . ARG A 1 133 ? 130.578 155.190 194.777 1.00 171.47 ? 133  ARG A NH1   1 
ATOM   473   N  NH2   . ARG A 1 133 ? 130.886 152.923 194.706 1.00 173.20 ? 133  ARG A NH2   1 
ATOM   474   N  N     . GLN A 1 134 ? 124.805 156.028 191.754 1.00 159.15 ? 134  GLN A N     1 
ATOM   475   C  CA    . GLN A 1 134 ? 124.310 156.739 190.583 1.00 159.26 ? 134  GLN A CA    1 
ATOM   476   C  C     . GLN A 1 134 ? 123.329 157.832 190.988 1.00 161.87 ? 134  GLN A C     1 
ATOM   477   O  O     . GLN A 1 134 ? 122.423 157.611 191.797 1.00 159.68 ? 134  GLN A O     1 
ATOM   478   C  CB    . GLN A 1 134 ? 123.640 155.765 189.614 1.00 156.62 ? 134  GLN A CB    1 
ATOM   479   C  CG    . GLN A 1 134 ? 124.604 154.844 188.891 1.00 152.77 ? 134  GLN A CG    1 
ATOM   480   C  CD    . GLN A 1 134 ? 125.519 155.590 187.946 1.00 146.40 ? 134  GLN A CD    1 
ATOM   481   O  OE1   . GLN A 1 134 ? 125.167 156.648 187.429 1.00 147.15 ? 134  GLN A OE1   1 
ATOM   482   N  NE2   . GLN A 1 134 ? 126.703 155.038 187.713 1.00 144.96 ? 134  GLN A NE2   1 
ATOM   483   N  N     . ALA A 1 135 ? 123.514 159.022 190.414 1.00 161.65 ? 135  ALA A N     1 
ATOM   484   C  CA    . ALA A 1 135 ? 122.638 160.145 190.727 1.00 162.37 ? 135  ALA A CA    1 
ATOM   485   C  C     . ALA A 1 135 ? 121.392 160.163 189.853 1.00 165.33 ? 135  ALA A C     1 
ATOM   486   O  O     . ALA A 1 135 ? 120.367 160.722 190.258 1.00 168.34 ? 135  ALA A O     1 
ATOM   487   C  CB    . ALA A 1 135 ? 123.398 161.463 190.580 1.00 161.96 ? 135  ALA A CB    1 
ATOM   488   N  N     . ASN A 1 136 ? 121.457 159.571 188.668 1.00 161.64 ? 136  ASN A N     1 
ATOM   489   C  CA    . ASN A 1 136 ? 120.299 159.525 187.783 1.00 157.65 ? 136  ASN A CA    1 
ATOM   490   C  C     . ASN A 1 136 ? 119.260 158.571 188.354 1.00 155.95 ? 136  ASN A C     1 
ATOM   491   O  O     . ASN A 1 136 ? 119.569 157.391 188.563 1.00 156.42 ? 136  ASN A O     1 
ATOM   492   C  CB    . ASN A 1 136 ? 120.724 159.081 186.387 1.00 151.66 ? 136  ASN A CB    1 
ATOM   493   C  CG    . ASN A 1 136 ? 119.686 159.398 185.331 1.00 152.89 ? 136  ASN A CG    1 
ATOM   494   O  OD1   . ASN A 1 136 ? 118.483 159.300 185.575 1.00 153.22 ? 136  ASN A OD1   1 
ATOM   495   N  ND2   . ASN A 1 136 ? 120.147 159.778 184.146 1.00 153.60 ? 136  ASN A ND2   1 
ATOM   496   N  N     . PRO A 1 137 ? 118.038 159.030 188.642 1.00 154.21 ? 137  PRO A N     1 
ATOM   497   C  CA    . PRO A 1 137 ? 117.034 158.112 189.206 1.00 156.35 ? 137  PRO A CA    1 
ATOM   498   C  C     . PRO A 1 137 ? 116.720 156.931 188.307 1.00 156.83 ? 137  PRO A C     1 
ATOM   499   O  O     . PRO A 1 137 ? 116.559 155.806 188.801 1.00 157.63 ? 137  PRO A O     1 
ATOM   500   C  CB    . PRO A 1 137 ? 115.810 159.018 189.404 1.00 163.80 ? 137  PRO A CB    1 
ATOM   501   C  CG    . PRO A 1 137 ? 116.369 160.398 189.496 1.00 161.48 ? 137  PRO A CG    1 
ATOM   502   C  CD    . PRO A 1 137 ? 117.550 160.416 188.574 1.00 156.44 ? 137  PRO A CD    1 
ATOM   503   N  N     . LYS A 1 138 ? 116.641 157.151 186.993 1.00 154.46 ? 138  LYS A N     1 
ATOM   504   C  CA    . LYS A 1 138 ? 116.321 156.055 186.086 1.00 152.92 ? 138  LYS A CA    1 
ATOM   505   C  C     . LYS A 1 138 ? 117.415 154.997 186.097 1.00 148.46 ? 138  LYS A C     1 
ATOM   506   O  O     . LYS A 1 138 ? 117.128 153.802 186.223 1.00 149.00 ? 138  LYS A O     1 
ATOM   507   C  CB    . LYS A 1 138 ? 116.102 156.579 184.668 1.00 149.51 ? 138  LYS A CB    1 
ATOM   508   C  CG    . LYS A 1 138 ? 116.051 155.479 183.618 1.00 144.02 ? 138  LYS A CG    1 
ATOM   509   C  CD    . LYS A 1 138 ? 116.022 156.041 182.207 1.00 142.84 ? 138  LYS A CD    1 
ATOM   510   C  CE    . LYS A 1 138 ? 114.722 156.782 181.940 1.00 149.76 ? 138  LYS A CE    1 
ATOM   511   N  NZ    . LYS A 1 138 ? 114.659 157.323 180.555 1.00 148.26 ? 138  LYS A NZ    1 
ATOM   512   N  N     . ILE A 1 139 ? 118.675 155.420 185.981 1.00 146.13 ? 139  ILE A N     1 
ATOM   513   C  CA    . ILE A 1 139 ? 119.780 154.466 185.998 1.00 142.99 ? 139  ILE A CA    1 
ATOM   514   C  C     . ILE A 1 139 ? 119.860 153.766 187.347 1.00 143.53 ? 139  ILE A C     1 
ATOM   515   O  O     . ILE A 1 139 ? 120.122 152.563 187.418 1.00 142.32 ? 139  ILE A O     1 
ATOM   516   C  CB    . ILE A 1 139 ? 121.103 155.165 185.641 1.00 143.12 ? 139  ILE A CB    1 
ATOM   517   C  CG1   . ILE A 1 139 ? 121.056 155.684 184.205 1.00 140.73 ? 139  ILE A CG1   1 
ATOM   518   C  CG2   . ILE A 1 139 ? 122.271 154.212 185.810 1.00 139.12 ? 139  ILE A CG2   1 
ATOM   519   C  CD1   . ILE A 1 139 ? 120.907 154.590 183.178 1.00 135.57 ? 139  ILE A CD1   1 
ATOM   520   N  N     . CYS A 1 140 ? 119.630 154.501 188.436 1.00 145.79 ? 140  CYS A N     1 
ATOM   521   C  CA    . CYS A 1 140 ? 119.685 153.891 189.761 1.00 146.14 ? 140  CYS A CA    1 
ATOM   522   C  C     . CYS A 1 140 ? 118.642 152.789 189.903 1.00 146.15 ? 140  CYS A C     1 
ATOM   523   O  O     . CYS A 1 140 ? 118.966 151.655 190.281 1.00 143.89 ? 140  CYS A O     1 
ATOM   524   C  CB    . CYS A 1 140 ? 119.493 154.961 190.836 1.00 151.66 ? 140  CYS A CB    1 
ATOM   525   S  SG    . CYS A 1 140 ? 119.299 154.319 192.513 1.00 152.90 ? 140  CYS A SG    1 
ATOM   526   N  N     . ASN A 1 141 ? 117.380 153.100 189.588 1.00 149.67 ? 141  ASN A N     1 
ATOM   527   C  CA    . ASN A 1 141 ? 116.323 152.099 189.703 1.00 149.30 ? 141  ASN A CA    1 
ATOM   528   C  C     . ASN A 1 141 ? 116.561 150.931 188.756 1.00 143.68 ? 141  ASN A C     1 
ATOM   529   O  O     . ASN A 1 141 ? 116.363 149.768 189.130 1.00 146.49 ? 141  ASN A O     1 
ATOM   530   C  CB    . ASN A 1 141 ? 114.959 152.735 189.435 1.00 158.08 ? 141  ASN A CB    1 
ATOM   531   C  CG    . ASN A 1 141 ? 114.693 153.937 190.316 1.00 172.98 ? 141  ASN A CG    1 
ATOM   532   O  OD1   . ASN A 1 141 ? 115.538 154.335 191.116 1.00 177.33 ? 141  ASN A OD1   1 
ATOM   533   N  ND2   . ASN A 1 141 ? 113.510 154.523 190.174 1.00 184.10 ? 141  ASN A ND2   1 
ATOM   534   N  N     . LEU A 1 142 ? 116.997 151.217 187.529 1.00 137.91 ? 142  LEU A N     1 
ATOM   535   C  CA    . LEU A 1 142 ? 117.180 150.160 186.544 1.00 133.74 ? 142  LEU A CA    1 
ATOM   536   C  C     . LEU A 1 142 ? 118.327 149.238 186.939 1.00 134.63 ? 142  LEU A C     1 
ATOM   537   O  O     . LEU A 1 142 ? 118.226 148.013 186.799 1.00 135.19 ? 142  LEU A O     1 
ATOM   538   C  CB    . LEU A 1 142 ? 117.417 150.788 185.171 1.00 131.73 ? 142  LEU A CB    1 
ATOM   539   C  CG    . LEU A 1 142 ? 117.009 150.010 183.922 1.00 125.80 ? 142  LEU A CG    1 
ATOM   540   C  CD1   . LEU A 1 142 ? 116.936 150.950 182.732 1.00 120.08 ? 142  LEU A CD1   1 
ATOM   541   C  CD2   . LEU A 1 142 ? 117.960 148.882 183.644 1.00 127.95 ? 142  LEU A CD2   1 
ATOM   542   N  N     . LEU A 1 143 ? 119.424 149.805 187.447 1.00 136.63 ? 143  LEU A N     1 
ATOM   543   C  CA    . LEU A 1 143 ? 120.548 148.989 187.887 1.00 133.68 ? 143  LEU A CA    1 
ATOM   544   C  C     . LEU A 1 143 ? 120.191 148.179 189.124 1.00 133.82 ? 143  LEU A C     1 
ATOM   545   O  O     . LEU A 1 143 ? 120.619 147.029 189.261 1.00 132.29 ? 143  LEU A O     1 
ATOM   546   C  CB    . LEU A 1 143 ? 121.765 149.875 188.155 1.00 136.03 ? 143  LEU A CB    1 
ATOM   547   C  CG    . LEU A 1 143 ? 122.666 150.177 186.958 1.00 131.27 ? 143  LEU A CG    1 
ATOM   548   C  CD1   . LEU A 1 143 ? 123.992 150.750 187.416 1.00 138.13 ? 143  LEU A CD1   1 
ATOM   549   C  CD2   . LEU A 1 143 ? 122.893 148.923 186.145 1.00 125.42 ? 143  LEU A CD2   1 
ATOM   550   N  N     . THR A 1 144 ? 119.409 148.756 190.041 1.00 135.10 ? 144  THR A N     1 
ATOM   551   C  CA    . THR A 1 144 ? 118.953 147.986 191.194 1.00 131.91 ? 144  THR A CA    1 
ATOM   552   C  C     . THR A 1 144 ? 118.103 146.801 190.752 1.00 135.34 ? 144  THR A C     1 
ATOM   553   O  O     . THR A 1 144 ? 118.273 145.677 191.244 1.00 141.37 ? 144  THR A O     1 
ATOM   554   C  CB    . THR A 1 144 ? 118.169 148.885 192.150 1.00 133.17 ? 144  THR A CB    1 
ATOM   555   O  OG1   . THR A 1 144 ? 119.039 149.888 192.688 1.00 135.36 ? 144  THR A OG1   1 
ATOM   556   C  CG2   . THR A 1 144 ? 117.584 148.070 193.290 1.00 139.32 ? 144  THR A CG2   1 
ATOM   557   N  N     . SER A 1 145 ? 117.184 147.035 189.811 1.00 134.31 ? 145  SER A N     1 
ATOM   558   C  CA    . SER A 1 145 ? 116.342 145.952 189.316 1.00 133.81 ? 145  SER A CA    1 
ATOM   559   C  C     . SER A 1 145 ? 117.171 144.881 188.619 1.00 135.76 ? 145  SER A C     1 
ATOM   560   O  O     . SER A 1 145 ? 116.941 143.682 188.816 1.00 142.33 ? 145  SER A O     1 
ATOM   561   C  CB    . SER A 1 145 ? 115.276 146.504 188.372 1.00 138.66 ? 145  SER A CB    1 
ATOM   562   O  OG    . SER A 1 145 ? 114.366 145.491 187.988 1.00 146.56 ? 145  SER A OG    1 
ATOM   563   N  N     . LYS A 1 146 ? 118.144 145.293 187.802 1.00 131.69 ? 146  LYS A N     1 
ATOM   564   C  CA    . LYS A 1 146 ? 118.999 144.325 187.123 1.00 130.70 ? 146  LYS A CA    1 
ATOM   565   C  C     . LYS A 1 146 ? 119.823 143.521 188.120 1.00 133.52 ? 146  LYS A C     1 
ATOM   566   O  O     . LYS A 1 146 ? 119.990 142.307 187.962 1.00 135.61 ? 146  LYS A O     1 
ATOM   567   C  CB    . LYS A 1 146 ? 119.910 145.036 186.124 1.00 127.44 ? 146  LYS A CB    1 
ATOM   568   C  CG    . LYS A 1 146 ? 120.020 144.342 184.778 1.00 123.82 ? 146  LYS A CG    1 
ATOM   569   C  CD    . LYS A 1 146 ? 120.669 142.976 184.896 1.00 119.63 ? 146  LYS A CD    1 
ATOM   570   C  CE    . LYS A 1 146 ? 120.739 142.283 183.549 1.00 121.06 ? 146  LYS A CE    1 
ATOM   571   N  NZ    . LYS A 1 146 ? 121.268 140.898 183.664 1.00 123.13 ? 146  LYS A NZ    1 
ATOM   572   N  N     . GLY A 1 147 ? 120.347 144.180 189.153 1.00 135.70 ? 147  GLY A N     1 
ATOM   573   C  CA    . GLY A 1 147 ? 121.106 143.463 190.162 1.00 136.94 ? 147  GLY A CA    1 
ATOM   574   C  C     . GLY A 1 147 ? 120.267 142.442 190.902 1.00 137.15 ? 147  GLY A C     1 
ATOM   575   O  O     . GLY A 1 147 ? 120.698 141.305 191.110 1.00 143.21 ? 147  GLY A O     1 
ATOM   576   N  N     . GLU A 1 149 ? 117.510 141.004 189.816 1.00 135.81 ? 149  GLU A N     1 
ATOM   577   C  CA    . GLU A 1 149 ? 117.177 139.935 188.880 1.00 137.60 ? 149  GLU A CA    1 
ATOM   578   C  C     . GLU A 1 149 ? 118.347 138.976 188.695 1.00 137.90 ? 149  GLU A C     1 
ATOM   579   O  O     . GLU A 1 149 ? 118.163 137.752 188.678 1.00 142.21 ? 149  GLU A O     1 
ATOM   580   C  CB    . GLU A 1 149 ? 116.751 140.531 187.539 1.00 136.18 ? 149  GLU A CB    1 
ATOM   581   C  CG    . GLU A 1 149 ? 116.642 139.518 186.415 1.00 136.92 ? 149  GLU A CG    1 
ATOM   582   C  CD    . GLU A 1 149 ? 116.437 140.173 185.063 1.00 144.78 ? 149  GLU A CD    1 
ATOM   583   O  OE1   . GLU A 1 149 ? 116.122 141.381 185.028 1.00 142.78 ? 149  GLU A OE1   1 
ATOM   584   O  OE2   . GLU A 1 149 ? 116.597 139.483 184.036 1.00 147.64 ? 149  GLU A OE2   1 
ATOM   585   N  N     . THR A 1 150 ? 119.561 139.513 188.564 1.00 135.68 ? 150  THR A N     1 
ATOM   586   C  CA    . THR A 1 150 ? 120.729 138.659 188.390 1.00 135.92 ? 150  THR A CA    1 
ATOM   587   C  C     . THR A 1 150 ? 120.998 137.831 189.641 1.00 140.53 ? 150  THR A C     1 
ATOM   588   O  O     . THR A 1 150 ? 121.405 136.670 189.546 1.00 143.62 ? 150  THR A O     1 
ATOM   589   C  CB    . THR A 1 150 ? 121.949 139.503 188.025 1.00 134.05 ? 150  THR A CB    1 
ATOM   590   O  OG1   . THR A 1 150 ? 121.629 140.343 186.910 1.00 140.62 ? 150  THR A OG1   1 
ATOM   591   C  CG2   . THR A 1 150 ? 123.113 138.614 187.646 1.00 131.18 ? 150  THR A CG2   1 
ATOM   592   N  N     . LEU A 1 151 ? 120.767 138.404 190.825 1.00 140.64 ? 151  LEU A N     1 
ATOM   593   C  CA    . LEU A 1 151 ? 120.937 137.633 192.053 1.00 142.04 ? 151  LEU A CA    1 
ATOM   594   C  C     . LEU A 1 151 ? 119.896 136.523 192.164 1.00 147.09 ? 151  LEU A C     1 
ATOM   595   O  O     . LEU A 1 151 ? 120.204 135.417 192.625 1.00 152.50 ? 151  LEU A O     1 
ATOM   596   C  CB    . LEU A 1 151 ? 120.873 138.558 193.266 1.00 146.19 ? 151  LEU A CB    1 
ATOM   597   C  CG    . LEU A 1 151 ? 122.038 139.537 193.393 1.00 148.59 ? 151  LEU A CG    1 
ATOM   598   C  CD1   . LEU A 1 151 ? 121.927 140.347 194.671 1.00 154.29 ? 151  LEU A CD1   1 
ATOM   599   C  CD2   . LEU A 1 151 ? 123.367 138.809 193.329 1.00 149.33 ? 151  LEU A CD2   1 
ATOM   600   N  N     . ASN A 1 152 ? 118.653 136.800 191.762 1.00 143.59 ? 152  ASN A N     1 
ATOM   601   C  CA    . ASN A 1 152 ? 117.635 135.753 191.763 1.00 140.80 ? 152  ASN A CA    1 
ATOM   602   C  C     . ASN A 1 152 ? 118.001 134.634 190.797 1.00 142.65 ? 152  ASN A C     1 
ATOM   603   O  O     . ASN A 1 152 ? 117.837 133.447 191.111 1.00 150.89 ? 152  ASN A O     1 
ATOM   604   C  CB    . ASN A 1 152 ? 116.270 136.340 191.412 1.00 140.61 ? 152  ASN A CB    1 
ATOM   605   C  CG    . ASN A 1 152 ? 115.771 137.313 192.459 1.00 147.43 ? 152  ASN A CG    1 
ATOM   606   O  OD1   . ASN A 1 152 ? 116.176 137.252 193.619 1.00 154.62 ? 152  ASN A OD1   1 
ATOM   607   N  ND2   . ASN A 1 152 ? 114.891 138.220 192.054 1.00 145.95 ? 152  ASN A ND2   1 
ATOM   608   N  N     . TRP A 1 153 ? 118.506 134.992 189.616 1.00 139.36 ? 153  TRP A N     1 
ATOM   609   C  CA    . TRP A 1 153 ? 118.968 133.973 188.680 1.00 140.48 ? 153  TRP A CA    1 
ATOM   610   C  C     . TRP A 1 153 ? 120.153 133.203 189.249 1.00 143.48 ? 153  TRP A C     1 
ATOM   611   O  O     . TRP A 1 153 ? 120.296 132.000 189.005 1.00 146.28 ? 153  TRP A O     1 
ATOM   612   C  CB    . TRP A 1 153 ? 119.334 134.610 187.342 1.00 136.78 ? 153  TRP A CB    1 
ATOM   613   C  CG    . TRP A 1 153 ? 120.449 133.910 186.644 1.00 131.77 ? 153  TRP A CG    1 
ATOM   614   C  CD1   . TRP A 1 153 ? 121.713 134.376 186.454 1.00 134.90 ? 153  TRP A CD1   1 
ATOM   615   C  CD2   . TRP A 1 153 ? 120.407 132.609 186.051 1.00 133.08 ? 153  TRP A CD2   1 
ATOM   616   N  NE1   . TRP A 1 153 ? 122.462 133.449 185.773 1.00 133.02 ? 153  TRP A NE1   1 
ATOM   617   C  CE2   . TRP A 1 153 ? 121.681 132.354 185.515 1.00 132.94 ? 153  TRP A CE2   1 
ATOM   618   C  CE3   . TRP A 1 153 ? 119.414 131.635 185.922 1.00 141.65 ? 153  TRP A CE3   1 
ATOM   619   C  CZ2   . TRP A 1 153 ? 121.990 131.168 184.859 1.00 136.26 ? 153  TRP A CZ2   1 
ATOM   620   C  CZ3   . TRP A 1 153 ? 119.723 130.457 185.269 1.00 143.16 ? 153  TRP A CZ3   1 
ATOM   621   C  CH2   . TRP A 1 153 ? 120.999 130.234 184.746 1.00 139.89 ? 153  TRP A CH2   1 
ATOM   622   N  N     . CYS A 1 154 ? 121.016 133.880 190.007 1.00 143.58 ? 154  CYS A N     1 
ATOM   623   C  CA    . CYS A 1 154 ? 122.125 133.197 190.663 1.00 143.90 ? 154  CYS A CA    1 
ATOM   624   C  C     . CYS A 1 154 ? 121.620 132.167 191.659 1.00 145.96 ? 154  CYS A C     1 
ATOM   625   O  O     . CYS A 1 154 ? 122.146 131.052 191.733 1.00 149.72 ? 154  CYS A O     1 
ATOM   626   C  CB    . CYS A 1 154 ? 123.018 134.212 191.370 1.00 148.26 ? 154  CYS A CB    1 
ATOM   627   S  SG    . CYS A 1 154 ? 124.323 134.877 190.345 1.00 155.43 ? 154  CYS A SG    1 
ATOM   628   N  N     . ALA A 1 155 ? 120.607 132.531 192.446 1.00 146.02 ? 155  ALA A N     1 
ATOM   629   C  CA    . ALA A 1 155 ? 120.022 131.582 193.388 1.00 147.16 ? 155  ALA A CA    1 
ATOM   630   C  C     . ALA A 1 155 ? 119.412 130.396 192.653 1.00 149.32 ? 155  ALA A C     1 
ATOM   631   O  O     . ALA A 1 155 ? 119.562 129.241 193.073 1.00 153.96 ? 155  ALA A O     1 
ATOM   632   C  CB    . ALA A 1 155 ? 118.974 132.279 194.255 1.00 155.05 ? 155  ALA A CB    1 
ATOM   633   N  N     . ARG A 1 156 ? 118.724 130.666 191.541 1.00 148.69 ? 156  ARG A N     1 
ATOM   634   C  CA    . ARG A 1 156 ? 118.138 129.583 190.756 1.00 150.72 ? 156  ARG A CA    1 
ATOM   635   C  C     . ARG A 1 156 ? 119.213 128.650 190.209 1.00 152.22 ? 156  ARG A C     1 
ATOM   636   O  O     . ARG A 1 156 ? 119.060 127.424 190.249 1.00 160.85 ? 156  ARG A O     1 
ATOM   637   C  CB    . ARG A 1 156 ? 117.292 130.154 189.620 1.00 151.51 ? 156  ARG A CB    1 
ATOM   638   C  CG    . ARG A 1 156 ? 117.158 129.232 188.422 1.00 154.86 ? 156  ARG A CG    1 
ATOM   639   C  CD    . ARG A 1 156 ? 116.131 129.755 187.434 1.00 161.16 ? 156  ARG A CD    1 
ATOM   640   N  NE    . ARG A 1 156 ? 115.815 128.767 186.410 1.00 167.93 ? 156  ARG A NE    1 
ATOM   641   C  CZ    . ARG A 1 156 ? 114.842 127.871 186.508 1.00 172.52 ? 156  ARG A CZ    1 
ATOM   642   N  NH1   . ARG A 1 156 ? 114.062 127.812 187.575 1.00 170.53 ? 156  ARG A NH1   1 
ATOM   643   N  NH2   . ARG A 1 156 ? 114.649 127.012 185.511 1.00 171.17 ? 156  ARG A NH2   1 
ATOM   644   N  N     . LEU A 1 157 ? 120.314 129.209 189.704 1.00 145.29 ? 157  LEU A N     1 
ATOM   645   C  CA    . LEU A 1 157 ? 121.384 128.378 189.159 1.00 146.14 ? 157  LEU A CA    1 
ATOM   646   C  C     . LEU A 1 157 ? 122.091 127.588 190.254 1.00 152.38 ? 157  LEU A C     1 
ATOM   647   O  O     . LEU A 1 157 ? 122.492 126.439 190.039 1.00 156.93 ? 157  LEU A O     1 
ATOM   648   C  CB    . LEU A 1 157 ? 122.384 129.241 188.392 1.00 142.73 ? 157  LEU A CB    1 
ATOM   649   C  CG    . LEU A 1 157 ? 123.482 128.472 187.661 1.00 139.61 ? 157  LEU A CG    1 
ATOM   650   C  CD1   . LEU A 1 157 ? 122.871 127.465 186.710 1.00 144.77 ? 157  LEU A CD1   1 
ATOM   651   C  CD2   . LEU A 1 157 ? 124.397 129.422 186.913 1.00 136.19 ? 157  LEU A CD2   1 
ATOM   652   N  N     . CYS A 1 158 ? 122.268 128.191 191.432 1.00 153.44 ? 158  CYS A N     1 
ATOM   653   C  CA    . CYS A 1 158 ? 122.856 127.463 192.549 1.00 156.50 ? 158  CYS A CA    1 
ATOM   654   C  C     . CYS A 1 158 ? 121.972 126.295 192.963 1.00 161.29 ? 158  CYS A C     1 
ATOM   655   O  O     . CYS A 1 158 ? 122.469 125.195 193.228 1.00 166.50 ? 158  CYS A O     1 
ATOM   656   C  CB    . CYS A 1 158 ? 123.093 128.405 193.729 1.00 160.92 ? 158  CYS A CB    1 
ATOM   657   S  SG    . CYS A 1 158 ? 123.793 127.608 195.191 1.00 177.32 ? 158  CYS A SG    1 
ATOM   658   N  N     . ASP A 1 159 ? 120.655 126.513 193.018 1.00 160.60 ? 159  ASP A N     1 
ATOM   659   C  CA    . ASP A 1 159 ? 119.743 125.411 193.310 1.00 161.98 ? 159  ASP A CA    1 
ATOM   660   C  C     . ASP A 1 159 ? 119.803 124.346 192.223 1.00 162.89 ? 159  ASP A C     1 
ATOM   661   O  O     . ASP A 1 159 ? 119.737 123.146 192.513 1.00 169.72 ? 159  ASP A O     1 
ATOM   662   C  CB    . ASP A 1 159 ? 118.317 125.935 193.473 1.00 163.41 ? 159  ASP A CB    1 
ATOM   663   C  CG    . ASP A 1 159 ? 118.113 126.669 194.783 1.00 167.78 ? 159  ASP A CG    1 
ATOM   664   O  OD1   . ASP A 1 159 ? 118.829 126.358 195.757 1.00 170.48 ? 159  ASP A OD1   1 
ATOM   665   O  OD2   . ASP A 1 159 ? 117.234 127.553 194.841 1.00 169.15 ? 159  ASP A OD2   1 
ATOM   666   N  N     . TRP A 1 160 ? 119.929 124.767 190.963 1.00 157.72 ? 160  TRP A N     1 
ATOM   667   C  CA    . TRP A 1 160 ? 120.028 123.815 189.862 1.00 160.30 ? 160  TRP A CA    1 
ATOM   668   C  C     . TRP A 1 160 ? 121.274 122.948 189.986 1.00 162.25 ? 160  TRP A C     1 
ATOM   669   O  O     . TRP A 1 160 ? 121.218 121.733 189.759 1.00 164.65 ? 160  TRP A O     1 
ATOM   670   C  CB    . TRP A 1 160 ? 120.020 124.563 188.530 1.00 158.61 ? 160  TRP A CB    1 
ATOM   671   C  CG    . TRP A 1 160 ? 120.056 123.676 187.329 1.00 159.98 ? 160  TRP A CG    1 
ATOM   672   C  CD1   . TRP A 1 160 ? 118.995 123.071 186.727 1.00 165.12 ? 160  TRP A CD1   1 
ATOM   673   C  CD2   . TRP A 1 160 ? 121.212 123.311 186.567 1.00 158.47 ? 160  TRP A CD2   1 
ATOM   674   N  NE1   . TRP A 1 160 ? 119.418 122.341 185.644 1.00 165.62 ? 160  TRP A NE1   1 
ATOM   675   C  CE2   . TRP A 1 160 ? 120.776 122.474 185.523 1.00 159.73 ? 160  TRP A CE2   1 
ATOM   676   C  CE3   . TRP A 1 160 ? 122.573 123.607 186.669 1.00 158.44 ? 160  TRP A CE3   1 
ATOM   677   C  CZ2   . TRP A 1 160 ? 121.651 121.928 184.589 1.00 154.87 ? 160  TRP A CZ2   1 
ATOM   678   C  CZ3   . TRP A 1 160 ? 123.440 123.066 185.739 1.00 158.17 ? 160  TRP A CZ3   1 
ATOM   679   C  CH2   . TRP A 1 160 ? 122.976 122.237 184.713 1.00 153.86 ? 160  TRP A CH2   1 
ATOM   680   N  N     . ILE A 1 161 ? 122.408 123.553 190.339 1.00 163.00 ? 161  ILE A N     1 
ATOM   681   C  CA    . ILE A 1 161 ? 123.631 122.779 190.534 1.00 164.90 ? 161  ILE A CA    1 
ATOM   682   C  C     . ILE A 1 161 ? 123.493 121.857 191.740 1.00 166.63 ? 161  ILE A C     1 
ATOM   683   O  O     . ILE A 1 161 ? 123.920 120.697 191.703 1.00 163.96 ? 161  ILE A O     1 
ATOM   684   C  CB    . ILE A 1 161 ? 124.845 123.715 190.665 1.00 164.50 ? 161  ILE A CB    1 
ATOM   685   C  CG1   . ILE A 1 161 ? 125.145 124.385 189.325 1.00 159.29 ? 161  ILE A CG1   1 
ATOM   686   C  CG2   . ILE A 1 161 ? 126.062 122.949 191.152 1.00 163.79 ? 161  ILE A CG2   1 
ATOM   687   C  CD1   . ILE A 1 161 ? 126.335 125.312 189.363 1.00 154.25 ? 161  ILE A CD1   1 
ATOM   688   N  N     . GLY A 1 163 ? 120.893 120.484 192.646 1.00 170.07 ? 163  GLY A N     1 
ATOM   689   C  CA    . GLY A 1 163 ? 120.023 119.415 192.209 1.00 170.05 ? 163  GLY A CA    1 
ATOM   690   C  C     . GLY A 1 163 ? 118.646 119.395 192.833 1.00 173.99 ? 163  GLY A C     1 
ATOM   691   O  O     . GLY A 1 163 ? 117.812 118.580 192.416 1.00 173.89 ? 163  GLY A O     1 
ATOM   692   N  N     . ARG A 1 164 ? 118.376 120.256 193.817 1.00 176.09 ? 164  ARG A N     1 
ATOM   693   C  CA    . ARG A 1 164 ? 117.038 120.305 194.399 1.00 176.36 ? 164  ARG A CA    1 
ATOM   694   C  C     . ARG A 1 164 ? 116.010 120.752 193.368 1.00 175.34 ? 164  ARG A C     1 
ATOM   695   O  O     . ARG A 1 164 ? 114.818 120.448 193.495 1.00 177.07 ? 164  ARG A O     1 
ATOM   696   C  CB    . ARG A 1 164 ? 117.021 121.230 195.616 1.00 175.18 ? 164  ARG A CB    1 
ATOM   697   C  CG    . ARG A 1 164 ? 117.853 122.489 195.458 1.00 173.57 ? 164  ARG A CG    1 
ATOM   698   C  CD    . ARG A 1 164 ? 118.116 123.141 196.806 1.00 173.71 ? 164  ARG A CD    1 
ATOM   699   N  NE    . ARG A 1 164 ? 116.898 123.687 197.392 1.00 178.16 ? 164  ARG A NE    1 
ATOM   700   C  CZ    . ARG A 1 164 ? 116.871 124.562 198.388 1.00 179.56 ? 164  ARG A CZ    1 
ATOM   701   N  NH1   . ARG A 1 164 ? 117.985 125.021 198.936 1.00 176.87 ? 164  ARG A NH1   1 
ATOM   702   N  NH2   . ARG A 1 164 ? 115.698 124.989 198.846 1.00 182.19 ? 164  ARG A NH2   1 
ATOM   703   N  N     . ILE A 1 165 ? 116.451 121.476 192.344 1.00 173.72 ? 165  ILE A N     1 
ATOM   704   C  CA    . ILE A 1 165 ? 115.613 121.856 191.214 1.00 176.82 ? 165  ILE A CA    1 
ATOM   705   C  C     . ILE A 1 165 ? 116.219 121.249 189.958 1.00 176.99 ? 165  ILE A C     1 
ATOM   706   O  O     . ILE A 1 165 ? 117.359 121.564 189.596 1.00 172.97 ? 165  ILE A O     1 
ATOM   707   C  CB    . ILE A 1 165 ? 115.493 123.384 191.086 1.00 175.50 ? 165  ILE A CB    1 
ATOM   708   C  CG1   . ILE A 1 165 ? 114.636 123.946 192.222 1.00 177.39 ? 165  ILE A CG1   1 
ATOM   709   C  CG2   . ILE A 1 165 ? 114.914 123.762 189.732 1.00 172.10 ? 165  ILE A CG2   1 
ATOM   710   C  CD1   . ILE A 1 165 ? 114.435 125.445 192.155 1.00 173.77 ? 165  ILE A CD1   1 
ATOM   711   N  N     . LYS A 1 166 ? 115.461 120.380 189.296 1.00 181.28 ? 166  LYS A N     1 
ATOM   712   C  CA    . LYS A 1 166 ? 115.907 119.708 188.084 1.00 178.75 ? 166  LYS A CA    1 
ATOM   713   C  C     . LYS A 1 166 ? 115.292 120.396 186.875 1.00 176.13 ? 166  LYS A C     1 
ATOM   714   O  O     . LYS A 1 166 ? 114.065 120.506 186.774 1.00 177.31 ? 166  LYS A O     1 
ATOM   715   C  CB    . LYS A 1 166 ? 115.532 118.225 188.105 1.00 180.29 ? 166  LYS A CB    1 
ATOM   716   C  CG    . LYS A 1 166 ? 116.157 117.442 189.253 1.00 184.25 ? 166  LYS A CG    1 
ATOM   717   C  CD    . LYS A 1 166 ? 115.705 115.991 189.251 1.00 182.44 ? 166  LYS A CD    1 
ATOM   718   C  CE    . LYS A 1 166 ? 116.314 115.223 190.414 1.00 181.12 ? 166  LYS A CE    1 
ATOM   719   N  NZ    . LYS A 1 166 ? 115.855 113.806 190.443 1.00 178.74 ? 166  LYS A NZ    1 
ATOM   720   N  N     . GLU A 1 167 ? 116.145 120.853 185.961 1.00 174.99 ? 167  GLU A N     1 
ATOM   721   C  CA    . GLU A 1 167 ? 115.695 121.575 184.782 1.00 174.77 ? 167  GLU A CA    1 
ATOM   722   C  C     . GLU A 1 167 ? 116.759 121.428 183.704 1.00 171.29 ? 167  GLU A C     1 
ATOM   723   O  O     . GLU A 1 167 ? 117.957 121.375 183.989 1.00 171.94 ? 167  GLU A O     1 
ATOM   724   C  CB    . GLU A 1 167 ? 115.391 123.044 185.128 1.00 177.12 ? 167  GLU A CB    1 
ATOM   725   C  CG    . GLU A 1 167 ? 114.611 123.847 184.081 1.00 177.87 ? 167  GLU A CG    1 
ATOM   726   C  CD    . GLU A 1 167 ? 115.445 124.315 182.901 1.00 175.18 ? 167  GLU A CD    1 
ATOM   727   O  OE1   . GLU A 1 167 ? 114.872 124.950 181.991 1.00 175.09 ? 167  GLU A OE1   1 
ATOM   728   O  OE2   . GLU A 1 167 ? 116.675 124.117 182.910 1.00 171.87 ? 167  GLU A OE2   1 
ATOM   729   N  N     . LYS A 1 168 ? 116.303 121.359 182.457 1.00 168.35 ? 168  LYS A N     1 
ATOM   730   C  CA    . LYS A 1 168 ? 117.155 121.029 181.322 1.00 168.77 ? 168  LYS A CA    1 
ATOM   731   C  C     . LYS A 1 168 ? 117.568 122.343 180.666 1.00 167.59 ? 168  LYS A C     1 
ATOM   732   O  O     . LYS A 1 168 ? 116.708 123.149 180.295 1.00 169.33 ? 168  LYS A O     1 
ATOM   733   C  CB    . LYS A 1 168 ? 116.392 120.107 180.359 1.00 168.36 ? 168  LYS A CB    1 
ATOM   734   C  CG    . LYS A 1 168 ? 116.586 120.202 178.824 1.00 165.86 ? 168  LYS A CG    1 
ATOM   735   C  CD    . LYS A 1 168 ? 118.023 120.405 178.346 1.00 164.71 ? 168  LYS A CD    1 
ATOM   736   C  CE    . LYS A 1 168 ? 118.085 120.626 176.845 1.00 165.79 ? 168  LYS A CE    1 
ATOM   737   N  NZ    . LYS A 1 168 ? 119.375 121.239 176.439 1.00 166.32 ? 168  LYS A NZ    1 
ATOM   738   N  N     . HIS A 1 169 ? 118.884 122.550 180.524 1.00 165.88 ? 169  HIS A N     1 
ATOM   739   C  CA    . HIS A 1 169 ? 119.457 123.734 179.891 1.00 164.41 ? 169  HIS A CA    1 
ATOM   740   C  C     . HIS A 1 169 ? 119.025 125.009 180.605 1.00 165.90 ? 169  HIS A C     1 
ATOM   741   O  O     . HIS A 1 169 ? 118.239 125.791 180.054 1.00 168.41 ? 169  HIS A O     1 
ATOM   742   C  CB    . HIS A 1 169 ? 119.058 123.799 178.415 1.00 165.47 ? 169  HIS A CB    1 
ATOM   743   C  CG    . HIS A 1 169 ? 120.089 124.433 177.536 1.00 169.73 ? 169  HIS A CG    1 
ATOM   744   N  ND1   . HIS A 1 169 ? 120.813 123.722 176.603 1.00 171.48 ? 169  HIS A ND1   1 
ATOM   745   C  CD2   . HIS A 1 169 ? 120.512 125.716 177.443 1.00 167.95 ? 169  HIS A CD2   1 
ATOM   746   C  CE1   . HIS A 1 169 ? 121.639 124.540 175.975 1.00 170.86 ? 169  HIS A CE1   1 
ATOM   747   N  NE2   . HIS A 1 169 ? 121.477 125.755 176.467 1.00 170.60 ? 169  HIS A NE2   1 
ATOM   748   N  N     . PRO A 1 170 ? 119.499 125.248 181.824 1.00 163.51 ? 170  PRO A N     1 
ATOM   749   C  CA    . PRO A 1 170 ? 119.076 126.447 182.552 1.00 157.24 ? 170  PRO A CA    1 
ATOM   750   C  C     . PRO A 1 170 ? 119.568 127.714 181.875 1.00 151.02 ? 170  PRO A C     1 
ATOM   751   O  O     . PRO A 1 170 ? 120.642 127.750 181.272 1.00 147.05 ? 170  PRO A O     1 
ATOM   752   C  CB    . PRO A 1 170 ? 119.718 126.268 183.931 1.00 158.75 ? 170  PRO A CB    1 
ATOM   753   C  CG    . PRO A 1 170 ? 120.925 125.445 183.663 1.00 160.52 ? 170  PRO A CG    1 
ATOM   754   C  CD    . PRO A 1 170 ? 120.558 124.516 182.537 1.00 163.54 ? 170  PRO A CD    1 
ATOM   755   N  N     . ARG A 1 171 ? 118.755 128.758 181.981 1.00 151.57 ? 171  ARG A N     1 
ATOM   756   C  CA    . ARG A 1 171 ? 119.037 130.066 181.413 1.00 145.56 ? 171  ARG A CA    1 
ATOM   757   C  C     . ARG A 1 171 ? 118.370 131.126 182.273 1.00 146.10 ? 171  ARG A C     1 
ATOM   758   O  O     . ARG A 1 171 ? 117.383 130.835 182.959 1.00 150.60 ? 171  ARG A O     1 
ATOM   759   C  CB    . ARG A 1 171 ? 118.534 130.165 179.965 1.00 139.17 ? 171  ARG A CB    1 
ATOM   760   C  CG    . ARG A 1 171 ? 119.564 129.730 178.949 1.00 138.11 ? 171  ARG A CG    1 
ATOM   761   C  CD    . ARG A 1 171 ? 120.656 130.770 178.843 1.00 133.42 ? 171  ARG A CD    1 
ATOM   762   N  NE    . ARG A 1 171 ? 121.882 130.234 178.268 1.00 136.83 ? 171  ARG A NE    1 
ATOM   763   C  CZ    . ARG A 1 171 ? 122.946 130.966 177.971 1.00 137.27 ? 171  ARG A CZ    1 
ATOM   764   N  NH1   . ARG A 1 171 ? 122.959 132.275 178.160 1.00 135.00 ? 171  ARG A NH1   1 
ATOM   765   N  NH2   . ARG A 1 171 ? 124.020 130.372 177.460 1.00 140.00 ? 171  ARG A NH2   1 
ATOM   766   N  N     . PRO A 1 172 ? 118.893 132.354 182.274 1.00 140.35 ? 172  PRO A N     1 
ATOM   767   C  CA    . PRO A 1 172 ? 118.274 133.407 183.086 1.00 139.79 ? 172  PRO A CA    1 
ATOM   768   C  C     . PRO A 1 172 ? 116.822 133.617 182.696 1.00 136.69 ? 172  PRO A C     1 
ATOM   769   O  O     . PRO A 1 172 ? 116.471 133.627 181.515 1.00 136.89 ? 172  PRO A O     1 
ATOM   770   C  CB    . PRO A 1 172 ? 119.128 134.644 182.779 1.00 135.54 ? 172  PRO A CB    1 
ATOM   771   C  CG    . PRO A 1 172 ? 119.891 134.302 181.542 1.00 133.24 ? 172  PRO A CG    1 
ATOM   772   C  CD    . PRO A 1 172 ? 120.113 132.831 181.607 1.00 134.25 ? 172  PRO A CD    1 
ATOM   773   N  N     . GLY A 1 173 ? 115.975 133.776 183.708 1.00 138.44 ? 173  GLY A N     1 
ATOM   774   C  CA    . GLY A 1 173 ? 114.564 133.971 183.456 1.00 145.07 ? 173  GLY A CA    1 
ATOM   775   C  C     . GLY A 1 173 ? 114.306 135.235 182.661 1.00 148.53 ? 173  GLY A C     1 
ATOM   776   O  O     . GLY A 1 173 ? 114.928 136.275 182.876 1.00 150.01 ? 173  GLY A O     1 
ATOM   777   N  N     . VAL A 1 174 ? 113.374 135.132 181.714 1.00 147.48 ? 174  VAL A N     1 
ATOM   778   C  CA    . VAL A 1 174 ? 113.020 136.282 180.896 1.00 143.46 ? 174  VAL A CA    1 
ATOM   779   C  C     . VAL A 1 174 ? 112.387 137.354 181.770 1.00 148.09 ? 174  VAL A C     1 
ATOM   780   O  O     . VAL A 1 174 ? 111.645 137.056 182.716 1.00 157.26 ? 174  VAL A O     1 
ATOM   781   C  CB    . VAL A 1 174 ? 112.101 135.868 179.738 1.00 141.73 ? 174  VAL A CB    1 
ATOM   782   C  CG1   . VAL A 1 174 ? 110.658 135.798 180.184 1.00 152.74 ? 174  VAL A CG1   1 
ATOM   783   C  CG2   . VAL A 1 174 ? 112.225 136.873 178.621 1.00 137.95 ? 174  VAL A CG2   1 
ATOM   784   N  N     . HIS A 1 175 ? 112.730 138.607 181.496 1.00 142.57 ? 175  HIS A N     1 
ATOM   785   C  CA    . HIS A 1 175 ? 112.205 139.735 182.251 1.00 142.24 ? 175  HIS A CA    1 
ATOM   786   C  C     . HIS A 1 175 ? 112.112 140.929 181.319 1.00 138.23 ? 175  HIS A C     1 
ATOM   787   O  O     . HIS A 1 175 ? 113.140 141.466 180.896 1.00 134.31 ? 175  HIS A O     1 
ATOM   788   C  CB    . HIS A 1 175 ? 113.097 140.053 183.453 1.00 142.83 ? 175  HIS A CB    1 
ATOM   789   C  CG    . HIS A 1 175 ? 112.475 140.993 184.435 1.00 148.65 ? 175  HIS A CG    1 
ATOM   790   N  ND1   . HIS A 1 175 ? 111.181 140.847 184.888 1.00 156.73 ? 175  HIS A ND1   1 
ATOM   791   C  CD2   . HIS A 1 175 ? 112.965 142.096 185.047 1.00 149.06 ? 175  HIS A CD2   1 
ATOM   792   C  CE1   . HIS A 1 175 ? 110.904 141.817 185.740 1.00 161.53 ? 175  HIS A CE1   1 
ATOM   793   N  NE2   . HIS A 1 175 ? 111.969 142.589 185.854 1.00 156.94 ? 175  HIS A NE2   1 
ATOM   794   N  N     . LYS A 1 176 ? 110.890 141.341 180.996 1.00 133.40 ? 176  LYS A N     1 
ATOM   795   C  CA    . LYS A 1 176 ? 110.660 142.516 180.171 1.00 124.79 ? 176  LYS A CA    1 
ATOM   796   C  C     . LYS A 1 176 ? 110.361 143.711 181.065 1.00 127.68 ? 176  LYS A C     1 
ATOM   797   O  O     . LYS A 1 176 ? 109.522 143.632 181.967 1.00 138.65 ? 176  LYS A O     1 
ATOM   798   C  CB    . LYS A 1 176 ? 109.519 142.288 179.176 1.00 125.57 ? 176  LYS A CB    1 
ATOM   799   C  CG    . LYS A 1 176 ? 108.191 141.891 179.790 1.00 137.08 ? 176  LYS A CG    1 
ATOM   800   C  CD    . LYS A 1 176 ? 107.039 142.218 178.852 1.00 138.08 ? 176  LYS A CD    1 
ATOM   801   C  CE    . LYS A 1 176 ? 107.339 141.778 177.429 1.00 132.88 ? 176  LYS A CE    1 
ATOM   802   N  NZ    . LYS A 1 176 ? 106.196 142.055 176.521 1.00 131.86 ? 176  LYS A NZ    1 
ATOM   803   N  N     . VAL A 1 177 ? 111.059 144.813 180.814 1.00 118.60 ? 177  VAL A N     1 
ATOM   804   C  CA    . VAL A 1 177 ? 110.985 146.007 181.644 1.00 119.65 ? 177  VAL A CA    1 
ATOM   805   C  C     . VAL A 1 177 ? 110.509 147.163 180.781 1.00 121.76 ? 177  VAL A C     1 
ATOM   806   O  O     . VAL A 1 177 ? 111.036 147.384 179.685 1.00 121.24 ? 177  VAL A O     1 
ATOM   807   C  CB    . VAL A 1 177 ? 112.342 146.329 182.291 1.00 121.83 ? 177  VAL A CB    1 
ATOM   808   C  CG1   . VAL A 1 177 ? 112.533 145.504 183.549 1.00 131.22 ? 177  VAL A CG1   1 
ATOM   809   C  CG2   . VAL A 1 177 ? 113.461 146.057 181.310 1.00 119.25 ? 177  VAL A CG2   1 
ATOM   810   N  N     . GLY A 1 178 ? 109.509 147.889 181.269 1.00 124.46 ? 178  GLY A N     1 
ATOM   811   C  CA    . GLY A 1 178 ? 108.958 149.031 180.566 1.00 123.85 ? 178  GLY A CA    1 
ATOM   812   C  C     . GLY A 1 178 ? 109.264 150.325 181.301 1.00 130.11 ? 178  GLY A C     1 
ATOM   813   O  O     . GLY A 1 178 ? 108.849 150.513 182.445 1.00 143.81 ? 178  GLY A O     1 
ATOM   814   N  N     . ILE A 1 179 ? 109.981 151.210 180.620 1.00 126.93 ? 179  ILE A N     1 
ATOM   815   C  CA    . ILE A 1 179 ? 110.305 152.520 181.171 1.00 135.08 ? 179  ILE A CA    1 
ATOM   816   C  C     . ILE A 1 179 ? 109.431 153.547 180.467 1.00 131.12 ? 179  ILE A C     1 
ATOM   817   O  O     . ILE A 1 179 ? 109.095 153.362 179.289 1.00 129.76 ? 179  ILE A O     1 
ATOM   818   C  CB    . ILE A 1 179 ? 111.793 152.853 180.998 1.00 137.75 ? 179  ILE A CB    1 
ATOM   819   C  CG1   . ILE A 1 179 ? 112.287 152.368 179.638 1.00 125.84 ? 179  ILE A CG1   1 
ATOM   820   C  CG2   . ILE A 1 179 ? 112.610 152.225 182.114 1.00 142.66 ? 179  ILE A CG2   1 
ATOM   821   C  CD1   . ILE A 1 179 ? 113.764 152.569 179.432 1.00 129.89 ? 179  ILE A CD1   1 
ATOM   822   N  N     . PRO A 1 180 ? 109.030 154.625 181.136 1.00 130.27 ? 180  PRO A N     1 
ATOM   823   C  CA    . PRO A 1 180 ? 108.269 155.668 180.446 1.00 131.87 ? 180  PRO A CA    1 
ATOM   824   C  C     . PRO A 1 180 ? 109.081 156.260 179.307 1.00 134.45 ? 180  PRO A C     1 
ATOM   825   O  O     . PRO A 1 180 ? 110.298 156.431 179.405 1.00 135.13 ? 180  PRO A O     1 
ATOM   826   C  CB    . PRO A 1 180 ? 108.002 156.703 181.544 1.00 132.68 ? 180  PRO A CB    1 
ATOM   827   C  CG    . PRO A 1 180 ? 108.146 155.949 182.821 1.00 139.99 ? 180  PRO A CG    1 
ATOM   828   C  CD    . PRO A 1 180 ? 109.204 154.923 182.566 1.00 137.73 ? 180  PRO A CD    1 
ATOM   829   N  N     . VAL A 1 181 ? 108.392 156.560 178.208 1.00 132.95 ? 181  VAL A N     1 
ATOM   830   C  CA    . VAL A 1 181 ? 109.054 157.154 177.056 1.00 128.16 ? 181  VAL A CA    1 
ATOM   831   C  C     . VAL A 1 181 ? 109.475 158.577 177.389 1.00 136.35 ? 181  VAL A C     1 
ATOM   832   O  O     . VAL A 1 181 ? 108.796 159.287 178.144 1.00 139.99 ? 181  VAL A O     1 
ATOM   833   C  CB    . VAL A 1 181 ? 108.134 157.117 175.826 1.00 126.61 ? 181  VAL A CB    1 
ATOM   834   C  CG1   . VAL A 1 181 ? 108.952 157.245 174.568 1.00 125.51 ? 181  VAL A CG1   1 
ATOM   835   C  CG2   . VAL A 1 181 ? 107.345 155.826 175.802 1.00 125.51 ? 181  VAL A CG2   1 
ATOM   836   N  N     . SER A 1 182 ? 110.611 158.997 176.830 1.00 136.26 ? 182  SER A N     1 
ATOM   837   C  CA    . SER A 1 182 ? 111.136 160.326 177.125 1.00 138.16 ? 182  SER A CA    1 
ATOM   838   C  C     . SER A 1 182 ? 110.186 161.418 176.649 1.00 139.29 ? 182  SER A C     1 
ATOM   839   O  O     . SER A 1 182 ? 109.981 162.419 177.346 1.00 138.92 ? 182  SER A O     1 
ATOM   840   C  CB    . SER A 1 182 ? 112.511 160.498 176.483 1.00 136.07 ? 182  SER A CB    1 
ATOM   841   O  OG    . SER A 1 182 ? 112.422 160.435 175.070 1.00 134.23 ? 182  SER A OG    1 
ATOM   842   N  N     . ASN A 1 183 ? 109.594 161.244 175.471 1.00 139.03 ? 183  ASN A N     1 
ATOM   843   C  CA    . ASN A 1 183 ? 108.732 162.251 174.867 1.00 137.87 ? 183  ASN A CA    1 
ATOM   844   C  C     . ASN A 1 183 ? 107.343 161.670 174.660 1.00 139.10 ? 183  ASN A C     1 
ATOM   845   O  O     . ASN A 1 183 ? 107.185 160.662 173.964 1.00 140.28 ? 183  ASN A O     1 
ATOM   846   C  CB    . ASN A 1 183 ? 109.310 162.733 173.537 1.00 136.08 ? 183  ASN A CB    1 
ATOM   847   C  CG    . ASN A 1 183 ? 109.891 161.603 172.719 1.00 132.73 ? 183  ASN A CG    1 
ATOM   848   O  OD1   . ASN A 1 183 ? 110.735 160.847 173.198 1.00 129.35 ? 183  ASN A OD1   1 
ATOM   849   N  ND2   . ASN A 1 183 ? 109.437 161.476 171.478 1.00 133.92 ? 183  ASN A ND2   1 
ATOM   850   N  N     . TRP A 1 184 ? 106.343 162.309 175.257 1.00 142.65 ? 184  TRP A N     1 
ATOM   851   C  CA    . TRP A 1 184 ? 104.946 161.972 175.033 1.00 148.43 ? 184  TRP A CA    1 
ATOM   852   C  C     . TRP A 1 184 ? 104.192 163.243 174.677 1.00 153.68 ? 184  TRP A C     1 
ATOM   853   O  O     . TRP A 1 184 ? 104.314 164.261 175.367 1.00 155.58 ? 184  TRP A O     1 
ATOM   854   C  CB    . TRP A 1 184 ? 104.322 161.302 176.264 1.00 147.28 ? 184  TRP A CB    1 
ATOM   855   C  CG    . TRP A 1 184 ? 102.872 160.985 176.095 1.00 149.59 ? 184  TRP A CG    1 
ATOM   856   C  CD1   . TRP A 1 184 ? 102.335 160.011 175.309 1.00 147.38 ? 184  TRP A CD1   1 
ATOM   857   C  CD2   . TRP A 1 184 ? 101.770 161.642 176.730 1.00 152.97 ? 184  TRP A CD2   1 
ATOM   858   N  NE1   . TRP A 1 184 ? 100.966 160.022 175.411 1.00 149.60 ? 184  TRP A NE1   1 
ATOM   859   C  CE2   . TRP A 1 184 ? 100.594 161.014 176.279 1.00 154.46 ? 184  TRP A CE2   1 
ATOM   860   C  CE3   . TRP A 1 184 ? 101.664 162.702 177.636 1.00 153.03 ? 184  TRP A CE3   1 
ATOM   861   C  CZ2   . TRP A 1 184 ? 99.327  161.411 176.700 1.00 157.11 ? 184  TRP A CZ2   1 
ATOM   862   C  CZ3   . TRP A 1 184 ? 100.405 163.094 178.054 1.00 155.11 ? 184  TRP A CZ3   1 
ATOM   863   C  CH2   . TRP A 1 184 ? 99.254  162.449 177.587 1.00 158.29 ? 184  TRP A CH2   1 
ATOM   864   N  N     . ASP A 1 185 ? 103.417 163.183 173.600 1.00 152.57 ? 185  ASP A N     1 
ATOM   865   C  CA    . ASP A 1 185 ? 102.735 164.363 173.086 1.00 152.23 ? 185  ASP A CA    1 
ATOM   866   C  C     . ASP A 1 185 ? 101.497 164.649 173.925 1.00 154.02 ? 185  ASP A C     1 
ATOM   867   O  O     . ASP A 1 185 ? 100.562 163.843 173.957 1.00 155.64 ? 185  ASP A O     1 
ATOM   868   C  CB    . ASP A 1 185 ? 102.357 164.159 171.621 1.00 153.65 ? 185  ASP A CB    1 
ATOM   869   C  CG    . ASP A 1 185 ? 103.552 163.825 170.754 1.00 150.59 ? 185  ASP A CG    1 
ATOM   870   O  OD1   . ASP A 1 185 ? 104.058 162.689 170.854 1.00 146.39 ? 185  ASP A OD1   1 
ATOM   871   O  OD2   . ASP A 1 185 ? 103.984 164.697 169.973 1.00 151.13 ? 185  ASP A OD2   1 
ATOM   872   N  N     . GLU A 1 186 ? 101.494 165.795 174.607 1.00 156.55 ? 186  GLU A N     1 
ATOM   873   C  CA    . GLU A 1 186 ? 100.316 166.193 175.370 1.00 161.29 ? 186  GLU A CA    1 
ATOM   874   C  C     . GLU A 1 186 ? 99.119  166.407 174.453 1.00 163.76 ? 186  GLU A C     1 
ATOM   875   O  O     . GLU A 1 186 ? 97.995  166.013 174.785 1.00 162.68 ? 186  GLU A O     1 
ATOM   876   C  CB    . GLU A 1 186 ? 100.608 167.460 176.174 1.00 162.81 ? 186  GLU A CB    1 
ATOM   877   C  CG    . GLU A 1 186 ? 101.573 167.267 177.333 1.00 162.07 ? 186  GLU A CG    1 
ATOM   878   C  CD    . GLU A 1 186 ? 103.025 167.274 176.895 1.00 160.58 ? 186  GLU A CD    1 
ATOM   879   O  OE1   . GLU A 1 186 ? 103.292 167.613 175.723 1.00 159.44 ? 186  GLU A OE1   1 
ATOM   880   O  OE2   . GLU A 1 186 ? 103.900 166.941 177.722 1.00 159.56 ? 186  GLU A OE2   1 
ATOM   881   N  N     . ASP A 1 187 ? 99.340  167.029 173.298 1.00 164.00 ? 187  ASP A N     1 
ATOM   882   C  CA    . ASP A 1 187 ? 98.287  167.288 172.321 1.00 165.16 ? 187  ASP A CA    1 
ATOM   883   C  C     . ASP A 1 187 ? 98.317  166.169 171.286 1.00 160.80 ? 187  ASP A C     1 
ATOM   884   O  O     . ASP A 1 187 ? 99.123  166.190 170.353 1.00 158.96 ? 187  ASP A O     1 
ATOM   885   C  CB    . ASP A 1 187 ? 98.473  168.658 171.677 1.00 171.84 ? 187  ASP A CB    1 
ATOM   886   C  CG    . ASP A 1 187 ? 99.930  168.989 171.426 1.00 171.85 ? 187  ASP A CG    1 
ATOM   887   O  OD1   . ASP A 1 187 ? 100.795 168.148 171.750 1.00 166.60 ? 187  ASP A OD1   1 
ATOM   888   O  OD2   . ASP A 1 187 ? 100.211 170.090 170.910 1.00 174.44 ? 187  ASP A OD2   1 
ATOM   889   N  N     . TRP A 1 188 ? 97.434  165.190 171.457 1.00 158.34 ? 188  TRP A N     1 
ATOM   890   C  CA    . TRP A 1 188 ? 97.325  164.069 170.537 1.00 150.13 ? 188  TRP A CA    1 
ATOM   891   C  C     . TRP A 1 188 ? 95.903  163.537 170.607 1.00 150.53 ? 188  TRP A C     1 
ATOM   892   O  O     . TRP A 1 188 ? 95.270  163.560 171.666 1.00 155.35 ? 188  TRP A O     1 
ATOM   893   C  CB    . TRP A 1 188 ? 98.335  162.967 170.874 1.00 144.77 ? 188  TRP A CB    1 
ATOM   894   C  CG    . TRP A 1 188 ? 98.608  162.028 169.747 1.00 141.64 ? 188  TRP A CG    1 
ATOM   895   C  CD1   . TRP A 1 188 ? 99.485  162.215 168.722 1.00 138.61 ? 188  TRP A CD1   1 
ATOM   896   C  CD2   . TRP A 1 188 ? 98.005  160.747 169.530 1.00 145.16 ? 188  TRP A CD2   1 
ATOM   897   N  NE1   . TRP A 1 188 ? 99.466  161.131 167.878 1.00 135.00 ? 188  TRP A NE1   1 
ATOM   898   C  CE2   . TRP A 1 188 ? 98.564  160.216 168.353 1.00 137.20 ? 188  TRP A CE2   1 
ATOM   899   C  CE3   . TRP A 1 188 ? 97.045  159.998 170.218 1.00 146.19 ? 188  TRP A CE3   1 
ATOM   900   C  CZ2   . TRP A 1 188 ? 98.195  158.974 167.846 1.00 128.61 ? 188  TRP A CZ2   1 
ATOM   901   C  CZ3   . TRP A 1 188 ? 96.683  158.764 169.714 1.00 140.29 ? 188  TRP A CZ3   1 
ATOM   902   C  CH2   . TRP A 1 188 ? 97.256  158.265 168.540 1.00 132.37 ? 188  TRP A CH2   1 
ATOM   903   N  N     . VAL A 1 189 ? 95.402  163.057 169.473 1.00 146.42 ? 189  VAL A N     1 
ATOM   904   C  CA    . VAL A 1 189 ? 94.023  162.599 169.358 1.00 149.93 ? 189  VAL A CA    1 
ATOM   905   C  C     . VAL A 1 189 ? 94.028  161.122 168.997 1.00 151.82 ? 189  VAL A C     1 
ATOM   906   O  O     . VAL A 1 189 ? 94.675  160.715 168.025 1.00 151.42 ? 189  VAL A O     1 
ATOM   907   C  CB    . VAL A 1 189 ? 93.238  163.415 168.316 1.00 153.21 ? 189  VAL A CB    1 
ATOM   908   C  CG1   . VAL A 1 189 ? 91.806  162.914 168.219 1.00 156.94 ? 189  VAL A CG1   1 
ATOM   909   C  CG2   . VAL A 1 189 ? 93.268  164.894 168.668 1.00 153.57 ? 189  VAL A CG2   1 
ATOM   910   N  N     . GLY A 1 190 ? 93.308  160.326 169.781 1.00 155.57 ? 190  GLY A N     1 
ATOM   911   C  CA    . GLY A 1 190 ? 93.156  158.916 169.523 1.00 156.18 ? 190  GLY A CA    1 
ATOM   912   C  C     . GLY A 1 190 ? 91.775  158.443 169.923 1.00 166.33 ? 190  GLY A C     1 
ATOM   913   O  O     . GLY A 1 190 ? 91.073  159.103 170.696 1.00 170.92 ? 190  GLY A O     1 
ATOM   914   N  N     . PRO A 1 191 ? 91.351  157.293 169.396 1.00 168.05 ? 191  PRO A N     1 
ATOM   915   C  CA    . PRO A 1 191 ? 90.000  156.799 169.700 1.00 174.66 ? 191  PRO A CA    1 
ATOM   916   C  C     . PRO A 1 191 ? 89.822  156.516 171.182 1.00 176.13 ? 191  PRO A C     1 
ATOM   917   O  O     . PRO A 1 191 ? 88.926  157.067 171.831 1.00 180.89 ? 191  PRO A O     1 
ATOM   918   C  CB    . PRO A 1 191 ? 89.896  155.515 168.865 1.00 171.79 ? 191  PRO A CB    1 
ATOM   919   C  CG    . PRO A 1 191 ? 90.992  155.621 167.840 1.00 167.56 ? 191  PRO A CG    1 
ATOM   920   C  CD    . PRO A 1 191 ? 92.089  156.384 168.506 1.00 162.05 ? 191  PRO A CD    1 
ATOM   921   N  N     . PHE A 1 192 ? 90.689  155.660 171.718 1.00 170.41 ? 192  PHE A N     1 
ATOM   922   C  CA    . PHE A 1 192 ? 90.786  155.384 173.143 1.00 167.28 ? 192  PHE A CA    1 
ATOM   923   C  C     . PHE A 1 192 ? 92.014  154.519 173.364 1.00 163.44 ? 192  PHE A C     1 
ATOM   924   O  O     . PHE A 1 192 ? 92.304  153.636 172.555 1.00 160.16 ? 192  PHE A O     1 
ATOM   925   C  CB    . PHE A 1 192 ? 89.538  154.673 173.683 1.00 170.11 ? 192  PHE A CB    1 
ATOM   926   C  CG    . PHE A 1 192 ? 89.564  154.457 175.171 1.00 171.95 ? 192  PHE A CG    1 
ATOM   927   C  CD1   . PHE A 1 192 ? 89.190  155.472 176.037 1.00 173.98 ? 192  PHE A CD1   1 
ATOM   928   C  CD2   . PHE A 1 192 ? 89.973  153.246 175.703 1.00 170.97 ? 192  PHE A CD2   1 
ATOM   929   C  CE1   . PHE A 1 192 ? 89.216  155.278 177.405 1.00 174.78 ? 192  PHE A CE1   1 
ATOM   930   C  CE2   . PHE A 1 192 ? 90.001  153.047 177.069 1.00 171.42 ? 192  PHE A CE2   1 
ATOM   931   C  CZ    . PHE A 1 192 ? 89.622  154.064 177.921 1.00 174.66 ? 192  PHE A CZ    1 
ATOM   932   N  N     . MET A 1 193 ? 92.729  154.779 174.453 1.00 163.09 ? 193  MET A N     1 
ATOM   933   C  CA    . MET A 1 193 ? 93.934  154.027 174.773 1.00 156.66 ? 193  MET A CA    1 
ATOM   934   C  C     . MET A 1 193 ? 94.229  154.184 176.254 1.00 157.95 ? 193  MET A C     1 
ATOM   935   O  O     . MET A 1 193 ? 93.881  155.206 176.853 1.00 161.76 ? 193  MET A O     1 
ATOM   936   C  CB    . MET A 1 193 ? 95.121  154.508 173.930 1.00 148.43 ? 193  MET A CB    1 
ATOM   937   C  CG    . MET A 1 193 ? 96.249  153.500 173.808 1.00 141.94 ? 193  MET A CG    1 
ATOM   938   S  SD    . MET A 1 193 ? 97.053  153.554 172.195 1.00 133.53 ? 193  MET A SD    1 
ATOM   939   C  CE    . MET A 1 193 ? 97.576  155.263 172.132 1.00 128.04 ? 193  MET A CE    1 
ATOM   940   N  N     . ASP A 1 194 ? 94.866  153.176 176.842 1.00 154.95 ? 194  ASP A N     1 
ATOM   941   C  CA    . ASP A 1 194 ? 95.202  153.243 178.254 1.00 152.18 ? 194  ASP A CA    1 
ATOM   942   C  C     . ASP A 1 194 ? 96.616  153.777 178.448 1.00 148.60 ? 194  ASP A C     1 
ATOM   943   O  O     . ASP A 1 194 ? 97.481  153.655 177.575 1.00 146.69 ? 194  ASP A O     1 
ATOM   944   C  CB    . ASP A 1 194 ? 95.049  151.868 178.909 1.00 151.51 ? 194  ASP A CB    1 
ATOM   945   C  CG    . ASP A 1 194 ? 95.820  150.784 178.185 1.00 151.54 ? 194  ASP A CG    1 
ATOM   946   O  OD1   . ASP A 1 194 ? 96.501  151.095 177.189 1.00 150.93 ? 194  ASP A OD1   1 
ATOM   947   O  OD2   . ASP A 1 194 ? 95.747  149.615 178.618 1.00 150.91 ? 194  ASP A OD2   1 
ATOM   948   N  N     . GLU A 1 195 ? 96.840  154.385 179.616 1.00 150.96 ? 195  GLU A N     1 
ATOM   949   C  CA    . GLU A 1 195 ? 98.108  155.060 179.875 1.00 151.57 ? 195  GLU A CA    1 
ATOM   950   C  C     . GLU A 1 195 ? 99.271  154.078 179.867 1.00 146.91 ? 195  GLU A C     1 
ATOM   951   O  O     . GLU A 1 195 ? 100.377 154.420 179.434 1.00 144.68 ? 195  GLU A O     1 
ATOM   952   C  CB    . GLU A 1 195 ? 98.018  155.836 181.198 1.00 153.03 ? 195  GLU A CB    1 
ATOM   953   C  CG    . GLU A 1 195 ? 97.750  155.023 182.478 1.00 154.43 ? 195  GLU A CG    1 
ATOM   954   C  CD    . GLU A 1 195 ? 98.957  154.261 183.008 1.00 153.17 ? 195  GLU A CD    1 
ATOM   955   O  OE1   . GLU A 1 195 ? 100.082 154.482 182.519 1.00 152.38 ? 195  GLU A OE1   1 
ATOM   956   O  OE2   . GLU A 1 195 ? 98.772  153.423 183.917 1.00 152.34 ? 195  GLU A OE2   1 
ATOM   957   N  N     . GLU A 1 196 ? 99.037  152.850 180.330 1.00 146.60 ? 196  GLU A N     1 
ATOM   958   C  CA    . GLU A 1 196 ? 100.119 151.878 180.435 1.00 147.61 ? 196  GLU A CA    1 
ATOM   959   C  C     . GLU A 1 196 ? 100.709 151.555 179.070 1.00 144.10 ? 196  GLU A C     1 
ATOM   960   O  O     . GLU A 1 196 ? 101.929 151.416 178.929 1.00 144.97 ? 196  GLU A O     1 
ATOM   961   C  CB    . GLU A 1 196 ? 99.616  150.607 181.118 1.00 151.43 ? 196  GLU A CB    1 
ATOM   962   C  CG    . GLU A 1 196 ? 100.668 149.529 181.272 1.00 149.18 ? 196  GLU A CG    1 
ATOM   963   C  CD    . GLU A 1 196 ? 100.144 148.313 182.005 1.00 155.31 ? 196  GLU A CD    1 
ATOM   964   O  OE1   . GLU A 1 196 ? 98.926  148.263 182.280 1.00 157.65 ? 196  GLU A OE1   1 
ATOM   965   O  OE2   . GLU A 1 196 ? 100.949 147.409 182.308 1.00 156.47 ? 196  GLU A OE2   1 
ATOM   966   N  N     . GLU A 1 197 ? 99.860  151.421 178.052 1.00 141.46 ? 197  GLU A N     1 
ATOM   967   C  CA    . GLU A 1 197 ? 100.365 151.145 176.713 1.00 138.06 ? 197  GLU A CA    1 
ATOM   968   C  C     . GLU A 1 197 ? 100.779 152.419 175.990 1.00 139.49 ? 197  GLU A C     1 
ATOM   969   O  O     . GLU A 1 197 ? 101.718 152.396 175.188 1.00 133.59 ? 197  GLU A O     1 
ATOM   970   C  CB    . GLU A 1 197 ? 99.310  150.397 175.901 1.00 139.55 ? 197  GLU A CB    1 
ATOM   971   C  CG    . GLU A 1 197 ? 99.771  149.965 174.526 1.00 139.10 ? 197  GLU A CG    1 
ATOM   972   C  CD    . GLU A 1 197 ? 98.659  149.327 173.724 1.00 141.78 ? 197  GLU A CD    1 
ATOM   973   O  OE1   . GLU A 1 197 ? 97.483  149.476 174.117 1.00 144.88 ? 197  GLU A OE1   1 
ATOM   974   O  OE2   . GLU A 1 197 ? 98.956  148.673 172.702 1.00 134.66 ? 197  GLU A OE2   1 
ATOM   975   N  N     . ALA A 1 198 ? 100.096 153.535 176.255 1.00 143.98 ? 198  ALA A N     1 
ATOM   976   C  CA    . ALA A 1 198 ? 100.385 154.759 175.515 1.00 137.26 ? 198  ALA A CA    1 
ATOM   977   C  C     . ALA A 1 198 ? 101.711 155.379 175.938 1.00 132.05 ? 198  ALA A C     1 
ATOM   978   O  O     . ALA A 1 198 ? 102.527 155.748 175.086 1.00 127.86 ? 198  ALA A O     1 
ATOM   979   C  CB    . ALA A 1 198 ? 99.246  155.761 175.696 1.00 137.82 ? 198  ALA A CB    1 
ATOM   980   N  N     . ARG A 1 199 ? 101.954 155.489 177.244 1.00 135.39 ? 199  ARG A N     1 
ATOM   981   C  CA    . ARG A 1 199 ? 103.080 156.263 177.750 1.00 135.18 ? 199  ARG A CA    1 
ATOM   982   C  C     . ARG A 1 199 ? 104.319 155.430 178.045 1.00 132.79 ? 199  ARG A C     1 
ATOM   983   O  O     . ARG A 1 199 ? 105.385 156.007 178.282 1.00 133.03 ? 199  ARG A O     1 
ATOM   984   C  CB    . ARG A 1 199 ? 102.674 157.014 179.025 1.00 136.58 ? 199  ARG A CB    1 
ATOM   985   C  CG    . ARG A 1 199 ? 103.440 158.309 179.248 1.00 139.76 ? 199  ARG A CG    1 
ATOM   986   C  CD    . ARG A 1 199 ? 102.653 159.335 180.058 1.00 145.54 ? 199  ARG A CD    1 
ATOM   987   N  NE    . ARG A 1 199 ? 101.368 159.677 179.461 1.00 149.02 ? 199  ARG A NE    1 
ATOM   988   C  CZ    . ARG A 1 199 ? 100.207 159.160 179.840 1.00 152.03 ? 199  ARG A CZ    1 
ATOM   989   N  NH1   . ARG A 1 199 ? 100.131 158.283 180.825 1.00 150.71 ? 199  ARG A NH1   1 
ATOM   990   N  NH2   . ARG A 1 199 ? 99.094  159.540 179.220 1.00 153.01 ? 199  ARG A NH2   1 
ATOM   991   N  N     . ARG A 1 200 ? 104.214 154.106 178.046 1.00 131.34 ? 200  ARG A N     1 
ATOM   992   C  CA    . ARG A 1 200 ? 105.305 153.238 178.469 1.00 126.17 ? 200  ARG A CA    1 
ATOM   993   C  C     . ARG A 1 200 ? 105.772 152.384 177.298 1.00 120.57 ? 200  ARG A C     1 
ATOM   994   O  O     . ARG A 1 200 ? 104.957 151.958 176.472 1.00 123.89 ? 200  ARG A O     1 
ATOM   995   C  CB    . ARG A 1 200 ? 104.855 152.350 179.628 1.00 131.73 ? 200  ARG A CB    1 
ATOM   996   C  CG    . ARG A 1 200 ? 105.972 151.881 180.537 1.00 135.05 ? 200  ARG A CG    1 
ATOM   997   C  CD    . ARG A 1 200 ? 105.408 151.216 181.791 1.00 141.56 ? 200  ARG A CD    1 
ATOM   998   N  NE    . ARG A 1 200 ? 104.359 151.982 182.461 1.00 145.03 ? 200  ARG A NE    1 
ATOM   999   C  CZ    . ARG A 1 200 ? 104.424 153.263 182.807 1.00 149.51 ? 200  ARG A CZ    1 
ATOM   1000  N  NH1   . ARG A 1 200 ? 105.525 153.977 182.641 1.00 146.40 ? 200  ARG A NH1   1 
ATOM   1001  N  NH2   . ARG A 1 200 ? 103.361 153.839 183.361 1.00 152.09 ? 200  ARG A NH2   1 
ATOM   1002  N  N     . MET A 1 201 ? 107.077 152.134 177.227 1.00 120.51 ? 201  MET A N     1 
ATOM   1003  C  CA    . MET A 1 201 ? 107.663 151.342 176.156 1.00 114.59 ? 201  MET A CA    1 
ATOM   1004  C  C     . MET A 1 201 ? 108.238 150.050 176.720 1.00 121.31 ? 201  MET A C     1 
ATOM   1005  O  O     . MET A 1 201 ? 109.011 150.068 177.681 1.00 130.02 ? 201  MET A O     1 
ATOM   1006  C  CB    . MET A 1 201 ? 108.751 152.127 175.419 1.00 113.68 ? 201  MET A CB    1 
ATOM   1007  C  CG    . MET A 1 201 ? 109.773 151.269 174.691 1.00 109.75 ? 201  MET A CG    1 
ATOM   1008  S  SD    . MET A 1 201 ? 111.259 150.939 175.648 1.00 123.22 ? 201  MET A SD    1 
ATOM   1009  C  CE    . MET A 1 201 ? 112.386 152.119 174.914 1.00 117.41 ? 201  MET A CE    1 
ATOM   1010  N  N     . TRP A 1 202 ? 107.868 148.936 176.100 1.00 116.89 ? 202  TRP A N     1 
ATOM   1011  C  CA    . TRP A 1 202 ? 108.167 147.589 176.563 1.00 113.50 ? 202  TRP A CA    1 
ATOM   1012  C  C     . TRP A 1 202 ? 109.346 147.008 175.792 1.00 111.62 ? 202  TRP A C     1 
ATOM   1013  O  O     . TRP A 1 202 ? 109.445 147.164 174.574 1.00 112.72 ? 202  TRP A O     1 
ATOM   1014  C  CB    . TRP A 1 202 ? 106.925 146.711 176.393 1.00 109.56 ? 202  TRP A CB    1 
ATOM   1015  C  CG    . TRP A 1 202 ? 105.806 147.093 177.313 1.00 114.85 ? 202  TRP A CG    1 
ATOM   1016  C  CD1   . TRP A 1 202 ? 104.540 147.437 176.955 1.00 121.13 ? 202  TRP A CD1   1 
ATOM   1017  C  CD2   . TRP A 1 202 ? 105.807 147.021 178.744 1.00 121.94 ? 202  TRP A CD2   1 
ATOM   1018  N  NE1   . TRP A 1 202 ? 103.776 147.671 178.069 1.00 129.33 ? 202  TRP A NE1   1 
ATOM   1019  C  CE2   . TRP A 1 202 ? 104.529 147.411 179.182 1.00 130.23 ? 202  TRP A CE2   1 
ATOM   1020  C  CE3   . TRP A 1 202 ? 106.773 146.693 179.696 1.00 122.40 ? 202  TRP A CE3   1 
ATOM   1021  C  CZ2   . TRP A 1 202 ? 104.192 147.486 180.530 1.00 135.10 ? 202  TRP A CZ2   1 
ATOM   1022  C  CZ3   . TRP A 1 202 ? 106.438 146.771 181.035 1.00 132.34 ? 202  TRP A CZ3   1 
ATOM   1023  C  CH2   . TRP A 1 202 ? 105.159 147.164 181.439 1.00 138.31 ? 202  TRP A CH2   1 
ATOM   1024  N  N     . TYR A 1 203 ? 110.242 146.337 176.514 1.00 110.51 ? 203  TYR A N     1 
ATOM   1025  C  CA    . TYR A 1 203 ? 111.452 145.794 175.914 1.00 105.73 ? 203  TYR A CA    1 
ATOM   1026  C  C     . TYR A 1 203 ? 111.828 144.488 176.597 1.00 109.27 ? 203  TYR A C     1 
ATOM   1027  O  O     . TYR A 1 203 ? 111.691 144.360 177.815 1.00 120.21 ? 203  TYR A O     1 
ATOM   1028  C  CB    . TYR A 1 203 ? 112.618 146.778 176.027 1.00 103.70 ? 203  TYR A CB    1 
ATOM   1029  C  CG    . TYR A 1 203 ? 113.976 146.122 175.957 1.00 105.92 ? 203  TYR A CG    1 
ATOM   1030  C  CD1   . TYR A 1 203 ? 114.474 145.648 174.755 1.00 111.51 ? 203  TYR A CD1   1 
ATOM   1031  C  CD2   . TYR A 1 203 ? 114.757 145.967 177.090 1.00 107.55 ? 203  TYR A CD2   1 
ATOM   1032  C  CE1   . TYR A 1 203 ? 115.710 145.049 174.680 1.00 112.64 ? 203  TYR A CE1   1 
ATOM   1033  C  CE2   . TYR A 1 203 ? 115.996 145.366 177.023 1.00 109.85 ? 203  TYR A CE2   1 
ATOM   1034  C  CZ    . TYR A 1 203 ? 116.466 144.910 175.815 1.00 108.61 ? 203  TYR A CZ    1 
ATOM   1035  O  OH    . TYR A 1 203 ? 117.698 144.310 175.735 1.00 105.24 ? 203  TYR A OH    1 
ATOM   1036  N  N     . THR A 1 204 ? 112.324 143.530 175.808 1.00 106.80 ? 204  THR A N     1 
ATOM   1037  C  CA    . THR A 1 204 ? 112.794 142.255 176.337 1.00 113.73 ? 204  THR A CA    1 
ATOM   1038  C  C     . THR A 1 204 ? 113.867 141.669 175.433 1.00 112.26 ? 204  THR A C     1 
ATOM   1039  O  O     . THR A 1 204 ? 113.646 141.552 174.220 1.00 113.77 ? 204  THR A O     1 
ATOM   1040  C  CB    . THR A 1 204 ? 111.652 141.246 176.490 1.00 118.92 ? 204  THR A CB    1 
ATOM   1041  O  OG1   . THR A 1 204 ? 112.195 139.923 176.584 1.00 113.52 ? 204  THR A OG1   1 
ATOM   1042  C  CG2   . THR A 1 204 ? 110.697 141.321 175.312 1.00 117.56 ? 204  THR A CG2   1 
ATOM   1043  N  N     . PRO A 1 205 ? 115.026 141.299 175.979 1.00 111.61 ? 205  PRO A N     1 
ATOM   1044  C  CA    . PRO A 1 205 ? 116.050 140.628 175.173 1.00 113.68 ? 205  PRO A CA    1 
ATOM   1045  C  C     . PRO A 1 205 ? 115.748 139.146 175.028 1.00 118.18 ? 205  PRO A C     1 
ATOM   1046  O  O     . PRO A 1 205 ? 115.223 138.499 175.936 1.00 123.20 ? 205  PRO A O     1 
ATOM   1047  C  CB    . PRO A 1 205 ? 117.327 140.858 175.990 1.00 112.04 ? 205  PRO A CB    1 
ATOM   1048  C  CG    . PRO A 1 205 ? 116.848 140.870 177.399 1.00 110.52 ? 205  PRO A CG    1 
ATOM   1049  C  CD    . PRO A 1 205 ? 115.428 141.405 177.392 1.00 111.49 ? 205  PRO A CD    1 
ATOM   1050  N  N     . VAL A 1 206 ? 116.085 138.598 173.865 1.00 117.42 ? 206  VAL A N     1 
ATOM   1051  C  CA    . VAL A 1 206 ? 115.722 137.226 173.545 1.00 118.49 ? 206  VAL A CA    1 
ATOM   1052  C  C     . VAL A 1 206 ? 116.979 136.421 173.262 1.00 120.59 ? 206  VAL A C     1 
ATOM   1053  O  O     . VAL A 1 206 ? 117.844 136.828 172.482 1.00 118.23 ? 206  VAL A O     1 
ATOM   1054  C  CB    . VAL A 1 206 ? 114.758 137.153 172.343 1.00 117.44 ? 206  VAL A CB    1 
ATOM   1055  C  CG1   . VAL A 1 206 ? 113.359 137.457 172.777 1.00 121.20 ? 206  VAL A CG1   1 
ATOM   1056  C  CG2   . VAL A 1 206 ? 115.167 138.121 171.291 1.00 112.43 ? 206  VAL A CG2   1 
ATOM   1057  N  N     . TYR A 1 207 ? 117.069 135.258 173.900 1.00 124.55 ? 207  TYR A N     1 
ATOM   1058  C  CA    . TYR A 1 207 ? 118.128 134.306 173.618 1.00 125.00 ? 207  TYR A CA    1 
ATOM   1059  C  C     . TYR A 1 207 ? 117.803 133.410 172.431 1.00 129.69 ? 207  TYR A C     1 
ATOM   1060  O  O     . TYR A 1 207 ? 118.732 132.932 171.773 1.00 129.86 ? 207  TYR A O     1 
ATOM   1061  C  CB    . TYR A 1 207 ? 118.390 133.415 174.843 1.00 118.35 ? 207  TYR A CB    1 
ATOM   1062  C  CG    . TYR A 1 207 ? 119.627 132.536 174.751 1.00 125.01 ? 207  TYR A CG    1 
ATOM   1063  C  CD1   . TYR A 1 207 ? 120.636 132.792 173.831 1.00 128.98 ? 207  TYR A CD1   1 
ATOM   1064  C  CD2   . TYR A 1 207 ? 119.736 131.393 175.525 1.00 131.85 ? 207  TYR A CD2   1 
ATOM   1065  C  CE1   . TYR A 1 207 ? 121.743 131.972 173.731 1.00 134.12 ? 207  TYR A CE1   1 
ATOM   1066  C  CE2   . TYR A 1 207 ? 120.836 130.562 175.423 1.00 136.50 ? 207  TYR A CE2   1 
ATOM   1067  C  CZ    . TYR A 1 207 ? 121.837 130.858 174.530 1.00 138.11 ? 207  TYR A CZ    1 
ATOM   1068  O  OH    . TYR A 1 207 ? 122.935 130.034 174.432 1.00 146.16 ? 207  TYR A OH    1 
ATOM   1069  N  N     . CYS A 1 208 ? 116.511 133.205 172.119 1.00 128.05 ? 208  CYS A N     1 
ATOM   1070  C  CA    . CYS A 1 208 ? 116.029 132.094 171.301 1.00 125.74 ? 208  CYS A CA    1 
ATOM   1071  C  C     . CYS A 1 208 ? 116.898 131.914 170.063 1.00 131.17 ? 208  CYS A C     1 
ATOM   1072  O  O     . CYS A 1 208 ? 116.842 132.731 169.137 1.00 130.61 ? 208  CYS A O     1 
ATOM   1073  C  CB    . CYS A 1 208 ? 114.570 132.320 170.895 1.00 125.39 ? 208  CYS A CB    1 
ATOM   1074  S  SG    . CYS A 1 208 ? 113.881 131.052 169.806 1.00 136.85 ? 208  CYS A SG    1 
ATOM   1075  N  N     . PRO A 1 209 ? 117.715 130.856 170.018 1.00 134.47 ? 209  PRO A N     1 
ATOM   1076  C  CA    . PRO A 1 209 ? 118.632 130.700 168.877 1.00 134.21 ? 209  PRO A CA    1 
ATOM   1077  C  C     . PRO A 1 209 ? 117.940 130.165 167.642 1.00 134.68 ? 209  PRO A C     1 
ATOM   1078  O  O     . PRO A 1 209 ? 118.156 130.677 166.537 1.00 137.80 ? 209  PRO A O     1 
ATOM   1079  C  CB    . PRO A 1 209 ? 119.683 129.720 169.416 1.00 131.67 ? 209  PRO A CB    1 
ATOM   1080  C  CG    . PRO A 1 209 ? 118.922 128.891 170.410 1.00 133.31 ? 209  PRO A CG    1 
ATOM   1081  C  CD    . PRO A 1 209 ? 117.915 129.817 171.043 1.00 132.97 ? 209  PRO A CD    1 
ATOM   1082  N  N     . HIS A 1 210 ? 117.102 129.155 167.807 1.00 131.67 ? 210  HIS A N     1 
ATOM   1083  C  CA    . HIS A 1 210 ? 116.329 128.585 166.721 1.00 132.98 ? 210  HIS A CA    1 
ATOM   1084  C  C     . HIS A 1 210 ? 114.926 129.152 166.833 1.00 128.76 ? 210  HIS A C     1 
ATOM   1085  O  O     . HIS A 1 210 ? 114.129 128.644 167.639 1.00 129.04 ? 210  HIS A O     1 
ATOM   1086  C  CB    . HIS A 1 210 ? 116.305 127.059 166.844 1.00 138.62 ? 210  HIS A CB    1 
ATOM   1087  C  CG    . HIS A 1 210 ? 117.637 126.412 166.633 1.00 150.91 ? 210  HIS A CG    1 
ATOM   1088  N  ND1   . HIS A 1 210 ? 118.476 126.799 165.615 1.00 152.85 ? 210  HIS A ND1   1 
ATOM   1089  C  CD2   . HIS A 1 210 ? 118.272 125.411 167.292 1.00 158.96 ? 210  HIS A CD2   1 
ATOM   1090  C  CE1   . HIS A 1 210 ? 119.570 126.062 165.651 1.00 155.03 ? 210  HIS A CE1   1 
ATOM   1091  N  NE2   . HIS A 1 210 ? 119.473 125.213 166.658 1.00 159.96 ? 210  HIS A NE2   1 
ATOM   1092  N  N     . PRO A 1 211 ? 114.562 130.175 166.060 1.00 122.85 ? 211  PRO A N     1 
ATOM   1093  C  CA    . PRO A 1 211 ? 113.378 130.975 166.418 1.00 121.59 ? 211  PRO A CA    1 
ATOM   1094  C  C     . PRO A 1 211 ? 112.069 130.186 166.463 1.00 124.30 ? 211  PRO A C     1 
ATOM   1095  O  O     . PRO A 1 211 ? 111.003 130.793 166.640 1.00 126.92 ? 211  PRO A O     1 
ATOM   1096  C  CB    . PRO A 1 211 ? 113.336 132.051 165.327 1.00 115.29 ? 211  PRO A CB    1 
ATOM   1097  C  CG    . PRO A 1 211 ? 114.729 132.066 164.754 1.00 115.81 ? 211  PRO A CG    1 
ATOM   1098  C  CD    . PRO A 1 211 ? 115.220 130.667 164.841 1.00 120.25 ? 211  PRO A CD    1 
ATOM   1099  N  N     . ILE A 1 212 ? 112.104 128.861 166.310 1.00 122.01 ? 212  ILE A N     1 
ATOM   1100  C  CA    . ILE A 1 212 ? 110.878 128.072 166.385 1.00 120.62 ? 212  ILE A CA    1 
ATOM   1101  C  C     . ILE A 1 212 ? 110.356 128.008 167.816 1.00 123.12 ? 212  ILE A C     1 
ATOM   1102  O  O     . ILE A 1 212 ? 109.148 128.146 168.048 1.00 126.45 ? 212  ILE A O     1 
ATOM   1103  C  CB    . ILE A 1 212 ? 111.085 126.664 165.785 1.00 119.79 ? 212  ILE A CB    1 
ATOM   1104  C  CG1   . ILE A 1 212 ? 111.950 126.700 164.519 1.00 118.34 ? 212  ILE A CG1   1 
ATOM   1105  C  CG2   . ILE A 1 212 ? 109.759 126.004 165.497 1.00 120.42 ? 212  ILE A CG2   1 
ATOM   1106  C  CD1   . ILE A 1 212 ? 113.431 126.571 164.758 1.00 123.04 ? 212  ILE A CD1   1 
ATOM   1107  N  N     . ASP A 1 213 ? 111.240 127.808 168.801 1.00 123.75 ? 213  ASP A N     1 
ATOM   1108  C  CA    . ASP A 1 213 ? 110.788 127.721 170.184 1.00 129.79 ? 213  ASP A CA    1 
ATOM   1109  C  C     . ASP A 1 213 ? 110.773 129.079 170.865 1.00 124.91 ? 213  ASP A C     1 
ATOM   1110  O  O     . ASP A 1 213 ? 111.024 129.165 172.071 1.00 126.37 ? 213  ASP A O     1 
ATOM   1111  C  CB    . ASP A 1 213 ? 111.644 126.749 170.993 1.00 133.60 ? 213  ASP A CB    1 
ATOM   1112  C  CG    . ASP A 1 213 ? 113.107 126.815 170.643 1.00 135.26 ? 213  ASP A CG    1 
ATOM   1113  O  OD1   . ASP A 1 213 ? 113.516 127.713 169.885 1.00 131.45 ? 213  ASP A OD1   1 
ATOM   1114  O  OD2   . ASP A 1 213 ? 113.846 125.943 171.150 1.00 138.91 ? 213  ASP A OD2   1 
ATOM   1115  N  N     . PHE A 1 214 ? 110.532 130.142 170.100 1.00 118.71 ? 214  PHE A N     1 
ATOM   1116  C  CA    . PHE A 1 214 ? 110.374 131.470 170.674 1.00 117.97 ? 214  PHE A CA    1 
ATOM   1117  C  C     . PHE A 1 214 ? 109.252 131.489 171.701 1.00 123.19 ? 214  PHE A C     1 
ATOM   1118  O  O     . PHE A 1 214 ? 109.401 132.068 172.782 1.00 130.52 ? 214  PHE A O     1 
ATOM   1119  C  CB    . PHE A 1 214 ? 110.099 132.464 169.551 1.00 119.28 ? 214  PHE A CB    1 
ATOM   1120  C  CG    . PHE A 1 214 ? 110.165 133.894 169.969 1.00 117.02 ? 214  PHE A CG    1 
ATOM   1121  C  CD1   . PHE A 1 214 ? 111.373 134.552 170.027 1.00 117.10 ? 214  PHE A CD1   1 
ATOM   1122  C  CD2   . PHE A 1 214 ? 109.016 134.581 170.300 1.00 112.33 ? 214  PHE A CD2   1 
ATOM   1123  C  CE1   . PHE A 1 214 ? 111.432 135.871 170.402 1.00 113.52 ? 214  PHE A CE1   1 
ATOM   1124  C  CE2   . PHE A 1 214 ? 109.072 135.900 170.682 1.00 108.95 ? 214  PHE A CE2   1 
ATOM   1125  C  CZ    . PHE A 1 214 ? 110.280 136.545 170.734 1.00 108.53 ? 214  PHE A CZ    1 
ATOM   1126  N  N     . SER A 1 215 ? 108.120 130.858 171.384 1.00 121.25 ? 215  SER A N     1 
ATOM   1127  C  CA    . SER A 1 215 ? 107.023 130.743 172.336 1.00 123.90 ? 215  SER A CA    1 
ATOM   1128  C  C     . SER A 1 215 ? 107.269 129.682 173.402 1.00 126.66 ? 215  SER A C     1 
ATOM   1129  O  O     . SER A 1 215 ? 106.632 129.733 174.459 1.00 127.77 ? 215  SER A O     1 
ATOM   1130  C  CB    . SER A 1 215 ? 105.712 130.440 171.605 1.00 126.09 ? 215  SER A CB    1 
ATOM   1131  O  OG    . SER A 1 215 ? 105.930 129.633 170.460 1.00 125.15 ? 215  SER A OG    1 
ATOM   1132  N  N     . ASN A 1 216 ? 108.175 128.732 173.160 1.00 127.04 ? 216  ASN A N     1 
ATOM   1133  C  CA    . ASN A 1 216 ? 108.420 127.674 174.133 1.00 128.29 ? 216  ASN A CA    1 
ATOM   1134  C  C     . ASN A 1 216 ? 109.252 128.152 175.315 1.00 127.57 ? 216  ASN A C     1 
ATOM   1135  O  O     . ASN A 1 216 ? 109.090 127.636 176.426 1.00 131.82 ? 216  ASN A O     1 
ATOM   1136  C  CB    . ASN A 1 216 ? 109.111 126.485 173.464 1.00 125.86 ? 216  ASN A CB    1 
ATOM   1137  C  CG    . ASN A 1 216 ? 108.217 125.773 172.469 1.00 127.35 ? 216  ASN A CG    1 
ATOM   1138  O  OD1   . ASN A 1 216 ? 108.685 125.250 171.459 1.00 124.86 ? 216  ASN A OD1   1 
ATOM   1139  N  ND2   . ASN A 1 216 ? 106.919 125.754 172.749 1.00 129.68 ? 216  ASN A ND2   1 
ATOM   1140  N  N     . LEU A 1 217 ? 110.135 129.126 175.105 1.00 124.71 ? 217  LEU A N     1 
ATOM   1141  C  CA    . LEU A 1 217 ? 111.000 129.614 176.171 1.00 124.40 ? 217  LEU A CA    1 
ATOM   1142  C  C     . LEU A 1 217 ? 110.319 130.639 177.066 1.00 129.78 ? 217  LEU A C     1 
ATOM   1143  O  O     . LEU A 1 217 ? 110.951 131.130 178.007 1.00 135.84 ? 217  LEU A O     1 
ATOM   1144  C  CB    . LEU A 1 217 ? 112.275 130.219 175.583 1.00 118.88 ? 217  LEU A CB    1 
ATOM   1145  C  CG    . LEU A 1 217 ? 113.095 129.330 174.652 1.00 123.05 ? 217  LEU A CG    1 
ATOM   1146  C  CD1   . LEU A 1 217 ? 114.430 129.978 174.334 1.00 120.73 ? 217  LEU A CD1   1 
ATOM   1147  C  CD2   . LEU A 1 217 ? 113.295 127.961 175.270 1.00 124.24 ? 217  LEU A CD2   1 
ATOM   1148  N  N     . GLY A 1 218 ? 109.062 130.978 176.797 1.00 131.29 ? 218  GLY A N     1 
ATOM   1149  C  CA    . GLY A 1 218 ? 108.327 131.908 177.624 1.00 133.45 ? 218  GLY A CA    1 
ATOM   1150  C  C     . GLY A 1 218 ? 108.279 133.328 177.109 1.00 133.07 ? 218  GLY A C     1 
ATOM   1151  O  O     . GLY A 1 218 ? 107.794 134.209 177.828 1.00 141.55 ? 218  GLY A O     1 
ATOM   1152  N  N     . TYR A 1 219 ? 108.765 133.580 175.898 1.00 125.88 ? 219  TYR A N     1 
ATOM   1153  C  CA    . TYR A 1 219 ? 108.752 134.931 175.362 1.00 126.00 ? 219  TYR A CA    1 
ATOM   1154  C  C     . TYR A 1 219 ? 107.363 135.277 174.841 1.00 126.85 ? 219  TYR A C     1 
ATOM   1155  O  O     . TYR A 1 219 ? 106.769 134.524 174.065 1.00 129.51 ? 219  TYR A O     1 
ATOM   1156  C  CB    . TYR A 1 219 ? 109.771 135.069 174.237 1.00 122.95 ? 219  TYR A CB    1 
ATOM   1157  C  CG    . TYR A 1 219 ? 111.201 134.844 174.660 1.00 122.36 ? 219  TYR A CG    1 
ATOM   1158  C  CD1   . TYR A 1 219 ? 111.931 135.839 175.287 1.00 120.23 ? 219  TYR A CD1   1 
ATOM   1159  C  CD2   . TYR A 1 219 ? 111.832 133.638 174.403 1.00 123.59 ? 219  TYR A CD2   1 
ATOM   1160  C  CE1   . TYR A 1 219 ? 113.247 135.631 175.660 1.00 117.19 ? 219  TYR A CE1   1 
ATOM   1161  C  CE2   . TYR A 1 219 ? 113.143 133.425 174.771 1.00 124.79 ? 219  TYR A CE2   1 
ATOM   1162  C  CZ    . TYR A 1 219 ? 113.845 134.423 175.399 1.00 119.80 ? 219  TYR A CZ    1 
ATOM   1163  O  OH    . TYR A 1 219 ? 115.152 134.207 175.768 1.00 117.69 ? 219  TYR A OH    1 
ATOM   1164  N  N     . ARG A 1 220 ? 106.844 136.423 175.271 1.00 124.56 ? 220  ARG A N     1 
ATOM   1165  C  CA    . ARG A 1 220 ? 105.552 136.898 174.802 1.00 123.78 ? 220  ARG A CA    1 
ATOM   1166  C  C     . ARG A 1 220 ? 105.677 138.336 174.329 1.00 127.58 ? 220  ARG A C     1 
ATOM   1167  O  O     . ARG A 1 220 ? 106.544 139.089 174.775 1.00 129.02 ? 220  ARG A O     1 
ATOM   1168  C  CB    . ARG A 1 220 ? 104.468 136.791 175.883 1.00 130.64 ? 220  ARG A CB    1 
ATOM   1169  C  CG    . ARG A 1 220 ? 104.463 135.479 176.636 1.00 136.76 ? 220  ARG A CG    1 
ATOM   1170  C  CD    . ARG A 1 220 ? 104.040 134.340 175.726 1.00 130.00 ? 220  ARG A CD    1 
ATOM   1171  N  NE    . ARG A 1 220 ? 104.446 133.044 176.255 1.00 135.62 ? 220  ARG A NE    1 
ATOM   1172  C  CZ    . ARG A 1 220 ? 104.128 131.879 175.710 1.00 139.39 ? 220  ARG A CZ    1 
ATOM   1173  N  NH1   . ARG A 1 220 ? 103.391 131.807 174.614 1.00 142.16 ? 220  ARG A NH1   1 
ATOM   1174  N  NH2   . ARG A 1 220 ? 104.561 130.758 176.278 1.00 141.00 ? 220  ARG A NH2   1 
ATOM   1175  N  N     . LEU A 1 221 ? 104.792 138.702 173.413 1.00 129.13 ? 221  LEU A N     1 
ATOM   1176  C  CA    . LEU A 1 221 ? 104.689 140.059 172.905 1.00 128.00 ? 221  LEU A CA    1 
ATOM   1177  C  C     . LEU A 1 221 ? 103.512 140.766 173.566 1.00 130.45 ? 221  LEU A C     1 
ATOM   1178  O  O     . LEU A 1 221 ? 102.625 140.137 174.151 1.00 132.40 ? 221  LEU A O     1 
ATOM   1179  C  CB    . LEU A 1 221 ? 104.523 140.057 171.384 1.00 121.59 ? 221  LEU A CB    1 
ATOM   1180  C  CG    . LEU A 1 221 ? 105.580 139.288 170.592 1.00 110.20 ? 221  LEU A CG    1 
ATOM   1181  C  CD1   . LEU A 1 221 ? 105.371 139.468 169.101 1.00 100.99 ? 221  LEU A CD1   1 
ATOM   1182  C  CD2   . LEU A 1 221 ? 106.970 139.733 170.992 1.00 111.77 ? 221  LEU A CD2   1 
ATOM   1183  N  N     . ARG A 1 222 ? 103.521 142.096 173.474 1.00 127.37 ? 222  ARG A N     1 
ATOM   1184  C  CA    . ARG A 1 222 ? 102.497 142.879 174.155 1.00 129.04 ? 222  ARG A CA    1 
ATOM   1185  C  C     . ARG A 1 222 ? 101.111 142.594 173.596 1.00 130.49 ? 222  ARG A C     1 
ATOM   1186  O  O     . ARG A 1 222 ? 100.116 142.679 174.321 1.00 131.00 ? 222  ARG A O     1 
ATOM   1187  C  CB    . ARG A 1 222 ? 102.820 144.365 174.065 1.00 126.40 ? 222  ARG A CB    1 
ATOM   1188  C  CG    . ARG A 1 222 ? 103.723 144.823 175.175 1.00 121.85 ? 222  ARG A CG    1 
ATOM   1189  C  CD    . ARG A 1 222 ? 103.123 144.480 176.527 1.00 122.56 ? 222  ARG A CD    1 
ATOM   1190  N  NE    . ARG A 1 222 ? 102.077 145.415 176.920 1.00 126.49 ? 222  ARG A NE    1 
ATOM   1191  C  CZ    . ARG A 1 222 ? 101.343 145.297 178.017 1.00 130.13 ? 222  ARG A CZ    1 
ATOM   1192  N  NH1   . ARG A 1 222 ? 101.521 144.297 178.863 1.00 126.10 ? 222  ARG A NH1   1 
ATOM   1193  N  NH2   . ARG A 1 222 ? 100.407 146.207 178.273 1.00 138.84 ? 222  ARG A NH2   1 
ATOM   1194  N  N     . CYS A 1 223 ? 101.024 142.248 172.311 1.00 124.92 ? 223  CYS A N     1 
ATOM   1195  C  CA    . CYS A 1 223 ? 99.734  141.860 171.752 1.00 125.77 ? 223  CYS A CA    1 
ATOM   1196  C  C     . CYS A 1 223 ? 99.172  140.643 172.474 1.00 132.04 ? 223  CYS A C     1 
ATOM   1197  O  O     . CYS A 1 223 ? 98.004  140.635 172.884 1.00 132.11 ? 223  CYS A O     1 
ATOM   1198  C  CB    . CYS A 1 223 ? 99.877  141.584 170.258 1.00 118.61 ? 223  CYS A CB    1 
ATOM   1199  S  SG    . CYS A 1 223 ? 100.512 142.984 169.324 1.00 130.91 ? 223  CYS A SG    1 
ATOM   1200  N  N     . VAL A 1 224 ? 100.000 139.613 172.662 1.00 130.57 ? 224  VAL A N     1 
ATOM   1201  C  CA    . VAL A 1 224 ? 99.551  138.415 173.362 1.00 127.88 ? 224  VAL A CA    1 
ATOM   1202  C  C     . VAL A 1 224 ? 99.235  138.730 174.819 1.00 129.96 ? 224  VAL A C     1 
ATOM   1203  O  O     . VAL A 1 224 ? 98.241  138.240 175.369 1.00 134.51 ? 224  VAL A O     1 
ATOM   1204  C  CB    . VAL A 1 224 ? 100.604 137.301 173.240 1.00 126.14 ? 224  VAL A CB    1 
ATOM   1205  C  CG1   . VAL A 1 224 ? 100.057 135.999 173.791 1.00 132.96 ? 224  VAL A CG1   1 
ATOM   1206  C  CG2   . VAL A 1 224 ? 101.029 137.136 171.797 1.00 118.16 ? 224  VAL A CG2   1 
ATOM   1207  N  N     . GLU A 1 225 ? 100.074 139.540 175.469 1.00 125.44 ? 225  GLU A N     1 
ATOM   1208  C  CA    . GLU A 1 225 ? 99.857  139.830 176.884 1.00 128.23 ? 225  GLU A CA    1 
ATOM   1209  C  C     . GLU A 1 225 ? 98.571  140.619 177.106 1.00 129.24 ? 225  GLU A C     1 
ATOM   1210  O  O     . GLU A 1 225 ? 97.831  140.354 178.060 1.00 128.26 ? 225  GLU A O     1 
ATOM   1211  C  CB    . GLU A 1 225 ? 101.055 140.580 177.461 1.00 135.27 ? 225  GLU A CB    1 
ATOM   1212  C  CG    . GLU A 1 225 ? 102.344 139.782 177.440 1.00 136.81 ? 225  GLU A CG    1 
ATOM   1213  C  CD    . GLU A 1 225 ? 103.536 140.593 177.900 1.00 142.01 ? 225  GLU A CD    1 
ATOM   1214  O  OE1   . GLU A 1 225 ? 103.357 141.784 178.227 1.00 142.27 ? 225  GLU A OE1   1 
ATOM   1215  O  OE2   . GLU A 1 225 ? 104.653 140.040 177.932 1.00 143.70 ? 225  GLU A OE2   1 
ATOM   1216  N  N     . THR A 1 226 ? 98.286  141.593 176.240 1.00 128.10 ? 226  THR A N     1 
ATOM   1217  C  CA    . THR A 1 226 ? 97.069  142.382 176.368 1.00 129.78 ? 226  THR A CA    1 
ATOM   1218  C  C     . THR A 1 226 ? 95.851  141.671 175.798 1.00 130.76 ? 226  THR A C     1 
ATOM   1219  O  O     . THR A 1 226 ? 94.724  142.116 176.042 1.00 134.95 ? 226  THR A O     1 
ATOM   1220  C  CB    . THR A 1 226 ? 97.245  143.734 175.675 1.00 128.08 ? 226  THR A CB    1 
ATOM   1221  O  OG1   . THR A 1 226 ? 98.616  144.139 175.760 1.00 127.37 ? 226  THR A OG1   1 
ATOM   1222  C  CG2   . THR A 1 226 ? 96.377  144.793 176.337 1.00 127.85 ? 226  THR A CG2   1 
ATOM   1223  N  N     . GLY A 1 227 ? 96.044  140.581 175.058 1.00 127.91 ? 227  GLY A N     1 
ATOM   1224  C  CA    . GLY A 1 227 ? 94.942  139.848 174.485 1.00 123.57 ? 227  GLY A CA    1 
ATOM   1225  C  C     . GLY A 1 227 ? 94.553  140.276 173.090 1.00 120.83 ? 227  GLY A C     1 
ATOM   1226  O  O     . GLY A 1 227 ? 93.679  139.641 172.487 1.00 124.65 ? 227  GLY A O     1 
ATOM   1227  N  N     . ARG A 1 228 ? 95.165  141.331 172.560 1.00 121.72 ? 228  ARG A N     1 
ATOM   1228  C  CA    . ARG A 1 228 ? 94.921  141.706 171.177 1.00 124.05 ? 228  ARG A CA    1 
ATOM   1229  C  C     . ARG A 1 228 ? 95.456  140.624 170.252 1.00 121.32 ? 228  ARG A C     1 
ATOM   1230  O  O     . ARG A 1 228 ? 96.570  140.125 170.431 1.00 122.65 ? 228  ARG A O     1 
ATOM   1231  C  CB    . ARG A 1 228 ? 95.566  143.053 170.859 1.00 121.15 ? 228  ARG A CB    1 
ATOM   1232  C  CG    . ARG A 1 228 ? 94.957  144.208 171.630 1.00 123.26 ? 228  ARG A CG    1 
ATOM   1233  C  CD    . ARG A 1 228 ? 95.716  145.498 171.397 1.00 120.77 ? 228  ARG A CD    1 
ATOM   1234  N  NE    . ARG A 1 228 ? 95.090  146.621 172.082 1.00 128.32 ? 228  ARG A NE    1 
ATOM   1235  C  CZ    . ARG A 1 228 ? 95.632  147.826 172.193 1.00 134.00 ? 228  ARG A CZ    1 
ATOM   1236  N  NH1   . ARG A 1 228 ? 96.802  148.110 171.647 1.00 128.56 ? 228  ARG A NH1   1 
ATOM   1237  N  NH2   . ARG A 1 228 ? 94.981  148.771 172.865 1.00 138.50 ? 228  ARG A NH2   1 
ATOM   1238  N  N     . ARG A 1 229 ? 94.651  140.260 169.259 1.00 117.98 ? 229  ARG A N     1 
ATOM   1239  C  CA    . ARG A 1 229 ? 94.902  139.084 168.434 1.00 117.84 ? 229  ARG A CA    1 
ATOM   1240  C  C     . ARG A 1 229 ? 95.050  139.564 166.999 1.00 120.47 ? 229  ARG A C     1 
ATOM   1241  O  O     . ARG A 1 229 ? 94.064  139.643 166.255 1.00 124.58 ? 229  ARG A O     1 
ATOM   1242  C  CB    . ARG A 1 229 ? 93.765  138.079 168.579 1.00 122.21 ? 229  ARG A CB    1 
ATOM   1243  C  CG    . ARG A 1 229 ? 94.217  136.657 168.745 1.00 127.02 ? 229  ARG A CG    1 
ATOM   1244  C  CD    . ARG A 1 229 ? 93.021  135.734 168.862 1.00 131.55 ? 229  ARG A CD    1 
ATOM   1245  N  NE    . ARG A 1 229 ? 92.284  135.920 170.111 1.00 129.84 ? 229  ARG A NE    1 
ATOM   1246  C  CZ    . ARG A 1 229 ? 92.781  135.774 171.334 1.00 131.65 ? 229  ARG A CZ    1 
ATOM   1247  N  NH1   . ARG A 1 229 ? 94.049  135.461 171.539 1.00 131.67 ? 229  ARG A NH1   1 
ATOM   1248  N  NH2   . ARG A 1 229 ? 91.982  135.954 172.381 1.00 131.24 ? 229  ARG A NH2   1 
ATOM   1249  N  N     . PRO A 1 230 ? 96.265  139.904 166.579 1.00 112.69 ? 230  PRO A N     1 
ATOM   1250  C  CA    . PRO A 1 230 ? 96.446  140.466 165.239 1.00 106.71 ? 230  PRO A CA    1 
ATOM   1251  C  C     . PRO A 1 230 ? 96.118  139.453 164.157 1.00 109.75 ? 230  PRO A C     1 
ATOM   1252  O  O     . PRO A 1 230 ? 96.301  138.246 164.322 1.00 113.96 ? 230  PRO A O     1 
ATOM   1253  C  CB    . PRO A 1 230 ? 97.928  140.853 165.212 1.00 95.44  ? 230  PRO A CB    1 
ATOM   1254  C  CG    . PRO A 1 230 ? 98.560  139.987 166.231 1.00 102.14 ? 230  PRO A CG    1 
ATOM   1255  C  CD    . PRO A 1 230 ? 97.537  139.796 167.309 1.00 108.80 ? 230  PRO A CD    1 
ATOM   1256  N  N     . ARG A 1 231 ? 95.614  139.968 163.035 1.00 104.64 ? 231  ARG A N     1 
ATOM   1257  C  CA    . ARG A 1 231 ? 95.277  139.141 161.888 1.00 103.59 ? 231  ARG A CA    1 
ATOM   1258  C  C     . ARG A 1 231 ? 96.140  139.419 160.671 1.00 98.62  ? 231  ARG A C     1 
ATOM   1259  O  O     . ARG A 1 231 ? 96.311  138.524 159.839 1.00 105.16 ? 231  ARG A O     1 
ATOM   1260  C  CB    . ARG A 1 231 ? 93.800  139.327 161.512 1.00 109.95 ? 231  ARG A CB    1 
ATOM   1261  C  CG    . ARG A 1 231 ? 92.821  139.023 162.642 1.00 110.77 ? 231  ARG A CG    1 
ATOM   1262  C  CD    . ARG A 1 231 ? 92.656  137.525 162.854 1.00 114.14 ? 231  ARG A CD    1 
ATOM   1263  N  NE    . ARG A 1 231 ? 93.820  136.933 163.501 1.00 112.58 ? 231  ARG A NE    1 
ATOM   1264  C  CZ    . ARG A 1 231 ? 94.095  135.637 163.514 1.00 117.24 ? 231  ARG A CZ    1 
ATOM   1265  N  NH1   . ARG A 1 231 ? 93.293  134.755 162.941 1.00 122.06 ? 231  ARG A NH1   1 
ATOM   1266  N  NH2   . ARG A 1 231 ? 95.207  135.217 164.110 1.00 116.01 ? 231  ARG A NH2   1 
ATOM   1267  N  N     . LEU A 1 232 ? 96.684  140.624 160.549 1.00 91.72  ? 232  LEU A N     1 
ATOM   1268  C  CA    . LEU A 1 232 ? 97.648  140.958 159.516 1.00 89.05  ? 232  LEU A CA    1 
ATOM   1269  C  C     . LEU A 1 232 ? 98.903  141.485 160.186 1.00 89.07  ? 232  LEU A C     1 
ATOM   1270  O  O     . LEU A 1 232 ? 98.834  142.391 161.019 1.00 98.48  ? 232  LEU A O     1 
ATOM   1271  C  CB    . LEU A 1 232 ? 97.096  142.004 158.547 1.00 90.28  ? 232  LEU A CB    1 
ATOM   1272  C  CG    . LEU A 1 232 ? 98.122  142.711 157.662 1.00 88.40  ? 232  LEU A CG    1 
ATOM   1273  C  CD1   . LEU A 1 232 ? 98.799  141.731 156.724 1.00 84.13  ? 232  LEU A CD1   1 
ATOM   1274  C  CD2   . LEU A 1 232 ? 97.465  143.832 156.884 1.00 98.90  ? 232  LEU A CD2   1 
ATOM   1275  N  N     . MET A 1 233 ? 100.047 140.916 159.830 1.00 87.08  ? 233  MET A N     1 
ATOM   1276  C  CA    . MET A 1 233 ? 101.310 141.334 160.413 1.00 86.07  ? 233  MET A CA    1 
ATOM   1277  C  C     . MET A 1 233 ? 102.275 141.696 159.296 1.00 83.66  ? 233  MET A C     1 
ATOM   1278  O  O     . MET A 1 233 ? 102.453 140.930 158.345 1.00 87.91  ? 233  MET A O     1 
ATOM   1279  C  CB    . MET A 1 233 ? 101.897 140.241 161.309 1.00 88.10  ? 233  MET A CB    1 
ATOM   1280  C  CG    . MET A 1 233 ? 103.402 140.160 161.288 1.00 95.59  ? 233  MET A CG    1 
ATOM   1281  S  SD    . MET A 1 233 ? 104.044 138.991 162.496 1.00 114.06 ? 233  MET A SD    1 
ATOM   1282  C  CE    . MET A 1 233 ? 102.825 137.696 162.365 1.00 98.65  ? 233  MET A CE    1 
ATOM   1283  N  N     . ILE A 1 234 ? 102.893 142.866 159.416 1.00 84.61  ? 234  ILE A N     1 
ATOM   1284  C  CA    . ILE A 1 234 ? 103.723 143.441 158.365 1.00 81.20  ? 234  ILE A CA    1 
ATOM   1285  C  C     . ILE A 1 234 ? 105.162 143.490 158.852 1.00 87.31  ? 234  ILE A C     1 
ATOM   1286  O  O     . ILE A 1 234 ? 105.419 143.865 160.000 1.00 95.39  ? 234  ILE A O     1 
ATOM   1287  C  CB    . ILE A 1 234 ? 103.244 144.850 157.971 1.00 81.14  ? 234  ILE A CB    1 
ATOM   1288  C  CG1   . ILE A 1 234 ? 101.752 144.841 157.646 1.00 90.70  ? 234  ILE A CG1   1 
ATOM   1289  C  CG2   . ILE A 1 234 ? 104.034 145.360 156.801 1.00 84.40  ? 234  ILE A CG2   1 
ATOM   1290  C  CD1   . ILE A 1 234 ? 101.191 146.211 157.357 1.00 94.07  ? 234  ILE A CD1   1 
ATOM   1291  N  N     . CYS A 1 235 ? 106.096 143.116 157.984 1.00 87.24  ? 235  CYS A N     1 
ATOM   1292  C  CA    . CYS A 1 235 ? 107.516 143.119 158.303 1.00 89.21  ? 235  CYS A CA    1 
ATOM   1293  C  C     . CYS A 1 235 ? 108.218 144.205 157.503 1.00 91.60  ? 235  CYS A C     1 
ATOM   1294  O  O     . CYS A 1 235 ? 107.964 144.361 156.305 1.00 97.19  ? 235  CYS A O     1 
ATOM   1295  C  CB    . CYS A 1 235 ? 108.151 141.761 158.009 1.00 87.29  ? 235  CYS A CB    1 
ATOM   1296  S  SG    . CYS A 1 235 ? 109.940 141.712 158.233 1.00 99.23  ? 235  CYS A SG    1 
ATOM   1297  N  N     . ILE A 1 236 ? 109.095 144.949 158.164 1.00 90.78  ? 236  ILE A N     1 
ATOM   1298  C  CA    . ILE A 1 236 ? 109.879 146.005 157.528 1.00 91.95  ? 236  ILE A CA    1 
ATOM   1299  C  C     . ILE A 1 236 ? 111.339 145.710 157.845 1.00 96.46  ? 236  ILE A C     1 
ATOM   1300  O  O     . ILE A 1 236 ? 111.868 146.135 158.874 1.00 103.70 ? 236  ILE A O     1 
ATOM   1301  C  CB    . ILE A 1 236 ? 109.480 147.402 158.006 1.00 87.91  ? 236  ILE A CB    1 
ATOM   1302  C  CG1   . ILE A 1 236 ? 107.981 147.629 157.833 1.00 85.38  ? 236  ILE A CG1   1 
ATOM   1303  C  CG2   . ILE A 1 236 ? 110.265 148.464 157.261 1.00 93.06  ? 236  ILE A CG2   1 
ATOM   1304  C  CD1   . ILE A 1 236 ? 107.544 149.009 158.239 1.00 83.43  ? 236  ILE A CD1   1 
ATOM   1305  N  N     . THR A 1 237 ? 112.006 144.978 156.959 1.00 93.35  ? 237  THR A N     1 
ATOM   1306  C  CA    . THR A 1 237 ? 113.427 144.725 157.138 1.00 98.26  ? 237  THR A CA    1 
ATOM   1307  C  C     . THR A 1 237 ? 114.215 146.000 156.883 1.00 106.03 ? 237  THR A C     1 
ATOM   1308  O  O     . THR A 1 237 ? 114.063 146.645 155.843 1.00 112.17 ? 237  THR A O     1 
ATOM   1309  C  CB    . THR A 1 237 ? 113.897 143.624 156.192 1.00 104.67 ? 237  THR A CB    1 
ATOM   1310  O  OG1   . THR A 1 237 ? 113.641 144.020 154.841 1.00 108.92 ? 237  THR A OG1   1 
ATOM   1311  C  CG2   . THR A 1 237 ? 113.154 142.336 156.474 1.00 105.63 ? 237  THR A CG2   1 
ATOM   1312  N  N     . MET A 1 238 ? 115.066 146.365 157.837 1.00 107.04 ? 238  MET A N     1 
ATOM   1313  C  CA    . MET A 1 238 ? 115.827 147.601 157.743 1.00 108.26 ? 238  MET A CA    1 
ATOM   1314  C  C     . MET A 1 238 ? 117.269 147.335 158.142 1.00 111.74 ? 238  MET A C     1 
ATOM   1315  O  O     . MET A 1 238 ? 117.532 146.613 159.107 1.00 115.43 ? 238  MET A O     1 
ATOM   1316  C  CB    . MET A 1 238 ? 115.214 148.698 158.624 1.00 101.98 ? 238  MET A CB    1 
ATOM   1317  C  CG    . MET A 1 238 ? 116.145 149.851 158.944 1.00 106.74 ? 238  MET A CG    1 
ATOM   1318  S  SD    . MET A 1 238 ? 115.895 150.514 160.596 1.00 123.75 ? 238  MET A SD    1 
ATOM   1319  C  CE    . MET A 1 238 ? 116.459 149.145 161.596 1.00 113.10 ? 238  MET A CE    1 
ATOM   1320  N  N     . TYR A 1 239 ? 118.198 147.923 157.392 1.00 116.35 ? 239  TYR A N     1 
ATOM   1321  C  CA    . TYR A 1 239 ? 119.625 147.704 157.608 1.00 116.43 ? 239  TYR A CA    1 
ATOM   1322  C  C     . TYR A 1 239 ? 120.390 148.852 156.975 1.00 122.41 ? 239  TYR A C     1 
ATOM   1323  O  O     . TYR A 1 239 ? 120.392 148.982 155.747 1.00 128.66 ? 239  TYR A O     1 
ATOM   1324  C  CB    . TYR A 1 239 ? 120.055 146.371 157.005 1.00 119.55 ? 239  TYR A CB    1 
ATOM   1325  C  CG    . TYR A 1 239 ? 121.539 146.237 156.752 1.00 123.89 ? 239  TYR A CG    1 
ATOM   1326  C  CD1   . TYR A 1 239 ? 122.413 145.902 157.773 1.00 127.51 ? 239  TYR A CD1   1 
ATOM   1327  C  CD2   . TYR A 1 239 ? 122.063 146.430 155.482 1.00 125.17 ? 239  TYR A CD2   1 
ATOM   1328  C  CE1   . TYR A 1 239 ? 123.767 145.767 157.536 1.00 131.01 ? 239  TYR A CE1   1 
ATOM   1329  C  CE2   . TYR A 1 239 ? 123.412 146.302 155.237 1.00 127.04 ? 239  TYR A CE2   1 
ATOM   1330  C  CZ    . TYR A 1 239 ? 124.260 145.971 156.268 1.00 132.19 ? 239  TYR A CZ    1 
ATOM   1331  O  OH    . TYR A 1 239 ? 125.608 145.842 156.028 1.00 136.36 ? 239  TYR A OH    1 
ATOM   1332  N  N     . ASN A 1 240 ? 121.040 149.670 157.804 1.00 122.77 ? 240  ASN A N     1 
ATOM   1333  C  CA    . ASN A 1 240 ? 121.875 150.780 157.344 1.00 126.78 ? 240  ASN A CA    1 
ATOM   1334  C  C     . ASN A 1 240 ? 121.030 151.676 156.427 1.00 126.18 ? 240  ASN A C     1 
ATOM   1335  O  O     . ASN A 1 240 ? 121.149 151.677 155.201 1.00 127.13 ? 240  ASN A O     1 
ATOM   1336  C  CB    . ASN A 1 240 ? 123.158 150.227 156.687 1.00 126.17 ? 240  ASN A CB    1 
ATOM   1337  C  CG    . ASN A 1 240 ? 123.812 151.162 155.665 1.00 131.15 ? 240  ASN A CG    1 
ATOM   1338  O  OD1   . ASN A 1 240 ? 123.542 152.361 155.601 1.00 135.24 ? 240  ASN A OD1   1 
ATOM   1339  N  ND2   . ASN A 1 240 ? 124.680 150.588 154.844 1.00 131.50 ? 240  ASN A ND2   1 
ATOM   1340  N  N     . GLU A 1 241 ? 120.091 152.373 157.050 1.00 123.01 ? 241  GLU A N     1 
ATOM   1341  C  CA    . GLU A 1 241 ? 119.190 153.241 156.317 1.00 122.60 ? 241  GLU A CA    1 
ATOM   1342  C  C     . GLU A 1 241 ? 118.968 154.529 157.078 1.00 129.87 ? 241  GLU A C     1 
ATOM   1343  O  O     . GLU A 1 241 ? 119.000 154.557 158.309 1.00 132.11 ? 241  GLU A O     1 
ATOM   1344  C  CB    . GLU A 1 241 ? 117.853 152.540 156.070 1.00 120.67 ? 241  GLU A CB    1 
ATOM   1345  C  CG    . GLU A 1 241 ? 117.978 151.056 155.762 1.00 123.90 ? 241  GLU A CG    1 
ATOM   1346  C  CD    . GLU A 1 241 ? 118.330 150.790 154.312 1.00 128.10 ? 241  GLU A CD    1 
ATOM   1347  O  OE1   . GLU A 1 241 ? 118.643 151.758 153.587 1.00 132.90 ? 241  GLU A OE1   1 
ATOM   1348  O  OE2   . GLU A 1 241 ? 118.294 149.613 153.897 1.00 122.52 ? 241  GLU A OE2   1 
ATOM   1349  N  N     . GLY A 1 242 ? 118.742 155.598 156.331 1.00 133.35 ? 242  GLY A N     1 
ATOM   1350  C  CA    . GLY A 1 242 ? 118.518 156.895 156.918 1.00 130.53 ? 242  GLY A CA    1 
ATOM   1351  C  C     . GLY A 1 242 ? 117.154 156.973 157.569 1.00 124.84 ? 242  GLY A C     1 
ATOM   1352  O  O     . GLY A 1 242 ? 116.261 156.170 157.287 1.00 126.75 ? 242  GLY A O     1 
ATOM   1353  N  N     . PRO A 1 243 ? 116.972 157.939 158.469 1.00 121.37 ? 243  PRO A N     1 
ATOM   1354  C  CA    . PRO A 1 243 ? 115.659 158.097 159.110 1.00 124.92 ? 243  PRO A CA    1 
ATOM   1355  C  C     . PRO A 1 243 ? 114.544 158.424 158.137 1.00 128.78 ? 243  PRO A C     1 
ATOM   1356  O  O     . PRO A 1 243 ? 113.381 158.113 158.421 1.00 130.21 ? 243  PRO A O     1 
ATOM   1357  C  CB    . PRO A 1 243 ? 115.886 159.248 160.101 1.00 125.80 ? 243  PRO A CB    1 
ATOM   1358  C  CG    . PRO A 1 243 ? 117.358 159.341 160.262 1.00 128.49 ? 243  PRO A CG    1 
ATOM   1359  C  CD    . PRO A 1 243 ? 117.951 158.917 158.963 1.00 128.14 ? 243  PRO A CD    1 
ATOM   1360  N  N     . GLN A 1 244 ? 114.859 159.063 157.008 1.00 126.21 ? 244  GLN A N     1 
ATOM   1361  C  CA    . GLN A 1 244 ? 113.811 159.519 156.101 1.00 128.48 ? 244  GLN A CA    1 
ATOM   1362  C  C     . GLN A 1 244 ? 113.049 158.350 155.492 1.00 128.65 ? 244  GLN A C     1 
ATOM   1363  O  O     . GLN A 1 244 ? 111.820 158.401 155.370 1.00 130.63 ? 244  GLN A O     1 
ATOM   1364  C  CB    . GLN A 1 244 ? 114.406 160.399 155.004 1.00 129.95 ? 244  GLN A CB    1 
ATOM   1365  C  CG    . GLN A 1 244 ? 113.357 161.081 154.144 1.00 135.53 ? 244  GLN A CG    1 
ATOM   1366  C  CD    . GLN A 1 244 ? 112.487 162.039 154.934 1.00 146.49 ? 244  GLN A CD    1 
ATOM   1367  O  OE1   . GLN A 1 244 ? 112.942 162.665 155.891 1.00 149.05 ? 244  GLN A OE1   1 
ATOM   1368  N  NE2   . GLN A 1 244 ? 111.224 162.153 154.539 1.00 147.81 ? 244  GLN A NE2   1 
ATOM   1369  N  N     . GLN A 1 245 ? 113.758 157.291 155.098 1.00 125.17 ? 245  GLN A N     1 
ATOM   1370  C  CA    . GLN A 1 245 ? 113.091 156.140 154.496 1.00 122.38 ? 245  GLN A CA    1 
ATOM   1371  C  C     . GLN A 1 245 ? 112.137 155.481 155.485 1.00 120.99 ? 245  GLN A C     1 
ATOM   1372  O  O     . GLN A 1 245 ? 110.986 155.172 155.149 1.00 121.86 ? 245  GLN A O     1 
ATOM   1373  C  CB    . GLN A 1 245 ? 114.130 155.137 153.999 1.00 119.24 ? 245  GLN A CB    1 
ATOM   1374  C  CG    . GLN A 1 245 ? 115.190 155.746 153.105 1.00 127.06 ? 245  GLN A CG    1 
ATOM   1375  C  CD    . GLN A 1 245 ? 116.165 154.717 152.578 1.00 128.80 ? 245  GLN A CD    1 
ATOM   1376  O  OE1   . GLN A 1 245 ? 116.069 153.534 152.899 1.00 132.27 ? 245  GLN A OE1   1 
ATOM   1377  N  NE2   . GLN A 1 245 ? 117.113 155.162 151.764 1.00 122.53 ? 245  GLN A NE2   1 
ATOM   1378  N  N     . LEU A 1 246 ? 112.601 155.268 156.717 1.00 115.77 ? 246  LEU A N     1 
ATOM   1379  C  CA    . LEU A 1 246 ? 111.754 154.644 157.726 1.00 110.48 ? 246  LEU A CA    1 
ATOM   1380  C  C     . LEU A 1 246 ? 110.567 155.531 158.074 1.00 112.23 ? 246  LEU A C     1 
ATOM   1381  O  O     . LEU A 1 246 ? 109.447 155.038 158.257 1.00 112.07 ? 246  LEU A O     1 
ATOM   1382  C  CB    . LEU A 1 246 ? 112.579 154.325 158.971 1.00 106.90 ? 246  LEU A CB    1 
ATOM   1383  C  CG    . LEU A 1 246 ? 111.864 153.567 160.084 1.00 104.66 ? 246  LEU A CG    1 
ATOM   1384  C  CD1   . LEU A 1 246 ? 111.379 152.226 159.574 1.00 102.08 ? 246  LEU A CD1   1 
ATOM   1385  C  CD2   . LEU A 1 246 ? 112.791 153.385 161.267 1.00 108.89 ? 246  LEU A CD2   1 
ATOM   1386  N  N     . LYS A 1 247 ? 110.788 156.845 158.166 1.00 111.93 ? 247  LYS A N     1 
ATOM   1387  C  CA    . LYS A 1 247 ? 109.687 157.754 158.460 1.00 112.93 ? 247  LYS A CA    1 
ATOM   1388  C  C     . LYS A 1 247 ? 108.653 157.741 157.344 1.00 116.84 ? 247  LYS A C     1 
ATOM   1389  O  O     . LYS A 1 247 ? 107.445 157.748 157.608 1.00 117.70 ? 247  LYS A O     1 
ATOM   1390  C  CB    . LYS A 1 247 ? 110.220 159.168 158.687 1.00 114.31 ? 247  LYS A CB    1 
ATOM   1391  C  CG    . LYS A 1 247 ? 109.143 160.190 159.012 1.00 118.91 ? 247  LYS A CG    1 
ATOM   1392  C  CD    . LYS A 1 247 ? 109.700 161.346 159.826 1.00 124.87 ? 247  LYS A CD    1 
ATOM   1393  C  CE    . LYS A 1 247 ? 110.943 161.935 159.184 1.00 127.96 ? 247  LYS A CE    1 
ATOM   1394  N  NZ    . LYS A 1 247 ? 111.567 162.971 160.051 1.00 124.47 ? 247  LYS A NZ    1 
ATOM   1395  N  N     . ALA A 1 248 ? 109.106 157.713 156.088 1.00 117.06 ? 248  ALA A N     1 
ATOM   1396  C  CA    . ALA A 1 248 ? 108.174 157.638 154.968 1.00 114.21 ? 248  ALA A CA    1 
ATOM   1397  C  C     . ALA A 1 248 ? 107.379 156.341 155.000 1.00 114.23 ? 248  ALA A C     1 
ATOM   1398  O  O     . ALA A 1 248 ? 106.160 156.346 154.785 1.00 116.40 ? 248  ALA A O     1 
ATOM   1399  C  CB    . ALA A 1 248 ? 108.930 157.771 153.647 1.00 109.29 ? 248  ALA A CB    1 
ATOM   1400  N  N     . THR A 1 249 ? 108.049 155.220 155.278 1.00 109.87 ? 249  THR A N     1 
ATOM   1401  C  CA    . THR A 1 249 ? 107.347 153.942 155.333 1.00 104.66 ? 249  THR A CA    1 
ATOM   1402  C  C     . THR A 1 249 ? 106.298 153.933 156.438 1.00 107.14 ? 249  THR A C     1 
ATOM   1403  O  O     . THR A 1 249 ? 105.164 153.484 156.226 1.00 110.70 ? 249  THR A O     1 
ATOM   1404  C  CB    . THR A 1 249 ? 108.340 152.801 155.534 1.00 98.84  ? 249  THR A CB    1 
ATOM   1405  O  OG1   . THR A 1 249 ? 109.390 152.903 154.566 1.00 104.37 ? 249  THR A OG1   1 
ATOM   1406  C  CG2   . THR A 1 249 ? 107.646 151.465 155.373 1.00 98.71  ? 249  THR A CG2   1 
ATOM   1407  N  N     . LEU A 1 250 ? 106.652 154.436 157.623 1.00 105.26 ? 250  LEU A N     1 
ATOM   1408  C  CA    . LEU A 1 250 ? 105.701 154.438 158.729 1.00 105.08 ? 250  LEU A CA    1 
ATOM   1409  C  C     . LEU A 1 250 ? 104.542 155.394 158.467 1.00 110.57 ? 250  LEU A C     1 
ATOM   1410  O  O     . LEU A 1 250 ? 103.390 155.083 158.795 1.00 113.57 ? 250  LEU A O     1 
ATOM   1411  C  CB    . LEU A 1 250 ? 106.415 154.785 160.033 1.00 99.54  ? 250  LEU A CB    1 
ATOM   1412  C  CG    . LEU A 1 250 ? 107.465 153.761 160.466 1.00 95.06  ? 250  LEU A CG    1 
ATOM   1413  C  CD1   . LEU A 1 250 ? 108.015 154.095 161.838 1.00 100.75 ? 250  LEU A CD1   1 
ATOM   1414  C  CD2   . LEU A 1 250 ? 106.877 152.365 160.452 1.00 93.04  ? 250  LEU A CD2   1 
ATOM   1415  N  N     . LYS A 1 251 ? 104.820 156.557 157.871 1.00 108.89 ? 251  LYS A N     1 
ATOM   1416  C  CA    . LYS A 1 251 ? 103.741 157.471 157.514 1.00 111.15 ? 251  LYS A CA    1 
ATOM   1417  C  C     . LYS A 1 251 ? 102.791 156.830 156.513 1.00 113.91 ? 251  LYS A C     1 
ATOM   1418  O  O     . LYS A 1 251 ? 101.567 156.962 156.632 1.00 118.07 ? 251  LYS A O     1 
ATOM   1419  C  CB    . LYS A 1 251 ? 104.314 158.769 156.948 1.00 114.74 ? 251  LYS A CB    1 
ATOM   1420  C  CG    . LYS A 1 251 ? 103.253 159.734 156.441 1.00 124.62 ? 251  LYS A CG    1 
ATOM   1421  C  CD    . LYS A 1 251 ? 103.863 160.872 155.641 1.00 129.43 ? 251  LYS A CD    1 
ATOM   1422  C  CE    . LYS A 1 251 ? 102.784 161.739 155.013 1.00 128.71 ? 251  LYS A CE    1 
ATOM   1423  N  NZ    . LYS A 1 251 ? 103.360 162.856 154.215 1.00 131.07 ? 251  LYS A NZ    1 
ATOM   1424  N  N     . LYS A 1 252 ? 103.335 156.129 155.518 1.00 109.18 ? 252  LYS A N     1 
ATOM   1425  C  CA    . LYS A 1 252 ? 102.482 155.482 154.527 1.00 109.84 ? 252  LYS A CA    1 
ATOM   1426  C  C     . LYS A 1 252 ? 101.648 154.370 155.154 1.00 112.12 ? 252  LYS A C     1 
ATOM   1427  O  O     . LYS A 1 252 ? 100.472 154.197 154.808 1.00 114.67 ? 252  LYS A O     1 
ATOM   1428  C  CB    . LYS A 1 252 ? 103.335 154.949 153.380 1.00 106.70 ? 252  LYS A CB    1 
ATOM   1429  C  CG    . LYS A 1 252 ? 103.416 155.892 152.190 1.00 110.26 ? 252  LYS A CG    1 
ATOM   1430  C  CD    . LYS A 1 252 ? 103.971 157.253 152.570 1.00 112.81 ? 252  LYS A CD    1 
ATOM   1431  C  CE    . LYS A 1 252 ? 103.907 158.219 151.399 1.00 111.85 ? 252  LYS A CE    1 
ATOM   1432  N  NZ    . LYS A 1 252 ? 104.407 159.571 151.769 1.00 119.16 ? 252  LYS A NZ    1 
ATOM   1433  N  N     . LEU A 1 253 ? 102.235 153.607 156.078 1.00 106.97 ? 253  LEU A N     1 
ATOM   1434  C  CA    . LEU A 1 253 ? 101.470 152.574 156.771 1.00 103.16 ? 253  LEU A CA    1 
ATOM   1435  C  C     . LEU A 1 253 ? 100.344 153.182 157.600 1.00 106.76 ? 253  LEU A C     1 
ATOM   1436  O  O     . LEU A 1 253 ? 99.227  152.648 157.639 1.00 113.50 ? 253  LEU A O     1 
ATOM   1437  C  CB    . LEU A 1 253 ? 102.395 151.738 157.650 1.00 98.30  ? 253  LEU A CB    1 
ATOM   1438  C  CG    . LEU A 1 253 ? 103.179 150.656 156.913 1.00 95.68  ? 253  LEU A CG    1 
ATOM   1439  C  CD1   . LEU A 1 253 ? 104.030 149.871 157.882 1.00 95.54  ? 253  LEU A CD1   1 
ATOM   1440  C  CD2   . LEU A 1 253 ? 102.233 149.738 156.173 1.00 96.77  ? 253  LEU A CD2   1 
ATOM   1441  N  N     . ALA A 1 254 ? 100.619 154.299 158.276 1.00 101.97 ? 254  ALA A N     1 
ATOM   1442  C  CA    . ALA A 1 254 ? 99.566  154.977 159.024 1.00 103.58 ? 254  ALA A CA    1 
ATOM   1443  C  C     . ALA A 1 254 ? 98.473  155.485 158.092 1.00 108.27 ? 254  ALA A C     1 
ATOM   1444  O  O     . ALA A 1 254 ? 97.288  155.465 158.443 1.00 114.45 ? 254  ALA A O     1 
ATOM   1445  C  CB    . ALA A 1 254 ? 100.155 156.122 159.841 1.00 111.08 ? 254  ALA A CB    1 
ATOM   1446  N  N     . ASN A 1 255 ? 98.854  155.951 156.901 1.00 106.22 ? 255  ASN A N     1 
ATOM   1447  C  CA    . ASN A 1 255 ? 97.856  156.361 155.917 1.00 111.06 ? 255  ASN A CA    1 
ATOM   1448  C  C     . ASN A 1 255 ? 96.985  155.185 155.492 1.00 114.88 ? 255  ASN A C     1 
ATOM   1449  O  O     . ASN A 1 255 ? 95.766  155.329 155.339 1.00 118.14 ? 255  ASN A O     1 
ATOM   1450  C  CB    . ASN A 1 255 ? 98.538  156.989 154.703 1.00 112.43 ? 255  ASN A CB    1 
ATOM   1451  C  CG    . ASN A 1 255 ? 99.151  158.336 155.014 1.00 116.89 ? 255  ASN A CG    1 
ATOM   1452  O  OD1   . ASN A 1 255 ? 99.340  158.691 156.176 1.00 116.49 ? 255  ASN A OD1   1 
ATOM   1453  N  ND2   . ASN A 1 255 ? 99.468  159.095 153.973 1.00 119.66 ? 255  ASN A ND2   1 
ATOM   1454  N  N     . ASN A 1 256 ? 97.594  154.014 155.287 1.00 111.01 ? 256  ASN A N     1 
ATOM   1455  C  CA    . ASN A 1 256 ? 96.806  152.829 154.954 1.00 105.98 ? 256  ASN A CA    1 
ATOM   1456  C  C     . ASN A 1 256 ? 95.839  152.476 156.076 1.00 110.77 ? 256  ASN A C     1 
ATOM   1457  O  O     . ASN A 1 256 ? 94.682  152.121 155.820 1.00 113.00 ? 256  ASN A O     1 
ATOM   1458  C  CB    . ASN A 1 256 ? 97.716  151.639 154.652 1.00 96.86  ? 256  ASN A CB    1 
ATOM   1459  C  CG    . ASN A 1 256 ? 98.645  151.898 153.494 1.00 103.65 ? 256  ASN A CG    1 
ATOM   1460  O  OD1   . ASN A 1 256 ? 99.862  151.802 153.626 1.00 104.21 ? 256  ASN A OD1   1 
ATOM   1461  N  ND2   . ASN A 1 256 ? 98.074  152.229 152.345 1.00 109.62 ? 256  ASN A ND2   1 
ATOM   1462  N  N     . LEU A 1 257 ? 96.297  152.556 157.326 1.00 111.00 ? 257  LEU A N     1 
ATOM   1463  C  CA    . LEU A 1 257 ? 95.408  152.263 158.447 1.00 107.84 ? 257  LEU A CA    1 
ATOM   1464  C  C     . LEU A 1 257 ? 94.257  153.261 158.514 1.00 112.54 ? 257  LEU A C     1 
ATOM   1465  O  O     . LEU A 1 257 ? 93.112  152.884 158.793 1.00 117.14 ? 257  LEU A O     1 
ATOM   1466  C  CB    . LEU A 1 257 ? 96.193  152.254 159.758 1.00 102.74 ? 257  LEU A CB    1 
ATOM   1467  C  CG    . LEU A 1 257 ? 97.317  151.225 159.892 1.00 98.79  ? 257  LEU A CG    1 
ATOM   1468  C  CD1   . LEU A 1 257 ? 97.617  150.958 161.354 1.00 98.58  ? 257  LEU A CD1   1 
ATOM   1469  C  CD2   . LEU A 1 257 ? 96.956  149.934 159.184 1.00 97.21  ? 257  LEU A CD2   1 
ATOM   1470  N  N     . ALA A 1 258 ? 94.540  154.540 158.260 1.00 112.67 ? 258  ALA A N     1 
ATOM   1471  C  CA    . ALA A 1 258 ? 93.476  155.540 158.246 1.00 115.23 ? 258  ALA A CA    1 
ATOM   1472  C  C     . ALA A 1 258 ? 92.473  155.260 157.135 1.00 121.86 ? 258  ALA A C     1 
ATOM   1473  O  O     . ALA A 1 258 ? 91.258  155.393 157.333 1.00 127.98 ? 258  ALA A O     1 
ATOM   1474  C  CB    . ALA A 1 258 ? 94.072  156.939 158.094 1.00 110.66 ? 258  ALA A CB    1 
ATOM   1475  N  N     . TYR A 1 259 ? 92.963  154.868 155.957 1.00 116.63 ? 259  TYR A N     1 
ATOM   1476  C  CA    . TYR A 1 259 ? 92.065  154.528 154.858 1.00 118.18 ? 259  TYR A CA    1 
ATOM   1477  C  C     . TYR A 1 259 ? 91.203  153.324 155.207 1.00 121.57 ? 259  TYR A C     1 
ATOM   1478  O  O     . TYR A 1 259 ? 90.016  153.278 154.861 1.00 126.29 ? 259  TYR A O     1 
ATOM   1479  C  CB    . TYR A 1 259 ? 92.869  154.262 153.587 1.00 113.62 ? 259  TYR A CB    1 
ATOM   1480  C  CG    . TYR A 1 259 ? 92.021  153.948 152.377 1.00 111.03 ? 259  TYR A CG    1 
ATOM   1481  C  CD1   . TYR A 1 259 ? 91.455  154.964 151.621 1.00 116.93 ? 259  TYR A CD1   1 
ATOM   1482  C  CD2   . TYR A 1 259 ? 91.797  152.638 151.984 1.00 107.98 ? 259  TYR A CD2   1 
ATOM   1483  C  CE1   . TYR A 1 259 ? 90.682  154.683 150.514 1.00 116.40 ? 259  TYR A CE1   1 
ATOM   1484  C  CE2   . TYR A 1 259 ? 91.026  152.349 150.877 1.00 111.81 ? 259  TYR A CE2   1 
ATOM   1485  C  CZ    . TYR A 1 259 ? 90.471  153.374 150.146 1.00 115.66 ? 259  TYR A CZ    1 
ATOM   1486  O  OH    . TYR A 1 259 ? 89.703  153.091 149.042 1.00 121.69 ? 259  TYR A OH    1 
ATOM   1487  N  N     . LEU A 1 260 ? 91.783  152.336 155.892 1.00 118.13 ? 260  LEU A N     1 
ATOM   1488  C  CA    . LEU A 1 260 ? 91.003  151.181 156.321 1.00 116.87 ? 260  LEU A CA    1 
ATOM   1489  C  C     . LEU A 1 260 ? 89.950  151.583 157.346 1.00 123.31 ? 260  LEU A C     1 
ATOM   1490  O  O     . LEU A 1 260 ? 88.850  151.020 157.373 1.00 129.33 ? 260  LEU A O     1 
ATOM   1491  C  CB    . LEU A 1 260 ? 91.928  150.105 156.887 1.00 113.39 ? 260  LEU A CB    1 
ATOM   1492  C  CG    . LEU A 1 260 ? 92.576  149.177 155.862 1.00 110.53 ? 260  LEU A CG    1 
ATOM   1493  C  CD1   . LEU A 1 260 ? 93.482  148.169 156.542 1.00 113.24 ? 260  LEU A CD1   1 
ATOM   1494  C  CD2   . LEU A 1 260 ? 91.509  148.473 155.052 1.00 114.81 ? 260  LEU A CD2   1 
ATOM   1495  N  N     . LYS A 1 261 ? 90.274  152.551 158.205 1.00 121.92 ? 261  LYS A N     1 
ATOM   1496  C  CA    . LYS A 1 261 ? 89.278  153.086 159.130 1.00 122.57 ? 261  LYS A CA    1 
ATOM   1497  C  C     . LYS A 1 261 ? 88.130  153.753 158.384 1.00 126.96 ? 261  LYS A C     1 
ATOM   1498  O  O     . LYS A 1 261 ? 86.957  153.558 158.721 1.00 129.62 ? 261  LYS A O     1 
ATOM   1499  C  CB    . LYS A 1 261 ? 89.924  154.083 160.090 1.00 124.25 ? 261  LYS A CB    1 
ATOM   1500  C  CG    . LYS A 1 261 ? 90.655  153.465 161.259 1.00 126.30 ? 261  LYS A CG    1 
ATOM   1501  C  CD    . LYS A 1 261 ? 90.407  154.268 162.531 1.00 127.36 ? 261  LYS A CD    1 
ATOM   1502  C  CE    . LYS A 1 261 ? 90.294  155.759 162.236 1.00 127.65 ? 261  LYS A CE    1 
ATOM   1503  N  NZ    . LYS A 1 261 ? 89.643  156.509 163.344 1.00 129.68 ? 261  LYS A NZ    1 
ATOM   1504  N  N     . GLU A 1 262 ? 88.447  154.543 157.363 1.00 128.33 ? 262  GLU A N     1 
ATOM   1505  C  CA    . GLU A 1 262 ? 87.423  155.377 156.733 1.00 134.97 ? 262  GLU A CA    1 
ATOM   1506  C  C     . GLU A 1 262 ? 86.555  154.633 155.726 1.00 138.80 ? 262  GLU A C     1 
ATOM   1507  O  O     . GLU A 1 262 ? 85.965  155.298 154.866 1.00 144.41 ? 262  GLU A O     1 
ATOM   1508  C  CB    . GLU A 1 262 ? 88.077  156.584 156.059 1.00 139.38 ? 262  GLU A CB    1 
ATOM   1509  C  CG    . GLU A 1 262 ? 88.822  157.494 157.020 1.00 145.02 ? 262  GLU A CG    1 
ATOM   1510  C  CD    . GLU A 1 262 ? 89.384  158.724 156.337 1.00 151.68 ? 262  GLU A CD    1 
ATOM   1511  O  OE1   . GLU A 1 262 ? 89.145  158.892 155.123 1.00 157.58 ? 262  GLU A OE1   1 
ATOM   1512  O  OE2   . GLU A 1 262 ? 90.061  159.524 157.015 1.00 144.70 ? 262  GLU A OE2   1 
ATOM   1513  N  N     . GLN A 1 263 ? 86.446  153.308 155.773 1.00 138.56 ? 263  GLN A N     1 
ATOM   1514  C  CA    . GLN A 1 263 ? 85.579  152.600 154.842 1.00 141.21 ? 263  GLN A CA    1 
ATOM   1515  C  C     . GLN A 1 263 ? 84.123  152.712 155.273 1.00 149.17 ? 263  GLN A C     1 
ATOM   1516  O  O     . GLN A 1 263 ? 83.801  152.582 156.457 1.00 148.47 ? 263  GLN A O     1 
ATOM   1517  C  CB    . GLN A 1 263 ? 85.990  151.135 154.751 1.00 136.80 ? 263  GLN A CB    1 
ATOM   1518  C  CG    . GLN A 1 263 ? 87.434  150.940 154.356 1.00 132.93 ? 263  GLN A CG    1 
ATOM   1519  C  CD    . GLN A 1 263 ? 87.644  149.674 153.567 1.00 137.04 ? 263  GLN A CD    1 
ATOM   1520  O  OE1   . GLN A 1 263 ? 87.961  148.625 154.124 1.00 133.60 ? 263  GLN A OE1   1 
ATOM   1521  N  NE2   . GLN A 1 263 ? 87.459  149.762 152.257 1.00 140.37 ? 263  GLN A NE2   1 
ATOM   1522  N  N     . MET A 1 264 ? 83.243  152.956 154.306 1.00 155.40 ? 264  MET A N     1 
ATOM   1523  C  CA    . MET A 1 264 ? 81.824  153.075 154.605 1.00 161.05 ? 264  MET A CA    1 
ATOM   1524  C  C     . MET A 1 264 ? 81.225  151.697 154.880 1.00 161.11 ? 264  MET A C     1 
ATOM   1525  O  O     . MET A 1 264 ? 81.322  150.798 154.040 1.00 159.52 ? 264  MET A O     1 
ATOM   1526  C  CB    . MET A 1 264 ? 81.087  153.741 153.444 1.00 165.42 ? 264  MET A CB    1 
ATOM   1527  C  CG    . MET A 1 264 ? 81.240  155.251 153.393 1.00 167.52 ? 264  MET A CG    1 
ATOM   1528  S  SD    . MET A 1 264 ? 80.260  156.096 154.647 1.00 192.13 ? 264  MET A SD    1 
ATOM   1529  C  CE    . MET A 1 264 ? 78.603  155.623 154.157 1.00 178.34 ? 264  MET A CE    1 
ATOM   1530  N  N     . PRO A 1 265 ? 80.602  151.501 156.037 1.00 164.63 ? 265  PRO A N     1 
ATOM   1531  C  CA    . PRO A 1 265 ? 79.964  150.217 156.335 1.00 163.91 ? 265  PRO A CA    1 
ATOM   1532  C  C     . PRO A 1 265 ? 78.689  150.016 155.528 1.00 168.66 ? 265  PRO A C     1 
ATOM   1533  O  O     . PRO A 1 265 ? 78.114  150.950 154.966 1.00 168.87 ? 265  PRO A O     1 
ATOM   1534  C  CB    . PRO A 1 265 ? 79.635  150.330 157.831 1.00 162.80 ? 265  PRO A CB    1 
ATOM   1535  C  CG    . PRO A 1 265 ? 80.601  151.328 158.357 1.00 162.56 ? 265  PRO A CG    1 
ATOM   1536  C  CD    . PRO A 1 265 ? 80.768  152.325 157.246 1.00 163.81 ? 265  PRO A CD    1 
ATOM   1537  N  N     . GLY A 1 266 ? 78.253  148.761 155.486 1.00 169.64 ? 266  GLY A N     1 
ATOM   1538  C  CA    . GLY A 1 266 ? 76.982  148.433 154.859 1.00 172.04 ? 266  GLY A CA    1 
ATOM   1539  C  C     . GLY A 1 266 ? 76.925  148.692 153.370 1.00 170.59 ? 266  GLY A C     1 
ATOM   1540  O  O     . GLY A 1 266 ? 75.903  149.173 152.865 1.00 171.28 ? 266  GLY A O     1 
ATOM   1541  N  N     . ASP A 1 267 ? 78.003  148.387 152.652 1.00 169.78 ? 267  ASP A N     1 
ATOM   1542  C  CA    . ASP A 1 267 ? 78.021  148.487 151.201 1.00 167.96 ? 267  ASP A CA    1 
ATOM   1543  C  C     . ASP A 1 267 ? 78.779  147.302 150.619 1.00 166.25 ? 267  ASP A C     1 
ATOM   1544  O  O     . ASP A 1 267 ? 79.540  146.626 151.316 1.00 162.32 ? 267  ASP A O     1 
ATOM   1545  C  CB    . ASP A 1 267 ? 78.637  149.816 150.727 1.00 165.51 ? 267  ASP A CB    1 
ATOM   1546  C  CG    . ASP A 1 267 ? 80.139  149.743 150.564 1.00 163.19 ? 267  ASP A CG    1 
ATOM   1547  O  OD1   . ASP A 1 267 ? 80.809  149.189 151.458 1.00 166.23 ? 267  ASP A OD1   1 
ATOM   1548  O  OD2   . ASP A 1 267 ? 80.654  150.265 149.553 1.00 158.78 ? 267  ASP A OD2   1 
ATOM   1549  N  N     . GLU A 1 268 ? 78.552  147.057 149.328 1.00 168.61 ? 268  GLU A N     1 
ATOM   1550  C  CA    . GLU A 1 268 ? 79.097  145.866 148.684 1.00 168.04 ? 268  GLU A CA    1 
ATOM   1551  C  C     . GLU A 1 268 ? 80.620  145.904 148.625 1.00 159.37 ? 268  GLU A C     1 
ATOM   1552  O  O     . GLU A 1 268 ? 81.283  144.880 148.826 1.00 155.16 ? 268  GLU A O     1 
ATOM   1553  C  CB    . GLU A 1 268 ? 78.514  145.729 147.278 1.00 176.02 ? 268  GLU A CB    1 
ATOM   1554  C  CG    . GLU A 1 268 ? 76.996  145.788 147.226 1.00 182.36 ? 268  GLU A CG    1 
ATOM   1555  C  CD    . GLU A 1 268 ? 76.466  145.906 145.809 1.00 190.66 ? 268  GLU A CD    1 
ATOM   1556  O  OE1   . GLU A 1 268 ? 77.287  146.016 144.874 1.00 188.08 ? 268  GLU A OE1   1 
ATOM   1557  O  OE2   . GLU A 1 268 ? 75.230  145.892 145.631 1.00 194.97 ? 268  GLU A OE2   1 
ATOM   1558  N  N     . LYS A 1 269 ? 81.191  147.076 148.345 1.00 158.72 ? 269  LYS A N     1 
ATOM   1559  C  CA    . LYS A 1 269 ? 82.609  147.159 148.013 1.00 155.00 ? 269  LYS A CA    1 
ATOM   1560  C  C     . LYS A 1 269 ? 83.519  146.984 149.225 1.00 151.88 ? 269  LYS A C     1 
ATOM   1561  O  O     . LYS A 1 269 ? 84.534  146.286 149.130 1.00 141.70 ? 269  LYS A O     1 
ATOM   1562  C  CB    . LYS A 1 269 ? 82.902  148.497 147.333 1.00 154.79 ? 269  LYS A CB    1 
ATOM   1563  C  CG    . LYS A 1 269 ? 84.327  148.646 146.838 1.00 149.49 ? 269  LYS A CG    1 
ATOM   1564  C  CD    . LYS A 1 269 ? 84.722  147.472 145.960 1.00 147.21 ? 269  LYS A CD    1 
ATOM   1565  C  CE    . LYS A 1 269 ? 84.004  147.522 144.621 1.00 151.55 ? 269  LYS A CE    1 
ATOM   1566  N  NZ    . LYS A 1 269 ? 84.876  147.064 143.506 1.00 156.80 ? 269  LYS A NZ    1 
ATOM   1567  N  N     . SER A 1 270 ? 83.187  147.601 150.356 1.00 156.30 ? 270  SER A N     1 
ATOM   1568  C  CA    . SER A 1 270 ? 84.111  147.643 151.481 1.00 149.36 ? 270  SER A CA    1 
ATOM   1569  C  C     . SER A 1 270 ? 84.217  146.288 152.169 1.00 143.79 ? 270  SER A C     1 
ATOM   1570  O  O     . SER A 1 270 ? 83.312  145.452 152.097 1.00 142.71 ? 270  SER A O     1 
ATOM   1571  C  CB    . SER A 1 270 ? 83.673  148.699 152.496 1.00 153.54 ? 270  SER A CB    1 
ATOM   1572  O  OG    . SER A 1 270 ? 83.590  149.980 151.898 1.00 159.10 ? 270  SER A OG    1 
ATOM   1573  N  N     . LEU A 1 271 ? 85.343  146.080 152.843 1.00 142.37 ? 271  LEU A N     1 
ATOM   1574  C  CA    . LEU A 1 271 ? 85.562  144.870 153.620 1.00 144.36 ? 271  LEU A CA    1 
ATOM   1575  C  C     . LEU A 1 271 ? 84.636  144.831 154.827 1.00 151.11 ? 271  LEU A C     1 
ATOM   1576  O  O     . LEU A 1 271 ? 84.201  145.865 155.340 1.00 157.16 ? 271  LEU A O     1 
ATOM   1577  C  CB    . LEU A 1 271 ? 87.014  144.783 154.089 1.00 135.08 ? 271  LEU A CB    1 
ATOM   1578  C  CG    . LEU A 1 271 ? 88.100  144.890 153.022 1.00 127.22 ? 271  LEU A CG    1 
ATOM   1579  C  CD1   . LEU A 1 271 ? 89.468  144.767 153.654 1.00 111.43 ? 271  LEU A CD1   1 
ATOM   1580  C  CD2   . LEU A 1 271 ? 87.902  143.817 151.974 1.00 127.24 ? 271  LEU A CD2   1 
ATOM   1581  N  N     . THR A 1 272 ? 84.335  143.617 155.277 1.00 151.53 ? 272  THR A N     1 
ATOM   1582  C  CA    . THR A 1 272 ? 83.527  143.401 156.465 1.00 153.78 ? 272  THR A CA    1 
ATOM   1583  C  C     . THR A 1 272 ? 84.266  142.467 157.410 1.00 147.10 ? 272  THR A C     1 
ATOM   1584  O  O     . THR A 1 272 ? 84.938  141.526 156.979 1.00 142.33 ? 272  THR A O     1 
ATOM   1585  C  CB    . THR A 1 272 ? 82.148  142.809 156.123 1.00 160.18 ? 272  THR A CB    1 
ATOM   1586  O  OG1   . THR A 1 272 ? 82.316  141.601 155.370 1.00 160.56 ? 272  THR A OG1   1 
ATOM   1587  C  CG2   . THR A 1 272 ? 81.324  143.798 155.310 1.00 160.85 ? 272  THR A CG2   1 
ATOM   1588  N  N     . GLY A 1 273 ? 84.143  142.741 158.705 1.00 145.79 ? 273  GLY A N     1 
ATOM   1589  C  CA    . GLY A 1 273 ? 84.720  141.871 159.708 1.00 143.82 ? 273  GLY A CA    1 
ATOM   1590  C  C     . GLY A 1 273 ? 85.853  142.480 160.507 1.00 135.98 ? 273  GLY A C     1 
ATOM   1591  O  O     . GLY A 1 273 ? 85.695  143.538 161.124 1.00 132.79 ? 273  GLY A O     1 
ATOM   1592  N  N     . ALA A 1 274 ? 87.008  141.812 160.497 1.00 131.71 ? 274  ALA A N     1 
ATOM   1593  C  CA    . ALA A 1 274 ? 88.116  142.199 161.361 1.00 127.48 ? 274  ALA A CA    1 
ATOM   1594  C  C     . ALA A 1 274 ? 88.757  143.517 160.954 1.00 123.37 ? 274  ALA A C     1 
ATOM   1595  O  O     . ALA A 1 274 ? 89.464  144.120 161.767 1.00 119.54 ? 274  ALA A O     1 
ATOM   1596  C  CB    . ALA A 1 274 ? 89.175  141.097 161.380 1.00 126.76 ? 274  ALA A CB    1 
ATOM   1597  N  N     . PHE A 1 275 ? 88.541  143.975 159.721 1.00 122.05 ? 275  PHE A N     1 
ATOM   1598  C  CA    . PHE A 1 275 ? 89.181  145.183 159.217 1.00 118.88 ? 275  PHE A CA    1 
ATOM   1599  C  C     . PHE A 1 275 ? 88.201  146.343 159.068 1.00 123.63 ? 275  PHE A C     1 
ATOM   1600  O  O     . PHE A 1 275 ? 88.361  147.181 158.176 1.00 120.05 ? 275  PHE A O     1 
ATOM   1601  C  CB    . PHE A 1 275 ? 89.874  144.891 157.888 1.00 111.58 ? 275  PHE A CB    1 
ATOM   1602  C  CG    . PHE A 1 275 ? 91.009  143.917 158.006 1.00 112.90 ? 275  PHE A CG    1 
ATOM   1603  C  CD1   . PHE A 1 275 ? 92.264  144.340 158.399 1.00 115.82 ? 275  PHE A CD1   1 
ATOM   1604  C  CD2   . PHE A 1 275 ? 90.814  142.573 157.743 1.00 112.58 ? 275  PHE A CD2   1 
ATOM   1605  C  CE1   . PHE A 1 275 ? 93.307  143.442 158.515 1.00 111.05 ? 275  PHE A CE1   1 
ATOM   1606  C  CE2   . PHE A 1 275 ? 91.853  141.672 157.855 1.00 105.65 ? 275  PHE A CE2   1 
ATOM   1607  C  CZ    . PHE A 1 275 ? 93.100  142.107 158.242 1.00 103.38 ? 275  PHE A CZ    1 
ATOM   1608  N  N     . ALA A 1 276 ? 87.190  146.407 159.928 1.00 128.85 ? 276  ALA A N     1 
ATOM   1609  C  CA    . ALA A 1 276 ? 86.215  147.488 159.889 1.00 129.46 ? 276  ALA A CA    1 
ATOM   1610  C  C     . ALA A 1 276 ? 86.825  148.743 160.511 1.00 129.98 ? 276  ALA A C     1 
ATOM   1611  O  O     . ALA A 1 276 ? 87.981  148.758 160.940 1.00 128.20 ? 276  ALA A O     1 
ATOM   1612  C  CB    . ALA A 1 276 ? 84.928  147.064 160.590 1.00 135.36 ? 276  ALA A CB    1 
ATOM   1613  N  N     . GLY A 1 277 ? 86.044  149.819 160.570 1.00 132.62 ? 277  GLY A N     1 
ATOM   1614  C  CA    . GLY A 1 277 ? 86.546  151.076 161.074 1.00 135.99 ? 277  GLY A CA    1 
ATOM   1615  C  C     . GLY A 1 277 ? 86.628  151.135 162.589 1.00 135.36 ? 277  GLY A C     1 
ATOM   1616  O  O     . GLY A 1 277 ? 86.030  150.324 163.294 1.00 130.50 ? 277  GLY A O     1 
ATOM   1617  N  N     . ASP A 1 278 ? 87.423  152.097 163.066 1.00 134.03 ? 278  ASP A N     1 
ATOM   1618  C  CA    . ASP A 1 278 ? 87.508  152.469 164.475 1.00 133.77 ? 278  ASP A CA    1 
ATOM   1619  C  C     . ASP A 1 278 ? 88.235  151.419 165.307 1.00 135.68 ? 278  ASP A C     1 
ATOM   1620  O  O     . ASP A 1 278 ? 88.430  151.610 166.512 1.00 139.46 ? 278  ASP A O     1 
ATOM   1621  C  CB    . ASP A 1 278 ? 86.113  152.734 165.052 1.00 136.83 ? 278  ASP A CB    1 
ATOM   1622  C  CG    . ASP A 1 278 ? 85.559  154.084 164.641 1.00 144.40 ? 278  ASP A CG    1 
ATOM   1623  O  OD1   . ASP A 1 278 ? 86.367  155.005 164.394 1.00 144.72 ? 278  ASP A OD1   1 
ATOM   1624  O  OD2   . ASP A 1 278 ? 84.321  154.228 164.564 1.00 148.75 ? 278  ASP A OD2   1 
ATOM   1625  N  N     . ASP A 1 279 ? 88.635  150.305 164.687 1.00 132.01 ? 279  ASP A N     1 
ATOM   1626  C  CA    . ASP A 1 279 ? 89.337  149.257 165.417 1.00 127.33 ? 279  ASP A CA    1 
ATOM   1627  C  C     . ASP A 1 279 ? 90.363  148.512 164.569 1.00 122.36 ? 279  ASP A C     1 
ATOM   1628  O  O     . ASP A 1 279 ? 90.892  147.492 165.028 1.00 119.25 ? 279  ASP A O     1 
ATOM   1629  C  CB    . ASP A 1 279 ? 88.338  148.254 166.006 1.00 129.95 ? 279  ASP A CB    1 
ATOM   1630  C  CG    . ASP A 1 279 ? 87.792  148.696 167.348 1.00 135.81 ? 279  ASP A CG    1 
ATOM   1631  O  OD1   . ASP A 1 279 ? 88.579  149.204 168.172 1.00 137.46 ? 279  ASP A OD1   1 
ATOM   1632  O  OD2   . ASP A 1 279 ? 86.575  148.536 167.579 1.00 137.33 ? 279  ASP A OD2   1 
ATOM   1633  N  N     . VAL A 1 280 ? 90.656  148.972 163.352 1.00 122.55 ? 280  VAL A N     1 
ATOM   1634  C  CA    . VAL A 1 280 ? 91.557  148.224 162.480 1.00 115.87 ? 280  VAL A CA    1 
ATOM   1635  C  C     . VAL A 1 280 ? 93.001  148.361 162.945 1.00 115.19 ? 280  VAL A C     1 
ATOM   1636  O  O     . VAL A 1 280 ? 93.844  147.507 162.651 1.00 115.93 ? 280  VAL A O     1 
ATOM   1637  C  CB    . VAL A 1 280 ? 91.386  148.673 161.018 1.00 114.26 ? 280  VAL A CB    1 
ATOM   1638  C  CG1   . VAL A 1 280 ? 91.995  150.044 160.806 1.00 113.91 ? 280  VAL A CG1   1 
ATOM   1639  C  CG2   . VAL A 1 280 ? 92.012  147.658 160.078 1.00 113.64 ? 280  VAL A CG2   1 
ATOM   1640  N  N     . TRP A 1 281 ? 93.315  149.437 163.671 1.00 115.34 ? 281  TRP A N     1 
ATOM   1641  C  CA    . TRP A 1 281 ? 94.683  149.644 164.132 1.00 112.88 ? 281  TRP A CA    1 
ATOM   1642  C  C     . TRP A 1 281 ? 95.118  148.604 165.155 1.00 114.68 ? 281  TRP A C     1 
ATOM   1643  O  O     . TRP A 1 281 ? 96.320  148.364 165.304 1.00 112.22 ? 281  TRP A O     1 
ATOM   1644  C  CB    . TRP A 1 281 ? 94.829  151.055 164.703 1.00 112.60 ? 281  TRP A CB    1 
ATOM   1645  C  CG    . TRP A 1 281 ? 94.195  151.248 166.045 1.00 117.22 ? 281  TRP A CG    1 
ATOM   1646  C  CD1   . TRP A 1 281 ? 92.934  151.702 166.294 1.00 122.35 ? 281  TRP A CD1   1 
ATOM   1647  C  CD2   . TRP A 1 281 ? 94.795  151.012 167.323 1.00 116.61 ? 281  TRP A CD2   1 
ATOM   1648  N  NE1   . TRP A 1 281 ? 92.708  151.754 167.646 1.00 126.74 ? 281  TRP A NE1   1 
ATOM   1649  C  CE2   . TRP A 1 281 ? 93.836  151.336 168.300 1.00 121.87 ? 281  TRP A CE2   1 
ATOM   1650  C  CE3   . TRP A 1 281 ? 96.049  150.553 167.735 1.00 115.91 ? 281  TRP A CE3   1 
ATOM   1651  C  CZ2   . TRP A 1 281 ? 94.090  151.215 169.661 1.00 124.83 ? 281  TRP A CZ2   1 
ATOM   1652  C  CZ3   . TRP A 1 281 ? 96.299  150.435 169.086 1.00 120.34 ? 281  TRP A CZ3   1 
ATOM   1653  C  CH2   . TRP A 1 281 ? 95.325  150.764 170.034 1.00 124.77 ? 281  TRP A CH2   1 
ATOM   1654  N  N     . GLN A 1 282 ? 94.174  147.983 165.863 1.00 115.94 ? 282  GLN A N     1 
ATOM   1655  C  CA    . GLN A 1 282 ? 94.501  146.931 166.817 1.00 113.76 ? 282  GLN A CA    1 
ATOM   1656  C  C     . GLN A 1 282 ? 94.815  145.598 166.155 1.00 110.00 ? 282  GLN A C     1 
ATOM   1657  O  O     . GLN A 1 282 ? 95.556  144.799 166.735 1.00 112.44 ? 282  GLN A O     1 
ATOM   1658  C  CB    . GLN A 1 282 ? 93.349  146.736 167.805 1.00 116.10 ? 282  GLN A CB    1 
ATOM   1659  C  CG    . GLN A 1 282 ? 93.037  147.950 168.654 1.00 120.56 ? 282  GLN A CG    1 
ATOM   1660  C  CD    . GLN A 1 282 ? 91.946  147.681 169.667 1.00 125.77 ? 282  GLN A CD    1 
ATOM   1661  O  OE1   . GLN A 1 282 ? 91.534  146.538 169.861 1.00 128.46 ? 282  GLN A OE1   1 
ATOM   1662  N  NE2   . GLN A 1 282 ? 91.471  148.734 170.320 1.00 127.52 ? 282  GLN A NE2   1 
ATOM   1663  N  N     . ASN A 1 283 ? 94.278  145.340 164.965 1.00 107.85 ? 283  ASN A N     1 
ATOM   1664  C  CA    . ASN A 1 283 ? 94.383  144.039 164.322 1.00 104.96 ? 283  ASN A CA    1 
ATOM   1665  C  C     . ASN A 1 283 ? 95.572  143.937 163.377 1.00 99.35  ? 283  ASN A C     1 
ATOM   1666  O  O     . ASN A 1 283 ? 95.742  142.902 162.727 1.00 104.38 ? 283  ASN A O     1 
ATOM   1667  C  CB    . ASN A 1 283 ? 93.094  143.727 163.562 1.00 110.59 ? 283  ASN A CB    1 
ATOM   1668  C  CG    . ASN A 1 283 ? 92.020  143.147 164.455 1.00 119.94 ? 283  ASN A CG    1 
ATOM   1669  O  OD1   . ASN A 1 283 ? 92.309  142.409 165.395 1.00 118.85 ? 283  ASN A OD1   1 
ATOM   1670  N  ND2   . ASN A 1 283 ? 90.768  143.481 164.166 1.00 123.40 ? 283  ASN A ND2   1 
ATOM   1671  N  N     . VAL A 1 284 ? 96.393  144.979 163.281 1.00 95.58  ? 284  VAL A N     1 
ATOM   1672  C  CA    . VAL A 1 284 ? 97.541  144.998 162.384 1.00 94.14  ? 284  VAL A CA    1 
ATOM   1673  C  C     . VAL A 1 284 ? 98.789  145.290 163.202 1.00 92.16  ? 284  VAL A C     1 
ATOM   1674  O  O     . VAL A 1 284 ? 98.845  146.295 163.919 1.00 102.65 ? 284  VAL A O     1 
ATOM   1675  C  CB    . VAL A 1 284 ? 97.370  146.041 161.266 1.00 96.18  ? 284  VAL A CB    1 
ATOM   1676  C  CG1   . VAL A 1 284 ? 98.697  146.303 160.581 1.00 88.32  ? 284  VAL A CG1   1 
ATOM   1677  C  CG2   . VAL A 1 284 ? 96.328  145.576 160.264 1.00 99.44  ? 284  VAL A CG2   1 
ATOM   1678  N  N     . LEU A 1 285 ? 99.786  144.419 163.090 1.00 89.14  ? 285  LEU A N     1 
ATOM   1679  C  CA    . LEU A 1 285 ? 101.063 144.587 163.767 1.00 90.90  ? 285  LEU A CA    1 
ATOM   1680  C  C     . LEU A 1 285 ? 102.157 144.792 162.731 1.00 89.41  ? 285  LEU A C     1 
ATOM   1681  O  O     . LEU A 1 285 ? 102.285 144.007 161.788 1.00 96.02  ? 285  LEU A O     1 
ATOM   1682  C  CB    . LEU A 1 285 ? 101.392 143.376 164.652 1.00 96.30  ? 285  LEU A CB    1 
ATOM   1683  C  CG    . LEU A 1 285 ? 102.799 143.264 165.250 1.00 94.60  ? 285  LEU A CG    1 
ATOM   1684  C  CD1   . LEU A 1 285 ? 102.732 142.654 166.631 1.00 92.60  ? 285  LEU A CD1   1 
ATOM   1685  C  CD2   . LEU A 1 285 ? 103.715 142.425 164.377 1.00 96.47  ? 285  LEU A CD2   1 
ATOM   1686  N  N     . VAL A 1 286 ? 102.947 145.844 162.912 1.00 90.01  ? 286  VAL A N     1 
ATOM   1687  C  CA    . VAL A 1 286 ? 104.047 146.171 162.015 1.00 88.86  ? 286  VAL A CA    1 
ATOM   1688  C  C     . VAL A 1 286 ? 105.343 145.817 162.722 1.00 87.88  ? 286  VAL A C     1 
ATOM   1689  O  O     . VAL A 1 286 ? 105.694 146.439 163.730 1.00 93.15  ? 286  VAL A O     1 
ATOM   1690  C  CB    . VAL A 1 286 ? 104.029 147.651 161.609 1.00 90.04  ? 286  VAL A CB    1 
ATOM   1691  C  CG1   . VAL A 1 286 ? 105.277 147.991 160.829 1.00 88.12  ? 286  VAL A CG1   1 
ATOM   1692  C  CG2   . VAL A 1 286 ? 102.794 147.944 160.784 1.00 96.03  ? 286  VAL A CG2   1 
ATOM   1693  N  N     . CYS A 1 287 ? 106.058 144.833 162.191 1.00 86.09  ? 287  CYS A N     1 
ATOM   1694  C  CA    . CYS A 1 287 ? 107.242 144.286 162.836 1.00 86.51  ? 287  CYS A CA    1 
ATOM   1695  C  C     . CYS A 1 287 ? 108.483 144.748 162.085 1.00 86.68  ? 287  CYS A C     1 
ATOM   1696  O  O     . CYS A 1 287 ? 108.727 144.312 160.957 1.00 86.65  ? 287  CYS A O     1 
ATOM   1697  C  CB    . CYS A 1 287 ? 107.173 142.761 162.883 1.00 86.94  ? 287  CYS A CB    1 
ATOM   1698  S  SG    . CYS A 1 287 ? 108.769 141.947 162.998 1.00 109.78 ? 287  CYS A SG    1 
ATOM   1699  N  N     . ILE A 1 288 ? 109.263 145.623 162.711 1.00 89.82  ? 288  ILE A N     1 
ATOM   1700  C  CA    . ILE A 1 288 ? 110.506 146.130 162.142 1.00 86.78  ? 288  ILE A CA    1 
ATOM   1701  C  C     . ILE A 1 288 ? 111.623 145.219 162.620 1.00 88.24  ? 288  ILE A C     1 
ATOM   1702  O  O     . ILE A 1 288 ? 111.812 145.038 163.828 1.00 95.68  ? 288  ILE A O     1 
ATOM   1703  C  CB    . ILE A 1 288 ? 110.772 147.585 162.548 1.00 85.31  ? 288  ILE A CB    1 
ATOM   1704  C  CG1   . ILE A 1 288 ? 109.543 148.452 162.280 1.00 92.09  ? 288  ILE A CG1   1 
ATOM   1705  C  CG2   . ILE A 1 288 ? 111.986 148.124 161.817 1.00 83.61  ? 288  ILE A CG2   1 
ATOM   1706  C  CD1   . ILE A 1 288 ? 109.718 149.891 162.694 1.00 95.80  ? 288  ILE A CD1   1 
ATOM   1707  N  N     . VAL A 1 289 ? 112.363 144.636 161.688 1.00 89.29  ? 289  VAL A N     1 
ATOM   1708  C  CA    . VAL A 1 289 ? 113.455 143.730 162.018 1.00 92.07  ? 289  VAL A CA    1 
ATOM   1709  C  C     . VAL A 1 289 ? 114.737 144.360 161.492 1.00 95.29  ? 289  VAL A C     1 
ATOM   1710  O  O     . VAL A 1 289 ? 114.923 144.502 160.279 1.00 101.00 ? 289  VAL A O     1 
ATOM   1711  C  CB    . VAL A 1 289 ? 113.234 142.329 161.441 1.00 92.01  ? 289  VAL A CB    1 
ATOM   1712  C  CG1   . VAL A 1 289 ? 114.537 141.565 161.412 1.00 91.69  ? 289  VAL A CG1   1 
ATOM   1713  C  CG2   . VAL A 1 289 ? 112.208 141.577 162.261 1.00 91.10  ? 289  VAL A CG2   1 
ATOM   1714  N  N     . ALA A 1 290 ? 115.623 144.750 162.401 1.00 95.57  ? 290  ALA A N     1 
ATOM   1715  C  CA    . ALA A 1 290 ? 116.934 145.234 162.008 1.00 93.31  ? 290  ALA A CA    1 
ATOM   1716  C  C     . ALA A 1 290 ? 117.835 144.060 161.651 1.00 100.11 ? 290  ALA A C     1 
ATOM   1717  O  O     . ALA A 1 290 ? 117.476 142.894 161.826 1.00 110.86 ? 290  ALA A O     1 
ATOM   1718  C  CB    . ALA A 1 290 ? 117.565 146.064 163.124 1.00 97.70  ? 290  ALA A CB    1 
ATOM   1719  N  N     . ASP A 1 291 ? 119.020 144.377 161.139 1.00 101.52 ? 291  ASP A N     1 
ATOM   1720  C  CA    . ASP A 1 291 ? 119.958 143.338 160.737 1.00 111.06 ? 291  ASP A CA    1 
ATOM   1721  C  C     . ASP A 1 291 ? 121.229 143.317 161.569 1.00 113.80 ? 291  ASP A C     1 
ATOM   1722  O  O     . ASP A 1 291 ? 121.883 142.273 161.649 1.00 119.52 ? 291  ASP A O     1 
ATOM   1723  C  CB    . ASP A 1 291 ? 120.329 143.500 159.261 1.00 116.18 ? 291  ASP A CB    1 
ATOM   1724  C  CG    . ASP A 1 291 ? 120.631 142.178 158.592 1.00 119.12 ? 291  ASP A CG    1 
ATOM   1725  O  OD1   . ASP A 1 291 ? 120.601 141.139 159.282 1.00 115.99 ? 291  ASP A OD1   1 
ATOM   1726  O  OD2   . ASP A 1 291 ? 120.892 142.179 157.372 1.00 123.22 ? 291  ASP A OD2   1 
ATOM   1727  N  N     . GLY A 1 292 ? 121.601 144.434 162.183 1.00 112.14 ? 292  GLY A N     1 
ATOM   1728  C  CA    . GLY A 1 292 ? 122.761 144.451 163.049 1.00 119.01 ? 292  GLY A CA    1 
ATOM   1729  C  C     . GLY A 1 292 ? 122.901 145.745 163.820 1.00 127.92 ? 292  GLY A C     1 
ATOM   1730  O  O     . GLY A 1 292 ? 122.826 146.828 163.236 1.00 133.75 ? 292  GLY A O     1 
ATOM   1731  N  N     . ARG A 1 293 ? 123.116 145.649 165.133 1.00 125.97 ? 293  ARG A N     1 
ATOM   1732  C  CA    . ARG A 1 293 ? 123.321 146.849 165.934 1.00 127.82 ? 293  ARG A CA    1 
ATOM   1733  C  C     . ARG A 1 293 ? 124.618 147.556 165.579 1.00 134.85 ? 293  ARG A C     1 
ATOM   1734  O  O     . ARG A 1 293 ? 124.789 148.729 165.926 1.00 140.02 ? 293  ARG A O     1 
ATOM   1735  C  CB    . ARG A 1 293 ? 123.303 146.498 167.420 1.00 125.78 ? 293  ARG A CB    1 
ATOM   1736  C  CG    . ARG A 1 293 ? 124.427 145.593 167.870 1.00 129.65 ? 293  ARG A CG    1 
ATOM   1737  C  CD    . ARG A 1 293 ? 124.570 145.643 169.378 1.00 131.39 ? 293  ARG A CD    1 
ATOM   1738  N  NE    . ARG A 1 293 ? 124.349 146.987 169.895 1.00 131.35 ? 293  ARG A NE    1 
ATOM   1739  C  CZ    . ARG A 1 293 ? 124.600 147.360 171.142 1.00 131.38 ? 293  ARG A CZ    1 
ATOM   1740  N  NH1   . ARG A 1 293 ? 125.078 146.508 172.034 1.00 133.72 ? 293  ARG A NH1   1 
ATOM   1741  N  NH2   . ARG A 1 293 ? 124.366 148.617 171.502 1.00 130.67 ? 293  ARG A NH2   1 
ATOM   1742  N  N     . GLU A 1 294 ? 125.529 146.868 164.896 1.00 134.54 ? 294  GLU A N     1 
ATOM   1743  C  CA    . GLU A 1 294 ? 126.782 147.457 164.455 1.00 140.03 ? 294  GLU A CA    1 
ATOM   1744  C  C     . GLU A 1 294 ? 126.656 148.208 163.137 1.00 141.78 ? 294  GLU A C     1 
ATOM   1745  O  O     . GLU A 1 294 ? 127.591 148.922 162.761 1.00 146.70 ? 294  GLU A O     1 
ATOM   1746  C  CB    . GLU A 1 294 ? 127.841 146.362 164.322 1.00 146.60 ? 294  GLU A CB    1 
ATOM   1747  C  CG    . GLU A 1 294 ? 127.895 145.726 162.944 1.00 147.34 ? 294  GLU A CG    1 
ATOM   1748  C  CD    . GLU A 1 294 ? 128.494 144.334 162.965 1.00 152.23 ? 294  GLU A CD    1 
ATOM   1749  O  OE1   . GLU A 1 294 ? 128.226 143.584 163.927 1.00 153.62 ? 294  GLU A OE1   1 
ATOM   1750  O  OE2   . GLU A 1 294 ? 129.231 143.990 162.018 1.00 150.68 ? 294  GLU A OE2   1 
ATOM   1751  N  N     . GLN A 1 295 ? 125.531 148.074 162.434 1.00 137.24 ? 295  GLN A N     1 
ATOM   1752  C  CA    . GLN A 1 295 ? 125.387 148.639 161.102 1.00 137.22 ? 295  GLN A CA    1 
ATOM   1753  C  C     . GLN A 1 295 ? 124.214 149.597 160.951 1.00 131.07 ? 295  GLN A C     1 
ATOM   1754  O  O     . GLN A 1 295 ? 124.160 150.319 159.950 1.00 136.04 ? 295  GLN A O     1 
ATOM   1755  C  CB    . GLN A 1 295 ? 125.251 147.516 160.064 1.00 135.64 ? 295  GLN A CB    1 
ATOM   1756  C  CG    . GLN A 1 295 ? 126.558 146.815 159.708 1.00 135.66 ? 295  GLN A CG    1 
ATOM   1757  C  CD    . GLN A 1 295 ? 127.550 147.712 158.982 1.00 145.35 ? 295  GLN A CD    1 
ATOM   1758  O  OE1   . GLN A 1 295 ? 127.280 148.883 158.721 1.00 147.02 ? 295  GLN A OE1   1 
ATOM   1759  N  NE2   . GLN A 1 295 ? 128.712 147.158 158.656 1.00 151.56 ? 295  GLN A NE2   1 
ATOM   1760  N  N     . VAL A 1 296 ? 123.274 149.623 161.896 1.00 125.17 ? 296  VAL A N     1 
ATOM   1761  C  CA    . VAL A 1 296 ? 122.161 150.560 161.803 1.00 124.33 ? 296  VAL A CA    1 
ATOM   1762  C  C     . VAL A 1 296 ? 122.686 151.985 161.899 1.00 129.02 ? 296  VAL A C     1 
ATOM   1763  O  O     . VAL A 1 296 ? 123.684 152.256 162.580 1.00 134.26 ? 296  VAL A O     1 
ATOM   1764  C  CB    . VAL A 1 296 ? 121.108 150.272 162.883 1.00 121.99 ? 296  VAL A CB    1 
ATOM   1765  C  CG1   . VAL A 1 296 ? 120.543 148.879 162.710 1.00 119.00 ? 296  VAL A CG1   1 
ATOM   1766  C  CG2   . VAL A 1 296 ? 121.714 150.423 164.264 1.00 125.35 ? 296  VAL A CG2   1 
ATOM   1767  N  N     . HIS A 1 297 ? 122.025 152.897 161.202 1.00 127.97 ? 297  HIS A N     1 
ATOM   1768  C  CA    . HIS A 1 297 ? 122.490 154.273 161.132 1.00 127.61 ? 297  HIS A CA    1 
ATOM   1769  C  C     . HIS A 1 297 ? 122.273 154.966 162.474 1.00 130.27 ? 297  HIS A C     1 
ATOM   1770  O  O     . HIS A 1 297 ? 121.201 154.815 163.077 1.00 130.97 ? 297  HIS A O     1 
ATOM   1771  C  CB    . HIS A 1 297 ? 121.747 155.012 160.022 1.00 129.53 ? 297  HIS A CB    1 
ATOM   1772  C  CG    . HIS A 1 297 ? 122.544 156.100 159.375 1.00 131.53 ? 297  HIS A CG    1 
ATOM   1773  N  ND1   . HIS A 1 297 ? 122.489 157.413 159.791 1.00 135.20 ? 297  HIS A ND1   1 
ATOM   1774  C  CD2   . HIS A 1 297 ? 123.407 156.072 158.333 1.00 130.78 ? 297  HIS A CD2   1 
ATOM   1775  C  CE1   . HIS A 1 297 ? 123.288 158.145 159.036 1.00 136.19 ? 297  HIS A CE1   1 
ATOM   1776  N  NE2   . HIS A 1 297 ? 123.857 157.355 158.144 1.00 134.93 ? 297  HIS A NE2   1 
ATOM   1777  N  N     . PRO A 1 298 ? 123.262 155.703 162.987 1.00 128.19 ? 298  PRO A N     1 
ATOM   1778  C  CA    . PRO A 1 298 ? 123.037 156.441 164.242 1.00 130.52 ? 298  PRO A CA    1 
ATOM   1779  C  C     . PRO A 1 298 ? 121.886 157.425 164.157 1.00 132.91 ? 298  PRO A C     1 
ATOM   1780  O  O     . PRO A 1 298 ? 121.160 157.612 165.142 1.00 135.66 ? 298  PRO A O     1 
ATOM   1781  C  CB    . PRO A 1 298 ? 124.380 157.145 164.472 1.00 128.33 ? 298  PRO A CB    1 
ATOM   1782  C  CG    . PRO A 1 298 ? 125.373 156.303 163.746 1.00 124.61 ? 298  PRO A CG    1 
ATOM   1783  C  CD    . PRO A 1 298 ? 124.658 155.790 162.533 1.00 123.76 ? 298  PRO A CD    1 
ATOM   1784  N  N     . LYS A 1 299 ? 121.689 158.061 163.001 1.00 129.67 ? 299  LYS A N     1 
ATOM   1785  C  CA    . LYS A 1 299 ? 120.516 158.909 162.831 1.00 129.95 ? 299  LYS A CA    1 
ATOM   1786  C  C     . LYS A 1 299 ? 119.232 158.091 162.870 1.00 127.99 ? 299  LYS A C     1 
ATOM   1787  O  O     . LYS A 1 299 ? 118.212 158.562 163.387 1.00 128.56 ? 299  LYS A O     1 
ATOM   1788  C  CB    . LYS A 1 299 ? 120.614 159.700 161.527 1.00 131.99 ? 299  LYS A CB    1 
ATOM   1789  C  CG    . LYS A 1 299 ? 121.955 160.379 161.296 1.00 137.47 ? 299  LYS A CG    1 
ATOM   1790  C  CD    . LYS A 1 299 ? 122.410 161.149 162.526 1.00 139.37 ? 299  LYS A CD    1 
ATOM   1791  C  CE    . LYS A 1 299 ? 123.425 162.219 162.162 1.00 143.79 ? 299  LYS A CE    1 
ATOM   1792  N  NZ    . LYS A 1 299 ? 123.035 162.954 160.928 1.00 141.78 ? 299  LYS A NZ    1 
ATOM   1793  N  N     . THR A 1 300 ? 119.312 156.849 162.403 1.00 126.04 ? 300  THR A N     1 
ATOM   1794  C  CA    . THR A 1 300 ? 118.172 155.947 162.433 1.00 127.49 ? 300  THR A CA    1 
ATOM   1795  C  C     . THR A 1 300 ? 117.828 155.649 163.891 1.00 126.72 ? 300  THR A C     1 
ATOM   1796  O  O     . THR A 1 300 ? 116.657 155.648 164.272 1.00 128.35 ? 300  THR A O     1 
ATOM   1797  C  CB    . THR A 1 300 ? 118.470 154.629 161.696 1.00 124.59 ? 300  THR A CB    1 
ATOM   1798  O  OG1   . THR A 1 300 ? 117.305 154.208 160.975 1.00 130.02 ? 300  THR A OG1   1 
ATOM   1799  C  CG2   . THR A 1 300 ? 118.868 153.544 162.685 1.00 118.46 ? 300  THR A CG2   1 
ATOM   1800  N  N     . LEU A 1 301 ? 118.853 155.395 164.703 1.00 123.96 ? 301  LEU A N     1 
ATOM   1801  C  CA    . LEU A 1 301 ? 118.649 155.120 166.122 1.00 125.22 ? 301  LEU A CA    1 
ATOM   1802  C  C     . LEU A 1 301 ? 118.101 156.343 166.847 1.00 126.15 ? 301  LEU A C     1 
ATOM   1803  O  O     . LEU A 1 301 ? 117.242 156.220 167.728 1.00 128.20 ? 301  LEU A O     1 
ATOM   1804  C  CB    . LEU A 1 301 ? 119.955 154.654 166.759 1.00 128.34 ? 301  LEU A CB    1 
ATOM   1805  C  CG    . LEU A 1 301 ? 120.442 153.287 166.284 1.00 126.45 ? 301  LEU A CG    1 
ATOM   1806  C  CD1   . LEU A 1 301 ? 121.731 152.903 166.988 1.00 127.11 ? 301  LEU A CD1   1 
ATOM   1807  C  CD2   . LEU A 1 301 ? 119.371 152.237 166.502 1.00 120.12 ? 301  LEU A CD2   1 
ATOM   1808  N  N     . ASP A 1 302 ? 118.590 157.533 166.494 1.00 125.15 ? 302  ASP A N     1 
ATOM   1809  C  CA    . ASP A 1 302 ? 118.052 158.754 167.086 1.00 125.88 ? 302  ASP A CA    1 
ATOM   1810  C  C     . ASP A 1 302 ? 116.581 158.930 166.735 1.00 126.93 ? 302  ASP A C     1 
ATOM   1811  O  O     . ASP A 1 302 ? 115.772 159.317 167.586 1.00 128.03 ? 302  ASP A O     1 
ATOM   1812  C  CB    . ASP A 1 302 ? 118.865 159.963 166.629 1.00 130.68 ? 302  ASP A CB    1 
ATOM   1813  C  CG    . ASP A 1 302 ? 120.293 159.926 167.132 1.00 136.25 ? 302  ASP A CG    1 
ATOM   1814  O  OD1   . ASP A 1 302 ? 120.660 158.938 167.799 1.00 138.68 ? 302  ASP A OD1   1 
ATOM   1815  O  OD2   . ASP A 1 302 ? 121.047 160.884 166.861 1.00 138.34 ? 302  ASP A OD2   1 
ATOM   1816  N  N     . TYR A 1 303 ? 116.211 158.638 165.487 1.00 125.50 ? 303  TYR A N     1 
ATOM   1817  C  CA    . TYR A 1 303 ? 114.802 158.686 165.109 1.00 121.45 ? 303  TYR A CA    1 
ATOM   1818  C  C     . TYR A 1 303 ? 113.985 157.670 165.896 1.00 120.26 ? 303  TYR A C     1 
ATOM   1819  O  O     . TYR A 1 303 ? 112.850 157.952 166.299 1.00 122.00 ? 303  TYR A O     1 
ATOM   1820  C  CB    . TYR A 1 303 ? 114.646 158.444 163.610 1.00 116.15 ? 303  TYR A CB    1 
ATOM   1821  C  CG    . TYR A 1 303 ? 113.204 158.378 163.170 1.00 113.47 ? 303  TYR A CG    1 
ATOM   1822  C  CD1   . TYR A 1 303 ? 112.395 159.502 163.213 1.00 116.42 ? 303  TYR A CD1   1 
ATOM   1823  C  CD2   . TYR A 1 303 ? 112.653 157.191 162.716 1.00 111.61 ? 303  TYR A CD2   1 
ATOM   1824  C  CE1   . TYR A 1 303 ? 111.076 159.446 162.816 1.00 117.68 ? 303  TYR A CE1   1 
ATOM   1825  C  CE2   . TYR A 1 303 ? 111.336 157.126 162.316 1.00 111.82 ? 303  TYR A CE2   1 
ATOM   1826  C  CZ    . TYR A 1 303 ? 110.553 158.255 162.368 1.00 117.55 ? 303  TYR A CZ    1 
ATOM   1827  O  OH    . TYR A 1 303 ? 109.238 158.198 161.970 1.00 119.69 ? 303  TYR A OH    1 
ATOM   1828  N  N     . LEU A 1 304 ? 114.542 156.478 166.113 1.00 118.32 ? 304  LEU A N     1 
ATOM   1829  C  CA    . LEU A 1 304 ? 113.819 155.452 166.855 1.00 117.55 ? 304  LEU A CA    1 
ATOM   1830  C  C     . LEU A 1 304 ? 113.598 155.878 168.301 1.00 120.71 ? 304  LEU A C     1 
ATOM   1831  O  O     . LEU A 1 304 ? 112.534 155.621 168.876 1.00 122.50 ? 304  LEU A O     1 
ATOM   1832  C  CB    . LEU A 1 304 ? 114.572 154.125 166.784 1.00 115.21 ? 304  LEU A CB    1 
ATOM   1833  C  CG    . LEU A 1 304 ? 114.570 153.457 165.407 1.00 111.52 ? 304  LEU A CG    1 
ATOM   1834  C  CD1   . LEU A 1 304 ? 115.405 152.190 165.415 1.00 112.71 ? 304  LEU A CD1   1 
ATOM   1835  C  CD2   . LEU A 1 304 ? 113.160 153.174 164.929 1.00 106.37 ? 304  LEU A CD2   1 
ATOM   1836  N  N     . GLU A 1 305 ? 114.593 156.531 168.906 1.00 121.96 ? 305  GLU A N     1 
ATOM   1837  C  CA    . GLU A 1 305 ? 114.370 157.154 170.208 1.00 122.53 ? 305  GLU A CA    1 
ATOM   1838  C  C     . GLU A 1 305 ? 113.291 158.223 170.130 1.00 123.62 ? 305  GLU A C     1 
ATOM   1839  O  O     . GLU A 1 305 ? 112.470 158.347 171.045 1.00 123.50 ? 305  GLU A O     1 
ATOM   1840  C  CB    . GLU A 1 305 ? 115.662 157.766 170.750 1.00 127.35 ? 305  GLU A CB    1 
ATOM   1841  C  CG    . GLU A 1 305 ? 116.874 156.858 170.729 1.00 131.66 ? 305  GLU A CG    1 
ATOM   1842  C  CD    . GLU A 1 305 ? 117.788 157.088 171.917 1.00 135.86 ? 305  GLU A CD    1 
ATOM   1843  O  OE1   . GLU A 1 305 ? 118.910 156.541 171.924 1.00 135.70 ? 305  GLU A OE1   1 
ATOM   1844  O  OE2   . GLU A 1 305 ? 117.385 157.822 172.844 1.00 137.53 ? 305  GLU A OE2   1 
ATOM   1845  N  N     . ALA A 1 306 ? 113.283 159.007 169.049 1.00 123.80 ? 306  ALA A N     1 
ATOM   1846  C  CA    . ALA A 1 306 ? 112.304 160.081 168.915 1.00 125.60 ? 306  ALA A CA    1 
ATOM   1847  C  C     . ALA A 1 306 ? 110.882 159.539 168.878 1.00 125.62 ? 306  ALA A C     1 
ATOM   1848  O  O     . ALA A 1 306 ? 109.975 160.118 169.486 1.00 130.55 ? 306  ALA A O     1 
ATOM   1849  C  CB    . ALA A 1 306 ? 112.597 160.903 167.661 1.00 126.67 ? 306  ALA A CB    1 
ATOM   1850  N  N     . ILE A 1 307 ? 110.663 158.429 168.173 1.00 121.46 ? 307  ILE A N     1 
ATOM   1851  C  CA    . ILE A 1 307 ? 109.327 157.846 168.090 1.00 118.35 ? 307  ILE A CA    1 
ATOM   1852  C  C     . ILE A 1 307 ? 109.091 156.983 169.321 1.00 118.44 ? 307  ILE A C     1 
ATOM   1853  O  O     . ILE A 1 307 ? 108.013 156.403 169.491 1.00 116.70 ? 307  ILE A O     1 
ATOM   1854  C  CB    . ILE A 1 307 ? 109.133 157.028 166.801 1.00 111.52 ? 307  ILE A CB    1 
ATOM   1855  C  CG1   . ILE A 1 307 ? 110.307 156.079 166.585 1.00 113.40 ? 307  ILE A CG1   1 
ATOM   1856  C  CG2   . ILE A 1 307 ? 108.990 157.951 165.609 1.00 113.94 ? 307  ILE A CG2   1 
ATOM   1857  C  CD1   . ILE A 1 307 ? 109.984 154.914 165.685 1.00 111.11 ? 307  ILE A CD1   1 
ATOM   1858  N  N     . GLY A 1 308 ? 110.097 156.897 170.187 1.00 122.30 ? 308  GLY A N     1 
ATOM   1859  C  CA    . GLY A 1 308 ? 109.974 156.163 171.430 1.00 123.81 ? 308  GLY A CA    1 
ATOM   1860  C  C     . GLY A 1 308 ? 109.912 154.662 171.257 1.00 117.93 ? 308  GLY A C     1 
ATOM   1861  O  O     . GLY A 1 308 ? 108.915 154.026 171.610 1.00 117.40 ? 308  GLY A O     1 
ATOM   1862  N  N     . LEU A 1 309 ? 110.975 154.085 170.703 1.00 116.35 ? 309  LEU A N     1 
ATOM   1863  C  CA    . LEU A 1 309 ? 111.012 152.649 170.470 1.00 110.66 ? 309  LEU A CA    1 
ATOM   1864  C  C     . LEU A 1 309 ? 112.412 152.066 170.663 1.00 114.44 ? 309  LEU A C     1 
ATOM   1865  O  O     . LEU A 1 309 ? 112.613 150.874 170.408 1.00 115.44 ? 309  LEU A O     1 
ATOM   1866  C  CB    . LEU A 1 309 ? 110.448 152.369 169.067 1.00 110.70 ? 309  LEU A CB    1 
ATOM   1867  C  CG    . LEU A 1 309 ? 110.519 151.053 168.302 1.00 105.51 ? 309  LEU A CG    1 
ATOM   1868  C  CD1   . LEU A 1 309 ? 109.265 150.869 167.482 1.00 104.38 ? 309  LEU A CD1   1 
ATOM   1869  C  CD2   . LEU A 1 309 ? 111.719 151.107 167.400 1.00 106.75 ? 309  LEU A CD2   1 
ATOM   1870  N  N     . TYR A 1 310 ? 113.373 152.850 171.145 1.00 120.31 ? 310  TYR A N     1 
ATOM   1871  C  CA    . TYR A 1 310 ? 114.726 152.355 171.359 1.00 116.62 ? 310  TYR A CA    1 
ATOM   1872  C  C     . TYR A 1 310 ? 115.338 153.119 172.525 1.00 125.06 ? 310  TYR A C     1 
ATOM   1873  O  O     . TYR A 1 310 ? 115.144 154.330 172.657 1.00 128.96 ? 310  TYR A O     1 
ATOM   1874  C  CB    . TYR A 1 310 ? 115.571 152.501 170.084 1.00 112.60 ? 310  TYR A CB    1 
ATOM   1875  C  CG    . TYR A 1 310 ? 117.042 152.149 170.207 1.00 117.78 ? 310  TYR A CG    1 
ATOM   1876  C  CD1   . TYR A 1 310 ? 117.939 152.991 170.850 1.00 119.31 ? 310  TYR A CD1   1 
ATOM   1877  C  CD2   . TYR A 1 310 ? 117.543 150.997 169.620 1.00 121.07 ? 310  TYR A CD2   1 
ATOM   1878  C  CE1   . TYR A 1 310 ? 119.278 152.672 170.944 1.00 122.09 ? 310  TYR A CE1   1 
ATOM   1879  C  CE2   . TYR A 1 310 ? 118.879 150.671 169.710 1.00 122.59 ? 310  TYR A CE2   1 
ATOM   1880  C  CZ    . TYR A 1 310 ? 119.742 151.512 170.369 1.00 121.83 ? 310  TYR A CZ    1 
ATOM   1881  O  OH    . TYR A 1 310 ? 121.076 151.190 170.456 1.00 125.21 ? 310  TYR A OH    1 
ATOM   1882  N  N     . ASP A 1 311 ? 116.077 152.399 173.367 1.00 124.29 ? 311  ASP A N     1 
ATOM   1883  C  CA    . ASP A 1 311 ? 116.735 153.013 174.519 1.00 123.75 ? 311  ASP A CA    1 
ATOM   1884  C  C     . ASP A 1 311 ? 118.092 152.357 174.709 1.00 123.39 ? 311  ASP A C     1 
ATOM   1885  O  O     . ASP A 1 311 ? 118.166 151.194 175.124 1.00 125.29 ? 311  ASP A O     1 
ATOM   1886  C  CB    . ASP A 1 311 ? 115.886 152.875 175.777 1.00 122.99 ? 311  ASP A CB    1 
ATOM   1887  C  CG    . ASP A 1 311 ? 116.096 154.018 176.748 1.00 128.61 ? 311  ASP A CG    1 
ATOM   1888  O  OD1   . ASP A 1 311 ? 115.656 155.145 176.440 1.00 128.79 ? 311  ASP A OD1   1 
ATOM   1889  O  OD2   . ASP A 1 311 ? 116.706 153.794 177.814 1.00 135.07 ? 311  ASP A OD2   1 
ATOM   1890  N  N     . GLU A 1 312 ? 119.159 153.103 174.413 1.00 123.82 ? 312  GLU A N     1 
ATOM   1891  C  CA    . GLU A 1 312 ? 120.505 152.541 174.458 1.00 123.16 ? 312  GLU A CA    1 
ATOM   1892  C  C     . GLU A 1 312 ? 120.895 152.129 175.871 1.00 125.28 ? 312  GLU A C     1 
ATOM   1893  O  O     . GLU A 1 312 ? 121.488 151.064 176.068 1.00 126.03 ? 312  GLU A O     1 
ATOM   1894  C  CB    . GLU A 1 312 ? 121.508 153.549 173.899 1.00 124.29 ? 312  GLU A CB    1 
ATOM   1895  C  CG    . GLU A 1 312 ? 122.968 153.139 174.038 1.00 127.65 ? 312  GLU A CG    1 
ATOM   1896  C  CD    . GLU A 1 312 ? 123.415 152.141 172.982 1.00 132.40 ? 312  GLU A CD    1 
ATOM   1897  O  OE1   . GLU A 1 312 ? 124.601 152.187 172.593 1.00 137.22 ? 312  GLU A OE1   1 
ATOM   1898  O  OE2   . GLU A 1 312 ? 122.591 151.318 172.533 1.00 132.18 ? 312  GLU A OE2   1 
ATOM   1899  N  N     . ASP A 1 313 ? 120.578 152.962 176.866 1.00 126.59 ? 313  ASP A N     1 
ATOM   1900  C  CA    . ASP A 1 313 ? 120.912 152.626 178.247 1.00 126.07 ? 313  ASP A CA    1 
ATOM   1901  C  C     . ASP A 1 313 ? 120.193 151.362 178.696 1.00 123.47 ? 313  ASP A C     1 
ATOM   1902  O  O     . ASP A 1 313 ? 120.803 150.463 179.291 1.00 123.88 ? 313  ASP A O     1 
ATOM   1903  C  CB    . ASP A 1 313 ? 120.556 153.792 179.168 1.00 127.58 ? 313  ASP A CB    1 
ATOM   1904  C  CG    . ASP A 1 313 ? 121.245 155.081 178.771 1.00 134.41 ? 313  ASP A CG    1 
ATOM   1905  O  OD1   . ASP A 1 313 ? 122.445 155.034 178.429 1.00 138.74 ? 313  ASP A OD1   1 
ATOM   1906  O  OD2   . ASP A 1 313 ? 120.587 156.141 178.801 1.00 136.63 ? 313  ASP A OD2   1 
ATOM   1907  N  N     . LEU A 1 314 ? 118.891 151.278 178.415 1.00 121.79 ? 314  LEU A N     1 
ATOM   1908  C  CA    . LEU A 1 314 ? 118.121 150.107 178.810 1.00 119.21 ? 314  LEU A CA    1 
ATOM   1909  C  C     . LEU A 1 314 ? 118.653 148.853 178.133 1.00 116.78 ? 314  LEU A C     1 
ATOM   1910  O  O     . LEU A 1 314 ? 118.785 147.805 178.772 1.00 118.71 ? 314  LEU A O     1 
ATOM   1911  C  CB    . LEU A 1 314 ? 116.646 150.318 178.475 1.00 117.48 ? 314  LEU A CB    1 
ATOM   1912  C  CG    . LEU A 1 314 ? 115.769 149.071 178.391 1.00 114.06 ? 314  LEU A CG    1 
ATOM   1913  C  CD1   . LEU A 1 314 ? 115.721 148.376 179.736 1.00 115.89 ? 314  LEU A CD1   1 
ATOM   1914  C  CD2   . LEU A 1 314 ? 114.373 149.420 177.913 1.00 115.78 ? 314  LEU A CD2   1 
ATOM   1915  N  N     . LEU A 1 315 ? 118.976 148.943 176.841 1.00 116.32 ? 315  LEU A N     1 
ATOM   1916  C  CA    . LEU A 1 315 ? 119.531 147.785 176.150 1.00 116.30 ? 315  LEU A CA    1 
ATOM   1917  C  C     . LEU A 1 315 ? 120.861 147.370 176.764 1.00 118.13 ? 315  LEU A C     1 
ATOM   1918  O  O     . LEU A 1 315 ? 121.073 146.189 177.067 1.00 118.34 ? 315  LEU A O     1 
ATOM   1919  C  CB    . LEU A 1 315 ? 119.684 148.092 174.658 1.00 115.78 ? 315  LEU A CB    1 
ATOM   1920  C  CG    . LEU A 1 315 ? 120.512 147.182 173.743 1.00 112.63 ? 315  LEU A CG    1 
ATOM   1921  C  CD1   . LEU A 1 315 ? 119.957 147.245 172.336 1.00 117.49 ? 315  LEU A CD1   1 
ATOM   1922  C  CD2   . LEU A 1 315 ? 121.979 147.575 173.720 1.00 114.88 ? 315  LEU A CD2   1 
ATOM   1923  N  N     . THR A 1 316 ? 121.756 148.337 176.987 1.00 120.57 ? 316  THR A N     1 
ATOM   1924  C  CA    . THR A 1 316 ? 123.091 148.026 177.485 1.00 120.60 ? 316  THR A CA    1 
ATOM   1925  C  C     . THR A 1 316 ? 123.039 147.401 178.871 1.00 121.79 ? 316  THR A C     1 
ATOM   1926  O  O     . THR A 1 316 ? 123.852 146.526 179.190 1.00 123.79 ? 316  THR A O     1 
ATOM   1927  C  CB    . THR A 1 316 ? 123.951 149.289 177.504 1.00 125.08 ? 316  THR A CB    1 
ATOM   1928  O  OG1   . THR A 1 316 ? 123.780 150.004 176.276 1.00 129.96 ? 316  THR A OG1   1 
ATOM   1929  C  CG2   . THR A 1 316 ? 125.415 148.929 177.666 1.00 128.55 ? 316  THR A CG2   1 
ATOM   1930  N  N     . ILE A 1 317 ? 122.097 147.828 179.712 1.00 120.87 ? 317  ILE A N     1 
ATOM   1931  C  CA    . ILE A 1 317 ? 122.042 147.259 181.054 1.00 114.93 ? 317  ILE A CA    1 
ATOM   1932  C  C     . ILE A 1 317 ? 121.308 145.924 181.049 1.00 114.83 ? 317  ILE A C     1 
ATOM   1933  O  O     . ILE A 1 317 ? 121.847 144.906 181.497 1.00 121.25 ? 317  ILE A O     1 
ATOM   1934  C  CB    . ILE A 1 317 ? 121.401 148.239 182.049 1.00 114.89 ? 317  ILE A CB    1 
ATOM   1935  C  CG1   . ILE A 1 317 ? 122.325 149.422 182.316 1.00 120.75 ? 317  ILE A CG1   1 
ATOM   1936  C  CG2   . ILE A 1 317 ? 121.134 147.527 183.351 1.00 119.95 ? 317  ILE A CG2   1 
ATOM   1937  C  CD1   . ILE A 1 317 ? 121.601 150.742 182.366 1.00 125.85 ? 317  ILE A CD1   1 
ATOM   1938  N  N     . ASN A 1 318 ? 120.071 145.896 180.546 1.00 112.66 ? 318  ASN A N     1 
ATOM   1939  C  CA    . ASN A 1 318 ? 119.259 144.689 180.620 1.00 113.42 ? 318  ASN A CA    1 
ATOM   1940  C  C     . ASN A 1 318 ? 119.764 143.562 179.729 1.00 118.44 ? 318  ASN A C     1 
ATOM   1941  O  O     . ASN A 1 318 ? 119.339 142.418 179.917 1.00 119.03 ? 318  ASN A O     1 
ATOM   1942  C  CB    . ASN A 1 318 ? 117.809 145.005 180.254 1.00 109.43 ? 318  ASN A CB    1 
ATOM   1943  C  CG    . ASN A 1 318 ? 116.948 145.266 181.468 1.00 110.50 ? 318  ASN A CG    1 
ATOM   1944  O  OD1   . ASN A 1 318 ? 116.978 146.350 182.043 1.00 111.58 ? 318  ASN A OD1   1 
ATOM   1945  N  ND2   . ASN A 1 318 ? 116.175 144.267 181.869 1.00 117.65 ? 318  ASN A ND2   1 
ATOM   1946  N  N     . SER A 1 319 ? 120.655 143.839 178.778 1.00 118.12 ? 319  SER A N     1 
ATOM   1947  C  CA    . SER A 1 319 ? 121.210 142.800 177.923 1.00 116.03 ? 319  SER A CA    1 
ATOM   1948  C  C     . SER A 1 319 ? 122.623 142.409 178.333 1.00 122.83 ? 319  SER A C     1 
ATOM   1949  O  O     . SER A 1 319 ? 123.397 141.939 177.493 1.00 127.32 ? 319  SER A O     1 
ATOM   1950  C  CB    . SER A 1 319 ? 121.192 143.251 176.464 1.00 117.73 ? 319  SER A CB    1 
ATOM   1951  O  OG    . SER A 1 319 ? 121.977 142.388 175.663 1.00 122.32 ? 319  SER A OG    1 
ATOM   1952  N  N     . ALA A 1 320 ? 122.975 142.600 179.605 1.00 122.40 ? 320  ALA A N     1 
ATOM   1953  C  CA    . ALA A 1 320 ? 124.346 142.357 180.040 1.00 123.61 ? 320  ALA A CA    1 
ATOM   1954  C  C     . ALA A 1 320 ? 124.669 140.869 180.064 1.00 128.20 ? 320  ALA A C     1 
ATOM   1955  O  O     . ALA A 1 320 ? 125.531 140.399 179.313 1.00 129.98 ? 320  ALA A O     1 
ATOM   1956  C  CB    . ALA A 1 320 ? 124.574 142.979 181.416 1.00 121.76 ? 320  ALA A CB    1 
ATOM   1957  N  N     . GLY A 1 321 ? 123.985 140.110 180.913 1.00 127.25 ? 321  GLY A N     1 
ATOM   1958  C  CA    . GLY A 1 321 ? 124.326 138.715 181.102 1.00 129.34 ? 321  GLY A CA    1 
ATOM   1959  C  C     . GLY A 1 321 ? 123.451 137.750 180.333 1.00 126.17 ? 321  GLY A C     1 
ATOM   1960  O  O     . GLY A 1 321 ? 123.730 136.548 180.297 1.00 127.30 ? 321  GLY A O     1 
ATOM   1961  N  N     . ILE A 1 322 ? 122.383 138.260 179.718 1.00 126.30 ? 322  ILE A N     1 
ATOM   1962  C  CA    . ILE A 1 322 ? 121.472 137.393 178.979 1.00 122.34 ? 322  ILE A CA    1 
ATOM   1963  C  C     . ILE A 1 322 ? 122.154 136.826 177.741 1.00 117.22 ? 322  ILE A C     1 
ATOM   1964  O  O     . ILE A 1 322 ? 121.916 135.674 177.359 1.00 119.94 ? 322  ILE A O     1 
ATOM   1965  C  CB    . ILE A 1 322 ? 120.184 138.152 178.619 1.00 124.04 ? 322  ILE A CB    1 
ATOM   1966  C  CG1   . ILE A 1 322 ? 119.714 138.999 179.802 1.00 130.36 ? 322  ILE A CG1   1 
ATOM   1967  C  CG2   . ILE A 1 322 ? 119.096 137.179 178.212 1.00 119.82 ? 322  ILE A CG2   1 
ATOM   1968  C  CD1   . ILE A 1 322 ? 119.281 138.188 181.002 1.00 131.05 ? 322  ILE A CD1   1 
ATOM   1969  N  N     . GLY A 1 323 ? 123.015 137.612 177.102 1.00 114.78 ? 323  GLY A N     1 
ATOM   1970  C  CA    . GLY A 1 323 ? 123.661 137.181 175.878 1.00 114.76 ? 323  GLY A CA    1 
ATOM   1971  C  C     . GLY A 1 323 ? 122.677 137.018 174.739 1.00 118.61 ? 323  GLY A C     1 
ATOM   1972  O  O     . GLY A 1 323 ? 122.730 136.037 173.993 1.00 122.18 ? 323  GLY A O     1 
ATOM   1973  N  N     . ALA A 1 324 ? 121.775 137.984 174.601 1.00 119.48 ? 324  ALA A N     1 
ATOM   1974  C  CA    . ALA A 1 324 ? 120.704 137.892 173.621 1.00 119.14 ? 324  ALA A CA    1 
ATOM   1975  C  C     . ALA A 1 324 ? 121.247 137.961 172.199 1.00 119.41 ? 324  ALA A C     1 
ATOM   1976  O  O     . ALA A 1 324 ? 122.173 138.717 171.895 1.00 117.35 ? 324  ALA A O     1 
ATOM   1977  C  CB    . ALA A 1 324 ? 119.687 139.010 173.844 1.00 118.22 ? 324  ALA A CB    1 
ATOM   1978  N  N     . GLN A 1 325 ? 120.654 137.150 171.320 1.00 121.02 ? 325  GLN A N     1 
ATOM   1979  C  CA    . GLN A 1 325 ? 120.998 137.201 169.903 1.00 118.63 ? 325  GLN A CA    1 
ATOM   1980  C  C     . GLN A 1 325 ? 120.378 138.417 169.228 1.00 116.09 ? 325  GLN A C     1 
ATOM   1981  O  O     . GLN A 1 325 ? 120.932 138.939 168.255 1.00 117.85 ? 325  GLN A O     1 
ATOM   1982  C  CB    . GLN A 1 325 ? 120.552 135.919 169.203 1.00 123.59 ? 325  GLN A CB    1 
ATOM   1983  C  CG    . GLN A 1 325 ? 120.730 134.665 170.035 1.00 129.08 ? 325  GLN A CG    1 
ATOM   1984  C  CD    . GLN A 1 325 ? 122.116 134.070 169.899 1.00 138.99 ? 325  GLN A CD    1 
ATOM   1985  O  OE1   . GLN A 1 325 ? 122.832 134.348 168.938 1.00 146.21 ? 325  GLN A OE1   1 
ATOM   1986  N  NE2   . GLN A 1 325 ? 122.504 133.248 170.866 1.00 137.63 ? 325  GLN A NE2   1 
ATOM   1987  N  N     . CYS A 1 326 ? 119.226 138.868 169.716 1.00 113.74 ? 326  CYS A N     1 
ATOM   1988  C  CA    . CYS A 1 326 ? 118.615 140.094 169.229 1.00 113.38 ? 326  CYS A CA    1 
ATOM   1989  C  C     . CYS A 1 326 ? 117.806 140.712 170.358 1.00 112.17 ? 326  CYS A C     1 
ATOM   1990  O  O     . CYS A 1 326 ? 117.526 140.059 171.365 1.00 117.50 ? 326  CYS A O     1 
ATOM   1991  C  CB    . CYS A 1 326 ? 117.743 139.844 167.990 1.00 114.13 ? 326  CYS A CB    1 
ATOM   1992  S  SG    . CYS A 1 326 ? 116.062 139.289 168.275 1.00 121.14 ? 326  CYS A SG    1 
ATOM   1993  N  N     . HIS A 1 327 ? 117.475 141.989 170.207 1.00 105.60 ? 327  HIS A N     1 
ATOM   1994  C  CA    . HIS A 1 327 ? 116.706 142.726 171.200 1.00 103.26 ? 327  HIS A CA    1 
ATOM   1995  C  C     . HIS A 1 327 ? 115.453 143.290 170.549 1.00 105.60 ? 327  HIS A C     1 
ATOM   1996  O  O     . HIS A 1 327 ? 115.540 143.989 169.535 1.00 112.54 ? 327  HIS A O     1 
ATOM   1997  C  CB    . HIS A 1 327 ? 117.541 143.853 171.807 1.00 104.06 ? 327  HIS A CB    1 
ATOM   1998  C  CG    . HIS A 1 327 ? 119.005 143.552 171.862 1.00 107.09 ? 327  HIS A CG    1 
ATOM   1999  N  ND1   . HIS A 1 327 ? 119.609 142.996 172.967 1.00 112.89 ? 327  HIS A ND1   1 
ATOM   2000  C  CD2   . HIS A 1 327 ? 119.987 143.730 170.947 1.00 108.58 ? 327  HIS A CD2   1 
ATOM   2001  C  CE1   . HIS A 1 327 ? 120.900 142.843 172.731 1.00 112.94 ? 327  HIS A CE1   1 
ATOM   2002  N  NE2   . HIS A 1 327 ? 121.155 143.281 171.512 1.00 110.98 ? 327  HIS A NE2   1 
ATOM   2003  N  N     . LEU A 1 328 ? 114.294 142.992 171.129 1.00 100.68 ? 328  LEU A N     1 
ATOM   2004  C  CA    . LEU A 1 328 ? 113.022 143.435 170.579 1.00 98.61  ? 328  LEU A CA    1 
ATOM   2005  C  C     . LEU A 1 328 ? 112.380 144.455 171.508 1.00 98.26  ? 328  LEU A C     1 
ATOM   2006  O  O     . LEU A 1 328 ? 112.246 144.212 172.711 1.00 101.85 ? 328  LEU A O     1 
ATOM   2007  C  CB    . LEU A 1 328 ? 112.080 142.250 170.325 1.00 95.04  ? 328  LEU A CB    1 
ATOM   2008  C  CG    . LEU A 1 328 ? 111.459 141.453 171.470 1.00 97.82  ? 328  LEU A CG    1 
ATOM   2009  C  CD1   . LEU A 1 328 ? 110.048 141.930 171.748 1.00 98.50  ? 328  LEU A CD1   1 
ATOM   2010  C  CD2   . LEU A 1 328 ? 111.448 139.986 171.113 1.00 103.94 ? 328  LEU A CD2   1 
ATOM   2011  N  N     . PHE A 1 329 ? 112.001 145.598 170.945 1.00 96.37  ? 329  PHE A N     1 
ATOM   2012  C  CA    . PHE A 1 329 ? 111.264 146.636 171.646 1.00 95.62  ? 329  PHE A CA    1 
ATOM   2013  C  C     . PHE A 1 329 ? 109.852 146.721 171.084 1.00 98.70  ? 329  PHE A C     1 
ATOM   2014  O  O     . PHE A 1 329 ? 109.641 146.608 169.875 1.00 107.22 ? 329  PHE A O     1 
ATOM   2015  C  CB    . PHE A 1 329 ? 111.938 148.005 171.510 1.00 97.55  ? 329  PHE A CB    1 
ATOM   2016  C  CG    . PHE A 1 329 ? 113.407 148.016 171.839 1.00 102.66 ? 329  PHE A CG    1 
ATOM   2017  C  CD1   . PHE A 1 329 ? 114.341 147.494 170.962 1.00 101.93 ? 329  PHE A CD1   1 
ATOM   2018  C  CD2   . PHE A 1 329 ? 113.854 148.591 173.014 1.00 106.53 ? 329  PHE A CD2   1 
ATOM   2019  C  CE1   . PHE A 1 329 ? 115.686 147.521 171.263 1.00 101.35 ? 329  PHE A CE1   1 
ATOM   2020  C  CE2   . PHE A 1 329 ? 115.198 148.622 173.318 1.00 107.41 ? 329  PHE A CE2   1 
ATOM   2021  C  CZ    . PHE A 1 329 ? 116.113 148.086 172.442 1.00 106.47 ? 329  PHE A CZ    1 
ATOM   2022  N  N     . GLU A 1 330 ? 108.885 146.927 171.969 1.00 95.88  ? 330  GLU A N     1 
ATOM   2023  C  CA    . GLU A 1 330 ? 107.487 147.005 171.575 1.00 99.26  ? 330  GLU A CA    1 
ATOM   2024  C  C     . GLU A 1 330 ? 106.903 148.338 172.013 1.00 103.62 ? 330  GLU A C     1 
ATOM   2025  O  O     . GLU A 1 330 ? 107.096 148.763 173.155 1.00 112.80 ? 330  GLU A O     1 
ATOM   2026  C  CB    . GLU A 1 330 ? 106.683 145.854 172.179 1.00 102.38 ? 330  GLU A CB    1 
ATOM   2027  C  CG    . GLU A 1 330 ? 107.376 144.509 172.079 1.00 106.13 ? 330  GLU A CG    1 
ATOM   2028  C  CD    . GLU A 1 330 ? 106.572 143.391 172.706 1.00 122.15 ? 330  GLU A CD    1 
ATOM   2029  O  OE1   . GLU A 1 330 ? 105.351 143.321 172.456 1.00 124.95 ? 330  GLU A OE1   1 
ATOM   2030  O  OE2   . GLU A 1 330 ? 107.163 142.583 173.452 1.00 126.56 ? 330  GLU A OE2   1 
ATOM   2031  N  N     . HIS A 1 331 ? 106.187 148.990 171.101 1.00 103.82 ? 331  HIS A N     1 
ATOM   2032  C  CA    . HIS A 1 331 ? 105.554 150.265 171.399 1.00 103.83 ? 331  HIS A CA    1 
ATOM   2033  C  C     . HIS A 1 331 ? 104.474 150.544 170.366 1.00 112.21 ? 331  HIS A C     1 
ATOM   2034  O  O     . HIS A 1 331 ? 104.713 150.455 169.160 1.00 115.31 ? 331  HIS A O     1 
ATOM   2035  C  CB    . HIS A 1 331 ? 106.570 151.411 171.417 1.00 100.76 ? 331  HIS A CB    1 
ATOM   2036  C  CG    . HIS A 1 331 ? 106.025 152.689 171.971 1.00 103.81 ? 331  HIS A CG    1 
ATOM   2037  N  ND1   . HIS A 1 331 ? 106.590 153.917 171.704 1.00 109.94 ? 331  HIS A ND1   1 
ATOM   2038  C  CD2   . HIS A 1 331 ? 104.961 152.932 172.772 1.00 108.46 ? 331  HIS A CD2   1 
ATOM   2039  C  CE1   . HIS A 1 331 ? 105.900 154.860 172.319 1.00 111.28 ? 331  HIS A CE1   1 
ATOM   2040  N  NE2   . HIS A 1 331 ? 104.906 154.289 172.973 1.00 112.83 ? 331  HIS A NE2   1 
ATOM   2041  N  N     . THR A 1 332 ? 103.283 150.885 170.856 1.00 111.48 ? 332  THR A N     1 
ATOM   2042  C  CA    . THR A 1 332 ? 102.189 151.344 170.003 1.00 109.30 ? 332  THR A CA    1 
ATOM   2043  C  C     . THR A 1 332 ? 102.459 152.810 169.681 1.00 111.38 ? 332  THR A C     1 
ATOM   2044  O  O     . THR A 1 332 ? 101.825 153.722 170.210 1.00 117.97 ? 332  THR A O     1 
ATOM   2045  C  CB    . THR A 1 332 ? 100.845 151.148 170.694 1.00 118.38 ? 332  THR A CB    1 
ATOM   2046  O  OG1   . THR A 1 332 ? 100.746 149.803 171.175 1.00 122.96 ? 332  THR A OG1   1 
ATOM   2047  C  CG2   . THR A 1 332 ? 99.705  151.414 169.727 1.00 117.20 ? 332  THR A CG2   1 
ATOM   2048  N  N     . LEU A 1 333 ? 103.430 153.028 168.798 1.00 109.03 ? 333  LEU A N     1 
ATOM   2049  C  CA    . LEU A 1 333 ? 103.954 154.368 168.581 1.00 110.07 ? 333  LEU A CA    1 
ATOM   2050  C  C     . LEU A 1 333 ? 102.901 155.285 167.970 1.00 112.01 ? 333  LEU A C     1 
ATOM   2051  O  O     . LEU A 1 333 ? 102.103 154.882 167.121 1.00 112.63 ? 333  LEU A O     1 
ATOM   2052  C  CB    . LEU A 1 333 ? 105.206 154.320 167.701 1.00 102.28 ? 333  LEU A CB    1 
ATOM   2053  C  CG    . LEU A 1 333 ? 105.313 153.371 166.505 1.00 93.34  ? 333  LEU A CG    1 
ATOM   2054  C  CD1   . LEU A 1 333 ? 104.416 153.782 165.360 1.00 98.77  ? 333  LEU A CD1   1 
ATOM   2055  C  CD2   . LEU A 1 333 ? 106.751 153.277 166.037 1.00 94.23  ? 333  LEU A CD2   1 
ATOM   2056  N  N     . GLN A 1 334 ? 102.893 156.528 168.440 1.00 113.30 ? 334  GLN A N     1 
ATOM   2057  C  CA    . GLN A 1 334 ? 101.993 157.561 167.948 1.00 120.24 ? 334  GLN A CA    1 
ATOM   2058  C  C     . GLN A 1 334 ? 102.798 158.511 167.078 1.00 123.94 ? 334  GLN A C     1 
ATOM   2059  O  O     . GLN A 1 334 ? 103.842 159.015 167.506 1.00 127.32 ? 334  GLN A O     1 
ATOM   2060  C  CB    . GLN A 1 334 ? 101.331 158.312 169.104 1.00 123.72 ? 334  GLN A CB    1 
ATOM   2061  C  CG    . GLN A 1 334 ? 100.619 157.419 170.104 1.00 125.71 ? 334  GLN A CG    1 
ATOM   2062  C  CD    . GLN A 1 334 ? 101.495 157.056 171.283 1.00 122.59 ? 334  GLN A CD    1 
ATOM   2063  O  OE1   . GLN A 1 334 ? 102.528 157.680 171.518 1.00 122.09 ? 334  GLN A OE1   1 
ATOM   2064  N  NE2   . GLN A 1 334 ? 101.086 156.042 172.034 1.00 123.35 ? 334  GLN A NE2   1 
ATOM   2065  N  N     . LEU A 1 335 ? 102.319 158.752 165.864 1.00 123.47 ? 335  LEU A N     1 
ATOM   2066  C  CA    . LEU A 1 335 ? 103.012 159.592 164.902 1.00 124.74 ? 335  LEU A CA    1 
ATOM   2067  C  C     . LEU A 1 335 ? 102.167 160.815 164.585 1.00 133.97 ? 335  LEU A C     1 
ATOM   2068  O  O     . LEU A 1 335 ? 100.943 160.721 164.456 1.00 139.82 ? 335  LEU A O     1 
ATOM   2069  C  CB    . LEU A 1 335 ? 103.324 158.816 163.622 1.00 117.79 ? 335  LEU A CB    1 
ATOM   2070  C  CG    . LEU A 1 335 ? 104.408 157.751 163.782 1.00 109.45 ? 335  LEU A CG    1 
ATOM   2071  C  CD1   . LEU A 1 335 ? 104.731 157.102 162.453 1.00 107.37 ? 335  LEU A CD1   1 
ATOM   2072  C  CD2   . LEU A 1 335 ? 105.648 158.369 164.388 1.00 107.34 ? 335  LEU A CD2   1 
ATOM   2073  N  N     . SER A 1 336 ? 102.827 161.964 164.468 1.00 133.65 ? 336  SER A N     1 
ATOM   2074  C  CA    . SER A 1 336 ? 102.162 163.220 164.159 1.00 139.88 ? 336  SER A CA    1 
ATOM   2075  C  C     . SER A 1 336 ? 102.818 163.833 162.933 1.00 145.27 ? 336  SER A C     1 
ATOM   2076  O  O     . SER A 1 336 ? 104.048 163.924 162.865 1.00 144.05 ? 336  SER A O     1 
ATOM   2077  C  CB    . SER A 1 336 ? 102.229 164.189 165.344 1.00 143.19 ? 336  SER A CB    1 
ATOM   2078  O  OG    . SER A 1 336 ? 101.615 165.426 165.028 1.00 150.94 ? 336  SER A OG    1 
ATOM   2079  N  N     . VAL A 1 337 ? 102.000 164.242 161.967 1.00 148.17 ? 337  VAL A N     1 
ATOM   2080  C  CA    . VAL A 1 337 ? 102.469 164.913 160.761 1.00 150.20 ? 337  VAL A CA    1 
ATOM   2081  C  C     . VAL A 1 337 ? 101.705 166.222 160.627 1.00 154.32 ? 337  VAL A C     1 
ATOM   2082  O  O     . VAL A 1 337 ? 100.502 166.218 160.337 1.00 152.36 ? 337  VAL A O     1 
ATOM   2083  C  CB    . VAL A 1 337 ? 102.287 164.040 159.510 1.00 142.68 ? 337  VAL A CB    1 
ATOM   2084  C  CG1   . VAL A 1 337 ? 102.645 164.828 158.262 1.00 143.95 ? 337  VAL A CG1   1 
ATOM   2085  C  CG2   . VAL A 1 337 ? 103.142 162.791 159.613 1.00 134.63 ? 337  VAL A CG2   1 
ATOM   2086  N  N     . ASN A 1 338 ? 102.406 167.336 160.830 1.00 156.09 ? 338  ASN A N     1 
ATOM   2087  C  CA    . ASN A 1 338 ? 101.836 168.687 160.746 1.00 158.71 ? 338  ASN A CA    1 
ATOM   2088  C  C     . ASN A 1 338 ? 100.691 168.766 161.754 1.00 158.64 ? 338  ASN A C     1 
ATOM   2089  O  O     . ASN A 1 338 ? 100.867 168.332 162.904 1.00 154.31 ? 338  ASN A O     1 
ATOM   2090  C  CB    . ASN A 1 338 ? 101.464 168.984 159.299 1.00 160.72 ? 338  ASN A CB    1 
ATOM   2091  C  CG    . ASN A 1 338 ? 102.505 168.485 158.317 1.00 158.68 ? 338  ASN A CG    1 
ATOM   2092  O  OD1   . ASN A 1 338 ? 103.667 168.292 158.673 1.00 155.30 ? 338  ASN A OD1   1 
ATOM   2093  N  ND2   . ASN A 1 338 ? 102.091 168.271 157.074 1.00 155.72 ? 338  ASN A ND2   1 
ATOM   2094  N  N     . GLY A 1 339 ? 99.528  169.293 161.388 1.00 161.72 ? 339  GLY A N     1 
ATOM   2095  C  CA    . GLY A 1 339 ? 98.391  169.355 162.277 1.00 160.95 ? 339  GLY A CA    1 
ATOM   2096  C  C     . GLY A 1 339 ? 97.523  168.122 162.291 1.00 161.05 ? 339  GLY A C     1 
ATOM   2097  O  O     . GLY A 1 339 ? 96.498  168.103 162.980 1.00 161.80 ? 339  GLY A O     1 
ATOM   2098  N  N     . LYS A 1 340 ? 97.897  167.086 161.547 1.00 158.90 ? 340  LYS A N     1 
ATOM   2099  C  CA    . LYS A 1 340 ? 97.143  165.843 161.498 1.00 158.65 ? 340  LYS A CA    1 
ATOM   2100  C  C     . LYS A 1 340 ? 97.895  164.754 162.251 1.00 155.31 ? 340  LYS A C     1 
ATOM   2101  O  O     . LYS A 1 340 ? 99.072  164.497 161.983 1.00 151.89 ? 340  LYS A O     1 
ATOM   2102  C  CB    . LYS A 1 340 ? 96.898  165.409 160.052 1.00 155.56 ? 340  LYS A CB    1 
ATOM   2103  C  CG    . LYS A 1 340 ? 95.841  164.327 159.901 1.00 156.08 ? 340  LYS A CG    1 
ATOM   2104  C  CD    . LYS A 1 340 ? 94.447  164.882 160.149 1.00 155.97 ? 340  LYS A CD    1 
ATOM   2105  C  CE    . LYS A 1 340 ? 93.390  163.797 160.026 1.00 151.14 ? 340  LYS A CE    1 
ATOM   2106  N  NZ    . LYS A 1 340 ? 93.899  162.471 160.473 1.00 150.78 ? 340  LYS A NZ    1 
ATOM   2107  N  N     . CYS A 1 341 ? 97.208  164.118 163.192 1.00 150.16 ? 341  CYS A N     1 
ATOM   2108  C  CA    . CYS A 1 341 ? 97.789  163.068 164.016 1.00 141.96 ? 341  CYS A CA    1 
ATOM   2109  C  C     . CYS A 1 341 ? 97.518  161.719 163.364 1.00 139.03 ? 341  CYS A C     1 
ATOM   2110  O  O     . CYS A 1 341 ? 96.358  161.351 163.147 1.00 139.55 ? 341  CYS A O     1 
ATOM   2111  C  CB    . CYS A 1 341 ? 97.215  163.113 165.431 1.00 146.56 ? 341  CYS A CB    1 
ATOM   2112  S  SG    . CYS A 1 341 ? 95.436  163.411 165.489 1.00 167.83 ? 341  CYS A SG    1 
ATOM   2113  N  N     . LEU A 1 342 ? 98.584  160.987 163.056 1.00 136.13 ? 342  LEU A N     1 
ATOM   2114  C  CA    . LEU A 1 342 ? 98.449  159.704 162.389 1.00 128.73 ? 342  LEU A CA    1 
ATOM   2115  C  C     . LEU A 1 342 ? 97.890  158.656 163.347 1.00 128.18 ? 342  LEU A C     1 
ATOM   2116  O  O     . LEU A 1 342 ? 97.899  158.821 164.569 1.00 132.66 ? 342  LEU A O     1 
ATOM   2117  C  CB    . LEU A 1 342 ? 99.799  159.249 161.838 1.00 122.24 ? 342  LEU A CB    1 
ATOM   2118  C  CG    . LEU A 1 342 ? 100.320 160.046 160.642 1.00 128.30 ? 342  LEU A CG    1 
ATOM   2119  C  CD1   . LEU A 1 342 ? 101.556 159.395 160.049 1.00 120.75 ? 342  LEU A CD1   1 
ATOM   2120  C  CD2   . LEU A 1 342 ? 99.235  160.191 159.589 1.00 128.61 ? 342  LEU A CD2   1 
ATOM   2121  N  N     . LEU A 1 343 ? 97.392  157.567 162.771 1.00 118.98 ? 343  LEU A N     1 
ATOM   2122  C  CA    . LEU A 1 343 ? 96.851  156.485 163.573 1.00 115.51 ? 343  LEU A CA    1 
ATOM   2123  C  C     . LEU A 1 343 ? 97.976  155.765 164.315 1.00 115.50 ? 343  LEU A C     1 
ATOM   2124  O  O     . LEU A 1 343 ? 99.091  155.644 163.802 1.00 118.99 ? 343  LEU A O     1 
ATOM   2125  C  CB    . LEU A 1 343 ? 96.103  155.490 162.693 1.00 109.93 ? 343  LEU A CB    1 
ATOM   2126  C  CG    . LEU A 1 343 ? 94.585  155.616 162.590 1.00 112.85 ? 343  LEU A CG    1 
ATOM   2127  C  CD1   . LEU A 1 343 ? 93.990  154.255 162.297 1.00 111.16 ? 343  LEU A CD1   1 
ATOM   2128  C  CD2   . LEU A 1 343 ? 93.977  156.216 163.844 1.00 117.36 ? 343  LEU A CD2   1 
ATOM   2129  N  N     . PRO A 1 344 ? 97.714  155.284 165.530 1.00 108.87 ? 344  PRO A N     1 
ATOM   2130  C  CA    . PRO A 1 344 ? 98.726  154.492 166.230 1.00 105.17 ? 344  PRO A CA    1 
ATOM   2131  C  C     . PRO A 1 344 ? 99.006  153.197 165.487 1.00 105.39 ? 344  PRO A C     1 
ATOM   2132  O  O     . PRO A 1 344 ? 98.110  152.579 164.911 1.00 113.04 ? 344  PRO A O     1 
ATOM   2133  C  CB    . PRO A 1 344 ? 98.090  154.231 167.598 1.00 111.65 ? 344  PRO A CB    1 
ATOM   2134  C  CG    . PRO A 1 344 ? 96.631  154.312 167.348 1.00 114.74 ? 344  PRO A CG    1 
ATOM   2135  C  CD    . PRO A 1 344 ? 96.452  155.355 166.284 1.00 112.40 ? 344  PRO A CD    1 
ATOM   2136  N  N     . ILE A 1 345 ? 100.270 152.788 165.506 1.00 104.49 ? 345  ILE A N     1 
ATOM   2137  C  CA    . ILE A 1 345 ? 100.720 151.592 164.806 1.00 103.96 ? 345  ILE A CA    1 
ATOM   2138  C  C     . ILE A 1 345 ? 101.289 150.631 165.837 1.00 106.78 ? 345  ILE A C     1 
ATOM   2139  O  O     . ILE A 1 345 ? 102.203 150.991 166.587 1.00 111.65 ? 345  ILE A O     1 
ATOM   2140  C  CB    . ILE A 1 345 ? 101.772 151.913 163.734 1.00 97.19  ? 345  ILE A CB    1 
ATOM   2141  C  CG1   . ILE A 1 345 ? 101.336 153.115 162.899 1.00 100.08 ? 345  ILE A CG1   1 
ATOM   2142  C  CG2   . ILE A 1 345 ? 102.001 150.717 162.845 1.00 91.65  ? 345  ILE A CG2   1 
ATOM   2143  C  CD1   . ILE A 1 345 ? 102.375 153.562 161.901 1.00 102.14 ? 345  ILE A CD1   1 
ATOM   2144  N  N     . GLN A 1 346 ? 100.757 149.414 165.873 1.00 101.63 ? 346  GLN A N     1 
ATOM   2145  C  CA    . GLN A 1 346 ? 101.253 148.395 166.787 1.00 101.70 ? 346  GLN A CA    1 
ATOM   2146  C  C     . GLN A 1 346 ? 102.577 147.865 166.256 1.00 100.74 ? 346  GLN A C     1 
ATOM   2147  O  O     . GLN A 1 346 ? 102.602 147.123 165.269 1.00 104.86 ? 346  GLN A O     1 
ATOM   2148  C  CB    . GLN A 1 346 ? 100.227 147.276 166.930 1.00 98.85  ? 346  GLN A CB    1 
ATOM   2149  C  CG    . GLN A 1 346 ? 100.167 146.664 168.308 1.00 106.03 ? 346  GLN A CG    1 
ATOM   2150  C  CD    . GLN A 1 346 ? 98.884  145.899 168.536 1.00 113.54 ? 346  GLN A CD    1 
ATOM   2151  O  OE1   . GLN A 1 346 ? 98.301  145.953 169.616 1.00 119.77 ? 346  GLN A OE1   1 
ATOM   2152  N  NE2   . GLN A 1 346 ? 98.431  145.188 167.513 1.00 110.83 ? 346  GLN A NE2   1 
ATOM   2153  N  N     . THR A 1 347 ? 103.676 148.238 166.906 1.00 96.31  ? 347  THR A N     1 
ATOM   2154  C  CA    . THR A 1 347 ? 105.006 148.019 166.359 1.00 95.87  ? 347  THR A CA    1 
ATOM   2155  C  C     . THR A 1 347 ? 105.846 147.159 167.288 1.00 93.58  ? 347  THR A C     1 
ATOM   2156  O  O     . THR A 1 347 ? 105.802 147.318 168.510 1.00 98.16  ? 347  THR A O     1 
ATOM   2157  C  CB    . THR A 1 347 ? 105.724 149.346 166.111 1.00 99.54  ? 347  THR A CB    1 
ATOM   2158  O  OG1   . THR A 1 347 ? 104.790 150.304 165.601 1.00 108.49 ? 347  THR A OG1   1 
ATOM   2159  C  CG2   . THR A 1 347 ? 106.853 149.164 165.113 1.00 97.39  ? 347  THR A CG2   1 
ATOM   2160  N  N     . VAL A 1 348 ? 106.606 146.244 166.692 1.00 94.59  ? 348  VAL A N     1 
ATOM   2161  C  CA    . VAL A 1 348 ? 107.597 145.433 167.388 1.00 90.14  ? 348  VAL A CA    1 
ATOM   2162  C  C     . VAL A 1 348 ? 108.895 145.570 166.609 1.00 87.54  ? 348  VAL A C     1 
ATOM   2163  O  O     . VAL A 1 348 ? 108.935 145.286 165.406 1.00 91.10  ? 348  VAL A O     1 
ATOM   2164  C  CB    . VAL A 1 348 ? 107.175 143.963 167.493 1.00 90.51  ? 348  VAL A CB    1 
ATOM   2165  C  CG1   . VAL A 1 348 ? 108.301 143.133 168.077 1.00 91.48  ? 348  VAL A CG1   1 
ATOM   2166  C  CG2   . VAL A 1 348 ? 105.922 143.833 168.339 1.00 94.94  ? 348  VAL A CG2   1 
ATOM   2167  N  N     . PHE A 1 349 ? 109.955 146.004 167.282 1.00 91.06  ? 349  PHE A N     1 
ATOM   2168  C  CA    . PHE A 1 349 ? 111.230 146.280 166.629 1.00 91.13  ? 349  PHE A CA    1 
ATOM   2169  C  C     . PHE A 1 349 ? 112.275 145.301 167.144 1.00 91.95  ? 349  PHE A C     1 
ATOM   2170  O  O     . PHE A 1 349 ? 112.825 145.487 168.232 1.00 96.47  ? 349  PHE A O     1 
ATOM   2171  C  CB    . PHE A 1 349 ? 111.656 147.721 166.880 1.00 92.88  ? 349  PHE A CB    1 
ATOM   2172  C  CG    . PHE A 1 349 ? 113.072 148.019 166.484 1.00 95.87  ? 349  PHE A CG    1 
ATOM   2173  C  CD1   . PHE A 1 349 ? 113.441 148.044 165.152 1.00 99.81  ? 349  PHE A CD1   1 
ATOM   2174  C  CD2   . PHE A 1 349 ? 114.027 148.307 167.439 1.00 98.68  ? 349  PHE A CD2   1 
ATOM   2175  C  CE1   . PHE A 1 349 ? 114.739 148.329 164.784 1.00 97.68  ? 349  PHE A CE1   1 
ATOM   2176  C  CE2   . PHE A 1 349 ? 115.324 148.595 167.075 1.00 96.02  ? 349  PHE A CE2   1 
ATOM   2177  C  CZ    . PHE A 1 349 ? 115.680 148.605 165.746 1.00 92.27  ? 349  PHE A CZ    1 
ATOM   2178  N  N     . ALA A 1 350 ? 112.567 144.276 166.350 1.00 95.02  ? 350  ALA A N     1 
ATOM   2179  C  CA    . ALA A 1 350 ? 113.524 143.239 166.712 1.00 94.94  ? 350  ALA A CA    1 
ATOM   2180  C  C     . ALA A 1 350 ? 114.866 143.599 166.095 1.00 97.10  ? 350  ALA A C     1 
ATOM   2181  O  O     . ALA A 1 350 ? 115.054 143.465 164.883 1.00 102.43 ? 350  ALA A O     1 
ATOM   2182  C  CB    . ALA A 1 350 ? 113.052 141.866 166.242 1.00 94.97  ? 350  ALA A CB    1 
ATOM   2183  N  N     . LEU A 1 351 ? 115.794 144.054 166.928 1.00 99.06  ? 351  LEU A N     1 
ATOM   2184  C  CA    . LEU A 1 351 ? 117.114 144.488 166.492 1.00 98.67  ? 351  LEU A CA    1 
ATOM   2185  C  C     . LEU A 1 351 ? 118.102 143.360 166.747 1.00 104.60 ? 351  LEU A C     1 
ATOM   2186  O  O     . LEU A 1 351 ? 118.318 142.973 167.899 1.00 110.67 ? 351  LEU A O     1 
ATOM   2187  C  CB    . LEU A 1 351 ? 117.521 145.767 167.226 1.00 98.28  ? 351  LEU A CB    1 
ATOM   2188  C  CG    . LEU A 1 351 ? 118.843 146.478 166.937 1.00 103.07 ? 351  LEU A CG    1 
ATOM   2189  C  CD1   . LEU A 1 351 ? 118.774 147.896 167.449 1.00 109.58 ? 351  LEU A CD1   1 
ATOM   2190  C  CD2   . LEU A 1 351 ? 119.985 145.772 167.616 1.00 106.63 ? 351  LEU A CD2   1 
ATOM   2191  N  N     . LYS A 1 352 ? 118.714 142.855 165.682 1.00 105.71 ? 352  LYS A N     1 
ATOM   2192  C  CA    . LYS A 1 352 ? 119.618 141.718 165.778 1.00 110.73 ? 352  LYS A CA    1 
ATOM   2193  C  C     . LYS A 1 352 ? 121.009 142.166 166.203 1.00 118.31 ? 352  LYS A C     1 
ATOM   2194  O  O     . LYS A 1 352 ? 121.555 143.133 165.668 1.00 124.16 ? 352  LYS A O     1 
ATOM   2195  C  CB    . LYS A 1 352 ? 119.680 140.972 164.445 1.00 106.94 ? 352  LYS A CB    1 
ATOM   2196  C  CG    . LYS A 1 352 ? 118.348 140.365 164.035 1.00 104.00 ? 352  LYS A CG    1 
ATOM   2197  C  CD    . LYS A 1 352 ? 118.522 139.194 163.086 1.00 107.00 ? 352  LYS A CD    1 
ATOM   2198  C  CE    . LYS A 1 352 ? 118.737 139.662 161.658 1.00 110.14 ? 352  LYS A CE    1 
ATOM   2199  N  NZ    . LYS A 1 352 ? 120.159 139.984 161.371 1.00 114.06 ? 352  LYS A NZ    1 
ATOM   2200  N  N     . GLU A 1 353 ? 121.576 141.454 167.179 1.00 117.54 ? 353  GLU A N     1 
ATOM   2201  C  CA    . GLU A 1 353 ? 122.887 141.822 167.704 1.00 122.03 ? 353  GLU A CA    1 
ATOM   2202  C  C     . GLU A 1 353 ? 123.983 141.583 166.674 1.00 128.29 ? 353  GLU A C     1 
ATOM   2203  O  O     . GLU A 1 353 ? 124.820 142.459 166.429 1.00 134.18 ? 353  GLU A O     1 
ATOM   2204  C  CB    . GLU A 1 353 ? 123.175 141.041 168.985 1.00 125.29 ? 353  GLU A CB    1 
ATOM   2205  C  CG    . GLU A 1 353 ? 124.634 141.047 169.403 1.00 131.91 ? 353  GLU A CG    1 
ATOM   2206  C  CD    . GLU A 1 353 ? 124.979 142.226 170.288 1.00 137.49 ? 353  GLU A CD    1 
ATOM   2207  O  OE1   . GLU A 1 353 ? 124.090 142.695 171.028 1.00 135.21 ? 353  GLU A OE1   1 
ATOM   2208  O  OE2   . GLU A 1 353 ? 126.140 142.684 170.243 1.00 141.81 ? 353  GLU A OE2   1 
ATOM   2209  N  N     . ASN A 1 354 ? 123.995 140.405 166.059 1.00 125.32 ? 354  ASN A N     1 
ATOM   2210  C  CA    . ASN A 1 354 ? 125.003 140.044 165.077 1.00 126.04 ? 354  ASN A CA    1 
ATOM   2211  C  C     . ASN A 1 354 ? 124.442 140.199 163.671 1.00 126.73 ? 354  ASN A C     1 
ATOM   2212  O  O     . ASN A 1 354 ? 123.280 139.878 163.410 1.00 129.12 ? 354  ASN A O     1 
ATOM   2213  C  CB    . ASN A 1 354 ? 125.488 138.607 165.286 1.00 126.61 ? 354  ASN A CB    1 
ATOM   2214  C  CG    . ASN A 1 354 ? 126.440 138.478 166.455 1.00 136.60 ? 354  ASN A CG    1 
ATOM   2215  O  OD1   . ASN A 1 354 ? 127.528 139.053 166.450 1.00 140.10 ? 354  ASN A OD1   1 
ATOM   2216  N  ND2   . ASN A 1 354 ? 126.037 137.718 167.466 1.00 143.21 ? 354  ASN A ND2   1 
ATOM   2217  N  N     . LYS A 1 355 ? 125.282 140.693 162.767 1.00 125.41 ? 355  LYS A N     1 
ATOM   2218  C  CA    . LYS A 1 355 ? 124.855 140.902 161.393 1.00 121.27 ? 355  LYS A CA    1 
ATOM   2219  C  C     . LYS A 1 355 ? 124.538 139.574 160.721 1.00 121.77 ? 355  LYS A C     1 
ATOM   2220  O  O     . LYS A 1 355 ? 125.234 138.574 160.917 1.00 127.18 ? 355  LYS A O     1 
ATOM   2221  C  CB    . LYS A 1 355 ? 125.932 141.640 160.600 1.00 124.55 ? 355  LYS A CB    1 
ATOM   2222  C  CG    . LYS A 1 355 ? 125.517 141.968 159.176 1.00 124.70 ? 355  LYS A CG    1 
ATOM   2223  C  CD    . LYS A 1 355 ? 126.681 142.488 158.356 1.00 132.63 ? 355  LYS A CD    1 
ATOM   2224  C  CE    . LYS A 1 355 ? 126.253 142.767 156.927 1.00 127.25 ? 355  LYS A CE    1 
ATOM   2225  N  NZ    . LYS A 1 355 ? 125.645 141.564 156.295 1.00 122.19 ? 355  LYS A NZ    1 
ATOM   2226  N  N     . ALA A 1 356 ? 123.475 139.571 159.923 1.00 120.47 ? 356  ALA A N     1 
ATOM   2227  C  CA    . ALA A 1 356 ? 123.069 138.397 159.170 1.00 118.95 ? 356  ALA A CA    1 
ATOM   2228  C  C     . ALA A 1 356 ? 122.445 138.868 157.864 1.00 122.08 ? 356  ALA A C     1 
ATOM   2229  O  O     . ALA A 1 356 ? 122.612 140.019 157.454 1.00 126.75 ? 356  ALA A O     1 
ATOM   2230  C  CB    . ALA A 1 356 ? 122.111 137.525 159.984 1.00 115.95 ? 356  ALA A CB    1 
ATOM   2231  N  N     . SER A 1 357 ? 121.726 137.968 157.205 1.00 117.81 ? 357  SER A N     1 
ATOM   2232  C  CA    . SER A 1 357 ? 121.134 138.303 155.922 1.00 117.84 ? 357  SER A CA    1 
ATOM   2233  C  C     . SER A 1 357 ? 119.648 138.616 156.068 1.00 118.53 ? 357  SER A C     1 
ATOM   2234  O  O     . SER A 1 357 ? 119.029 138.377 157.110 1.00 119.60 ? 357  SER A O     1 
ATOM   2235  C  CB    . SER A 1 357 ? 121.334 137.160 154.929 1.00 121.32 ? 357  SER A CB    1 
ATOM   2236  O  OG    . SER A 1 357 ? 121.298 135.907 155.586 1.00 123.30 ? 357  SER A OG    1 
ATOM   2237  N  N     . LYS A 1 358 ? 119.078 139.172 154.995 1.00 116.15 ? 358  LYS A N     1 
ATOM   2238  C  CA    . LYS A 1 358 ? 117.634 139.365 154.944 1.00 111.08 ? 358  LYS A CA    1 
ATOM   2239  C  C     . LYS A 1 358 ? 116.902 138.042 155.105 1.00 114.06 ? 358  LYS A C     1 
ATOM   2240  O  O     . LYS A 1 358 ? 115.795 138.003 155.653 1.00 116.57 ? 358  LYS A O     1 
ATOM   2241  C  CB    . LYS A 1 358 ? 117.242 140.037 153.629 1.00 112.86 ? 358  LYS A CB    1 
ATOM   2242  C  CG    . LYS A 1 358 ? 115.750 140.252 153.448 1.00 111.62 ? 358  LYS A CG    1 
ATOM   2243  C  CD    . LYS A 1 358 ? 115.442 140.797 152.066 1.00 115.65 ? 358  LYS A CD    1 
ATOM   2244  C  CE    . LYS A 1 358 ? 113.958 141.056 151.892 1.00 116.56 ? 358  LYS A CE    1 
ATOM   2245  N  NZ    . LYS A 1 358 ? 113.648 141.620 150.550 1.00 125.13 ? 358  LYS A NZ    1 
ATOM   2246  N  N     . LEU A 1 359 ? 117.512 136.947 154.648 1.00 116.19 ? 359  LEU A N     1 
ATOM   2247  C  CA    . LEU A 1 359 ? 116.934 135.632 154.883 1.00 112.03 ? 359  LEU A CA    1 
ATOM   2248  C  C     . LEU A 1 359 ? 116.855 135.322 156.370 1.00 113.91 ? 359  LEU A C     1 
ATOM   2249  O  O     . LEU A 1 359 ? 115.854 134.771 156.833 1.00 117.39 ? 359  LEU A O     1 
ATOM   2250  C  CB    . LEU A 1 359 ? 117.747 134.563 154.157 1.00 112.68 ? 359  LEU A CB    1 
ATOM   2251  C  CG    . LEU A 1 359 ? 117.150 133.159 154.177 1.00 111.55 ? 359  LEU A CG    1 
ATOM   2252  C  CD1   . LEU A 1 359 ? 115.697 133.220 153.766 1.00 109.24 ? 359  LEU A CD1   1 
ATOM   2253  C  CD2   . LEU A 1 359 ? 117.928 132.233 153.261 1.00 125.54 ? 359  LEU A CD2   1 
ATOM   2254  N  N     . ASP A 1 360 ? 117.887 135.678 157.138 1.00 113.60 ? 360  ASP A N     1 
ATOM   2255  C  CA    . ASP A 1 360 ? 117.843 135.462 158.582 1.00 115.43 ? 360  ASP A CA    1 
ATOM   2256  C  C     . ASP A 1 360 ? 116.843 136.395 159.253 1.00 113.57 ? 360  ASP A C     1 
ATOM   2257  O  O     . ASP A 1 360 ? 116.183 136.014 160.228 1.00 113.93 ? 360  ASP A O     1 
ATOM   2258  C  CB    . ASP A 1 360 ? 119.235 135.645 159.181 1.00 120.42 ? 360  ASP A CB    1 
ATOM   2259  C  CG    . ASP A 1 360 ? 119.426 134.865 160.466 1.00 124.90 ? 360  ASP A CG    1 
ATOM   2260  O  OD1   . ASP A 1 360 ? 118.443 134.690 161.213 1.00 122.86 ? 360  ASP A OD1   1 
ATOM   2261  O  OD2   . ASP A 1 360 ? 120.564 134.423 160.729 1.00 129.75 ? 360  ASP A OD2   1 
ATOM   2262  N  N     . SER A 1 361 ? 116.732 137.629 158.758 1.00 113.66 ? 361  SER A N     1 
ATOM   2263  C  CA    . SER A 1 361 ? 115.715 138.535 159.279 1.00 111.08 ? 361  SER A CA    1 
ATOM   2264  C  C     . SER A 1 361 ? 114.322 137.952 159.087 1.00 108.36 ? 361  SER A C     1 
ATOM   2265  O  O     . SER A 1 361 ? 113.499 137.964 160.011 1.00 110.74 ? 361  SER A O     1 
ATOM   2266  C  CB    . SER A 1 361 ? 115.826 139.896 158.596 1.00 111.75 ? 361  SER A CB    1 
ATOM   2267  O  OG    . SER A 1 361 ? 117.097 140.476 158.823 1.00 112.81 ? 361  SER A OG    1 
ATOM   2268  N  N     . HIS A 1 362 ? 114.048 137.418 157.896 1.00 105.43 ? 362  HIS A N     1 
ATOM   2269  C  CA    . HIS A 1 362 ? 112.770 136.758 157.662 1.00 103.29 ? 362  HIS A CA    1 
ATOM   2270  C  C     . HIS A 1 362 ? 112.636 135.485 158.483 1.00 105.79 ? 362  HIS A C     1 
ATOM   2271  O  O     . HIS A 1 362 ? 111.527 135.134 158.885 1.00 108.95 ? 362  HIS A O     1 
ATOM   2272  C  CB    . HIS A 1 362 ? 112.589 136.448 156.180 1.00 104.54 ? 362  HIS A CB    1 
ATOM   2273  C  CG    . HIS A 1 362 ? 112.237 137.643 155.355 1.00 102.67 ? 362  HIS A CG    1 
ATOM   2274  N  ND1   . HIS A 1 362 ? 112.248 137.627 153.978 1.00 103.44 ? 362  HIS A ND1   1 
ATOM   2275  C  CD2   . HIS A 1 362 ? 111.863 138.893 155.715 1.00 100.55 ? 362  HIS A CD2   1 
ATOM   2276  C  CE1   . HIS A 1 362 ? 111.895 138.816 153.525 1.00 106.34 ? 362  HIS A CE1   1 
ATOM   2277  N  NE2   . HIS A 1 362 ? 111.659 139.603 154.558 1.00 107.27 ? 362  HIS A NE2   1 
ATOM   2278  N  N     . HIS A 1 363 ? 113.739 134.779 158.736 1.00 108.25 ? 363  HIS A N     1 
ATOM   2279  C  CA    . HIS A 1 363 ? 113.681 133.610 159.605 1.00 110.71 ? 363  HIS A CA    1 
ATOM   2280  C  C     . HIS A 1 363 ? 113.162 133.994 160.980 1.00 108.74 ? 363  HIS A C     1 
ATOM   2281  O  O     . HIS A 1 363 ? 112.167 133.438 161.462 1.00 109.12 ? 363  HIS A O     1 
ATOM   2282  C  CB    . HIS A 1 363 ? 115.065 132.970 159.712 1.00 109.50 ? 363  HIS A CB    1 
ATOM   2283  C  CG    . HIS A 1 363 ? 115.070 131.640 160.399 1.00 109.74 ? 363  HIS A CG    1 
ATOM   2284  N  ND1   . HIS A 1 363 ? 113.921 131.022 160.839 1.00 113.88 ? 363  HIS A ND1   1 
ATOM   2285  C  CD2   . HIS A 1 363 ? 116.090 130.809 160.720 1.00 111.49 ? 363  HIS A CD2   1 
ATOM   2286  C  CE1   . HIS A 1 363 ? 114.231 129.868 161.401 1.00 116.83 ? 363  HIS A CE1   1 
ATOM   2287  N  NE2   . HIS A 1 363 ? 115.541 129.715 161.341 1.00 116.86 ? 363  HIS A NE2   1 
ATOM   2288  N  N     . TRP A 1 364 ? 113.800 134.987 161.600 1.00 106.87 ? 364  TRP A N     1 
ATOM   2289  C  CA    . TRP A 1 364 ? 113.330 135.476 162.891 1.00 104.99 ? 364  TRP A CA    1 
ATOM   2290  C  C     . TRP A 1 364 ? 111.872 135.895 162.809 1.00 106.25 ? 364  TRP A C     1 
ATOM   2291  O  O     . TRP A 1 364 ? 111.019 135.359 163.528 1.00 111.83 ? 364  TRP A O     1 
ATOM   2292  C  CB    . TRP A 1 364 ? 114.194 136.647 163.354 1.00 101.99 ? 364  TRP A CB    1 
ATOM   2293  C  CG    . TRP A 1 364 ? 115.262 136.256 164.304 1.00 108.27 ? 364  TRP A CG    1 
ATOM   2294  C  CD1   . TRP A 1 364 ? 116.580 136.056 164.024 1.00 114.71 ? 364  TRP A CD1   1 
ATOM   2295  C  CD2   . TRP A 1 364 ? 115.107 136.017 165.704 1.00 110.94 ? 364  TRP A CD2   1 
ATOM   2296  N  NE1   . TRP A 1 364 ? 117.256 135.703 165.165 1.00 115.92 ? 364  TRP A NE1   1 
ATOM   2297  C  CE2   . TRP A 1 364 ? 116.372 135.673 166.211 1.00 115.99 ? 364  TRP A CE2   1 
ATOM   2298  C  CE3   . TRP A 1 364 ? 114.018 136.058 166.578 1.00 111.94 ? 364  TRP A CE3   1 
ATOM   2299  C  CZ2   . TRP A 1 364 ? 116.579 135.374 167.552 1.00 119.97 ? 364  TRP A CZ2   1 
ATOM   2300  C  CZ3   . TRP A 1 364 ? 114.225 135.761 167.906 1.00 118.11 ? 364  TRP A CZ3   1 
ATOM   2301  C  CH2   . TRP A 1 364 ? 115.494 135.424 168.382 1.00 122.48 ? 364  TRP A CH2   1 
ATOM   2302  N  N     . TYR A 1 365 ? 111.560 136.788 161.868 1.00 102.76 ? 365  TYR A N     1 
ATOM   2303  C  CA    . TYR A 1 365 ? 110.215 137.336 161.751 1.00 100.10 ? 365  TYR A CA    1 
ATOM   2304  C  C     . TYR A 1 365 ? 109.182 136.229 161.614 1.00 99.93  ? 365  TYR A C     1 
ATOM   2305  O  O     . TYR A 1 365 ? 108.384 135.989 162.530 1.00 105.66 ? 365  TYR A O     1 
ATOM   2306  C  CB    . TYR A 1 365 ? 110.166 138.281 160.552 1.00 100.40 ? 365  TYR A CB    1 
ATOM   2307  C  CG    . TYR A 1 365 ? 108.783 138.588 160.045 1.00 97.75  ? 365  TYR A CG    1 
ATOM   2308  C  CD1   . TYR A 1 365 ? 107.883 139.292 160.820 1.00 98.82  ? 365  TYR A CD1   1 
ATOM   2309  C  CD2   . TYR A 1 365 ? 108.381 138.177 158.784 1.00 96.62  ? 365  TYR A CD2   1 
ATOM   2310  C  CE1   . TYR A 1 365 ? 106.627 139.579 160.358 1.00 94.06  ? 365  TYR A CE1   1 
ATOM   2311  C  CE2   . TYR A 1 365 ? 107.121 138.457 158.314 1.00 94.38  ? 365  TYR A CE2   1 
ATOM   2312  C  CZ    . TYR A 1 365 ? 106.248 139.158 159.108 1.00 91.81  ? 365  TYR A CZ    1 
ATOM   2313  O  OH    . TYR A 1 365 ? 104.988 139.449 158.651 1.00 92.32  ? 365  TYR A OH    1 
ATOM   2314  N  N     . PHE A 1 366 ? 109.237 135.492 160.504 1.00 99.09  ? 366  PHE A N     1 
ATOM   2315  C  CA    . PHE A 1 366 ? 108.285 134.433 160.215 1.00 102.74 ? 366  PHE A CA    1 
ATOM   2316  C  C     . PHE A 1 366 ? 108.229 133.451 161.369 1.00 109.00 ? 366  PHE A C     1 
ATOM   2317  O  O     . PHE A 1 366 ? 107.235 133.439 162.098 1.00 114.52 ? 366  PHE A O     1 
ATOM   2318  C  CB    . PHE A 1 366 ? 108.664 133.702 158.928 1.00 99.66  ? 366  PHE A CB    1 
ATOM   2319  C  CG    . PHE A 1 366 ? 108.121 134.337 157.686 1.00 99.27  ? 366  PHE A CG    1 
ATOM   2320  C  CD1   . PHE A 1 366 ? 106.771 134.278 157.399 1.00 99.89  ? 366  PHE A CD1   1 
ATOM   2321  C  CD2   . PHE A 1 366 ? 108.960 134.990 156.803 1.00 103.00 ? 366  PHE A CD2   1 
ATOM   2322  C  CE1   . PHE A 1 366 ? 106.270 134.858 156.256 1.00 99.78  ? 366  PHE A CE1   1 
ATOM   2323  C  CE2   . PHE A 1 366 ? 108.462 135.573 155.660 1.00 104.34 ? 366  PHE A CE2   1 
ATOM   2324  C  CZ    . PHE A 1 366 ? 107.116 135.508 155.386 1.00 102.08 ? 366  PHE A CZ    1 
ATOM   2325  N  N     . ASN A 1 367 ? 109.313 132.708 161.611 1.00 107.09 ? 367  ASN A N     1 
ATOM   2326  C  CA    . ASN A 1 367 ? 109.243 131.629 162.584 1.00 107.98 ? 367  ASN A CA    1 
ATOM   2327  C  C     . ASN A 1 367 ? 108.757 132.156 163.926 1.00 112.67 ? 367  ASN A C     1 
ATOM   2328  O  O     . ASN A 1 367 ? 107.624 131.861 164.317 1.00 119.71 ? 367  ASN A O     1 
ATOM   2329  C  CB    . ASN A 1 367 ? 110.602 130.946 162.723 1.00 107.79 ? 367  ASN A CB    1 
ATOM   2330  C  CG    . ASN A 1 367 ? 110.811 129.860 161.689 1.00 108.73 ? 367  ASN A CG    1 
ATOM   2331  O  OD1   . ASN A 1 367 ? 111.250 130.128 160.573 1.00 109.73 ? 367  ASN A OD1   1 
ATOM   2332  N  ND2   . ASN A 1 367 ? 110.491 128.626 162.054 1.00 110.21 ? 367  ASN A ND2   1 
ATOM   2333  N  N     . ALA A 1 368 ? 109.536 133.018 164.585 1.00 106.60 ? 368  ALA A N     1 
ATOM   2334  C  CA    . ALA A 1 368 ? 109.178 133.428 165.936 1.00 105.45 ? 368  ALA A CA    1 
ATOM   2335  C  C     . ALA A 1 368 ? 107.812 134.105 165.968 1.00 110.43 ? 368  ALA A C     1 
ATOM   2336  O  O     . ALA A 1 368 ? 106.851 133.571 166.541 1.00 116.78 ? 368  ALA A O     1 
ATOM   2337  C  CB    . ALA A 1 368 ? 110.255 134.358 166.495 1.00 105.26 ? 368  ALA A CB    1 
ATOM   2338  N  N     . PHE A 1 369 ? 107.694 135.274 165.333 1.00 106.86 ? 369  PHE A N     1 
ATOM   2339  C  CA    . PHE A 1 369 ? 106.511 136.086 165.569 1.00 106.72 ? 369  PHE A CA    1 
ATOM   2340  C  C     . PHE A 1 369 ? 105.267 135.474 164.934 1.00 108.67 ? 369  PHE A C     1 
ATOM   2341  O  O     . PHE A 1 369 ? 104.193 135.485 165.549 1.00 111.92 ? 369  PHE A O     1 
ATOM   2342  C  CB    . PHE A 1 369 ? 106.751 137.505 165.056 1.00 107.21 ? 369  PHE A CB    1 
ATOM   2343  C  CG    . PHE A 1 369 ? 108.044 138.108 165.537 1.00 107.13 ? 369  PHE A CG    1 
ATOM   2344  C  CD1   . PHE A 1 369 ? 108.523 137.833 166.804 1.00 105.72 ? 369  PHE A CD1   1 
ATOM   2345  C  CD2   . PHE A 1 369 ? 108.784 138.938 164.717 1.00 104.98 ? 369  PHE A CD2   1 
ATOM   2346  C  CE1   . PHE A 1 369 ? 109.711 138.380 167.244 1.00 106.87 ? 369  PHE A CE1   1 
ATOM   2347  C  CE2   . PHE A 1 369 ? 109.973 139.488 165.155 1.00 99.71  ? 369  PHE A CE2   1 
ATOM   2348  C  CZ    . PHE A 1 369 ? 110.436 139.207 166.419 1.00 101.96 ? 369  PHE A CZ    1 
ATOM   2349  N  N     . ALA A 1 370 ? 105.370 134.966 163.701 1.00 105.12 ? 370  ALA A N     1 
ATOM   2350  C  CA    . ALA A 1 370 ? 104.213 134.345 163.078 1.00 109.73 ? 370  ALA A CA    1 
ATOM   2351  C  C     . ALA A 1 370 ? 103.774 133.102 163.839 1.00 115.34 ? 370  ALA A C     1 
ATOM   2352  O  O     . ALA A 1 370 ? 102.580 132.930 164.103 1.00 120.26 ? 370  ALA A O     1 
ATOM   2353  C  CB    . ALA A 1 370 ? 104.525 134.008 161.623 1.00 107.38 ? 370  ALA A CB    1 
ATOM   2354  N  N     . GLU A 1 371 ? 104.714 132.227 164.223 1.00 114.13 ? 371  GLU A N     1 
ATOM   2355  C  CA    . GLU A 1 371 ? 104.330 131.035 164.965 1.00 116.32 ? 371  GLU A CA    1 
ATOM   2356  C  C     . GLU A 1 371 ? 103.722 131.401 166.310 1.00 118.56 ? 371  GLU A C     1 
ATOM   2357  O  O     . GLU A 1 371 ? 102.948 130.625 166.880 1.00 126.34 ? 371  GLU A O     1 
ATOM   2358  C  CB    . GLU A 1 371 ? 105.544 130.126 165.154 1.00 116.15 ? 371  GLU A CB    1 
ATOM   2359  C  CG    . GLU A 1 371 ? 105.815 129.200 163.982 1.00 122.78 ? 371  GLU A CG    1 
ATOM   2360  C  CD    . GLU A 1 371 ? 104.826 128.058 163.898 1.00 133.14 ? 371  GLU A CD    1 
ATOM   2361  O  OE1   . GLU A 1 371 ? 104.120 127.803 164.896 1.00 137.50 ? 371  GLU A OE1   1 
ATOM   2362  O  OE2   . GLU A 1 371 ? 104.753 127.413 162.831 1.00 137.52 ? 371  GLU A OE2   1 
ATOM   2363  N  N     . GLN A 1 372 ? 104.057 132.580 166.838 1.00 113.21 ? 372  GLN A N     1 
ATOM   2364  C  CA    . GLN A 1 372 ? 103.434 133.001 168.087 1.00 113.15 ? 372  GLN A CA    1 
ATOM   2365  C  C     . GLN A 1 372 ? 102.013 133.505 167.869 1.00 116.38 ? 372  GLN A C     1 
ATOM   2366  O  O     . GLN A 1 372 ? 101.049 132.898 168.348 1.00 124.24 ? 372  GLN A O     1 
ATOM   2367  C  CB    . GLN A 1 372 ? 104.273 134.076 168.770 1.00 110.50 ? 372  GLN A CB    1 
ATOM   2368  C  CG    . GLN A 1 372 ? 103.812 134.335 170.183 1.00 110.68 ? 372  GLN A CG    1 
ATOM   2369  C  CD    . GLN A 1 372 ? 104.947 134.624 171.119 1.00 120.03 ? 372  GLN A CD    1 
ATOM   2370  O  OE1   . GLN A 1 372 ? 106.093 134.287 170.844 1.00 118.34 ? 372  GLN A OE1   1 
ATOM   2371  N  NE2   . GLN A 1 372 ? 104.636 135.251 172.242 1.00 127.18 ? 372  GLN A NE2   1 
ATOM   2372  N  N     . ILE A 1 373 ? 101.855 134.614 167.143 1.00 111.87 ? 373  ILE A N     1 
ATOM   2373  C  CA    . ILE A 1 373 ? 100.555 135.288 167.164 1.00 112.14 ? 373  ILE A CA    1 
ATOM   2374  C  C     . ILE A 1 373 ? 99.587  134.644 166.181 1.00 115.20 ? 373  ILE A C     1 
ATOM   2375  O  O     . ILE A 1 373 ? 98.372  134.866 166.260 1.00 118.46 ? 373  ILE A O     1 
ATOM   2376  C  CB    . ILE A 1 373 ? 100.691 136.802 166.916 1.00 106.62 ? 373  ILE A CB    1 
ATOM   2377  C  CG1   . ILE A 1 373 ? 101.734 137.112 165.855 1.00 106.75 ? 373  ILE A CG1   1 
ATOM   2378  C  CG2   . ILE A 1 373 ? 101.037 137.524 168.204 1.00 109.81 ? 373  ILE A CG2   1 
ATOM   2379  C  CD1   . ILE A 1 373 ? 101.971 138.589 165.678 1.00 101.32 ? 373  ILE A CD1   1 
ATOM   2380  N  N     . GLN A 1 374 ? 100.097 133.838 165.245 1.00 113.09 ? 374  GLN A N     1 
ATOM   2381  C  CA    . GLN A 1 374 ? 99.281  133.090 164.294 1.00 113.18 ? 374  GLN A CA    1 
ATOM   2382  C  C     . GLN A 1 374 ? 98.372  134.025 163.507 1.00 109.20 ? 374  GLN A C     1 
ATOM   2383  O  O     . GLN A 1 374 ? 97.159  134.058 163.744 1.00 109.90 ? 374  GLN A O     1 
ATOM   2384  C  CB    . GLN A 1 374 ? 98.457  132.020 165.013 1.00 120.27 ? 374  GLN A CB    1 
ATOM   2385  C  CG    . GLN A 1 374 ? 98.250  130.755 164.203 1.00 121.77 ? 374  GLN A CG    1 
ATOM   2386  C  CD    . GLN A 1 374 ? 99.514  129.927 164.073 1.00 124.10 ? 374  GLN A CD    1 
ATOM   2387  O  OE1   . GLN A 1 374 ? 99.624  129.078 163.190 1.00 128.93 ? 374  GLN A OE1   1 
ATOM   2388  N  NE2   . GLN A 1 374 ? 100.470 130.160 164.963 1.00 122.15 ? 374  GLN A NE2   1 
ATOM   2389  N  N     . PRO A 1 375 ? 98.914  134.795 162.576 1.00 105.93 ? 375  PRO A N     1 
ATOM   2390  C  CA    . PRO A 1 375 ? 98.103  135.747 161.820 1.00 105.95 ? 375  PRO A CA    1 
ATOM   2391  C  C     . PRO A 1 375 ? 97.266  135.028 160.769 1.00 109.08 ? 375  PRO A C     1 
ATOM   2392  O  O     . PRO A 1 375 ? 97.350  133.816 160.589 1.00 116.12 ? 375  PRO A O     1 
ATOM   2393  C  CB    . PRO A 1 375 ? 99.154  136.644 161.175 1.00 101.76 ? 375  PRO A CB    1 
ATOM   2394  C  CG    . PRO A 1 375 ? 100.286 135.720 160.927 1.00 106.00 ? 375  PRO A CG    1 
ATOM   2395  C  CD    . PRO A 1 375 ? 100.297 134.743 162.076 1.00 107.20 ? 375  PRO A CD    1 
ATOM   2396  N  N     . GLU A 1 376 ? 96.447  135.808 160.069 1.00 104.75 ? 376  GLU A N     1 
ATOM   2397  C  CA    . GLU A 1 376 ? 95.672  135.309 158.942 1.00 100.04 ? 376  GLU A CA    1 
ATOM   2398  C  C     . GLU A 1 376 ? 96.343  135.628 157.614 1.00 100.23 ? 376  GLU A C     1 
ATOM   2399  O  O     . GLU A 1 376 ? 96.354  134.792 156.708 1.00 110.88 ? 376  GLU A O     1 
ATOM   2400  C  CB    . GLU A 1 376 ? 94.254  135.890 158.978 1.00 105.61 ? 376  GLU A CB    1 
ATOM   2401  C  CG    . GLU A 1 376 ? 93.328  135.339 157.911 1.00 112.54 ? 376  GLU A CG    1 
ATOM   2402  C  CD    . GLU A 1 376 ? 91.903  135.832 158.068 1.00 122.86 ? 376  GLU A CD    1 
ATOM   2403  O  OE1   . GLU A 1 376 ? 91.612  136.496 159.085 1.00 123.82 ? 376  GLU A OE1   1 
ATOM   2404  O  OE2   . GLU A 1 376 ? 91.074  135.556 157.176 1.00 121.66 ? 376  GLU A OE2   1 
ATOM   2405  N  N     . TYR A 1 377 ? 96.908  136.825 157.485 1.00 96.07  ? 377  TYR A N     1 
ATOM   2406  C  CA    . TYR A 1 377 ? 97.731  137.196 156.346 1.00 91.26  ? 377  TYR A CA    1 
ATOM   2407  C  C     . TYR A 1 377 ? 99.045  137.780 156.840 1.00 88.35  ? 377  TYR A C     1 
ATOM   2408  O  O     . TYR A 1 377 ? 99.089  138.487 157.849 1.00 96.37  ? 377  TYR A O     1 
ATOM   2409  C  CB    . TYR A 1 377 ? 97.023  138.204 155.435 1.00 87.86  ? 377  TYR A CB    1 
ATOM   2410  C  CG    . TYR A 1 377 ? 95.537  137.985 155.331 1.00 93.05  ? 377  TYR A CG    1 
ATOM   2411  C  CD1   . TYR A 1 377 ? 95.020  137.039 154.463 1.00 95.65  ? 377  TYR A CD1   1 
ATOM   2412  C  CD2   . TYR A 1 377 ? 94.651  138.715 156.105 1.00 103.35 ? 377  TYR A CD2   1 
ATOM   2413  C  CE1   . TYR A 1 377 ? 93.666  136.827 154.364 1.00 104.63 ? 377  TYR A CE1   1 
ATOM   2414  C  CE2   . TYR A 1 377 ? 93.291  138.510 156.013 1.00 107.64 ? 377  TYR A CE2   1 
ATOM   2415  C  CZ    . TYR A 1 377 ? 92.806  137.564 155.140 1.00 108.67 ? 377  TYR A CZ    1 
ATOM   2416  O  OH    . TYR A 1 377 ? 91.453  137.350 155.041 1.00 113.26 ? 377  TYR A OH    1 
ATOM   2417  N  N     . THR A 1 378 ? 100.118 137.482 156.115 1.00 84.85  ? 378  THR A N     1 
ATOM   2418  C  CA    . THR A 1 378 ? 101.457 137.934 156.477 1.00 81.78  ? 378  THR A CA    1 
ATOM   2419  C  C     . THR A 1 378 ? 102.031 138.698 155.295 1.00 86.31  ? 378  THR A C     1 
ATOM   2420  O  O     . THR A 1 378 ? 102.167 138.140 154.202 1.00 94.40  ? 378  THR A O     1 
ATOM   2421  C  CB    . THR A 1 378 ? 102.356 136.760 156.853 1.00 84.38  ? 378  THR A CB    1 
ATOM   2422  O  OG1   . THR A 1 378 ? 101.985 136.265 158.144 1.00 94.69  ? 378  THR A OG1   1 
ATOM   2423  C  CG2   . THR A 1 378 ? 103.802 137.189 156.875 1.00 81.30  ? 378  THR A CG2   1 
ATOM   2424  N  N     . ALA A 1 379 ? 102.368 139.963 155.512 1.00 85.74  ? 379  ALA A N     1 
ATOM   2425  C  CA    . ALA A 1 379 ? 102.887 140.830 154.466 1.00 82.69  ? 379  ALA A CA    1 
ATOM   2426  C  C     . ALA A 1 379 ? 104.349 141.144 154.736 1.00 83.87  ? 379  ALA A C     1 
ATOM   2427  O  O     . ALA A 1 379 ? 104.757 141.297 155.890 1.00 91.82  ? 379  ALA A O     1 
ATOM   2428  C  CB    . ALA A 1 379 ? 102.082 142.127 154.376 1.00 81.88  ? 379  ALA A CB    1 
ATOM   2429  N  N     . VAL A 1 380 ? 105.134 141.234 153.669 1.00 83.36  ? 380  VAL A N     1 
ATOM   2430  C  CA    . VAL A 1 380 ? 106.560 141.514 153.761 1.00 83.21  ? 380  VAL A CA    1 
ATOM   2431  C  C     . VAL A 1 380 ? 106.889 142.677 152.841 1.00 90.69  ? 380  VAL A C     1 
ATOM   2432  O  O     . VAL A 1 380 ? 106.555 142.645 151.652 1.00 98.24  ? 380  VAL A O     1 
ATOM   2433  C  CB    . VAL A 1 380 ? 107.409 140.286 153.388 1.00 86.88  ? 380  VAL A CB    1 
ATOM   2434  C  CG1   . VAL A 1 380 ? 108.873 140.657 153.380 1.00 89.45  ? 380  VAL A CG1   1 
ATOM   2435  C  CG2   . VAL A 1 380 ? 107.152 139.149 154.355 1.00 89.86  ? 380  VAL A CG2   1 
ATOM   2436  N  N     . MET A 1 381 ? 107.553 143.692 153.385 1.00 92.56  ? 381  MET A N     1 
ATOM   2437  C  CA    . MET A 1 381 ? 108.063 144.786 152.575 1.00 96.84  ? 381  MET A CA    1 
ATOM   2438  C  C     . MET A 1 381 ? 109.468 145.130 153.037 1.00 101.90 ? 381  MET A C     1 
ATOM   2439  O  O     . MET A 1 381 ? 109.854 144.863 154.177 1.00 107.52 ? 381  MET A O     1 
ATOM   2440  C  CB    . MET A 1 381 ? 107.173 146.033 152.641 1.00 91.39  ? 381  MET A CB    1 
ATOM   2441  C  CG    . MET A 1 381 ? 107.430 146.918 153.846 1.00 92.13  ? 381  MET A CG    1 
ATOM   2442  S  SD    . MET A 1 381 ? 106.152 148.160 154.101 1.00 102.79 ? 381  MET A SD    1 
ATOM   2443  C  CE    . MET A 1 381 ? 104.676 147.180 153.910 1.00 97.56  ? 381  MET A CE    1 
ATOM   2444  N  N     . ASP A 1 382 ? 110.238 145.710 152.126 1.00 104.06 ? 382  ASP A N     1 
ATOM   2445  C  CA    . ASP A 1 382 ? 111.529 146.274 152.473 1.00 105.99 ? 382  ASP A CA    1 
ATOM   2446  C  C     . ASP A 1 382 ? 111.300 147.664 153.055 1.00 108.14 ? 382  ASP A C     1 
ATOM   2447  O  O     . ASP A 1 382 ? 110.182 148.182 153.055 1.00 112.01 ? 382  ASP A O     1 
ATOM   2448  C  CB    . ASP A 1 382 ? 112.443 146.307 151.252 1.00 111.85 ? 382  ASP A CB    1 
ATOM   2449  C  CG    . ASP A 1 382 ? 112.910 144.930 150.840 1.00 123.73 ? 382  ASP A CG    1 
ATOM   2450  O  OD1   . ASP A 1 382 ? 112.408 143.939 151.410 1.00 129.76 ? 382  ASP A OD1   1 
ATOM   2451  O  OD2   . ASP A 1 382 ? 113.776 144.837 149.947 1.00 127.73 ? 382  ASP A OD2   1 
ATOM   2452  N  N     . VAL A 1 383 ? 112.357 148.296 153.543 1.00 108.00 ? 383  VAL A N     1 
ATOM   2453  C  CA    . VAL A 1 383 ? 112.272 149.642 154.090 1.00 107.99 ? 383  VAL A CA    1 
ATOM   2454  C  C     . VAL A 1 383 ? 112.399 150.625 152.937 1.00 114.64 ? 383  VAL A C     1 
ATOM   2455  O  O     . VAL A 1 383 ? 113.083 150.347 151.944 1.00 119.30 ? 383  VAL A O     1 
ATOM   2456  C  CB    . VAL A 1 383 ? 113.349 149.881 155.161 1.00 105.44 ? 383  VAL A CB    1 
ATOM   2457  C  CG1   . VAL A 1 383 ? 114.663 150.240 154.521 1.00 108.85 ? 383  VAL A CG1   1 
ATOM   2458  C  CG2   . VAL A 1 383 ? 112.909 150.975 156.115 1.00 108.03 ? 383  VAL A CG2   1 
ATOM   2459  N  N     . GLY A 1 384 ? 111.696 151.746 153.036 1.00 112.03 ? 384  GLY A N     1 
ATOM   2460  C  CA    . GLY A 1 384 ? 111.708 152.744 151.993 1.00 109.86 ? 384  GLY A CA    1 
ATOM   2461  C  C     . GLY A 1 384 ? 110.601 152.603 150.974 1.00 105.73 ? 384  GLY A C     1 
ATOM   2462  O  O     . GLY A 1 384 ? 110.499 153.448 150.079 1.00 110.22 ? 384  GLY A O     1 
ATOM   2463  N  N     . THR A 1 385 ? 109.785 151.557 151.068 1.00 100.60 ? 385  THR A N     1 
ATOM   2464  C  CA    . THR A 1 385 ? 108.684 151.365 150.131 1.00 103.16 ? 385  THR A CA    1 
ATOM   2465  C  C     . THR A 1 385 ? 107.458 152.117 150.633 1.00 102.96 ? 385  THR A C     1 
ATOM   2466  O  O     . THR A 1 385 ? 106.861 151.740 151.645 1.00 104.76 ? 385  THR A O     1 
ATOM   2467  C  CB    . THR A 1 385 ? 108.377 149.880 149.967 1.00 101.80 ? 385  THR A CB    1 
ATOM   2468  O  OG1   . THR A 1 385 ? 108.208 149.282 151.256 1.00 105.92 ? 385  THR A OG1   1 
ATOM   2469  C  CG2   . THR A 1 385 ? 109.510 149.182 149.240 1.00 102.75 ? 385  THR A CG2   1 
ATOM   2470  N  N     . MET A 1 386 ? 107.078 153.175 149.927 1.00 101.67 ? 386  MET A N     1 
ATOM   2471  C  CA    . MET A 1 386 ? 105.900 153.965 150.264 1.00 100.62 ? 386  MET A CA    1 
ATOM   2472  C  C     . MET A 1 386 ? 104.693 153.345 149.572 1.00 103.94 ? 386  MET A C     1 
ATOM   2473  O  O     . MET A 1 386 ? 104.710 153.132 148.356 1.00 109.38 ? 386  MET A O     1 
ATOM   2474  C  CB    . MET A 1 386 ? 106.079 155.422 149.844 1.00 105.65 ? 386  MET A CB    1 
ATOM   2475  C  CG    . MET A 1 386 ? 107.113 156.189 150.643 1.00 111.01 ? 386  MET A CG    1 
ATOM   2476  S  SD    . MET A 1 386 ? 108.777 155.991 149.989 1.00 113.82 ? 386  MET A SD    1 
ATOM   2477  C  CE    . MET A 1 386 ? 108.825 157.316 148.788 1.00 111.76 ? 386  MET A CE    1 
ATOM   2478  N  N     . LEU A 1 387 ? 103.649 153.060 150.341 1.00 103.13 ? 387  LEU A N     1 
ATOM   2479  C  CA    . LEU A 1 387 ? 102.422 152.509 149.788 1.00 101.33 ? 387  LEU A CA    1 
ATOM   2480  C  C     . LEU A 1 387 ? 101.366 153.599 149.665 1.00 104.75 ? 387  LEU A C     1 
ATOM   2481  O  O     . LEU A 1 387 ? 101.277 154.500 150.500 1.00 111.44 ? 387  LEU A O     1 
ATOM   2482  C  CB    . LEU A 1 387 ? 101.884 151.377 150.665 1.00 93.28  ? 387  LEU A CB    1 
ATOM   2483  C  CG    . LEU A 1 387 ? 102.877 150.442 151.354 1.00 93.20  ? 387  LEU A CG    1 
ATOM   2484  C  CD1   . LEU A 1 387 ? 102.132 149.376 152.131 1.00 97.23  ? 387  LEU A CD1   1 
ATOM   2485  C  CD2   . LEU A 1 387 ? 103.806 149.804 150.350 1.00 96.54  ? 387  LEU A CD2   1 
ATOM   2486  N  N     . THR A 1 388 ? 100.549 153.502 148.622 1.00 99.02  ? 388  THR A N     1 
ATOM   2487  C  CA    . THR A 1 388 ? 99.449  154.439 148.472 1.00 104.36 ? 388  THR A CA    1 
ATOM   2488  C  C     . THR A 1 388 ? 98.410  154.195 149.564 1.00 108.22 ? 388  THR A C     1 
ATOM   2489  O  O     . THR A 1 388 ? 98.527  153.277 150.379 1.00 110.01 ? 388  THR A O     1 
ATOM   2490  C  CB    . THR A 1 388 ? 98.830  154.319 147.083 1.00 107.90 ? 388  THR A CB    1 
ATOM   2491  O  OG1   . THR A 1 388 ? 98.838  152.946 146.675 1.00 107.07 ? 388  THR A OG1   1 
ATOM   2492  C  CG2   . THR A 1 388 ? 99.612  155.150 146.082 1.00 110.12 ? 388  THR A CG2   1 
ATOM   2493  N  N     . LYS A 1 389 ? 97.372  155.031 149.586 1.00 112.00 ? 389  LYS A N     1 
ATOM   2494  C  CA    . LYS A 1 389 ? 96.340  154.895 150.605 1.00 113.74 ? 389  LYS A CA    1 
ATOM   2495  C  C     . LYS A 1 389 ? 95.584  153.577 150.513 1.00 116.43 ? 389  LYS A C     1 
ATOM   2496  O  O     . LYS A 1 389 ? 94.990  153.157 151.510 1.00 118.00 ? 389  LYS A O     1 
ATOM   2497  C  CB    . LYS A 1 389 ? 95.341  156.048 150.509 1.00 112.87 ? 389  LYS A CB    1 
ATOM   2498  C  CG    . LYS A 1 389 ? 95.866  157.386 150.996 1.00 114.58 ? 389  LYS A CG    1 
ATOM   2499  C  CD    . LYS A 1 389 ? 94.755  158.431 151.076 1.00 120.21 ? 389  LYS A CD    1 
ATOM   2500  C  CE    . LYS A 1 389 ? 93.793  158.371 149.892 1.00 119.81 ? 389  LYS A CE    1 
ATOM   2501  N  NZ    . LYS A 1 389 ? 94.480  158.378 148.569 1.00 115.16 ? 389  LYS A NZ    1 
ATOM   2502  N  N     . SER A 1 390 ? 95.592  152.916 149.357 1.00 110.57 ? 390  SER A N     1 
ATOM   2503  C  CA    . SER A 1 390 ? 94.736  151.758 149.134 1.00 109.22 ? 390  SER A CA    1 
ATOM   2504  C  C     . SER A 1 390 ? 95.509  150.479 148.840 1.00 111.48 ? 390  SER A C     1 
ATOM   2505  O  O     . SER A 1 390 ? 94.912  149.516 148.347 1.00 119.28 ? 390  SER A O     1 
ATOM   2506  C  CB    . SER A 1 390 ? 93.757  152.044 147.994 1.00 112.31 ? 390  SER A CB    1 
ATOM   2507  O  OG    . SER A 1 390 ? 92.935  153.158 148.296 1.00 117.58 ? 390  SER A OG    1 
ATOM   2508  N  N     . ALA A 1 391 ? 96.811  150.434 149.125 1.00 105.64 ? 391  ALA A N     1 
ATOM   2509  C  CA    . ALA A 1 391 ? 97.570  149.211 148.880 1.00 107.40 ? 391  ALA A CA    1 
ATOM   2510  C  C     . ALA A 1 391 ? 97.082  148.072 149.767 1.00 106.97 ? 391  ALA A C     1 
ATOM   2511  O  O     . ALA A 1 391 ? 96.763  146.978 149.278 1.00 110.44 ? 391  ALA A O     1 
ATOM   2512  C  CB    . ALA A 1 391 ? 99.059  149.464 149.103 1.00 106.00 ? 391  ALA A CB    1 
ATOM   2513  N  N     . LEU A 1 392 ? 97.011  148.313 151.078 1.00 101.80 ? 392  LEU A N     1 
ATOM   2514  C  CA    . LEU A 1 392 ? 96.533  147.280 151.989 1.00 101.27 ? 392  LEU A CA    1 
ATOM   2515  C  C     . LEU A 1 392 ? 95.076  146.943 151.717 1.00 104.11 ? 392  LEU A C     1 
ATOM   2516  O  O     . LEU A 1 392 ? 94.682  145.774 151.785 1.00 106.61 ? 392  LEU A O     1 
ATOM   2517  C  CB    . LEU A 1 392 ? 96.721  147.724 153.439 1.00 100.21 ? 392  LEU A CB    1 
ATOM   2518  C  CG    . LEU A 1 392 ? 98.145  147.677 153.994 1.00 95.49  ? 392  LEU A CG    1 
ATOM   2519  C  CD1   . LEU A 1 392 ? 98.120  147.599 155.508 1.00 91.28  ? 392  LEU A CD1   1 
ATOM   2520  C  CD2   . LEU A 1 392 ? 98.899  146.496 153.419 1.00 96.17  ? 392  LEU A CD2   1 
ATOM   2521  N  N     . TYR A 1 393 ? 94.258  147.950 151.404 1.00 104.90 ? 393  TYR A N     1 
ATOM   2522  C  CA    . TYR A 1 393 ? 92.860  147.678 151.094 1.00 104.65 ? 393  TYR A CA    1 
ATOM   2523  C  C     . TYR A 1 393 ? 92.732  146.769 149.883 1.00 107.32 ? 393  TYR A C     1 
ATOM   2524  O  O     . TYR A 1 393 ? 91.934  145.829 149.888 1.00 113.79 ? 393  TYR A O     1 
ATOM   2525  C  CB    . TYR A 1 393 ? 92.087  148.970 150.856 1.00 107.77 ? 393  TYR A CB    1 
ATOM   2526  C  CG    . TYR A 1 393 ? 90.779  148.712 150.145 1.00 110.76 ? 393  TYR A CG    1 
ATOM   2527  C  CD1   . TYR A 1 393 ? 89.757  148.014 150.766 1.00 111.39 ? 393  TYR A CD1   1 
ATOM   2528  C  CD2   . TYR A 1 393 ? 90.576  149.147 148.844 1.00 115.04 ? 393  TYR A CD2   1 
ATOM   2529  C  CE1   . TYR A 1 393 ? 88.567  147.763 150.116 1.00 122.08 ? 393  TYR A CE1   1 
ATOM   2530  C  CE2   . TYR A 1 393 ? 89.388  148.903 148.188 1.00 120.46 ? 393  TYR A CE2   1 
ATOM   2531  C  CZ    . TYR A 1 393 ? 88.387  148.212 148.829 1.00 128.76 ? 393  TYR A CZ    1 
ATOM   2532  O  OH    . TYR A 1 393 ? 87.200  147.965 148.181 1.00 140.25 ? 393  TYR A OH    1 
ATOM   2533  N  N     . HIS A 1 394 ? 93.505  147.035 148.829 1.00 104.20 ? 394  HIS A N     1 
ATOM   2534  C  CA    . HIS A 1 394 ? 93.411  146.200 147.637 1.00 104.50 ? 394  HIS A CA    1 
ATOM   2535  C  C     . HIS A 1 394 ? 93.923  144.791 147.902 1.00 107.06 ? 394  HIS A C     1 
ATOM   2536  O  O     . HIS A 1 394 ? 93.323  143.812 147.440 1.00 112.93 ? 394  HIS A O     1 
ATOM   2537  C  CB    . HIS A 1 394 ? 94.161  146.848 146.476 1.00 101.93 ? 394  HIS A CB    1 
ATOM   2538  C  CG    . HIS A 1 394 ? 93.426  147.993 145.856 1.00 108.47 ? 394  HIS A CG    1 
ATOM   2539  N  ND1   . HIS A 1 394 ? 93.811  149.305 146.022 1.00 110.82 ? 394  HIS A ND1   1 
ATOM   2540  C  CD2   . HIS A 1 394 ? 92.315  148.022 145.083 1.00 111.93 ? 394  HIS A CD2   1 
ATOM   2541  C  CE1   . HIS A 1 394 ? 92.975  150.092 145.368 1.00 112.78 ? 394  HIS A CE1   1 
ATOM   2542  N  NE2   . HIS A 1 394 ? 92.057  149.338 144.791 1.00 118.08 ? 394  HIS A NE2   1 
ATOM   2543  N  N     . LEU A 1 395 ? 95.019  144.662 148.653 1.00 105.14 ? 395  LEU A N     1 
ATOM   2544  C  CA    . LEU A 1 395 ? 95.524  143.330 148.972 1.00 105.26 ? 395  LEU A CA    1 
ATOM   2545  C  C     . LEU A 1 395 ? 94.502  142.529 149.769 1.00 106.02 ? 395  LEU A C     1 
ATOM   2546  O  O     . LEU A 1 395 ? 94.239  141.356 149.470 1.00 108.35 ? 395  LEU A O     1 
ATOM   2547  C  CB    . LEU A 1 395 ? 96.840  143.434 149.739 1.00 96.31  ? 395  LEU A CB    1 
ATOM   2548  C  CG    . LEU A 1 395 ? 98.090  143.227 148.890 1.00 89.94  ? 395  LEU A CG    1 
ATOM   2549  C  CD1   . LEU A 1 395 ? 99.281  143.013 149.780 1.00 88.91  ? 395  LEU A CD1   1 
ATOM   2550  C  CD2   . LEU A 1 395 ? 97.900  142.040 147.974 1.00 97.52  ? 395  LEU A CD2   1 
ATOM   2551  N  N     . LEU A 1 396 ? 93.894  143.152 150.777 1.00 103.51 ? 396  LEU A N     1 
ATOM   2552  C  CA    . LEU A 1 396 ? 92.928  142.431 151.595 1.00 102.83 ? 396  LEU A CA    1 
ATOM   2553  C  C     . LEU A 1 396 ? 91.639  142.169 150.827 1.00 106.27 ? 396  LEU A C     1 
ATOM   2554  O  O     . LEU A 1 396 ? 90.987  141.144 151.039 1.00 111.94 ? 396  LEU A O     1 
ATOM   2555  C  CB    . LEU A 1 396 ? 92.654  143.203 152.882 1.00 107.83 ? 396  LEU A CB    1 
ATOM   2556  C  CG    . LEU A 1 396 ? 93.899  143.443 153.736 1.00 103.39 ? 396  LEU A CG    1 
ATOM   2557  C  CD1   . LEU A 1 396 ? 93.524  144.072 155.060 1.00 108.04 ? 396  LEU A CD1   1 
ATOM   2558  C  CD2   . LEU A 1 396 ? 94.666  142.153 153.945 1.00 94.77  ? 396  LEU A CD2   1 
ATOM   2559  N  N     . PHE A 1 397 ? 91.256  143.072 149.924 1.00 105.90 ? 397  PHE A N     1 
ATOM   2560  C  CA    . PHE A 1 397 ? 90.104  142.806 149.073 1.00 110.23 ? 397  PHE A CA    1 
ATOM   2561  C  C     . PHE A 1 397 ? 90.349  141.581 148.209 1.00 113.25 ? 397  PHE A C     1 
ATOM   2562  O  O     . PHE A 1 397 ? 89.486  140.704 148.097 1.00 120.02 ? 397  PHE A O     1 
ATOM   2563  C  CB    . PHE A 1 397 ? 89.794  144.025 148.207 1.00 113.13 ? 397  PHE A CB    1 
ATOM   2564  C  CG    . PHE A 1 397 ? 88.501  143.917 147.458 1.00 118.24 ? 397  PHE A CG    1 
ATOM   2565  C  CD1   . PHE A 1 397 ? 87.301  144.215 148.075 1.00 123.70 ? 397  PHE A CD1   1 
ATOM   2566  C  CD2   . PHE A 1 397 ? 88.486  143.519 146.133 1.00 126.38 ? 397  PHE A CD2   1 
ATOM   2567  C  CE1   . PHE A 1 397 ? 86.110  144.116 147.387 1.00 133.57 ? 397  PHE A CE1   1 
ATOM   2568  C  CE2   . PHE A 1 397 ? 87.299  143.419 145.439 1.00 133.36 ? 397  PHE A CE2   1 
ATOM   2569  C  CZ    . PHE A 1 397 ? 86.109  143.718 146.066 1.00 135.00 ? 397  PHE A CZ    1 
ATOM   2570  N  N     . ALA A 1 398 ? 91.535  141.495 147.606 1.00 108.58 ? 398  ALA A N     1 
ATOM   2571  C  CA    . ALA A 1 398 ? 91.876  140.311 146.826 1.00 110.26 ? 398  ALA A CA    1 
ATOM   2572  C  C     . ALA A 1 398 ? 91.812  139.058 147.688 1.00 112.36 ? 398  ALA A C     1 
ATOM   2573  O  O     . ALA A 1 398 ? 91.190  138.060 147.307 1.00 116.80 ? 398  ALA A O     1 
ATOM   2574  C  CB    . ALA A 1 398 ? 93.264  140.471 146.207 1.00 106.23 ? 398  ALA A CB    1 
ATOM   2575  N  N     . PHE A 1 399 ? 92.420  139.109 148.876 1.00 108.79 ? 399  PHE A N     1 
ATOM   2576  C  CA    . PHE A 1 399 ? 92.497  137.919 149.718 1.00 106.32 ? 399  PHE A CA    1 
ATOM   2577  C  C     . PHE A 1 399 ? 91.116  137.453 150.171 1.00 110.12 ? 399  PHE A C     1 
ATOM   2578  O  O     . PHE A 1 399 ? 90.815  136.256 150.123 1.00 118.64 ? 399  PHE A O     1 
ATOM   2579  C  CB    . PHE A 1 399 ? 93.393  138.191 150.924 1.00 104.57 ? 399  PHE A CB    1 
ATOM   2580  C  CG    . PHE A 1 399 ? 94.837  137.864 150.690 1.00 100.68 ? 399  PHE A CG    1 
ATOM   2581  C  CD1   . PHE A 1 399 ? 95.222  136.586 150.345 1.00 98.36  ? 399  PHE A CD1   1 
ATOM   2582  C  CD2   . PHE A 1 399 ? 95.810  138.837 150.820 1.00 104.19 ? 399  PHE A CD2   1 
ATOM   2583  C  CE1   . PHE A 1 399 ? 96.548  136.285 150.132 1.00 99.45  ? 399  PHE A CE1   1 
ATOM   2584  C  CE2   . PHE A 1 399 ? 97.136  138.539 150.608 1.00 95.97  ? 399  PHE A CE2   1 
ATOM   2585  C  CZ    . PHE A 1 399 ? 97.505  137.263 150.263 1.00 95.22  ? 399  PHE A CZ    1 
ATOM   2586  N  N     . GLU A 1 400 ? 90.266  138.379 150.622 1.00 105.34 ? 400  GLU A N     1 
ATOM   2587  C  CA    . GLU A 1 400 ? 88.915  138.004 151.035 1.00 110.12 ? 400  GLU A CA    1 
ATOM   2588  C  C     . GLU A 1 400 ? 88.069  137.516 149.865 1.00 115.21 ? 400  GLU A C     1 
ATOM   2589  O  O     . GLU A 1 400 ? 87.409  136.476 149.970 1.00 119.50 ? 400  GLU A O     1 
ATOM   2590  C  CB    . GLU A 1 400 ? 88.224  139.175 151.738 1.00 113.30 ? 400  GLU A CB    1 
ATOM   2591  C  CG    . GLU A 1 400 ? 88.344  139.219 153.268 1.00 119.42 ? 400  GLU A CG    1 
ATOM   2592  C  CD    . GLU A 1 400 ? 89.749  139.414 153.805 1.00 118.85 ? 400  GLU A CD    1 
ATOM   2593  O  OE1   . GLU A 1 400 ? 90.708  139.505 153.016 1.00 116.81 ? 400  GLU A OE1   1 
ATOM   2594  O  OE2   . GLU A 1 400 ? 89.893  139.481 155.043 1.00 115.98 ? 400  GLU A OE2   1 
ATOM   2595  N  N     . ARG A 1 401 ? 88.061  138.243 148.745 1.00 114.22 ? 401  ARG A N     1 
ATOM   2596  C  CA    . ARG A 1 401 ? 87.118  137.907 147.683 1.00 117.13 ? 401  ARG A CA    1 
ATOM   2597  C  C     . ARG A 1 401 ? 87.543  136.664 146.912 1.00 120.03 ? 401  ARG A C     1 
ATOM   2598  O  O     . ARG A 1 401 ? 86.692  135.963 146.354 1.00 127.76 ? 401  ARG A O     1 
ATOM   2599  C  CB    . ARG A 1 401 ? 86.933  139.095 146.739 1.00 116.72 ? 401  ARG A CB    1 
ATOM   2600  C  CG    . ARG A 1 401 ? 86.464  140.367 147.428 1.00 121.20 ? 401  ARG A CG    1 
ATOM   2601  C  CD    . ARG A 1 401 ? 84.942  140.428 147.481 1.00 125.45 ? 401  ARG A CD    1 
ATOM   2602  N  NE    . ARG A 1 401 ? 84.446  141.515 148.318 1.00 129.44 ? 401  ARG A NE    1 
ATOM   2603  C  CZ    . ARG A 1 401 ? 84.540  141.556 149.641 1.00 132.81 ? 401  ARG A CZ    1 
ATOM   2604  N  NH1   . ARG A 1 401 ? 85.094  140.570 150.327 1.00 125.58 ? 401  ARG A NH1   1 
ATOM   2605  N  NH2   . ARG A 1 401 ? 84.057  142.609 150.293 1.00 139.62 ? 401  ARG A NH2   1 
ATOM   2606  N  N     . ASN A 1 402 ? 88.843  136.363 146.860 1.00 116.29 ? 402  ASN A N     1 
ATOM   2607  C  CA    . ASN A 1 402 ? 89.265  135.200 146.089 1.00 116.73 ? 402  ASN A CA    1 
ATOM   2608  C  C     . ASN A 1 402 ? 89.199  133.922 146.915 1.00 117.36 ? 402  ASN A C     1 
ATOM   2609  O  O     . ASN A 1 402 ? 88.720  132.891 146.432 1.00 123.62 ? 402  ASN A O     1 
ATOM   2610  C  CB    . ASN A 1 402 ? 90.674  135.414 145.542 1.00 111.16 ? 402  ASN A CB    1 
ATOM   2611  C  CG    . ASN A 1 402 ? 90.953  134.576 144.312 1.00 111.08 ? 402  ASN A CG    1 
ATOM   2612  O  OD1   . ASN A 1 402 ? 90.516  133.431 144.216 1.00 112.75 ? 402  ASN A OD1   1 
ATOM   2613  N  ND2   . ASN A 1 402 ? 91.673  135.149 143.358 1.00 114.60 ? 402  ASN A ND2   1 
ATOM   2614  N  N     . HIS A 1 403 ? 89.696  133.965 148.151 1.00 115.48 ? 403  HIS A N     1 
ATOM   2615  C  CA    . HIS A 1 403 ? 89.721  132.849 149.093 1.00 117.33 ? 403  HIS A CA    1 
ATOM   2616  C  C     . HIS A 1 403 ? 90.597  131.699 148.615 1.00 113.14 ? 403  HIS A C     1 
ATOM   2617  O  O     . HIS A 1 403 ? 90.582  130.630 149.235 1.00 113.22 ? 403  HIS A O     1 
ATOM   2618  C  CB    . HIS A 1 403 ? 88.316  132.312 149.405 1.00 122.44 ? 403  HIS A CB    1 
ATOM   2619  C  CG    . HIS A 1 403 ? 88.039  132.154 150.867 1.00 128.34 ? 403  HIS A CG    1 
ATOM   2620  N  ND1   . HIS A 1 403 ? 88.829  131.386 151.695 1.00 125.75 ? 403  HIS A ND1   1 
ATOM   2621  C  CD2   . HIS A 1 403 ? 87.061  132.667 151.649 1.00 134.97 ? 403  HIS A CD2   1 
ATOM   2622  C  CE1   . HIS A 1 403 ? 88.348  131.432 152.925 1.00 134.47 ? 403  HIS A CE1   1 
ATOM   2623  N  NE2   . HIS A 1 403 ? 87.276  132.203 152.924 1.00 142.00 ? 403  HIS A NE2   1 
ATOM   2624  N  N     . GLN A 1 404 ? 91.351  131.876 147.534 1.00 110.91 ? 404  GLN A N     1 
ATOM   2625  C  CA    . GLN A 1 404 ? 92.225  130.846 146.991 1.00 108.86 ? 404  GLN A CA    1 
ATOM   2626  C  C     . GLN A 1 404 ? 93.670  131.304 146.871 1.00 108.64 ? 404  GLN A C     1 
ATOM   2627  O  O     . GLN A 1 404 ? 94.568  130.462 146.776 1.00 105.32 ? 404  GLN A O     1 
ATOM   2628  C  CB    . GLN A 1 404 ? 91.713  130.403 145.617 1.00 111.38 ? 404  GLN A CB    1 
ATOM   2629  C  CG    . GLN A 1 404 ? 92.326  129.120 145.089 1.00 108.31 ? 404  GLN A CG    1 
ATOM   2630  C  CD    . GLN A 1 404 ? 92.075  128.931 143.608 1.00 111.76 ? 404  GLN A CD    1 
ATOM   2631  O  OE1   . GLN A 1 404 ? 91.187  129.558 143.033 1.00 112.46 ? 404  GLN A OE1   1 
ATOM   2632  N  NE2   . GLN A 1 404 ? 92.857  128.062 142.983 1.00 112.18 ? 404  GLN A NE2   1 
ATOM   2633  N  N     . ILE A 1 405 ? 93.915  132.609 146.882 1.00 109.19 ? 405  ILE A N     1 
ATOM   2634  C  CA    . ILE A 1 405 ? 95.243  133.165 146.648 1.00 98.85  ? 405  ILE A CA    1 
ATOM   2635  C  C     . ILE A 1 405 ? 96.157  132.744 147.789 1.00 99.70  ? 405  ILE A C     1 
ATOM   2636  O  O     . ILE A 1 405 ? 95.883  133.040 148.956 1.00 103.48 ? 405  ILE A O     1 
ATOM   2637  C  CB    . ILE A 1 405 ? 95.186  134.693 146.533 1.00 97.95  ? 405  ILE A CB    1 
ATOM   2638  C  CG1   . ILE A 1 405 ? 94.254  135.111 145.402 1.00 101.90 ? 405  ILE A CG1   1 
ATOM   2639  C  CG2   . ILE A 1 405 ? 96.568  135.255 146.296 1.00 99.50  ? 405  ILE A CG2   1 
ATOM   2640  C  CD1   . ILE A 1 405 ? 94.026  136.597 145.342 1.00 110.32 ? 405  ILE A CD1   1 
ATOM   2641  N  N     . GLY A 1 406 ? 97.246  132.063 147.453 1.00 100.69 ? 406  GLY A N     1 
ATOM   2642  C  CA    . GLY A 1 406 ? 98.205  131.636 148.451 1.00 104.26 ? 406  GLY A CA    1 
ATOM   2643  C  C     . GLY A 1 406 ? 99.260  132.684 148.724 1.00 96.74  ? 406  GLY A C     1 
ATOM   2644  O  O     . GLY A 1 406 ? 100.128 132.499 149.580 1.00 101.04 ? 406  GLY A O     1 
ATOM   2645  N  N     . GLY A 1 407 ? 99.198  133.789 147.989 1.00 92.39  ? 407  GLY A N     1 
ATOM   2646  C  CA    . GLY A 1 407 ? 100.140 134.875 148.155 1.00 91.78  ? 407  GLY A CA    1 
ATOM   2647  C  C     . GLY A 1 407 ? 100.055 135.863 147.013 1.00 96.27  ? 407  GLY A C     1 
ATOM   2648  O  O     . GLY A 1 407 ? 99.773  135.476 145.877 1.00 106.73 ? 407  GLY A O     1 
ATOM   2649  N  N     . ALA A 1 408 ? 100.298 137.139 147.289 1.00 91.55  ? 408  ALA A N     1 
ATOM   2650  C  CA    . ALA A 1 408 ? 100.182 138.168 146.271 1.00 90.40  ? 408  ALA A CA    1 
ATOM   2651  C  C     . ALA A 1 408 ? 101.323 139.159 146.425 1.00 91.38  ? 408  ALA A C     1 
ATOM   2652  O  O     . ALA A 1 408 ? 101.913 139.296 147.498 1.00 99.03  ? 408  ALA A O     1 
ATOM   2653  C  CB    . ALA A 1 408 ? 98.834  138.892 146.351 1.00 89.78  ? 408  ALA A CB    1 
ATOM   2654  N  N     . CYS A 1 409 ? 101.629 139.851 145.332 1.00 88.25  ? 409  CYS A N     1 
ATOM   2655  C  CA    . CYS A 1 409 ? 102.675 140.860 145.324 1.00 92.10  ? 409  CYS A CA    1 
ATOM   2656  C  C     . CYS A 1 409 ? 102.126 142.140 144.717 1.00 99.14  ? 409  CYS A C     1 
ATOM   2657  O  O     . CYS A 1 409 ? 101.383 142.100 143.734 1.00 107.84 ? 409  CYS A O     1 
ATOM   2658  C  CB    . CYS A 1 409 ? 103.903 140.390 144.538 1.00 99.75  ? 409  CYS A CB    1 
ATOM   2659  S  SG    . CYS A 1 409 ? 103.566 139.948 142.825 1.00 117.37 ? 409  CYS A SG    1 
ATOM   2660  N  N     . GLY A 1 410 ? 102.493 143.274 145.311 1.00 99.42  ? 410  GLY A N     1 
ATOM   2661  C  CA    . GLY A 1 410 ? 102.049 144.562 144.829 1.00 97.03  ? 410  GLY A CA    1 
ATOM   2662  C  C     . GLY A 1 410 ? 102.936 145.103 143.726 1.00 97.87  ? 410  GLY A C     1 
ATOM   2663  O  O     . GLY A 1 410 ? 104.060 144.656 143.507 1.00 99.71  ? 410  GLY A O     1 
ATOM   2664  N  N     . GLN A 1 411 ? 102.402 146.089 143.015 1.00 103.64 ? 411  GLN A N     1 
ATOM   2665  C  CA    . GLN A 1 411 ? 103.146 146.740 141.949 1.00 102.36 ? 411  GLN A CA    1 
ATOM   2666  C  C     . GLN A 1 411 ? 104.301 147.543 142.528 1.00 102.19 ? 411  GLN A C     1 
ATOM   2667  O  O     . GLN A 1 411 ? 104.158 148.214 143.553 1.00 105.02 ? 411  GLN A O     1 
ATOM   2668  C  CB    . GLN A 1 411 ? 102.227 147.651 141.137 1.00 104.00 ? 411  GLN A CB    1 
ATOM   2669  C  CG    . GLN A 1 411 ? 102.922 148.376 140.003 1.00 106.75 ? 411  GLN A CG    1 
ATOM   2670  C  CD    . GLN A 1 411 ? 101.963 149.183 139.160 1.00 113.40 ? 411  GLN A CD    1 
ATOM   2671  O  OE1   . GLN A 1 411 ? 100.791 149.328 139.502 1.00 116.23 ? 411  GLN A OE1   1 
ATOM   2672  N  NE2   . GLN A 1 411 ? 102.452 149.705 138.043 1.00 116.30 ? 411  GLN A NE2   1 
ATOM   2673  N  N     . LEU A 1 412 ? 105.452 147.466 141.869 1.00 100.83 ? 412  LEU A N     1 
ATOM   2674  C  CA    . LEU A 1 412 ? 106.645 148.193 142.275 1.00 101.42 ? 412  LEU A CA    1 
ATOM   2675  C  C     . LEU A 1 412 ? 106.834 149.382 141.345 1.00 106.44 ? 412  LEU A C     1 
ATOM   2676  O  O     . LEU A 1 412 ? 106.874 149.216 140.122 1.00 114.86 ? 412  LEU A O     1 
ATOM   2677  C  CB    . LEU A 1 412 ? 107.874 147.285 142.240 1.00 104.58 ? 412  LEU A CB    1 
ATOM   2678  C  CG    . LEU A 1 412 ? 109.042 147.707 143.125 1.00 104.06 ? 412  LEU A CG    1 
ATOM   2679  C  CD1   . LEU A 1 412 ? 108.599 147.702 144.574 1.00 104.17 ? 412  LEU A CD1   1 
ATOM   2680  C  CD2   . LEU A 1 412 ? 110.227 146.784 142.922 1.00 112.75 ? 412  LEU A CD2   1 
ATOM   2681  N  N     . THR A 1 413 ? 106.947 150.576 141.920 1.00 100.42 ? 413  THR A N     1 
ATOM   2682  C  CA    . THR A 1 413 ? 106.984 151.804 141.143 1.00 101.72 ? 413  THR A CA    1 
ATOM   2683  C  C     . THR A 1 413 ? 108.071 152.715 141.700 1.00 110.80 ? 413  THR A C     1 
ATOM   2684  O  O     . THR A 1 413 ? 108.338 152.735 142.903 1.00 117.75 ? 413  THR A O     1 
ATOM   2685  C  CB    . THR A 1 413 ? 105.604 152.483 141.152 1.00 110.21 ? 413  THR A CB    1 
ATOM   2686  O  OG1   . THR A 1 413 ? 104.745 151.823 140.215 1.00 111.83 ? 413  THR A OG1   1 
ATOM   2687  C  CG2   . THR A 1 413 ? 105.694 153.953 140.782 1.00 116.62 ? 413  THR A CG2   1 
ATOM   2688  N  N     . VAL A 1 414 ? 108.717 153.462 140.807 1.00 110.60 ? 414  VAL A N     1 
ATOM   2689  C  CA    . VAL A 1 414 ? 109.724 154.451 141.176 1.00 115.18 ? 414  VAL A CA    1 
ATOM   2690  C  C     . VAL A 1 414 ? 109.014 155.728 141.603 1.00 126.57 ? 414  VAL A C     1 
ATOM   2691  O  O     . VAL A 1 414 ? 108.132 156.223 140.890 1.00 130.25 ? 414  VAL A O     1 
ATOM   2692  C  CB    . VAL A 1 414 ? 110.687 154.721 140.009 1.00 112.26 ? 414  VAL A CB    1 
ATOM   2693  C  CG1   . VAL A 1 414 ? 111.664 155.817 140.372 1.00 119.94 ? 414  VAL A CG1   1 
ATOM   2694  C  CG2   . VAL A 1 414 ? 111.427 153.453 139.631 1.00 107.93 ? 414  VAL A CG2   1 
ATOM   2695  N  N     . ASP A 1 415 ? 109.383 156.257 142.770 1.00 128.16 ? 415  ASP A N     1 
ATOM   2696  C  CA    . ASP A 1 415 ? 108.768 157.485 143.255 1.00 132.36 ? 415  ASP A CA    1 
ATOM   2697  C  C     . ASP A 1 415 ? 109.213 158.655 142.390 1.00 138.54 ? 415  ASP A C     1 
ATOM   2698  O  O     . ASP A 1 415 ? 110.365 158.705 141.948 1.00 137.78 ? 415  ASP A O     1 
ATOM   2699  C  CB    . ASP A 1 415 ? 109.152 157.755 144.707 1.00 131.71 ? 415  ASP A CB    1 
ATOM   2700  C  CG    . ASP A 1 415 ? 110.598 157.419 144.997 1.00 137.12 ? 415  ASP A CG    1 
ATOM   2701  O  OD1   . ASP A 1 415 ? 111.206 156.676 144.202 1.00 136.09 ? 415  ASP A OD1   1 
ATOM   2702  O  OD2   . ASP A 1 415 ? 111.138 157.931 146.001 1.00 142.57 ? 415  ASP A OD2   1 
ATOM   2703  N  N     . ASN A 1 416 ? 108.307 159.606 142.173 1.00 143.91 ? 416  ASN A N     1 
ATOM   2704  C  CA    . ASN A 1 416 ? 108.574 160.800 141.377 1.00 146.50 ? 416  ASN A CA    1 
ATOM   2705  C  C     . ASN A 1 416 ? 109.194 160.445 140.030 1.00 146.71 ? 416  ASN A C     1 
ATOM   2706  O  O     . ASN A 1 416 ? 110.329 160.847 139.747 1.00 147.86 ? 416  ASN A O     1 
ATOM   2707  C  CB    . ASN A 1 416 ? 109.493 161.755 142.139 1.00 147.00 ? 416  ASN A CB    1 
ATOM   2708  C  CG    . ASN A 1 416 ? 108.804 162.406 143.316 1.00 152.66 ? 416  ASN A CG    1 
ATOM   2709  O  OD1   . ASN A 1 416 ? 107.782 161.918 143.799 1.00 154.84 ? 416  ASN A OD1   1 
ATOM   2710  N  ND2   . ASN A 1 416 ? 109.360 163.515 143.788 1.00 157.94 ? 416  ASN A ND2   1 
ATOM   2711  N  N     . PRO A 1 417 ? 108.495 159.693 139.177 1.00 145.09 ? 417  PRO A N     1 
ATOM   2712  C  CA    . PRO A 1 417 ? 109.073 159.394 137.859 1.00 141.80 ? 417  PRO A CA    1 
ATOM   2713  C  C     . PRO A 1 417 ? 109.017 160.579 136.915 1.00 149.95 ? 417  PRO A C     1 
ATOM   2714  O  O     . PRO A 1 417 ? 109.929 160.761 136.099 1.00 150.42 ? 417  PRO A O     1 
ATOM   2715  C  CB    . PRO A 1 417 ? 108.216 158.223 137.368 1.00 135.37 ? 417  PRO A CB    1 
ATOM   2716  C  CG    . PRO A 1 417 ? 106.890 158.449 138.012 1.00 139.86 ? 417  PRO A CG    1 
ATOM   2717  C  CD    . PRO A 1 417 ? 107.158 159.095 139.344 1.00 143.64 ? 417  PRO A CD    1 
ATOM   2718  N  N     . PHE A 1 418 ? 107.959 161.389 136.998 1.00 151.36 ? 418  PHE A N     1 
ATOM   2719  C  CA    . PHE A 1 418 ? 107.878 162.592 136.179 1.00 151.46 ? 418  PHE A CA    1 
ATOM   2720  C  C     . PHE A 1 418 ? 108.993 163.566 136.533 1.00 151.93 ? 418  PHE A C     1 
ATOM   2721  O  O     . PHE A 1 418 ? 109.636 164.137 135.645 1.00 152.55 ? 418  PHE A O     1 
ATOM   2722  C  CB    . PHE A 1 418 ? 106.515 163.258 136.363 1.00 153.59 ? 418  PHE A CB    1 
ATOM   2723  C  CG    . PHE A 1 418 ? 105.367 162.457 135.819 1.00 157.03 ? 418  PHE A CG    1 
ATOM   2724  C  CD1   . PHE A 1 418 ? 105.573 161.485 134.856 1.00 154.03 ? 418  PHE A CD1   1 
ATOM   2725  C  CD2   . PHE A 1 418 ? 104.078 162.675 136.277 1.00 158.52 ? 418  PHE A CD2   1 
ATOM   2726  C  CE1   . PHE A 1 418 ? 104.515 160.749 134.357 1.00 153.93 ? 418  PHE A CE1   1 
ATOM   2727  C  CE2   . PHE A 1 418 ? 103.016 161.942 135.783 1.00 158.01 ? 418  PHE A CE2   1 
ATOM   2728  C  CZ    . PHE A 1 418 ? 103.236 160.978 134.822 1.00 155.30 ? 418  PHE A CZ    1 
ATOM   2729  N  N     . GLU A 1 419 ? 109.236 163.763 137.825 1.00 150.42 ? 419  GLU A N     1 
ATOM   2730  C  CA    . GLU A 1 419 ? 110.290 164.657 138.274 1.00 152.17 ? 419  GLU A CA    1 
ATOM   2731  C  C     . GLU A 1 419 ? 111.657 164.047 137.982 1.00 151.30 ? 419  GLU A C     1 
ATOM   2732  O  O     . GLU A 1 419 ? 111.830 162.826 137.984 1.00 149.62 ? 419  GLU A O     1 
ATOM   2733  C  CB    . GLU A 1 419 ? 110.123 164.951 139.769 1.00 153.99 ? 419  GLU A CB    1 
ATOM   2734  C  CG    . GLU A 1 419 ? 111.253 165.733 140.430 1.00 158.31 ? 419  GLU A CG    1 
ATOM   2735  C  CD    . GLU A 1 419 ? 112.362 164.846 140.966 1.00 158.51 ? 419  GLU A CD    1 
ATOM   2736  O  OE1   . GLU A 1 419 ? 112.261 163.610 140.831 1.00 156.86 ? 419  GLU A OE1   1 
ATOM   2737  O  OE2   . GLU A 1 419 ? 113.337 165.390 141.524 1.00 161.03 ? 419  GLU A OE2   1 
ATOM   2738  N  N     . ASN A 1 420 ? 112.632 164.920 137.721 1.00 151.92 ? 420  ASN A N     1 
ATOM   2739  C  CA    . ASN A 1 420 ? 113.996 164.510 137.382 1.00 152.78 ? 420  ASN A CA    1 
ATOM   2740  C  C     . ASN A 1 420 ? 114.008 163.595 136.161 1.00 150.74 ? 420  ASN A C     1 
ATOM   2741  O  O     . ASN A 1 420 ? 114.640 162.538 136.159 1.00 145.90 ? 420  ASN A O     1 
ATOM   2742  C  CB    . ASN A 1 420 ? 114.691 163.842 138.570 1.00 153.87 ? 420  ASN A CB    1 
ATOM   2743  C  CG    . ASN A 1 420 ? 116.179 164.131 138.610 1.00 154.98 ? 420  ASN A CG    1 
ATOM   2744  O  OD1   . ASN A 1 420 ? 116.660 165.056 137.957 1.00 152.87 ? 420  ASN A OD1   1 
ATOM   2745  N  ND2   . ASN A 1 420 ? 116.916 163.337 139.378 1.00 151.02 ? 420  ASN A ND2   1 
ATOM   2746  N  N     . LEU A 1 421 ? 113.294 164.007 135.112 1.00 152.29 ? 421  LEU A N     1 
ATOM   2747  C  CA    . LEU A 1 421 ? 113.272 163.236 133.877 1.00 147.33 ? 421  LEU A CA    1 
ATOM   2748  C  C     . LEU A 1 421 ? 114.598 163.313 133.132 1.00 142.75 ? 421  LEU A C     1 
ATOM   2749  O  O     . LEU A 1 421 ? 114.829 162.518 132.216 1.00 140.57 ? 421  LEU A O     1 
ATOM   2750  C  CB    . LEU A 1 421 ? 112.131 163.720 132.981 1.00 147.69 ? 421  LEU A CB    1 
ATOM   2751  C  CG    . LEU A 1 421 ? 111.682 162.791 131.854 1.00 145.19 ? 421  LEU A CG    1 
ATOM   2752  C  CD1   . LEU A 1 421 ? 111.468 161.384 132.383 1.00 141.36 ? 421  LEU A CD1   1 
ATOM   2753  C  CD2   . LEU A 1 421 ? 110.416 163.319 131.201 1.00 147.00 ? 421  LEU A CD2   1 
ATOM   2754  N  N     . SER A 1 422 ? 115.475 164.245 133.511 1.00 142.34 ? 422  SER A N     1 
ATOM   2755  C  CA    . SER A 1 422 ? 116.772 164.360 132.858 1.00 142.59 ? 422  SER A CA    1 
ATOM   2756  C  C     . SER A 1 422 ? 117.694 163.194 133.185 1.00 138.60 ? 422  SER A C     1 
ATOM   2757  O  O     . SER A 1 422 ? 118.626 162.927 132.420 1.00 134.90 ? 422  SER A O     1 
ATOM   2758  C  CB    . SER A 1 422 ? 117.445 165.674 133.253 1.00 144.93 ? 422  SER A CB    1 
ATOM   2759  O  OG    . SER A 1 422 ? 118.412 165.464 134.267 1.00 145.29 ? 422  SER A OG    1 
ATOM   2760  N  N     . ASN A 1 423 ? 117.462 162.499 134.296 1.00 138.09 ? 423  ASN A N     1 
ATOM   2761  C  CA    . ASN A 1 423 ? 118.274 161.341 134.649 1.00 133.78 ? 423  ASN A CA    1 
ATOM   2762  C  C     . ASN A 1 423 ? 117.853 160.157 133.792 1.00 131.84 ? 423  ASN A C     1 
ATOM   2763  O  O     . ASN A 1 423 ? 116.670 159.805 133.746 1.00 134.87 ? 423  ASN A O     1 
ATOM   2764  C  CB    . ASN A 1 423 ? 118.130 161.011 136.132 1.00 132.87 ? 423  ASN A CB    1 
ATOM   2765  C  CG    . ASN A 1 423 ? 119.283 160.179 136.655 1.00 128.78 ? 423  ASN A CG    1 
ATOM   2766  O  OD1   . ASN A 1 423 ? 120.063 159.627 135.882 1.00 127.50 ? 423  ASN A OD1   1 
ATOM   2767  N  ND2   . ASN A 1 423 ? 119.396 160.086 137.973 1.00 128.95 ? 423  ASN A ND2   1 
ATOM   2768  N  N     . TRP A 1 424 ? 118.820 159.543 133.111 1.00 128.40 ? 424  TRP A N     1 
ATOM   2769  C  CA    . TRP A 1 424 ? 118.496 158.466 132.186 1.00 125.65 ? 424  TRP A CA    1 
ATOM   2770  C  C     . TRP A 1 424 ? 118.349 157.134 132.911 1.00 121.24 ? 424  TRP A C     1 
ATOM   2771  O  O     . TRP A 1 424 ? 117.500 156.316 132.542 1.00 120.90 ? 424  TRP A O     1 
ATOM   2772  C  CB    . TRP A 1 424 ? 119.567 158.379 131.099 1.00 124.36 ? 424  TRP A CB    1 
ATOM   2773  C  CG    . TRP A 1 424 ? 119.416 159.441 130.049 1.00 127.06 ? 424  TRP A CG    1 
ATOM   2774  C  CD1   . TRP A 1 424 ? 119.601 160.780 130.216 1.00 132.09 ? 424  TRP A CD1   1 
ATOM   2775  C  CD2   . TRP A 1 424 ? 119.048 159.257 128.676 1.00 125.24 ? 424  TRP A CD2   1 
ATOM   2776  N  NE1   . TRP A 1 424 ? 119.373 161.443 129.037 1.00 130.83 ? 424  TRP A NE1   1 
ATOM   2777  C  CE2   . TRP A 1 424 ? 119.032 160.531 128.075 1.00 126.86 ? 424  TRP A CE2   1 
ATOM   2778  C  CE3   . TRP A 1 424 ? 118.733 158.142 127.897 1.00 123.17 ? 424  TRP A CE3   1 
ATOM   2779  C  CZ2   . TRP A 1 424 ? 118.712 160.719 126.735 1.00 123.16 ? 424  TRP A CZ2   1 
ATOM   2780  C  CZ3   . TRP A 1 424 ? 118.415 158.334 126.565 1.00 124.77 ? 424  TRP A CZ3   1 
ATOM   2781  C  CH2   . TRP A 1 424 ? 118.408 159.611 125.998 1.00 124.41 ? 424  TRP A CH2   1 
ATOM   2782  N  N     . VAL A 1 425 ? 119.147 156.910 133.956 1.00 116.54 ? 425  VAL A N     1 
ATOM   2783  C  CA    . VAL A 1 425 ? 119.112 155.632 134.664 1.00 112.84 ? 425  VAL A CA    1 
ATOM   2784  C  C     . VAL A 1 425 ? 117.805 155.470 135.431 1.00 115.65 ? 425  VAL A C     1 
ATOM   2785  O  O     . VAL A 1 425 ? 117.191 154.397 135.417 1.00 119.07 ? 425  VAL A O     1 
ATOM   2786  C  CB    . VAL A 1 425 ? 120.332 155.505 135.592 1.00 115.70 ? 425  VAL A CB    1 
ATOM   2787  C  CG1   . VAL A 1 425 ? 120.220 154.260 136.440 1.00 116.67 ? 425  VAL A CG1   1 
ATOM   2788  C  CG2   . VAL A 1 425 ? 121.610 155.481 134.778 1.00 117.71 ? 425  VAL A CG2   1 
ATOM   2789  N  N     . ILE A 1 426 ? 117.363 156.525 136.119 1.00 116.40 ? 426  ILE A N     1 
ATOM   2790  C  CA    . ILE A 1 426 ? 116.101 156.452 136.851 1.00 115.00 ? 426  ILE A CA    1 
ATOM   2791  C  C     . ILE A 1 426 ? 114.944 156.214 135.893 1.00 114.18 ? 426  ILE A C     1 
ATOM   2792  O  O     . ILE A 1 426 ? 114.044 155.412 136.168 1.00 114.57 ? 426  ILE A O     1 
ATOM   2793  C  CB    . ILE A 1 426 ? 115.883 157.728 137.685 1.00 115.08 ? 426  ILE A CB    1 
ATOM   2794  C  CG1   . ILE A 1 426 ? 116.885 157.801 138.834 1.00 123.29 ? 426  ILE A CG1   1 
ATOM   2795  C  CG2   . ILE A 1 426 ? 114.463 157.781 138.219 1.00 107.75 ? 426  ILE A CG2   1 
ATOM   2796  C  CD1   . ILE A 1 426 ? 116.731 159.045 139.677 1.00 130.03 ? 426  ILE A CD1   1 
ATOM   2797  N  N     . SER A 1 427 ? 114.946 156.907 134.754 1.00 111.80 ? 427  SER A N     1 
ATOM   2798  C  CA    . SER A 1 427 ? 113.892 156.696 133.770 1.00 108.45 ? 427  SER A CA    1 
ATOM   2799  C  C     . SER A 1 427 ? 113.915 155.270 133.235 1.00 109.02 ? 427  SER A C     1 
ATOM   2800  O  O     . SER A 1 427 ? 112.863 154.634 133.117 1.00 111.72 ? 427  SER A O     1 
ATOM   2801  C  CB    . SER A 1 427 ? 114.026 157.704 132.633 1.00 114.83 ? 427  SER A CB    1 
ATOM   2802  O  OG    . SER A 1 427 ? 113.984 159.030 133.127 1.00 125.34 ? 427  SER A OG    1 
ATOM   2803  N  N     . ALA A 1 428 ? 115.099 154.747 132.916 1.00 105.62 ? 428  ALA A N     1 
ATOM   2804  C  CA    . ALA A 1 428 ? 115.182 153.380 132.416 1.00 100.12 ? 428  ALA A CA    1 
ATOM   2805  C  C     . ALA A 1 428 ? 114.672 152.387 133.448 1.00 99.58  ? 428  ALA A C     1 
ATOM   2806  O  O     . ALA A 1 428 ? 113.986 151.419 133.103 1.00 102.27 ? 428  ALA A O     1 
ATOM   2807  C  CB    . ALA A 1 428 ? 116.618 153.050 132.020 1.00 104.98 ? 428  ALA A CB    1 
ATOM   2808  N  N     . GLN A 1 429 ? 114.994 152.612 134.722 1.00 102.31 ? 429  GLN A N     1 
ATOM   2809  C  CA    . GLN A 1 429 ? 114.483 151.743 135.775 1.00 103.73 ? 429  GLN A CA    1 
ATOM   2810  C  C     . GLN A 1 429 ? 112.968 151.834 135.881 1.00 104.76 ? 429  GLN A C     1 
ATOM   2811  O  O     . GLN A 1 429 ? 112.294 150.819 136.087 1.00 109.27 ? 429  GLN A O     1 
ATOM   2812  C  CB    . GLN A 1 429 ? 115.136 152.097 137.105 1.00 104.00 ? 429  GLN A CB    1 
ATOM   2813  C  CG    . GLN A 1 429 ? 116.536 151.561 137.247 1.00 108.37 ? 429  GLN A CG    1 
ATOM   2814  C  CD    . GLN A 1 429 ? 117.183 151.990 138.538 1.00 122.38 ? 429  GLN A CD    1 
ATOM   2815  O  OE1   . GLN A 1 429 ? 117.227 151.231 139.504 1.00 128.55 ? 429  GLN A OE1   1 
ATOM   2816  N  NE2   . GLN A 1 429 ? 117.691 153.215 138.566 1.00 122.62 ? 429  GLN A NE2   1 
ATOM   2817  N  N     . HIS A 1 430 ? 112.415 153.040 135.752 1.00 101.51 ? 430  HIS A N     1 
ATOM   2818  C  CA    . HIS A 1 430 ? 110.964 153.197 135.780 1.00 101.13 ? 430  HIS A CA    1 
ATOM   2819  C  C     . HIS A 1 430 ? 110.308 152.443 134.631 1.00 100.98 ? 430  HIS A C     1 
ATOM   2820  O  O     . HIS A 1 430 ? 109.293 151.760 134.816 1.00 104.47 ? 430  HIS A O     1 
ATOM   2821  C  CB    . HIS A 1 430 ? 110.597 154.677 135.722 1.00 105.40 ? 430  HIS A CB    1 
ATOM   2822  C  CG    . HIS A 1 430 ? 109.125 154.931 135.765 1.00 105.01 ? 430  HIS A CG    1 
ATOM   2823  N  ND1   . HIS A 1 430 ? 108.506 155.852 134.950 1.00 111.06 ? 430  HIS A ND1   1 
ATOM   2824  C  CD2   . HIS A 1 430 ? 108.147 154.379 136.521 1.00 107.80 ? 430  HIS A CD2   1 
ATOM   2825  C  CE1   . HIS A 1 430 ? 107.210 155.858 135.203 1.00 117.20 ? 430  HIS A CE1   1 
ATOM   2826  N  NE2   . HIS A 1 430 ? 106.966 154.975 136.154 1.00 114.86 ? 430  HIS A NE2   1 
ATOM   2827  N  N     . PHE A 1 431 ? 110.874 152.565 133.430 1.00 98.25  ? 431  PHE A N     1 
ATOM   2828  C  CA    . PHE A 1 431 ? 110.329 151.851 132.280 1.00 93.81  ? 431  PHE A CA    1 
ATOM   2829  C  C     . PHE A 1 431 ? 110.411 150.350 132.488 1.00 97.47  ? 431  PHE A C     1 
ATOM   2830  O  O     . PHE A 1 431 ? 109.464 149.619 132.175 1.00 100.45 ? 431  PHE A O     1 
ATOM   2831  C  CB    . PHE A 1 431 ? 111.074 152.243 131.006 1.00 98.82  ? 431  PHE A CB    1 
ATOM   2832  C  CG    . PHE A 1 431 ? 110.510 151.626 129.755 1.00 97.25  ? 431  PHE A CG    1 
ATOM   2833  C  CD1   . PHE A 1 431 ? 110.872 150.349 129.366 1.00 93.58  ? 431  PHE A CD1   1 
ATOM   2834  C  CD2   . PHE A 1 431 ? 109.613 152.323 128.971 1.00 104.94 ? 431  PHE A CD2   1 
ATOM   2835  C  CE1   . PHE A 1 431 ? 110.358 149.786 128.220 1.00 94.31  ? 431  PHE A CE1   1 
ATOM   2836  C  CE2   . PHE A 1 431 ? 109.099 151.762 127.822 1.00 106.21 ? 431  PHE A CE2   1 
ATOM   2837  C  CZ    . PHE A 1 431 ? 109.469 150.493 127.449 1.00 100.19 ? 431  PHE A CZ    1 
ATOM   2838  N  N     . GLU A 1 432 ? 111.546 149.867 132.998 1.00 99.56  ? 432  GLU A N     1 
ATOM   2839  C  CA    . GLU A 1 432 ? 111.690 148.439 133.236 1.00 96.92  ? 432  GLU A CA    1 
ATOM   2840  C  C     . GLU A 1 432 ? 110.669 147.955 134.249 1.00 99.13  ? 432  GLU A C     1 
ATOM   2841  O  O     . GLU A 1 432 ? 110.040 146.914 134.052 1.00 101.47 ? 432  GLU A O     1 
ATOM   2842  C  CB    . GLU A 1 432 ? 113.101 148.114 133.717 1.00 98.30  ? 432  GLU A CB    1 
ATOM   2843  C  CG    . GLU A 1 432 ? 113.279 146.654 134.090 1.00 104.60 ? 432  GLU A CG    1 
ATOM   2844  C  CD    . GLU A 1 432 ? 114.487 146.414 134.967 1.00 112.51 ? 432  GLU A CD    1 
ATOM   2845  O  OE1   . GLU A 1 432 ? 115.195 147.391 135.282 1.00 113.56 ? 432  GLU A OE1   1 
ATOM   2846  O  OE2   . GLU A 1 432 ? 114.731 145.249 135.341 1.00 118.79 ? 432  GLU A OE2   1 
ATOM   2847  N  N     . TYR A 1 433 ? 110.476 148.709 135.332 1.00 97.59  ? 433  TYR A N     1 
ATOM   2848  C  CA    . TYR A 1 433 ? 109.494 148.316 136.336 1.00 95.70  ? 433  TYR A CA    1 
ATOM   2849  C  C     . TYR A 1 433 ? 108.098 148.263 135.737 1.00 98.19  ? 433  TYR A C     1 
ATOM   2850  O  O     . TYR A 1 433 ? 107.364 147.291 135.938 1.00 101.40 ? 433  TYR A O     1 
ATOM   2851  C  CB    . TYR A 1 433 ? 109.525 149.282 137.517 1.00 95.04  ? 433  TYR A CB    1 
ATOM   2852  C  CG    . TYR A 1 433 ? 110.691 149.091 138.452 1.00 97.41  ? 433  TYR A CG    1 
ATOM   2853  C  CD1   . TYR A 1 433 ? 111.678 148.156 138.186 1.00 99.00  ? 433  TYR A CD1   1 
ATOM   2854  C  CD2   . TYR A 1 433 ? 110.803 149.848 139.604 1.00 104.01 ? 433  TYR A CD2   1 
ATOM   2855  C  CE1   . TYR A 1 433 ? 112.744 147.986 139.041 1.00 106.11 ? 433  TYR A CE1   1 
ATOM   2856  C  CE2   . TYR A 1 433 ? 111.859 149.683 140.463 1.00 105.92 ? 433  TYR A CE2   1 
ATOM   2857  C  CZ    . TYR A 1 433 ? 112.827 148.754 140.179 1.00 107.59 ? 433  TYR A CZ    1 
ATOM   2858  O  OH    . TYR A 1 433 ? 113.881 148.598 141.044 1.00 117.69 ? 433  TYR A OH    1 
ATOM   2859  N  N     . LYS A 1 434 ? 107.720 149.293 134.979 1.00 98.76  ? 434  LYS A N     1 
ATOM   2860  C  CA    . LYS A 1 434 ? 106.361 149.352 134.454 1.00 97.43  ? 434  LYS A CA    1 
ATOM   2861  C  C     . LYS A 1 434 ? 106.113 148.238 133.445 1.00 99.49  ? 434  LYS A C     1 
ATOM   2862  O  O     . LYS A 1 434 ? 105.088 147.548 133.506 1.00 106.92 ? 434  LYS A O     1 
ATOM   2863  C  CB    . LYS A 1 434 ? 106.101 150.720 133.830 1.00 95.85  ? 434  LYS A CB    1 
ATOM   2864  C  CG    . LYS A 1 434 ? 105.908 151.809 134.861 1.00 103.97 ? 434  LYS A CG    1 
ATOM   2865  C  CD    . LYS A 1 434 ? 104.467 151.900 135.310 1.00 110.63 ? 434  LYS A CD    1 
ATOM   2866  C  CE    . LYS A 1 434 ? 104.332 152.833 136.500 1.00 116.95 ? 434  LYS A CE    1 
ATOM   2867  N  NZ    . LYS A 1 434 ? 104.313 152.089 137.786 1.00 116.98 ? 434  LYS A NZ    1 
ATOM   2868  N  N     . ILE A 1 435 ? 107.049 148.034 132.516 1.00 96.74  ? 435  ILE A N     1 
ATOM   2869  C  CA    . ILE A 1 435 ? 106.870 146.994 131.510 1.00 97.32  ? 435  ILE A CA    1 
ATOM   2870  C  C     . ILE A 1 435 ? 106.908 145.613 132.148 1.00 103.53 ? 435  ILE A C     1 
ATOM   2871  O  O     . ILE A 1 435 ? 106.069 144.756 131.844 1.00 107.77 ? 435  ILE A O     1 
ATOM   2872  C  CB    . ILE A 1 435 ? 107.921 147.139 130.397 1.00 94.40  ? 435  ILE A CB    1 
ATOM   2873  C  CG1   . ILE A 1 435 ? 107.510 148.257 129.444 1.00 101.36 ? 435  ILE A CG1   1 
ATOM   2874  C  CG2   . ILE A 1 435 ? 108.090 145.835 129.646 1.00 93.56  ? 435  ILE A CG2   1 
ATOM   2875  C  CD1   . ILE A 1 435 ? 106.104 148.108 128.913 1.00 102.09 ? 435  ILE A CD1   1 
ATOM   2876  N  N     . SER A 1 436 ? 107.871 145.370 133.040 1.00 102.64 ? 436  SER A N     1 
ATOM   2877  C  CA    . SER A 1 436 ? 107.943 144.084 133.717 1.00 102.30 ? 436  SER A CA    1 
ATOM   2878  C  C     . SER A 1 436 ? 106.648 143.796 134.456 1.00 100.97 ? 436  SER A C     1 
ATOM   2879  O  O     . SER A 1 436 ? 106.005 142.769 134.213 1.00 109.77 ? 436  SER A O     1 
ATOM   2880  C  CB    . SER A 1 436 ? 109.130 144.065 134.679 1.00 99.22  ? 436  SER A CB    1 
ATOM   2881  O  OG    . SER A 1 436 ? 109.196 142.838 135.382 1.00 102.75 ? 436  SER A OG    1 
ATOM   2882  N  N     . ASN A 1 437 ? 106.217 144.726 135.313 1.00 93.76  ? 437  ASN A N     1 
ATOM   2883  C  CA    . ASN A 1 437 ? 104.946 144.580 136.008 1.00 97.08  ? 437  ASN A CA    1 
ATOM   2884  C  C     . ASN A 1 437 ? 103.836 144.238 135.029 1.00 104.03 ? 437  ASN A C     1 
ATOM   2885  O  O     . ASN A 1 437 ? 103.349 143.106 135.012 1.00 115.15 ? 437  ASN A O     1 
ATOM   2886  C  CB    . ASN A 1 437 ? 104.613 145.862 136.770 1.00 99.15  ? 437  ASN A CB    1 
ATOM   2887  C  CG    . ASN A 1 437 ? 105.406 146.001 138.047 1.00 108.67 ? 437  ASN A CG    1 
ATOM   2888  O  OD1   . ASN A 1 437 ? 105.796 145.009 138.660 1.00 112.92 ? 437  ASN A OD1   1 
ATOM   2889  N  ND2   . ASN A 1 437 ? 105.654 147.237 138.454 1.00 108.47 ? 437  ASN A ND2   1 
ATOM   2890  N  N     . ILE A 1 438 ? 103.513 145.166 134.127 1.00 100.40 ? 438  ILE A N     1 
ATOM   2891  C  CA    . ILE A 1 438 ? 102.351 145.008 133.262 1.00 101.92 ? 438  ILE A CA    1 
ATOM   2892  C  C     . ILE A 1 438 ? 102.441 143.676 132.532 1.00 107.69 ? 438  ILE A C     1 
ATOM   2893  O  O     . ILE A 1 438 ? 101.712 142.735 132.865 1.00 114.22 ? 438  ILE A O     1 
ATOM   2894  C  CB    . ILE A 1 438 ? 102.247 146.178 132.268 1.00 98.07  ? 438  ILE A CB    1 
ATOM   2895  C  CG1   . ILE A 1 438 ? 101.876 147.466 133.001 1.00 106.26 ? 438  ILE A CG1   1 
ATOM   2896  C  CG2   . ILE A 1 438 ? 101.218 145.878 131.197 1.00 100.54 ? 438  ILE A CG2   1 
ATOM   2897  C  CD1   . ILE A 1 438 ? 101.734 148.661 132.094 1.00 111.72 ? 438  ILE A CD1   1 
ATOM   2898  N  N     . LEU A 1 439 ? 103.430 143.536 131.647 1.00 101.55 ? 439  LEU A N     1 
ATOM   2899  C  CA    . LEU A 1 439 ? 103.486 142.364 130.781 1.00 102.60 ? 439  LEU A CA    1 
ATOM   2900  C  C     . LEU A 1 439 ? 103.676 141.084 131.587 1.00 108.55 ? 439  LEU A C     1 
ATOM   2901  O  O     . LEU A 1 439 ? 102.794 140.214 131.617 1.00 116.20 ? 439  LEU A O     1 
ATOM   2902  C  CB    . LEU A 1 439 ? 104.609 142.534 129.757 1.00 102.52 ? 439  LEU A CB    1 
ATOM   2903  C  CG    . LEU A 1 439 ? 104.216 143.068 128.379 1.00 100.32 ? 439  LEU A CG    1 
ATOM   2904  C  CD1   . LEU A 1 439 ? 103.513 144.403 128.499 1.00 104.68 ? 439  LEU A CD1   1 
ATOM   2905  C  CD2   . LEU A 1 439 ? 105.437 143.193 127.489 1.00 102.23 ? 439  LEU A CD2   1 
ATOM   2906  N  N     . ASP A 1 440 ? 104.827 140.952 132.254 1.00 101.84 ? 440  ASP A N     1 
ATOM   2907  C  CA    . ASP A 1 440 ? 105.172 139.679 132.871 1.00 103.53 ? 440  ASP A CA    1 
ATOM   2908  C  C     . ASP A 1 440 ? 104.211 139.330 133.999 1.00 105.86 ? 440  ASP A C     1 
ATOM   2909  O  O     . ASP A 1 440 ? 103.725 138.197 134.076 1.00 111.33 ? 440  ASP A O     1 
ATOM   2910  C  CB    . ASP A 1 440 ? 106.609 139.721 133.383 1.00 109.21 ? 440  ASP A CB    1 
ATOM   2911  C  CG    . ASP A 1 440 ? 107.611 139.289 132.337 1.00 118.12 ? 440  ASP A CG    1 
ATOM   2912  O  OD1   . ASP A 1 440 ? 107.526 138.130 131.880 1.00 122.14 ? 440  ASP A OD1   1 
ATOM   2913  O  OD2   . ASP A 1 440 ? 108.481 140.104 131.969 1.00 117.96 ? 440  ASP A OD2   1 
ATOM   2914  N  N     . LYS A 1 441 ? 103.942 140.276 134.904 1.00 102.61 ? 441  LYS A N     1 
ATOM   2915  C  CA    . LYS A 1 441 ? 103.102 139.961 136.047 1.00 102.33 ? 441  LYS A CA    1 
ATOM   2916  C  C     . LYS A 1 441 ? 101.661 139.709 135.629 1.00 104.09 ? 441  LYS A C     1 
ATOM   2917  O  O     . LYS A 1 441 ? 100.993 138.860 136.220 1.00 109.28 ? 441  LYS A O     1 
ATOM   2918  C  CB    . LYS A 1 441 ? 103.180 141.083 137.077 1.00 103.56 ? 441  LYS A CB    1 
ATOM   2919  C  CG    . LYS A 1 441 ? 104.562 141.258 137.668 1.00 101.41 ? 441  LYS A CG    1 
ATOM   2920  C  CD    . LYS A 1 441 ? 105.083 139.953 138.232 1.00 106.54 ? 441  LYS A CD    1 
ATOM   2921  C  CE    . LYS A 1 441 ? 106.403 140.162 138.945 1.00 118.54 ? 441  LYS A CE    1 
ATOM   2922  N  NZ    . LYS A 1 441 ? 106.289 141.210 139.994 1.00 117.75 ? 441  LYS A NZ    1 
ATOM   2923  N  N     . SER A 1 442 ? 101.151 140.422 134.618 1.00 97.53  ? 442  SER A N     1 
ATOM   2924  C  CA    . SER A 1 442 ? 99.806  140.125 134.146 1.00 103.45 ? 442  SER A CA    1 
ATOM   2925  C  C     . SER A 1 442 ? 99.741  138.726 133.549 1.00 108.02 ? 442  SER A C     1 
ATOM   2926  O  O     . SER A 1 442 ? 98.819  137.952 133.844 1.00 111.00 ? 442  SER A O     1 
ATOM   2927  C  CB    . SER A 1 442 ? 99.373  141.176 133.128 1.00 105.11 ? 442  SER A CB    1 
ATOM   2928  O  OG    . SER A 1 442 ? 99.373  142.467 133.710 1.00 113.31 ? 442  SER A OG    1 
ATOM   2929  N  N     . LEU A 1 443 ? 100.734 138.370 132.729 1.00 106.85 ? 443  LEU A N     1 
ATOM   2930  C  CA    . LEU A 1 443 ? 100.752 137.035 132.142 1.00 102.82 ? 443  LEU A CA    1 
ATOM   2931  C  C     . LEU A 1 443 ? 100.846 135.960 133.217 1.00 103.43 ? 443  LEU A C     1 
ATOM   2932  O  O     . LEU A 1 443 ? 100.184 134.921 133.127 1.00 105.45 ? 443  LEU A O     1 
ATOM   2933  C  CB    . LEU A 1 443 ? 101.912 136.914 131.158 1.00 96.63  ? 443  LEU A CB    1 
ATOM   2934  C  CG    . LEU A 1 443 ? 102.206 135.518 130.618 1.00 95.21  ? 443  LEU A CG    1 
ATOM   2935  C  CD1   . LEU A 1 443 ? 101.006 134.958 129.884 1.00 97.63  ? 443  LEU A CD1   1 
ATOM   2936  C  CD2   . LEU A 1 443 ? 103.397 135.585 129.698 1.00 96.87  ? 443  LEU A CD2   1 
ATOM   2937  N  N     . GLU A 1 444 ? 101.660 136.195 134.245 1.00 100.12 ? 444  GLU A N     1 
ATOM   2938  C  CA    . GLU A 1 444 ? 101.846 135.191 135.286 1.00 101.75 ? 444  GLU A CA    1 
ATOM   2939  C  C     . GLU A 1 444 ? 100.624 135.088 136.193 1.00 103.91 ? 444  GLU A C     1 
ATOM   2940  O  O     . GLU A 1 444 ? 100.232 133.985 136.589 1.00 109.36 ? 444  GLU A O     1 
ATOM   2941  C  CB    . GLU A 1 444 ? 103.100 135.515 136.094 1.00 104.80 ? 444  GLU A CB    1 
ATOM   2942  C  CG    . GLU A 1 444 ? 104.362 134.891 135.529 1.00 107.74 ? 444  GLU A CG    1 
ATOM   2943  C  CD    . GLU A 1 444 ? 105.614 135.642 135.928 1.00 122.04 ? 444  GLU A CD    1 
ATOM   2944  O  OE1   . GLU A 1 444 ? 105.725 136.837 135.591 1.00 127.85 ? 444  GLU A OE1   1 
ATOM   2945  O  OE2   . GLU A 1 444 ? 106.491 135.036 136.578 1.00 122.33 ? 444  GLU A OE2   1 
ATOM   2946  N  N     . SER A 1 445 ? 100.008 136.222 136.534 1.00 96.85  ? 445  SER A N     1 
ATOM   2947  C  CA    . SER A 1 445 ? 98.805  136.211 137.354 1.00 96.59  ? 445  SER A CA    1 
ATOM   2948  C  C     . SER A 1 445 ? 97.612  135.627 136.620 1.00 100.56 ? 445  SER A C     1 
ATOM   2949  O  O     . SER A 1 445 ? 96.673  135.156 137.271 1.00 99.39  ? 445  SER A O     1 
ATOM   2950  C  CB    . SER A 1 445 ? 98.473  137.625 137.823 1.00 102.45 ? 445  SER A CB    1 
ATOM   2951  O  OG    . SER A 1 445 ? 97.170  137.676 138.372 1.00 107.52 ? 445  SER A OG    1 
ATOM   2952  N  N     . CYS A 1 446 ? 97.614  135.661 135.286 1.00 101.17 ? 446  CYS A N     1 
ATOM   2953  C  CA    . CYS A 1 446 ? 96.587  134.934 134.550 1.00 100.66 ? 446  CYS A CA    1 
ATOM   2954  C  C     . CYS A 1 446 ? 96.671  133.442 134.834 1.00 103.34 ? 446  CYS A C     1 
ATOM   2955  O  O     . CYS A 1 446 ? 95.645  132.770 134.981 1.00 105.84 ? 446  CYS A O     1 
ATOM   2956  C  CB    . CYS A 1 446 ? 96.720  135.200 133.053 1.00 95.61  ? 446  CYS A CB    1 
ATOM   2957  S  SG    . CYS A 1 446 ? 95.986  136.746 132.524 1.00 110.93 ? 446  CYS A SG    1 
ATOM   2958  N  N     . PHE A 1 447 ? 97.885  132.911 134.923 1.00 100.26 ? 447  PHE A N     1 
ATOM   2959  C  CA    . PHE A 1 447 ? 98.105  131.487 135.118 1.00 95.81  ? 447  PHE A CA    1 
ATOM   2960  C  C     . PHE A 1 447 ? 98.348  131.116 136.573 1.00 97.09  ? 447  PHE A C     1 
ATOM   2961  O  O     . PHE A 1 447 ? 98.635  129.951 136.860 1.00 102.02 ? 447  PHE A O     1 
ATOM   2962  C  CB    . PHE A 1 447 ? 99.279  131.032 134.251 1.00 94.45  ? 447  PHE A CB    1 
ATOM   2963  C  CG    . PHE A 1 447 ? 98.928  130.894 132.800 1.00 101.15 ? 447  PHE A CG    1 
ATOM   2964  C  CD1   . PHE A 1 447 ? 97.608  130.764 132.406 1.00 108.71 ? 447  PHE A CD1   1 
ATOM   2965  C  CD2   . PHE A 1 447 ? 99.910  130.897 131.832 1.00 97.79  ? 447  PHE A CD2   1 
ATOM   2966  C  CE1   . PHE A 1 447 ? 97.277  130.639 131.075 1.00 107.73 ? 447  PHE A CE1   1 
ATOM   2967  C  CE2   . PHE A 1 447 ? 99.586  130.772 130.501 1.00 101.80 ? 447  PHE A CE2   1 
ATOM   2968  C  CZ    . PHE A 1 447 ? 98.268  130.643 130.121 1.00 108.38 ? 447  PHE A CZ    1 
ATOM   2969  N  N     . GLY A 1 448 ? 98.237  132.070 137.490 1.00 100.61 ? 448  GLY A N     1 
ATOM   2970  C  CA    . GLY A 1 448 ? 98.316  131.778 138.912 1.00 104.53 ? 448  GLY A CA    1 
ATOM   2971  C  C     . GLY A 1 448 ? 99.662  131.309 139.418 1.00 102.32 ? 448  GLY A C     1 
ATOM   2972  O  O     . GLY A 1 448 ? 99.718  130.403 140.257 1.00 108.26 ? 448  GLY A O     1 
ATOM   2973  N  N     . PHE A 1 449 ? 100.749 131.899 138.931 1.00 98.42  ? 449  PHE A N     1 
ATOM   2974  C  CA    . PHE A 1 449 ? 102.080 131.611 139.454 1.00 102.80 ? 449  PHE A CA    1 
ATOM   2975  C  C     . PHE A 1 449 ? 102.972 132.796 139.134 1.00 111.29 ? 449  PHE A C     1 
ATOM   2976  O  O     . PHE A 1 449 ? 103.198 133.092 137.959 1.00 113.37 ? 449  PHE A O     1 
ATOM   2977  C  CB    . PHE A 1 449 ? 102.654 130.330 138.852 1.00 100.31 ? 449  PHE A CB    1 
ATOM   2978  C  CG    . PHE A 1 449 ? 104.135 130.182 139.045 1.00 106.21 ? 449  PHE A CG    1 
ATOM   2979  C  CD1   . PHE A 1 449 ? 104.646 129.716 140.240 1.00 106.36 ? 449  PHE A CD1   1 
ATOM   2980  C  CD2   . PHE A 1 449 ? 105.017 130.504 138.030 1.00 109.60 ? 449  PHE A CD2   1 
ATOM   2981  C  CE1   . PHE A 1 449 ? 106.005 129.577 140.422 1.00 108.21 ? 449  PHE A CE1   1 
ATOM   2982  C  CE2   . PHE A 1 449 ? 106.377 130.368 138.207 1.00 108.31 ? 449  PHE A CE2   1 
ATOM   2983  C  CZ    . PHE A 1 449 ? 106.871 129.903 139.403 1.00 108.49 ? 449  PHE A CZ    1 
ATOM   2984  N  N     . ILE A 1 450 ? 103.489 133.458 140.165 1.00 113.44 ? 450  ILE A N     1 
ATOM   2985  C  CA    . ILE A 1 450 ? 104.224 134.704 140.004 1.00 109.46 ? 450  ILE A CA    1 
ATOM   2986  C  C     . ILE A 1 450 ? 105.611 134.557 140.609 1.00 117.47 ? 450  ILE A C     1 
ATOM   2987  O  O     . ILE A 1 450 ? 105.756 134.112 141.752 1.00 125.23 ? 450  ILE A O     1 
ATOM   2988  C  CB    . ILE A 1 450 ? 103.480 135.885 140.657 1.00 106.33 ? 450  ILE A CB    1 
ATOM   2989  C  CG1   . ILE A 1 450 ? 102.293 136.300 139.798 1.00 111.15 ? 450  ILE A CG1   1 
ATOM   2990  C  CG2   . ILE A 1 450 ? 104.412 137.060 140.856 1.00 107.86 ? 450  ILE A CG2   1 
ATOM   2991  C  CD1   . ILE A 1 450 ? 101.471 137.387 140.417 1.00 112.82 ? 450  ILE A CD1   1 
ATOM   2992  N  N     . SER A 1 451 ? 106.628 134.932 139.839 1.00 121.52 ? 451  SER A N     1 
ATOM   2993  C  CA    . SER A 1 451 ? 107.988 135.073 140.344 1.00 127.21 ? 451  SER A CA    1 
ATOM   2994  C  C     . SER A 1 451 ? 108.116 136.484 140.905 1.00 126.81 ? 451  SER A C     1 
ATOM   2995  O  O     . SER A 1 451 ? 108.304 137.443 140.150 1.00 124.98 ? 451  SER A O     1 
ATOM   2996  C  CB    . SER A 1 451 ? 109.013 134.817 139.243 1.00 130.24 ? 451  SER A CB    1 
ATOM   2997  O  OG    . SER A 1 451 ? 108.871 133.513 138.707 1.00 130.06 ? 451  SER A OG    1 
ATOM   2998  N  N     . VAL A 1 452 ? 108.007 136.607 142.228 1.00 127.20 ? 452  VAL A N     1 
ATOM   2999  C  CA    . VAL A 1 452 ? 107.933 137.918 142.863 1.00 128.20 ? 452  VAL A CA    1 
ATOM   3000  C  C     . VAL A 1 452 ? 109.226 138.683 142.622 1.00 134.00 ? 452  VAL A C     1 
ATOM   3001  O  O     . VAL A 1 452 ? 110.327 138.147 142.794 1.00 135.76 ? 452  VAL A O     1 
ATOM   3002  C  CB    . VAL A 1 452 ? 107.645 137.774 144.364 1.00 121.27 ? 452  VAL A CB    1 
ATOM   3003  C  CG1   . VAL A 1 452 ? 107.510 139.141 145.008 1.00 121.47 ? 452  VAL A CG1   1 
ATOM   3004  C  CG2   . VAL A 1 452 ? 106.383 136.961 144.583 1.00 116.00 ? 452  VAL A CG2   1 
ATOM   3005  N  N     . LEU A 1 453 ? 109.093 139.940 142.209 1.00 135.37 ? 453  LEU A N     1 
ATOM   3006  C  CA    . LEU A 1 453 ? 110.255 140.799 142.053 1.00 137.19 ? 453  LEU A CA    1 
ATOM   3007  C  C     . LEU A 1 453 ? 110.918 141.023 143.409 1.00 138.19 ? 453  LEU A C     1 
ATOM   3008  O  O     . LEU A 1 453 ? 110.227 141.228 144.412 1.00 136.20 ? 453  LEU A O     1 
ATOM   3009  C  CB    . LEU A 1 453 ? 109.854 142.142 141.445 1.00 136.46 ? 453  LEU A CB    1 
ATOM   3010  C  CG    . LEU A 1 453 ? 109.620 142.199 139.936 1.00 133.29 ? 453  LEU A CG    1 
ATOM   3011  C  CD1   . LEU A 1 453 ? 109.171 143.591 139.522 1.00 119.90 ? 453  LEU A CD1   1 
ATOM   3012  C  CD2   . LEU A 1 453 ? 110.876 141.793 139.187 1.00 130.46 ? 453  LEU A CD2   1 
ATOM   3013  N  N     . PRO A 1 454 ? 112.247 140.972 143.479 1.00 139.44 ? 454  PRO A N     1 
ATOM   3014  C  CA    . PRO A 1 454 ? 112.922 141.224 144.756 1.00 136.47 ? 454  PRO A CA    1 
ATOM   3015  C  C     . PRO A 1 454 ? 112.663 142.640 145.247 1.00 133.22 ? 454  PRO A C     1 
ATOM   3016  O  O     . PRO A 1 454 ? 112.632 143.595 144.467 1.00 126.32 ? 454  PRO A O     1 
ATOM   3017  C  CB    . PRO A 1 454 ? 114.402 140.997 144.426 1.00 131.46 ? 454  PRO A CB    1 
ATOM   3018  C  CG    . PRO A 1 454 ? 114.494 141.176 142.953 1.00 133.50 ? 454  PRO A CG    1 
ATOM   3019  C  CD    . PRO A 1 454 ? 113.197 140.688 142.393 1.00 135.88 ? 454  PRO A CD    1 
ATOM   3020  N  N     . GLY A 1 455 ? 112.472 142.766 146.557 1.00 132.99 ? 455  GLY A N     1 
ATOM   3021  C  CA    . GLY A 1 455 ? 112.165 144.039 147.171 1.00 131.53 ? 455  GLY A CA    1 
ATOM   3022  C  C     . GLY A 1 455 ? 110.725 144.480 147.048 1.00 131.70 ? 455  GLY A C     1 
ATOM   3023  O  O     . GLY A 1 455 ? 110.353 145.494 147.652 1.00 128.98 ? 455  GLY A O     1 
ATOM   3024  N  N     . ALA A 1 456 ? 109.901 143.756 146.295 1.00 130.02 ? 456  ALA A N     1 
ATOM   3025  C  CA    . ALA A 1 456 ? 108.513 144.137 146.106 1.00 120.81 ? 456  ALA A CA    1 
ATOM   3026  C  C     . ALA A 1 456 ? 107.714 143.896 147.383 1.00 112.14 ? 456  ALA A C     1 
ATOM   3027  O  O     . ALA A 1 456 ? 108.062 143.062 148.222 1.00 108.00 ? 456  ALA A O     1 
ATOM   3028  C  CB    . ALA A 1 456 ? 107.897 143.368 144.939 1.00 116.20 ? 456  ALA A CB    1 
ATOM   3029  N  N     . PHE A 1 457 ? 106.628 144.646 147.524 1.00 107.37 ? 457  PHE A N     1 
ATOM   3030  C  CA    . PHE A 1 457 ? 105.734 144.523 148.668 1.00 99.11  ? 457  PHE A CA    1 
ATOM   3031  C  C     . PHE A 1 457 ? 104.822 143.328 148.421 1.00 99.69  ? 457  PHE A C     1 
ATOM   3032  O  O     . PHE A 1 457 ? 103.790 143.452 147.755 1.00 105.68 ? 457  PHE A O     1 
ATOM   3033  C  CB    . PHE A 1 457 ? 104.938 145.809 148.870 1.00 94.12  ? 457  PHE A CB    1 
ATOM   3034  C  CG    . PHE A 1 457 ? 103.716 145.640 149.717 1.00 94.76  ? 457  PHE A CG    1 
ATOM   3035  C  CD1   . PHE A 1 457 ? 103.822 145.255 151.040 1.00 97.51  ? 457  PHE A CD1   1 
ATOM   3036  C  CD2   . PHE A 1 457 ? 102.461 145.879 149.195 1.00 98.65  ? 457  PHE A CD2   1 
ATOM   3037  C  CE1   . PHE A 1 457 ? 102.700 145.103 151.823 1.00 103.18 ? 457  PHE A CE1   1 
ATOM   3038  C  CE2   . PHE A 1 457 ? 101.338 145.732 149.973 1.00 103.24 ? 457  PHE A CE2   1 
ATOM   3039  C  CZ    . PHE A 1 457 ? 101.457 145.342 151.289 1.00 106.32 ? 457  PHE A CZ    1 
ATOM   3040  N  N     . SER A 1 458 ? 105.212 142.171 148.943 1.00 92.86  ? 458  SER A N     1 
ATOM   3041  C  CA    . SER A 1 458 ? 104.476 140.933 148.755 1.00 91.66  ? 458  SER A CA    1 
ATOM   3042  C  C     . SER A 1 458 ? 103.845 140.502 150.070 1.00 88.27  ? 458  SER A C     1 
ATOM   3043  O  O     . SER A 1 458 ? 104.368 140.761 151.155 1.00 92.13  ? 458  SER A O     1 
ATOM   3044  C  CB    . SER A 1 458 ? 105.388 139.827 148.213 1.00 96.25  ? 458  SER A CB    1 
ATOM   3045  O  OG    . SER A 1 458 ? 106.515 139.646 149.049 1.00 99.66  ? 458  SER A OG    1 
ATOM   3046  N  N     . ALA A 1 459 ? 102.701 139.834 149.961 1.00 87.18  ? 459  ALA A N     1 
ATOM   3047  C  CA    . ALA A 1 459 ? 101.980 139.366 151.133 1.00 82.22  ? 459  ALA A CA    1 
ATOM   3048  C  C     . ALA A 1 459 ? 101.491 137.950 150.886 1.00 88.28  ? 459  ALA A C     1 
ATOM   3049  O  O     . ALA A 1 459 ? 101.176 137.574 149.755 1.00 99.58  ? 459  ALA A O     1 
ATOM   3050  C  CB    . ALA A 1 459 ? 100.797 140.275 151.472 1.00 85.87  ? 459  ALA A CB    1 
ATOM   3051  N  N     . TYR A 1 460 ? 101.423 137.172 151.962 1.00 87.90  ? 460  TYR A N     1 
ATOM   3052  C  CA    . TYR A 1 460 ? 100.926 135.807 151.917 1.00 89.70  ? 460  TYR A CA    1 
ATOM   3053  C  C     . TYR A 1 460 ? 99.888  135.642 153.014 1.00 90.68  ? 460  TYR A C     1 
ATOM   3054  O  O     . TYR A 1 460 ? 99.729  136.507 153.880 1.00 100.45 ? 460  TYR A O     1 
ATOM   3055  C  CB    . TYR A 1 460 ? 102.054 134.790 152.103 1.00 84.36  ? 460  TYR A CB    1 
ATOM   3056  C  CG    . TYR A 1 460 ? 103.266 135.020 151.236 1.00 87.83  ? 460  TYR A CG    1 
ATOM   3057  C  CD1   . TYR A 1 460 ? 104.291 135.854 151.653 1.00 90.08  ? 460  TYR A CD1   1 
ATOM   3058  C  CD2   . TYR A 1 460 ? 103.401 134.375 150.017 1.00 94.81  ? 460  TYR A CD2   1 
ATOM   3059  C  CE1   . TYR A 1 460 ? 105.406 136.057 150.870 1.00 99.79  ? 460  TYR A CE1   1 
ATOM   3060  C  CE2   . TYR A 1 460 ? 104.512 134.571 149.228 1.00 99.58  ? 460  TYR A CE2   1 
ATOM   3061  C  CZ    . TYR A 1 460 ? 105.511 135.413 149.659 1.00 106.35 ? 460  TYR A CZ    1 
ATOM   3062  O  OH    . TYR A 1 460 ? 106.621 135.613 148.875 1.00 113.84 ? 460  TYR A OH    1 
ATOM   3063  N  N     . ARG A 1 461 ? 99.180  134.521 152.985 1.00 83.46  ? 461  ARG A N     1 
ATOM   3064  C  CA    . ARG A 1 461 ? 98.303  134.139 154.078 1.00 93.38  ? 461  ARG A CA    1 
ATOM   3065  C  C     . ARG A 1 461 ? 98.942  132.984 154.833 1.00 100.08 ? 461  ARG A C     1 
ATOM   3066  O  O     . ARG A 1 461 ? 99.507  132.069 154.227 1.00 106.74 ? 461  ARG A O     1 
ATOM   3067  C  CB    . ARG A 1 461 ? 96.901  133.768 153.580 1.00 93.95  ? 461  ARG A CB    1 
ATOM   3068  C  CG    . ARG A 1 461 ? 96.765  132.403 152.947 1.00 98.30  ? 461  ARG A CG    1 
ATOM   3069  C  CD    . ARG A 1 461 ? 95.563  132.356 152.027 1.00 97.15  ? 461  ARG A CD    1 
ATOM   3070  N  NE    . ARG A 1 461 ? 94.361  132.850 152.685 1.00 95.44  ? 461  ARG A NE    1 
ATOM   3071  C  CZ    . ARG A 1 461 ? 93.339  133.411 152.054 1.00 100.17 ? 461  ARG A CZ    1 
ATOM   3072  N  NH1   . ARG A 1 461 ? 93.343  133.576 150.742 1.00 99.72  ? 461  ARG A NH1   1 
ATOM   3073  N  NH2   . ARG A 1 461 ? 92.287  133.818 152.757 1.00 106.45 ? 461  ARG A NH2   1 
ATOM   3074  N  N     . TYR A 1 462 ? 98.884  133.047 156.161 1.00 101.74 ? 462  TYR A N     1 
ATOM   3075  C  CA    . TYR A 1 462 ? 99.597  132.075 156.977 1.00 104.90 ? 462  TYR A CA    1 
ATOM   3076  C  C     . TYR A 1 462 ? 98.803  130.783 157.106 1.00 110.31 ? 462  TYR A C     1 
ATOM   3077  O  O     . TYR A 1 462 ? 98.542  130.308 158.215 1.00 121.61 ? 462  TYR A O     1 
ATOM   3078  C  CB    . TYR A 1 462 ? 99.902  132.656 158.355 1.00 107.25 ? 462  TYR A CB    1 
ATOM   3079  C  CG    . TYR A 1 462 ? 101.178 132.122 158.947 1.00 105.71 ? 462  TYR A CG    1 
ATOM   3080  C  CD1   . TYR A 1 462 ? 102.403 132.432 158.383 1.00 104.09 ? 462  TYR A CD1   1 
ATOM   3081  C  CD2   . TYR A 1 462 ? 101.160 131.304 160.064 1.00 111.54 ? 462  TYR A CD2   1 
ATOM   3082  C  CE1   . TYR A 1 462 ? 103.575 131.945 158.914 1.00 112.93 ? 462  TYR A CE1   1 
ATOM   3083  C  CE2   . TYR A 1 462 ? 102.326 130.813 160.604 1.00 118.37 ? 462  TYR A CE2   1 
ATOM   3084  C  CZ    . TYR A 1 462 ? 103.531 131.135 160.024 1.00 121.34 ? 462  TYR A CZ    1 
ATOM   3085  O  OH    . TYR A 1 462 ? 104.700 130.648 160.557 1.00 125.53 ? 462  TYR A OH    1 
ATOM   3086  N  N     . GLU A 1 463 ? 98.412  130.219 155.968 1.00 106.21 ? 463  GLU A N     1 
ATOM   3087  C  CA    . GLU A 1 463 ? 97.771  128.915 155.907 1.00 108.53 ? 463  GLU A CA    1 
ATOM   3088  C  C     . GLU A 1 463 ? 98.436  128.123 154.793 1.00 112.77 ? 463  GLU A C     1 
ATOM   3089  O  O     . GLU A 1 463 ? 98.452  126.889 154.810 1.00 121.25 ? 463  GLU A O     1 
ATOM   3090  C  CB    . GLU A 1 463 ? 96.268  129.061 155.665 1.00 114.90 ? 463  GLU A CB    1 
ATOM   3091  C  CG    . GLU A 1 463 ? 95.459  127.798 155.899 1.00 123.96 ? 463  GLU A CG    1 
ATOM   3092  C  CD    . GLU A 1 463 ? 93.973  128.017 155.686 1.00 132.93 ? 463  GLU A CD    1 
ATOM   3093  O  OE1   . GLU A 1 463 ? 93.564  129.184 155.515 1.00 132.71 ? 463  GLU A OE1   1 
ATOM   3094  O  OE2   . GLU A 1 463 ? 93.215  127.025 155.688 1.00 137.31 ? 463  GLU A OE2   1 
ATOM   3095  N  N     . ALA A 1 464 ? 98.994  128.846 153.822 1.00 110.47 ? 464  ALA A N     1 
ATOM   3096  C  CA    . ALA A 1 464 ? 99.717  128.257 152.705 1.00 112.93 ? 464  ALA A CA    1 
ATOM   3097  C  C     . ALA A 1 464 ? 101.223 128.341 152.869 1.00 113.67 ? 464  ALA A C     1 
ATOM   3098  O  O     . ALA A 1 464 ? 101.957 127.946 151.958 1.00 121.68 ? 464  ALA A O     1 
ATOM   3099  C  CB    . ALA A 1 464 ? 99.326  128.952 151.400 1.00 109.76 ? 464  ALA A CB    1 
ATOM   3100  N  N     . ILE A 1 465 ? 101.694 128.857 153.995 1.00 107.40 ? 465  ILE A N     1 
ATOM   3101  C  CA    . ILE A 1 465 ? 103.109 129.075 154.241 1.00 109.42 ? 465  ILE A CA    1 
ATOM   3102  C  C     . ILE A 1 465 ? 103.551 128.405 155.544 1.00 118.06 ? 465  ILE A C     1 
ATOM   3103  O  O     . ILE A 1 465 ? 104.745 128.244 155.788 1.00 118.08 ? 465  ILE A O     1 
ATOM   3104  C  CB    . ILE A 1 465 ? 103.427 130.583 154.195 1.00 105.43 ? 465  ILE A CB    1 
ATOM   3105  C  CG1   . ILE A 1 465 ? 104.028 130.953 152.840 1.00 102.83 ? 465  ILE A CG1   1 
ATOM   3106  C  CG2   . ILE A 1 465 ? 104.268 131.071 155.355 1.00 109.93 ? 465  ILE A CG2   1 
ATOM   3107  C  CD1   . ILE A 1 465 ? 104.579 132.344 152.799 1.00 104.79 ? 465  ILE A CD1   1 
ATOM   3108  N  N     . ARG A 1 466 ? 102.585 127.905 156.319 1.00 119.30 ? 466  ARG A N     1 
ATOM   3109  C  CA    . ARG A 1 466 ? 102.832 127.438 157.681 1.00 117.55 ? 466  ARG A CA    1 
ATOM   3110  C  C     . ARG A 1 466 ? 104.003 126.463 157.757 1.00 120.71 ? 466  ARG A C     1 
ATOM   3111  O  O     . ARG A 1 466 ? 104.906 126.632 158.584 1.00 123.06 ? 466  ARG A O     1 
ATOM   3112  C  CB    . ARG A 1 466 ? 101.559 126.789 158.225 1.00 120.87 ? 466  ARG A CB    1 
ATOM   3113  C  CG    . ARG A 1 466 ? 101.653 126.266 159.644 1.00 123.96 ? 466  ARG A CG    1 
ATOM   3114  C  CD    . ARG A 1 466 ? 101.690 127.384 160.662 1.00 123.08 ? 466  ARG A CD    1 
ATOM   3115  N  NE    . ARG A 1 466 ? 101.095 126.970 161.927 1.00 129.92 ? 466  ARG A NE    1 
ATOM   3116  C  CZ    . ARG A 1 466 ? 101.727 126.270 162.857 1.00 129.84 ? 466  ARG A CZ    1 
ATOM   3117  N  NH1   . ARG A 1 466 ? 102.977 125.873 162.692 1.00 131.34 ? 466  ARG A NH1   1 
ATOM   3118  N  NH2   . ARG A 1 466 ? 101.086 125.954 163.979 1.00 127.33 ? 466  ARG A NH2   1 
ATOM   3119  N  N     . GLY A 1 467 ? 104.016 125.446 156.902 1.00 120.25 ? 467  GLY A N     1 
ATOM   3120  C  CA    . GLY A 1 467 ? 104.981 124.372 157.058 1.00 119.97 ? 467  GLY A CA    1 
ATOM   3121  C  C     . GLY A 1 467 ? 106.029 124.231 155.973 1.00 118.56 ? 467  GLY A C     1 
ATOM   3122  O  O     . GLY A 1 467 ? 107.058 124.917 155.989 1.00 117.37 ? 467  GLY A O     1 
ATOM   3123  N  N     . ALA A 1 468 ? 105.776 123.313 155.041 1.00 121.03 ? 468  ALA A N     1 
ATOM   3124  C  CA    . ALA A 1 468 ? 106.768 122.977 154.023 1.00 118.85 ? 468  ALA A CA    1 
ATOM   3125  C  C     . ALA A 1 468 ? 107.260 124.169 153.210 1.00 117.54 ? 468  ALA A C     1 
ATOM   3126  O  O     . ALA A 1 468 ? 108.468 124.213 152.914 1.00 121.15 ? 468  ALA A O     1 
ATOM   3127  C  CB    . ALA A 1 468 ? 106.206 121.888 153.100 1.00 116.69 ? 468  ALA A CB    1 
ATOM   3128  N  N     . PRO A 1 469 ? 106.421 125.120 152.779 1.00 114.61 ? 469  PRO A N     1 
ATOM   3129  C  CA    . PRO A 1 469 ? 106.976 126.289 152.078 1.00 113.04 ? 469  PRO A CA    1 
ATOM   3130  C  C     . PRO A 1 469 ? 108.010 127.047 152.890 1.00 117.33 ? 469  PRO A C     1 
ATOM   3131  O  O     . PRO A 1 469 ? 109.078 127.374 152.362 1.00 118.75 ? 469  PRO A O     1 
ATOM   3132  C  CB    . PRO A 1 469 ? 105.736 127.143 151.797 1.00 112.31 ? 469  PRO A CB    1 
ATOM   3133  C  CG    . PRO A 1 469 ? 104.644 126.163 151.684 1.00 113.29 ? 469  PRO A CG    1 
ATOM   3134  C  CD    . PRO A 1 469 ? 104.949 125.098 152.697 1.00 114.77 ? 469  PRO A CD    1 
ATOM   3135  N  N     . LEU A 1 470 ? 107.740 127.319 154.170 1.00 118.95 ? 470  LEU A N     1 
ATOM   3136  C  CA    . LEU A 1 470 ? 108.725 128.036 154.973 1.00 115.14 ? 470  LEU A CA    1 
ATOM   3137  C  C     . LEU A 1 470 ? 109.957 127.182 155.231 1.00 120.81 ? 470  LEU A C     1 
ATOM   3138  O  O     . LEU A 1 470 ? 111.074 127.709 155.294 1.00 120.89 ? 470  LEU A O     1 
ATOM   3139  C  CB    . LEU A 1 470 ? 108.140 128.473 156.314 1.00 109.25 ? 470  LEU A CB    1 
ATOM   3140  C  CG    . LEU A 1 470 ? 107.506 129.857 156.439 1.00 107.13 ? 470  LEU A CG    1 
ATOM   3141  C  CD1   . LEU A 1 470 ? 106.567 129.881 157.641 1.00 115.66 ? 470  LEU A CD1   1 
ATOM   3142  C  CD2   . LEU A 1 470 ? 108.512 130.976 156.492 1.00 109.90 ? 470  LEU A CD2   1 
ATOM   3143  N  N     . ASP A 1 471 ? 109.770 125.873 155.415 1.00 123.49 ? 471  ASP A N     1 
ATOM   3144  C  CA    . ASP A 1 471 ? 110.914 124.992 155.618 1.00 122.18 ? 471  ASP A CA    1 
ATOM   3145  C  C     . ASP A 1 471 ? 111.837 125.014 154.408 1.00 123.65 ? 471  ASP A C     1 
ATOM   3146  O  O     . ASP A 1 471 ? 113.061 125.117 154.550 1.00 125.49 ? 471  ASP A O     1 
ATOM   3147  C  CB    . ASP A 1 471 ? 110.434 123.571 155.907 1.00 125.28 ? 471  ASP A CB    1 
ATOM   3148  C  CG    . ASP A 1 471 ? 110.428 123.249 157.387 1.00 134.81 ? 471  ASP A CG    1 
ATOM   3149  O  OD1   . ASP A 1 471 ? 110.403 124.195 158.202 1.00 136.35 ? 471  ASP A OD1   1 
ATOM   3150  O  OD2   . ASP A 1 471 ? 110.444 122.050 157.737 1.00 142.34 ? 471  ASP A OD2   1 
ATOM   3151  N  N     . ALA A 1 472 ? 111.267 124.937 153.205 1.00 122.96 ? 472  ALA A N     1 
ATOM   3152  C  CA    . ALA A 1 472 ? 112.074 125.067 151.997 1.00 119.38 ? 472  ALA A CA    1 
ATOM   3153  C  C     . ALA A 1 472 ? 112.716 126.445 151.918 1.00 119.33 ? 472  ALA A C     1 
ATOM   3154  O  O     . ALA A 1 472 ? 113.882 126.571 151.533 1.00 127.06 ? 472  ALA A O     1 
ATOM   3155  C  CB    . ALA A 1 472 ? 111.221 124.799 150.759 1.00 116.91 ? 472  ALA A CB    1 
ATOM   3156  N  N     . TYR A 1 473 ? 111.968 127.487 152.289 1.00 116.11 ? 473  TYR A N     1 
ATOM   3157  C  CA    . TYR A 1 473 ? 112.493 128.848 152.268 1.00 116.00 ? 473  TYR A CA    1 
ATOM   3158  C  C     . TYR A 1 473 ? 113.757 128.970 153.112 1.00 117.87 ? 473  TYR A C     1 
ATOM   3159  O  O     . TYR A 1 473 ? 114.760 129.537 152.665 1.00 115.90 ? 473  TYR A O     1 
ATOM   3160  C  CB    . TYR A 1 473 ? 111.413 129.806 152.774 1.00 116.27 ? 473  TYR A CB    1 
ATOM   3161  C  CG    . TYR A 1 473 ? 111.707 131.282 152.632 1.00 113.12 ? 473  TYR A CG    1 
ATOM   3162  C  CD1   . TYR A 1 473 ? 112.677 131.745 151.762 1.00 113.75 ? 473  TYR A CD1   1 
ATOM   3163  C  CD2   . TYR A 1 473 ? 111.012 132.214 153.389 1.00 113.10 ? 473  TYR A CD2   1 
ATOM   3164  C  CE1   . TYR A 1 473 ? 112.935 133.096 151.640 1.00 114.27 ? 473  TYR A CE1   1 
ATOM   3165  C  CE2   . TYR A 1 473 ? 111.265 133.561 153.274 1.00 112.05 ? 473  TYR A CE2   1 
ATOM   3166  C  CZ    . TYR A 1 473 ? 112.229 133.998 152.400 1.00 110.69 ? 473  TYR A CZ    1 
ATOM   3167  O  OH    . TYR A 1 473 ? 112.486 135.343 152.283 1.00 111.56 ? 473  TYR A OH    1 
ATOM   3168  N  N     . PHE A 1 474 ? 113.728 128.441 154.334 1.00 121.06 ? 474  PHE A N     1 
ATOM   3169  C  CA    . PHE A 1 474 ? 114.834 128.572 155.275 1.00 119.59 ? 474  PHE A CA    1 
ATOM   3170  C  C     . PHE A 1 474 ? 115.732 127.343 155.315 1.00 125.26 ? 474  PHE A C     1 
ATOM   3171  O  O     . PHE A 1 474 ? 116.479 127.166 156.285 1.00 127.29 ? 474  PHE A O     1 
ATOM   3172  C  CB    . PHE A 1 474 ? 114.305 128.868 156.677 1.00 116.28 ? 474  PHE A CB    1 
ATOM   3173  C  CG    . PHE A 1 474 ? 113.502 130.123 156.760 1.00 108.70 ? 474  PHE A CG    1 
ATOM   3174  C  CD1   . PHE A 1 474 ? 113.915 131.264 156.103 1.00 110.33 ? 474  PHE A CD1   1 
ATOM   3175  C  CD2   . PHE A 1 474 ? 112.339 130.167 157.498 1.00 107.41 ? 474  PHE A CD2   1 
ATOM   3176  C  CE1   . PHE A 1 474 ? 113.178 132.422 156.175 1.00 111.66 ? 474  PHE A CE1   1 
ATOM   3177  C  CE2   . PHE A 1 474 ? 111.607 131.324 157.579 1.00 108.26 ? 474  PHE A CE2   1 
ATOM   3178  C  CZ    . PHE A 1 474 ? 112.019 132.450 156.909 1.00 107.50 ? 474  PHE A CZ    1 
ATOM   3179  N  N     . GLN A 1 475 ? 115.627 126.464 154.317 1.00 129.04 ? 475  GLN A N     1 
ATOM   3180  C  CA    . GLN A 1 475 ? 116.552 125.342 154.202 1.00 130.13 ? 475  GLN A CA    1 
ATOM   3181  C  C     . GLN A 1 475 ? 118.005 125.800 154.215 1.00 131.36 ? 475  GLN A C     1 
ATOM   3182  O  O     . GLN A 1 475 ? 118.873 125.110 154.760 1.00 136.60 ? 475  GLN A O     1 
ATOM   3183  C  CB    . GLN A 1 475 ? 116.243 124.561 152.926 1.00 132.33 ? 475  GLN A CB    1 
ATOM   3184  C  CG    . GLN A 1 475 ? 117.110 123.344 152.696 1.00 138.70 ? 475  GLN A CG    1 
ATOM   3185  C  CD    . GLN A 1 475 ? 116.625 122.515 151.525 1.00 148.11 ? 475  GLN A CD    1 
ATOM   3186  O  OE1   . GLN A 1 475 ? 117.401 121.794 150.899 1.00 156.69 ? 475  GLN A OE1   1 
ATOM   3187  N  NE2   . GLN A 1 475 ? 115.338 122.612 151.221 1.00 143.84 ? 475  GLN A NE2   1 
ATOM   3188  N  N     . THR A 1 476 ? 118.292 126.963 153.626 1.00 129.96 ? 476  THR A N     1 
ATOM   3189  C  CA    . THR A 1 476 ? 119.667 127.455 153.601 1.00 133.36 ? 476  THR A CA    1 
ATOM   3190  C  C     . THR A 1 476 ? 120.185 127.726 155.008 1.00 133.12 ? 476  THR A C     1 
ATOM   3191  O  O     . THR A 1 476 ? 121.338 127.412 155.326 1.00 134.77 ? 476  THR A O     1 
ATOM   3192  C  CB    . THR A 1 476 ? 119.760 128.714 152.741 1.00 135.70 ? 476  THR A CB    1 
ATOM   3193  O  OG1   . THR A 1 476 ? 119.630 128.354 151.362 1.00 141.61 ? 476  THR A OG1   1 
ATOM   3194  C  CG2   . THR A 1 476 ? 121.096 129.408 152.943 1.00 132.20 ? 476  THR A CG2   1 
ATOM   3195  N  N     . LEU A 1 477 ? 119.351 128.313 155.866 1.00 132.80 ? 477  LEU A N     1 
ATOM   3196  C  CA    . LEU A 1 477 ? 119.772 128.567 157.238 1.00 130.27 ? 477  LEU A CA    1 
ATOM   3197  C  C     . LEU A 1 477 ? 119.800 127.291 158.067 1.00 132.21 ? 477  LEU A C     1 
ATOM   3198  O  O     . LEU A 1 477 ? 120.716 127.097 158.872 1.00 131.91 ? 477  LEU A O     1 
ATOM   3199  C  CB    . LEU A 1 477 ? 118.847 129.593 157.886 1.00 125.16 ? 477  LEU A CB    1 
ATOM   3200  C  CG    . LEU A 1 477 ? 118.909 130.994 157.288 1.00 122.27 ? 477  LEU A CG    1 
ATOM   3201  C  CD1   . LEU A 1 477 ? 118.104 131.941 158.137 1.00 120.52 ? 477  LEU A CD1   1 
ATOM   3202  C  CD2   . LEU A 1 477 ? 120.346 131.465 157.179 1.00 123.98 ? 477  LEU A CD2   1 
ATOM   3203  N  N     . ASN A 1 478 ? 118.807 126.417 157.890 1.00 133.73 ? 478  ASN A N     1 
ATOM   3204  C  CA    . ASN A 1 478 ? 118.740 125.205 158.701 1.00 132.71 ? 478  ASN A CA    1 
ATOM   3205  C  C     . ASN A 1 478 ? 119.887 124.253 158.382 1.00 134.03 ? 478  ASN A C     1 
ATOM   3206  O  O     . ASN A 1 478 ? 120.478 123.660 159.292 1.00 134.84 ? 478  ASN A O     1 
ATOM   3207  C  CB    . ASN A 1 478 ? 117.394 124.514 158.499 1.00 132.65 ? 478  ASN A CB    1 
ATOM   3208  C  CG    . ASN A 1 478 ? 116.231 125.360 158.972 1.00 132.34 ? 478  ASN A CG    1 
ATOM   3209  O  OD1   . ASN A 1 478 ? 116.409 126.309 159.735 1.00 127.91 ? 478  ASN A OD1   1 
ATOM   3210  N  ND2   . ASN A 1 478 ? 115.031 125.020 158.521 1.00 135.13 ? 478  ASN A ND2   1 
ATOM   3211  N  N     . ILE A 1 479 ? 120.220 124.094 157.104 1.00 134.98 ? 479  ILE A N     1 
ATOM   3212  C  CA    . ILE A 1 479 ? 121.265 123.180 156.660 1.00 137.60 ? 479  ILE A CA    1 
ATOM   3213  C  C     . ILE A 1 479 ? 122.373 123.999 156.016 1.00 145.19 ? 479  ILE A C     1 
ATOM   3214  O  O     . ILE A 1 479 ? 122.110 124.802 155.115 1.00 148.32 ? 479  ILE A O     1 
ATOM   3215  C  CB    . ILE A 1 479 ? 120.719 122.132 155.676 1.00 135.26 ? 479  ILE A CB    1 
ATOM   3216  C  CG1   . ILE A 1 479 ? 119.599 121.325 156.331 1.00 134.47 ? 479  ILE A CG1   1 
ATOM   3217  C  CG2   . ILE A 1 479 ? 121.831 121.218 155.201 1.00 139.68 ? 479  ILE A CG2   1 
ATOM   3218  C  CD1   . ILE A 1 479 ? 118.972 120.303 155.416 1.00 135.65 ? 479  ILE A CD1   1 
ATOM   3219  N  N     . GLU A 1 480 ? 123.607 123.787 156.469 1.00 150.20 ? 480  GLU A N     1 
ATOM   3220  C  CA    . GLU A 1 480 ? 124.725 124.586 155.994 1.00 152.66 ? 480  GLU A CA    1 
ATOM   3221  C  C     . GLU A 1 480 ? 124.972 124.352 154.507 1.00 154.54 ? 480  GLU A C     1 
ATOM   3222  O  O     . GLU A 1 480 ? 124.622 123.313 153.940 1.00 152.94 ? 480  GLU A O     1 
ATOM   3223  C  CB    . GLU A 1 480 ? 125.991 124.279 156.795 1.00 154.29 ? 480  GLU A CB    1 
ATOM   3224  C  CG    . GLU A 1 480 ? 126.676 122.978 156.426 1.00 158.70 ? 480  GLU A CG    1 
ATOM   3225  C  CD    . GLU A 1 480 ? 126.071 121.779 157.129 1.00 161.03 ? 480  GLU A CD    1 
ATOM   3226  O  OE1   . GLU A 1 480 ? 126.844 120.905 157.569 1.00 165.28 ? 480  GLU A OE1   1 
ATOM   3227  O  OE2   . GLU A 1 480 ? 124.829 121.705 157.238 1.00 157.42 ? 480  GLU A OE2   1 
ATOM   3228  N  N     . LEU A 1 481 ? 125.583 125.356 153.875 1.00 157.59 ? 481  LEU A N     1 
ATOM   3229  C  CA    . LEU A 1 481 ? 125.708 125.389 152.423 1.00 158.52 ? 481  LEU A CA    1 
ATOM   3230  C  C     . LEU A 1 481 ? 126.616 124.290 151.885 1.00 159.41 ? 481  LEU A C     1 
ATOM   3231  O  O     . LEU A 1 481 ? 126.602 124.030 150.678 1.00 157.30 ? 481  LEU A O     1 
ATOM   3232  C  CB    . LEU A 1 481 ? 126.219 126.764 151.993 1.00 157.39 ? 481  LEU A CB    1 
ATOM   3233  C  CG    . LEU A 1 481 ? 125.146 127.855 152.012 1.00 156.31 ? 481  LEU A CG    1 
ATOM   3234  C  CD1   . LEU A 1 481 ? 125.327 128.759 153.224 1.00 151.44 ? 481  LEU A CD1   1 
ATOM   3235  C  CD2   . LEU A 1 481 ? 125.168 128.666 150.733 1.00 157.35 ? 481  LEU A CD2   1 
ATOM   3236  N  N     . ASP A 1 482 ? 127.418 123.657 152.743 1.00 163.48 ? 482  ASP A N     1 
ATOM   3237  C  CA    . ASP A 1 482 ? 128.305 122.591 152.286 1.00 164.81 ? 482  ASP A CA    1 
ATOM   3238  C  C     . ASP A 1 482 ? 127.521 121.380 151.795 1.00 159.52 ? 482  ASP A C     1 
ATOM   3239  O  O     . ASP A 1 482 ? 127.830 120.817 150.740 1.00 158.16 ? 482  ASP A O     1 
ATOM   3240  C  CB    . ASP A 1 482 ? 129.262 122.194 153.411 1.00 166.55 ? 482  ASP A CB    1 
ATOM   3241  C  CG    . ASP A 1 482 ? 130.177 123.326 153.821 1.00 169.09 ? 482  ASP A CG    1 
ATOM   3242  O  OD1   . ASP A 1 482 ? 130.470 124.193 152.968 1.00 166.63 ? 482  ASP A OD1   1 
ATOM   3243  O  OD2   . ASP A 1 482 ? 130.603 123.358 154.996 1.00 170.42 ? 482  ASP A OD2   1 
ATOM   3244  N  N     . VAL A 1 483 ? 126.512 120.956 152.555 1.00 157.96 ? 483  VAL A N     1 
ATOM   3245  C  CA    . VAL A 1 483 ? 125.700 119.817 152.141 1.00 156.98 ? 483  VAL A CA    1 
ATOM   3246  C  C     . VAL A 1 483 ? 124.824 120.192 150.954 1.00 156.31 ? 483  VAL A C     1 
ATOM   3247  O  O     . VAL A 1 483 ? 124.661 119.409 150.010 1.00 154.70 ? 483  VAL A O     1 
ATOM   3248  C  CB    . VAL A 1 483 ? 124.863 119.308 153.327 1.00 156.73 ? 483  VAL A CB    1 
ATOM   3249  C  CG1   . VAL A 1 483 ? 123.634 118.566 152.830 1.00 152.65 ? 483  VAL A CG1   1 
ATOM   3250  C  CG2   . VAL A 1 483 ? 125.710 118.429 154.233 1.00 155.71 ? 483  VAL A CG2   1 
ATOM   3251  N  N     . LEU A 1 484 ? 124.242 121.391 150.986 1.00 156.63 ? 484  LEU A N     1 
ATOM   3252  C  CA    . LEU A 1 484 ? 123.329 121.812 149.930 1.00 153.66 ? 484  LEU A CA    1 
ATOM   3253  C  C     . LEU A 1 484 ? 124.049 121.968 148.596 1.00 156.64 ? 484  LEU A C     1 
ATOM   3254  O  O     . LEU A 1 484 ? 123.547 121.526 147.556 1.00 156.45 ? 484  LEU A O     1 
ATOM   3255  C  CB    . LEU A 1 484 ? 122.639 123.114 150.330 1.00 150.37 ? 484  LEU A CB    1 
ATOM   3256  C  CG    . LEU A 1 484 ? 121.805 123.008 151.602 1.00 150.38 ? 484  LEU A CG    1 
ATOM   3257  C  CD1   . LEU A 1 484 ? 121.211 124.354 151.986 1.00 146.82 ? 484  LEU A CD1   1 
ATOM   3258  C  CD2   . LEU A 1 484 ? 120.728 121.951 151.425 1.00 147.82 ? 484  LEU A CD2   1 
ATOM   3259  N  N     . GLY A 1 485 ? 125.222 122.594 148.602 1.00 157.10 ? 485  GLY A N     1 
ATOM   3260  C  CA    . GLY A 1 485 ? 125.977 122.805 147.389 1.00 154.80 ? 485  GLY A CA    1 
ATOM   3261  C  C     . GLY A 1 485 ? 125.944 124.249 146.929 1.00 156.12 ? 485  GLY A C     1 
ATOM   3262  O  O     . GLY A 1 485 ? 125.391 125.123 147.604 1.00 158.63 ? 485  GLY A O     1 
ATOM   3263  N  N     . PRO A 1 486 ? 126.541 124.532 145.763 1.00 155.65 ? 486  PRO A N     1 
ATOM   3264  C  CA    . PRO A 1 486 ? 126.571 125.916 145.269 1.00 157.23 ? 486  PRO A CA    1 
ATOM   3265  C  C     . PRO A 1 486 ? 125.295 126.304 144.539 1.00 152.37 ? 486  PRO A C     1 
ATOM   3266  O  O     . PRO A 1 486 ? 124.879 127.474 144.541 1.00 149.79 ? 486  PRO A O     1 
ATOM   3267  C  CB    . PRO A 1 486 ? 127.781 125.926 144.327 1.00 153.15 ? 486  PRO A CB    1 
ATOM   3268  C  CG    . PRO A 1 486 ? 128.009 124.481 143.945 1.00 152.39 ? 486  PRO A CG    1 
ATOM   3269  C  CD    . PRO A 1 486 ? 127.178 123.591 144.829 1.00 152.98 ? 486  PRO A CD    1 
ATOM   3270  N  N     . PHE A 1 487 ? 124.673 125.306 143.907 1.00 148.75 ? 487  PHE A N     1 
ATOM   3271  C  CA    . PHE A 1 487 ? 123.403 125.526 143.230 1.00 147.75 ? 487  PHE A CA    1 
ATOM   3272  C  C     . PHE A 1 487 ? 122.358 126.044 144.204 1.00 150.29 ? 487  PHE A C     1 
ATOM   3273  O  O     . PHE A 1 487 ? 121.686 127.041 143.934 1.00 150.17 ? 487  PHE A O     1 
ATOM   3274  C  CB    . PHE A 1 487 ? 122.930 124.227 142.572 1.00 145.57 ? 487  PHE A CB    1 
ATOM   3275  C  CG    . PHE A 1 487 ? 121.878 124.425 141.517 1.00 146.34 ? 487  PHE A CG    1 
ATOM   3276  C  CD1   . PHE A 1 487 ? 122.227 124.797 140.231 1.00 146.52 ? 487  PHE A CD1   1 
ATOM   3277  C  CD2   . PHE A 1 487 ? 120.539 124.234 141.811 1.00 146.27 ? 487  PHE A CD2   1 
ATOM   3278  C  CE1   . PHE A 1 487 ? 121.260 124.978 139.260 1.00 144.09 ? 487  PHE A CE1   1 
ATOM   3279  C  CE2   . PHE A 1 487 ? 119.569 124.412 140.841 1.00 143.39 ? 487  PHE A CE2   1 
ATOM   3280  C  CZ    . PHE A 1 487 ? 119.931 124.785 139.567 1.00 142.08 ? 487  PHE A CZ    1 
ATOM   3281  N  N     . ILE A 1 488 ? 122.244 125.403 145.368 1.00 150.26 ? 488  ILE A N     1 
ATOM   3282  C  CA    . ILE A 1 488 ? 121.234 125.795 146.345 1.00 146.42 ? 488  ILE A CA    1 
ATOM   3283  C  C     . ILE A 1 488 ? 121.551 127.168 146.934 1.00 147.18 ? 488  ILE A C     1 
ATOM   3284  O  O     . ILE A 1 488 ? 120.645 127.955 147.227 1.00 150.15 ? 488  ILE A O     1 
ATOM   3285  C  CB    . ILE A 1 488 ? 121.108 124.710 147.428 1.00 149.29 ? 488  ILE A CB    1 
ATOM   3286  C  CG1   . ILE A 1 488 ? 120.417 123.475 146.850 1.00 151.48 ? 488  ILE A CG1   1 
ATOM   3287  C  CG2   . ILE A 1 488 ? 120.320 125.213 148.612 1.00 147.34 ? 488  ILE A CG2   1 
ATOM   3288  C  CD1   . ILE A 1 488 ? 119.068 123.767 146.237 1.00 146.07 ? 488  ILE A CD1   1 
ATOM   3289  N  N     . GLY A 1 489 ? 122.834 127.488 147.106 1.00 146.32 ? 489  GLY A N     1 
ATOM   3290  C  CA    . GLY A 1 489 ? 123.182 128.804 147.622 1.00 149.00 ? 489  GLY A CA    1 
ATOM   3291  C  C     . GLY A 1 489 ? 122.807 129.927 146.671 1.00 150.51 ? 489  GLY A C     1 
ATOM   3292  O  O     . GLY A 1 489 ? 122.054 130.842 147.034 1.00 149.75 ? 489  GLY A O     1 
ATOM   3293  N  N     . MET A 1 491 ? 120.813 129.687 144.494 1.00 146.26 ? 491  MET A N     1 
ATOM   3294  C  CA    . MET A 1 491 ? 119.376 129.514 144.381 1.00 147.69 ? 491  MET A CA    1 
ATOM   3295  C  C     . MET A 1 491 ? 118.629 130.347 145.410 1.00 148.43 ? 491  MET A C     1 
ATOM   3296  O  O     . MET A 1 491 ? 117.642 131.016 145.086 1.00 143.81 ? 491  MET A O     1 
ATOM   3297  C  CB    . MET A 1 491 ? 119.095 128.030 144.568 1.00 148.07 ? 491  MET A CB    1 
ATOM   3298  C  CG    . MET A 1 491 ? 117.730 127.656 144.961 1.00 145.02 ? 491  MET A CG    1 
ATOM   3299  S  SD    . MET A 1 491 ? 116.950 127.193 143.444 1.00 155.60 ? 491  MET A SD    1 
ATOM   3300  C  CE    . MET A 1 491 ? 117.507 125.494 143.360 1.00 146.28 ? 491  MET A CE    1 
ATOM   3301  N  N     . TYR A 1 492 ? 119.083 130.306 146.658 1.00 151.37 ? 492  TYR A N     1 
ATOM   3302  C  CA    . TYR A 1 492 ? 118.435 130.995 147.766 1.00 151.71 ? 492  TYR A CA    1 
ATOM   3303  C  C     . TYR A 1 492 ? 118.977 132.393 148.009 1.00 151.98 ? 492  TYR A C     1 
ATOM   3304  O  O     . TYR A 1 492 ? 118.605 133.008 149.015 1.00 151.15 ? 492  TYR A O     1 
ATOM   3305  C  CB    . TYR A 1 492 ? 118.554 130.170 149.047 1.00 148.98 ? 492  TYR A CB    1 
ATOM   3306  C  CG    . TYR A 1 492 ? 117.618 128.986 149.103 1.00 149.81 ? 492  TYR A CG    1 
ATOM   3307  C  CD1   . TYR A 1 492 ? 116.310 129.141 149.527 1.00 144.51 ? 492  TYR A CD1   1 
ATOM   3308  C  CD2   . TYR A 1 492 ? 118.031 127.724 148.715 1.00 150.94 ? 492  TYR A CD2   1 
ATOM   3309  C  CE1   . TYR A 1 492 ? 115.446 128.073 149.576 1.00 142.36 ? 492  TYR A CE1   1 
ATOM   3310  C  CE2   . TYR A 1 492 ? 117.171 126.644 148.761 1.00 150.03 ? 492  TYR A CE2   1 
ATOM   3311  C  CZ    . TYR A 1 492 ? 115.880 126.824 149.192 1.00 146.08 ? 492  TYR A CZ    1 
ATOM   3312  O  OH    . TYR A 1 492 ? 115.020 125.750 149.239 1.00 145.72 ? 492  TYR A OH    1 
ATOM   3313  N  N     . LEU A 1 493 ? 119.858 132.900 147.143 1.00 151.07 ? 493  LEU A N     1 
ATOM   3314  C  CA    . LEU A 1 493 ? 120.178 134.323 147.216 1.00 151.54 ? 493  LEU A CA    1 
ATOM   3315  C  C     . LEU A 1 493 ? 118.924 135.189 147.204 1.00 150.40 ? 493  LEU A C     1 
ATOM   3316  O  O     . LEU A 1 493 ? 118.800 136.113 148.015 1.00 146.53 ? 493  LEU A O     1 
ATOM   3317  C  CB    . LEU A 1 493 ? 121.096 134.729 146.068 1.00 151.45 ? 493  LEU A CB    1 
ATOM   3318  C  CG    . LEU A 1 493 ? 122.586 134.621 146.373 1.00 151.53 ? 493  LEU A CG    1 
ATOM   3319  C  CD1   . LEU A 1 493 ? 123.376 135.567 145.487 1.00 151.12 ? 493  LEU A CD1   1 
ATOM   3320  C  CD2   . LEU A 1 493 ? 122.862 134.901 147.843 1.00 149.43 ? 493  LEU A CD2   1 
ATOM   3321  N  N     . ALA A 1 494 ? 117.982 134.908 146.303 1.00 146.76 ? 494  ALA A N     1 
ATOM   3322  C  CA    . ALA A 1 494 ? 116.679 135.576 146.277 1.00 142.44 ? 494  ALA A CA    1 
ATOM   3323  C  C     . ALA A 1 494 ? 115.629 134.472 146.291 1.00 138.99 ? 494  ALA A C     1 
ATOM   3324  O  O     . ALA A 1 494 ? 115.213 133.978 145.240 1.00 133.73 ? 494  ALA A O     1 
ATOM   3325  C  CB    . ALA A 1 494 ? 116.531 136.491 145.070 1.00 136.99 ? 494  ALA A CB    1 
ATOM   3326  N  N     . GLU A 1 495 ? 115.199 134.093 147.492 1.00 132.19 ? 495  GLU A N     1 
ATOM   3327  C  CA    . GLU A 1 495 ? 114.337 132.940 147.691 1.00 127.04 ? 495  GLU A CA    1 
ATOM   3328  C  C     . GLU A 1 495 ? 112.867 133.311 147.821 1.00 127.73 ? 495  GLU A C     1 
ATOM   3329  O  O     . GLU A 1 495 ? 112.055 132.455 148.182 1.00 130.60 ? 495  GLU A O     1 
ATOM   3330  C  CB    . GLU A 1 495 ? 114.792 132.157 148.920 1.00 126.55 ? 495  GLU A CB    1 
ATOM   3331  N  N     . ASP A 1 496 ? 112.506 134.565 147.549 1.00 127.00 ? 496  ASP A N     1 
ATOM   3332  C  CA    . ASP A 1 496 ? 111.092 134.914 147.489 1.00 126.13 ? 496  ASP A CA    1 
ATOM   3333  C  C     . ASP A 1 496 ? 110.403 134.166 146.355 1.00 123.41 ? 496  ASP A C     1 
ATOM   3334  O  O     . ASP A 1 496 ? 109.260 133.717 146.499 1.00 123.94 ? 496  ASP A O     1 
ATOM   3335  C  CB    . ASP A 1 496 ? 110.928 136.423 147.330 1.00 128.46 ? 496  ASP A CB    1 
ATOM   3336  C  CG    . ASP A 1 496 ? 109.563 136.910 147.777 1.00 135.25 ? 496  ASP A CG    1 
ATOM   3337  O  OD1   . ASP A 1 496 ? 108.760 136.080 148.250 1.00 131.76 ? 496  ASP A OD1   1 
ATOM   3338  O  OD2   . ASP A 1 496 ? 109.296 138.125 147.664 1.00 139.66 ? 496  ASP A OD2   1 
ATOM   3339  N  N     . ARG A 1 497 ? 111.094 134.004 145.224 1.00 122.61 ? 497  ARG A N     1 
ATOM   3340  C  CA    . ARG A 1 497 ? 110.574 133.159 144.156 1.00 125.42 ? 497  ARG A CA    1 
ATOM   3341  C  C     . ARG A 1 497 ? 110.440 131.711 144.610 1.00 123.57 ? 497  ARG A C     1 
ATOM   3342  O  O     . ARG A 1 497 ? 109.529 131.001 144.170 1.00 124.69 ? 497  ARG A O     1 
ATOM   3343  C  CB    . ARG A 1 497 ? 111.484 133.243 142.934 1.00 126.67 ? 497  ARG A CB    1 
ATOM   3344  C  CG    . ARG A 1 497 ? 111.764 134.652 142.448 1.00 130.39 ? 497  ARG A CG    1 
ATOM   3345  C  CD    . ARG A 1 497 ? 112.227 134.645 141.002 1.00 134.35 ? 497  ARG A CD    1 
ATOM   3346  N  NE    . ARG A 1 497 ? 112.333 135.989 140.449 1.00 139.03 ? 497  ARG A NE    1 
ATOM   3347  C  CZ    . ARG A 1 497 ? 112.431 136.258 139.155 1.00 143.02 ? 497  ARG A CZ    1 
ATOM   3348  N  NH1   . ARG A 1 497 ? 112.437 135.296 138.248 1.00 142.25 ? 497  ARG A NH1   1 
ATOM   3349  N  NH2   . ARG A 1 497 ? 112.526 137.525 138.761 1.00 146.69 ? 497  ARG A NH2   1 
ATOM   3350  N  N     . ILE A 1 498 ? 111.335 131.258 145.489 1.00 118.33 ? 498  ILE A N     1 
ATOM   3351  C  CA    . ILE A 1 498 ? 111.258 129.893 146.001 1.00 117.80 ? 498  ILE A CA    1 
ATOM   3352  C  C     . ILE A 1 498 ? 110.035 129.731 146.893 1.00 118.27 ? 498  ILE A C     1 
ATOM   3353  O  O     . ILE A 1 498 ? 109.323 128.722 146.829 1.00 119.98 ? 498  ILE A O     1 
ATOM   3354  C  CB    . ILE A 1 498 ? 112.553 129.536 146.747 1.00 119.64 ? 498  ILE A CB    1 
ATOM   3355  C  CG1   . ILE A 1 498 ? 113.624 129.137 145.744 1.00 128.06 ? 498  ILE A CG1   1 
ATOM   3356  C  CG2   . ILE A 1 498 ? 112.313 128.410 147.734 1.00 120.35 ? 498  ILE A CG2   1 
ATOM   3357  C  CD1   . ILE A 1 498 ? 114.978 129.088 146.338 1.00 138.22 ? 498  ILE A CD1   1 
ATOM   3358  N  N     . LEU A 1 499 ? 109.778 130.726 147.743 1.00 115.51 ? 499  LEU A N     1 
ATOM   3359  C  CA    . LEU A 1 499 ? 108.550 130.724 148.528 1.00 111.67 ? 499  LEU A CA    1 
ATOM   3360  C  C     . LEU A 1 499 ? 107.330 130.720 147.621 1.00 114.63 ? 499  LEU A C     1 
ATOM   3361  O  O     . LEU A 1 499 ? 106.347 130.022 147.892 1.00 115.74 ? 499  LEU A O     1 
ATOM   3362  C  CB    . LEU A 1 499 ? 108.514 131.935 149.456 1.00 109.95 ? 499  LEU A CB    1 
ATOM   3363  C  CG    . LEU A 1 499 ? 107.588 131.828 150.666 1.00 107.26 ? 499  LEU A CG    1 
ATOM   3364  C  CD1   . LEU A 1 499 ? 107.494 130.394 151.154 1.00 111.43 ? 499  LEU A CD1   1 
ATOM   3365  C  CD2   . LEU A 1 499 ? 108.045 132.753 151.775 1.00 107.83 ? 499  LEU A CD2   1 
ATOM   3366  N  N     . SER A 1 500 ? 107.378 131.494 146.536 1.00 114.48 ? 500  SER A N     1 
ATOM   3367  C  CA    . SER A 1 500 ? 106.274 131.513 145.584 1.00 110.09 ? 500  SER A CA    1 
ATOM   3368  C  C     . SER A 1 500 ? 106.028 130.128 145.002 1.00 109.89 ? 500  SER A C     1 
ATOM   3369  O  O     . SER A 1 500 ? 104.889 129.643 144.970 1.00 114.63 ? 500  SER A O     1 
ATOM   3370  C  CB    . SER A 1 500 ? 106.574 132.512 144.469 1.00 113.30 ? 500  SER A CB    1 
ATOM   3371  O  OG    . SER A 1 500 ? 106.844 133.795 145.002 1.00 121.64 ? 500  SER A OG    1 
ATOM   3372  N  N     . PHE A 1 501 ? 107.093 129.470 144.543 1.00 108.79 ? 501  PHE A N     1 
ATOM   3373  C  CA    . PHE A 1 501 ? 106.932 128.159 143.928 1.00 108.81 ? 501  PHE A CA    1 
ATOM   3374  C  C     . PHE A 1 501 ? 106.448 127.128 144.938 1.00 110.30 ? 501  PHE A C     1 
ATOM   3375  O  O     . PHE A 1 501 ? 105.631 126.264 144.605 1.00 113.98 ? 501  PHE A O     1 
ATOM   3376  C  CB    . PHE A 1 501 ? 108.237 127.694 143.292 1.00 109.76 ? 501  PHE A CB    1 
ATOM   3377  C  CG    . PHE A 1 501 ? 108.114 126.376 142.591 1.00 109.67 ? 501  PHE A CG    1 
ATOM   3378  C  CD1   . PHE A 1 501 ? 107.451 126.285 141.382 1.00 108.73 ? 501  PHE A CD1   1 
ATOM   3379  C  CD2   . PHE A 1 501 ? 108.638 125.228 143.148 1.00 111.36 ? 501  PHE A CD2   1 
ATOM   3380  C  CE1   . PHE A 1 501 ? 107.326 125.076 140.739 1.00 111.25 ? 501  PHE A CE1   1 
ATOM   3381  C  CE2   . PHE A 1 501 ? 108.516 124.016 142.508 1.00 110.48 ? 501  PHE A CE2   1 
ATOM   3382  C  CZ    . PHE A 1 501 ? 107.859 123.941 141.303 1.00 113.76 ? 501  PHE A CZ    1 
ATOM   3383  N  N     . GLU A 1 502 ? 106.949 127.189 146.173 1.00 107.18 ? 502  GLU A N     1 
ATOM   3384  C  CA    . GLU A 1 502 ? 106.523 126.224 147.180 1.00 108.45 ? 502  GLU A CA    1 
ATOM   3385  C  C     . GLU A 1 502 ? 105.072 126.449 147.582 1.00 108.80 ? 502  GLU A C     1 
ATOM   3386  O  O     . GLU A 1 502 ? 104.350 125.494 147.886 1.00 109.86 ? 502  GLU A O     1 
ATOM   3387  C  CB    . GLU A 1 502 ? 107.441 126.295 148.397 1.00 111.92 ? 502  GLU A CB    1 
ATOM   3388  C  CG    . GLU A 1 502 ? 108.848 125.794 148.135 1.00 115.06 ? 502  GLU A CG    1 
ATOM   3389  C  CD    . GLU A 1 502 ? 108.894 124.300 147.891 1.00 118.49 ? 502  GLU A CD    1 
ATOM   3390  O  OE1   . GLU A 1 502 ? 107.972 123.593 148.348 1.00 118.41 ? 502  GLU A OE1   1 
ATOM   3391  O  OE2   . GLU A 1 502 ? 109.854 123.829 147.248 1.00 121.88 ? 502  GLU A OE2   1 
ATOM   3392  N  N     . VAL A 1 503 ? 104.629 127.707 147.602 1.00 107.38 ? 503  VAL A N     1 
ATOM   3393  C  CA    . VAL A 1 503 ? 103.218 127.991 147.846 1.00 103.67 ? 503  VAL A CA    1 
ATOM   3394  C  C     . VAL A 1 503 ? 102.368 127.431 146.713 1.00 106.82 ? 503  VAL A C     1 
ATOM   3395  O  O     . VAL A 1 503 ? 101.298 126.855 146.940 1.00 111.31 ? 503  VAL A O     1 
ATOM   3396  C  CB    . VAL A 1 503 ? 102.999 129.503 148.025 1.00 101.52 ? 503  VAL A CB    1 
ATOM   3397  C  CG1   . VAL A 1 503 ? 101.538 129.857 147.835 1.00 101.17 ? 503  VAL A CG1   1 
ATOM   3398  C  CG2   . VAL A 1 503 ? 103.476 129.943 149.390 1.00 105.72 ? 503  VAL A CG2   1 
ATOM   3399  N  N     . VAL A 1 504 ? 102.838 127.590 145.474 1.00 106.77 ? 504  VAL A N     1 
ATOM   3400  C  CA    . VAL A 1 504 ? 102.071 127.114 144.325 1.00 104.37 ? 504  VAL A CA    1 
ATOM   3401  C  C     . VAL A 1 504 ? 101.989 125.592 144.315 1.00 109.46 ? 504  VAL A C     1 
ATOM   3402  O  O     . VAL A 1 504 ? 100.929 125.017 144.041 1.00 115.58 ? 504  VAL A O     1 
ATOM   3403  C  CB    . VAL A 1 504 ? 102.675 127.658 143.018 1.00 100.51 ? 504  VAL A CB    1 
ATOM   3404  C  CG1   . VAL A 1 504 ? 102.022 126.999 141.823 1.00 99.47  ? 504  VAL A CG1   1 
ATOM   3405  C  CG2   . VAL A 1 504 ? 102.492 129.157 142.946 1.00 106.08 ? 504  VAL A CG2   1 
ATOM   3406  N  N     . ALA A 1 505 ? 103.095 124.915 144.619 1.00 108.01 ? 505  ALA A N     1 
ATOM   3407  C  CA    . ALA A 1 505 ? 103.181 123.463 144.527 1.00 107.46 ? 505  ALA A CA    1 
ATOM   3408  C  C     . ALA A 1 505 ? 103.194 122.786 145.893 1.00 111.09 ? 505  ALA A C     1 
ATOM   3409  O  O     . ALA A 1 505 ? 103.864 121.763 146.069 1.00 114.95 ? 505  ALA A O     1 
ATOM   3410  C  CB    . ALA A 1 505 ? 104.418 123.060 143.727 1.00 106.66 ? 505  ALA A CB    1 
ATOM   3411  N  N     . ARG A 1 506 ? 102.473 123.333 146.866 1.00 110.56 ? 506  ARG A N     1 
ATOM   3412  C  CA    . ARG A 1 506 ? 102.373 122.683 148.164 1.00 113.78 ? 506  ARG A CA    1 
ATOM   3413  C  C     . ARG A 1 506 ? 101.492 121.444 148.060 1.00 121.70 ? 506  ARG A C     1 
ATOM   3414  O  O     . ARG A 1 506 ? 100.462 121.451 147.383 1.00 125.85 ? 506  ARG A O     1 
ATOM   3415  C  CB    . ARG A 1 506 ? 101.814 123.648 149.206 1.00 115.90 ? 506  ARG A CB    1 
ATOM   3416  C  CG    . ARG A 1 506 ? 102.175 123.284 150.636 1.00 114.86 ? 506  ARG A CG    1 
ATOM   3417  C  CD    . ARG A 1 506 ? 101.403 124.121 151.639 1.00 106.74 ? 506  ARG A CD    1 
ATOM   3418  N  NE    . ARG A 1 506 ? 101.889 123.924 152.999 1.00 112.53 ? 506  ARG A NE    1 
ATOM   3419  C  CZ    . ARG A 1 506 ? 101.226 124.286 154.087 1.00 120.99 ? 506  ARG A CZ    1 
ATOM   3420  N  NH1   . ARG A 1 506 ? 100.036 124.860 154.013 1.00 125.12 ? 506  ARG A NH1   1 
ATOM   3421  N  NH2   . ARG A 1 506 ? 101.767 124.063 155.281 1.00 123.09 ? 506  ARG A NH2   1 
ATOM   3422  N  N     . LYS A 1 507 ? 101.904 120.376 148.738 1.00 119.32 ? 507  LYS A N     1 
ATOM   3423  C  CA    . LYS A 1 507 ? 101.230 119.093 148.598 1.00 121.13 ? 507  LYS A CA    1 
ATOM   3424  C  C     . LYS A 1 507 ? 99.824  119.137 149.186 1.00 122.99 ? 507  LYS A C     1 
ATOM   3425  O  O     . LYS A 1 507 ? 99.585  119.759 150.224 1.00 123.84 ? 507  LYS A O     1 
ATOM   3426  C  CB    . LYS A 1 507 ? 102.049 117.994 149.274 1.00 124.07 ? 507  LYS A CB    1 
ATOM   3427  C  CG    . LYS A 1 507 ? 101.372 116.633 149.292 1.00 127.50 ? 507  LYS A CG    1 
ATOM   3428  C  CD    . LYS A 1 507 ? 102.381 115.499 149.375 1.00 130.34 ? 507  LYS A CD    1 
ATOM   3429  C  CE    . LYS A 1 507 ? 103.357 115.708 150.518 1.00 137.84 ? 507  LYS A CE    1 
ATOM   3430  N  NZ    . LYS A 1 507 ? 104.427 114.675 150.518 1.00 135.39 ? 507  LYS A NZ    1 
ATOM   3431  N  N     . ASN A 1 508 ? 98.888  118.483 148.496 1.00 125.34 ? 508  ASN A N     1 
ATOM   3432  C  CA    . ASN A 1 508 ? 97.515  118.272 148.953 1.00 128.96 ? 508  ASN A CA    1 
ATOM   3433  C  C     . ASN A 1 508 ? 96.706  119.563 149.042 1.00 130.20 ? 508  ASN A C     1 
ATOM   3434  O  O     . ASN A 1 508 ? 95.603  119.565 149.598 1.00 133.53 ? 508  ASN A O     1 
ATOM   3435  C  CB    . ASN A 1 508 ? 97.478  117.539 150.298 1.00 131.61 ? 508  ASN A CB    1 
ATOM   3436  C  CG    . ASN A 1 508 ? 98.097  116.160 150.225 1.00 132.74 ? 508  ASN A CG    1 
ATOM   3437  O  OD1   . ASN A 1 508 ? 98.174  115.558 149.155 1.00 132.11 ? 508  ASN A OD1   1 
ATOM   3438  N  ND2   . ASN A 1 508 ? 98.542  115.650 151.367 1.00 136.14 ? 508  ASN A ND2   1 
ATOM   3439  N  N     . CYS A 1 509 ? 97.218  120.668 148.508 1.00 123.49 ? 509  CYS A N     1 
ATOM   3440  C  CA    . CYS A 1 509 ? 96.480  121.922 148.508 1.00 120.76 ? 509  CYS A CA    1 
ATOM   3441  C  C     . CYS A 1 509 ? 96.842  122.735 147.274 1.00 117.07 ? 509  CYS A C     1 
ATOM   3442  O  O     . CYS A 1 509 ? 97.979  122.701 146.800 1.00 114.71 ? 509  CYS A O     1 
ATOM   3443  C  CB    . CYS A 1 509 ? 96.751  122.725 149.783 1.00 122.81 ? 509  CYS A CB    1 
ATOM   3444  S  SG    . CYS A 1 509 ? 98.488  123.053 150.082 1.00 128.72 ? 509  CYS A SG    1 
ATOM   3445  N  N     . ASN A 1 510 ? 95.859  123.471 146.764 1.00 115.76 ? 510  ASN A N     1 
ATOM   3446  C  CA    . ASN A 1 510 ? 95.987  124.238 145.526 1.00 113.35 ? 510  ASN A CA    1 
ATOM   3447  C  C     . ASN A 1 510 ? 95.984  125.730 145.848 1.00 115.70 ? 510  ASN A C     1 
ATOM   3448  O  O     . ASN A 1 510 ? 94.935  126.378 145.853 1.00 121.18 ? 510  ASN A O     1 
ATOM   3449  C  CB    . ASN A 1 510 ? 94.866  123.871 144.549 1.00 113.43 ? 510  ASN A CB    1 
ATOM   3450  C  CG    . ASN A 1 510 ? 93.487  123.985 145.170 1.00 116.18 ? 510  ASN A CG    1 
ATOM   3451  O  OD1   . ASN A 1 510 ? 93.352  124.175 146.377 1.00 117.15 ? 510  ASN A OD1   1 
ATOM   3452  N  ND2   . ASN A 1 510 ? 92.455  123.874 144.344 1.00 118.73 ? 510  ASN A ND2   1 
ATOM   3453  N  N     . TRP A 1 511 ? 97.165  126.281 146.108 1.00 110.61 ? 511  TRP A N     1 
ATOM   3454  C  CA    . TRP A 1 511 ? 97.332  127.715 146.290 1.00 105.63 ? 511  TRP A CA    1 
ATOM   3455  C  C     . TRP A 1 511 ? 97.944  128.314 145.034 1.00 107.29 ? 511  TRP A C     1 
ATOM   3456  O  O     . TRP A 1 511 ? 99.013  127.883 144.594 1.00 110.64 ? 511  TRP A O     1 
ATOM   3457  C  CB    . TRP A 1 511 ? 98.213  128.037 147.498 1.00 100.78 ? 511  TRP A CB    1 
ATOM   3458  C  CG    . TRP A 1 511 ? 97.775  127.403 148.769 1.00 104.24 ? 511  TRP A CG    1 
ATOM   3459  C  CD1   . TRP A 1 511 ? 98.306  126.300 149.357 1.00 112.88 ? 511  TRP A CD1   1 
ATOM   3460  C  CD2   . TRP A 1 511 ? 96.710  127.839 149.621 1.00 105.70 ? 511  TRP A CD2   1 
ATOM   3461  N  NE1   . TRP A 1 511 ? 97.641  126.017 150.524 1.00 117.01 ? 511  TRP A NE1   1 
ATOM   3462  C  CE2   . TRP A 1 511 ? 96.655  126.949 150.707 1.00 110.33 ? 511  TRP A CE2   1 
ATOM   3463  C  CE3   . TRP A 1 511 ? 95.800  128.897 149.571 1.00 107.65 ? 511  TRP A CE3   1 
ATOM   3464  C  CZ2   . TRP A 1 511 ? 95.726  127.082 151.732 1.00 111.98 ? 511  TRP A CZ2   1 
ATOM   3465  C  CZ3   . TRP A 1 511 ? 94.879  129.026 150.589 1.00 107.74 ? 511  TRP A CZ3   1 
ATOM   3466  C  CH2   . TRP A 1 511 ? 94.848  128.125 151.655 1.00 110.25 ? 511  TRP A CH2   1 
ATOM   3467  N  N     . THR A 1 512 ? 97.263  129.297 144.461 1.00 102.88 ? 512  THR A N     1 
ATOM   3468  C  CA    . THR A 1 512 ? 97.792  130.079 143.358 1.00 103.25 ? 512  THR A CA    1 
ATOM   3469  C  C     . THR A 1 512 ? 98.175  131.457 143.874 1.00 103.92 ? 512  THR A C     1 
ATOM   3470  O  O     . THR A 1 512 ? 97.909  131.809 145.025 1.00 104.69 ? 512  THR A O     1 
ATOM   3471  C  CB    . THR A 1 512 ? 96.773  130.205 142.221 1.00 108.65 ? 512  THR A CB    1 
ATOM   3472  O  OG1   . THR A 1 512 ? 95.943  131.349 142.451 1.00 116.04 ? 512  THR A OG1   1 
ATOM   3473  C  CG2   . THR A 1 512 ? 95.904  128.966 142.150 1.00 110.27 ? 512  THR A CG2   1 
ATOM   3474  N  N     . MET A 1 513 ? 98.800  132.244 143.012 1.00 100.84 ? 513  MET A N     1 
ATOM   3475  C  CA    . MET A 1 513 ? 99.155  133.611 143.352 1.00 98.03  ? 513  MET A CA    1 
ATOM   3476  C  C     . MET A 1 513 ? 98.343  134.594 142.521 1.00 101.13 ? 513  MET A C     1 
ATOM   3477  O  O     . MET A 1 513 ? 97.565  134.219 141.641 1.00 106.94 ? 513  MET A O     1 
ATOM   3478  C  CB    . MET A 1 513 ? 100.652 133.862 143.163 1.00 93.45  ? 513  MET A CB    1 
ATOM   3479  C  CG    . MET A 1 513 ? 101.544 132.818 143.795 1.00 99.83  ? 513  MET A CG    1 
ATOM   3480  S  SD    . MET A 1 513 ? 102.049 133.343 145.440 1.00 124.94 ? 513  MET A SD    1 
ATOM   3481  C  CE    . MET A 1 513 ? 103.584 134.179 145.080 1.00 117.08 ? 513  MET A CE    1 
ATOM   3482  N  N     . HIS A 1 514 ? 98.536  135.874 142.824 1.00 94.70  ? 514  HIS A N     1 
ATOM   3483  C  CA    . HIS A 1 514 ? 97.784  136.942 142.189 1.00 98.52  ? 514  HIS A CA    1 
ATOM   3484  C  C     . HIS A 1 514 ? 98.651  138.189 142.158 1.00 102.53 ? 514  HIS A C     1 
ATOM   3485  O  O     . HIS A 1 514 ? 99.574  138.346 142.960 1.00 107.50 ? 514  HIS A O     1 
ATOM   3486  C  CB    . HIS A 1 514 ? 96.473  137.208 142.933 1.00 97.06  ? 514  HIS A CB    1 
ATOM   3487  C  CG    . HIS A 1 514 ? 95.561  138.177 142.249 1.00 104.58 ? 514  HIS A CG    1 
ATOM   3488  N  ND1   . HIS A 1 514 ? 95.332  139.450 142.721 1.00 111.16 ? 514  HIS A ND1   1 
ATOM   3489  C  CD2   . HIS A 1 514 ? 94.837  138.062 141.112 1.00 109.46 ? 514  HIS A CD2   1 
ATOM   3490  C  CE1   . HIS A 1 514 ? 94.498  140.075 141.910 1.00 114.06 ? 514  HIS A CE1   1 
ATOM   3491  N  NE2   . HIS A 1 514 ? 94.182  139.254 140.925 1.00 114.11 ? 514  HIS A NE2   1 
ATOM   3492  N  N     . TYR A 1 515 ? 98.347  139.075 141.217 1.00 100.46 ? 515  TYR A N     1 
ATOM   3493  C  CA    . TYR A 1 515 ? 99.052  140.342 141.072 1.00 101.66 ? 515  TYR A CA    1 
ATOM   3494  C  C     . TYR A 1 515 ? 98.040  141.464 141.225 1.00 108.12 ? 515  TYR A C     1 
ATOM   3495  O  O     . TYR A 1 515 ? 97.077  141.545 140.456 1.00 113.38 ? 515  TYR A O     1 
ATOM   3496  C  CB    . TYR A 1 515 ? 99.757  140.426 139.718 1.00 102.45 ? 515  TYR A CB    1 
ATOM   3497  C  CG    . TYR A 1 515 ? 100.277 141.798 139.370 1.00 107.12 ? 515  TYR A CG    1 
ATOM   3498  C  CD1   . TYR A 1 515 ? 101.441 142.283 139.941 1.00 107.29 ? 515  TYR A CD1   1 
ATOM   3499  C  CD2   . TYR A 1 515 ? 99.610  142.603 138.460 1.00 109.51 ? 515  TYR A CD2   1 
ATOM   3500  C  CE1   . TYR A 1 515 ? 101.922 143.533 139.622 1.00 111.40 ? 515  TYR A CE1   1 
ATOM   3501  C  CE2   . TYR A 1 515 ? 100.083 143.854 138.135 1.00 110.89 ? 515  TYR A CE2   1 
ATOM   3502  C  CZ    . TYR A 1 515 ? 101.239 144.314 138.718 1.00 113.54 ? 515  TYR A CZ    1 
ATOM   3503  O  OH    . TYR A 1 515 ? 101.715 145.562 138.395 1.00 114.37 ? 515  TYR A OH    1 
ATOM   3504  N  N     . VAL A 1 516 ? 98.260  142.326 142.210 1.00 106.05 ? 516  VAL A N     1 
ATOM   3505  C  CA    . VAL A 1 516 ? 97.348  143.419 142.514 1.00 107.42 ? 516  VAL A CA    1 
ATOM   3506  C  C     . VAL A 1 516 ? 97.863  144.682 141.836 1.00 108.95 ? 516  VAL A C     1 
ATOM   3507  O  O     . VAL A 1 516 ? 98.828  145.304 142.296 1.00 107.12 ? 516  VAL A O     1 
ATOM   3508  C  CB    . VAL A 1 516 ? 97.188  143.603 144.030 1.00 107.70 ? 516  VAL A CB    1 
ATOM   3509  C  CG1   . VAL A 1 516 ? 96.294  142.518 144.584 1.00 102.60 ? 516  VAL A CG1   1 
ATOM   3510  C  CG2   . VAL A 1 516 ? 98.537  143.515 144.710 1.00 107.50 ? 516  VAL A CG2   1 
ATOM   3511  N  N     . LYS A 1 517 ? 97.220  145.054 140.730 1.00 113.28 ? 517  LYS A N     1 
ATOM   3512  C  CA    . LYS A 1 517 ? 97.650  146.214 139.961 1.00 112.20 ? 517  LYS A CA    1 
ATOM   3513  C  C     . LYS A 1 517 ? 97.496  147.509 140.744 1.00 111.98 ? 517  LYS A C     1 
ATOM   3514  O  O     . LYS A 1 517 ? 98.364  148.383 140.662 1.00 111.46 ? 517  LYS A O     1 
ATOM   3515  C  CB    . LYS A 1 517 ? 96.859  146.286 138.653 1.00 113.00 ? 517  LYS A CB    1 
ATOM   3516  C  CG    . LYS A 1 517 ? 97.584  146.963 137.503 1.00 113.95 ? 517  LYS A CG    1 
ATOM   3517  C  CD    . LYS A 1 517 ? 96.647  147.879 136.733 1.00 114.65 ? 517  LYS A CD    1 
ATOM   3518  C  CE    . LYS A 1 517 ? 96.499  149.231 137.408 1.00 119.65 ? 517  LYS A CE    1 
ATOM   3519  N  NZ    . LYS A 1 517 ? 97.678  150.104 137.161 1.00 120.58 ? 517  LYS A NZ    1 
ATOM   3520  N  N     . ASP A 1 518 ? 96.417  147.646 141.508 1.00 110.61 ? 518  ASP A N     1 
ATOM   3521  C  CA    . ASP A 1 518 ? 96.095  148.892 142.186 1.00 111.62 ? 518  ASP A CA    1 
ATOM   3522  C  C     . ASP A 1 518 ? 96.844  149.080 143.499 1.00 112.95 ? 518  ASP A C     1 
ATOM   3523  O  O     . ASP A 1 518 ? 96.817  150.183 144.053 1.00 115.54 ? 518  ASP A O     1 
ATOM   3524  C  CB    . ASP A 1 518 ? 94.587  148.968 142.439 1.00 114.46 ? 518  ASP A CB    1 
ATOM   3525  C  CG    . ASP A 1 518 ? 93.776  148.847 141.164 1.00 118.79 ? 518  ASP A CG    1 
ATOM   3526  O  OD1   . ASP A 1 518 ? 94.056  149.599 140.208 1.00 121.32 ? 518  ASP A OD1   1 
ATOM   3527  O  OD2   . ASP A 1 518 ? 92.863  147.996 141.115 1.00 117.97 ? 518  ASP A OD2   1 
ATOM   3528  N  N     . ALA A 1 519 ? 97.512  148.045 144.010 1.00 109.60 ? 519  ALA A N     1 
ATOM   3529  C  CA    . ALA A 1 519 ? 98.244  148.147 145.273 1.00 105.85 ? 519  ALA A CA    1 
ATOM   3530  C  C     . ALA A 1 519 ? 99.692  148.517 144.971 1.00 107.33 ? 519  ALA A C     1 
ATOM   3531  O  O     . ALA A 1 519 ? 100.626 147.736 145.163 1.00 107.31 ? 519  ALA A O     1 
ATOM   3532  C  CB    . ALA A 1 519 ? 98.146  146.848 146.060 1.00 106.06 ? 519  ALA A CB    1 
ATOM   3533  N  N     . VAL A 1 520 ? 99.874  149.745 144.500 1.00 107.43 ? 520  VAL A N     1 
ATOM   3534  C  CA    . VAL A 1 520 ? 101.175 150.229 144.057 1.00 103.59 ? 520  VAL A CA    1 
ATOM   3535  C  C     . VAL A 1 520 ? 102.039 150.550 145.269 1.00 98.79  ? 520  VAL A C     1 
ATOM   3536  O  O     . VAL A 1 520 ? 101.620 151.285 146.171 1.00 101.08 ? 520  VAL A O     1 
ATOM   3537  C  CB    . VAL A 1 520 ? 101.021 151.455 143.142 1.00 104.60 ? 520  VAL A CB    1 
ATOM   3538  C  CG1   . VAL A 1 520 ? 100.036 152.441 143.734 1.00 105.18 ? 520  VAL A CG1   1 
ATOM   3539  C  CG2   . VAL A 1 520 ? 102.364 152.122 142.919 1.00 105.00 ? 520  VAL A CG2   1 
ATOM   3540  N  N     . ALA A 1 521 ? 103.246 149.991 145.292 1.00 96.18  ? 521  ALA A N     1 
ATOM   3541  C  CA    . ALA A 1 521 ? 104.217 150.233 146.350 1.00 97.47  ? 521  ALA A CA    1 
ATOM   3542  C  C     . ALA A 1 521 ? 105.397 150.980 145.753 1.00 103.07 ? 521  ALA A C     1 
ATOM   3543  O  O     . ALA A 1 521 ? 106.191 150.394 145.012 1.00 107.07 ? 521  ALA A O     1 
ATOM   3544  C  CB    . ALA A 1 521 ? 104.679 148.921 146.985 1.00 98.01  ? 521  ALA A CB    1 
ATOM   3545  N  N     . ARG A 1 522 ? 105.522 152.261 146.083 1.00 106.55 ? 522  ARG A N     1 
ATOM   3546  C  CA    . ARG A 1 522 ? 106.528 153.130 145.485 1.00 107.29 ? 522  ARG A CA    1 
ATOM   3547  C  C     . ARG A 1 522 ? 107.824 153.020 146.275 1.00 107.28 ? 522  ARG A C     1 
ATOM   3548  O  O     . ARG A 1 522 ? 107.856 153.339 147.467 1.00 111.79 ? 522  ARG A O     1 
ATOM   3549  C  CB    . ARG A 1 522 ? 106.038 154.578 145.440 1.00 108.60 ? 522  ARG A CB    1 
ATOM   3550  C  CG    . ARG A 1 522 ? 105.041 154.849 144.322 1.00 109.54 ? 522  ARG A CG    1 
ATOM   3551  C  CD    . ARG A 1 522 ? 104.273 156.155 144.496 1.00 109.78 ? 522  ARG A CD    1 
ATOM   3552  N  NE    . ARG A 1 522 ? 103.687 156.308 145.823 1.00 114.73 ? 522  ARG A NE    1 
ATOM   3553  C  CZ    . ARG A 1 522 ? 104.190 157.073 146.782 1.00 117.14 ? 522  ARG A CZ    1 
ATOM   3554  N  NH1   . ARG A 1 522 ? 105.301 157.767 146.601 1.00 118.69 ? 522  ARG A NH1   1 
ATOM   3555  N  NH2   . ARG A 1 522 ? 103.559 157.148 147.950 1.00 114.05 ? 522  ARG A NH2   1 
ATOM   3556  N  N     . THR A 1 523 ? 108.886 152.571 145.613 1.00 106.37 ? 523  THR A N     1 
ATOM   3557  C  CA    . THR A 1 523 ? 110.202 152.468 146.218 1.00 111.33 ? 523  THR A CA    1 
ATOM   3558  C  C     . THR A 1 523 ? 111.143 153.467 145.555 1.00 117.28 ? 523  THR A C     1 
ATOM   3559  O  O     . THR A 1 523 ? 110.776 154.152 144.601 1.00 121.72 ? 523  THR A O     1 
ATOM   3560  C  CB    . THR A 1 523 ? 110.739 151.043 146.099 1.00 115.48 ? 523  THR A CB    1 
ATOM   3561  O  OG1   . THR A 1 523 ? 112.089 151.004 146.578 1.00 125.54 ? 523  THR A OG1   1 
ATOM   3562  C  CG2   . THR A 1 523 ? 110.722 150.605 144.653 1.00 109.65 ? 523  THR A CG2   1 
ATOM   3563  N  N     . ASP A 1 524 ? 112.384 153.529 146.038 1.00 120.72 ? 524  ASP A N     1 
ATOM   3564  C  CA    . ASP A 1 524 ? 113.359 154.529 145.597 1.00 127.00 ? 524  ASP A CA    1 
ATOM   3565  C  C     . ASP A 1 524 ? 114.580 153.799 145.043 1.00 129.64 ? 524  ASP A C     1 
ATOM   3566  O  O     . ASP A 1 524 ? 115.352 153.201 145.794 1.00 132.12 ? 524  ASP A O     1 
ATOM   3567  C  CB    . ASP A 1 524 ? 113.732 155.468 146.738 1.00 128.73 ? 524  ASP A CB    1 
ATOM   3568  C  CG    . ASP A 1 524 ? 114.261 156.796 146.244 1.00 136.25 ? 524  ASP A CG    1 
ATOM   3569  O  OD1   . ASP A 1 524 ? 114.900 156.821 145.172 1.00 137.06 ? 524  ASP A OD1   1 
ATOM   3570  O  OD2   . ASP A 1 524 ? 114.032 157.817 146.927 1.00 137.98 ? 524  ASP A OD2   1 
ATOM   3571  N  N     . VAL A 1 525 ? 114.746 153.858 143.726 1.00 129.52 ? 525  VAL A N     1 
ATOM   3572  C  CA    . VAL A 1 525 ? 115.806 153.144 143.018 1.00 127.89 ? 525  VAL A CA    1 
ATOM   3573  C  C     . VAL A 1 525 ? 117.109 153.932 143.078 1.00 130.22 ? 525  VAL A C     1 
ATOM   3574  O  O     . VAL A 1 525 ? 117.081 155.154 143.284 1.00 136.63 ? 525  VAL A O     1 
ATOM   3575  C  CB    . VAL A 1 525 ? 115.410 152.887 141.558 1.00 125.72 ? 525  VAL A CB    1 
ATOM   3576  C  CG1   . VAL A 1 525 ? 114.507 151.682 141.470 1.00 125.76 ? 525  VAL A CG1   1 
ATOM   3577  C  CG2   . VAL A 1 525 ? 114.751 154.119 140.970 1.00 124.39 ? 525  VAL A CG2   1 
ATOM   3578  N  N     . PRO A 1 526 ? 118.263 153.287 142.911 1.00 129.69 ? 526  PRO A N     1 
ATOM   3579  C  CA    . PRO A 1 526 ? 119.513 154.041 142.784 1.00 133.89 ? 526  PRO A CA    1 
ATOM   3580  C  C     . PRO A 1 526 ? 119.514 154.896 141.529 1.00 135.06 ? 526  PRO A C     1 
ATOM   3581  O  O     . PRO A 1 526 ? 118.983 154.513 140.485 1.00 133.73 ? 526  PRO A O     1 
ATOM   3582  C  CB    . PRO A 1 526 ? 120.583 152.947 142.708 1.00 127.85 ? 526  PRO A CB    1 
ATOM   3583  C  CG    . PRO A 1 526 ? 119.853 151.731 142.263 1.00 123.50 ? 526  PRO A CG    1 
ATOM   3584  C  CD    . PRO A 1 526 ? 118.498 151.835 142.886 1.00 129.04 ? 526  PRO A CD    1 
ATOM   3585  N  N     . HIS A 1 527 ? 120.130 156.069 141.641 1.00 135.15 ? 527  HIS A N     1 
ATOM   3586  C  CA    . HIS A 1 527 ? 120.210 157.014 140.537 1.00 133.85 ? 527  HIS A CA    1 
ATOM   3587  C  C     . HIS A 1 527 ? 121.538 156.955 139.798 1.00 133.69 ? 527  HIS A C     1 
ATOM   3588  O  O     . HIS A 1 527 ? 121.764 157.764 138.894 1.00 130.93 ? 527  HIS A O     1 
ATOM   3589  C  CB    . HIS A 1 527 ? 119.970 158.437 141.046 1.00 137.93 ? 527  HIS A CB    1 
ATOM   3590  C  CG    . HIS A 1 527 ? 120.398 158.652 142.463 1.00 147.37 ? 527  HIS A CG    1 
ATOM   3591  N  ND1   . HIS A 1 527 ? 121.677 158.388 142.902 1.00 149.59 ? 527  HIS A ND1   1 
ATOM   3592  C  CD2   . HIS A 1 527 ? 119.715 159.101 143.542 1.00 150.15 ? 527  HIS A CD2   1 
ATOM   3593  C  CE1   . HIS A 1 527 ? 121.765 158.669 144.189 1.00 150.84 ? 527  HIS A CE1   1 
ATOM   3594  N  NE2   . HIS A 1 527 ? 120.588 159.103 144.602 1.00 153.98 ? 527  HIS A NE2   1 
ATOM   3595  N  N     . ASP A 1 528 ? 122.416 156.023 140.155 1.00 135.84 ? 528  ASP A N     1 
ATOM   3596  C  CA    . ASP A 1 528 ? 123.723 155.901 139.531 1.00 138.51 ? 528  ASP A CA    1 
ATOM   3597  C  C     . ASP A 1 528 ? 123.840 154.548 138.849 1.00 133.79 ? 528  ASP A C     1 
ATOM   3598  O  O     . ASP A 1 528 ? 123.258 153.550 139.288 1.00 135.97 ? 528  ASP A O     1 
ATOM   3599  C  CB    . ASP A 1 528 ? 124.857 156.071 140.550 1.00 144.57 ? 528  ASP A CB    1 
ATOM   3600  C  CG    . ASP A 1 528 ? 125.195 157.525 140.808 1.00 155.37 ? 528  ASP A CG    1 
ATOM   3601  O  OD1   . ASP A 1 528 ? 125.074 158.339 139.869 1.00 161.06 ? 528  ASP A OD1   1 
ATOM   3602  O  OD2   . ASP A 1 528 ? 125.584 157.853 141.949 1.00 153.92 ? 528  ASP A OD2   1 
ATOM   3603  N  N     . LEU A 1 529 ? 124.612 154.528 137.761 1.00 127.33 ? 529  LEU A N     1 
ATOM   3604  C  CA    . LEU A 1 529 ? 124.799 153.291 137.015 1.00 124.61 ? 529  LEU A CA    1 
ATOM   3605  C  C     . LEU A 1 529 ? 125.463 152.216 137.864 1.00 128.49 ? 529  LEU A C     1 
ATOM   3606  O  O     . LEU A 1 529 ? 125.149 151.035 137.710 1.00 132.03 ? 529  LEU A O     1 
ATOM   3607  C  CB    . LEU A 1 529 ? 125.619 153.553 135.753 1.00 122.16 ? 529  LEU A CB    1 
ATOM   3608  C  CG    . LEU A 1 529 ? 125.728 152.379 134.779 1.00 120.46 ? 529  LEU A CG    1 
ATOM   3609  C  CD1   . LEU A 1 529 ? 124.355 151.978 134.276 1.00 121.04 ? 529  LEU A CD1   1 
ATOM   3610  C  CD2   . LEU A 1 529 ? 126.640 152.725 133.618 1.00 121.92 ? 529  LEU A CD2   1 
ATOM   3611  N  N     . VAL A 1 530 ? 126.358 152.597 138.776 1.00 128.24 ? 530  VAL A N     1 
ATOM   3612  C  CA    . VAL A 1 530 ? 127.043 151.602 139.598 1.00 133.03 ? 530  VAL A CA    1 
ATOM   3613  C  C     . VAL A 1 530 ? 126.081 150.967 140.601 1.00 135.54 ? 530  VAL A C     1 
ATOM   3614  O  O     . VAL A 1 530 ? 126.086 149.742 140.805 1.00 136.69 ? 530  VAL A O     1 
ATOM   3615  C  CB    . VAL A 1 530 ? 128.262 152.240 140.286 1.00 133.48 ? 530  VAL A CB    1 
ATOM   3616  C  CG1   . VAL A 1 530 ? 129.349 152.511 139.263 1.00 129.31 ? 530  VAL A CG1   1 
ATOM   3617  C  CG2   . VAL A 1 530 ? 127.872 153.533 140.981 1.00 135.34 ? 530  VAL A CG2   1 
ATOM   3618  N  N     . GLY A 1 531 ? 125.244 151.782 141.246 1.00 132.42 ? 531  GLY A N     1 
ATOM   3619  C  CA    . GLY A 1 531 ? 124.234 151.230 142.130 1.00 130.59 ? 531  GLY A CA    1 
ATOM   3620  C  C     . GLY A 1 531 ? 123.247 150.355 141.386 1.00 129.89 ? 531  GLY A C     1 
ATOM   3621  O  O     . GLY A 1 531 ? 122.848 149.292 141.874 1.00 133.51 ? 531  GLY A O     1 
ATOM   3622  N  N     . LEU A 1 532 ? 122.845 150.787 140.187 1.00 124.84 ? 532  LEU A N     1 
ATOM   3623  C  CA    . LEU A 1 532 ? 121.991 149.951 139.354 1.00 123.37 ? 532  LEU A CA    1 
ATOM   3624  C  C     . LEU A 1 532 ? 122.675 148.633 139.023 1.00 126.11 ? 532  LEU A C     1 
ATOM   3625  O  O     . LEU A 1 532 ? 122.031 147.582 139.003 1.00 131.11 ? 532  LEU A O     1 
ATOM   3626  C  CB    . LEU A 1 532 ? 121.613 150.689 138.073 1.00 117.54 ? 532  LEU A CB    1 
ATOM   3627  C  CG    . LEU A 1 532 ? 120.680 149.906 137.151 1.00 114.22 ? 532  LEU A CG    1 
ATOM   3628  C  CD1   . LEU A 1 532 ? 119.440 149.476 137.904 1.00 118.26 ? 532  LEU A CD1   1 
ATOM   3629  C  CD2   . LEU A 1 532 ? 120.311 150.715 135.924 1.00 114.98 ? 532  LEU A CD2   1 
ATOM   3630  N  N     . ILE A 1 533 ? 123.983 148.672 138.768 1.00 124.55 ? 533  ILE A N     1 
ATOM   3631  C  CA    . ILE A 1 533 ? 124.720 147.459 138.428 1.00 124.64 ? 533  ILE A CA    1 
ATOM   3632  C  C     . ILE A 1 533 ? 124.694 146.478 139.591 1.00 129.11 ? 533  ILE A C     1 
ATOM   3633  O  O     . ILE A 1 533 ? 124.420 145.287 139.414 1.00 134.18 ? 533  ILE A O     1 
ATOM   3634  C  CB    . ILE A 1 533 ? 126.160 147.808 138.017 1.00 118.08 ? 533  ILE A CB    1 
ATOM   3635  C  CG1   . ILE A 1 533 ? 126.199 148.263 136.561 1.00 116.20 ? 533  ILE A CG1   1 
ATOM   3636  C  CG2   . ILE A 1 533 ? 127.077 146.616 138.215 1.00 119.40 ? 533  ILE A CG2   1 
ATOM   3637  C  CD1   . ILE A 1 533 ? 127.569 148.641 136.093 1.00 118.50 ? 533  ILE A CD1   1 
ATOM   3638  N  N     . SER A 1 534 ? 124.970 146.967 140.802 1.00 127.71 ? 534  SER A N     1 
ATOM   3639  C  CA    . SER A 1 534 ? 124.959 146.081 141.967 1.00 129.65 ? 534  SER A CA    1 
ATOM   3640  C  C     . SER A 1 534 ? 123.564 145.509 142.216 1.00 133.88 ? 534  SER A C     1 
ATOM   3641  O  O     . SER A 1 534 ? 123.394 144.291 142.416 1.00 135.16 ? 534  SER A O     1 
ATOM   3642  C  CB    . SER A 1 534 ? 125.461 146.832 143.199 1.00 127.82 ? 534  SER A CB    1 
ATOM   3643  O  OG    . SER A 1 534 ? 126.741 147.390 142.966 1.00 123.78 ? 534  SER A OG    1 
ATOM   3644  N  N     . GLN A 1 535 ? 122.550 146.377 142.195 1.00 132.25 ? 535  GLN A N     1 
ATOM   3645  C  CA    . GLN A 1 535 ? 121.184 145.929 142.431 1.00 133.67 ? 535  GLN A CA    1 
ATOM   3646  C  C     . GLN A 1 535 ? 120.771 144.886 141.403 1.00 132.08 ? 535  GLN A C     1 
ATOM   3647  O  O     . GLN A 1 535 ? 120.200 143.846 141.750 1.00 135.21 ? 535  GLN A O     1 
ATOM   3648  C  CB    . GLN A 1 535 ? 120.233 147.123 142.390 1.00 131.02 ? 535  GLN A CB    1 
ATOM   3649  C  CG    . GLN A 1 535 ? 118.804 146.787 142.750 1.00 133.61 ? 535  GLN A CG    1 
ATOM   3650  C  CD    . GLN A 1 535 ? 117.878 147.967 142.573 1.00 133.62 ? 535  GLN A CD    1 
ATOM   3651  O  OE1   . GLN A 1 535 ? 118.191 148.904 141.843 1.00 132.89 ? 535  GLN A OE1   1 
ATOM   3652  N  NE2   . GLN A 1 535 ? 116.736 147.933 143.246 1.00 136.61 ? 535  GLN A NE2   1 
ATOM   3653  N  N     . ARG A 1 536 ? 121.070 145.139 140.129 1.00 127.08 ? 536  ARG A N     1 
ATOM   3654  C  CA    . ARG A 1 536 ? 120.655 144.219 139.084 1.00 127.59 ? 536  ARG A CA    1 
ATOM   3655  C  C     . ARG A 1 536 ? 121.482 142.946 139.101 1.00 132.41 ? 536  ARG A C     1 
ATOM   3656  O  O     . ARG A 1 536 ? 120.999 141.901 138.666 1.00 133.38 ? 536  ARG A O     1 
ATOM   3657  C  CB    . ARG A 1 536 ? 120.736 144.900 137.722 1.00 121.60 ? 536  ARG A CB    1 
ATOM   3658  C  CG    . ARG A 1 536 ? 119.610 145.881 137.500 1.00 116.70 ? 536  ARG A CG    1 
ATOM   3659  C  CD    . ARG A 1 536 ? 118.267 145.251 137.800 1.00 115.22 ? 536  ARG A CD    1 
ATOM   3660  N  NE    . ARG A 1 536 ? 117.170 146.086 137.330 1.00 116.58 ? 536  ARG A NE    1 
ATOM   3661  C  CZ    . ARG A 1 536 ? 116.648 147.083 138.031 1.00 125.09 ? 536  ARG A CZ    1 
ATOM   3662  N  NH1   . ARG A 1 536 ? 117.109 147.400 139.229 1.00 127.38 ? 536  ARG A NH1   1 
ATOM   3663  N  NH2   . ARG A 1 536 ? 115.642 147.781 137.515 1.00 123.96 ? 536  ARG A NH2   1 
ATOM   3664  N  N     . LYS A 1 537 ? 122.709 142.997 139.619 1.00 132.47 ? 537  LYS A N     1 
ATOM   3665  C  CA    . LYS A 1 537 ? 123.448 141.761 139.837 1.00 135.94 ? 537  LYS A CA    1 
ATOM   3666  C  C     . LYS A 1 537 ? 122.706 140.869 140.819 1.00 138.23 ? 537  LYS A C     1 
ATOM   3667  O  O     . LYS A 1 537 ? 122.461 139.686 140.544 1.00 140.95 ? 537  LYS A O     1 
ATOM   3668  C  CB    . LYS A 1 537 ? 124.850 142.066 140.355 1.00 134.20 ? 537  LYS A CB    1 
ATOM   3669  C  CG    . LYS A 1 537 ? 125.483 140.921 141.128 1.00 132.21 ? 537  LYS A CG    1 
ATOM   3670  C  CD    . LYS A 1 537 ? 126.289 141.426 142.309 1.00 132.22 ? 537  LYS A CD    1 
ATOM   3671  C  CE    . LYS A 1 537 ? 126.944 140.281 143.062 1.00 140.36 ? 537  LYS A CE    1 
ATOM   3672  N  NZ    . LYS A 1 537 ? 125.953 139.263 143.506 1.00 145.53 ? 537  LYS A NZ    1 
ATOM   3673  N  N     . ARG A 1 538 ? 122.321 141.436 141.965 1.00 135.73 ? 538  ARG A N     1 
ATOM   3674  C  CA    . ARG A 1 538 ? 121.537 140.678 142.941 1.00 136.62 ? 538  ARG A CA    1 
ATOM   3675  C  C     . ARG A 1 538 ? 120.255 140.134 142.314 1.00 134.24 ? 538  ARG A C     1 
ATOM   3676  O  O     . ARG A 1 538 ? 119.944 138.933 142.419 1.00 133.50 ? 538  ARG A O     1 
ATOM   3677  C  CB    . ARG A 1 538 ? 121.212 141.570 144.140 1.00 137.46 ? 538  ARG A CB    1 
ATOM   3678  C  CG    . ARG A 1 538 ? 122.285 141.606 145.212 1.00 139.99 ? 538  ARG A CG    1 
ATOM   3679  C  CD    . ARG A 1 538 ? 122.384 140.281 145.943 1.00 149.37 ? 538  ARG A CD    1 
ATOM   3680  N  NE    . ARG A 1 538 ? 121.208 140.047 146.774 1.00 156.46 ? 538  ARG A NE    1 
ATOM   3681  C  CZ    . ARG A 1 538 ? 120.933 138.903 147.386 1.00 153.78 ? 538  ARG A CZ    1 
ATOM   3682  N  NH1   . ARG A 1 538 ? 121.734 137.857 147.288 1.00 150.59 ? 538  ARG A NH1   1 
ATOM   3683  N  NH2   . ARG A 1 538 ? 119.827 138.809 148.118 1.00 153.40 ? 538  ARG A NH2   1 
ATOM   3684  N  N     . TRP A 1 539 ? 119.507 141.010 141.638 1.00 132.50 ? 539  TRP A N     1 
ATOM   3685  C  CA    . TRP A 1 539 ? 118.223 140.622 141.066 1.00 130.48 ? 539  TRP A CA    1 
ATOM   3686  C  C     . TRP A 1 539 ? 118.380 139.511 140.037 1.00 132.26 ? 539  TRP A C     1 
ATOM   3687  O  O     . TRP A 1 539 ? 117.639 138.525 140.059 1.00 134.00 ? 539  TRP A O     1 
ATOM   3688  C  CB    . TRP A 1 539 ? 117.546 141.830 140.423 1.00 131.86 ? 539  TRP A CB    1 
ATOM   3689  C  CG    . TRP A 1 539 ? 117.039 142.851 141.379 1.00 129.83 ? 539  TRP A CG    1 
ATOM   3690  C  CD1   . TRP A 1 539 ? 117.517 143.128 142.625 1.00 130.32 ? 539  TRP A CD1   1 
ATOM   3691  C  CD2   . TRP A 1 539 ? 115.929 143.726 141.171 1.00 128.94 ? 539  TRP A CD2   1 
ATOM   3692  N  NE1   . TRP A 1 539 ? 116.783 144.134 143.199 1.00 132.06 ? 539  TRP A NE1   1 
ATOM   3693  C  CE2   . TRP A 1 539 ? 115.798 144.515 142.327 1.00 131.75 ? 539  TRP A CE2   1 
ATOM   3694  C  CE3   . TRP A 1 539 ? 115.032 143.919 140.117 1.00 126.01 ? 539  TRP A CE3   1 
ATOM   3695  C  CZ2   . TRP A 1 539 ? 114.809 145.481 142.460 1.00 131.96 ? 539  TRP A CZ2   1 
ATOM   3696  C  CZ3   . TRP A 1 539 ? 114.053 144.879 140.250 1.00 129.75 ? 539  TRP A CZ3   1 
ATOM   3697  C  CH2   . TRP A 1 539 ? 113.947 145.646 141.413 1.00 133.45 ? 539  TRP A CH2   1 
ATOM   3698  N  N     . LEU A 1 540 ? 119.333 139.658 139.116 1.00 130.96 ? 540  LEU A N     1 
ATOM   3699  C  CA    . LEU A 1 540 ? 119.491 138.674 138.056 1.00 134.46 ? 540  LEU A CA    1 
ATOM   3700  C  C     . LEU A 1 540 ? 119.986 137.350 138.610 1.00 138.98 ? 540  LEU A C     1 
ATOM   3701  O  O     . LEU A 1 540 ? 119.578 136.286 138.134 1.00 142.38 ? 540  LEU A O     1 
ATOM   3702  C  CB    . LEU A 1 540 ? 120.445 139.197 136.985 1.00 130.30 ? 540  LEU A CB    1 
ATOM   3703  C  CG    . LEU A 1 540 ? 119.912 140.271 136.033 1.00 132.34 ? 540  LEU A CG    1 
ATOM   3704  C  CD1   . LEU A 1 540 ? 121.028 140.815 135.159 1.00 132.19 ? 540  LEU A CD1   1 
ATOM   3705  C  CD2   . LEU A 1 540 ? 118.782 139.726 135.169 1.00 137.16 ? 540  LEU A CD2   1 
ATOM   3706  N  N     . ASN A 1 541 ? 120.880 137.391 139.603 1.00 136.22 ? 541  ASN A N     1 
ATOM   3707  C  CA    . ASN A 1 541 ? 121.352 136.161 140.229 1.00 134.79 ? 541  ASN A CA    1 
ATOM   3708  C  C     . ASN A 1 541 ? 120.179 135.362 140.778 1.00 132.47 ? 541  ASN A C     1 
ATOM   3709  O  O     . ASN A 1 541 ? 119.977 134.178 140.437 1.00 127.79 ? 541  ASN A O     1 
ATOM   3710  C  CB    . ASN A 1 541 ? 122.320 136.520 141.357 1.00 132.46 ? 541  ASN A CB    1 
ATOM   3711  C  CG    . ASN A 1 541 ? 123.642 135.832 141.220 1.00 133.87 ? 541  ASN A CG    1 
ATOM   3712  O  OD1   . ASN A 1 541 ? 123.869 135.119 140.253 1.00 135.34 ? 541  ASN A OD1   1 
ATOM   3713  N  ND2   . ASN A 1 541 ? 124.534 136.055 142.179 1.00 136.38 ? 541  ASN A ND2   1 
ATOM   3714  N  N     . GLY A 1 542 ? 119.366 136.021 141.606 1.00 135.94 ? 542  GLY A N     1 
ATOM   3715  C  CA    . GLY A 1 542 ? 118.217 135.343 142.179 1.00 137.58 ? 542  GLY A CA    1 
ATOM   3716  C  C     . GLY A 1 542 ? 117.241 134.868 141.123 1.00 136.91 ? 542  GLY A C     1 
ATOM   3717  O  O     . GLY A 1 542 ? 116.756 133.736 141.173 1.00 138.88 ? 542  GLY A O     1 
ATOM   3718  N  N     . ALA A 1 543 ? 116.946 135.729 140.143 1.00 135.27 ? 543  ALA A N     1 
ATOM   3719  C  CA    . ALA A 1 543 ? 115.981 135.375 139.109 1.00 134.32 ? 543  ALA A CA    1 
ATOM   3720  C  C     . ALA A 1 543 ? 116.441 134.167 138.309 1.00 132.78 ? 543  ALA A C     1 
ATOM   3721  O  O     . ALA A 1 543 ? 115.654 133.250 138.059 1.00 133.63 ? 543  ALA A O     1 
ATOM   3722  C  CB    . ALA A 1 543 ? 115.739 136.565 138.182 1.00 136.04 ? 543  ALA A CB    1 
ATOM   3723  N  N     . PHE A 1 544 ? 117.715 134.136 137.911 1.00 131.07 ? 544  PHE A N     1 
ATOM   3724  C  CA    . PHE A 1 544 ? 118.206 133.030 137.096 1.00 132.27 ? 544  PHE A CA    1 
ATOM   3725  C  C     . PHE A 1 544 ? 118.142 131.713 137.854 1.00 132.50 ? 544  PHE A C     1 
ATOM   3726  O  O     . PHE A 1 544 ? 117.648 130.704 137.329 1.00 132.06 ? 544  PHE A O     1 
ATOM   3727  C  CB    . PHE A 1 544 ? 119.633 133.311 136.626 1.00 130.61 ? 544  PHE A CB    1 
ATOM   3728  C  CG    . PHE A 1 544 ? 120.168 132.275 135.683 1.00 126.75 ? 544  PHE A CG    1 
ATOM   3729  C  CD1   . PHE A 1 544 ? 119.616 132.117 134.425 1.00 123.36 ? 544  PHE A CD1   1 
ATOM   3730  C  CD2   . PHE A 1 544 ? 121.224 131.460 136.052 1.00 126.44 ? 544  PHE A CD2   1 
ATOM   3731  C  CE1   . PHE A 1 544 ? 120.100 131.165 133.555 1.00 121.13 ? 544  PHE A CE1   1 
ATOM   3732  C  CE2   . PHE A 1 544 ? 121.714 130.506 135.184 1.00 123.10 ? 544  PHE A CE2   1 
ATOM   3733  C  CZ    . PHE A 1 544 ? 121.151 130.359 133.934 1.00 119.66 ? 544  PHE A CZ    1 
ATOM   3734  N  N     . PHE A 1 545 ? 118.623 131.690 139.099 1.00 133.76 ? 545  PHE A N     1 
ATOM   3735  C  CA    . PHE A 1 545 ? 118.624 130.384 139.754 1.00 132.84 ? 545  PHE A CA    1 
ATOM   3736  C  C     . PHE A 1 545 ? 117.246 129.962 140.253 1.00 131.16 ? 545  PHE A C     1 
ATOM   3737  O  O     . PHE A 1 545 ? 116.943 128.762 140.269 1.00 129.60 ? 545  PHE A O     1 
ATOM   3738  C  CB    . PHE A 1 545 ? 119.672 130.345 140.856 1.00 138.29 ? 545  PHE A CB    1 
ATOM   3739  C  CG    . PHE A 1 545 ? 121.014 129.936 140.349 1.00 137.75 ? 545  PHE A CG    1 
ATOM   3740  C  CD1   . PHE A 1 545 ? 121.293 128.602 140.127 1.00 140.54 ? 545  PHE A CD1   1 
ATOM   3741  C  CD2   . PHE A 1 545 ? 121.966 130.873 140.019 1.00 136.04 ? 545  PHE A CD2   1 
ATOM   3742  C  CE1   . PHE A 1 545 ? 122.515 128.210 139.633 1.00 140.47 ? 545  PHE A CE1   1 
ATOM   3743  C  CE2   . PHE A 1 545 ? 123.185 130.480 139.520 1.00 134.18 ? 545  PHE A CE2   1 
ATOM   3744  C  CZ    . PHE A 1 545 ? 123.461 129.150 139.329 1.00 135.04 ? 545  PHE A CZ    1 
ATOM   3745  N  N     . ALA A 1 546 ? 116.376 130.908 140.608 1.00 130.31 ? 546  ALA A N     1 
ATOM   3746  C  CA    . ALA A 1 546 ? 114.998 130.539 140.899 1.00 129.77 ? 546  ALA A CA    1 
ATOM   3747  C  C     . ALA A 1 546 ? 114.295 130.033 139.646 1.00 129.28 ? 546  ALA A C     1 
ATOM   3748  O  O     . ALA A 1 546 ? 113.450 129.133 139.718 1.00 129.44 ? 546  ALA A O     1 
ATOM   3749  C  CB    . ALA A 1 546 ? 114.257 131.729 141.494 1.00 129.78 ? 546  ALA A CB    1 
ATOM   3750  N  N     . THR A 1 547 ? 114.630 130.601 138.485 1.00 125.09 ? 547  THR A N     1 
ATOM   3751  C  CA    . THR A 1 547 ? 114.079 130.113 137.229 1.00 122.14 ? 547  THR A CA    1 
ATOM   3752  C  C     . THR A 1 547 ? 114.527 128.686 136.951 1.00 123.23 ? 547  THR A C     1 
ATOM   3753  O  O     . THR A 1 547 ? 113.727 127.849 136.518 1.00 126.21 ? 547  THR A O     1 
ATOM   3754  C  CB    . THR A 1 547 ? 114.499 131.035 136.088 1.00 120.11 ? 547  THR A CB    1 
ATOM   3755  O  OG1   . THR A 1 547 ? 113.943 132.338 136.296 1.00 125.21 ? 547  THR A OG1   1 
ATOM   3756  C  CG2   . THR A 1 547 ? 114.016 130.490 134.765 1.00 118.12 ? 547  THR A CG2   1 
ATOM   3757  N  N     . LEU A 1 548 ? 115.806 128.392 137.189 1.00 122.07 ? 548  LEU A N     1 
ATOM   3758  C  CA    . LEU A 1 548 ? 116.277 127.020 137.017 1.00 121.16 ? 548  LEU A CA    1 
ATOM   3759  C  C     . LEU A 1 548 ? 115.568 126.071 137.975 1.00 122.90 ? 548  LEU A C     1 
ATOM   3760  O  O     . LEU A 1 548 ? 115.204 124.952 137.594 1.00 125.34 ? 548  LEU A O     1 
ATOM   3761  C  CB    . LEU A 1 548 ? 117.792 126.948 137.202 1.00 122.09 ? 548  LEU A CB    1 
ATOM   3762  C  CG    . LEU A 1 548 ? 118.617 126.919 135.913 1.00 118.48 ? 548  LEU A CG    1 
ATOM   3763  C  CD1   . LEU A 1 548 ? 118.243 128.066 134.993 1.00 118.55 ? 548  LEU A CD1   1 
ATOM   3764  C  CD2   . LEU A 1 548 ? 120.101 126.946 136.229 1.00 122.89 ? 548  LEU A CD2   1 
ATOM   3765  N  N     . PHE A 1 549 ? 115.356 126.503 139.221 1.00 120.15 ? 549  PHE A N     1 
ATOM   3766  C  CA    . PHE A 1 549 ? 114.602 125.685 140.168 1.00 118.04 ? 549  PHE A CA    1 
ATOM   3767  C  C     . PHE A 1 549 ? 113.195 125.404 139.669 1.00 117.65 ? 549  PHE A C     1 
ATOM   3768  O  O     . PHE A 1 549 ? 112.731 124.259 139.712 1.00 118.24 ? 549  PHE A O     1 
ATOM   3769  C  CB    . PHE A 1 549 ? 114.536 126.381 141.520 1.00 121.26 ? 549  PHE A CB    1 
ATOM   3770  C  CG    . PHE A 1 549 ? 113.772 125.622 142.568 1.00 117.53 ? 549  PHE A CG    1 
ATOM   3771  C  CD1   . PHE A 1 549 ? 114.338 124.537 143.208 1.00 115.00 ? 549  PHE A CD1   1 
ATOM   3772  C  CD2   . PHE A 1 549 ? 112.510 126.032 142.953 1.00 119.49 ? 549  PHE A CD2   1 
ATOM   3773  C  CE1   . PHE A 1 549 ? 113.649 123.851 144.183 1.00 117.00 ? 549  PHE A CE1   1 
ATOM   3774  C  CE2   . PHE A 1 549 ? 111.818 125.350 143.931 1.00 119.81 ? 549  PHE A CE2   1 
ATOM   3775  C  CZ    . PHE A 1 549 ? 112.387 124.258 144.545 1.00 119.23 ? 549  PHE A CZ    1 
ATOM   3776  N  N     . SER A 1 550 ? 112.491 126.442 139.218 1.00 114.67 ? 550  SER A N     1 
ATOM   3777  C  CA    . SER A 1 550 ? 111.129 126.254 138.739 1.00 114.56 ? 550  SER A CA    1 
ATOM   3778  C  C     . SER A 1 550 ? 111.098 125.321 137.538 1.00 117.17 ? 550  SER A C     1 
ATOM   3779  O  O     . SER A 1 550 ? 110.234 124.442 137.446 1.00 118.53 ? 550  SER A O     1 
ATOM   3780  C  CB    . SER A 1 550 ? 110.509 127.605 138.390 1.00 117.03 ? 550  SER A CB    1 
ATOM   3781  O  OG    . SER A 1 550 ? 109.267 127.438 137.733 1.00 127.05 ? 550  SER A OG    1 
ATOM   3782  N  N     . ILE A 1 551 ? 112.048 125.487 136.616 1.00 115.81 ? 551  ILE A N     1 
ATOM   3783  C  CA    . ILE A 1 551 ? 112.094 124.643 135.427 1.00 113.45 ? 551  ILE A CA    1 
ATOM   3784  C  C     . ILE A 1 551 ? 112.330 123.189 135.810 1.00 116.23 ? 551  ILE A C     1 
ATOM   3785  O  O     . ILE A 1 551 ? 111.679 122.279 135.283 1.00 116.51 ? 551  ILE A O     1 
ATOM   3786  C  CB    . ILE A 1 551 ? 113.170 125.158 134.455 1.00 113.32 ? 551  ILE A CB    1 
ATOM   3787  C  CG1   . ILE A 1 551 ? 112.681 126.419 133.744 1.00 113.69 ? 551  ILE A CG1   1 
ATOM   3788  C  CG2   . ILE A 1 551 ? 113.540 124.089 133.445 1.00 111.31 ? 551  ILE A CG2   1 
ATOM   3789  C  CD1   . ILE A 1 551 ? 113.723 127.060 132.865 1.00 114.99 ? 551  ILE A CD1   1 
ATOM   3790  N  N     . TRP A 1 552 ? 113.255 122.943 136.741 1.00 117.86 ? 552  TRP A N     1 
ATOM   3791  C  CA    . TRP A 1 552 ? 113.606 121.565 137.066 1.00 119.43 ? 552  TRP A CA    1 
ATOM   3792  C  C     . TRP A 1 552 ? 112.539 120.895 137.924 1.00 117.72 ? 552  TRP A C     1 
ATOM   3793  O  O     . TRP A 1 552 ? 112.307 119.688 137.798 1.00 123.32 ? 552  TRP A O     1 
ATOM   3794  C  CB    . TRP A 1 552 ? 114.963 121.514 137.765 1.00 120.34 ? 552  TRP A CB    1 
ATOM   3795  C  CG    . TRP A 1 552 ? 115.448 120.117 138.018 1.00 129.26 ? 552  TRP A CG    1 
ATOM   3796  C  CD1   . TRP A 1 552 ? 115.842 119.592 139.214 1.00 131.77 ? 552  TRP A CD1   1 
ATOM   3797  C  CD2   . TRP A 1 552 ? 115.596 119.066 137.052 1.00 134.03 ? 552  TRP A CD2   1 
ATOM   3798  N  NE1   . TRP A 1 552 ? 116.221 118.281 139.055 1.00 135.38 ? 552  TRP A NE1   1 
ATOM   3799  C  CE2   . TRP A 1 552 ? 116.080 117.935 137.737 1.00 137.90 ? 552  TRP A CE2   1 
ATOM   3800  C  CE3   . TRP A 1 552 ? 115.366 118.972 135.675 1.00 130.74 ? 552  TRP A CE3   1 
ATOM   3801  C  CZ2   . TRP A 1 552 ? 116.337 116.727 137.094 1.00 137.67 ? 552  TRP A CZ2   1 
ATOM   3802  C  CZ3   . TRP A 1 552 ? 115.620 117.772 135.040 1.00 130.26 ? 552  TRP A CZ3   1 
ATOM   3803  C  CH2   . TRP A 1 552 ? 116.101 116.666 135.748 1.00 135.12 ? 552  TRP A CH2   1 
ATOM   3804  N  N     . ASN A 1 553 ? 111.881 121.650 138.801 1.00 112.21 ? 553  ASN A N     1 
ATOM   3805  C  CA    . ASN A 1 553 ? 110.920 121.085 139.738 1.00 113.16 ? 553  ASN A CA    1 
ATOM   3806  C  C     . ASN A 1 553 ? 109.475 121.345 139.340 1.00 111.47 ? 553  ASN A C     1 
ATOM   3807  O  O     . ASN A 1 553 ? 108.574 121.133 140.157 1.00 113.19 ? 553  ASN A O     1 
ATOM   3808  C  CB    . ASN A 1 553 ? 111.174 121.633 141.142 1.00 112.47 ? 553  ASN A CB    1 
ATOM   3809  C  CG    . ASN A 1 553 ? 112.556 121.299 141.650 1.00 115.35 ? 553  ASN A CG    1 
ATOM   3810  O  OD1   . ASN A 1 553 ? 113.526 121.314 140.895 1.00 119.41 ? 553  ASN A OD1   1 
ATOM   3811  N  ND2   . ASN A 1 553 ? 112.656 120.994 142.937 1.00 114.70 ? 553  ASN A ND2   1 
ATOM   3812  N  N     . TRP A 1 554 ? 109.228 121.795 138.108 1.00 109.53 ? 554  TRP A N     1 
ATOM   3813  C  CA    . TRP A 1 554 ? 107.859 122.080 137.697 1.00 109.08 ? 554  TRP A CA    1 
ATOM   3814  C  C     . TRP A 1 554 ? 106.996 120.827 137.682 1.00 114.32 ? 554  TRP A C     1 
ATOM   3815  O  O     . TRP A 1 554 ? 105.764 120.925 137.678 1.00 117.72 ? 554  TRP A O     1 
ATOM   3816  C  CB    . TRP A 1 554 ? 107.852 122.742 136.322 1.00 108.60 ? 554  TRP A CB    1 
ATOM   3817  C  CG    . TRP A 1 554 ? 106.554 123.388 135.990 1.00 106.73 ? 554  TRP A CG    1 
ATOM   3818  C  CD1   . TRP A 1 554 ? 105.495 122.816 135.355 1.00 108.58 ? 554  TRP A CD1   1 
ATOM   3819  C  CD2   . TRP A 1 554 ? 106.168 124.732 136.283 1.00 108.09 ? 554  TRP A CD2   1 
ATOM   3820  N  NE1   . TRP A 1 554 ? 104.472 123.721 135.231 1.00 111.83 ? 554  TRP A NE1   1 
ATOM   3821  C  CE2   . TRP A 1 554 ? 104.862 124.907 135.793 1.00 111.76 ? 554  TRP A CE2   1 
ATOM   3822  C  CE3   . TRP A 1 554 ? 106.802 125.806 136.911 1.00 108.41 ? 554  TRP A CE3   1 
ATOM   3823  C  CZ2   . TRP A 1 554 ? 104.178 126.111 135.912 1.00 111.77 ? 554  TRP A CZ2   1 
ATOM   3824  C  CZ3   . TRP A 1 554 ? 106.123 126.999 137.027 1.00 106.75 ? 554  TRP A CZ3   1 
ATOM   3825  C  CH2   . TRP A 1 554 ? 104.824 127.142 136.532 1.00 107.46 ? 554  TRP A CH2   1 
ATOM   3826  N  N     . GLY A 1 555 ? 107.612 119.644 137.678 1.00 112.88 ? 555  GLY A N     1 
ATOM   3827  C  CA    . GLY A 1 555 ? 106.838 118.418 137.735 1.00 113.38 ? 555  GLY A CA    1 
ATOM   3828  C  C     . GLY A 1 555 ? 106.130 118.205 139.055 1.00 115.25 ? 555  GLY A C     1 
ATOM   3829  O  O     . GLY A 1 555 ? 105.175 117.423 139.116 1.00 119.22 ? 555  GLY A O     1 
ATOM   3830  N  N     . ARG A 1 556 ? 106.571 118.891 140.111 1.00 109.95 ? 556  ARG A N     1 
ATOM   3831  C  CA    . ARG A 1 556 ? 105.951 118.728 141.419 1.00 112.63 ? 556  ARG A CA    1 
ATOM   3832  C  C     . ARG A 1 556 ? 104.504 119.199 141.437 1.00 114.94 ? 556  ARG A C     1 
ATOM   3833  O  O     . ARG A 1 556 ? 103.712 118.686 142.233 1.00 119.37 ? 556  ARG A O     1 
ATOM   3834  C  CB    . ARG A 1 556 ? 106.755 119.480 142.479 1.00 110.64 ? 556  ARG A CB    1 
ATOM   3835  C  CG    . ARG A 1 556 ? 106.383 119.110 143.901 1.00 111.55 ? 556  ARG A CG    1 
ATOM   3836  C  CD    . ARG A 1 556 ? 107.100 119.982 144.912 1.00 112.19 ? 556  ARG A CD    1 
ATOM   3837  N  NE    . ARG A 1 556 ? 108.546 119.947 144.739 1.00 115.94 ? 556  ARG A NE    1 
ATOM   3838  C  CZ    . ARG A 1 556 ? 109.396 120.699 145.423 1.00 118.15 ? 556  ARG A CZ    1 
ATOM   3839  N  NH1   . ARG A 1 556 ? 108.976 121.564 146.331 1.00 117.11 ? 556  ARG A NH1   1 
ATOM   3840  N  NH2   . ARG A 1 556 ? 110.699 120.579 145.192 1.00 118.92 ? 556  ARG A NH2   1 
ATOM   3841  N  N     . ILE A 1 557 ? 104.139 120.149 140.574 1.00 109.88 ? 557  ILE A N     1 
ATOM   3842  C  CA    . ILE A 1 557 ? 102.767 120.649 140.557 1.00 109.99 ? 557  ILE A CA    1 
ATOM   3843  C  C     . ILE A 1 557 ? 101.792 119.529 140.221 1.00 114.82 ? 557  ILE A C     1 
ATOM   3844  O  O     . ILE A 1 557 ? 100.739 119.392 140.855 1.00 118.30 ? 557  ILE A O     1 
ATOM   3845  C  CB    . ILE A 1 557 ? 102.640 121.827 139.576 1.00 106.16 ? 557  ILE A CB    1 
ATOM   3846  C  CG1   . ILE A 1 557 ? 103.597 122.951 139.971 1.00 107.64 ? 557  ILE A CG1   1 
ATOM   3847  C  CG2   . ILE A 1 557 ? 101.214 122.334 139.537 1.00 108.22 ? 557  ILE A CG2   1 
ATOM   3848  C  CD1   . ILE A 1 557 ? 103.450 124.196 139.138 1.00 103.94 ? 557  ILE A CD1   1 
ATOM   3849  N  N     . TYR A 1 558 ? 102.122 118.712 139.221 1.00 113.59 ? 558  TYR A N     1 
ATOM   3850  C  CA    . TYR A 1 558 ? 101.278 117.569 138.888 1.00 114.53 ? 558  TYR A CA    1 
ATOM   3851  C  C     . TYR A 1 558 ? 101.552 116.376 139.796 1.00 114.88 ? 558  TYR A C     1 
ATOM   3852  O  O     . TYR A 1 558 ? 100.653 115.566 140.046 1.00 114.38 ? 558  TYR A O     1 
ATOM   3853  C  CB    . TYR A 1 558 ? 101.474 117.179 137.424 1.00 110.60 ? 558  TYR A CB    1 
ATOM   3854  C  CG    . TYR A 1 558 ? 101.902 118.326 136.541 1.00 111.29 ? 558  TYR A CG    1 
ATOM   3855  C  CD1   . TYR A 1 558 ? 100.990 119.293 136.146 1.00 113.40 ? 558  TYR A CD1   1 
ATOM   3856  C  CD2   . TYR A 1 558 ? 103.213 118.449 136.112 1.00 110.43 ? 558  TYR A CD2   1 
ATOM   3857  C  CE1   . TYR A 1 558 ? 101.368 120.344 135.343 1.00 112.05 ? 558  TYR A CE1   1 
ATOM   3858  C  CE2   . TYR A 1 558 ? 103.602 119.501 135.308 1.00 112.31 ? 558  TYR A CE2   1 
ATOM   3859  C  CZ    . TYR A 1 558 ? 102.673 120.445 134.928 1.00 110.53 ? 558  TYR A CZ    1 
ATOM   3860  O  OH    . TYR A 1 558 ? 103.049 121.496 134.128 1.00 105.17 ? 558  TYR A OH    1 
ATOM   3861  N  N     . SER A 1 559 ? 102.782 116.248 140.297 1.00 113.79 ? 559  SER A N     1 
ATOM   3862  C  CA    . SER A 1 559 ? 103.133 115.070 141.083 1.00 117.44 ? 559  SER A CA    1 
ATOM   3863  C  C     . SER A 1 559 ? 102.474 115.086 142.457 1.00 118.96 ? 559  SER A C     1 
ATOM   3864  O  O     . SER A 1 559 ? 102.001 114.048 142.933 1.00 120.47 ? 559  SER A O     1 
ATOM   3865  C  CB    . SER A 1 559 ? 104.650 114.968 141.221 1.00 120.42 ? 559  SER A CB    1 
ATOM   3866  O  OG    . SER A 1 559 ? 105.004 114.090 142.274 1.00 127.12 ? 559  SER A OG    1 
ATOM   3867  N  N     . GLU A 1 560 ? 102.429 116.245 143.111 1.00 118.52 ? 560  GLU A N     1 
ATOM   3868  C  CA    . GLU A 1 560 ? 102.018 116.334 144.507 1.00 120.93 ? 560  GLU A CA    1 
ATOM   3869  C  C     . GLU A 1 560 ? 100.755 117.148 144.734 1.00 120.83 ? 560  GLU A C     1 
ATOM   3870  O  O     . GLU A 1 560 ? 99.862  116.696 145.452 1.00 126.10 ? 560  GLU A O     1 
ATOM   3871  C  CB    . GLU A 1 560 ? 103.151 116.933 145.347 1.00 119.37 ? 560  GLU A CB    1 
ATOM   3872  C  CG    . GLU A 1 560 ? 104.429 116.115 145.324 1.00 119.66 ? 560  GLU A CG    1 
ATOM   3873  C  CD    . GLU A 1 560 ? 105.504 116.690 146.223 1.00 125.96 ? 560  GLU A CD    1 
ATOM   3874  O  OE1   . GLU A 1 560 ? 105.222 117.679 146.930 1.00 131.38 ? 560  GLU A OE1   1 
ATOM   3875  O  OE2   . GLU A 1 560 ? 106.631 116.152 146.223 1.00 125.28 ? 560  GLU A OE2   1 
ATOM   3876  N  N     . SER A 1 561 ? 100.653 118.335 144.143 1.00 116.51 ? 561  SER A N     1 
ATOM   3877  C  CA    . SER A 1 561 ? 99.531  119.219 144.414 1.00 116.61 ? 561  SER A CA    1 
ATOM   3878  C  C     . SER A 1 561 ? 98.227  118.623 143.888 1.00 121.04 ? 561  SER A C     1 
ATOM   3879  O  O     . SER A 1 561 ? 98.213  117.712 143.057 1.00 127.43 ? 561  SER A O     1 
ATOM   3880  C  CB    . SER A 1 561 ? 99.768  120.587 143.782 1.00 112.86 ? 561  SER A CB    1 
ATOM   3881  O  OG    . SER A 1 561 ? 98.566  121.333 143.736 1.00 115.29 ? 561  SER A OG    1 
ATOM   3882  N  N     . LYS A 1 562 ? 97.110  119.155 144.393 1.00 118.21 ? 562  LYS A N     1 
ATOM   3883  C  CA    . LYS A 1 562 ? 95.776  118.807 143.901 1.00 117.33 ? 562  LYS A CA    1 
ATOM   3884  C  C     . LYS A 1 562 ? 95.179  120.066 143.283 1.00 113.89 ? 562  LYS A C     1 
ATOM   3885  O  O     . LYS A 1 562 ? 94.414  120.788 143.924 1.00 113.38 ? 562  LYS A O     1 
ATOM   3886  C  CB    . LYS A 1 562 ? 94.885  118.248 145.009 1.00 119.13 ? 562  LYS A CB    1 
ATOM   3887  C  CG    . LYS A 1 562 ? 95.570  117.302 145.973 1.00 126.52 ? 562  LYS A CG    1 
ATOM   3888  C  CD    . LYS A 1 562 ? 94.672  117.016 147.168 1.00 131.18 ? 562  LYS A CD    1 
ATOM   3889  C  CE    . LYS A 1 562 ? 93.366  116.363 146.745 1.00 135.52 ? 562  LYS A CE    1 
ATOM   3890  N  NZ    . LYS A 1 562 ? 93.581  115.033 146.116 1.00 134.97 ? 562  LYS A NZ    1 
ATOM   3891  N  N     . HIS A 1 563 ? 95.522  120.313 142.025 1.00 111.73 ? 563  HIS A N     1 
ATOM   3892  C  CA    . HIS A 1 563 ? 94.948  121.398 141.253 1.00 109.39 ? 563  HIS A CA    1 
ATOM   3893  C  C     . HIS A 1 563 ? 93.840  120.854 140.359 1.00 110.61 ? 563  HIS A C     1 
ATOM   3894  O  O     . HIS A 1 563 ? 93.731  119.650 140.119 1.00 112.77 ? 563  HIS A O     1 
ATOM   3895  C  CB    . HIS A 1 563 ? 96.020  122.097 140.415 1.00 113.52 ? 563  HIS A CB    1 
ATOM   3896  C  CG    . HIS A 1 563 ? 96.764  123.171 141.144 1.00 114.91 ? 563  HIS A CG    1 
ATOM   3897  N  ND1   . HIS A 1 563 ? 97.976  122.952 141.761 1.00 113.49 ? 563  HIS A ND1   1 
ATOM   3898  C  CD2   . HIS A 1 563 ? 96.469  124.477 141.348 1.00 115.51 ? 563  HIS A CD2   1 
ATOM   3899  C  CE1   . HIS A 1 563 ? 98.396  124.076 142.314 1.00 110.68 ? 563  HIS A CE1   1 
ATOM   3900  N  NE2   . HIS A 1 563 ? 97.499  125.016 142.079 1.00 111.26 ? 563  HIS A NE2   1 
ATOM   3901  N  N     . THR A 1 564 ? 93.010  121.758 139.853 1.00 111.13 ? 564  THR A N     1 
ATOM   3902  C  CA    . THR A 1 564 ? 92.036  121.369 138.851 1.00 115.91 ? 564  THR A CA    1 
ATOM   3903  C  C     . THR A 1 564 ? 92.760  120.965 137.568 1.00 117.17 ? 564  THR A C     1 
ATOM   3904  O  O     . THR A 1 564 ? 93.905  121.351 137.326 1.00 118.39 ? 564  THR A O     1 
ATOM   3905  C  CB    . THR A 1 564 ? 91.062  122.514 138.578 1.00 118.95 ? 564  THR A CB    1 
ATOM   3906  O  OG1   . THR A 1 564 ? 90.865  123.266 139.780 1.00 121.91 ? 564  THR A OG1   1 
ATOM   3907  C  CG2   . THR A 1 564 ? 89.716  121.972 138.116 1.00 119.46 ? 564  THR A CG2   1 
ATOM   3908  N  N     . PHE A 1 565 ? 92.089  120.149 136.754 1.00 115.62 ? 565  PHE A N     1 
ATOM   3909  C  CA    . PHE A 1 565 ? 92.693  119.708 135.500 1.00 114.41 ? 565  PHE A CA    1 
ATOM   3910  C  C     . PHE A 1 565 ? 92.976  120.891 134.581 1.00 116.63 ? 565  PHE A C     1 
ATOM   3911  O  O     . PHE A 1 565 ? 94.021  120.939 133.917 1.00 120.95 ? 565  PHE A O     1 
ATOM   3912  C  CB    . PHE A 1 565 ? 91.783  118.689 134.815 1.00 115.21 ? 565  PHE A CB    1 
ATOM   3913  C  CG    . PHE A 1 565 ? 92.374  118.080 133.577 1.00 120.22 ? 565  PHE A CG    1 
ATOM   3914  C  CD1   . PHE A 1 565 ? 93.416  117.175 133.665 1.00 117.86 ? 565  PHE A CD1   1 
ATOM   3915  C  CD2   . PHE A 1 565 ? 91.877  118.404 132.325 1.00 125.15 ? 565  PHE A CD2   1 
ATOM   3916  C  CE1   . PHE A 1 565 ? 93.956  116.610 132.530 1.00 123.93 ? 565  PHE A CE1   1 
ATOM   3917  C  CE2   . PHE A 1 565 ? 92.417  117.845 131.185 1.00 124.24 ? 565  PHE A CE2   1 
ATOM   3918  C  CZ    . PHE A 1 565 ? 93.458  116.946 131.289 1.00 126.42 ? 565  PHE A CZ    1 
ATOM   3919  N  N     . VAL A 1 566 ? 92.061  121.862 134.536 1.00 110.69 ? 566  VAL A N     1 
ATOM   3920  C  CA    . VAL A 1 566 ? 92.297  123.062 133.741 1.00 109.21 ? 566  VAL A CA    1 
ATOM   3921  C  C     . VAL A 1 566 ? 93.498  123.829 134.284 1.00 112.30 ? 566  VAL A C     1 
ATOM   3922  O  O     . VAL A 1 566 ? 94.287  124.395 133.518 1.00 117.99 ? 566  VAL A O     1 
ATOM   3923  C  CB    . VAL A 1 566 ? 91.025  123.931 133.683 1.00 110.41 ? 566  VAL A CB    1 
ATOM   3924  C  CG1   . VAL A 1 566 ? 89.855  123.104 133.178 1.00 114.49 ? 566  VAL A CG1   1 
ATOM   3925  C  CG2   . VAL A 1 566 ? 90.698  124.530 135.042 1.00 110.92 ? 566  VAL A CG2   1 
ATOM   3926  N  N     . ARG A 1 567 ? 93.669  123.845 135.608 1.00 109.83 ? 567  ARG A N     1 
ATOM   3927  C  CA    . ARG A 1 567 ? 94.840  124.491 136.192 1.00 110.36 ? 567  ARG A CA    1 
ATOM   3928  C  C     . ARG A 1 567 ? 96.121  123.766 135.812 1.00 109.32 ? 567  ARG A C     1 
ATOM   3929  O  O     . ARG A 1 567 ? 97.139  124.403 135.528 1.00 113.11 ? 567  ARG A O     1 
ATOM   3930  C  CB    . ARG A 1 567 ? 94.702  124.570 137.710 1.00 114.22 ? 567  ARG A CB    1 
ATOM   3931  C  CG    . ARG A 1 567 ? 93.949  125.790 138.184 1.00 118.72 ? 567  ARG A CG    1 
ATOM   3932  C  CD    . ARG A 1 567 ? 94.798  127.033 138.005 1.00 111.65 ? 567  ARG A CD    1 
ATOM   3933  N  NE    . ARG A 1 567 ? 94.086  128.244 138.393 1.00 114.69 ? 567  ARG A NE    1 
ATOM   3934  C  CZ    . ARG A 1 567 ? 94.588  129.466 138.291 1.00 117.58 ? 567  ARG A CZ    1 
ATOM   3935  N  NH1   . ARG A 1 567 ? 95.805  129.675 137.821 1.00 111.55 ? 567  ARG A NH1   1 
ATOM   3936  N  NH2   . ARG A 1 567 ? 93.847  130.504 138.668 1.00 125.73 ? 567  ARG A NH2   1 
ATOM   3937  N  N     . LYS A 1 568 ? 96.094  122.433 135.805 1.00 108.75 ? 568  LYS A N     1 
ATOM   3938  C  CA    . LYS A 1 568 ? 97.275  121.677 135.401 1.00 109.12 ? 568  LYS A CA    1 
ATOM   3939  C  C     . LYS A 1 568 ? 97.632  121.958 133.948 1.00 112.14 ? 568  LYS A C     1 
ATOM   3940  O  O     . LYS A 1 568 ? 98.810  122.117 133.608 1.00 112.50 ? 568  LYS A O     1 
ATOM   3941  C  CB    . LYS A 1 568 ? 97.043  120.183 135.616 1.00 110.64 ? 568  LYS A CB    1 
ATOM   3942  C  CG    . LYS A 1 568 ? 96.680  119.810 137.041 1.00 112.97 ? 568  LYS A CG    1 
ATOM   3943  C  CD    . LYS A 1 568 ? 97.913  119.462 137.851 1.00 111.60 ? 568  LYS A CD    1 
ATOM   3944  C  CE    . LYS A 1 568 ? 97.551  118.691 139.108 1.00 109.83 ? 568  LYS A CE    1 
ATOM   3945  N  NZ    . LYS A 1 568 ? 97.577  117.222 138.886 1.00 103.92 ? 568  LYS A NZ    1 
ATOM   3946  N  N     . MET A 1 569 ? 96.627  122.018 133.073 1.00 111.91 ? 569  MET A N     1 
ATOM   3947  C  CA    . MET A 1 569 ? 96.898  122.313 131.669 1.00 110.08 ? 569  MET A CA    1 
ATOM   3948  C  C     . MET A 1 569 ? 97.430  123.731 131.488 1.00 105.78 ? 569  MET A C     1 
ATOM   3949  O  O     . MET A 1 569 ? 98.355  123.960 130.697 1.00 108.86 ? 569  MET A O     1 
ATOM   3950  C  CB    . MET A 1 569 ? 95.639  122.090 130.836 1.00 112.13 ? 569  MET A CB    1 
ATOM   3951  C  CG    . MET A 1 569 ? 95.412  120.632 130.495 1.00 116.97 ? 569  MET A CG    1 
ATOM   3952  S  SD    . MET A 1 569 ? 96.969  119.729 130.401 1.00 138.06 ? 569  MET A SD    1 
ATOM   3953  C  CE    . MET A 1 569 ? 96.792  118.571 131.754 1.00 121.12 ? 569  MET A CE    1 
ATOM   3954  N  N     . ALA A 1 570 ? 96.859  124.698 132.211 1.00 101.96 ? 570  ALA A N     1 
ATOM   3955  C  CA    . ALA A 1 570 ? 97.369  126.063 132.145 1.00 101.25 ? 570  ALA A CA    1 
ATOM   3956  C  C     . ALA A 1 570 ? 98.807  126.131 132.638 1.00 102.12 ? 570  ALA A C     1 
ATOM   3957  O  O     . ALA A 1 570 ? 99.637  126.848 132.068 1.00 105.60 ? 570  ALA A O     1 
ATOM   3958  C  CB    . ALA A 1 570 ? 96.476  126.998 132.959 1.00 100.33 ? 570  ALA A CB    1 
ATOM   3959  N  N     . PHE A 1 571 ? 99.122  125.381 133.692 1.00 102.19 ? 571  PHE A N     1 
ATOM   3960  C  CA    . PHE A 1 571 ? 100.485 125.360 134.206 1.00 100.64 ? 571  PHE A CA    1 
ATOM   3961  C  C     . PHE A 1 571 ? 101.442 124.718 133.212 1.00 103.35 ? 571  PHE A C     1 
ATOM   3962  O  O     . PHE A 1 571 ? 102.589 125.150 133.084 1.00 102.83 ? 571  PHE A O     1 
ATOM   3963  C  CB    . PHE A 1 571 ? 100.521 124.633 135.546 1.00 103.14 ? 571  PHE A CB    1 
ATOM   3964  C  CG    . PHE A 1 571 ? 100.324 125.537 136.722 1.00 101.92 ? 571  PHE A CG    1 
ATOM   3965  C  CD1   . PHE A 1 571 ? 100.779 126.840 136.687 1.00 96.71  ? 571  PHE A CD1   1 
ATOM   3966  C  CD2   . PHE A 1 571 ? 99.661  125.095 137.850 1.00 109.67 ? 571  PHE A CD2   1 
ATOM   3967  C  CE1   . PHE A 1 571 ? 100.598 127.676 137.761 1.00 102.76 ? 571  PHE A CE1   1 
ATOM   3968  C  CE2   . PHE A 1 571 ? 99.474  125.930 138.927 1.00 107.89 ? 571  PHE A CE2   1 
ATOM   3969  C  CZ    . PHE A 1 571 ? 99.943  127.223 138.882 1.00 107.89 ? 571  PHE A CZ    1 
ATOM   3970  N  N     . LEU A 1 572 ? 100.994 123.681 132.502 1.00 105.18 ? 572  LEU A N     1 
ATOM   3971  C  CA    . LEU A 1 572 ? 101.842 123.072 131.480 1.00 103.76 ? 572  LEU A CA    1 
ATOM   3972  C  C     . LEU A 1 572 ? 102.116 124.043 130.336 1.00 100.72 ? 572  LEU A C     1 
ATOM   3973  O  O     . LEU A 1 572 ? 103.254 124.148 129.853 1.00 102.15 ? 572  LEU A O     1 
ATOM   3974  C  CB    . LEU A 1 572 ? 101.190 121.795 130.955 1.00 103.46 ? 572  LEU A CB    1 
ATOM   3975  C  CG    . LEU A 1 572 ? 102.088 120.878 130.128 1.00 101.67 ? 572  LEU A CG    1 
ATOM   3976  C  CD1   . LEU A 1 572 ? 103.358 120.550 130.889 1.00 95.16  ? 572  LEU A CD1   1 
ATOM   3977  C  CD2   . LEU A 1 572 ? 101.346 119.609 129.751 1.00 108.15 ? 572  LEU A CD2   1 
ATOM   3978  N  N     . VAL A 1 573 ? 101.084 124.763 129.890 1.00 97.45  ? 573  VAL A N     1 
ATOM   3979  C  CA    . VAL A 1 573 ? 101.274 125.758 128.837 1.00 93.43  ? 573  VAL A CA    1 
ATOM   3980  C  C     . VAL A 1 573 ? 102.244 126.837 129.303 1.00 96.90  ? 573  VAL A C     1 
ATOM   3981  O  O     . VAL A 1 573 ? 103.156 127.246 128.568 1.00 101.15 ? 573  VAL A O     1 
ATOM   3982  C  CB    . VAL A 1 573 ? 99.922  126.359 128.417 1.00 92.17  ? 573  VAL A CB    1 
ATOM   3983  C  CG1   . VAL A 1 573 ? 100.135 127.546 127.499 1.00 94.73  ? 573  VAL A CG1   1 
ATOM   3984  C  CG2   . VAL A 1 573 ? 99.065  125.307 127.740 1.00 95.99  ? 573  VAL A CG2   1 
ATOM   3985  N  N     . PHE A 1 574 ? 102.068 127.309 130.539 1.00 99.57  ? 574  PHE A N     1 
ATOM   3986  C  CA    . PHE A 1 574 ? 102.970 128.326 131.059 1.00 99.51  ? 574  PHE A CA    1 
ATOM   3987  C  C     . PHE A 1 574 ? 104.380 127.786 131.219 1.00 98.54  ? 574  PHE A C     1 
ATOM   3988  O  O     . PHE A 1 574 ? 105.342 128.539 131.083 1.00 99.96  ? 574  PHE A O     1 
ATOM   3989  C  CB    . PHE A 1 574 ? 102.473 128.866 132.396 1.00 100.32 ? 574  PHE A CB    1 
ATOM   3990  C  CG    . PHE A 1 574 ? 103.443 129.797 133.059 1.00 95.74  ? 574  PHE A CG    1 
ATOM   3991  C  CD1   . PHE A 1 574 ? 103.541 131.113 132.648 1.00 100.64 ? 574  PHE A CD1   1 
ATOM   3992  C  CD2   . PHE A 1 574 ? 104.265 129.359 134.077 1.00 95.69  ? 574  PHE A CD2   1 
ATOM   3993  C  CE1   . PHE A 1 574 ? 104.434 131.973 133.245 1.00 104.01 ? 574  PHE A CE1   1 
ATOM   3994  C  CE2   . PHE A 1 574 ? 105.161 130.216 134.676 1.00 97.00  ? 574  PHE A CE2   1 
ATOM   3995  C  CZ    . PHE A 1 574 ? 105.244 131.525 134.261 1.00 100.89 ? 574  PHE A CZ    1 
ATOM   3996  N  N     . TYR A 1 575 ? 104.527 126.498 131.527 1.00 98.47  ? 575  TYR A N     1 
ATOM   3997  C  CA    . TYR A 1 575 ? 105.860 125.921 131.644 1.00 100.43 ? 575  TYR A CA    1 
ATOM   3998  C  C     . TYR A 1 575 ? 106.554 125.875 130.294 1.00 101.56 ? 575  TYR A C     1 
ATOM   3999  O  O     . TYR A 1 575 ? 107.755 126.146 130.199 1.00 104.19 ? 575  TYR A O     1 
ATOM   4000  C  CB    . TYR A 1 575 ? 105.779 124.524 132.252 1.00 101.49 ? 575  TYR A CB    1 
ATOM   4001  C  CG    . TYR A 1 575 ? 107.107 123.812 132.322 1.00 103.57 ? 575  TYR A CG    1 
ATOM   4002  C  CD1   . TYR A 1 575 ? 108.123 124.280 133.140 1.00 107.90 ? 575  TYR A CD1   1 
ATOM   4003  C  CD2   . TYR A 1 575 ? 107.342 122.665 131.581 1.00 105.97 ? 575  TYR A CD2   1 
ATOM   4004  C  CE1   . TYR A 1 575 ? 109.336 123.632 133.213 1.00 110.87 ? 575  TYR A CE1   1 
ATOM   4005  C  CE2   . TYR A 1 575 ? 108.552 122.009 131.648 1.00 111.56 ? 575  TYR A CE2   1 
ATOM   4006  C  CZ    . TYR A 1 575 ? 109.545 122.498 132.467 1.00 112.11 ? 575  TYR A CZ    1 
ATOM   4007  O  OH    . TYR A 1 575 ? 110.755 121.851 132.540 1.00 117.52 ? 575  TYR A OH    1 
ATOM   4008  N  N     . VAL A 1 576 ? 105.813 125.536 129.238 1.00 100.94 ? 576  VAL A N     1 
ATOM   4009  C  CA    . VAL A 1 576 ? 106.388 125.579 127.895 1.00 97.89  ? 576  VAL A CA    1 
ATOM   4010  C  C     . VAL A 1 576 ? 106.825 127.000 127.556 1.00 98.91  ? 576  VAL A C     1 
ATOM   4011  O  O     . VAL A 1 576 ? 107.942 127.232 127.067 1.00 101.28 ? 576  VAL A O     1 
ATOM   4012  C  CB    . VAL A 1 576 ? 105.385 125.036 126.862 1.00 96.30  ? 576  VAL A CB    1 
ATOM   4013  C  CG1   . VAL A 1 576 ? 105.826 125.397 125.457 1.00 90.12  ? 576  VAL A CG1   1 
ATOM   4014  C  CG2   . VAL A 1 576 ? 105.245 123.533 127.007 1.00 102.54 ? 576  VAL A CG2   1 
ATOM   4015  N  N     . TYR A 1 577 ? 105.954 127.976 127.831 1.00 101.96 ? 577  TYR A N     1 
ATOM   4016  C  CA    . TYR A 1 577 ? 106.308 129.366 127.557 1.00 101.57 ? 577  TYR A CA    1 
ATOM   4017  C  C     . TYR A 1 577 ? 107.518 129.801 128.370 1.00 100.62 ? 577  TYR A C     1 
ATOM   4018  O  O     . TYR A 1 577 ? 108.389 130.513 127.865 1.00 103.01 ? 577  TYR A O     1 
ATOM   4019  C  CB    . TYR A 1 577 ? 105.132 130.294 127.847 1.00 99.68  ? 577  TYR A CB    1 
ATOM   4020  C  CG    . TYR A 1 577 ? 105.574 131.723 128.060 1.00 98.15  ? 577  TYR A CG    1 
ATOM   4021  C  CD1   . TYR A 1 577 ? 105.860 132.546 126.984 1.00 102.12 ? 577  TYR A CD1   1 
ATOM   4022  C  CD2   . TYR A 1 577 ? 105.720 132.243 129.338 1.00 94.67  ? 577  TYR A CD2   1 
ATOM   4023  C  CE1   . TYR A 1 577 ? 106.271 133.848 127.172 1.00 102.29 ? 577  TYR A CE1   1 
ATOM   4024  C  CE2   . TYR A 1 577 ? 106.136 133.540 129.535 1.00 92.40  ? 577  TYR A CE2   1 
ATOM   4025  C  CZ    . TYR A 1 577 ? 106.407 134.339 128.449 1.00 99.08  ? 577  TYR A CZ    1 
ATOM   4026  O  OH    . TYR A 1 577 ? 106.816 135.637 128.644 1.00 106.16 ? 577  TYR A OH    1 
ATOM   4027  N  N     . HIS A 1 578 ? 107.568 129.413 129.643 1.00 96.96  ? 578  HIS A N     1 
ATOM   4028  C  CA    . HIS A 1 578 ? 108.665 129.806 130.516 1.00 95.27  ? 578  HIS A CA    1 
ATOM   4029  C  C     . HIS A 1 578 ? 109.976 129.198 130.050 1.00 101.59 ? 578  HIS A C     1 
ATOM   4030  O  O     . HIS A 1 578 ? 111.020 129.857 130.083 1.00 103.86 ? 578  HIS A O     1 
ATOM   4031  C  CB    . HIS A 1 578 ? 108.352 129.383 131.950 1.00 96.98  ? 578  HIS A CB    1 
ATOM   4032  C  CG    . HIS A 1 578 ? 109.266 129.975 132.974 1.00 102.02 ? 578  HIS A CG    1 
ATOM   4033  N  ND1   . HIS A 1 578 ? 109.639 131.301 132.962 1.00 109.33 ? 578  HIS A ND1   1 
ATOM   4034  C  CD2   . HIS A 1 578 ? 109.867 129.424 134.055 1.00 106.17 ? 578  HIS A CD2   1 
ATOM   4035  C  CE1   . HIS A 1 578 ? 110.439 131.540 133.985 1.00 114.45 ? 578  HIS A CE1   1 
ATOM   4036  N  NE2   . HIS A 1 578 ? 110.594 130.418 134.664 1.00 115.13 ? 578  HIS A NE2   1 
ATOM   4037  N  N     . LEU A 1 579 ? 109.943 127.938 129.615 1.00 105.79 ? 579  LEU A N     1 
ATOM   4038  C  CA    . LEU A 1 579 ? 111.140 127.305 129.078 1.00 104.24 ? 579  LEU A CA    1 
ATOM   4039  C  C     . LEU A 1 579 ? 111.636 128.046 127.843 1.00 103.07 ? 579  LEU A C     1 
ATOM   4040  O  O     . LEU A 1 579 ? 112.830 128.348 127.725 1.00 105.75 ? 579  LEU A O     1 
ATOM   4041  C  CB    . LEU A 1 579 ? 110.847 125.842 128.752 1.00 103.13 ? 579  LEU A CB    1 
ATOM   4042  C  CG    . LEU A 1 579 ? 111.586 124.802 129.590 1.00 105.41 ? 579  LEU A CG    1 
ATOM   4043  C  CD1   . LEU A 1 579 ? 111.445 123.427 128.967 1.00 112.07 ? 579  LEU A CD1   1 
ATOM   4044  C  CD2   . LEU A 1 579 ? 113.045 125.184 129.727 1.00 103.47 ? 579  LEU A CD2   1 
ATOM   4045  N  N     . LEU A 1 580 ? 110.725 128.367 126.919 1.00 101.18 ? 580  LEU A N     1 
ATOM   4046  C  CA    . LEU A 1 580 ? 111.134 129.098 125.721 1.00 98.90  ? 580  LEU A CA    1 
ATOM   4047  C  C     . LEU A 1 580 ? 111.688 130.475 126.071 1.00 101.79 ? 580  LEU A C     1 
ATOM   4048  O  O     . LEU A 1 580 ? 112.716 130.897 125.528 1.00 106.50 ? 580  LEU A O     1 
ATOM   4049  C  CB    . LEU A 1 580 ? 109.960 129.228 124.753 1.00 100.31 ? 580  LEU A CB    1 
ATOM   4050  C  CG    . LEU A 1 580 ? 109.483 127.941 124.083 1.00 114.20 ? 580  LEU A CG    1 
ATOM   4051  C  CD1   . LEU A 1 580 ? 108.550 128.266 122.931 1.00 120.70 ? 580  LEU A CD1   1 
ATOM   4052  C  CD2   . LEU A 1 580 ? 110.665 127.119 123.602 1.00 115.94 ? 580  LEU A CD2   1 
ATOM   4053  N  N     . TYR A 1 581 ? 111.020 131.187 126.980 1.00 102.08 ? 581  TYR A N     1 
ATOM   4054  C  CA    . TYR A 1 581 ? 111.448 132.531 127.346 1.00 101.57 ? 581  TYR A CA    1 
ATOM   4055  C  C     . TYR A 1 581 ? 112.808 132.513 128.029 1.00 103.20 ? 581  TYR A C     1 
ATOM   4056  O  O     . TYR A 1 581 ? 113.658 133.366 127.755 1.00 109.96 ? 581  TYR A O     1 
ATOM   4057  C  CB    . TYR A 1 581 ? 110.402 133.177 128.252 1.00 101.91 ? 581  TYR A CB    1 
ATOM   4058  C  CG    . TYR A 1 581 ? 110.726 134.589 128.671 1.00 101.93 ? 581  TYR A CG    1 
ATOM   4059  C  CD1   . TYR A 1 581 ? 110.505 135.654 127.813 1.00 106.29 ? 581  TYR A CD1   1 
ATOM   4060  C  CD2   . TYR A 1 581 ? 111.244 134.858 129.928 1.00 103.36 ? 581  TYR A CD2   1 
ATOM   4061  C  CE1   . TYR A 1 581 ? 110.796 136.946 128.192 1.00 113.41 ? 581  TYR A CE1   1 
ATOM   4062  C  CE2   . TYR A 1 581 ? 111.538 136.147 130.316 1.00 109.42 ? 581  TYR A CE2   1 
ATOM   4063  C  CZ    . TYR A 1 581 ? 111.312 137.187 129.444 1.00 114.31 ? 581  TYR A CZ    1 
ATOM   4064  O  OH    . TYR A 1 581 ? 111.604 138.475 129.826 1.00 117.63 ? 581  TYR A OH    1 
ATOM   4065  N  N     . THR A 1 582 ? 113.031 131.551 128.926 1.00 99.62  ? 582  THR A N     1 
ATOM   4066  C  CA    . THR A 1 582 ? 114.319 131.451 129.599 1.00 99.35  ? 582  THR A CA    1 
ATOM   4067  C  C     . THR A 1 582 ? 115.421 131.074 128.620 1.00 100.78 ? 582  THR A C     1 
ATOM   4068  O  O     . THR A 1 582 ? 116.536 131.604 128.695 1.00 101.78 ? 582  THR A O     1 
ATOM   4069  C  CB    . THR A 1 582 ? 114.232 130.432 130.733 1.00 100.11 ? 582  THR A CB    1 
ATOM   4070  O  OG1   . THR A 1 582 ? 113.363 130.938 131.751 1.00 109.83 ? 582  THR A OG1   1 
ATOM   4071  C  CG2   . THR A 1 582 ? 115.602 130.183 131.335 1.00 94.88  ? 582  THR A CG2   1 
ATOM   4072  N  N     . ALA A 1 583 ? 115.128 130.166 127.685 1.00 99.53  ? 583  ALA A N     1 
ATOM   4073  C  CA    . ALA A 1 583 ? 116.118 129.815 126.674 1.00 95.97  ? 583  ALA A CA    1 
ATOM   4074  C  C     . ALA A 1 583 ? 116.479 131.023 125.822 1.00 100.19 ? 583  ALA A C     1 
ATOM   4075  O  O     . ALA A 1 583 ? 117.653 131.230 125.494 1.00 104.73 ? 583  ALA A O     1 
ATOM   4076  C  CB    . ALA A 1 583 ? 115.598 128.676 125.800 1.00 93.76  ? 583  ALA A CB    1 
ATOM   4077  N  N     . PHE A 1 584 ? 115.485 131.832 125.452 1.00 101.72 ? 584  PHE A N     1 
ATOM   4078  C  CA    . PHE A 1 584 ? 115.772 133.033 124.674 1.00 100.93 ? 584  PHE A CA    1 
ATOM   4079  C  C     . PHE A 1 584 ? 116.580 134.037 125.485 1.00 100.29 ? 584  PHE A C     1 
ATOM   4080  O  O     . PHE A 1 584 ? 117.525 134.644 124.970 1.00 105.68 ? 584  PHE A O     1 
ATOM   4081  C  CB    . PHE A 1 584 ? 114.475 133.670 124.180 1.00 99.46  ? 584  PHE A CB    1 
ATOM   4082  C  CG    . PHE A 1 584 ? 114.673 134.995 123.503 1.00 100.03 ? 584  PHE A CG    1 
ATOM   4083  C  CD1   . PHE A 1 584 ? 115.042 135.056 122.173 1.00 104.31 ? 584  PHE A CD1   1 
ATOM   4084  C  CD2   . PHE A 1 584 ? 114.483 136.178 124.193 1.00 100.50 ? 584  PHE A CD2   1 
ATOM   4085  C  CE1   . PHE A 1 584 ? 115.225 136.270 121.545 1.00 107.13 ? 584  PHE A CE1   1 
ATOM   4086  C  CE2   . PHE A 1 584 ? 114.664 137.395 123.570 1.00 103.15 ? 584  PHE A CE2   1 
ATOM   4087  C  CZ    . PHE A 1 584 ? 115.035 137.440 122.245 1.00 103.48 ? 584  PHE A CZ    1 
ATOM   4088  N  N     . GLY A 1 585 ? 116.223 134.228 126.756 1.00 98.18  ? 585  GLY A N     1 
ATOM   4089  C  CA    . GLY A 1 585 ? 116.933 135.190 127.578 1.00 98.77  ? 585  GLY A CA    1 
ATOM   4090  C  C     . GLY A 1 585 ? 118.346 134.762 127.911 1.00 101.26 ? 585  GLY A C     1 
ATOM   4091  O  O     . GLY A 1 585 ? 119.196 135.602 128.216 1.00 102.62 ? 585  GLY A O     1 
ATOM   4092  N  N     . PHE A 1 586 ? 118.617 133.456 127.873 1.00 102.72 ? 586  PHE A N     1 
ATOM   4093  C  CA    . PHE A 1 586 ? 119.977 132.984 128.099 1.00 103.06 ? 586  PHE A CA    1 
ATOM   4094  C  C     . PHE A 1 586 ? 120.907 133.435 126.981 1.00 103.14 ? 586  PHE A C     1 
ATOM   4095  O  O     . PHE A 1 586 ? 122.045 133.844 127.235 1.00 102.45 ? 586  PHE A O     1 
ATOM   4096  C  CB    . PHE A 1 586 ? 119.987 131.463 128.231 1.00 102.85 ? 586  PHE A CB    1 
ATOM   4097  C  CG    . PHE A 1 586 ? 121.318 130.897 128.625 1.00 103.13 ? 586  PHE A CG    1 
ATOM   4098  C  CD1   . PHE A 1 586 ? 121.784 131.035 129.918 1.00 104.73 ? 586  PHE A CD1   1 
ATOM   4099  C  CD2   . PHE A 1 586 ? 122.098 130.222 127.706 1.00 104.02 ? 586  PHE A CD2   1 
ATOM   4100  C  CE1   . PHE A 1 586 ? 123.005 130.514 130.286 1.00 107.03 ? 586  PHE A CE1   1 
ATOM   4101  C  CE2   . PHE A 1 586 ? 123.319 129.699 128.069 1.00 107.09 ? 586  PHE A CE2   1 
ATOM   4102  C  CZ    . PHE A 1 586 ? 123.773 129.845 129.360 1.00 106.89 ? 586  PHE A CZ    1 
ATOM   4103  N  N     . PHE A 1 587 ? 120.440 133.367 125.735 1.00 101.57 ? 587  PHE A N     1 
ATOM   4104  C  CA    . PHE A 1 587 ? 121.201 133.807 124.567 1.00 97.28  ? 587  PHE A CA    1 
ATOM   4105  C  C     . PHE A 1 587 ? 120.888 135.250 124.200 1.00 97.35  ? 587  PHE A C     1 
ATOM   4106  O  O     . PHE A 1 587 ? 121.004 135.640 123.036 1.00 98.35  ? 587  PHE A O     1 
ATOM   4107  C  CB    . PHE A 1 587 ? 120.931 132.889 123.380 1.00 94.23  ? 587  PHE A CB    1 
ATOM   4108  C  CG    . PHE A 1 587 ? 121.332 131.464 123.610 1.00 97.37  ? 587  PHE A CG    1 
ATOM   4109  C  CD1   . PHE A 1 587 ? 122.647 131.070 123.459 1.00 102.28 ? 587  PHE A CD1   1 
ATOM   4110  C  CD2   . PHE A 1 587 ? 120.393 130.517 123.969 1.00 98.76  ? 587  PHE A CD2   1 
ATOM   4111  C  CE1   . PHE A 1 587 ? 123.018 129.760 123.668 1.00 106.51 ? 587  PHE A CE1   1 
ATOM   4112  C  CE2   . PHE A 1 587 ? 120.759 129.206 124.179 1.00 102.71 ? 587  PHE A CE2   1 
ATOM   4113  C  CZ    . PHE A 1 587 ? 122.073 128.827 124.028 1.00 107.01 ? 587  PHE A CZ    1 
ATOM   4114  N  N     . LEU A 1 588 ? 120.468 136.055 125.169 1.00 97.22  ? 588  LEU A N     1 
ATOM   4115  C  CA    . LEU A 1 588 ? 120.106 137.444 124.915 1.00 95.77  ? 588  LEU A CA    1 
ATOM   4116  C  C     . LEU A 1 588 ? 121.280 138.288 124.424 1.00 98.25  ? 588  LEU A C     1 
ATOM   4117  O  O     . LEU A 1 588 ? 121.100 139.065 123.480 1.00 102.61 ? 588  LEU A O     1 
ATOM   4118  C  CB    . LEU A 1 588 ? 119.488 138.077 126.164 1.00 97.38  ? 588  LEU A CB    1 
ATOM   4119  C  CG    . LEU A 1 588 ? 118.656 139.329 125.895 1.00 99.42  ? 588  LEU A CG    1 
ATOM   4120  C  CD1   . LEU A 1 588 ? 117.717 139.098 124.727 1.00 97.99  ? 588  LEU A CD1   1 
ATOM   4121  C  CD2   . LEU A 1 588 ? 117.878 139.723 127.136 1.00 105.54 ? 588  LEU A CD2   1 
ATOM   4122  N  N     . PRO A 1 589 ? 122.474 138.215 125.031 1.00 98.69  ? 589  PRO A N     1 
ATOM   4123  C  CA    . PRO A 1 589 ? 123.591 139.005 124.482 1.00 94.98  ? 589  PRO A CA    1 
ATOM   4124  C  C     . PRO A 1 589 ? 123.939 138.636 123.053 1.00 94.46  ? 589  PRO A C     1 
ATOM   4125  O  O     . PRO A 1 589 ? 124.150 139.525 122.216 1.00 95.11  ? 589  PRO A O     1 
ATOM   4126  C  CB    . PRO A 1 589 ? 124.745 138.695 125.443 1.00 95.53  ? 589  PRO A CB    1 
ATOM   4127  C  CG    . PRO A 1 589 ? 124.091 138.297 126.698 1.00 99.84  ? 589  PRO A CG    1 
ATOM   4128  C  CD    . PRO A 1 589 ? 122.859 137.556 126.292 1.00 100.46 ? 589  PRO A CD    1 
ATOM   4129  N  N     . ALA A 1 590 ? 123.997 137.338 122.749 1.00 94.05  ? 590  ALA A N     1 
ATOM   4130  C  CA    . ALA A 1 590 ? 124.299 136.911 121.389 1.00 90.64  ? 590  ALA A CA    1 
ATOM   4131  C  C     . ALA A 1 590 ? 123.221 137.370 120.419 1.00 93.99  ? 590  ALA A C     1 
ATOM   4132  O  O     . ALA A 1 590 ? 123.529 137.844 119.321 1.00 101.17 ? 590  ALA A O     1 
ATOM   4133  C  CB    . ALA A 1 590 ? 124.457 135.394 121.337 1.00 93.05  ? 590  ALA A CB    1 
ATOM   4134  N  N     . ASN A 1 591 ? 121.951 137.242 120.808 1.00 94.40  ? 591  ASN A N     1 
ATOM   4135  C  CA    . ASN A 1 591 ? 120.867 137.670 119.930 1.00 93.59  ? 591  ASN A CA    1 
ATOM   4136  C  C     . ASN A 1 591 ? 120.897 139.174 119.699 1.00 93.82  ? 591  ASN A C     1 
ATOM   4137  O  O     . ASN A 1 591 ? 120.661 139.634 118.580 1.00 98.60  ? 591  ASN A O     1 
ATOM   4138  C  CB    . ASN A 1 591 ? 119.521 137.241 120.506 1.00 96.65  ? 591  ASN A CB    1 
ATOM   4139  C  CG    . ASN A 1 591 ? 119.220 135.784 120.248 1.00 104.60 ? 591  ASN A CG    1 
ATOM   4140  O  OD1   . ASN A 1 591 ? 119.680 135.211 119.264 1.00 104.30 ? 591  ASN A OD1   1 
ATOM   4141  N  ND2   . ASN A 1 591 ? 118.442 135.175 121.133 1.00 106.21 ? 591  ASN A ND2   1 
ATOM   4142  N  N     . LEU A 1 592 ? 121.182 139.956 120.741 1.00 93.68  ? 592  LEU A N     1 
ATOM   4143  C  CA    . LEU A 1 592 ? 121.272 141.403 120.572 1.00 90.83  ? 592  LEU A CA    1 
ATOM   4144  C  C     . LEU A 1 592 ? 122.416 141.774 119.641 1.00 93.95  ? 592  LEU A C     1 
ATOM   4145  O  O     . LEU A 1 592 ? 122.261 142.621 118.752 1.00 99.90  ? 592  LEU A O     1 
ATOM   4146  C  CB    . LEU A 1 592 ? 121.451 142.084 121.927 1.00 91.93  ? 592  LEU A CB    1 
ATOM   4147  C  CG    . LEU A 1 592 ? 121.738 143.582 121.833 1.00 88.41  ? 592  LEU A CG    1 
ATOM   4148  C  CD1   . LEU A 1 592 ? 120.484 144.344 121.450 1.00 94.35  ? 592  LEU A CD1   1 
ATOM   4149  C  CD2   . LEU A 1 592 ? 122.315 144.106 123.130 1.00 95.98  ? 592  LEU A CD2   1 
ATOM   4150  N  N     . TYR A 1 593 ? 123.582 141.151 119.835 1.00 94.61  ? 593  TYR A N     1 
ATOM   4151  C  CA    . TYR A 1 593 ? 124.716 141.442 118.968 1.00 96.26  ? 593  TYR A CA    1 
ATOM   4152  C  C     . TYR A 1 593 ? 124.398 141.084 117.525 1.00 95.60  ? 593  TYR A C     1 
ATOM   4153  O  O     . TYR A 1 593 ? 124.689 141.854 116.606 1.00 100.42 ? 593  TYR A O     1 
ATOM   4154  C  CB    . TYR A 1 593 ? 125.958 140.693 119.440 1.00 98.41  ? 593  TYR A CB    1 
ATOM   4155  C  CG    . TYR A 1 593 ? 127.021 140.577 118.373 1.00 101.72 ? 593  TYR A CG    1 
ATOM   4156  C  CD1   . TYR A 1 593 ? 127.855 141.645 118.081 1.00 105.02 ? 593  TYR A CD1   1 
ATOM   4157  C  CD2   . TYR A 1 593 ? 127.191 139.403 117.656 1.00 104.33 ? 593  TYR A CD2   1 
ATOM   4158  C  CE1   . TYR A 1 593 ? 128.825 141.548 117.108 1.00 108.92 ? 593  TYR A CE1   1 
ATOM   4159  C  CE2   . TYR A 1 593 ? 128.158 139.298 116.681 1.00 106.08 ? 593  TYR A CE2   1 
ATOM   4160  C  CZ    . TYR A 1 593 ? 128.972 140.373 116.412 1.00 111.39 ? 593  TYR A CZ    1 
ATOM   4161  O  OH    . TYR A 1 593 ? 129.938 140.272 115.441 1.00 116.20 ? 593  TYR A OH    1 
ATOM   4162  N  N     . LEU A 1 594 ? 123.792 139.915 117.308 1.00 94.76  ? 594  LEU A N     1 
ATOM   4163  C  CA    . LEU A 1 594 ? 123.460 139.498 115.952 1.00 95.88  ? 594  LEU A CA    1 
ATOM   4164  C  C     . LEU A 1 594 ? 122.435 140.429 115.323 1.00 100.64 ? 594  LEU A C     1 
ATOM   4165  O  O     . LEU A 1 594 ? 122.558 140.790 114.150 1.00 106.00 ? 594  LEU A O     1 
ATOM   4166  C  CB    . LEU A 1 594 ? 122.946 138.061 115.954 1.00 95.77  ? 594  LEU A CB    1 
ATOM   4167  C  CG    . LEU A 1 594 ? 123.991 137.007 116.303 1.00 99.52  ? 594  LEU A CG    1 
ATOM   4168  C  CD1   . LEU A 1 594 ? 123.324 135.679 116.585 1.00 99.82  ? 594  LEU A CD1   1 
ATOM   4169  C  CD2   . LEU A 1 594 ? 124.998 136.881 115.186 1.00 98.15  ? 594  LEU A CD2   1 
ATOM   4170  N  N     . ALA A 1 595 ? 121.419 140.835 116.086 1.00 97.72  ? 595  ALA A N     1 
ATOM   4171  C  CA    . ALA A 1 595 ? 120.396 141.720 115.543 1.00 95.15  ? 595  ALA A CA    1 
ATOM   4172  C  C     . ALA A 1 595 ? 120.992 143.059 115.137 1.00 98.32  ? 595  ALA A C     1 
ATOM   4173  O  O     . ALA A 1 595 ? 120.775 143.534 114.015 1.00 105.38 ? 595  ALA A O     1 
ATOM   4174  C  CB    . ALA A 1 595 ? 119.276 141.914 116.564 1.00 95.10  ? 595  ALA A CB    1 
ATOM   4175  N  N     . LEU A 1 596 ? 121.757 143.682 116.038 1.00 95.05  ? 596  LEU A N     1 
ATOM   4176  C  CA    . LEU A 1 596 ? 122.389 144.953 115.705 1.00 98.18  ? 596  LEU A CA    1 
ATOM   4177  C  C     . LEU A 1 596 ? 123.306 144.801 114.501 1.00 105.17 ? 596  LEU A C     1 
ATOM   4178  O  O     . LEU A 1 596 ? 123.180 145.536 113.512 1.00 110.72 ? 596  LEU A O     1 
ATOM   4179  C  CB    . LEU A 1 596 ? 123.171 145.487 116.904 1.00 95.56  ? 596  LEU A CB    1 
ATOM   4180  C  CG    . LEU A 1 596 ? 122.361 145.953 118.111 1.00 102.73 ? 596  LEU A CG    1 
ATOM   4181  C  CD1   . LEU A 1 596 ? 123.259 146.667 119.103 1.00 104.77 ? 596  LEU A CD1   1 
ATOM   4182  C  CD2   . LEU A 1 596 ? 121.219 146.846 117.674 1.00 102.10 ? 596  LEU A CD2   1 
ATOM   4183  N  N     . PHE A 1 597 ? 124.219 143.826 114.559 1.00 103.69 ? 597  PHE A N     1 
ATOM   4184  C  CA    . PHE A 1 597 ? 125.162 143.594 113.474 1.00 101.38 ? 597  PHE A CA    1 
ATOM   4185  C  C     . PHE A 1 597 ? 124.433 143.455 112.149 1.00 102.01 ? 597  PHE A C     1 
ATOM   4186  O  O     . PHE A 1 597 ? 124.594 144.291 111.254 1.00 110.45 ? 597  PHE A O     1 
ATOM   4187  C  CB    . PHE A 1 597 ? 125.992 142.346 113.780 1.00 102.39 ? 597  PHE A CB    1 
ATOM   4188  C  CG    . PHE A 1 597 ? 126.783 141.832 112.614 1.00 101.07 ? 597  PHE A CG    1 
ATOM   4189  C  CD1   . PHE A 1 597 ? 127.921 142.491 112.192 1.00 103.77 ? 597  PHE A CD1   1 
ATOM   4190  C  CD2   . PHE A 1 597 ? 126.407 140.674 111.963 1.00 102.67 ? 597  PHE A CD2   1 
ATOM   4191  C  CE1   . PHE A 1 597 ? 128.657 142.015 111.130 1.00 105.98 ? 597  PHE A CE1   1 
ATOM   4192  C  CE2   . PHE A 1 597 ? 127.140 140.194 110.901 1.00 97.70  ? 597  PHE A CE2   1 
ATOM   4193  C  CZ    . PHE A 1 597 ? 128.267 140.865 110.485 1.00 99.59  ? 597  PHE A CZ    1 
ATOM   4194  N  N     . PHE A 1 598 ? 123.558 142.454 112.041 1.00 96.75  ? 598  PHE A N     1 
ATOM   4195  C  CA    . PHE A 1 598 ? 122.833 142.208 110.806 1.00 99.63  ? 598  PHE A CA    1 
ATOM   4196  C  C     . PHE A 1 598 ? 122.122 143.472 110.362 1.00 105.20 ? 598  PHE A C     1 
ATOM   4197  O  O     . PHE A 1 598 ? 122.590 144.110 109.416 1.00 115.80 ? 598  PHE A O     1 
ATOM   4198  C  CB    . PHE A 1 598 ? 121.839 141.061 110.978 1.00 99.47  ? 598  PHE A CB    1 
ATOM   4199  C  CG    . PHE A 1 598 ? 122.466 139.702 110.892 1.00 103.38 ? 598  PHE A CG    1 
ATOM   4200  C  CD1   . PHE A 1 598 ? 123.650 139.518 110.205 1.00 103.94 ? 598  PHE A CD1   1 
ATOM   4201  C  CD2   . PHE A 1 598 ? 121.877 138.612 111.501 1.00 106.65 ? 598  PHE A CD2   1 
ATOM   4202  C  CE1   . PHE A 1 598 ? 124.231 138.273 110.125 1.00 101.15 ? 598  PHE A CE1   1 
ATOM   4203  C  CE2   . PHE A 1 598 ? 122.456 137.366 111.422 1.00 104.06 ? 598  PHE A CE2   1 
ATOM   4204  C  CZ    . PHE A 1 598 ? 123.634 137.197 110.734 1.00 100.38 ? 598  PHE A CZ    1 
ATOM   4205  N  N     . ILE A 1 599 ? 121.106 143.921 111.106 1.00 101.64 ? 599  ILE A N     1 
ATOM   4206  C  CA    . ILE A 1 599 ? 120.268 145.013 110.624 1.00 105.76 ? 599  ILE A CA    1 
ATOM   4207  C  C     . ILE A 1 599 ? 121.139 146.201 110.247 1.00 110.80 ? 599  ILE A C     1 
ATOM   4208  O  O     . ILE A 1 599 ? 121.337 146.475 109.058 1.00 119.34 ? 599  ILE A O     1 
ATOM   4209  C  CB    . ILE A 1 599 ? 119.228 145.436 111.676 1.00 99.22  ? 599  ILE A CB    1 
ATOM   4210  C  CG1   . ILE A 1 599 ? 118.244 144.306 111.955 1.00 98.66  ? 599  ILE A CG1   1 
ATOM   4211  C  CG2   . ILE A 1 599 ? 118.482 146.673 111.216 1.00 101.57 ? 599  ILE A CG2   1 
ATOM   4212  C  CD1   . ILE A 1 599 ? 117.198 144.670 112.977 1.00 96.17  ? 599  ILE A CD1   1 
ATOM   4213  N  N     . VAL A 1 600 ? 121.785 146.816 111.237 1.00 103.36 ? 600  VAL A N     1 
ATOM   4214  C  CA    . VAL A 1 600 ? 122.450 148.089 110.987 1.00 103.61 ? 600  VAL A CA    1 
ATOM   4215  C  C     . VAL A 1 600 ? 123.616 147.904 110.025 1.00 111.96 ? 600  VAL A C     1 
ATOM   4216  O  O     . VAL A 1 600 ? 123.635 148.474 108.928 1.00 119.68 ? 600  VAL A O     1 
ATOM   4217  C  CB    . VAL A 1 600 ? 122.909 148.725 112.308 1.00 105.67 ? 600  VAL A CB    1 
ATOM   4218  C  CG1   . VAL A 1 600 ? 123.612 150.039 112.038 1.00 110.57 ? 600  VAL A CG1   1 
ATOM   4219  C  CG2   . VAL A 1 600 ? 121.722 148.930 113.222 1.00 109.80 ? 600  VAL A CG2   1 
ATOM   4220  N  N     . PHE A 1 601 ? 124.599 147.091 110.409 1.00 109.06 ? 601  PHE A N     1 
ATOM   4221  C  CA    . PHE A 1 601 ? 125.870 147.143 109.708 1.00 109.92 ? 601  PHE A CA    1 
ATOM   4222  C  C     . PHE A 1 601 ? 125.879 146.294 108.444 1.00 112.78 ? 601  PHE A C     1 
ATOM   4223  O  O     . PHE A 1 601 ? 126.607 146.625 107.505 1.00 121.42 ? 601  PHE A O     1 
ATOM   4224  C  CB    . PHE A 1 601 ? 126.983 146.747 110.672 1.00 105.16 ? 601  PHE A CB    1 
ATOM   4225  C  CG    . PHE A 1 601 ? 127.049 147.634 111.881 1.00 108.71 ? 601  PHE A CG    1 
ATOM   4226  C  CD1   . PHE A 1 601 ? 126.321 147.334 113.017 1.00 108.73 ? 601  PHE A CD1   1 
ATOM   4227  C  CD2   . PHE A 1 601 ? 127.804 148.792 111.866 1.00 113.91 ? 601  PHE A CD2   1 
ATOM   4228  C  CE1   . PHE A 1 601 ? 126.361 148.159 114.122 1.00 106.00 ? 601  PHE A CE1   1 
ATOM   4229  C  CE2   . PHE A 1 601 ? 127.850 149.619 112.970 1.00 114.07 ? 601  PHE A CE2   1 
ATOM   4230  C  CZ    . PHE A 1 601 ? 127.128 149.301 114.099 1.00 104.65 ? 601  PHE A CZ    1 
ATOM   4231  N  N     . GLN A 1 602 ? 125.089 145.221 108.364 1.00 110.78 ? 602  GLN A N     1 
ATOM   4232  C  CA    . GLN A 1 602 ? 124.934 144.539 107.094 1.00 118.76 ? 602  GLN A CA    1 
ATOM   4233  C  C     . GLN A 1 602 ? 123.739 145.053 106.302 1.00 125.89 ? 602  GLN A C     1 
ATOM   4234  O  O     . GLN A 1 602 ? 123.358 144.424 105.309 1.00 133.88 ? 602  GLN A O     1 
ATOM   4235  C  CB    . GLN A 1 602 ? 124.817 143.029 107.307 1.00 117.03 ? 602  GLN A CB    1 
ATOM   4236  C  CG    . GLN A 1 602 ? 126.142 142.342 107.571 1.00 113.27 ? 602  GLN A CG    1 
ATOM   4237  C  CD    . GLN A 1 602 ? 126.105 140.870 107.221 1.00 115.37 ? 602  GLN A CD    1 
ATOM   4238  O  OE1   . GLN A 1 602 ? 125.168 140.398 106.578 1.00 119.72 ? 602  GLN A OE1   1 
ATOM   4239  N  NE2   . GLN A 1 602 ? 127.131 140.137 107.631 1.00 110.09 ? 602  GLN A NE2   1 
ATOM   4240  N  N     . GLY A 1 603 ? 123.125 146.160 106.724 1.00 121.65 ? 603  GLY A N     1 
ATOM   4241  C  CA    . GLY A 1 603 ? 122.330 146.933 105.799 1.00 128.22 ? 603  GLY A CA    1 
ATOM   4242  C  C     . GLY A 1 603 ? 123.166 148.052 105.222 1.00 131.30 ? 603  GLY A C     1 
ATOM   4243  O  O     . GLY A 1 603 ? 123.012 148.424 104.056 1.00 137.67 ? 603  GLY A O     1 
ATOM   4244  N  N     . PHE A 1 604 ? 124.063 148.597 106.047 1.00 126.22 ? 604  PHE A N     1 
ATOM   4245  C  CA    . PHE A 1 604 ? 124.952 149.652 105.577 1.00 126.92 ? 604  PHE A CA    1 
ATOM   4246  C  C     . PHE A 1 604 ? 126.004 149.108 104.617 1.00 128.56 ? 604  PHE A C     1 
ATOM   4247  O  O     . PHE A 1 604 ? 126.242 149.693 103.554 1.00 133.29 ? 604  PHE A O     1 
ATOM   4248  C  CB    . PHE A 1 604 ? 125.617 150.343 106.765 1.00 122.27 ? 604  PHE A CB    1 
ATOM   4249  C  CG    . PHE A 1 604 ? 126.584 151.419 106.375 1.00 123.52 ? 604  PHE A CG    1 
ATOM   4250  C  CD1   . PHE A 1 604 ? 126.130 152.651 105.940 1.00 128.45 ? 604  PHE A CD1   1 
ATOM   4251  C  CD2   . PHE A 1 604 ? 127.947 151.201 106.446 1.00 124.78 ? 604  PHE A CD2   1 
ATOM   4252  C  CE1   . PHE A 1 604 ? 127.018 153.644 105.582 1.00 129.92 ? 604  PHE A CE1   1 
ATOM   4253  C  CE2   . PHE A 1 604 ? 128.839 152.191 106.089 1.00 125.74 ? 604  PHE A CE2   1 
ATOM   4254  C  CZ    . PHE A 1 604 ? 128.374 153.414 105.656 1.00 124.80 ? 604  PHE A CZ    1 
ATOM   4255  N  N     . GLN A 1 605 ? 126.640 147.990 104.971 1.00 124.55 ? 605  GLN A N     1 
ATOM   4256  C  CA    . GLN A 1 605 ? 127.725 147.464 104.151 1.00 128.08 ? 605  GLN A CA    1 
ATOM   4257  C  C     . GLN A 1 605 ? 127.204 146.838 102.864 1.00 130.62 ? 605  GLN A C     1 
ATOM   4258  O  O     . GLN A 1 605 ? 127.805 147.011 101.797 1.00 135.63 ? 605  GLN A O     1 
ATOM   4259  C  CB    . GLN A 1 605 ? 128.534 146.444 104.952 1.00 125.21 ? 605  GLN A CB    1 
ATOM   4260  C  CG    . GLN A 1 605 ? 129.498 145.627 104.116 1.00 126.07 ? 605  GLN A CG    1 
ATOM   4261  C  CD    . GLN A 1 605 ? 130.244 144.594 104.931 1.00 129.17 ? 605  GLN A CD    1 
ATOM   4262  O  OE1   . GLN A 1 605 ? 131.118 144.928 105.728 1.00 125.73 ? 605  GLN A OE1   1 
ATOM   4263  N  NE2   . GLN A 1 605 ? 129.901 143.327 104.734 1.00 132.26 ? 605  GLN A NE2   1 
ATOM   4264  N  N     . GLN A 1 606 ? 126.084 146.122 102.936 1.00 125.37 ? 606  GLN A N     1 
ATOM   4265  C  CA    . GLN A 1 606 ? 125.563 145.387 101.793 1.00 131.02 ? 606  GLN A CA    1 
ATOM   4266  C  C     . GLN A 1 606 ? 124.408 146.109 101.111 1.00 134.58 ? 606  GLN A C     1 
ATOM   4267  O  O     . GLN A 1 606 ? 123.701 145.502 100.298 1.00 139.50 ? 606  GLN A O     1 
ATOM   4268  C  CB    . GLN A 1 606 ? 125.140 143.983 102.224 1.00 129.20 ? 606  GLN A CB    1 
ATOM   4269  C  CG    . GLN A 1 606 ? 126.199 143.263 103.039 1.00 129.27 ? 606  GLN A CG    1 
ATOM   4270  C  CD    . GLN A 1 606 ? 126.092 141.758 102.939 1.00 136.95 ? 606  GLN A CD    1 
ATOM   4271  O  OE1   . GLN A 1 606 ? 127.091 141.046 103.034 1.00 139.99 ? 606  GLN A OE1   1 
ATOM   4272  N  NE2   . GLN A 1 606 ? 124.876 141.263 102.744 1.00 138.20 ? 606  GLN A NE2   1 
ATOM   4273  N  N     . ASN A 1 607 ? 124.216 147.393 101.417 1.00 131.48 ? 607  ASN A N     1 
ATOM   4274  C  CA    . ASN A 1 607 ? 123.200 148.235 100.787 1.00 134.32 ? 607  ASN A CA    1 
ATOM   4275  C  C     . ASN A 1 607 ? 121.829 147.576 100.974 1.00 137.76 ? 607  ASN A C     1 
ATOM   4276  O  O     . ASN A 1 607 ? 121.269 146.950 100.072 1.00 142.61 ? 607  ASN A O     1 
ATOM   4277  C  CB    . ASN A 1 607 ? 123.561 148.493 99.308  1.00 139.34 ? 607  ASN A CB    1 
ATOM   4278  C  CG    . ASN A 1 607 ? 122.415 149.081 98.459  1.00 143.21 ? 607  ASN A CG    1 
ATOM   4279  O  OD1   . ASN A 1 607 ? 121.248 149.118 98.840  1.00 142.28 ? 607  ASN A OD1   1 
ATOM   4280  N  ND2   . ASN A 1 607 ? 122.778 149.542 97.271  1.00 147.82 ? 607  ASN A ND2   1 
ATOM   4281  N  N     . ARG A 1 608 ? 121.356 147.620 102.217 1.00 135.52 ? 608  ARG A N     1 
ATOM   4282  C  CA    . ARG A 1 608 ? 120.013 147.171 102.543 1.00 135.16 ? 608  ARG A CA    1 
ATOM   4283  C  C     . ARG A 1 608 ? 119.207 148.223 103.286 1.00 140.33 ? 608  ARG A C     1 
ATOM   4284  O  O     . ARG A 1 608 ? 118.010 148.017 103.517 1.00 146.93 ? 608  ARG A O     1 
ATOM   4285  C  CB    . ARG A 1 608 ? 120.068 145.875 103.357 1.00 127.52 ? 608  ARG A CB    1 
ATOM   4286  C  CG    . ARG A 1 608 ? 120.254 144.654 102.485 1.00 128.44 ? 608  ARG A CG    1 
ATOM   4287  C  CD    . ARG A 1 608 ? 120.055 143.376 103.261 1.00 126.53 ? 608  ARG A CD    1 
ATOM   4288  N  NE    . ARG A 1 608 ? 121.182 143.123 104.150 1.00 124.90 ? 608  ARG A NE    1 
ATOM   4289  C  CZ    . ARG A 1 608 ? 121.612 141.915 104.483 1.00 125.26 ? 608  ARG A CZ    1 
ATOM   4290  N  NH1   . ARG A 1 608 ? 121.045 140.822 103.999 1.00 124.97 ? 608  ARG A NH1   1 
ATOM   4291  N  NH2   . ARG A 1 608 ? 122.639 141.801 105.316 1.00 123.49 ? 608  ARG A NH2   1 
ATOM   4292  N  N     . LEU A 1 609 ? 119.822 149.338 103.666 1.00 136.10 ? 609  LEU A N     1 
ATOM   4293  C  CA    . LEU A 1 609 ? 119.075 150.462 104.209 1.00 134.47 ? 609  LEU A CA    1 
ATOM   4294  C  C     . LEU A 1 609 ? 118.287 151.116 103.082 1.00 142.17 ? 609  LEU A C     1 
ATOM   4295  O  O     . LEU A 1 609 ? 118.870 151.734 102.186 1.00 144.71 ? 609  LEU A O     1 
ATOM   4296  C  CB    . LEU A 1 609 ? 120.026 151.461 104.861 1.00 131.51 ? 609  LEU A CB    1 
ATOM   4297  C  CG    . LEU A 1 609 ? 121.109 150.874 105.767 1.00 124.97 ? 609  LEU A CG    1 
ATOM   4298  C  CD1   . LEU A 1 609 ? 121.963 151.976 106.368 1.00 125.64 ? 609  LEU A CD1   1 
ATOM   4299  C  CD2   . LEU A 1 609 ? 120.500 150.016 106.859 1.00 126.23 ? 609  LEU A CD2   1 
ATOM   4300  N  N     . GLU A 1 610 ? 116.964 150.977 103.121 1.00 143.02 ? 610  GLU A N     1 
ATOM   4301  C  CA    . GLU A 1 610 ? 116.127 151.402 102.007 1.00 146.30 ? 610  GLU A CA    1 
ATOM   4302  C  C     . GLU A 1 610 ? 116.136 152.908 101.781 1.00 147.62 ? 610  GLU A C     1 
ATOM   4303  O  O     . GLU A 1 610 ? 115.689 153.357 100.721 1.00 148.27 ? 610  GLU A O     1 
ATOM   4304  C  CB    . GLU A 1 610 ? 114.689 150.925 102.224 1.00 147.27 ? 610  GLU A CB    1 
ATOM   4305  C  CG    . GLU A 1 610 ? 114.534 149.415 102.289 1.00 152.52 ? 610  GLU A CG    1 
ATOM   4306  C  CD    . GLU A 1 610 ? 114.672 148.757 100.931 1.00 163.39 ? 610  GLU A CD    1 
ATOM   4307  O  OE1   . GLU A 1 610 ? 114.439 149.441 99.912  1.00 165.79 ? 610  GLU A OE1   1 
ATOM   4308  O  OE2   . GLU A 1 610 ? 115.010 147.555 100.880 1.00 168.22 ? 610  GLU A OE2   1 
ATOM   4309  N  N     . PHE A 1 611 ? 116.637 153.695 102.731 1.00 143.05 ? 611  PHE A N     1 
ATOM   4310  C  CA    . PHE A 1 611 ? 116.625 155.146 102.618 1.00 138.40 ? 611  PHE A CA    1 
ATOM   4311  C  C     . PHE A 1 611 ? 117.944 155.717 102.116 1.00 141.00 ? 611  PHE A C     1 
ATOM   4312  O  O     . PHE A 1 611 ? 118.102 156.941 102.085 1.00 143.05 ? 611  PHE A O     1 
ATOM   4313  C  CB    . PHE A 1 611 ? 116.267 155.780 103.963 1.00 135.92 ? 611  PHE A CB    1 
ATOM   4314  C  CG    . PHE A 1 611 ? 117.258 155.499 105.055 1.00 135.43 ? 611  PHE A CG    1 
ATOM   4315  C  CD1   . PHE A 1 611 ? 117.154 154.355 105.825 1.00 133.95 ? 611  PHE A CD1   1 
ATOM   4316  C  CD2   . PHE A 1 611 ? 118.286 156.387 105.320 1.00 138.11 ? 611  PHE A CD2   1 
ATOM   4317  C  CE1   . PHE A 1 611 ? 118.061 154.099 106.832 1.00 130.78 ? 611  PHE A CE1   1 
ATOM   4318  C  CE2   . PHE A 1 611 ? 119.195 156.134 106.327 1.00 136.31 ? 611  PHE A CE2   1 
ATOM   4319  C  CZ    . PHE A 1 611 ? 119.082 154.989 107.083 1.00 131.98 ? 611  PHE A CZ    1 
ATOM   4320  N  N     . ILE A 1 612 ? 118.894 154.869 101.723 1.00 144.55 ? 612  ILE A N     1 
ATOM   4321  C  CA    . ILE A 1 612 ? 120.189 155.339 101.246 1.00 147.47 ? 612  ILE A CA    1 
ATOM   4322  C  C     . ILE A 1 612 ? 120.747 154.305 100.279 1.00 150.17 ? 612  ILE A C     1 
ATOM   4323  O  O     . ILE A 1 612 ? 120.477 153.109 100.400 1.00 148.41 ? 612  ILE A O     1 
ATOM   4324  C  CB    . ILE A 1 612 ? 121.158 155.612 102.426 1.00 139.00 ? 612  ILE A CB    1 
ATOM   4325  C  CG1   . ILE A 1 612 ? 122.258 156.583 102.002 1.00 143.28 ? 612  ILE A CG1   1 
ATOM   4326  C  CG2   . ILE A 1 612 ? 121.756 154.320 102.952 1.00 136.88 ? 612  ILE A CG2   1 
ATOM   4327  C  CD1   . ILE A 1 612 ? 123.211 156.938 103.118 1.00 143.93 ? 612  ILE A CD1   1 
ATOM   4328  N  N     . ASP A 1 613 ? 121.508 154.774 99.295  1.00 151.11 ? 613  ASP A N     1 
ATOM   4329  C  CA    . ASP A 1 613 ? 122.134 153.914 98.297  1.00 152.01 ? 613  ASP A CA    1 
ATOM   4330  C  C     . ASP A 1 613 ? 123.637 153.909 98.542  1.00 153.24 ? 613  ASP A C     1 
ATOM   4331  O  O     . ASP A 1 613 ? 124.329 154.879 98.216  1.00 157.57 ? 613  ASP A O     1 
ATOM   4332  C  CB    . ASP A 1 613 ? 121.810 154.389 96.882  1.00 155.14 ? 613  ASP A CB    1 
ATOM   4333  C  CG    . ASP A 1 613 ? 120.556 153.749 96.326  1.00 157.32 ? 613  ASP A CG    1 
ATOM   4334  O  OD1   . ASP A 1 613 ? 120.237 152.612 96.733  1.00 155.14 ? 613  ASP A OD1   1 
ATOM   4335  O  OD2   . ASP A 1 613 ? 119.890 154.380 95.478  1.00 162.85 ? 613  ASP A OD2   1 
ATOM   4336  N  N     . THR A 1 614 ? 124.137 152.817 99.116  1.00 150.37 ? 614  THR A N     1 
ATOM   4337  C  CA    . THR A 1 614 ? 125.564 152.616 99.328  1.00 151.90 ? 614  THR A CA    1 
ATOM   4338  C  C     . THR A 1 614 ? 126.136 151.608 98.336  1.00 154.14 ? 614  THR A C     1 
ATOM   4339  O  O     . THR A 1 614 ? 126.996 150.798 98.690  1.00 155.07 ? 614  THR A O     1 
ATOM   4340  C  CB    . THR A 1 614 ? 125.837 152.164 100.761 1.00 146.90 ? 614  THR A CB    1 
ATOM   4341  O  OG1   . THR A 1 614 ? 125.226 150.889 100.985 1.00 144.87 ? 614  THR A OG1   1 
ATOM   4342  C  CG2   . THR A 1 614 ? 125.267 153.165 101.746 1.00 142.68 ? 614  THR A CG2   1 
ATOM   4343  N  N     . SER A 1 615 ? 125.654 151.643 97.092  1.00 156.32 ? 615  SER A N     1 
ATOM   4344  C  CA    . SER A 1 615 ? 126.015 150.615 96.122  1.00 161.27 ? 615  SER A CA    1 
ATOM   4345  C  C     . SER A 1 615 ? 127.510 150.620 95.832  1.00 167.60 ? 615  SER A C     1 
ATOM   4346  O  O     . SER A 1 615 ? 128.174 149.582 95.935  1.00 168.68 ? 615  SER A O     1 
ATOM   4347  C  CB    . SER A 1 615 ? 125.216 150.810 94.833  1.00 162.65 ? 615  SER A CB    1 
ATOM   4348  O  OG    . SER A 1 615 ? 123.838 150.557 95.043  1.00 158.93 ? 615  SER A OG    1 
ATOM   4349  N  N     . GLU A 1 616 ? 128.063 151.777 95.469  1.00 168.69 ? 616  GLU A N     1 
ATOM   4350  C  CA    . GLU A 1 616 ? 129.494 151.855 95.150  1.00 166.62 ? 616  GLU A CA    1 
ATOM   4351  C  C     . GLU A 1 616 ? 130.300 152.318 96.361  1.00 163.14 ? 616  GLU A C     1 
ATOM   4352  O  O     . GLU A 1 616 ? 131.125 151.566 96.887  1.00 161.25 ? 616  GLU A O     1 
ATOM   4353  C  CB    . GLU A 1 616 ? 129.728 152.754 93.928  1.00 167.39 ? 616  GLU A CB    1 
ATOM   4354  C  CG    . GLU A 1 616 ? 129.111 154.158 93.964  1.00 168.95 ? 616  GLU A CG    1 
ATOM   4355  C  CD    . GLU A 1 616 ? 127.603 154.163 93.797  1.00 170.89 ? 616  GLU A CD    1 
ATOM   4356  O  OE1   . GLU A 1 616 ? 127.047 153.132 93.364  1.00 172.29 ? 616  GLU A OE1   1 
ATOM   4357  O  OE2   . GLU A 1 616 ? 126.974 155.199 94.098  1.00 168.88 ? 616  GLU A OE2   1 
ATOM   4358  N  N     . TYR A 1 617 ? 130.047 153.544 96.827  1.00 160.85 ? 617  TYR A N     1 
ATOM   4359  C  CA    . TYR A 1 617 ? 130.773 154.142 97.943  1.00 158.01 ? 617  TYR A CA    1 
ATOM   4360  C  C     . TYR A 1 617 ? 132.282 154.023 97.757  1.00 162.75 ? 617  TYR A C     1 
ATOM   4361  O  O     . TYR A 1 617 ? 132.766 153.849 96.634  1.00 169.58 ? 617  TYR A O     1 
ATOM   4362  C  CB    . TYR A 1 617 ? 130.339 153.521 99.270  1.00 151.99 ? 617  TYR A CB    1 
ATOM   4363  C  CG    . TYR A 1 617 ? 129.456 154.439 100.084 1.00 152.69 ? 617  TYR A CG    1 
ATOM   4364  C  CD1   . TYR A 1 617 ? 128.354 155.058 99.511  1.00 152.91 ? 617  TYR A CD1   1 
ATOM   4365  C  CD2   . TYR A 1 617 ? 129.726 154.694 101.421 1.00 148.49 ? 617  TYR A CD2   1 
ATOM   4366  C  CE1   . TYR A 1 617 ? 127.543 155.899 100.246 1.00 147.59 ? 617  TYR A CE1   1 
ATOM   4367  C  CE2   . TYR A 1 617 ? 128.921 155.535 102.164 1.00 142.70 ? 617  TYR A CE2   1 
ATOM   4368  C  CZ    . TYR A 1 617 ? 127.832 156.134 101.571 1.00 142.57 ? 617  TYR A CZ    1 
ATOM   4369  O  OH    . TYR A 1 617 ? 127.026 156.972 102.305 1.00 144.00 ? 617  TYR A OH    1 
ATOM   4370  N  N     . SER A 1 618 ? 133.039 154.140 98.849  1.00 157.35 ? 618  SER A N     1 
ATOM   4371  C  CA    . SER A 1 618 ? 134.490 154.028 98.744  1.00 156.90 ? 618  SER A CA    1 
ATOM   4372  C  C     . SER A 1 618 ? 134.946 152.575 98.739  1.00 152.01 ? 618  SER A C     1 
ATOM   4373  O  O     . SER A 1 618 ? 136.046 152.277 98.261  1.00 151.58 ? 618  SER A O     1 
ATOM   4374  C  CB    . SER A 1 618 ? 135.159 154.784 99.887  1.00 155.26 ? 618  SER A CB    1 
ATOM   4375  O  OG    . SER A 1 618 ? 135.264 153.964 101.037 1.00 151.90 ? 618  SER A OG    1 
ATOM   4376  N  N     . GLN A 1 619 ? 134.130 151.672 99.284  1.00 148.60 ? 619  GLN A N     1 
ATOM   4377  C  CA    . GLN A 1 619 ? 134.345 150.239 99.443  1.00 149.66 ? 619  GLN A CA    1 
ATOM   4378  C  C     . GLN A 1 619 ? 135.371 150.034 100.566 1.00 147.04 ? 619  GLN A C     1 
ATOM   4379  O  O     . GLN A 1 619 ? 135.606 148.906 100.975 1.00 146.02 ? 619  GLN A O     1 
ATOM   4380  C  CB    . GLN A 1 619 ? 134.816 149.552 98.140  1.00 153.78 ? 619  GLN A CB    1 
ATOM   4381  C  CG    . GLN A 1 619 ? 135.166 148.038 98.080  1.00 153.04 ? 619  GLN A CG    1 
ATOM   4382  C  CD    . GLN A 1 619 ? 134.383 147.136 99.035  1.00 149.57 ? 619  GLN A CD    1 
ATOM   4383  O  OE1   . GLN A 1 619 ? 134.853 146.762 100.105 1.00 146.52 ? 619  GLN A OE1   1 
ATOM   4384  N  NE2   . GLN A 1 619 ? 133.167 146.786 98.634  1.00 148.20 ? 619  GLN A NE2   1 
ATOM   4385  N  N     . THR A 1 620 ? 135.963 151.099 101.101 1.00 147.63 ? 620  THR A N     1 
ATOM   4386  C  CA    . THR A 1 620 ? 136.791 151.002 102.292 1.00 146.77 ? 620  THR A CA    1 
ATOM   4387  C  C     . THR A 1 620 ? 135.999 151.246 103.569 1.00 141.81 ? 620  THR A C     1 
ATOM   4388  O  O     . THR A 1 620 ? 136.263 150.586 104.579 1.00 140.12 ? 620  THR A O     1 
ATOM   4389  C  CB    . THR A 1 620 ? 137.962 151.994 102.202 1.00 147.75 ? 620  THR A CB    1 
ATOM   4390  O  OG1   . THR A 1 620 ? 139.005 151.432 101.395 1.00 152.82 ? 620  THR A OG1   1 
ATOM   4391  C  CG2   . THR A 1 620 ? 138.523 152.325 103.579 1.00 142.09 ? 620  THR A CG2   1 
ATOM   4392  N  N     . VAL A 1 621 ? 135.002 152.129 103.533 1.00 140.00 ? 621  VAL A N     1 
ATOM   4393  C  CA    . VAL A 1 621 ? 134.200 152.431 104.712 1.00 136.84 ? 621  VAL A CA    1 
ATOM   4394  C  C     . VAL A 1 621 ? 133.097 151.391 104.847 1.00 133.98 ? 621  VAL A C     1 
ATOM   4395  O  O     . VAL A 1 621 ? 132.566 151.173 105.942 1.00 133.45 ? 621  VAL A O     1 
ATOM   4396  C  CB    . VAL A 1 621 ? 133.622 153.857 104.648 1.00 136.48 ? 621  VAL A CB    1 
ATOM   4397  C  CG1   . VAL A 1 621 ? 134.676 154.831 104.158 1.00 137.49 ? 621  VAL A CG1   1 
ATOM   4398  C  CG2   . VAL A 1 621 ? 132.394 153.905 103.757 1.00 136.67 ? 621  VAL A CG2   1 
ATOM   4399  N  N     . LEU A 1 622 ? 132.758 150.728 103.738 1.00 133.69 ? 622  LEU A N     1 
ATOM   4400  C  CA    . LEU A 1 622 ? 131.733 149.691 103.784 1.00 131.79 ? 622  LEU A CA    1 
ATOM   4401  C  C     . LEU A 1 622 ? 132.158 148.539 104.685 1.00 133.61 ? 622  LEU A C     1 
ATOM   4402  O  O     . LEU A 1 622 ? 131.369 148.063 105.509 1.00 131.51 ? 622  LEU A O     1 
ATOM   4403  C  CB    . LEU A 1 622 ? 131.434 149.188 102.374 1.00 134.64 ? 622  LEU A CB    1 
ATOM   4404  C  CG    . LEU A 1 622 ? 130.073 149.588 101.806 1.00 135.45 ? 622  LEU A CG    1 
ATOM   4405  C  CD1   . LEU A 1 622 ? 129.866 151.084 101.931 1.00 137.03 ? 622  LEU A CD1   1 
ATOM   4406  C  CD2   . LEU A 1 622 ? 129.951 149.147 100.360 1.00 139.31 ? 622  LEU A CD2   1 
ATOM   4407  N  N     . ASP A 1 623 ? 133.400 148.077 104.544 1.00 133.07 ? 623  ASP A N     1 
ATOM   4408  C  CA    . ASP A 1 623 ? 133.942 147.100 105.476 1.00 128.22 ? 623  ASP A CA    1 
ATOM   4409  C  C     . ASP A 1 623 ? 134.397 147.739 106.778 1.00 122.39 ? 623  ASP A C     1 
ATOM   4410  O  O     . ASP A 1 623 ? 134.434 147.058 107.810 1.00 119.26 ? 623  ASP A O     1 
ATOM   4411  C  CB    . ASP A 1 623 ? 135.112 146.349 104.837 1.00 128.23 ? 623  ASP A CB    1 
ATOM   4412  C  CG    . ASP A 1 623 ? 134.657 145.197 103.965 1.00 138.48 ? 623  ASP A CG    1 
ATOM   4413  O  OD1   . ASP A 1 623 ? 134.344 145.434 102.780 1.00 142.93 ? 623  ASP A OD1   1 
ATOM   4414  O  OD2   . ASP A 1 623 ? 134.614 144.053 104.465 1.00 141.46 ? 623  ASP A OD2   1 
ATOM   4415  N  N     . CYS A 1 624 ? 134.740 149.029 106.749 1.00 125.68 ? 624  CYS A N     1 
ATOM   4416  C  CA    . CYS A 1 624 ? 135.214 149.699 107.953 1.00 126.04 ? 624  CYS A CA    1 
ATOM   4417  C  C     . CYS A 1 624 ? 134.119 149.790 109.004 1.00 120.10 ? 624  CYS A C     1 
ATOM   4418  O  O     . CYS A 1 624 ? 134.396 149.687 110.201 1.00 118.31 ? 624  CYS A O     1 
ATOM   4419  C  CB    . CYS A 1 624 ? 135.744 151.090 107.613 1.00 131.13 ? 624  CYS A CB    1 
ATOM   4420  S  SG    . CYS A 1 624 ? 136.401 152.003 109.020 1.00 135.38 ? 624  CYS A SG    1 
ATOM   4421  N  N     . ALA A 1 625 ? 132.870 149.993 108.582 1.00 118.20 ? 625  ALA A N     1 
ATOM   4422  C  CA    . ALA A 1 625 ? 131.774 150.060 109.544 1.00 115.30 ? 625  ALA A CA    1 
ATOM   4423  C  C     . ALA A 1 625 ? 131.637 148.750 110.310 1.00 117.23 ? 625  ALA A C     1 
ATOM   4424  O  O     . ALA A 1 625 ? 131.574 148.740 111.546 1.00 118.69 ? 625  ALA A O     1 
ATOM   4425  C  CB    . ALA A 1 625 ? 130.469 150.406 108.830 1.00 117.18 ? 625  ALA A CB    1 
ATOM   4426  N  N     . VAL A 1 626 ? 131.608 147.629 109.587 1.00 117.05 ? 626  VAL A N     1 
ATOM   4427  C  CA    . VAL A 1 626 ? 131.480 146.326 110.232 1.00 112.30 ? 626  VAL A CA    1 
ATOM   4428  C  C     . VAL A 1 626 ? 132.695 146.039 111.102 1.00 113.31 ? 626  VAL A C     1 
ATOM   4429  O  O     . VAL A 1 626 ? 132.566 145.539 112.226 1.00 112.90 ? 626  VAL A O     1 
ATOM   4430  C  CB    . VAL A 1 626 ? 131.263 145.226 109.178 1.00 110.79 ? 626  VAL A CB    1 
ATOM   4431  C  CG1   . VAL A 1 626 ? 131.560 143.859 109.765 1.00 103.44 ? 626  VAL A CG1   1 
ATOM   4432  C  CG2   . VAL A 1 626 ? 129.841 145.279 108.658 1.00 117.21 ? 626  VAL A CG2   1 
ATOM   4433  N  N     . TYR A 1 627 ? 133.895 146.346 110.601 1.00 114.64 ? 627  TYR A N     1 
ATOM   4434  C  CA    . TYR A 1 627 ? 135.101 146.081 111.378 1.00 112.37 ? 627  TYR A CA    1 
ATOM   4435  C  C     . TYR A 1 627 ? 135.121 146.898 112.663 1.00 111.70 ? 627  TYR A C     1 
ATOM   4436  O  O     . TYR A 1 627 ? 135.455 146.377 113.733 1.00 112.73 ? 627  TYR A O     1 
ATOM   4437  C  CB    . TYR A 1 627 ? 136.339 146.374 110.535 1.00 113.26 ? 627  TYR A CB    1 
ATOM   4438  C  CG    . TYR A 1 627 ? 136.884 145.160 109.822 1.00 114.03 ? 627  TYR A CG    1 
ATOM   4439  C  CD1   . TYR A 1 627 ? 137.315 144.051 110.532 1.00 113.46 ? 627  TYR A CD1   1 
ATOM   4440  C  CD2   . TYR A 1 627 ? 136.960 145.122 108.438 1.00 117.39 ? 627  TYR A CD2   1 
ATOM   4441  C  CE1   . TYR A 1 627 ? 137.811 142.939 109.884 1.00 118.60 ? 627  TYR A CE1   1 
ATOM   4442  C  CE2   . TYR A 1 627 ? 137.454 144.015 107.782 1.00 117.68 ? 627  TYR A CE2   1 
ATOM   4443  C  CZ    . TYR A 1 627 ? 137.878 142.927 108.509 1.00 120.37 ? 627  TYR A CZ    1 
ATOM   4444  O  OH    . TYR A 1 627 ? 138.372 141.821 107.857 1.00 127.83 ? 627  TYR A OH    1 
ATOM   4445  N  N     . ILE A 1 628 ? 134.752 148.179 112.581 1.00 111.41 ? 628  ILE A N     1 
ATOM   4446  C  CA    . ILE A 1 628 ? 134.735 149.036 113.760 1.00 111.08 ? 628  ILE A CA    1 
ATOM   4447  C  C     . ILE A 1 628 ? 133.704 148.540 114.760 1.00 111.01 ? 628  ILE A C     1 
ATOM   4448  O  O     . ILE A 1 628 ? 133.978 148.465 115.963 1.00 113.51 ? 628  ILE A O     1 
ATOM   4449  C  CB    . ILE A 1 628 ? 134.475 150.499 113.355 1.00 112.31 ? 628  ILE A CB    1 
ATOM   4450  C  CG1   . ILE A 1 628 ? 135.793 151.220 113.084 1.00 114.96 ? 628  ILE A CG1   1 
ATOM   4451  C  CG2   . ILE A 1 628 ? 133.700 151.233 114.435 1.00 110.47 ? 628  ILE A CG2   1 
ATOM   4452  C  CD1   . ILE A 1 628 ? 135.615 152.575 112.449 1.00 117.45 ? 628  ILE A CD1   1 
ATOM   4453  N  N     . TYR A 1 629 ? 132.507 148.189 114.286 1.00 109.64 ? 629  TYR A N     1 
ATOM   4454  C  CA    . TYR A 1 629 ? 131.482 147.699 115.200 1.00 109.01 ? 629  TYR A CA    1 
ATOM   4455  C  C     . TYR A 1 629 ? 131.931 146.421 115.892 1.00 112.53 ? 629  TYR A C     1 
ATOM   4456  O  O     . TYR A 1 629 ? 131.795 146.281 117.112 1.00 116.82 ? 629  TYR A O     1 
ATOM   4457  C  CB    . TYR A 1 629 ? 130.171 147.465 114.457 1.00 105.40 ? 629  TYR A CB    1 
ATOM   4458  C  CG    . TYR A 1 629 ? 129.185 146.637 115.244 1.00 105.01 ? 629  TYR A CG    1 
ATOM   4459  C  CD1   . TYR A 1 629 ? 128.579 147.145 116.383 1.00 108.67 ? 629  TYR A CD1   1 
ATOM   4460  C  CD2   . TYR A 1 629 ? 128.859 145.350 114.850 1.00 106.70 ? 629  TYR A CD2   1 
ATOM   4461  C  CE1   . TYR A 1 629 ? 127.677 146.395 117.104 1.00 110.98 ? 629  TYR A CE1   1 
ATOM   4462  C  CE2   . TYR A 1 629 ? 127.959 144.593 115.566 1.00 105.71 ? 629  TYR A CE2   1 
ATOM   4463  C  CZ    . TYR A 1 629 ? 127.371 145.121 116.691 1.00 107.67 ? 629  TYR A CZ    1 
ATOM   4464  O  OH    . TYR A 1 629 ? 126.472 144.370 117.407 1.00 108.93 ? 629  TYR A OH    1 
ATOM   4465  N  N     . ASN A 1 630 ? 132.484 145.479 115.126 1.00 110.86 ? 630  ASN A N     1 
ATOM   4466  C  CA    . ASN A 1 630 ? 132.900 144.206 115.699 1.00 108.09 ? 630  ASN A CA    1 
ATOM   4467  C  C     . ASN A 1 630 ? 134.015 144.402 116.716 1.00 111.37 ? 630  ASN A C     1 
ATOM   4468  O  O     . ASN A 1 630 ? 133.973 143.842 117.818 1.00 112.47 ? 630  ASN A O     1 
ATOM   4469  C  CB    . ASN A 1 630 ? 133.343 143.260 114.585 1.00 109.44 ? 630  ASN A CB    1 
ATOM   4470  C  CG    . ASN A 1 630 ? 132.439 142.058 114.452 1.00 115.41 ? 630  ASN A CG    1 
ATOM   4471  O  OD1   . ASN A 1 630 ? 131.576 141.821 115.295 1.00 117.10 ? 630  ASN A OD1   1 
ATOM   4472  N  ND2   . ASN A 1 630 ? 132.624 141.294 113.384 1.00 118.16 ? 630  ASN A ND2   1 
ATOM   4473  N  N     . PHE A 1 631 ? 135.019 145.212 116.368 1.00 112.20 ? 631  PHE A N     1 
ATOM   4474  C  CA    . PHE A 1 631 ? 136.142 145.426 117.271 1.00 112.18 ? 631  PHE A CA    1 
ATOM   4475  C  C     . PHE A 1 631 ? 135.708 146.160 118.532 1.00 113.57 ? 631  PHE A C     1 
ATOM   4476  O  O     . PHE A 1 631 ? 136.122 145.795 119.638 1.00 115.70 ? 631  PHE A O     1 
ATOM   4477  C  CB    . PHE A 1 631 ? 137.249 146.193 116.553 1.00 112.28 ? 631  PHE A CB    1 
ATOM   4478  C  CG    . PHE A 1 631 ? 138.187 145.313 115.784 1.00 120.78 ? 631  PHE A CG    1 
ATOM   4479  C  CD1   . PHE A 1 631 ? 137.933 143.959 115.653 1.00 123.11 ? 631  PHE A CD1   1 
ATOM   4480  C  CD2   . PHE A 1 631 ? 139.316 145.837 115.182 1.00 125.77 ? 631  PHE A CD2   1 
ATOM   4481  C  CE1   . PHE A 1 631 ? 138.789 143.145 114.945 1.00 121.06 ? 631  PHE A CE1   1 
ATOM   4482  C  CE2   . PHE A 1 631 ? 140.175 145.027 114.472 1.00 124.52 ? 631  PHE A CE2   1 
ATOM   4483  C  CZ    . PHE A 1 631 ? 139.910 143.678 114.354 1.00 121.74 ? 631  PHE A CZ    1 
ATOM   4484  N  N     . SER A 1 632 ? 134.873 147.193 118.391 1.00 111.67 ? 632  SER A N     1 
ATOM   4485  C  CA    . SER A 1 632 ? 134.393 147.915 119.561 1.00 110.99 ? 632  SER A CA    1 
ATOM   4486  C  C     . SER A 1 632 ? 133.566 147.012 120.463 1.00 111.96 ? 632  SER A C     1 
ATOM   4487  O  O     . SER A 1 632 ? 133.742 147.021 121.686 1.00 117.22 ? 632  SER A O     1 
ATOM   4488  C  CB    . SER A 1 632 ? 133.576 149.130 119.127 1.00 111.85 ? 632  SER A CB    1 
ATOM   4489  O  OG    . SER A 1 632 ? 132.629 149.483 120.119 1.00 117.85 ? 632  SER A OG    1 
ATOM   4490  N  N     . TYR A 1 633 ? 132.669 146.213 119.880 1.00 107.72 ? 633  TYR A N     1 
ATOM   4491  C  CA    . TYR A 1 633 ? 131.839 145.327 120.685 1.00 106.51 ? 633  TYR A CA    1 
ATOM   4492  C  C     . TYR A 1 633 ? 132.687 144.296 121.416 1.00 111.45 ? 633  TYR A C     1 
ATOM   4493  O  O     . TYR A 1 633 ? 132.482 144.039 122.607 1.00 119.71 ? 633  TYR A O     1 
ATOM   4494  C  CB    . TYR A 1 633 ? 130.799 144.641 119.801 1.00 106.25 ? 633  TYR A CB    1 
ATOM   4495  C  CG    . TYR A 1 633 ? 129.524 144.282 120.523 1.00 105.04 ? 633  TYR A CG    1 
ATOM   4496  C  CD1   . TYR A 1 633 ? 128.477 145.186 120.610 1.00 106.61 ? 633  TYR A CD1   1 
ATOM   4497  C  CD2   . TYR A 1 633 ? 129.368 143.041 121.118 1.00 105.81 ? 633  TYR A CD2   1 
ATOM   4498  C  CE1   . TYR A 1 633 ? 127.310 144.864 121.270 1.00 109.38 ? 633  TYR A CE1   1 
ATOM   4499  C  CE2   . TYR A 1 633 ? 128.204 142.710 121.780 1.00 108.21 ? 633  TYR A CE2   1 
ATOM   4500  C  CZ    . TYR A 1 633 ? 127.179 143.625 121.852 1.00 111.14 ? 633  TYR A CZ    1 
ATOM   4501  O  OH    . TYR A 1 633 ? 126.019 143.298 122.512 1.00 114.21 ? 633  TYR A OH    1 
ATOM   4502  N  N     . LEU A 1 634 ? 133.663 143.705 120.723 1.00 110.02 ? 634  LEU A N     1 
ATOM   4503  C  CA    . LEU A 1 634 ? 134.485 142.676 121.349 1.00 112.61 ? 634  LEU A CA    1 
ATOM   4504  C  C     . LEU A 1 634 ? 135.372 143.261 122.442 1.00 114.37 ? 634  LEU A C     1 
ATOM   4505  O  O     . LEU A 1 634 ? 135.510 142.670 123.521 1.00 118.76 ? 634  LEU A O     1 
ATOM   4506  C  CB    . LEU A 1 634 ? 135.323 141.965 120.290 1.00 117.40 ? 634  LEU A CB    1 
ATOM   4507  C  CG    . LEU A 1 634 ? 134.636 140.767 119.633 1.00 117.42 ? 634  LEU A CG    1 
ATOM   4508  C  CD1   . LEU A 1 634 ? 135.504 140.184 118.533 1.00 123.93 ? 634  LEU A CD1   1 
ATOM   4509  C  CD2   . LEU A 1 634 ? 134.297 139.712 120.671 1.00 112.30 ? 634  LEU A CD2   1 
ATOM   4510  N  N     . PHE A 1 635 ? 135.982 144.421 122.186 1.00 110.05 ? 635  PHE A N     1 
ATOM   4511  C  CA    . PHE A 1 635 ? 136.806 145.059 123.205 1.00 113.37 ? 635  PHE A CA    1 
ATOM   4512  C  C     . PHE A 1 635 ? 135.975 145.455 124.417 1.00 114.65 ? 635  PHE A C     1 
ATOM   4513  O  O     . PHE A 1 635 ? 136.401 145.255 125.561 1.00 116.86 ? 635  PHE A O     1 
ATOM   4514  C  CB    . PHE A 1 635 ? 137.516 146.280 122.621 1.00 112.90 ? 635  PHE A CB    1 
ATOM   4515  C  CG    . PHE A 1 635 ? 138.702 145.940 121.763 1.00 114.43 ? 635  PHE A CG    1 
ATOM   4516  C  CD1   . PHE A 1 635 ? 139.202 144.650 121.725 1.00 113.49 ? 635  PHE A CD1   1 
ATOM   4517  C  CD2   . PHE A 1 635 ? 139.322 146.914 121.001 1.00 117.46 ? 635  PHE A CD2   1 
ATOM   4518  C  CE1   . PHE A 1 635 ? 140.291 144.339 120.939 1.00 116.54 ? 635  PHE A CE1   1 
ATOM   4519  C  CE2   . PHE A 1 635 ? 140.413 146.607 120.214 1.00 117.53 ? 635  PHE A CE2   1 
ATOM   4520  C  CZ    . PHE A 1 635 ? 140.897 145.319 120.183 1.00 118.44 ? 635  PHE A CZ    1 
ATOM   4521  N  N     . GLY A 1 636 ? 134.786 146.016 124.188 1.00 110.93 ? 636  GLY A N     1 
ATOM   4522  C  CA    . GLY A 1 636 ? 133.917 146.356 125.299 1.00 112.96 ? 636  GLY A CA    1 
ATOM   4523  C  C     . GLY A 1 636 ? 133.500 145.141 126.099 1.00 113.00 ? 636  GLY A C     1 
ATOM   4524  O  O     . GLY A 1 636 ? 133.465 145.181 127.328 1.00 118.08 ? 636  GLY A O     1 
ATOM   4525  N  N     . LEU A 1 637 ? 133.189 144.038 125.415 1.00 108.55 ? 637  LEU A N     1 
ATOM   4526  C  CA    . LEU A 1 637 ? 132.794 142.822 126.117 1.00 108.75 ? 637  LEU A CA    1 
ATOM   4527  C  C     . LEU A 1 637 ? 133.941 142.272 126.957 1.00 114.04 ? 637  LEU A C     1 
ATOM   4528  O  O     . LEU A 1 637 ? 133.735 141.850 128.101 1.00 118.97 ? 637  LEU A O     1 
ATOM   4529  C  CB    . LEU A 1 637 ? 132.310 141.778 125.113 1.00 109.78 ? 637  LEU A CB    1 
ATOM   4530  C  CG    . LEU A 1 637 ? 130.808 141.776 124.832 1.00 110.01 ? 637  LEU A CG    1 
ATOM   4531  C  CD1   . LEU A 1 637 ? 130.417 140.555 124.023 1.00 110.03 ? 637  LEU A CD1   1 
ATOM   4532  C  CD2   . LEU A 1 637 ? 130.021 141.838 126.126 1.00 113.60 ? 637  LEU A CD2   1 
ATOM   4533  N  N     . LEU A 1 638 ? 135.158 142.269 126.407 1.00 113.12 ? 638  LEU A N     1 
ATOM   4534  C  CA    . LEU A 1 638 ? 136.305 141.779 127.167 1.00 114.92 ? 638  LEU A CA    1 
ATOM   4535  C  C     . LEU A 1 638 ? 136.585 142.662 128.378 1.00 118.43 ? 638  LEU A C     1 
ATOM   4536  O  O     . LEU A 1 638 ? 136.831 142.159 129.485 1.00 120.50 ? 638  LEU A O     1 
ATOM   4537  C  CB    . LEU A 1 638 ? 137.535 141.703 126.264 1.00 112.41 ? 638  LEU A CB    1 
ATOM   4538  C  CG    . LEU A 1 638 ? 138.838 141.287 126.944 1.00 113.80 ? 638  LEU A CG    1 
ATOM   4539  C  CD1   . LEU A 1 638 ? 138.736 139.861 127.457 1.00 113.09 ? 638  LEU A CD1   1 
ATOM   4540  C  CD2   . LEU A 1 638 ? 140.009 141.436 125.990 1.00 113.94 ? 638  LEU A CD2   1 
ATOM   4541  N  N     . MET A 1 639 ? 136.552 143.983 128.186 1.00 115.04 ? 639  MET A N     1 
ATOM   4542  C  CA    . MET A 1 639 ? 136.770 144.900 129.298 1.00 113.75 ? 639  MET A CA    1 
ATOM   4543  C  C     . MET A 1 639 ? 135.698 144.727 130.363 1.00 116.76 ? 639  MET A C     1 
ATOM   4544  O  O     . MET A 1 639 ? 135.991 144.761 131.564 1.00 121.56 ? 639  MET A O     1 
ATOM   4545  C  CB    . MET A 1 639 ? 136.800 146.338 128.784 1.00 110.34 ? 639  MET A CB    1 
ATOM   4546  C  CG    . MET A 1 639 ? 137.097 147.376 129.842 1.00 115.44 ? 639  MET A CG    1 
ATOM   4547  S  SD    . MET A 1 639 ? 137.095 149.062 129.206 1.00 144.52 ? 639  MET A SD    1 
ATOM   4548  C  CE    . MET A 1 639 ? 137.099 148.774 127.439 1.00 120.68 ? 639  MET A CE    1 
ATOM   4549  N  N     . LEU A 1 640 ? 134.447 144.538 129.940 1.00 114.86 ? 640  LEU A N     1 
ATOM   4550  C  CA    . LEU A 1 640 ? 133.361 144.312 130.884 1.00 112.73 ? 640  LEU A CA    1 
ATOM   4551  C  C     . LEU A 1 640 ? 133.572 143.033 131.673 1.00 115.88 ? 640  LEU A C     1 
ATOM   4552  O  O     . LEU A 1 640 ? 133.384 143.017 132.890 1.00 120.84 ? 640  LEU A O     1 
ATOM   4553  C  CB    . LEU A 1 640 ? 132.031 144.265 130.139 1.00 108.19 ? 640  LEU A CB    1 
ATOM   4554  C  CG    . LEU A 1 640 ? 131.215 145.549 130.164 1.00 108.68 ? 640  LEU A CG    1 
ATOM   4555  C  CD1   . LEU A 1 640 ? 132.092 146.717 129.802 1.00 108.57 ? 640  LEU A CD1   1 
ATOM   4556  C  CD2   . LEU A 1 640 ? 130.093 145.418 129.164 1.00 117.39 ? 640  LEU A CD2   1 
ATOM   4557  N  N     . ILE A 1 641 ? 133.966 141.950 131.002 1.00 114.43 ? 641  ILE A N     1 
ATOM   4558  C  CA    . ILE A 1 641 ? 134.211 140.702 131.717 1.00 114.49 ? 641  ILE A CA    1 
ATOM   4559  C  C     . ILE A 1 641 ? 135.293 140.903 132.768 1.00 119.75 ? 641  ILE A C     1 
ATOM   4560  O  O     . ILE A 1 641 ? 135.103 140.576 133.950 1.00 125.27 ? 641  ILE A O     1 
ATOM   4561  C  CB    . ILE A 1 641 ? 134.580 139.580 130.731 1.00 113.75 ? 641  ILE A CB    1 
ATOM   4562  C  CG1   . ILE A 1 641 ? 133.335 139.088 129.994 1.00 118.14 ? 641  ILE A CG1   1 
ATOM   4563  C  CG2   . ILE A 1 641 ? 135.251 138.432 131.463 1.00 114.01 ? 641  ILE A CG2   1 
ATOM   4564  C  CD1   . ILE A 1 641 ? 133.584 137.892 129.106 1.00 114.90 ? 641  ILE A CD1   1 
ATOM   4565  N  N     . ILE A 1 642 ? 136.425 141.488 132.364 1.00 119.89 ? 642  ILE A N     1 
ATOM   4566  C  CA    . ILE A 1 642 ? 137.544 141.654 133.288 1.00 123.41 ? 642  ILE A CA    1 
ATOM   4567  C  C     . ILE A 1 642 ? 137.139 142.518 134.476 1.00 126.86 ? 642  ILE A C     1 
ATOM   4568  O  O     . ILE A 1 642 ? 137.298 142.116 135.638 1.00 129.41 ? 642  ILE A O     1 
ATOM   4569  C  CB    . ILE A 1 642 ? 138.760 142.244 132.551 1.00 118.33 ? 642  ILE A CB    1 
ATOM   4570  C  CG1   . ILE A 1 642 ? 139.366 141.209 131.604 1.00 117.17 ? 642  ILE A CG1   1 
ATOM   4571  C  CG2   . ILE A 1 642 ? 139.799 142.726 133.545 1.00 115.30 ? 642  ILE A CG2   1 
ATOM   4572  C  CD1   . ILE A 1 642 ? 140.613 141.688 130.899 1.00 114.87 ? 642  ILE A CD1   1 
ATOM   4573  N  N     . ILE A 1 643 ? 136.572 143.695 134.209 1.00 123.67 ? 643  ILE A N     1 
ATOM   4574  C  CA    . ILE A 1 643 ? 136.245 144.625 135.284 1.00 123.55 ? 643  ILE A CA    1 
ATOM   4575  C  C     . ILE A 1 643 ? 135.163 144.047 136.186 1.00 128.10 ? 643  ILE A C     1 
ATOM   4576  O  O     . ILE A 1 643 ? 135.279 144.079 137.417 1.00 130.58 ? 643  ILE A O     1 
ATOM   4577  C  CB    . ILE A 1 643 ? 135.826 145.987 134.706 1.00 119.66 ? 643  ILE A CB    1 
ATOM   4578  C  CG1   . ILE A 1 643 ? 137.053 146.766 134.246 1.00 119.80 ? 643  ILE A CG1   1 
ATOM   4579  C  CG2   . ILE A 1 643 ? 135.065 146.789 135.735 1.00 127.73 ? 643  ILE A CG2   1 
ATOM   4580  C  CD1   . ILE A 1 643 ? 136.718 147.936 133.373 1.00 121.78 ? 643  ILE A CD1   1 
ATOM   4581  N  N     . GLY A 1 644 ? 134.096 143.508 135.593 1.00 126.58 ? 644  GLY A N     1 
ATOM   4582  C  CA    . GLY A 1 644 ? 132.993 143.011 136.390 1.00 130.13 ? 644  GLY A CA    1 
ATOM   4583  C  C     . GLY A 1 644 ? 133.389 141.861 137.290 1.00 134.84 ? 644  GLY A C     1 
ATOM   4584  O  O     . GLY A 1 644 ? 133.136 141.894 138.495 1.00 140.87 ? 644  GLY A O     1 
ATOM   4585  N  N     . LEU A 1 645 ? 134.153 140.996 136.714 1.00 130.40 ? 645  LEU A N     1 
ATOM   4586  C  CA    . LEU A 1 645 ? 134.559 139.846 137.400 1.00 134.11 ? 645  LEU A CA    1 
ATOM   4587  C  C     . LEU A 1 645 ? 135.737 140.097 138.259 1.00 135.33 ? 645  LEU A C     1 
ATOM   4588  O  O     . LEU A 1 645 ? 136.125 139.268 139.026 1.00 139.54 ? 645  LEU A O     1 
ATOM   4589  C  CB    . LEU A 1 645 ? 134.839 138.777 136.397 1.00 130.76 ? 645  LEU A CB    1 
ATOM   4590  C  CG    . LEU A 1 645 ? 135.648 137.652 136.925 1.00 131.34 ? 645  LEU A CG    1 
ATOM   4591  C  CD1   . LEU A 1 645 ? 135.389 136.520 136.008 1.00 131.90 ? 645  LEU A CD1   1 
ATOM   4592  C  CD2   . LEU A 1 645 ? 137.089 138.021 136.840 1.00 129.45 ? 645  LEU A CD2   1 
ATOM   4593  N  N     . GLY A 1 646 ? 136.291 141.275 138.195 1.00 132.70 ? 646  GLY A N     1 
ATOM   4594  C  CA    . GLY A 1 646 ? 137.445 141.545 139.011 1.00 136.43 ? 646  GLY A CA    1 
ATOM   4595  C  C     . GLY A 1 646 ? 137.196 142.435 140.180 1.00 139.04 ? 646  GLY A C     1 
ATOM   4596  O  O     . GLY A 1 646 ? 136.853 142.007 141.225 1.00 140.33 ? 646  GLY A O     1 
ATOM   4597  N  N     . ASN A 1 647 ? 137.365 143.702 139.970 1.00 139.43 ? 647  ASN A N     1 
ATOM   4598  C  CA    . ASN A 1 647 ? 137.179 144.702 141.010 1.00 142.93 ? 647  ASN A CA    1 
ATOM   4599  C  C     . ASN A 1 647 ? 135.706 145.073 141.193 1.00 141.78 ? 647  ASN A C     1 
ATOM   4600  O  O     . ASN A 1 647 ? 134.848 144.783 140.356 1.00 138.44 ? 647  ASN A O     1 
ATOM   4601  C  CB    . ASN A 1 647 ? 138.032 145.937 140.707 1.00 142.20 ? 647  ASN A CB    1 
ATOM   4602  C  CG    . ASN A 1 647 ? 137.593 146.679 139.455 1.00 140.85 ? 647  ASN A CG    1 
ATOM   4603  O  OD1   . ASN A 1 647 ? 136.545 146.408 138.873 1.00 140.62 ? 647  ASN A OD1   1 
ATOM   4604  N  ND2   . ASN A 1 647 ? 138.423 147.617 139.025 1.00 138.73 ? 647  ASN A ND2   1 
ATOM   4605  N  N     . ASN A 1 648 ? 135.429 145.717 142.323 1.00 140.69 ? 648  ASN A N     1 
ATOM   4606  C  CA    . ASN A 1 648 ? 134.073 146.128 142.657 1.00 142.39 ? 648  ASN A CA    1 
ATOM   4607  C  C     . ASN A 1 648 ? 133.688 147.348 141.821 1.00 142.07 ? 648  ASN A C     1 
ATOM   4608  O  O     . ASN A 1 648 ? 134.433 148.330 141.773 1.00 144.03 ? 648  ASN A O     1 
ATOM   4609  C  CB    . ASN A 1 648 ? 133.991 146.432 144.162 1.00 147.15 ? 648  ASN A CB    1 
ATOM   4610  C  CG    . ASN A 1 648 ? 132.644 147.010 144.613 1.00 149.73 ? 648  ASN A CG    1 
ATOM   4611  O  OD1   . ASN A 1 648 ? 131.898 147.619 143.850 1.00 146.95 ? 648  ASN A OD1   1 
ATOM   4612  N  ND2   . ASN A 1 648 ? 132.337 146.807 145.888 1.00 152.52 ? 648  ASN A ND2   1 
ATOM   4613  N  N     . PRO A 1 649 ? 132.525 147.319 141.151 1.00 138.05 ? 649  PRO A N     1 
ATOM   4614  C  CA    . PRO A 1 649 ? 132.074 148.440 140.316 1.00 137.88 ? 649  PRO A CA    1 
ATOM   4615  C  C     . PRO A 1 649 ? 131.664 149.678 141.109 1.00 141.26 ? 649  PRO A C     1 
ATOM   4616  O  O     . PRO A 1 649 ? 130.522 150.131 141.041 1.00 140.71 ? 649  PRO A O     1 
ATOM   4617  C  CB    . PRO A 1 649 ? 130.882 147.842 139.564 1.00 133.05 ? 649  PRO A CB    1 
ATOM   4618  C  CG    . PRO A 1 649 ? 130.384 146.770 140.448 1.00 133.29 ? 649  PRO A CG    1 
ATOM   4619  C  CD    . PRO A 1 649 ? 131.606 146.176 141.070 1.00 136.33 ? 649  PRO A CD    1 
ATOM   4620  N  N     . LYS A 1 650 ? 132.600 150.221 141.873 1.00 142.70 ? 650  LYS A N     1 
ATOM   4621  C  CA    . LYS A 1 650 ? 132.443 151.513 142.527 1.00 142.79 ? 650  LYS A CA    1 
ATOM   4622  C  C     . LYS A 1 650 ? 133.604 152.446 142.240 1.00 143.27 ? 650  LYS A C     1 
ATOM   4623  O  O     . LYS A 1 650 ? 133.427 153.666 142.236 1.00 142.98 ? 650  LYS A O     1 
ATOM   4624  C  CB    . LYS A 1 650 ? 132.293 151.333 144.043 1.00 143.79 ? 650  LYS A CB    1 
ATOM   4625  C  CG    . LYS A 1 650 ? 131.373 152.349 144.699 1.00 144.82 ? 650  LYS A CG    1 
ATOM   4626  C  CD    . LYS A 1 650 ? 129.914 152.046 144.407 1.00 147.78 ? 650  LYS A CD    1 
ATOM   4627  C  CE    . LYS A 1 650 ? 129.484 150.738 145.050 1.00 146.36 ? 650  LYS A CE    1 
ATOM   4628  N  NZ    . LYS A 1 650 ? 128.033 150.474 144.852 1.00 142.11 ? 650  LYS A NZ    1 
ATOM   4629  N  N     . HIS A 1 651 ? 134.792 151.892 142.001 1.00 144.02 ? 651  HIS A N     1 
ATOM   4630  C  CA    . HIS A 1 651 ? 135.937 152.704 141.613 1.00 146.15 ? 651  HIS A CA    1 
ATOM   4631  C  C     . HIS A 1 651 ? 136.069 152.793 140.099 1.00 147.80 ? 651  HIS A C     1 
ATOM   4632  O  O     . HIS A 1 651 ? 136.835 153.620 139.592 1.00 152.33 ? 651  HIS A O     1 
ATOM   4633  C  CB    . HIS A 1 651 ? 137.209 152.129 142.232 1.00 145.82 ? 651  HIS A CB    1 
ATOM   4634  C  CG    . HIS A 1 651 ? 137.065 150.711 142.690 1.00 146.34 ? 651  HIS A CG    1 
ATOM   4635  N  ND1   . HIS A 1 651 ? 136.418 150.369 143.858 1.00 145.54 ? 651  HIS A ND1   1 
ATOM   4636  C  CD2   . HIS A 1 651 ? 137.480 149.548 142.136 1.00 146.15 ? 651  HIS A CD2   1 
ATOM   4637  C  CE1   . HIS A 1 651 ? 136.444 149.057 144.005 1.00 147.50 ? 651  HIS A CE1   1 
ATOM   4638  N  NE2   . HIS A 1 651 ? 137.082 148.535 142.973 1.00 149.99 ? 651  HIS A NE2   1 
ATOM   4639  N  N     . MET A 1 652 ? 135.333 151.956 139.364 1.00 142.57 ? 652  MET A N     1 
ATOM   4640  C  CA    . MET A 1 652 ? 135.275 152.024 137.909 1.00 139.39 ? 652  MET A CA    1 
ATOM   4641  C  C     . MET A 1 652 ? 134.034 152.745 137.410 1.00 136.67 ? 652  MET A C     1 
ATOM   4642  O  O     . MET A 1 652 ? 133.474 152.361 136.373 1.00 136.27 ? 652  MET A O     1 
ATOM   4643  C  CB    . MET A 1 652 ? 135.350 150.623 137.305 1.00 135.61 ? 652  MET A CB    1 
ATOM   4644  C  CG    . MET A 1 652 ? 136.161 149.648 138.115 1.00 136.27 ? 652  MET A CG    1 
ATOM   4645  S  SD    . MET A 1 652 ? 137.865 150.213 138.261 1.00 151.22 ? 652  MET A SD    1 
ATOM   4646  C  CE    . MET A 1 652 ? 138.514 149.760 136.653 1.00 135.41 ? 652  MET A CE    1 
ATOM   4647  N  N     . LYS A 1 653 ? 133.583 153.773 138.129 1.00 136.68 ? 653  LYS A N     1 
ATOM   4648  C  CA    . LYS A 1 653 ? 132.427 154.534 137.677 1.00 136.80 ? 653  LYS A CA    1 
ATOM   4649  C  C     . LYS A 1 653 ? 132.686 155.161 136.315 1.00 139.10 ? 653  LYS A C     1 
ATOM   4650  O  O     . LYS A 1 653 ? 131.816 155.136 135.438 1.00 139.40 ? 653  LYS A O     1 
ATOM   4651  C  CB    . LYS A 1 653 ? 132.070 155.608 138.705 1.00 136.53 ? 653  LYS A CB    1 
ATOM   4652  C  CG    . LYS A 1 653 ? 131.163 156.701 138.168 1.00 143.72 ? 653  LYS A CG    1 
ATOM   4653  C  CD    . LYS A 1 653 ? 131.059 157.863 139.142 1.00 147.23 ? 653  LYS A CD    1 
ATOM   4654  C  CE    . LYS A 1 653 ? 130.222 158.991 138.562 1.00 150.35 ? 653  LYS A CE    1 
ATOM   4655  N  NZ    . LYS A 1 653 ? 130.111 160.142 139.499 1.00 146.74 ? 653  LYS A NZ    1 
ATOM   4656  N  N     . LEU A 1 654 ? 133.885 155.713 136.114 1.00 137.81 ? 654  LEU A N     1 
ATOM   4657  C  CA    . LEU A 1 654 ? 134.208 156.331 134.832 1.00 137.37 ? 654  LEU A CA    1 
ATOM   4658  C  C     . LEU A 1 654 ? 134.203 155.310 133.701 1.00 136.93 ? 654  LEU A C     1 
ATOM   4659  O  O     . LEU A 1 654 ? 133.644 155.570 132.631 1.00 138.34 ? 654  LEU A O     1 
ATOM   4660  C  CB    . LEU A 1 654 ? 135.561 157.035 134.914 1.00 135.96 ? 654  LEU A CB    1 
ATOM   4661  C  CG    . LEU A 1 654 ? 135.554 158.393 135.615 1.00 141.02 ? 654  LEU A CG    1 
ATOM   4662  C  CD1   . LEU A 1 654 ? 136.920 159.054 135.520 1.00 146.38 ? 654  LEU A CD1   1 
ATOM   4663  C  CD2   . LEU A 1 654 ? 134.476 159.292 135.030 1.00 137.89 ? 654  LEU A CD2   1 
ATOM   4664  N  N     . THR A 1 655 ? 134.812 154.142 133.918 1.00 134.56 ? 655  THR A N     1 
ATOM   4665  C  CA    . THR A 1 655 ? 134.853 153.130 132.866 1.00 133.46 ? 655  THR A CA    1 
ATOM   4666  C  C     . THR A 1 655 ? 133.460 152.603 132.543 1.00 132.19 ? 655  THR A C     1 
ATOM   4667  O  O     . THR A 1 655 ? 133.111 152.426 131.367 1.00 133.76 ? 655  THR A O     1 
ATOM   4668  C  CB    . THR A 1 655 ? 135.771 151.981 133.274 1.00 128.68 ? 655  THR A CB    1 
ATOM   4669  O  OG1   . THR A 1 655 ? 136.920 152.504 133.951 1.00 133.17 ? 655  THR A OG1   1 
ATOM   4670  C  CG2   . THR A 1 655 ? 136.224 151.215 132.048 1.00 122.74 ? 655  THR A CG2   1 
ATOM   4671  N  N     . TYR A 1 656 ? 132.651 152.339 133.571 1.00 130.91 ? 656  TYR A N     1 
ATOM   4672  C  CA    . TYR A 1 656 ? 131.302 151.845 133.324 1.00 127.72 ? 656  TYR A CA    1 
ATOM   4673  C  C     . TYR A 1 656 ? 130.450 152.895 132.628 1.00 129.22 ? 656  TYR A C     1 
ATOM   4674  O  O     . TYR A 1 656 ? 129.659 152.565 131.740 1.00 130.54 ? 656  TYR A O     1 
ATOM   4675  C  CB    . TYR A 1 656 ? 130.649 151.397 134.628 1.00 127.09 ? 656  TYR A CB    1 
ATOM   4676  C  CG    . TYR A 1 656 ? 130.973 149.970 134.991 1.00 121.91 ? 656  TYR A CG    1 
ATOM   4677  C  CD1   . TYR A 1 656 ? 130.475 148.917 134.241 1.00 116.59 ? 656  TYR A CD1   1 
ATOM   4678  C  CD2   . TYR A 1 656 ? 131.773 149.676 136.081 1.00 123.02 ? 656  TYR A CD2   1 
ATOM   4679  C  CE1   . TYR A 1 656 ? 130.765 147.611 134.566 1.00 113.73 ? 656  TYR A CE1   1 
ATOM   4680  C  CE2   . TYR A 1 656 ? 132.068 148.374 136.412 1.00 120.33 ? 656  TYR A CE2   1 
ATOM   4681  C  CZ    . TYR A 1 656 ? 131.562 147.345 135.653 1.00 116.61 ? 656  TYR A CZ    1 
ATOM   4682  O  OH    . TYR A 1 656 ? 131.856 146.044 135.984 1.00 119.03 ? 656  TYR A OH    1 
ATOM   4683  N  N     . TYR A 1 657 ? 130.596 154.165 133.010 1.00 127.49 ? 657  TYR A N     1 
ATOM   4684  C  CA    . TYR A 1 657 ? 129.863 155.219 132.321 1.00 130.36 ? 657  TYR A CA    1 
ATOM   4685  C  C     . TYR A 1 657 ? 130.319 155.344 130.875 1.00 131.61 ? 657  TYR A C     1 
ATOM   4686  O  O     . TYR A 1 657 ? 129.505 155.596 129.982 1.00 134.74 ? 657  TYR A O     1 
ATOM   4687  C  CB    . TYR A 1 657 ? 130.025 156.549 133.053 1.00 136.57 ? 657  TYR A CB    1 
ATOM   4688  C  CG    . TYR A 1 657 ? 129.217 157.670 132.442 1.00 147.33 ? 657  TYR A CG    1 
ATOM   4689  C  CD1   . TYR A 1 657 ? 127.864 157.806 132.719 1.00 151.48 ? 657  TYR A CD1   1 
ATOM   4690  C  CD2   . TYR A 1 657 ? 129.806 158.591 131.585 1.00 147.35 ? 657  TYR A CD2   1 
ATOM   4691  C  CE1   . TYR A 1 657 ? 127.120 158.828 132.162 1.00 158.02 ? 657  TYR A CE1   1 
ATOM   4692  C  CE2   . TYR A 1 657 ? 129.070 159.617 131.023 1.00 149.05 ? 657  TYR A CE2   1 
ATOM   4693  C  CZ    . TYR A 1 657 ? 127.727 159.731 131.315 1.00 157.67 ? 657  TYR A CZ    1 
ATOM   4694  O  OH    . TYR A 1 657 ? 126.989 160.750 130.759 1.00 159.60 ? 657  TYR A OH    1 
ATOM   4695  N  N     . PHE A 1 658 ? 131.617 155.166 130.622 1.00 128.78 ? 658  PHE A N     1 
ATOM   4696  C  CA    . PHE A 1 658 ? 132.120 155.202 129.253 1.00 132.09 ? 658  PHE A CA    1 
ATOM   4697  C  C     . PHE A 1 658 ? 131.504 154.095 128.410 1.00 130.22 ? 658  PHE A C     1 
ATOM   4698  O  O     . PHE A 1 658 ? 131.036 154.337 127.291 1.00 129.02 ? 658  PHE A O     1 
ATOM   4699  C  CB    . PHE A 1 658 ? 133.644 155.090 129.257 1.00 132.59 ? 658  PHE A CB    1 
ATOM   4700  C  CG    . PHE A 1 658 ? 134.241 154.908 127.893 1.00 133.50 ? 658  PHE A CG    1 
ATOM   4701  C  CD1   . PHE A 1 658 ? 134.199 155.928 126.960 1.00 134.81 ? 658  PHE A CD1   1 
ATOM   4702  C  CD2   . PHE A 1 658 ? 134.851 153.714 127.547 1.00 130.76 ? 658  PHE A CD2   1 
ATOM   4703  C  CE1   . PHE A 1 658 ? 134.751 155.760 125.705 1.00 135.31 ? 658  PHE A CE1   1 
ATOM   4704  C  CE2   . PHE A 1 658 ? 135.405 153.541 126.296 1.00 132.09 ? 658  PHE A CE2   1 
ATOM   4705  C  CZ    . PHE A 1 658 ? 135.354 154.564 125.373 1.00 133.58 ? 658  PHE A CZ    1 
ATOM   4706  N  N     . VAL A 1 659 ? 131.493 152.868 128.933 1.00 128.77 ? 659  VAL A N     1 
ATOM   4707  C  CA    . VAL A 1 659 ? 130.925 151.757 128.174 1.00 124.82 ? 659  VAL A CA    1 
ATOM   4708  C  C     . VAL A 1 659 ? 129.426 151.950 127.979 1.00 127.73 ? 659  VAL A C     1 
ATOM   4709  O  O     . VAL A 1 659 ? 128.883 151.679 126.899 1.00 129.35 ? 659  VAL A O     1 
ATOM   4710  C  CB    . VAL A 1 659 ? 131.237 150.415 128.856 1.00 117.74 ? 659  VAL A CB    1 
ATOM   4711  C  CG1   . VAL A 1 659 ? 130.502 149.299 128.146 1.00 116.47 ? 659  VAL A CG1   1 
ATOM   4712  C  CG2   . VAL A 1 659 ? 132.730 150.160 128.848 1.00 116.89 ? 659  VAL A CG2   1 
ATOM   4713  N  N     . GLY A 1 660 ? 128.731 152.413 129.019 1.00 126.69 ? 660  GLY A N     1 
ATOM   4714  C  CA    . GLY A 1 660 ? 127.308 152.666 128.889 1.00 123.24 ? 660  GLY A CA    1 
ATOM   4715  C  C     . GLY A 1 660 ? 127.002 153.736 127.862 1.00 126.42 ? 660  GLY A C     1 
ATOM   4716  O  O     . GLY A 1 660 ? 126.047 153.614 127.096 1.00 128.09 ? 660  GLY A O     1 
ATOM   4717  N  N     . ALA A 1 661 ? 127.814 154.794 127.824 1.00 125.37 ? 661  ALA A N     1 
ATOM   4718  C  CA    . ALA A 1 661 ? 127.626 155.839 126.824 1.00 128.82 ? 661  ALA A CA    1 
ATOM   4719  C  C     . ALA A 1 661 ? 127.910 155.319 125.422 1.00 129.34 ? 661  ALA A C     1 
ATOM   4720  O  O     . ALA A 1 661 ? 127.208 155.676 124.470 1.00 131.20 ? 661  ALA A O     1 
ATOM   4721  C  CB    . ALA A 1 661 ? 128.517 157.038 127.145 1.00 130.77 ? 661  ALA A CB    1 
ATOM   4722  N  N     . VAL A 1 662 ? 128.935 154.476 125.274 1.00 127.00 ? 662  VAL A N     1 
ATOM   4723  C  CA    . VAL A 1 662 ? 129.234 153.897 123.966 1.00 126.88 ? 662  VAL A CA    1 
ATOM   4724  C  C     . VAL A 1 662 ? 128.061 153.056 123.480 1.00 128.12 ? 662  VAL A C     1 
ATOM   4725  O  O     . VAL A 1 662 ? 127.615 153.178 122.332 1.00 131.73 ? 662  VAL A O     1 
ATOM   4726  C  CB    . VAL A 1 662 ? 130.531 153.071 124.026 1.00 122.96 ? 662  VAL A CB    1 
ATOM   4727  C  CG1   . VAL A 1 662 ? 130.646 152.178 122.805 1.00 117.69 ? 662  VAL A CG1   1 
ATOM   4728  C  CG2   . VAL A 1 662 ? 131.734 153.987 124.126 1.00 128.08 ? 662  VAL A CG2   1 
ATOM   4729  N  N     . PHE A 1 663 ? 127.529 152.202 124.357 1.00 123.76 ? 663  PHE A N     1 
ATOM   4730  C  CA    . PHE A 1 663 ? 126.401 151.359 123.972 1.00 121.61 ? 663  PHE A CA    1 
ATOM   4731  C  C     . PHE A 1 663 ? 125.146 152.187 123.719 1.00 123.82 ? 663  PHE A C     1 
ATOM   4732  O  O     . PHE A 1 663 ? 124.356 151.871 122.822 1.00 126.22 ? 663  PHE A O     1 
ATOM   4733  C  CB    . PHE A 1 663 ? 126.153 150.297 125.040 1.00 120.40 ? 663  PHE A CB    1 
ATOM   4734  C  CG    . PHE A 1 663 ? 127.142 149.166 125.010 1.00 117.77 ? 663  PHE A CG    1 
ATOM   4735  C  CD1   . PHE A 1 663 ? 127.981 148.992 123.925 1.00 115.22 ? 663  PHE A CD1   1 
ATOM   4736  C  CD2   . PHE A 1 663 ? 127.229 148.273 126.063 1.00 117.35 ? 663  PHE A CD2   1 
ATOM   4737  C  CE1   . PHE A 1 663 ? 128.889 147.953 123.893 1.00 114.50 ? 663  PHE A CE1   1 
ATOM   4738  C  CE2   . PHE A 1 663 ? 128.136 147.232 126.035 1.00 111.53 ? 663  PHE A CE2   1 
ATOM   4739  C  CZ    . PHE A 1 663 ? 128.966 147.073 124.949 1.00 107.95 ? 663  PHE A CZ    1 
ATOM   4740  N  N     . GLY A 1 664 ? 124.945 153.256 124.491 1.00 122.35 ? 664  GLY A N     1 
ATOM   4741  C  CA    . GLY A 1 664 ? 123.801 154.121 124.255 1.00 127.24 ? 664  GLY A CA    1 
ATOM   4742  C  C     . GLY A 1 664 ? 123.876 154.843 122.925 1.00 131.74 ? 664  GLY A C     1 
ATOM   4743  O  O     . GLY A 1 664 ? 122.868 154.987 122.229 1.00 133.87 ? 664  GLY A O     1 
ATOM   4744  N  N     . LEU A 1 665 ? 125.067 155.316 122.554 1.00 128.96 ? 665  LEU A N     1 
ATOM   4745  C  CA    . LEU A 1 665 ? 125.235 155.933 121.243 1.00 129.44 ? 665  LEU A CA    1 
ATOM   4746  C  C     . LEU A 1 665 ? 125.047 154.909 120.132 1.00 127.60 ? 665  LEU A C     1 
ATOM   4747  O  O     . LEU A 1 665 ? 124.444 155.207 119.090 1.00 133.48 ? 665  LEU A O     1 
ATOM   4748  C  CB    . LEU A 1 665 ? 126.610 156.591 121.150 1.00 130.86 ? 665  LEU A CB    1 
ATOM   4749  C  CG    . LEU A 1 665 ? 126.777 157.856 121.993 1.00 134.37 ? 665  LEU A CG    1 
ATOM   4750  C  CD1   . LEU A 1 665 ? 128.166 158.442 121.816 1.00 134.58 ? 665  LEU A CD1   1 
ATOM   4751  C  CD2   . LEU A 1 665 ? 125.710 158.881 121.646 1.00 136.95 ? 665  LEU A CD2   1 
ATOM   4752  N  N     . MET A 1 666 ? 125.544 153.688 120.343 1.00 122.47 ? 666  MET A N     1 
ATOM   4753  C  CA    . MET A 1 666 ? 125.344 152.633 119.359 1.00 122.90 ? 666  MET A CA    1 
ATOM   4754  C  C     . MET A 1 666 ? 123.864 152.317 119.186 1.00 126.98 ? 666  MET A C     1 
ATOM   4755  O  O     . MET A 1 666 ? 123.405 152.055 118.069 1.00 130.23 ? 666  MET A O     1 
ATOM   4756  C  CB    . MET A 1 666 ? 126.127 151.385 119.765 1.00 117.56 ? 666  MET A CB    1 
ATOM   4757  C  CG    . MET A 1 666 ? 125.666 150.105 119.099 1.00 116.44 ? 666  MET A CG    1 
ATOM   4758  S  SD    . MET A 1 666 ? 126.536 148.664 119.736 1.00 119.83 ? 666  MET A SD    1 
ATOM   4759  C  CE    . MET A 1 666 ? 128.207 149.303 119.819 1.00 111.65 ? 666  MET A CE    1 
ATOM   4760  N  N     . MET A 1 667 ? 123.135 152.376 120.298 1.00 124.09 ? 667  MET A N     1 
ATOM   4761  C  CA    . MET A 1 667 ? 121.702 152.145 120.300 1.00 120.80 ? 667  MET A CA    1 
ATOM   4762  C  C     . MET A 1 667 ? 121.072 153.252 119.469 1.00 125.31 ? 667  MET A C     1 
ATOM   4763  O  O     . MET A 1 667 ? 120.334 152.981 118.522 1.00 128.80 ? 667  MET A O     1 
ATOM   4764  C  CB    . MET A 1 667 ? 121.151 152.172 121.725 1.00 114.39 ? 667  MET A CB    1 
ATOM   4765  C  CG    . MET A 1 667 ? 121.470 150.927 122.538 1.00 112.43 ? 667  MET A CG    1 
ATOM   4766  S  SD    . MET A 1 667 ? 121.321 149.410 121.575 1.00 119.51 ? 667  MET A SD    1 
ATOM   4767  C  CE    . MET A 1 667 ? 119.944 148.618 122.401 1.00 114.07 ? 667  MET A CE    1 
ATOM   4768  N  N     . MET A 1 668 ? 121.364 154.502 119.823 1.00 124.28 ? 668  MET A N     1 
ATOM   4769  C  CA    . MET A 1 668 ? 120.830 155.621 119.049 1.00 128.35 ? 668  MET A CA    1 
ATOM   4770  C  C     . MET A 1 668 ? 121.005 155.384 117.558 1.00 127.65 ? 668  MET A C     1 
ATOM   4771  O  O     . MET A 1 668 ? 120.049 155.515 116.777 1.00 127.87 ? 668  MET A O     1 
ATOM   4772  C  CB    . MET A 1 668 ? 121.501 156.933 119.451 1.00 133.48 ? 668  MET A CB    1 
ATOM   4773  C  CG    . MET A 1 668 ? 121.009 157.534 120.743 1.00 139.30 ? 668  MET A CG    1 
ATOM   4774  S  SD    . MET A 1 668 ? 119.323 157.017 121.092 1.00 152.71 ? 668  MET A SD    1 
ATOM   4775  C  CE    . MET A 1 668 ? 119.351 157.026 122.869 1.00 129.51 ? 668  MET A CE    1 
ATOM   4776  N  N     . LEU A 1 669 ? 122.221 155.024 117.146 1.00 125.36 ? 669  LEU A N     1 
ATOM   4777  C  CA    . LEU A 1 669 ? 122.454 154.745 115.736 1.00 123.06 ? 669  LEU A CA    1 
ATOM   4778  C  C     . LEU A 1 669 ? 121.540 153.629 115.250 1.00 124.83 ? 669  LEU A C     1 
ATOM   4779  O  O     . LEU A 1 669 ? 120.884 153.762 114.210 1.00 126.83 ? 669  LEU A O     1 
ATOM   4780  C  CB    . LEU A 1 669 ? 123.919 154.382 115.514 1.00 122.18 ? 669  LEU A CB    1 
ATOM   4781  C  CG    . LEU A 1 669 ? 124.333 153.968 114.103 1.00 128.22 ? 669  LEU A CG    1 
ATOM   4782  C  CD1   . LEU A 1 669 ? 124.205 155.134 113.137 1.00 126.13 ? 669  LEU A CD1   1 
ATOM   4783  C  CD2   . LEU A 1 669 ? 125.753 153.441 114.125 1.00 127.93 ? 669  LEU A CD2   1 
ATOM   4784  N  N     . SER A 1 670 ? 121.443 152.545 116.022 1.00 121.38 ? 670  SER A N     1 
ATOM   4785  C  CA    . SER A 1 670 ? 120.616 151.411 115.625 1.00 120.68 ? 670  SER A CA    1 
ATOM   4786  C  C     . SER A 1 670 ? 119.141 151.785 115.564 1.00 124.22 ? 670  SER A C     1 
ATOM   4787  O  O     . SER A 1 670 ? 118.420 151.333 114.671 1.00 128.18 ? 670  SER A O     1 
ATOM   4788  C  CB    . SER A 1 670 ? 120.832 150.244 116.586 1.00 117.63 ? 670  SER A CB    1 
ATOM   4789  O  OG    . SER A 1 670 ? 122.204 149.898 116.677 1.00 118.79 ? 670  SER A OG    1 
ATOM   4790  N  N     . SER A 1 671 ? 118.709 152.580 116.539 1.00 121.34 ? 671  SER A N     1 
ATOM   4791  C  CA    . SER A 1 671 ? 117.326 153.025 116.630 1.00 122.41 ? 671  SER A CA    1 
ATOM   4792  C  C     . SER A 1 671 ? 116.930 153.801 115.385 1.00 125.39 ? 671  SER A C     1 
ATOM   4793  O  O     . SER A 1 671 ? 115.984 153.430 114.691 1.00 131.77 ? 671  SER A O     1 
ATOM   4794  C  CB    . SER A 1 671 ? 117.122 153.889 117.876 1.00 121.40 ? 671  SER A CB    1 
ATOM   4795  O  OG    . SER A 1 671 ? 115.982 153.470 118.606 1.00 128.02 ? 671  SER A OG    1 
ATOM   4796  N  N     . LEU A 1 672 ? 117.654 154.879 115.102 1.00 120.86 ? 672  LEU A N     1 
ATOM   4797  C  CA    . LEU A 1 672 ? 117.343 155.679 113.919 1.00 124.11 ? 672  LEU A CA    1 
ATOM   4798  C  C     . LEU A 1 672 ? 117.492 154.876 112.630 1.00 124.69 ? 672  LEU A C     1 
ATOM   4799  O  O     . LEU A 1 672 ? 116.709 155.064 111.692 1.00 127.82 ? 672  LEU A O     1 
ATOM   4800  C  CB    . LEU A 1 672 ? 118.165 156.970 113.867 1.00 126.98 ? 672  LEU A CB    1 
ATOM   4801  C  CG    . LEU A 1 672 ? 117.854 158.084 114.883 1.00 127.74 ? 672  LEU A CG    1 
ATOM   4802  C  CD1   . LEU A 1 672 ? 116.345 158.302 114.972 1.00 124.94 ? 672  LEU A CD1   1 
ATOM   4803  C  CD2   . LEU A 1 672 ? 118.428 157.901 116.263 1.00 124.38 ? 672  LEU A CD2   1 
ATOM   4804  N  N     . VAL A 1 673 ? 118.468 153.965 112.559 1.00 122.16 ? 673  VAL A N     1 
ATOM   4805  C  CA    . VAL A 1 673 ? 118.591 153.128 111.367 1.00 122.87 ? 673  VAL A CA    1 
ATOM   4806  C  C     . VAL A 1 673 ? 117.363 152.237 111.200 1.00 126.38 ? 673  VAL A C     1 
ATOM   4807  O  O     . VAL A 1 673 ? 116.825 152.095 110.095 1.00 132.02 ? 673  VAL A O     1 
ATOM   4808  C  CB    . VAL A 1 673 ? 119.894 152.309 111.421 1.00 117.67 ? 673  VAL A CB    1 
ATOM   4809  C  CG1   . VAL A 1 673 ? 119.887 151.228 110.364 1.00 120.09 ? 673  VAL A CG1   1 
ATOM   4810  C  CG2   . VAL A 1 673 ? 121.088 153.223 111.207 1.00 117.81 ? 673  VAL A CG2   1 
ATOM   4811  N  N     . GLY A 1 674 ? 116.893 151.632 112.292 1.00 121.59 ? 674  GLY A N     1 
ATOM   4812  C  CA    . GLY A 1 674 ? 115.708 150.794 112.213 1.00 123.15 ? 674  GLY A CA    1 
ATOM   4813  C  C     . GLY A 1 674 ? 114.458 151.578 111.865 1.00 129.23 ? 674  GLY A C     1 
ATOM   4814  O  O     . GLY A 1 674 ? 113.619 151.115 111.087 1.00 133.82 ? 674  GLY A O     1 
ATOM   4815  N  N     . ALA A 1 675 ? 114.312 152.773 112.441 1.00 126.14 ? 675  ALA A N     1 
ATOM   4816  C  CA    . ALA A 1 675 ? 113.176 153.620 112.099 1.00 126.54 ? 675  ALA A CA    1 
ATOM   4817  C  C     . ALA A 1 675 ? 113.205 154.003 110.627 1.00 130.08 ? 675  ALA A C     1 
ATOM   4818  O  O     . ALA A 1 675 ? 112.168 153.985 109.952 1.00 133.48 ? 675  ALA A O     1 
ATOM   4819  C  CB    . ALA A 1 675 ? 113.164 154.867 112.981 1.00 121.71 ? 675  ALA A CB    1 
ATOM   4820  N  N     . GLY A 1 676 ? 114.385 154.352 110.110 1.00 128.06 ? 676  GLY A N     1 
ATOM   4821  C  CA    . GLY A 1 676 ? 114.501 154.652 108.695 1.00 131.08 ? 676  GLY A CA    1 
ATOM   4822  C  C     . GLY A 1 676 ? 114.153 153.464 107.820 1.00 133.67 ? 676  GLY A C     1 
ATOM   4823  O  O     . GLY A 1 676 ? 113.462 153.609 106.810 1.00 137.14 ? 676  GLY A O     1 
ATOM   4824  N  N     . ILE A 1 677 ? 114.620 152.272 108.200 1.00 130.51 ? 677  ILE A N     1 
ATOM   4825  C  CA    . ILE A 1 677 ? 114.308 151.075 107.425 1.00 130.85 ? 677  ILE A CA    1 
ATOM   4826  C  C     . ILE A 1 677 ? 112.805 150.834 107.400 1.00 137.07 ? 677  ILE A C     1 
ATOM   4827  O  O     . ILE A 1 677 ? 112.218 150.579 106.340 1.00 143.47 ? 677  ILE A O     1 
ATOM   4828  C  CB    . ILE A 1 677 ? 115.062 149.857 107.987 1.00 123.79 ? 677  ILE A CB    1 
ATOM   4829  C  CG1   . ILE A 1 677 ? 116.551 149.948 107.662 1.00 122.97 ? 677  ILE A CG1   1 
ATOM   4830  C  CG2   . ILE A 1 677 ? 114.482 148.569 107.434 1.00 127.05 ? 677  ILE A CG2   1 
ATOM   4831  C  CD1   . ILE A 1 677 ? 117.421 149.188 108.630 1.00 119.90 ? 677  ILE A CD1   1 
ATOM   4832  N  N     . PHE A 1 678 ? 112.156 150.924 108.563 1.00 134.91 ? 678  PHE A N     1 
ATOM   4833  C  CA    . PHE A 1 678 ? 110.715 150.702 108.617 1.00 137.27 ? 678  PHE A CA    1 
ATOM   4834  C  C     . PHE A 1 678 ? 109.951 151.741 107.807 1.00 141.21 ? 678  PHE A C     1 
ATOM   4835  O  O     . PHE A 1 678 ? 109.003 151.401 107.089 1.00 140.64 ? 678  PHE A O     1 
ATOM   4836  C  CB    . PHE A 1 678 ? 110.227 150.702 110.063 1.00 131.06 ? 678  PHE A CB    1 
ATOM   4837  C  CG    . PHE A 1 678 ? 108.872 150.088 110.233 1.00 133.67 ? 678  PHE A CG    1 
ATOM   4838  C  CD1   . PHE A 1 678 ? 108.528 148.938 109.546 1.00 137.55 ? 678  PHE A CD1   1 
ATOM   4839  C  CD2   . PHE A 1 678 ? 107.928 150.680 111.053 1.00 133.37 ? 678  PHE A CD2   1 
ATOM   4840  C  CE1   . PHE A 1 678 ? 107.275 148.379 109.690 1.00 135.61 ? 678  PHE A CE1   1 
ATOM   4841  C  CE2   . PHE A 1 678 ? 106.674 150.127 111.200 1.00 133.02 ? 678  PHE A CE2   1 
ATOM   4842  C  CZ    . PHE A 1 678 ? 106.346 148.977 110.514 1.00 130.50 ? 678  PHE A CZ    1 
ATOM   4843  N  N     . PHE A 1 679 ? 110.345 153.012 107.903 1.00 140.25 ? 679  PHE A N     1 
ATOM   4844  C  CA    . PHE A 1 679 ? 109.582 154.057 107.229 1.00 139.38 ? 679  PHE A CA    1 
ATOM   4845  C  C     . PHE A 1 679 ? 109.833 154.065 105.727 1.00 142.71 ? 679  PHE A C     1 
ATOM   4846  O  O     . PHE A 1 679 ? 108.971 154.509 104.961 1.00 148.44 ? 679  PHE A O     1 
ATOM   4847  C  CB    . PHE A 1 679 ? 109.901 155.423 107.839 1.00 133.42 ? 679  PHE A CB    1 
ATOM   4848  C  CG    . PHE A 1 679 ? 109.480 155.563 109.280 1.00 135.90 ? 679  PHE A CG    1 
ATOM   4849  C  CD1   . PHE A 1 679 ? 108.730 154.578 109.905 1.00 134.09 ? 679  PHE A CD1   1 
ATOM   4850  C  CD2   . PHE A 1 679 ? 109.833 156.687 110.008 1.00 138.08 ? 679  PHE A CD2   1 
ATOM   4851  C  CE1   . PHE A 1 679 ? 108.346 154.710 111.224 1.00 134.69 ? 679  PHE A CE1   1 
ATOM   4852  C  CE2   . PHE A 1 679 ? 109.450 156.824 111.329 1.00 139.13 ? 679  PHE A CE2   1 
ATOM   4853  C  CZ    . PHE A 1 679 ? 108.706 155.834 111.937 1.00 138.59 ? 679  PHE A CZ    1 
ATOM   4854  N  N     . SER A 1 680 ? 110.998 153.585 105.283 1.00 137.84 ? 680  SER A N     1 
ATOM   4855  C  CA    . SER A 1 680 ? 111.268 153.509 103.853 1.00 137.83 ? 680  SER A CA    1 
ATOM   4856  C  C     . SER A 1 680 ? 110.719 152.237 103.224 1.00 146.30 ? 680  SER A C     1 
ATOM   4857  O  O     . SER A 1 680 ? 110.453 152.225 102.018 1.00 151.49 ? 680  SER A O     1 
ATOM   4858  C  CB    . SER A 1 680 ? 112.769 153.614 103.602 1.00 137.42 ? 680  SER A CB    1 
ATOM   4859  O  OG    . SER A 1 680 ? 113.269 154.839 104.102 1.00 140.39 ? 680  SER A OG    1 
ATOM   4860  N  N     . THR A 1 681 ? 110.555 151.171 104.003 1.00 148.39 ? 681  THR A N     1 
ATOM   4861  C  CA    . THR A 1 681 ? 109.921 149.967 103.491 1.00 152.28 ? 681  THR A CA    1 
ATOM   4862  C  C     . THR A 1 681 ? 108.481 150.284 103.083 1.00 156.93 ? 681  THR A C     1 
ATOM   4863  O  O     . THR A 1 681 ? 107.796 151.062 103.754 1.00 155.97 ? 681  THR A O     1 
ATOM   4864  C  CB    . THR A 1 681 ? 109.943 148.870 104.556 1.00 148.15 ? 681  THR A CB    1 
ATOM   4865  O  OG1   . THR A 1 681 ? 111.226 148.851 105.192 1.00 146.38 ? 681  THR A OG1   1 
ATOM   4866  C  CG2   . THR A 1 681 ? 109.682 147.501 103.946 1.00 147.24 ? 681  THR A CG2   1 
ATOM   4867  N  N     . PRO A 1 682 ? 107.989 149.694 101.984 1.00 157.28 ? 682  PRO A N     1 
ATOM   4868  C  CA    . PRO A 1 682 ? 106.612 149.980 101.552 1.00 157.95 ? 682  PRO A CA    1 
ATOM   4869  C  C     . PRO A 1 682 ? 105.535 149.482 102.508 1.00 160.20 ? 682  PRO A C     1 
ATOM   4870  O  O     . PRO A 1 682 ? 104.346 149.528 102.176 1.00 158.91 ? 682  PRO A O     1 
ATOM   4871  C  CB    . PRO A 1 682 ? 106.520 149.279 100.188 1.00 157.01 ? 682  PRO A CB    1 
ATOM   4872  C  CG    . PRO A 1 682 ? 107.628 148.280 100.185 1.00 151.26 ? 682  PRO A CG    1 
ATOM   4873  C  CD    . PRO A 1 682 ? 108.726 148.916 100.975 1.00 150.98 ? 682  PRO A CD    1 
ATOM   4874  N  N     . ALA A 1 683 ? 105.936 149.001 103.687 1.00 160.85 ? 683  ALA A N     1 
ATOM   4875  C  CA    . ALA A 1 683 ? 105.026 148.697 104.793 1.00 155.74 ? 683  ALA A CA    1 
ATOM   4876  C  C     . ALA A 1 683 ? 103.967 147.670 104.377 1.00 156.09 ? 683  ALA A C     1 
ATOM   4877  O  O     . ALA A 1 683 ? 102.765 147.939 104.347 1.00 158.11 ? 683  ALA A O     1 
ATOM   4878  C  CB    . ALA A 1 683 ? 104.373 149.978 105.327 1.00 155.07 ? 683  ALA A CB    1 
ATOM   4879  N  N     . THR A 1 684 ? 104.456 146.477 104.054 1.00 151.72 ? 684  THR A N     1 
ATOM   4880  C  CA    . THR A 1 684 ? 103.560 145.390 103.700 1.00 149.09 ? 684  THR A CA    1 
ATOM   4881  C  C     . THR A 1 684 ? 102.834 144.876 104.940 1.00 143.99 ? 684  THR A C     1 
ATOM   4882  O  O     . THR A 1 684 ? 103.162 145.229 106.075 1.00 141.23 ? 684  THR A O     1 
ATOM   4883  C  CB    . THR A 1 684 ? 104.328 144.253 103.029 1.00 146.61 ? 684  THR A CB    1 
ATOM   4884  O  OG1   . THR A 1 684 ? 103.496 143.087 102.963 1.00 144.63 ? 684  THR A OG1   1 
ATOM   4885  C  CG2   . THR A 1 684 ? 105.590 143.927 103.806 1.00 143.56 ? 684  THR A CG2   1 
ATOM   4886  N  N     . VAL A 1 685 ? 101.819 144.040 104.705 1.00 143.23 ? 685  VAL A N     1 
ATOM   4887  C  CA    . VAL A 1 685 ? 100.967 143.568 105.795 1.00 143.00 ? 685  VAL A CA    1 
ATOM   4888  C  C     . VAL A 1 685 ? 101.773 142.759 106.803 1.00 136.13 ? 685  VAL A C     1 
ATOM   4889  O  O     . VAL A 1 685 ? 101.631 142.937 108.019 1.00 135.22 ? 685  VAL A O     1 
ATOM   4890  C  CB    . VAL A 1 685 ? 99.783  142.758 105.236 1.00 144.55 ? 685  VAL A CB    1 
ATOM   4891  C  CG1   . VAL A 1 685 ? 98.953  142.185 106.371 1.00 136.91 ? 685  VAL A CG1   1 
ATOM   4892  C  CG2   . VAL A 1 685 ? 98.926  143.634 104.336 1.00 148.78 ? 685  VAL A CG2   1 
ATOM   4893  N  N     . HIS A 1 686 ? 102.625 141.856 106.318 1.00 134.48 ? 686  HIS A N     1 
ATOM   4894  C  CA    . HIS A 1 686 ? 103.446 141.066 107.229 1.00 136.37 ? 686  HIS A CA    1 
ATOM   4895  C  C     . HIS A 1 686 ? 104.369 141.955 108.049 1.00 133.21 ? 686  HIS A C     1 
ATOM   4896  O  O     . HIS A 1 686 ? 104.500 141.774 109.265 1.00 129.38 ? 686  HIS A O     1 
ATOM   4897  C  CB    . HIS A 1 686 ? 104.255 140.034 106.446 1.00 141.70 ? 686  HIS A CB    1 
ATOM   4898  C  CG    . HIS A 1 686 ? 105.379 139.431 107.228 1.00 144.54 ? 686  HIS A CG    1 
ATOM   4899  N  ND1   . HIS A 1 686 ? 105.217 138.323 108.030 1.00 144.52 ? 686  HIS A ND1   1 
ATOM   4900  C  CD2   . HIS A 1 686 ? 106.683 139.781 107.328 1.00 143.60 ? 686  HIS A CD2   1 
ATOM   4901  C  CE1   . HIS A 1 686 ? 106.372 138.017 108.593 1.00 143.15 ? 686  HIS A CE1   1 
ATOM   4902  N  NE2   . HIS A 1 686 ? 107.279 138.886 108.183 1.00 144.70 ? 686  HIS A NE2   1 
ATOM   4903  N  N     . SER A 1 687 ? 105.008 142.931 107.400 1.00 136.53 ? 687  SER A N     1 
ATOM   4904  C  CA    . SER A 1 687 ? 105.928 143.814 108.108 1.00 136.42 ? 687  SER A CA    1 
ATOM   4905  C  C     . SER A 1 687 ? 105.205 144.628 109.171 1.00 131.79 ? 687  SER A C     1 
ATOM   4906  O  O     . SER A 1 687 ? 105.689 144.758 110.300 1.00 126.91 ? 687  SER A O     1 
ATOM   4907  C  CB    . SER A 1 687 ? 106.636 144.739 107.119 1.00 144.88 ? 687  SER A CB    1 
ATOM   4908  O  OG    . SER A 1 687 ? 107.402 145.717 107.799 1.00 146.03 ? 687  SER A OG    1 
ATOM   4909  N  N     . ILE A 1 688 ? 104.040 145.185 108.833 1.00 132.83 ? 688  ILE A N     1 
ATOM   4910  C  CA    . ILE A 1 688 ? 103.345 146.034 109.795 1.00 126.84 ? 688  ILE A CA    1 
ATOM   4911  C  C     . ILE A 1 688 ? 102.812 145.199 110.952 1.00 120.42 ? 688  ILE A C     1 
ATOM   4912  O  O     . ILE A 1 688 ? 102.879 145.618 112.112 1.00 117.75 ? 688  ILE A O     1 
ATOM   4913  C  CB    . ILE A 1 688 ? 102.232 146.855 109.112 1.00 128.49 ? 688  ILE A CB    1 
ATOM   4914  C  CG1   . ILE A 1 688 ? 101.483 147.703 110.139 1.00 126.61 ? 688  ILE A CG1   1 
ATOM   4915  C  CG2   . ILE A 1 688 ? 101.235 145.969 108.414 1.00 128.85 ? 688  ILE A CG2   1 
ATOM   4916  C  CD1   . ILE A 1 688 ? 100.591 148.753 109.514 1.00 123.84 ? 688  ILE A CD1   1 
ATOM   4917  N  N     . VAL A 1 689 ? 102.307 143.994 110.668 1.00 121.36 ? 689  VAL A N     1 
ATOM   4918  C  CA    . VAL A 1 689 ? 101.825 143.128 111.741 1.00 117.32 ? 689  VAL A CA    1 
ATOM   4919  C  C     . VAL A 1 689 ? 102.970 142.752 112.672 1.00 114.89 ? 689  VAL A C     1 
ATOM   4920  O  O     . VAL A 1 689 ? 102.840 142.818 113.900 1.00 116.66 ? 689  VAL A O     1 
ATOM   4921  C  CB    . VAL A 1 689 ? 101.134 141.881 111.160 1.00 116.73 ? 689  VAL A CB    1 
ATOM   4922  C  CG1   . VAL A 1 689 ? 101.259 140.704 112.115 1.00 104.83 ? 689  VAL A CG1   1 
ATOM   4923  C  CG2   . VAL A 1 689 ? 99.673  142.177 110.874 1.00 124.79 ? 689  VAL A CG2   1 
ATOM   4924  N  N     . VAL A 1 690 ? 104.115 142.366 112.103 1.00 117.05 ? 690  VAL A N     1 
ATOM   4925  C  CA    . VAL A 1 690 ? 105.245 141.959 112.933 1.00 117.24 ? 690  VAL A CA    1 
ATOM   4926  C  C     . VAL A 1 690 ? 105.755 143.134 113.755 1.00 114.43 ? 690  VAL A C     1 
ATOM   4927  O  O     . VAL A 1 690 ? 106.036 142.992 114.948 1.00 112.06 ? 690  VAL A O     1 
ATOM   4928  C  CB    . VAL A 1 690 ? 106.358 141.341 112.067 1.00 122.68 ? 690  VAL A CB    1 
ATOM   4929  C  CG1   . VAL A 1 690 ? 107.716 141.539 112.721 1.00 107.54 ? 690  VAL A CG1   1 
ATOM   4930  C  CG2   . VAL A 1 690 ? 106.090 139.862 111.841 1.00 126.27 ? 690  VAL A CG2   1 
ATOM   4931  N  N     . SER A 1 691 ? 105.873 144.313 113.144 1.00 116.74 ? 691  SER A N     1 
ATOM   4932  C  CA    . SER A 1 691 ? 106.374 145.467 113.883 1.00 114.29 ? 691  SER A CA    1 
ATOM   4933  C  C     . SER A 1 691 ? 105.427 145.852 115.010 1.00 108.98 ? 691  SER A C     1 
ATOM   4934  O  O     . SER A 1 691 ? 105.862 146.099 116.142 1.00 108.80 ? 691  SER A O     1 
ATOM   4935  C  CB    . SER A 1 691 ? 106.587 146.645 112.937 1.00 125.13 ? 691  SER A CB    1 
ATOM   4936  O  OG    . SER A 1 691 ? 106.891 147.820 113.664 1.00 126.57 ? 691  SER A OG    1 
ATOM   4937  N  N     . ILE A 1 692 ? 104.124 145.909 114.719 1.00 110.98 ? 692  ILE A N     1 
ATOM   4938  C  CA    . ILE A 1 692 ? 103.137 146.208 115.754 1.00 111.01 ? 692  ILE A CA    1 
ATOM   4939  C  C     . ILE A 1 692 ? 103.278 145.211 116.895 1.00 108.20 ? 692  ILE A C     1 
ATOM   4940  O  O     . ILE A 1 692 ? 103.683 145.566 118.007 1.00 109.69 ? 692  ILE A O     1 
ATOM   4941  C  CB    . ILE A 1 692 ? 101.716 146.201 115.157 1.00 110.62 ? 692  ILE A CB    1 
ATOM   4942  C  CG1   . ILE A 1 692 ? 101.368 147.567 114.559 1.00 114.37 ? 692  ILE A CG1   1 
ATOM   4943  C  CG2   . ILE A 1 692 ? 100.671 145.852 116.201 1.00 100.79 ? 692  ILE A CG2   1 
ATOM   4944  C  CD1   . ILE A 1 692 ? 99.902  147.710 114.159 1.00 112.48 ? 692  ILE A CD1   1 
ATOM   4945  N  N     . LEU A 1 693 ? 102.991 143.948 116.601 1.00 105.10 ? 693  LEU A N     1 
ATOM   4946  C  CA    . LEU A 1 693 ? 103.059 142.879 117.595 1.00 104.05 ? 693  LEU A CA    1 
ATOM   4947  C  C     . LEU A 1 693 ? 104.409 142.704 118.302 1.00 107.01 ? 693  LEU A C     1 
ATOM   4948  O  O     . LEU A 1 693 ? 104.468 142.087 119.366 1.00 105.83 ? 693  LEU A O     1 
ATOM   4949  C  CB    . LEU A 1 693 ? 102.632 141.548 116.966 1.00 103.07 ? 693  LEU A CB    1 
ATOM   4950  C  CG    . LEU A 1 693 ? 102.430 140.377 117.930 1.00 101.99 ? 693  LEU A CG    1 
ATOM   4951  C  CD1   . LEU A 1 693 ? 101.149 139.625 117.600 1.00 107.56 ? 693  LEU A CD1   1 
ATOM   4952  C  CD2   . LEU A 1 693 ? 103.628 139.441 117.899 1.00 100.37 ? 693  LEU A CD2   1 
ATOM   4953  N  N     . THR A 1 694 ? 105.488 143.234 117.730 1.00 109.65 ? 694  THR A N     1 
ATOM   4954  C  CA    . THR A 1 694 ? 106.797 143.077 118.355 1.00 107.53 ? 694  THR A CA    1 
ATOM   4955  C  C     . THR A 1 694 ? 107.169 144.263 119.242 1.00 106.22 ? 694  THR A C     1 
ATOM   4956  O  O     . THR A 1 694 ? 107.530 144.073 120.407 1.00 108.75 ? 694  THR A O     1 
ATOM   4957  C  CB    . THR A 1 694 ? 107.870 142.863 117.281 1.00 111.12 ? 694  THR A CB    1 
ATOM   4958  O  OG1   . THR A 1 694 ? 107.859 141.492 116.867 1.00 114.87 ? 694  THR A OG1   1 
ATOM   4959  C  CG2   . THR A 1 694 ? 109.254 143.198 117.829 1.00 104.66 ? 694  THR A CG2   1 
ATOM   4960  N  N     . VAL A 1 695 ? 107.085 145.486 118.725 1.00 105.32 ? 695  VAL A N     1 
ATOM   4961  C  CA    . VAL A 1 695 ? 107.510 146.666 119.466 1.00 103.71 ? 695  VAL A CA    1 
ATOM   4962  C  C     . VAL A 1 695 ? 106.330 147.402 120.084 1.00 107.27 ? 695  VAL A C     1 
ATOM   4963  O  O     . VAL A 1 695 ? 106.377 147.775 121.256 1.00 112.16 ? 695  VAL A O     1 
ATOM   4964  C  CB    . VAL A 1 695 ? 108.327 147.608 118.557 1.00 103.31 ? 695  VAL A CB    1 
ATOM   4965  C  CG1   . VAL A 1 695 ? 108.620 148.910 119.274 1.00 103.37 ? 695  VAL A CG1   1 
ATOM   4966  C  CG2   . VAL A 1 695 ? 109.617 146.940 118.131 1.00 105.20 ? 695  VAL A CG2   1 
ATOM   4967  N  N     . GLY A 1 696 ? 105.263 147.619 119.320 1.00 105.38 ? 696  GLY A N     1 
ATOM   4968  C  CA    . GLY A 1 696 ? 104.154 148.363 119.861 1.00 108.72 ? 696  GLY A CA    1 
ATOM   4969  C  C     . GLY A 1 696 ? 103.319 147.593 120.847 1.00 110.34 ? 696  GLY A C     1 
ATOM   4970  O  O     . GLY A 1 696 ? 102.293 148.103 121.302 1.00 111.58 ? 696  GLY A O     1 
ATOM   4971  N  N     . VAL A 1 697 ? 103.720 146.361 121.165 1.00 108.08 ? 697  VAL A N     1 
ATOM   4972  C  CA    . VAL A 1 697 ? 103.033 145.590 122.193 1.00 108.28 ? 697  VAL A CA    1 
ATOM   4973  C  C     . VAL A 1 697 ? 103.123 146.304 123.535 1.00 109.37 ? 697  VAL A C     1 
ATOM   4974  O  O     . VAL A 1 697 ? 102.183 146.270 124.340 1.00 117.68 ? 697  VAL A O     1 
ATOM   4975  C  CB    . VAL A 1 697 ? 103.606 144.160 122.246 1.00 102.55 ? 697  VAL A CB    1 
ATOM   4976  C  CG1   . VAL A 1 697 ? 104.834 144.077 123.129 1.00 103.33 ? 697  VAL A CG1   1 
ATOM   4977  C  CG2   . VAL A 1 697 ? 102.567 143.208 122.729 1.00 98.03  ? 697  VAL A CG2   1 
ATOM   4978  N  N     . TYR A 1 698 ? 104.240 146.993 123.779 1.00 102.94 ? 698  TYR A N     1 
ATOM   4979  C  CA    . TYR A 1 698 ? 104.397 147.776 124.998 1.00 108.22 ? 698  TYR A CA    1 
ATOM   4980  C  C     . TYR A 1 698 ? 103.315 148.842 125.087 1.00 112.81 ? 698  TYR A C     1 
ATOM   4981  O  O     . TYR A 1 698 ? 102.620 148.965 126.102 1.00 116.42 ? 698  TYR A O     1 
ATOM   4982  C  CB    . TYR A 1 698 ? 105.783 148.422 125.013 1.00 108.74 ? 698  TYR A CB    1 
ATOM   4983  C  CG    . TYR A 1 698 ? 106.938 147.450 125.117 1.00 109.63 ? 698  TYR A CG    1 
ATOM   4984  C  CD1   . TYR A 1 698 ? 106.723 146.084 125.198 1.00 110.46 ? 698  TYR A CD1   1 
ATOM   4985  C  CD2   . TYR A 1 698 ? 108.247 147.904 125.142 1.00 108.67 ? 698  TYR A CD2   1 
ATOM   4986  C  CE1   . TYR A 1 698 ? 107.772 145.198 125.289 1.00 111.40 ? 698  TYR A CE1   1 
ATOM   4987  C  CE2   . TYR A 1 698 ? 109.305 147.023 125.232 1.00 104.50 ? 698  TYR A CE2   1 
ATOM   4988  C  CZ    . TYR A 1 698 ? 109.060 145.672 125.308 1.00 108.52 ? 698  TYR A CZ    1 
ATOM   4989  O  OH    . TYR A 1 698 ? 110.106 144.786 125.403 1.00 115.81 ? 698  TYR A OH    1 
ATOM   4990  N  N     . PHE A 1 699 ? 103.138 149.598 124.004 1.00 108.87 ? 699  PHE A N     1 
ATOM   4991  C  CA    . PHE A 1 699 ? 102.173 150.689 123.997 1.00 109.79 ? 699  PHE A CA    1 
ATOM   4992  C  C     . PHE A 1 699 ? 100.746 150.161 124.006 1.00 112.21 ? 699  PHE A C     1 
ATOM   4993  O  O     . PHE A 1 699 ? 99.860  150.773 124.608 1.00 116.70 ? 699  PHE A O     1 
ATOM   4994  C  CB    . PHE A 1 699 ? 102.419 151.576 122.780 1.00 110.46 ? 699  PHE A CB    1 
ATOM   4995  C  CG    . PHE A 1 699 ? 103.822 152.101 122.696 1.00 111.66 ? 699  PHE A CG    1 
ATOM   4996  C  CD1   . PHE A 1 699 ? 104.176 153.278 123.325 1.00 114.45 ? 699  PHE A CD1   1 
ATOM   4997  C  CD2   . PHE A 1 699 ? 104.790 151.408 121.993 1.00 111.07 ? 699  PHE A CD2   1 
ATOM   4998  C  CE1   . PHE A 1 699 ? 105.466 153.756 123.250 1.00 113.73 ? 699  PHE A CE1   1 
ATOM   4999  C  CE2   . PHE A 1 699 ? 106.081 151.882 121.917 1.00 111.68 ? 699  PHE A CE2   1 
ATOM   5000  C  CZ    . PHE A 1 699 ? 106.419 153.057 122.545 1.00 112.16 ? 699  PHE A CZ    1 
ATOM   5001  N  N     . ILE A 1 700 ? 100.506 149.021 123.357 1.00 107.10 ? 700  ILE A N     1 
ATOM   5002  C  CA    . ILE A 1 700 ? 99.167  148.436 123.349 1.00 107.82 ? 700  ILE A CA    1 
ATOM   5003  C  C     . ILE A 1 700 ? 98.770  148.006 124.755 1.00 112.16 ? 700  ILE A C     1 
ATOM   5004  O  O     . ILE A 1 700 ? 97.678  148.330 125.238 1.00 117.70 ? 700  ILE A O     1 
ATOM   5005  C  CB    . ILE A 1 700 ? 99.101  147.259 122.361 1.00 102.61 ? 700  ILE A CB    1 
ATOM   5006  C  CG1   . ILE A 1 700 ? 99.057  147.769 120.922 1.00 107.74 ? 700  ILE A CG1   1 
ATOM   5007  C  CG2   . ILE A 1 700 ? 97.889  146.392 122.649 1.00 106.86 ? 700  ILE A CG2   1 
ATOM   5008  C  CD1   . ILE A 1 700 ? 99.017  146.667 119.890 1.00 109.34 ? 700  ILE A CD1   1 
ATOM   5009  N  N     . ALA A 1 701 ? 99.659  147.282 125.441 1.00 107.99 ? 701  ALA A N     1 
ATOM   5010  C  CA    . ALA A 1 701 ? 99.364  146.859 126.805 1.00 103.89 ? 701  ALA A CA    1 
ATOM   5011  C  C     . ALA A 1 701 ? 99.238  148.056 127.738 1.00 111.00 ? 701  ALA A C     1 
ATOM   5012  O  O     . ALA A 1 701 ? 98.375  148.075 128.625 1.00 116.61 ? 701  ALA A O     1 
ATOM   5013  C  CB    . ALA A 1 701 ? 100.441 145.898 127.302 1.00 98.59  ? 701  ALA A CB    1 
ATOM   5014  N  N     . SER A 1 702 ? 100.087 149.069 127.554 1.00 109.28 ? 702  SER A N     1 
ATOM   5015  C  CA    . SER A 1 702 ? 100.011 150.258 128.394 1.00 114.29 ? 702  SER A CA    1 
ATOM   5016  C  C     . SER A 1 702 ? 98.692  150.996 128.199 1.00 116.67 ? 702  SER A C     1 
ATOM   5017  O  O     . SER A 1 702 ? 98.060  151.420 129.173 1.00 121.24 ? 702  SER A O     1 
ATOM   5018  C  CB    . SER A 1 702 ? 101.197 151.169 128.095 1.00 114.24 ? 702  SER A CB    1 
ATOM   5019  O  OG    . SER A 1 702 ? 102.406 150.436 128.152 1.00 112.04 ? 702  SER A OG    1 
ATOM   5020  N  N     . ALA A 1 703 ? 98.253  151.153 126.949 1.00 111.76 ? 703  ALA A N     1 
ATOM   5021  C  CA    . ALA A 1 703 ? 96.974  151.804 126.694 1.00 114.26 ? 703  ALA A CA    1 
ATOM   5022  C  C     . ALA A 1 703 ? 95.822  150.978 127.246 1.00 117.99 ? 703  ALA A C     1 
ATOM   5023  O  O     . ALA A 1 703 ? 94.832  151.535 127.735 1.00 120.29 ? 703  ALA A O     1 
ATOM   5024  C  CB    . ALA A 1 703 ? 96.797  152.044 125.196 1.00 115.30 ? 703  ALA A CB    1 
ATOM   5025  N  N     . LEU A 1 704 ? 95.930  149.649 127.175 1.00 114.76 ? 704  LEU A N     1 
ATOM   5026  C  CA    . LEU A 1 704 ? 94.897  148.797 127.755 1.00 110.91 ? 704  LEU A CA    1 
ATOM   5027  C  C     . LEU A 1 704 ? 94.814  148.992 129.262 1.00 114.26 ? 704  LEU A C     1 
ATOM   5028  O  O     . LEU A 1 704 ? 93.718  149.089 129.825 1.00 119.81 ? 704  LEU A O     1 
ATOM   5029  C  CB    . LEU A 1 704 ? 95.178  147.334 127.417 1.00 107.98 ? 704  LEU A CB    1 
ATOM   5030  C  CG    . LEU A 1 704 ? 94.129  146.289 127.801 1.00 110.39 ? 704  LEU A CG    1 
ATOM   5031  C  CD1   . LEU A 1 704 ? 92.722  146.865 127.758 1.00 112.49 ? 704  LEU A CD1   1 
ATOM   5032  C  CD2   . LEU A 1 704 ? 94.238  145.078 126.900 1.00 109.25 ? 704  LEU A CD2   1 
ATOM   5033  N  N     . HIS A 1 705 ? 95.961  149.071 129.930 1.00 114.28 ? 705  HIS A N     1 
ATOM   5034  C  CA    . HIS A 1 705 ? 95.994  149.268 131.372 1.00 116.41 ? 705  HIS A CA    1 
ATOM   5035  C  C     . HIS A 1 705 ? 95.768  150.717 131.776 1.00 119.60 ? 705  HIS A C     1 
ATOM   5036  O  O     . HIS A 1 705 ? 95.687  151.006 132.974 1.00 118.67 ? 705  HIS A O     1 
ATOM   5037  C  CB    . HIS A 1 705 ? 97.323  148.774 131.946 1.00 114.01 ? 705  HIS A CB    1 
ATOM   5038  C  CG    . HIS A 1 705 ? 97.362  147.298 132.185 1.00 115.51 ? 705  HIS A CG    1 
ATOM   5039  N  ND1   . HIS A 1 705 ? 98.348  146.690 132.929 1.00 118.33 ? 705  HIS A ND1   1 
ATOM   5040  C  CD2   . HIS A 1 705 ? 96.532  146.308 131.780 1.00 112.87 ? 705  HIS A CD2   1 
ATOM   5041  C  CE1   . HIS A 1 705 ? 98.126  145.389 132.972 1.00 115.34 ? 705  HIS A CE1   1 
ATOM   5042  N  NE2   . HIS A 1 705 ? 97.030  145.131 132.282 1.00 111.97 ? 705  HIS A NE2   1 
ATOM   5043  N  N     . GLY A 1 706 ? 95.673  151.631 130.815 1.00 122.97 ? 706  GLY A N     1 
ATOM   5044  C  CA    . GLY A 1 706 ? 95.360  153.011 131.109 1.00 124.33 ? 706  GLY A CA    1 
ATOM   5045  C  C     . GLY A 1 706 ? 96.546  153.885 131.439 1.00 125.09 ? 706  GLY A C     1 
ATOM   5046  O  O     . GLY A 1 706 ? 96.377  155.103 131.573 1.00 128.43 ? 706  GLY A O     1 
ATOM   5047  N  N     . GLU A 1 707 ? 97.738  153.311 131.581 1.00 122.40 ? 707  GLU A N     1 
ATOM   5048  C  CA    . GLU A 1 707 ? 98.941  154.082 131.876 1.00 124.70 ? 707  GLU A CA    1 
ATOM   5049  C  C     . GLU A 1 707 ? 99.909  153.914 130.702 1.00 125.52 ? 707  GLU A C     1 
ATOM   5050  O  O     . GLU A 1 707 ? 100.633 152.930 130.569 1.00 123.16 ? 707  GLU A O     1 
ATOM   5051  C  CB    . GLU A 1 707 ? 99.499  153.677 133.250 1.00 121.35 ? 707  GLU A CB    1 
ATOM   5052  C  CG    . GLU A 1 707 ? 100.591 152.627 133.336 1.00 122.35 ? 707  GLU A CG    1 
ATOM   5053  C  CD    . GLU A 1 707 ? 101.046 152.397 134.758 1.00 130.09 ? 707  GLU A CD    1 
ATOM   5054  O  OE1   . GLU A 1 707 ? 100.932 151.252 135.242 1.00 128.48 ? 707  GLU A OE1   1 
ATOM   5055  O  OE2   . GLU A 1 707 ? 101.492 153.368 135.400 1.00 131.60 ? 707  GLU A OE2   1 
ATOM   5056  N  N     . VAL A 1 708 ? 99.850  154.880 129.790 1.00 125.25 ? 708  VAL A N     1 
ATOM   5057  C  CA    . VAL A 1 708 ? 100.649 154.863 128.576 1.00 120.91 ? 708  VAL A CA    1 
ATOM   5058  C  C     . VAL A 1 708 ? 101.600 156.052 128.512 1.00 120.96 ? 708  VAL A C     1 
ATOM   5059  O  O     . VAL A 1 708 ? 102.570 156.031 127.752 1.00 121.81 ? 708  VAL A O     1 
ATOM   5060  C  CB    . VAL A 1 708 ? 99.742  154.811 127.326 1.00 121.19 ? 708  VAL A CB    1 
ATOM   5061  C  CG1   . VAL A 1 708 ? 99.081  156.159 127.087 1.00 130.56 ? 708  VAL A CG1   1 
ATOM   5062  C  CG2   . VAL A 1 708 ? 100.528 154.362 126.106 1.00 117.16 ? 708  VAL A CG2   1 
ATOM   5063  N  N     . HIS A 1 709 ? 101.336 157.098 129.299 1.00 120.50 ? 709  HIS A N     1 
ATOM   5064  C  CA    . HIS A 1 709 ? 102.218 158.260 129.307 1.00 125.07 ? 709  HIS A CA    1 
ATOM   5065  C  C     . HIS A 1 709 ? 103.617 157.895 129.780 1.00 127.04 ? 709  HIS A C     1 
ATOM   5066  O  O     . HIS A 1 709 ? 104.607 158.438 129.275 1.00 129.00 ? 709  HIS A O     1 
ATOM   5067  C  CB    . HIS A 1 709 ? 101.633 159.361 130.190 1.00 129.16 ? 709  HIS A CB    1 
ATOM   5068  C  CG    . HIS A 1 709 ? 100.875 158.848 131.375 1.00 132.80 ? 709  HIS A CG    1 
ATOM   5069  N  ND1   . HIS A 1 709 ? 99.544  158.497 131.311 1.00 132.86 ? 709  HIS A ND1   1 
ATOM   5070  C  CD2   . HIS A 1 709 ? 101.261 158.626 132.653 1.00 133.43 ? 709  HIS A CD2   1 
ATOM   5071  C  CE1   . HIS A 1 709 ? 99.142  158.083 132.499 1.00 133.24 ? 709  HIS A CE1   1 
ATOM   5072  N  NE2   . HIS A 1 709 ? 100.166 158.151 133.331 1.00 134.33 ? 709  HIS A NE2   1 
ATOM   5073  N  N     . HIS A 1 710 ? 103.717 156.978 130.744 1.00 123.78 ? 710  HIS A N     1 
ATOM   5074  C  CA    . HIS A 1 710 ? 105.023 156.566 131.244 1.00 121.15 ? 710  HIS A CA    1 
ATOM   5075  C  C     . HIS A 1 710 ? 105.867 155.972 130.124 1.00 121.47 ? 710  HIS A C     1 
ATOM   5076  O  O     . HIS A 1 710 ? 107.027 156.360 129.931 1.00 124.37 ? 710  HIS A O     1 
ATOM   5077  C  CB    . HIS A 1 710 ? 104.844 155.552 132.371 1.00 115.63 ? 710  HIS A CB    1 
ATOM   5078  C  CG    . HIS A 1 710 ? 104.230 156.128 133.609 1.00 124.82 ? 710  HIS A CG    1 
ATOM   5079  N  ND1   . HIS A 1 710 ? 104.715 157.260 134.225 1.00 132.61 ? 710  HIS A ND1   1 
ATOM   5080  C  CD2   . HIS A 1 710 ? 103.164 155.728 134.341 1.00 125.97 ? 710  HIS A CD2   1 
ATOM   5081  C  CE1   . HIS A 1 710 ? 103.976 157.532 135.286 1.00 133.88 ? 710  HIS A CE1   1 
ATOM   5082  N  NE2   . HIS A 1 710 ? 103.028 156.617 135.379 1.00 128.78 ? 710  HIS A NE2   1 
ATOM   5083  N  N     . ILE A 1 711 ? 105.288 155.048 129.357 1.00 116.66 ? 711  ILE A N     1 
ATOM   5084  C  CA    . ILE A 1 711 ? 106.005 154.434 128.244 1.00 113.10 ? 711  ILE A CA    1 
ATOM   5085  C  C     . ILE A 1 711 ? 106.297 155.471 127.166 1.00 115.79 ? 711  ILE A C     1 
ATOM   5086  O  O     . ILE A 1 711 ? 107.400 155.517 126.610 1.00 115.51 ? 711  ILE A O     1 
ATOM   5087  C  CB    . ILE A 1 711 ? 105.203 153.246 127.687 1.00 111.39 ? 711  ILE A CB    1 
ATOM   5088  C  CG1   . ILE A 1 711 ? 104.867 152.266 128.811 1.00 106.17 ? 711  ILE A CG1   1 
ATOM   5089  C  CG2   . ILE A 1 711 ? 105.973 152.554 126.585 1.00 111.56 ? 711  ILE A CG2   1 
ATOM   5090  C  CD1   . ILE A 1 711 ? 106.067 151.767 129.566 1.00 103.07 ? 711  ILE A CD1   1 
ATOM   5091  N  N     . PHE A 1 712 ? 105.313 156.323 126.861 1.00 118.33 ? 712  PHE A N     1 
ATOM   5092  C  CA    . PHE A 1 712 ? 105.509 157.360 125.852 1.00 117.30 ? 712  PHE A CA    1 
ATOM   5093  C  C     . PHE A 1 712 ? 106.707 158.238 126.179 1.00 119.13 ? 712  PHE A C     1 
ATOM   5094  O  O     . PHE A 1 712 ? 107.452 158.644 125.280 1.00 124.69 ? 712  PHE A O     1 
ATOM   5095  C  CB    . PHE A 1 712 ? 104.250 158.218 125.720 1.00 122.58 ? 712  PHE A CB    1 
ATOM   5096  C  CG    . PHE A 1 712 ? 103.337 157.799 124.604 1.00 129.16 ? 712  PHE A CG    1 
ATOM   5097  C  CD1   . PHE A 1 712 ? 103.619 156.684 123.836 1.00 128.17 ? 712  PHE A CD1   1 
ATOM   5098  C  CD2   . PHE A 1 712 ? 102.196 158.531 124.318 1.00 134.87 ? 712  PHE A CD2   1 
ATOM   5099  C  CE1   . PHE A 1 712 ? 102.778 156.305 122.807 1.00 134.24 ? 712  PHE A CE1   1 
ATOM   5100  C  CE2   . PHE A 1 712 ? 101.352 158.156 123.291 1.00 140.24 ? 712  PHE A CE2   1 
ATOM   5101  C  CZ    . PHE A 1 712 ? 101.644 157.041 122.535 1.00 141.18 ? 712  PHE A CZ    1 
ATOM   5102  N  N     . MET A 1 713 ? 106.912 158.545 127.461 1.00 117.97 ? 713  MET A N     1 
ATOM   5103  C  CA    . MET A 1 713 ? 108.013 159.434 127.817 1.00 120.30 ? 713  MET A CA    1 
ATOM   5104  C  C     . MET A 1 713 ? 109.323 158.677 128.002 1.00 118.60 ? 713  MET A C     1 
ATOM   5105  O  O     . MET A 1 713 ? 110.402 159.261 127.852 1.00 122.52 ? 713  MET A O     1 
ATOM   5106  C  CB    . MET A 1 713 ? 107.676 160.223 129.080 1.00 122.17 ? 713  MET A CB    1 
ATOM   5107  C  CG    . MET A 1 713 ? 106.428 161.076 128.975 1.00 130.90 ? 713  MET A CG    1 
ATOM   5108  S  SD    . MET A 1 713 ? 106.197 162.085 130.448 1.00 161.82 ? 713  MET A SD    1 
ATOM   5109  C  CE    . MET A 1 713 ? 106.893 161.009 131.699 1.00 143.17 ? 713  MET A CE    1 
ATOM   5110  N  N     . THR A 1 714 ? 109.263 157.386 128.328 1.00 114.31 ? 714  THR A N     1 
ATOM   5111  C  CA    . THR A 1 714 ? 110.462 156.673 128.745 1.00 110.08 ? 714  THR A CA    1 
ATOM   5112  C  C     . THR A 1 714 ? 110.953 155.635 127.737 1.00 111.20 ? 714  THR A C     1 
ATOM   5113  O  O     . THR A 1 714 ? 111.943 154.938 128.010 1.00 109.02 ? 714  THR A O     1 
ATOM   5114  C  CB    . THR A 1 714 ? 110.201 156.011 130.099 1.00 105.54 ? 714  THR A CB    1 
ATOM   5115  O  OG1   . THR A 1 714 ? 109.415 156.896 130.903 1.00 113.49 ? 714  THR A OG1   1 
ATOM   5116  C  CG2   . THR A 1 714 ? 111.492 155.808 130.811 1.00 106.09 ? 714  THR A CG2   1 
ATOM   5117  N  N     . PHE A 1 715 ? 110.300 155.515 126.578 1.00 115.23 ? 715  PHE A N     1 
ATOM   5118  C  CA    . PHE A 1 715 ? 110.752 154.547 125.584 1.00 111.82 ? 715  PHE A CA    1 
ATOM   5119  C  C     . PHE A 1 715 ? 112.190 154.809 125.159 1.00 112.00 ? 715  PHE A C     1 
ATOM   5120  O  O     . PHE A 1 715 ? 113.011 153.887 125.136 1.00 112.57 ? 715  PHE A O     1 
ATOM   5121  C  CB    . PHE A 1 715 ? 109.827 154.570 124.369 1.00 114.47 ? 715  PHE A CB    1 
ATOM   5122  C  CG    . PHE A 1 715 ? 110.124 153.495 123.367 1.00 120.94 ? 715  PHE A CG    1 
ATOM   5123  C  CD1   . PHE A 1 715 ? 109.820 152.172 123.643 1.00 119.49 ? 715  PHE A CD1   1 
ATOM   5124  C  CD2   . PHE A 1 715 ? 110.707 153.803 122.151 1.00 124.67 ? 715  PHE A CD2   1 
ATOM   5125  C  CE1   . PHE A 1 715 ? 110.094 151.176 122.726 1.00 117.82 ? 715  PHE A CE1   1 
ATOM   5126  C  CE2   . PHE A 1 715 ? 110.982 152.811 121.228 1.00 126.52 ? 715  PHE A CE2   1 
ATOM   5127  C  CZ    . PHE A 1 715 ? 110.675 151.495 121.517 1.00 123.68 ? 715  PHE A CZ    1 
ATOM   5128  N  N     . THR A 1 716 ? 112.515 156.059 124.822 1.00 112.07 ? 716  THR A N     1 
ATOM   5129  C  CA    . THR A 1 716 ? 113.872 156.377 124.384 1.00 112.27 ? 716  THR A CA    1 
ATOM   5130  C  C     . THR A 1 716 ? 114.882 156.162 125.505 1.00 110.20 ? 716  THR A C     1 
ATOM   5131  O  O     . THR A 1 716 ? 115.977 155.630 125.272 1.00 110.63 ? 716  THR A O     1 
ATOM   5132  C  CB    . THR A 1 716 ? 113.933 157.815 123.872 1.00 110.41 ? 716  THR A CB    1 
ATOM   5133  O  OG1   . THR A 1 716 ? 115.298 158.247 123.819 1.00 111.26 ? 716  THR A OG1   1 
ATOM   5134  C  CG2   . THR A 1 716 ? 113.140 158.745 124.777 1.00 107.24 ? 716  THR A CG2   1 
ATOM   5135  N  N     . HIS A 1 717 ? 114.528 156.560 126.730 1.00 110.30 ? 717  HIS A N     1 
ATOM   5136  C  CA    . HIS A 1 717 ? 115.443 156.409 127.856 1.00 109.53 ? 717  HIS A CA    1 
ATOM   5137  C  C     . HIS A 1 717 ? 115.775 154.947 128.108 1.00 108.30 ? 717  HIS A C     1 
ATOM   5138  O  O     . HIS A 1 717 ? 116.923 154.611 128.418 1.00 111.65 ? 717  HIS A O     1 
ATOM   5139  C  CB    . HIS A 1 717 ? 114.847 157.041 129.113 1.00 112.99 ? 717  HIS A CB    1 
ATOM   5140  C  CG    . HIS A 1 717 ? 114.637 158.519 129.009 1.00 119.39 ? 717  HIS A CG    1 
ATOM   5141  N  ND1   . HIS A 1 717 ? 115.554 159.433 129.481 1.00 121.39 ? 717  HIS A ND1   1 
ATOM   5142  C  CD2   . HIS A 1 717 ? 113.617 159.242 128.491 1.00 121.12 ? 717  HIS A CD2   1 
ATOM   5143  C  CE1   . HIS A 1 717 ? 115.108 160.655 129.257 1.00 125.62 ? 717  HIS A CE1   1 
ATOM   5144  N  NE2   . HIS A 1 717 ? 113.935 160.567 128.657 1.00 122.46 ? 717  HIS A NE2   1 
ATOM   5145  N  N     . TYR A 1 718 ? 114.785 154.059 127.992 1.00 107.19 ? 718  TYR A N     1 
ATOM   5146  C  CA    . TYR A 1 718 ? 115.078 152.642 128.183 1.00 105.34 ? 718  TYR A CA    1 
ATOM   5147  C  C     . TYR A 1 718 ? 115.802 152.059 126.977 1.00 107.43 ? 718  TYR A C     1 
ATOM   5148  O  O     . TYR A 1 718 ? 116.645 151.169 127.126 1.00 106.97 ? 718  TYR A O     1 
ATOM   5149  C  CB    . TYR A 1 718 ? 113.803 151.854 128.456 1.00 104.26 ? 718  TYR A CB    1 
ATOM   5150  C  CG    . TYR A 1 718 ? 114.046 150.367 128.604 1.00 98.31  ? 718  TYR A CG    1 
ATOM   5151  C  CD1   . TYR A 1 718 ? 114.663 149.860 129.736 1.00 102.89 ? 718  TYR A CD1   1 
ATOM   5152  C  CD2   . TYR A 1 718 ? 113.663 149.474 127.613 1.00 98.62  ? 718  TYR A CD2   1 
ATOM   5153  C  CE1   . TYR A 1 718 ? 114.888 148.508 129.882 1.00 106.71 ? 718  TYR A CE1   1 
ATOM   5154  C  CE2   . TYR A 1 718 ? 113.883 148.118 127.752 1.00 102.26 ? 718  TYR A CE2   1 
ATOM   5155  C  CZ    . TYR A 1 718 ? 114.497 147.642 128.889 1.00 109.38 ? 718  TYR A CZ    1 
ATOM   5156  O  OH    . TYR A 1 718 ? 114.724 146.295 129.037 1.00 119.91 ? 718  TYR A OH    1 
ATOM   5157  N  N     . THR A 1 719 ? 115.480 152.540 125.774 1.00 109.32 ? 719  THR A N     1 
ATOM   5158  C  CA    . THR A 1 719 ? 116.132 152.028 124.575 1.00 108.03 ? 719  THR A CA    1 
ATOM   5159  C  C     . THR A 1 719 ? 117.624 152.322 124.606 1.00 111.78 ? 719  THR A C     1 
ATOM   5160  O  O     . THR A 1 719 ? 118.439 151.499 124.175 1.00 114.04 ? 719  THR A O     1 
ATOM   5161  C  CB    . THR A 1 719 ? 115.478 152.633 123.332 1.00 109.74 ? 719  THR A CB    1 
ATOM   5162  O  OG1   . THR A 1 719 ? 114.277 151.912 123.034 1.00 118.01 ? 719  THR A OG1   1 
ATOM   5163  C  CG2   . THR A 1 719 ? 116.405 152.545 122.131 1.00 110.92 ? 719  THR A CG2   1 
ATOM   5164  N  N     . ALA A 1 720 ? 118.005 153.478 125.151 1.00 114.20 ? 720  ALA A N     1 
ATOM   5165  C  CA    . ALA A 1 720 ? 119.421 153.797 125.270 1.00 111.47 ? 720  ALA A CA    1 
ATOM   5166  C  C     . ALA A 1 720 ? 120.162 152.870 126.219 1.00 107.26 ? 720  ALA A C     1 
ATOM   5167  O  O     . ALA A 1 720 ? 121.396 152.826 126.174 1.00 111.44 ? 720  ALA A O     1 
ATOM   5168  C  CB    . ALA A 1 720 ? 119.598 155.232 125.752 1.00 115.86 ? 720  ALA A CB    1 
ATOM   5169  N  N     . LEU A 1 721 ? 119.450 152.121 127.058 1.00 105.73 ? 721  LEU A N     1 
ATOM   5170  C  CA    . LEU A 1 721 ? 120.081 151.337 128.108 1.00 107.83 ? 721  LEU A CA    1 
ATOM   5171  C  C     . LEU A 1 721 ? 119.856 149.840 127.939 1.00 107.79 ? 721  LEU A C     1 
ATOM   5172  O  O     . LEU A 1 721 ? 120.225 149.071 128.828 1.00 109.53 ? 721  LEU A O     1 
ATOM   5173  C  CB    . LEU A 1 721 ? 119.570 151.793 129.480 1.00 106.38 ? 721  LEU A CB    1 
ATOM   5174  C  CG    . LEU A 1 721 ? 120.594 151.806 130.615 1.00 105.15 ? 721  LEU A CG    1 
ATOM   5175  C  CD1   . LEU A 1 721 ? 121.950 152.236 130.091 1.00 106.46 ? 721  LEU A CD1   1 
ATOM   5176  C  CD2   . LEU A 1 721 ? 120.148 152.711 131.744 1.00 108.87 ? 721  LEU A CD2   1 
ATOM   5177  N  N     . ILE A 1 722 ? 119.265 149.406 126.830 1.00 105.50 ? 722  ILE A N     1 
ATOM   5178  C  CA    . ILE A 1 722 ? 119.036 147.984 126.574 1.00 103.54 ? 722  ILE A CA    1 
ATOM   5179  C  C     . ILE A 1 722 ? 120.352 147.208 126.531 1.00 106.91 ? 722  ILE A C     1 
ATOM   5180  O  O     . ILE A 1 722 ? 120.470 146.180 127.216 1.00 111.37 ? 722  ILE A O     1 
ATOM   5181  C  CB    . ILE A 1 722 ? 118.239 147.774 125.275 1.00 105.25 ? 722  ILE A CB    1 
ATOM   5182  C  CG1   . ILE A 1 722 ? 116.757 148.067 125.500 1.00 110.94 ? 722  ILE A CG1   1 
ATOM   5183  C  CG2   . ILE A 1 722 ? 118.425 146.361 124.763 1.00 101.02 ? 722  ILE A CG2   1 
ATOM   5184  C  CD1   . ILE A 1 722 ? 115.851 147.491 124.436 1.00 116.47 ? 722  ILE A CD1   1 
ATOM   5185  N  N     . PRO A 1 723 ? 121.361 147.636 125.757 1.00 109.29 ? 723  PRO A N     1 
ATOM   5186  C  CA    . PRO A 1 723 ? 122.583 146.823 125.684 1.00 109.22 ? 723  PRO A CA    1 
ATOM   5187  C  C     . PRO A 1 723 ? 123.382 146.867 126.963 1.00 110.66 ? 723  PRO A C     1 
ATOM   5188  O  O     . PRO A 1 723 ? 123.924 145.838 127.382 1.00 114.02 ? 723  PRO A O     1 
ATOM   5189  C  CB    . PRO A 1 723 ? 123.357 147.453 124.522 1.00 108.65 ? 723  PRO A CB    1 
ATOM   5190  C  CG    . PRO A 1 723 ? 122.940 148.848 124.548 1.00 112.80 ? 723  PRO A CG    1 
ATOM   5191  C  CD    . PRO A 1 723 ? 121.491 148.848 124.932 1.00 113.84 ? 723  PRO A CD    1 
ATOM   5192  N  N     . SER A 1 724 ? 123.487 148.039 127.588 1.00 107.96 ? 724  SER A N     1 
ATOM   5193  C  CA    . SER A 1 724 ? 124.122 148.110 128.895 1.00 111.38 ? 724  SER A CA    1 
ATOM   5194  C  C     . SER A 1 724 ? 123.437 147.163 129.864 1.00 108.33 ? 724  SER A C     1 
ATOM   5195  O  O     . SER A 1 724 ? 124.094 146.333 130.499 1.00 108.02 ? 724  SER A O     1 
ATOM   5196  C  CB    . SER A 1 724 ? 124.092 149.541 129.423 1.00 114.46 ? 724  SER A CB    1 
ATOM   5197  O  OG    . SER A 1 724 ? 124.287 149.558 130.824 1.00 115.84 ? 724  SER A OG    1 
ATOM   5198  N  N     . PHE A 1 725 ? 122.108 147.227 129.934 1.00 108.11 ? 725  PHE A N     1 
ATOM   5199  C  CA    . PHE A 1 725 ? 121.323 146.323 130.761 1.00 106.58 ? 725  PHE A CA    1 
ATOM   5200  C  C     . PHE A 1 725 ? 121.748 144.885 130.529 1.00 104.32 ? 725  PHE A C     1 
ATOM   5201  O  O     . PHE A 1 725 ? 122.394 144.285 131.394 1.00 109.82 ? 725  PHE A O     1 
ATOM   5202  C  CB    . PHE A 1 725 ? 119.832 146.471 130.451 1.00 106.48 ? 725  PHE A CB    1 
ATOM   5203  C  CG    . PHE A 1 725 ? 119.053 147.173 131.521 1.00 109.58 ? 725  PHE A CG    1 
ATOM   5204  C  CD1   . PHE A 1 725 ? 119.049 148.552 131.606 1.00 109.83 ? 725  PHE A CD1   1 
ATOM   5205  C  CD2   . PHE A 1 725 ? 118.316 146.449 132.437 1.00 111.45 ? 725  PHE A CD2   1 
ATOM   5206  C  CE1   . PHE A 1 725 ? 118.330 149.196 132.587 1.00 105.94 ? 725  PHE A CE1   1 
ATOM   5207  C  CE2   . PHE A 1 725 ? 117.597 147.087 133.420 1.00 114.56 ? 725  PHE A CE2   1 
ATOM   5208  C  CZ    . PHE A 1 725 ? 117.603 148.462 133.495 1.00 112.33 ? 725  PHE A CZ    1 
ATOM   5209  N  N     . VAL A 1 726 ? 121.384 144.337 129.375 1.00 104.65 ? 726  VAL A N     1 
ATOM   5210  C  CA    . VAL A 1 726 ? 121.686 142.949 129.031 1.00 105.53 ? 726  VAL A CA    1 
ATOM   5211  C  C     . VAL A 1 726 ? 123.140 142.502 129.208 1.00 109.81 ? 726  VAL A C     1 
ATOM   5212  O  O     . VAL A 1 726 ? 123.414 141.543 129.928 1.00 115.30 ? 726  VAL A O     1 
ATOM   5213  C  CB    . VAL A 1 726 ? 121.250 142.628 127.587 1.00 99.67  ? 726  VAL A CB    1 
ATOM   5214  C  CG1   . VAL A 1 726 ? 121.726 143.716 126.636 1.00 97.90  ? 726  VAL A CG1   1 
ATOM   5215  C  CG2   . VAL A 1 726 ? 121.783 141.268 127.162 1.00 101.46 ? 726  VAL A CG2   1 
ATOM   5216  N  N     . ASN A 1 727 ? 124.066 143.194 128.552 1.00 108.20 ? 727  ASN A N     1 
ATOM   5217  C  CA    . ASN A 1 727 ? 125.473 142.818 128.603 1.00 107.23 ? 727  ASN A CA    1 
ATOM   5218  C  C     . ASN A 1 727 ? 126.051 143.003 130.001 1.00 111.38 ? 727  ASN A C     1 
ATOM   5219  O  O     . ASN A 1 727 ? 126.473 142.034 130.642 1.00 116.67 ? 727  ASN A O     1 
ATOM   5220  C  CB    . ASN A 1 727 ? 126.258 143.634 127.577 1.00 107.63 ? 727  ASN A CB    1 
ATOM   5221  C  CG    . ASN A 1 727 ? 126.337 142.950 126.231 1.00 112.76 ? 727  ASN A CG    1 
ATOM   5222  O  OD1   . ASN A 1 727 ? 126.464 141.730 126.151 1.00 119.02 ? 727  ASN A OD1   1 
ATOM   5223  N  ND2   . ASN A 1 727 ? 126.254 143.732 125.164 1.00 107.94 ? 727  ASN A ND2   1 
ATOM   5224  N  N     . ILE A 1 728 ? 126.083 144.247 130.492 1.00 108.02 ? 728  ILE A N     1 
ATOM   5225  C  CA    . ILE A 1 728 ? 126.782 144.537 131.739 1.00 104.82 ? 728  ILE A CA    1 
ATOM   5226  C  C     . ILE A 1 728 ? 126.144 143.785 132.898 1.00 109.88 ? 728  ILE A C     1 
ATOM   5227  O  O     . ILE A 1 728 ? 126.838 143.161 133.711 1.00 115.04 ? 728  ILE A O     1 
ATOM   5228  C  CB    . ILE A 1 728 ? 126.793 146.052 132.008 1.00 103.89 ? 728  ILE A CB    1 
ATOM   5229  C  CG1   . ILE A 1 728 ? 127.352 146.814 130.810 1.00 107.29 ? 728  ILE A CG1   1 
ATOM   5230  C  CG2   . ILE A 1 728 ? 127.610 146.356 133.245 1.00 105.31 ? 728  ILE A CG2   1 
ATOM   5231  C  CD1   . ILE A 1 728 ? 127.479 148.301 131.041 1.00 115.17 ? 728  ILE A CD1   1 
ATOM   5232  N  N     . PHE A 1 729 ? 124.812 143.850 133.011 1.00 111.64 ? 729  PHE A N     1 
ATOM   5233  C  CA    . PHE A 1 729 ? 124.156 143.288 134.180 1.00 110.22 ? 729  PHE A CA    1 
ATOM   5234  C  C     . PHE A 1 729 ? 124.272 141.770 134.197 1.00 115.28 ? 729  PHE A C     1 
ATOM   5235  O  O     . PHE A 1 729 ? 124.558 141.185 135.246 1.00 123.92 ? 729  PHE A O     1 
ATOM   5236  C  CB    . PHE A 1 729 ? 122.693 143.727 134.212 1.00 109.92 ? 729  PHE A CB    1 
ATOM   5237  C  CG    . PHE A 1 729 ? 122.499 145.214 134.367 1.00 109.85 ? 729  PHE A CG    1 
ATOM   5238  C  CD1   . PHE A 1 729 ? 123.580 146.069 134.490 1.00 108.96 ? 729  PHE A CD1   1 
ATOM   5239  C  CD2   . PHE A 1 729 ? 121.230 145.757 134.358 1.00 113.63 ? 729  PHE A CD2   1 
ATOM   5240  C  CE1   . PHE A 1 729 ? 123.396 147.426 134.618 1.00 111.73 ? 729  PHE A CE1   1 
ATOM   5241  C  CE2   . PHE A 1 729 ? 121.042 147.115 134.487 1.00 113.92 ? 729  PHE A CE2   1 
ATOM   5242  C  CZ    . PHE A 1 729 ? 122.128 147.949 134.616 1.00 112.72 ? 729  PHE A CZ    1 
ATOM   5243  N  N     . THR A 1 730 ? 124.110 141.147 133.034 1.00 110.16 ? 730  THR A N     1 
ATOM   5244  C  CA    . THR A 1 730 ? 124.220 139.699 132.921 1.00 113.14 ? 730  THR A CA    1 
ATOM   5245  C  C     . THR A 1 730 ? 125.649 139.230 133.196 1.00 117.32 ? 730  THR A C     1 
ATOM   5246  O  O     . THR A 1 730 ? 125.857 138.188 133.818 1.00 121.22 ? 730  THR A O     1 
ATOM   5247  C  CB    . THR A 1 730 ? 123.786 139.206 131.528 1.00 115.18 ? 730  THR A CB    1 
ATOM   5248  O  OG1   . THR A 1 730 ? 122.378 138.938 131.530 1.00 118.29 ? 730  THR A OG1   1 
ATOM   5249  C  CG2   . THR A 1 730 ? 124.538 137.939 131.153 1.00 110.34 ? 730  THR A CG2   1 
ATOM   5250  N  N     . ILE A 1 731 ? 126.630 140.000 132.731 1.00 114.91 ? 731  ILE A N     1 
ATOM   5251  C  CA    . ILE A 1 731 ? 128.031 139.651 132.935 1.00 117.08 ? 731  ILE A CA    1 
ATOM   5252  C  C     . ILE A 1 731 ? 128.392 139.749 134.410 1.00 124.80 ? 731  ILE A C     1 
ATOM   5253  O  O     . ILE A 1 731 ? 129.005 138.837 134.973 1.00 129.26 ? 731  ILE A O     1 
ATOM   5254  C  CB    . ILE A 1 731 ? 128.937 140.541 132.065 1.00 116.99 ? 731  ILE A CB    1 
ATOM   5255  C  CG1   . ILE A 1 731 ? 129.120 139.914 130.683 1.00 117.70 ? 731  ILE A CG1   1 
ATOM   5256  C  CG2   . ILE A 1 731 ? 130.289 140.738 132.727 1.00 116.71 ? 731  ILE A CG2   1 
ATOM   5257  C  CD1   . ILE A 1 731 ? 129.893 140.778 129.719 1.00 114.73 ? 731  ILE A CD1   1 
ATOM   5258  N  N     . TYR A 1 732 ? 127.997 140.843 135.066 1.00 128.46 ? 732  TYR A N     1 
ATOM   5259  C  CA    . TYR A 1 732 ? 128.270 140.973 136.494 1.00 129.14 ? 732  TYR A CA    1 
ATOM   5260  C  C     . TYR A 1 732 ? 127.532 139.920 137.315 1.00 128.94 ? 732  TYR A C     1 
ATOM   5261  O  O     . TYR A 1 732 ? 128.107 139.346 138.247 1.00 130.70 ? 732  TYR A O     1 
ATOM   5262  C  CB    . TYR A 1 732 ? 127.928 142.381 136.981 1.00 121.12 ? 732  TYR A CB    1 
ATOM   5263  C  CG    . TYR A 1 732 ? 128.591 142.706 138.297 1.00 126.55 ? 732  TYR A CG    1 
ATOM   5264  C  CD1   . TYR A 1 732 ? 129.946 142.494 138.490 1.00 131.36 ? 732  TYR A CD1   1 
ATOM   5265  C  CD2   . TYR A 1 732 ? 127.853 143.209 139.355 1.00 131.26 ? 732  TYR A CD2   1 
ATOM   5266  C  CE1   . TYR A 1 732 ? 130.545 142.775 139.703 1.00 133.07 ? 732  TYR A CE1   1 
ATOM   5267  C  CE2   . TYR A 1 732 ? 128.442 143.495 140.567 1.00 130.12 ? 732  TYR A CE2   1 
ATOM   5268  C  CZ    . TYR A 1 732 ? 129.787 143.276 140.737 1.00 130.44 ? 732  TYR A CZ    1 
ATOM   5269  O  OH    . TYR A 1 732 ? 130.370 143.560 141.949 1.00 130.17 ? 732  TYR A OH    1 
ATOM   5270  N  N     . SER A 1 733 ? 126.264 139.651 136.994 1.00 124.44 ? 733  SER A N     1 
ATOM   5271  C  CA    . SER A 1 733 ? 125.498 138.688 137.779 1.00 128.90 ? 733  SER A CA    1 
ATOM   5272  C  C     . SER A 1 733 ? 126.079 137.285 137.665 1.00 133.76 ? 733  SER A C     1 
ATOM   5273  O  O     . SER A 1 733 ? 126.317 136.621 138.680 1.00 141.04 ? 733  SER A O     1 
ATOM   5274  C  CB    . SER A 1 733 ? 124.036 138.695 137.335 1.00 131.32 ? 733  SER A CB    1 
ATOM   5275  O  OG    . SER A 1 733 ? 123.409 137.462 137.638 1.00 136.15 ? 733  SER A OG    1 
ATOM   5276  N  N     . PHE A 1 734 ? 126.315 136.815 136.439 1.00 129.50 ? 734  PHE A N     1 
ATOM   5277  C  CA    . PHE A 1 734 ? 126.898 135.498 136.232 1.00 131.80 ? 734  PHE A CA    1 
ATOM   5278  C  C     . PHE A 1 734 ? 128.353 135.431 136.666 1.00 134.77 ? 734  PHE A C     1 
ATOM   5279  O  O     . PHE A 1 734 ? 128.860 134.335 136.927 1.00 135.08 ? 734  PHE A O     1 
ATOM   5280  C  CB    . PHE A 1 734 ? 126.802 135.103 134.760 1.00 125.77 ? 734  PHE A CB    1 
ATOM   5281  C  CG    . PHE A 1 734 ? 125.509 134.449 134.390 1.00 122.06 ? 734  PHE A CG    1 
ATOM   5282  C  CD1   . PHE A 1 734 ? 124.337 135.183 134.356 1.00 124.65 ? 734  PHE A CD1   1 
ATOM   5283  C  CD2   . PHE A 1 734 ? 125.463 133.106 134.072 1.00 120.87 ? 734  PHE A CD2   1 
ATOM   5284  C  CE1   . PHE A 1 734 ? 123.144 134.589 134.011 1.00 125.65 ? 734  PHE A CE1   1 
ATOM   5285  C  CE2   . PHE A 1 734 ? 124.272 132.506 133.727 1.00 123.41 ? 734  PHE A CE2   1 
ATOM   5286  C  CZ    . PHE A 1 734 ? 123.111 133.249 133.696 1.00 125.03 ? 734  PHE A CZ    1 
ATOM   5287  N  N     . CYS A 1 735 ? 129.027 136.572 136.752 1.00 135.85 ? 735  CYS A N     1 
ATOM   5288  C  CA    . CYS A 1 735 ? 130.451 136.620 137.035 1.00 136.05 ? 735  CYS A CA    1 
ATOM   5289  C  C     . CYS A 1 735 ? 130.760 136.579 138.527 1.00 138.87 ? 735  CYS A C     1 
ATOM   5290  O  O     . CYS A 1 735 ? 131.930 136.431 138.894 1.00 141.77 ? 735  CYS A O     1 
ATOM   5291  C  CB    . CYS A 1 735 ? 131.041 137.886 136.409 1.00 134.93 ? 735  CYS A CB    1 
ATOM   5292  S  SG    . CYS A 1 735 ? 131.849 137.621 134.813 1.00 148.69 ? 735  CYS A SG    1 
ATOM   5293  N  N     . ASN A 1 736 ? 129.753 136.710 139.387 1.00 136.73 ? 736  ASN A N     1 
ATOM   5294  C  CA    . ASN A 1 736 ? 129.912 136.716 140.840 1.00 142.01 ? 736  ASN A CA    1 
ATOM   5295  C  C     . ASN A 1 736 ? 128.948 135.730 141.486 1.00 147.13 ? 736  ASN A C     1 
ATOM   5296  O  O     . ASN A 1 736 ? 128.225 136.048 142.430 1.00 152.01 ? 736  ASN A O     1 
ATOM   5297  C  CB    . ASN A 1 736 ? 129.707 138.111 141.424 1.00 143.41 ? 736  ASN A CB    1 
ATOM   5298  C  CG    . ASN A 1 736 ? 130.902 139.015 141.208 1.00 139.71 ? 736  ASN A CG    1 
ATOM   5299  O  OD1   . ASN A 1 736 ? 131.554 138.958 140.168 1.00 138.92 ? 736  ASN A OD1   1 
ATOM   5300  N  ND2   . ASN A 1 736 ? 131.189 139.865 142.187 1.00 139.62 ? 736  ASN A ND2   1 
ATOM   5301  N  N     . LEU A 1 737 ? 128.918 134.507 140.970 1.00 144.68 ? 737  LEU A N     1 
ATOM   5302  C  CA    . LEU A 1 737 ? 128.090 133.473 141.571 1.00 145.61 ? 737  LEU A CA    1 
ATOM   5303  C  C     . LEU A 1 737 ? 128.625 132.990 142.907 1.00 152.51 ? 737  LEU A C     1 
ATOM   5304  O  O     . LEU A 1 737 ? 127.891 132.318 143.639 1.00 154.64 ? 737  LEU A O     1 
ATOM   5305  C  CB    . LEU A 1 737 ? 127.987 132.268 140.640 1.00 141.03 ? 737  LEU A CB    1 
ATOM   5306  C  CG    . LEU A 1 737 ? 126.994 132.234 139.477 1.00 142.63 ? 737  LEU A CG    1 
ATOM   5307  C  CD1   . LEU A 1 737 ? 126.946 130.838 138.822 1.00 142.26 ? 737  LEU A CD1   1 
ATOM   5308  C  CD2   . LEU A 1 737 ? 125.587 132.683 139.902 1.00 139.55 ? 737  LEU A CD2   1 
ATOM   5309  N  N     . LYS A 1 762 ? 138.713 122.315 186.492 1.00 175.46 ? 762  LYS A N     1 
ATOM   5310  C  CA    . LYS A 1 762 ? 139.822 121.877 187.332 1.00 180.90 ? 762  LYS A CA    1 
ATOM   5311  C  C     . LYS A 1 762 ? 140.684 120.837 186.624 1.00 180.22 ? 762  LYS A C     1 
ATOM   5312  O  O     . LYS A 1 762 ? 140.785 119.694 187.069 1.00 179.98 ? 762  LYS A O     1 
ATOM   5313  C  CB    . LYS A 1 762 ? 139.301 121.312 188.655 1.00 185.93 ? 762  LYS A CB    1 
ATOM   5314  C  CG    . LYS A 1 762 ? 138.586 122.331 189.525 1.00 189.20 ? 762  LYS A CG    1 
ATOM   5315  C  CD    . LYS A 1 762 ? 139.536 123.435 189.960 1.00 187.71 ? 762  LYS A CD    1 
ATOM   5316  C  CE    . LYS A 1 762 ? 138.845 124.439 190.866 1.00 191.53 ? 762  LYS A CE    1 
ATOM   5317  N  NZ    . LYS A 1 762 ? 139.780 125.504 191.321 1.00 192.15 ? 762  LYS A NZ    1 
ATOM   5318  N  N     . GLY A 1 763 ? 141.303 121.244 185.517 1.00 176.81 ? 763  GLY A N     1 
ATOM   5319  C  CA    . GLY A 1 763 ? 142.192 120.383 184.773 1.00 170.05 ? 763  GLY A CA    1 
ATOM   5320  C  C     . GLY A 1 763 ? 143.651 120.733 184.998 1.00 167.11 ? 763  GLY A C     1 
ATOM   5321  O  O     . GLY A 1 763 ? 144.003 121.878 185.271 1.00 165.21 ? 763  GLY A O     1 
ATOM   5322  N  N     . ASP A 1 764 ? 144.504 119.722 184.874 1.00 166.51 ? 764  ASP A N     1 
ATOM   5323  C  CA    . ASP A 1 764 ? 145.936 119.901 185.051 1.00 162.98 ? 764  ASP A CA    1 
ATOM   5324  C  C     . ASP A 1 764 ? 146.557 120.360 183.732 1.00 160.73 ? 764  ASP A C     1 
ATOM   5325  O  O     . ASP A 1 764 ? 145.857 120.663 182.761 1.00 161.43 ? 764  ASP A O     1 
ATOM   5326  C  CB    . ASP A 1 764 ? 146.571 118.613 185.568 1.00 163.54 ? 764  ASP A CB    1 
ATOM   5327  C  CG    . ASP A 1 764 ? 146.133 117.396 184.785 1.00 163.74 ? 764  ASP A CG    1 
ATOM   5328  O  OD1   . ASP A 1 764 ? 144.968 117.366 184.337 1.00 163.97 ? 764  ASP A OD1   1 
ATOM   5329  O  OD2   . ASP A 1 764 ? 146.953 116.469 184.617 1.00 163.31 ? 764  ASP A OD2   1 
ATOM   5330  N  N     . PHE A 1 765 ? 147.890 120.413 183.683 1.00 156.65 ? 765  PHE A N     1 
ATOM   5331  C  CA    . PHE A 1 765 ? 148.555 120.939 182.496 1.00 152.73 ? 765  PHE A CA    1 
ATOM   5332  C  C     . PHE A 1 765 ? 148.399 120.011 181.299 1.00 154.67 ? 765  PHE A C     1 
ATOM   5333  O  O     . PHE A 1 765 ? 148.349 120.475 180.155 1.00 155.50 ? 765  PHE A O     1 
ATOM   5334  C  CB    . PHE A 1 765 ? 150.029 121.208 182.777 1.00 145.34 ? 765  PHE A CB    1 
ATOM   5335  C  CG    . PHE A 1 765 ? 150.619 122.231 181.863 1.00 140.93 ? 765  PHE A CG    1 
ATOM   5336  C  CD1   . PHE A 1 765 ? 150.150 123.530 181.869 1.00 140.33 ? 765  PHE A CD1   1 
ATOM   5337  C  CD2   . PHE A 1 765 ? 151.623 121.889 180.978 1.00 141.33 ? 765  PHE A CD2   1 
ATOM   5338  C  CE1   . PHE A 1 765 ? 150.674 124.469 181.014 1.00 140.51 ? 765  PHE A CE1   1 
ATOM   5339  C  CE2   . PHE A 1 765 ? 152.157 122.827 180.124 1.00 139.96 ? 765  PHE A CE2   1 
ATOM   5340  C  CZ    . PHE A 1 765 ? 151.682 124.119 180.143 1.00 137.49 ? 765  PHE A CZ    1 
ATOM   5341  N  N     . LYS A 1 766 ? 148.337 118.699 181.531 1.00 155.80 ? 766  LYS A N     1 
ATOM   5342  C  CA    . LYS A 1 766 ? 148.061 117.793 180.421 1.00 157.29 ? 766  LYS A CA    1 
ATOM   5343  C  C     . LYS A 1 766 ? 146.694 118.073 179.814 1.00 157.49 ? 766  LYS A C     1 
ATOM   5344  O  O     . LYS A 1 766 ? 146.552 118.103 178.585 1.00 158.01 ? 766  LYS A O     1 
ATOM   5345  C  CB    . LYS A 1 766 ? 148.160 116.333 180.879 1.00 160.64 ? 766  LYS A CB    1 
ATOM   5346  C  CG    . LYS A 1 766 ? 149.402 115.936 181.708 1.00 163.34 ? 766  LYS A CG    1 
ATOM   5347  C  CD    . LYS A 1 766 ? 150.691 116.721 181.407 1.00 164.55 ? 766  LYS A CD    1 
ATOM   5348  C  CE    . LYS A 1 766 ? 151.159 116.562 179.960 1.00 168.54 ? 766  LYS A CE    1 
ATOM   5349  N  NZ    . LYS A 1 766 ? 152.543 117.074 179.760 1.00 168.21 ? 766  LYS A NZ    1 
ATOM   5350  N  N     . ASP A 1 767 ? 145.685 118.306 180.656 1.00 157.02 ? 767  ASP A N     1 
ATOM   5351  C  CA    . ASP A 1 767 ? 144.365 118.672 180.154 1.00 158.52 ? 767  ASP A CA    1 
ATOM   5352  C  C     . ASP A 1 767 ? 144.405 120.005 179.417 1.00 156.82 ? 767  ASP A C     1 
ATOM   5353  O  O     . ASP A 1 767 ? 143.745 120.170 178.385 1.00 157.23 ? 767  ASP A O     1 
ATOM   5354  C  CB    . ASP A 1 767 ? 143.363 118.724 181.307 1.00 163.50 ? 767  ASP A CB    1 
ATOM   5355  C  CG    . ASP A 1 767 ? 142.052 119.370 180.910 1.00 167.80 ? 767  ASP A CG    1 
ATOM   5356  O  OD1   . ASP A 1 767 ? 141.271 118.732 180.173 1.00 167.91 ? 767  ASP A OD1   1 
ATOM   5357  O  OD2   . ASP A 1 767 ? 141.802 120.518 181.333 1.00 168.35 ? 767  ASP A OD2   1 
ATOM   5358  N  N     . VAL A 1 768 ? 145.166 120.972 179.935 1.00 153.47 ? 768  VAL A N     1 
ATOM   5359  C  CA    . VAL A 1 768 ? 145.259 122.273 179.274 1.00 152.32 ? 768  VAL A CA    1 
ATOM   5360  C  C     . VAL A 1 768 ? 145.889 122.132 177.894 1.00 153.79 ? 768  VAL A C     1 
ATOM   5361  O  O     . VAL A 1 768 ? 145.419 122.726 176.915 1.00 157.10 ? 768  VAL A O     1 
ATOM   5362  C  CB    . VAL A 1 768 ? 146.043 123.266 180.152 1.00 152.94 ? 768  VAL A CB    1 
ATOM   5363  C  CG1   . VAL A 1 768 ? 146.270 124.566 179.404 1.00 152.01 ? 768  VAL A CG1   1 
ATOM   5364  C  CG2   . VAL A 1 768 ? 145.299 123.524 181.447 1.00 155.14 ? 768  VAL A CG2   1 
ATOM   5365  N  N     . ILE A 1 769 ? 146.962 121.348 177.794 1.00 151.99 ? 769  ILE A N     1 
ATOM   5366  C  CA    . ILE A 1 769 ? 147.631 121.149 176.511 1.00 149.63 ? 769  ILE A CA    1 
ATOM   5367  C  C     . ILE A 1 769 ? 146.714 120.413 175.542 1.00 152.77 ? 769  ILE A C     1 
ATOM   5368  O  O     . ILE A 1 769 ? 146.665 120.731 174.347 1.00 153.58 ? 769  ILE A O     1 
ATOM   5369  C  CB    . ILE A 1 769 ? 148.964 120.407 176.718 1.00 148.24 ? 769  ILE A CB    1 
ATOM   5370  C  CG1   . ILE A 1 769 ? 150.033 121.378 177.220 1.00 141.05 ? 769  ILE A CG1   1 
ATOM   5371  C  CG2   . ILE A 1 769 ? 149.422 119.745 175.433 1.00 150.88 ? 769  ILE A CG2   1 
ATOM   5372  C  CD1   . ILE A 1 769 ? 150.051 122.694 176.483 1.00 137.83 ? 769  ILE A CD1   1 
ATOM   5373  N  N     . ALA A 1 770 ? 145.969 119.423 176.040 1.00 153.48 ? 770  ALA A N     1 
ATOM   5374  C  CA    . ALA A 1 770 ? 145.007 118.731 175.190 1.00 152.44 ? 770  ALA A CA    1 
ATOM   5375  C  C     . ALA A 1 770 ? 143.935 119.687 174.682 1.00 153.10 ? 770  ALA A C     1 
ATOM   5376  O  O     . ALA A 1 770 ? 143.526 119.610 173.519 1.00 154.51 ? 770  ALA A O     1 
ATOM   5377  C  CB    . ALA A 1 770 ? 144.373 117.567 175.951 1.00 154.83 ? 770  ALA A CB    1 
ATOM   5378  N  N     . LYS A 1 771 ? 143.463 120.591 175.543 1.00 153.75 ? 771  LYS A N     1 
ATOM   5379  C  CA    . LYS A 1 771 ? 142.474 121.577 175.117 1.00 155.58 ? 771  LYS A CA    1 
ATOM   5380  C  C     . LYS A 1 771 ? 143.042 122.509 174.053 1.00 157.15 ? 771  LYS A C     1 
ATOM   5381  O  O     . LYS A 1 771 ? 142.360 122.831 173.072 1.00 160.22 ? 771  LYS A O     1 
ATOM   5382  C  CB    . LYS A 1 771 ? 141.980 122.378 176.321 1.00 157.39 ? 771  LYS A CB    1 
ATOM   5383  C  CG    . LYS A 1 771 ? 140.907 123.399 175.989 1.00 157.65 ? 771  LYS A CG    1 
ATOM   5384  C  CD    . LYS A 1 771 ? 140.486 124.174 177.226 1.00 157.89 ? 771  LYS A CD    1 
ATOM   5385  C  CE    . LYS A 1 771 ? 139.959 123.245 178.307 1.00 156.22 ? 771  LYS A CE    1 
ATOM   5386  N  NZ    . LYS A 1 771 ? 139.610 123.986 179.551 1.00 152.92 ? 771  LYS A NZ    1 
ATOM   5387  N  N     . ARG A 1 772 ? 144.286 122.961 174.234 1.00 156.05 ? 772  ARG A N     1 
ATOM   5388  C  CA    . ARG A 1 772 ? 144.917 123.804 173.220 1.00 153.75 ? 772  ARG A CA    1 
ATOM   5389  C  C     . ARG A 1 772 ? 145.029 123.072 171.890 1.00 154.03 ? 772  ARG A C     1 
ATOM   5390  O  O     . ARG A 1 772 ? 144.742 123.643 170.830 1.00 156.03 ? 772  ARG A O     1 
ATOM   5391  C  CB    . ARG A 1 772 ? 146.301 124.260 173.683 1.00 155.05 ? 772  ARG A CB    1 
ATOM   5392  C  CG    . ARG A 1 772 ? 146.351 124.996 175.012 1.00 157.42 ? 772  ARG A CG    1 
ATOM   5393  C  CD    . ARG A 1 772 ? 145.177 125.949 175.198 1.00 157.38 ? 772  ARG A CD    1 
ATOM   5394  N  NE    . ARG A 1 772 ? 145.350 126.832 176.348 1.00 160.53 ? 772  ARG A NE    1 
ATOM   5395  C  CZ    . ARG A 1 772 ? 146.337 127.706 176.500 1.00 160.23 ? 772  ARG A CZ    1 
ATOM   5396  N  NH1   . ARG A 1 772 ? 147.252 127.893 175.562 1.00 160.21 ? 772  ARG A NH1   1 
ATOM   5397  N  NH2   . ARG A 1 772 ? 146.401 128.423 177.618 1.00 155.50 ? 772  ARG A NH2   1 
ATOM   5398  N  N     . ARG A 1 773 ? 145.447 121.804 171.926 1.00 153.41 ? 773  ARG A N     1 
ATOM   5399  C  CA    . ARG A 1 773 ? 145.574 121.030 170.696 1.00 154.75 ? 773  ARG A CA    1 
ATOM   5400  C  C     . ARG A 1 773 ? 144.221 120.831 170.027 1.00 156.11 ? 773  ARG A C     1 
ATOM   5401  O  O     . ARG A 1 773 ? 144.109 120.912 168.798 1.00 158.71 ? 773  ARG A O     1 
ATOM   5402  C  CB    . ARG A 1 773 ? 146.229 119.682 170.992 1.00 153.58 ? 773  ARG A CB    1 
ATOM   5403  C  CG    . ARG A 1 773 ? 147.669 119.580 170.529 1.00 154.17 ? 773  ARG A CG    1 
ATOM   5404  C  CD    . ARG A 1 773 ? 148.581 120.437 171.389 1.00 156.64 ? 773  ARG A CD    1 
ATOM   5405  N  NE    . ARG A 1 773 ? 149.970 120.364 170.954 1.00 156.27 ? 773  ARG A NE    1 
ATOM   5406  C  CZ    . ARG A 1 773 ? 150.793 119.365 171.242 1.00 157.67 ? 773  ARG A CZ    1 
ATOM   5407  N  NH1   . ARG A 1 773 ? 150.398 118.332 171.969 1.00 158.62 ? 773  ARG A NH1   1 
ATOM   5408  N  NH2   . ARG A 1 773 ? 152.043 119.403 170.791 1.00 153.96 ? 773  ARG A NH2   1 
ATOM   5409  N  N     . ALA A 1 774 ? 143.181 120.561 170.819 1.00 154.50 ? 774  ALA A N     1 
ATOM   5410  C  CA    . ALA A 1 774 ? 141.846 120.393 170.258 1.00 154.21 ? 774  ALA A CA    1 
ATOM   5411  C  C     . ALA A 1 774 ? 141.353 121.679 169.612 1.00 153.80 ? 774  ALA A C     1 
ATOM   5412  O  O     . ALA A 1 774 ? 140.752 121.647 168.533 1.00 156.18 ? 774  ALA A O     1 
ATOM   5413  C  CB    . ALA A 1 774 ? 140.874 119.929 171.342 1.00 155.59 ? 774  ALA A CB    1 
ATOM   5414  N  N     . LEU A 1 775 ? 141.590 122.823 170.258 1.00 153.14 ? 775  LEU A N     1 
ATOM   5415  C  CA    . LEU A 1 775 ? 141.191 124.095 169.664 1.00 153.01 ? 775  LEU A CA    1 
ATOM   5416  C  C     . LEU A 1 775 ? 141.947 124.361 168.369 1.00 156.96 ? 775  LEU A C     1 
ATOM   5417  O  O     . LEU A 1 775 ? 141.359 124.823 167.383 1.00 159.44 ? 775  LEU A O     1 
ATOM   5418  C  CB    . LEU A 1 775 ? 141.406 125.237 170.656 1.00 154.89 ? 775  LEU A CB    1 
ATOM   5419  C  CG    . LEU A 1 775 ? 140.485 125.255 171.878 1.00 158.45 ? 775  LEU A CG    1 
ATOM   5420  C  CD1   . LEU A 1 775 ? 140.800 126.444 172.773 1.00 159.21 ? 775  LEU A CD1   1 
ATOM   5421  C  CD2   . LEU A 1 775 ? 139.027 125.271 171.448 1.00 157.69 ? 775  LEU A CD2   1 
ATOM   5422  N  N     . GLU A 1 776 ? 143.252 124.075 168.349 1.00 158.66 ? 776  GLU A N     1 
ATOM   5423  C  CA    . GLU A 1 776 ? 144.026 124.260 167.126 1.00 158.89 ? 776  GLU A CA    1 
ATOM   5424  C  C     . GLU A 1 776 ? 143.500 123.376 166.003 1.00 159.61 ? 776  GLU A C     1 
ATOM   5425  O  O     . GLU A 1 776 ? 143.347 123.830 164.862 1.00 162.96 ? 776  GLU A O     1 
ATOM   5426  C  CB    . GLU A 1 776 ? 145.504 123.963 167.386 1.00 157.83 ? 776  GLU A CB    1 
ATOM   5427  C  CG    . GLU A 1 776 ? 146.228 124.976 168.269 1.00 157.53 ? 776  GLU A CG    1 
ATOM   5428  C  CD    . GLU A 1 776 ? 146.540 126.289 167.566 1.00 155.81 ? 776  GLU A CD    1 
ATOM   5429  O  OE1   . GLU A 1 776 ? 147.386 127.046 168.087 1.00 153.71 ? 776  GLU A OE1   1 
ATOM   5430  O  OE2   . GLU A 1 776 ? 145.954 126.566 166.498 1.00 154.50 ? 776  GLU A OE2   1 
ATOM   5431  N  N     . GLU A 1 777 ? 143.213 122.108 166.309 1.00 159.07 ? 777  GLU A N     1 
ATOM   5432  C  CA    . GLU A 1 777 ? 142.707 121.198 165.288 1.00 160.52 ? 777  GLU A CA    1 
ATOM   5433  C  C     . GLU A 1 777 ? 141.336 121.632 164.789 1.00 160.67 ? 777  GLU A C     1 
ATOM   5434  O  O     . GLU A 1 777 ? 141.055 121.555 163.588 1.00 162.05 ? 777  GLU A O     1 
ATOM   5435  C  CB    . GLU A 1 777 ? 142.653 119.772 165.834 1.00 160.92 ? 777  GLU A CB    1 
ATOM   5436  C  CG    . GLU A 1 777 ? 143.992 119.037 165.848 1.00 162.06 ? 777  GLU A CG    1 
ATOM   5437  C  CD    . GLU A 1 777 ? 144.875 119.346 164.648 1.00 163.53 ? 777  GLU A CD    1 
ATOM   5438  O  OE1   . GLU A 1 777 ? 144.362 119.402 163.510 1.00 163.13 ? 777  GLU A OE1   1 
ATOM   5439  O  OE2   . GLU A 1 777 ? 146.093 119.536 164.847 1.00 163.67 ? 777  GLU A OE2   1 
ATOM   5440  N  N     . LEU A 1 778 ? 140.465 122.081 165.694 1.00 160.67 ? 778  LEU A N     1 
ATOM   5441  C  CA    . LEU A 1 778 ? 139.148 122.552 165.280 1.00 159.63 ? 778  LEU A CA    1 
ATOM   5442  C  C     . LEU A 1 778 ? 139.261 123.781 164.389 1.00 159.91 ? 778  LEU A C     1 
ATOM   5443  O  O     . LEU A 1 778 ? 138.543 123.900 163.390 1.00 162.43 ? 778  LEU A O     1 
ATOM   5444  C  CB    . LEU A 1 778 ? 138.286 122.853 166.505 1.00 158.89 ? 778  LEU A CB    1 
ATOM   5445  C  CG    . LEU A 1 778 ? 137.223 121.810 166.852 1.00 154.87 ? 778  LEU A CG    1 
ATOM   5446  C  CD1   . LEU A 1 778 ? 136.032 121.931 165.916 1.00 151.51 ? 778  LEU A CD1   1 
ATOM   5447  C  CD2   . LEU A 1 778 ? 137.807 120.406 166.803 1.00 153.96 ? 778  LEU A CD2   1 
ATOM   5448  N  N     . ARG A 1 779 ? 140.160 124.705 164.733 1.00 158.91 ? 779  ARG A N     1 
ATOM   5449  C  CA    . ARG A 1 779 ? 140.372 125.880 163.894 1.00 159.26 ? 779  ARG A CA    1 
ATOM   5450  C  C     . ARG A 1 779 ? 140.883 125.482 162.516 1.00 160.02 ? 779  ARG A C     1 
ATOM   5451  O  O     . ARG A 1 779 ? 140.442 126.024 161.496 1.00 161.80 ? 779  ARG A O     1 
ATOM   5452  C  CB    . ARG A 1 779 ? 141.352 126.834 164.571 1.00 158.86 ? 779  ARG A CB    1 
ATOM   5453  C  CG    . ARG A 1 779 ? 141.077 128.303 164.314 1.00 160.47 ? 779  ARG A CG    1 
ATOM   5454  C  CD    . ARG A 1 779 ? 141.965 129.167 165.198 1.00 164.10 ? 779  ARG A CD    1 
ATOM   5455  N  NE    . ARG A 1 779 ? 143.367 128.771 165.108 1.00 165.42 ? 779  ARG A NE    1 
ATOM   5456  C  CZ    . ARG A 1 779 ? 144.097 128.789 163.999 1.00 163.56 ? 779  ARG A CZ    1 
ATOM   5457  N  NH1   . ARG A 1 779 ? 143.623 129.272 162.861 1.00 162.44 ? 779  ARG A NH1   1 
ATOM   5458  N  NH2   . ARG A 1 779 ? 145.337 128.315 164.033 1.00 159.20 ? 779  ARG A NH2   1 
ATOM   5459  N  N     . ARG A 1 780 ? 141.823 124.534 162.467 1.00 158.72 ? 780  ARG A N     1 
ATOM   5460  C  CA    . ARG A 1 780 ? 142.350 124.089 161.181 1.00 159.05 ? 780  ARG A CA    1 
ATOM   5461  C  C     . ARG A 1 780 ? 141.271 123.419 160.340 1.00 161.34 ? 780  ARG A C     1 
ATOM   5462  O  O     . ARG A 1 780 ? 141.184 123.656 159.129 1.00 162.69 ? 780  ARG A O     1 
ATOM   5463  C  CB    . ARG A 1 780 ? 143.529 123.142 161.395 1.00 159.55 ? 780  ARG A CB    1 
ATOM   5464  C  CG    . ARG A 1 780 ? 144.729 123.452 160.521 1.00 161.97 ? 780  ARG A CG    1 
ATOM   5465  C  CD    . ARG A 1 780 ? 145.439 124.713 160.984 1.00 164.29 ? 780  ARG A CD    1 
ATOM   5466  N  NE    . ARG A 1 780 ? 146.033 124.553 162.306 1.00 168.42 ? 780  ARG A NE    1 
ATOM   5467  C  CZ    . ARG A 1 780 ? 147.192 123.953 162.537 1.00 164.62 ? 780  ARG A CZ    1 
ATOM   5468  N  NH1   . ARG A 1 780 ? 147.913 123.438 161.554 1.00 158.38 ? 780  ARG A NH1   1 
ATOM   5469  N  NH2   . ARG A 1 780 ? 147.641 123.867 163.786 1.00 159.59 ? 780  ARG A NH2   1 
ATOM   5470  N  N     . GLU A 1 781 ? 140.441 122.578 160.961 1.00 162.60 ? 781  GLU A N     1 
ATOM   5471  C  CA    . GLU A 1 781 ? 139.363 121.929 160.223 1.00 161.79 ? 781  GLU A CA    1 
ATOM   5472  C  C     . GLU A 1 781 ? 138.345 122.946 159.726 1.00 161.99 ? 781  GLU A C     1 
ATOM   5473  O  O     . GLU A 1 781 ? 137.830 122.821 158.612 1.00 164.35 ? 781  GLU A O     1 
ATOM   5474  C  CB    . GLU A 1 781 ? 138.683 120.868 161.091 1.00 161.10 ? 781  GLU A CB    1 
ATOM   5475  C  CG    . GLU A 1 781 ? 139.571 119.705 161.566 1.00 166.87 ? 781  GLU A CG    1 
ATOM   5476  C  CD    . GLU A 1 781 ? 140.173 118.848 160.452 1.00 167.41 ? 781  GLU A CD    1 
ATOM   5477  O  OE1   . GLU A 1 781 ? 140.262 119.288 159.287 1.00 165.17 ? 781  GLU A OE1   1 
ATOM   5478  O  OE2   . GLU A 1 781 ? 140.569 117.703 160.757 1.00 168.04 ? 781  GLU A OE2   1 
ATOM   5479  N  N     . GLU A 1 782 ? 138.037 123.958 160.540 1.00 161.87 ? 782  GLU A N     1 
ATOM   5480  C  CA    . GLU A 1 782 ? 137.116 125.000 160.099 1.00 159.97 ? 782  GLU A CA    1 
ATOM   5481  C  C     . GLU A 1 782 ? 137.690 125.788 158.930 1.00 159.96 ? 782  GLU A C     1 
ATOM   5482  O  O     . GLU A 1 782 ? 136.972 126.111 157.976 1.00 161.99 ? 782  GLU A O     1 
ATOM   5483  C  CB    . GLU A 1 782 ? 136.781 125.934 161.263 1.00 158.43 ? 782  GLU A CB    1 
ATOM   5484  C  CG    . GLU A 1 782 ? 135.810 127.076 160.939 1.00 161.63 ? 782  GLU A CG    1 
ATOM   5485  C  CD    . GLU A 1 782 ? 134.461 126.627 160.380 1.00 165.14 ? 782  GLU A CD    1 
ATOM   5486  O  OE1   . GLU A 1 782 ? 134.189 125.411 160.293 1.00 162.86 ? 782  GLU A OE1   1 
ATOM   5487  O  OE2   . GLU A 1 782 ? 133.659 127.515 160.021 1.00 167.59 ? 782  GLU A OE2   1 
ATOM   5488  N  N     . LYS A 1 783 ? 138.984 126.110 158.986 1.00 157.01 ? 783  LYS A N     1 
ATOM   5489  C  CA    . LYS A 1 783 ? 139.618 126.812 157.875 1.00 155.11 ? 783  LYS A CA    1 
ATOM   5490  C  C     . LYS A 1 783 ? 139.594 125.967 156.609 1.00 157.59 ? 783  LYS A C     1 
ATOM   5491  O  O     . LYS A 1 783 ? 139.316 126.476 155.517 1.00 161.53 ? 783  LYS A O     1 
ATOM   5492  C  CB    . LYS A 1 783 ? 141.052 127.191 158.241 1.00 157.71 ? 783  LYS A CB    1 
ATOM   5493  C  CG    . LYS A 1 783 ? 141.598 128.371 157.458 1.00 160.86 ? 783  LYS A CG    1 
ATOM   5494  C  CD    . LYS A 1 783 ? 142.708 129.074 158.221 1.00 160.13 ? 783  LYS A CD    1 
ATOM   5495  C  CE    . LYS A 1 783 ? 142.203 129.627 159.543 1.00 164.99 ? 783  LYS A CE    1 
ATOM   5496  N  NZ    . LYS A 1 783 ? 141.096 130.602 159.350 1.00 167.82 ? 783  LYS A NZ    1 
ATOM   5497  N  N     . GLU A 1 784 ? 139.879 124.669 156.737 1.00 156.19 ? 784  GLU A N     1 
ATOM   5498  C  CA    . GLU A 1 784 ? 139.832 123.783 155.579 1.00 157.89 ? 784  GLU A CA    1 
ATOM   5499  C  C     . GLU A 1 784 ? 138.420 123.682 155.015 1.00 157.47 ? 784  GLU A C     1 
ATOM   5500  O  O     . GLU A 1 784 ? 138.232 123.656 153.795 1.00 158.50 ? 784  GLU A O     1 
ATOM   5501  C  CB    . GLU A 1 784 ? 140.362 122.400 155.956 1.00 160.45 ? 784  GLU A CB    1 
ATOM   5502  C  CG    . GLU A 1 784 ? 140.325 121.391 154.821 1.00 163.44 ? 784  GLU A CG    1 
ATOM   5503  C  CD    . GLU A 1 784 ? 140.861 120.034 155.230 1.00 165.00 ? 784  GLU A CD    1 
ATOM   5504  O  OE1   . GLU A 1 784 ? 141.360 119.908 156.367 1.00 166.51 ? 784  GLU A OE1   1 
ATOM   5505  O  OE2   . GLU A 1 784 ? 140.782 119.093 154.413 1.00 162.90 ? 784  GLU A OE2   1 
ATOM   5506  N  N     . ARG A 1 785 ? 137.413 123.617 155.889 1.00 156.15 ? 785  ARG A N     1 
ATOM   5507  C  CA    . ARG A 1 785 ? 136.031 123.548 155.426 1.00 155.08 ? 785  ARG A CA    1 
ATOM   5508  C  C     . ARG A 1 785 ? 135.625 124.823 154.700 1.00 155.27 ? 785  ARG A C     1 
ATOM   5509  O  O     . ARG A 1 785 ? 134.945 124.769 153.671 1.00 157.34 ? 785  ARG A O     1 
ATOM   5510  C  CB    . ARG A 1 785 ? 135.096 123.283 156.604 1.00 159.79 ? 785  ARG A CB    1 
ATOM   5511  C  CG    . ARG A 1 785 ? 134.039 122.231 156.332 1.00 163.17 ? 785  ARG A CG    1 
ATOM   5512  C  CD    . ARG A 1 785 ? 132.849 122.398 157.262 1.00 167.60 ? 785  ARG A CD    1 
ATOM   5513  N  NE    . ARG A 1 785 ? 133.238 122.329 158.665 1.00 172.73 ? 785  ARG A NE    1 
ATOM   5514  C  CZ    . ARG A 1 785 ? 133.471 121.201 159.323 1.00 178.93 ? 785  ARG A CZ    1 
ATOM   5515  N  NH1   . ARG A 1 785 ? 133.360 120.022 158.734 1.00 180.69 ? 785  ARG A NH1   1 
ATOM   5516  N  NH2   . ARG A 1 785 ? 133.823 121.259 160.604 1.00 178.75 ? 785  ARG A NH2   1 
ATOM   5517  N  N     . VAL A 1 786 ? 136.028 125.982 155.225 1.00 155.60 ? 786  VAL A N     1 
ATOM   5518  C  CA    . VAL A 1 786 ? 135.720 127.244 154.556 1.00 155.29 ? 786  VAL A CA    1 
ATOM   5519  C  C     . VAL A 1 786 ? 136.426 127.317 153.208 1.00 157.21 ? 786  VAL A C     1 
ATOM   5520  O  O     . VAL A 1 786 ? 135.856 127.788 152.214 1.00 158.83 ? 786  VAL A O     1 
ATOM   5521  C  CB    . VAL A 1 786 ? 136.091 128.433 155.462 1.00 159.52 ? 786  VAL A CB    1 
ATOM   5522  C  CG1   . VAL A 1 786 ? 136.042 129.736 154.684 1.00 160.63 ? 786  VAL A CG1   1 
ATOM   5523  C  CG2   . VAL A 1 786 ? 135.155 128.493 156.657 1.00 159.22 ? 786  VAL A CG2   1 
ATOM   5524  N  N     . GLU A 1 787 ? 137.677 126.855 153.150 1.00 157.04 ? 787  GLU A N     1 
ATOM   5525  C  CA    . GLU A 1 787 ? 138.399 126.840 151.883 1.00 156.87 ? 787  GLU A CA    1 
ATOM   5526  C  C     . GLU A 1 787 ? 137.725 125.918 150.875 1.00 154.44 ? 787  GLU A C     1 
ATOM   5527  O  O     . GLU A 1 787 ? 137.631 126.252 149.692 1.00 155.65 ? 787  GLU A O     1 
ATOM   5528  C  CB    . GLU A 1 787 ? 139.854 126.426 152.109 1.00 161.77 ? 787  GLU A CB    1 
ATOM   5529  C  CG    . GLU A 1 787 ? 140.471 125.645 150.959 1.00 163.73 ? 787  GLU A CG    1 
ATOM   5530  C  CD    . GLU A 1 787 ? 141.985 125.739 150.933 1.00 170.71 ? 787  GLU A CD    1 
ATOM   5531  O  OE1   . GLU A 1 787 ? 142.538 126.095 149.872 1.00 168.94 ? 787  GLU A OE1   1 
ATOM   5532  O  OE2   . GLU A 1 787 ? 142.621 125.458 151.970 1.00 174.89 ? 787  GLU A OE2   1 
ATOM   5533  N  N     . ASN A 1 788 ? 137.253 124.754 151.323 1.00 152.43 ? 788  ASN A N     1 
ATOM   5534  C  CA    . ASN A 1 788 ? 136.544 123.845 150.426 1.00 150.25 ? 788  ASN A CA    1 
ATOM   5535  C  C     . ASN A 1 788 ? 135.231 124.452 149.946 1.00 150.72 ? 788  ASN A C     1 
ATOM   5536  O  O     . ASN A 1 788 ? 134.860 124.303 148.774 1.00 150.60 ? 788  ASN A O     1 
ATOM   5537  C  CB    . ASN A 1 788 ? 136.295 122.512 151.126 1.00 152.74 ? 788  ASN A CB    1 
ATOM   5538  C  CG    . ASN A 1 788 ? 136.268 121.348 150.162 1.00 154.42 ? 788  ASN A CG    1 
ATOM   5539  O  OD1   . ASN A 1 788 ? 135.200 120.869 149.780 1.00 157.58 ? 788  ASN A OD1   1 
ATOM   5540  N  ND2   . ASN A 1 788 ? 137.445 120.881 149.762 1.00 153.07 ? 788  ASN A ND2   1 
ATOM   5541  N  N     . ARG A 1 789 ? 134.508 125.126 150.843 1.00 154.05 ? 789  ARG A N     1 
ATOM   5542  C  CA    . ARG A 1 789 ? 133.294 125.829 150.445 1.00 153.96 ? 789  ARG A CA    1 
ATOM   5543  C  C     . ARG A 1 789 ? 133.591 126.850 149.359 1.00 151.39 ? 789  ARG A C     1 
ATOM   5544  O  O     . ARG A 1 789 ? 132.913 126.891 148.327 1.00 153.83 ? 789  ARG A O     1 
ATOM   5545  C  CB    . ARG A 1 789 ? 132.671 126.524 151.655 1.00 156.45 ? 789  ARG A CB    1 
ATOM   5546  C  CG    . ARG A 1 789 ? 131.326 127.170 151.369 1.00 156.18 ? 789  ARG A CG    1 
ATOM   5547  C  CD    . ARG A 1 789 ? 130.606 127.573 152.648 1.00 162.79 ? 789  ARG A CD    1 
ATOM   5548  N  NE    . ARG A 1 789 ? 130.696 126.559 153.695 1.00 165.60 ? 789  ARG A NE    1 
ATOM   5549  C  CZ    . ARG A 1 789 ? 130.550 126.798 154.990 1.00 167.33 ? 789  ARG A CZ    1 
ATOM   5550  N  NH1   . ARG A 1 789 ? 130.384 128.030 155.450 1.00 167.78 ? 789  ARG A NH1   1 
ATOM   5551  N  NH2   . ARG A 1 789 ? 130.577 125.777 155.843 1.00 166.04 ? 789  ARG A NH2   1 
ATOM   5552  N  N     . LYS A 1 790 ? 134.617 127.676 149.571 1.00 149.10 ? 790  LYS A N     1 
ATOM   5553  C  CA    . LYS A 1 790 ? 134.956 128.696 148.585 1.00 146.41 ? 790  LYS A CA    1 
ATOM   5554  C  C     . LYS A 1 790 ? 135.427 128.064 147.282 1.00 146.91 ? 790  LYS A C     1 
ATOM   5555  O  O     . LYS A 1 790 ? 135.132 128.574 146.197 1.00 147.29 ? 790  LYS A O     1 
ATOM   5556  C  CB    . LYS A 1 790 ? 136.021 129.639 149.141 1.00 150.45 ? 790  LYS A CB    1 
ATOM   5557  C  CG    . LYS A 1 790 ? 135.492 130.675 150.127 1.00 157.21 ? 790  LYS A CG    1 
ATOM   5558  C  CD    . LYS A 1 790 ? 134.045 131.045 149.843 1.00 155.80 ? 790  LYS A CD    1 
ATOM   5559  C  CE    . LYS A 1 790 ? 133.546 132.105 150.812 1.00 155.10 ? 790  LYS A CE    1 
ATOM   5560  N  NZ    . LYS A 1 790 ? 132.110 132.438 150.589 1.00 152.40 ? 790  LYS A NZ    1 
ATOM   5561  N  N     . LYS A 1 791 ? 136.162 126.954 147.367 1.00 149.32 ? 791  LYS A N     1 
ATOM   5562  C  CA    . LYS A 1 791 ? 136.629 126.272 146.164 1.00 147.88 ? 791  LYS A CA    1 
ATOM   5563  C  C     . LYS A 1 791 ? 135.460 125.770 145.327 1.00 144.69 ? 791  LYS A C     1 
ATOM   5564  O  O     . LYS A 1 791 ? 135.386 126.040 144.124 1.00 146.67 ? 791  LYS A O     1 
ATOM   5565  C  CB    . LYS A 1 791 ? 137.560 125.119 146.544 1.00 148.01 ? 791  LYS A CB    1 
ATOM   5566  C  CG    . LYS A 1 791 ? 137.448 123.906 145.630 1.00 145.83 ? 791  LYS A CG    1 
ATOM   5567  C  CD    . LYS A 1 791 ? 138.260 122.721 146.129 1.00 146.45 ? 791  LYS A CD    1 
ATOM   5568  C  CE    . LYS A 1 791 ? 138.038 121.497 145.248 1.00 148.65 ? 791  LYS A CE    1 
ATOM   5569  N  NZ    . LYS A 1 791 ? 138.780 120.303 145.741 1.00 150.48 ? 791  LYS A NZ    1 
ATOM   5570  N  N     . ASN A 1 792 ? 134.524 125.049 145.952 1.00 140.94 ? 792  ASN A N     1 
ATOM   5571  C  CA    . ASN A 1 792 ? 133.360 124.567 145.215 1.00 138.99 ? 792  ASN A CA    1 
ATOM   5572  C  C     . ASN A 1 792 ? 132.545 125.733 144.674 1.00 141.24 ? 792  ASN A C     1 
ATOM   5573  O  O     . ASN A 1 792 ? 132.056 125.693 143.537 1.00 143.80 ? 792  ASN A O     1 
ATOM   5574  C  CB    . ASN A 1 792 ? 132.493 123.686 146.115 1.00 143.35 ? 792  ASN A CB    1 
ATOM   5575  C  CG    . ASN A 1 792 ? 132.997 122.260 146.200 1.00 148.69 ? 792  ASN A CG    1 
ATOM   5576  O  OD1   . ASN A 1 792 ? 134.153 121.977 145.890 1.00 149.29 ? 792  ASN A OD1   1 
ATOM   5577  N  ND2   . ASN A 1 792 ? 132.128 121.350 146.628 1.00 150.30 ? 792  ASN A ND2   1 
ATOM   5578  N  N     . PHE A 1 793 ? 132.414 126.791 145.475 1.00 143.55 ? 793  PHE A N     1 
ATOM   5579  C  CA    . PHE A 1 793 ? 131.560 127.918 145.132 1.00 143.75 ? 793  PHE A CA    1 
ATOM   5580  C  C     . PHE A 1 793 ? 132.102 128.627 143.901 1.00 142.16 ? 793  PHE A C     1 
ATOM   5581  O  O     . PHE A 1 793 ? 131.382 128.833 142.913 1.00 144.14 ? 793  PHE A O     1 
ATOM   5582  C  CB    . PHE A 1 793 ? 131.530 128.859 146.335 1.00 151.48 ? 793  PHE A CB    1 
ATOM   5583  C  CG    . PHE A 1 793 ? 130.353 128.657 147.243 1.00 158.20 ? 793  PHE A CG    1 
ATOM   5584  C  CD1   . PHE A 1 793 ? 129.538 127.545 147.109 1.00 154.62 ? 793  PHE A CD1   1 
ATOM   5585  C  CD2   . PHE A 1 793 ? 130.084 129.559 148.255 1.00 161.90 ? 793  PHE A CD2   1 
ATOM   5586  C  CE1   . PHE A 1 793 ? 128.470 127.349 147.956 1.00 157.41 ? 793  PHE A CE1   1 
ATOM   5587  C  CE2   . PHE A 1 793 ? 129.034 129.354 149.116 1.00 163.77 ? 793  PHE A CE2   1 
ATOM   5588  C  CZ    . PHE A 1 793 ? 128.219 128.253 148.962 1.00 162.34 ? 793  PHE A CZ    1 
ATOM   5589  N  N     . GLU A 1 794 ? 133.400 128.949 143.928 1.00 142.38 ? 794  GLU A N     1 
ATOM   5590  C  CA    . GLU A 1 794 ? 134.056 129.605 142.805 1.00 138.84 ? 794  GLU A CA    1 
ATOM   5591  C  C     . GLU A 1 794 ? 134.116 128.699 141.587 1.00 134.01 ? 794  GLU A C     1 
ATOM   5592  O  O     . GLU A 1 794 ? 134.002 129.175 140.454 1.00 134.83 ? 794  GLU A O     1 
ATOM   5593  C  CB    . GLU A 1 794 ? 135.466 130.048 143.200 1.00 144.34 ? 794  GLU A CB    1 
ATOM   5594  C  CG    . GLU A 1 794 ? 135.501 131.223 144.161 1.00 149.32 ? 794  GLU A CG    1 
ATOM   5595  C  CD    . GLU A 1 794 ? 136.913 131.609 144.541 1.00 151.57 ? 794  GLU A CD    1 
ATOM   5596  O  OE1   . GLU A 1 794 ? 137.792 130.728 144.469 1.00 148.62 ? 794  GLU A OE1   1 
ATOM   5597  O  OE2   . GLU A 1 794 ? 137.145 132.783 144.909 1.00 153.83 ? 794  GLU A OE2   1 
ATOM   5598  N  N     . ALA A 1 795 ? 134.326 127.395 141.790 1.00 134.92 ? 795  ALA A N     1 
ATOM   5599  C  CA    . ALA A 1 795 ? 134.370 126.479 140.658 1.00 132.82 ? 795  ALA A CA    1 
ATOM   5600  C  C     . ALA A 1 795 ? 133.034 126.437 139.934 1.00 130.00 ? 795  ALA A C     1 
ATOM   5601  O  O     . ALA A 1 795 ? 132.987 126.466 138.700 1.00 131.99 ? 795  ALA A O     1 
ATOM   5602  C  CB    . ALA A 1 795 ? 134.769 125.082 141.129 1.00 134.51 ? 795  ALA A CB    1 
ATOM   5603  N  N     . PHE A 1 796 ? 131.934 126.378 140.685 1.00 130.24 ? 796  PHE A N     1 
ATOM   5604  C  CA    . PHE A 1 796 ? 130.620 126.387 140.052 1.00 129.86 ? 796  PHE A CA    1 
ATOM   5605  C  C     . PHE A 1 796 ? 130.360 127.727 139.374 1.00 128.82 ? 796  PHE A C     1 
ATOM   5606  O  O     . PHE A 1 796 ? 129.790 127.782 138.274 1.00 129.22 ? 796  PHE A O     1 
ATOM   5607  C  CB    . PHE A 1 796 ? 129.543 126.074 141.088 1.00 134.37 ? 796  PHE A CB    1 
ATOM   5608  C  CG    . PHE A 1 796 ? 128.151 126.079 140.536 1.00 134.22 ? 796  PHE A CG    1 
ATOM   5609  C  CD1   . PHE A 1 796 ? 127.678 124.999 139.811 1.00 131.49 ? 796  PHE A CD1   1 
ATOM   5610  C  CD2   . PHE A 1 796 ? 127.313 127.158 140.744 1.00 137.74 ? 796  PHE A CD2   1 
ATOM   5611  C  CE1   . PHE A 1 796 ? 126.395 124.996 139.303 1.00 135.73 ? 796  PHE A CE1   1 
ATOM   5612  C  CE2   . PHE A 1 796 ? 126.031 127.161 140.238 1.00 138.62 ? 796  PHE A CE2   1 
ATOM   5613  C  CZ    . PHE A 1 796 ? 125.571 126.079 139.516 1.00 137.46 ? 796  PHE A CZ    1 
ATOM   5614  N  N     . ARG A 1 797 ? 130.785 128.823 140.012 1.00 128.74 ? 797  ARG A N     1 
ATOM   5615  C  CA    . ARG A 1 797 ? 130.645 130.138 139.393 1.00 129.89 ? 797  ARG A CA    1 
ATOM   5616  C  C     . ARG A 1 797 ? 131.347 130.182 138.045 1.00 126.82 ? 797  ARG A C     1 
ATOM   5617  O  O     . ARG A 1 797 ? 130.752 130.585 137.040 1.00 125.58 ? 797  ARG A O     1 
ATOM   5618  C  CB    . ARG A 1 797 ? 131.192 131.214 140.346 1.00 137.06 ? 797  ARG A CB    1 
ATOM   5619  C  CG    . ARG A 1 797 ? 131.273 132.681 139.840 1.00 138.62 ? 797  ARG A CG    1 
ATOM   5620  C  CD    . ARG A 1 797 ? 132.306 133.006 138.767 1.00 136.73 ? 797  ARG A CD    1 
ATOM   5621  N  NE    . ARG A 1 797 ? 133.651 132.704 139.234 1.00 141.09 ? 797  ARG A NE    1 
ATOM   5622  C  CZ    . ARG A 1 797 ? 134.350 133.491 140.040 1.00 143.35 ? 797  ARG A CZ    1 
ATOM   5623  N  NH1   . ARG A 1 797 ? 133.867 134.647 140.467 1.00 141.79 ? 797  ARG A NH1   1 
ATOM   5624  N  NH2   . ARG A 1 797 ? 135.558 133.106 140.436 1.00 143.06 ? 797  ARG A NH2   1 
ATOM   5625  N  N     . THR A 1 798 ? 132.612 129.766 138.011 1.00 128.61 ? 798  THR A N     1 
ATOM   5626  C  CA    . THR A 1 798 ? 133.386 129.826 136.779 1.00 124.01 ? 798  THR A CA    1 
ATOM   5627  C  C     . THR A 1 798 ? 132.829 128.873 135.732 1.00 120.79 ? 798  THR A C     1 
ATOM   5628  O  O     . THR A 1 798 ? 132.806 129.200 134.544 1.00 122.00 ? 798  THR A O     1 
ATOM   5629  C  CB    . THR A 1 798 ? 134.854 129.520 137.066 1.00 128.13 ? 798  THR A CB    1 
ATOM   5630  O  OG1   . THR A 1 798 ? 135.390 130.532 137.925 1.00 132.41 ? 798  THR A OG1   1 
ATOM   5631  C  CG2   . THR A 1 798 ? 135.658 129.496 135.779 1.00 124.55 ? 798  THR A CG2   1 
ATOM   5632  N  N     . ASN A 1 799 ? 132.371 127.690 136.147 1.00 120.55 ? 799  ASN A N     1 
ATOM   5633  C  CA    . ASN A 1 799 ? 131.807 126.754 135.181 1.00 119.64 ? 799  ASN A CA    1 
ATOM   5634  C  C     . ASN A 1 799 ? 130.557 127.321 134.523 1.00 119.23 ? 799  ASN A C     1 
ATOM   5635  O  O     . ASN A 1 799 ? 130.418 127.268 133.295 1.00 121.03 ? 799  ASN A O     1 
ATOM   5636  C  CB    . ASN A 1 799 ? 131.502 125.419 135.856 1.00 123.45 ? 799  ASN A CB    1 
ATOM   5637  C  CG    . ASN A 1 799 ? 132.755 124.656 136.225 1.00 132.03 ? 799  ASN A CG    1 
ATOM   5638  O  OD1   . ASN A 1 799 ? 133.854 125.209 136.218 1.00 131.80 ? 799  ASN A OD1   1 
ATOM   5639  N  ND2   . ASN A 1 799 ? 132.597 123.379 136.550 1.00 137.48 ? 799  ASN A ND2   1 
ATOM   5640  N  N     . VAL A 1 800 ? 129.641 127.884 135.316 1.00 116.68 ? 800  VAL A N     1 
ATOM   5641  C  CA    . VAL A 1 800 ? 128.423 128.441 134.731 1.00 113.60 ? 800  VAL A CA    1 
ATOM   5642  C  C     . VAL A 1 800 ? 128.751 129.656 133.872 1.00 113.19 ? 800  VAL A C     1 
ATOM   5643  O  O     . VAL A 1 800 ? 128.177 129.843 132.791 1.00 111.92 ? 800  VAL A O     1 
ATOM   5644  C  CB    . VAL A 1 800 ? 127.396 128.774 135.828 1.00 115.23 ? 800  VAL A CB    1 
ATOM   5645  C  CG1   . VAL A 1 800 ? 126.491 129.910 135.387 1.00 116.81 ? 800  VAL A CG1   1 
ATOM   5646  C  CG2   . VAL A 1 800 ? 126.570 127.545 136.158 1.00 120.80 ? 800  VAL A CG2   1 
ATOM   5647  N  N     . LEU A 1 801 ? 129.679 130.501 134.331 1.00 116.21 ? 801  LEU A N     1 
ATOM   5648  C  CA    . LEU A 1 801 ? 130.067 131.667 133.544 1.00 112.97 ? 801  LEU A CA    1 
ATOM   5649  C  C     . LEU A 1 801 ? 130.678 131.260 132.212 1.00 111.11 ? 801  LEU A C     1 
ATOM   5650  O  O     . LEU A 1 801 ? 130.367 131.852 131.173 1.00 112.44 ? 801  LEU A O     1 
ATOM   5651  C  CB    . LEU A 1 801 ? 131.049 132.530 134.330 1.00 112.22 ? 801  LEU A CB    1 
ATOM   5652  C  CG    . LEU A 1 801 ? 131.724 133.624 133.507 1.00 105.48 ? 801  LEU A CG    1 
ATOM   5653  C  CD1   . LEU A 1 801 ? 130.710 134.654 133.054 1.00 108.67 ? 801  LEU A CD1   1 
ATOM   5654  C  CD2   . LEU A 1 801 ? 132.839 134.273 134.298 1.00 116.11 ? 801  LEU A CD2   1 
ATOM   5655  N  N     . LEU A 1 802 ? 131.567 130.265 132.224 1.00 112.56 ? 802  LEU A N     1 
ATOM   5656  C  CA    . LEU A 1 802 ? 132.165 129.794 130.983 1.00 109.82 ? 802  LEU A CA    1 
ATOM   5657  C  C     . LEU A 1 802 ? 131.113 129.198 130.065 1.00 108.56 ? 802  LEU A C     1 
ATOM   5658  O  O     . LEU A 1 802 ? 131.119 129.460 128.859 1.00 111.59 ? 802  LEU A O     1 
ATOM   5659  C  CB    . LEU A 1 802 ? 133.263 128.775 131.279 1.00 105.73 ? 802  LEU A CB    1 
ATOM   5660  C  CG    . LEU A 1 802 ? 134.572 129.352 131.813 1.00 109.75 ? 802  LEU A CG    1 
ATOM   5661  C  CD1   . LEU A 1 802 ? 135.591 128.250 132.032 1.00 115.06 ? 802  LEU A CD1   1 
ATOM   5662  C  CD2   . LEU A 1 802 ? 135.110 130.404 130.867 1.00 107.12 ? 802  LEU A CD2   1 
ATOM   5663  N  N     . THR A 1 803 ? 130.191 128.406 130.617 1.00 103.75 ? 803  THR A N     1 
ATOM   5664  C  CA    . THR A 1 803 ? 129.120 127.851 129.798 1.00 102.74 ? 803  THR A CA    1 
ATOM   5665  C  C     . THR A 1 803 ? 128.323 128.959 129.125 1.00 106.01 ? 803  THR A C     1 
ATOM   5666  O  O     . THR A 1 803 ? 128.109 128.933 127.910 1.00 108.96 ? 803  THR A O     1 
ATOM   5667  C  CB    . THR A 1 803 ? 128.204 126.973 130.648 1.00 106.85 ? 803  THR A CB    1 
ATOM   5668  O  OG1   . THR A 1 803 ? 128.960 125.892 131.204 1.00 116.28 ? 803  THR A OG1   1 
ATOM   5669  C  CG2   . THR A 1 803 ? 127.076 126.412 129.804 1.00 102.53 ? 803  THR A CG2   1 
ATOM   5670  N  N     . TRP A 1 804 ? 127.914 129.967 129.896 1.00 106.45 ? 804  TRP A N     1 
ATOM   5671  C  CA    . TRP A 1 804 ? 127.116 131.060 129.346 1.00 106.04 ? 804  TRP A CA    1 
ATOM   5672  C  C     . TRP A 1 804 ? 127.884 131.831 128.279 1.00 107.52 ? 804  TRP A C     1 
ATOM   5673  O  O     . TRP A 1 804 ? 127.396 132.017 127.155 1.00 109.12 ? 804  TRP A O     1 
ATOM   5674  C  CB    . TRP A 1 804 ? 126.684 131.992 130.477 1.00 107.11 ? 804  TRP A CB    1 
ATOM   5675  C  CG    . TRP A 1 804 ? 125.975 133.223 130.024 1.00 107.43 ? 804  TRP A CG    1 
ATOM   5676  C  CD1   . TRP A 1 804 ? 124.736 133.299 129.467 1.00 110.34 ? 804  TRP A CD1   1 
ATOM   5677  C  CD2   . TRP A 1 804 ? 126.466 134.565 130.097 1.00 109.44 ? 804  TRP A CD2   1 
ATOM   5678  N  NE1   . TRP A 1 804 ? 124.422 134.606 129.187 1.00 112.27 ? 804  TRP A NE1   1 
ATOM   5679  C  CE2   . TRP A 1 804 ? 125.470 135.402 129.565 1.00 109.32 ? 804  TRP A CE2   1 
ATOM   5680  C  CE3   . TRP A 1 804 ? 127.652 135.139 130.560 1.00 115.14 ? 804  TRP A CE3   1 
ATOM   5681  C  CZ2   . TRP A 1 804 ? 125.623 136.781 129.482 1.00 109.09 ? 804  TRP A CZ2   1 
ATOM   5682  C  CZ3   . TRP A 1 804 ? 127.802 136.506 130.476 1.00 117.11 ? 804  TRP A CZ3   1 
ATOM   5683  C  CH2   . TRP A 1 804 ? 126.794 137.312 129.941 1.00 113.52 ? 804  TRP A CH2   1 
ATOM   5684  N  N     . ALA A 1 805 ? 129.096 132.282 128.611 1.00 107.67 ? 805  ALA A N     1 
ATOM   5685  C  CA    . ALA A 1 805 ? 129.855 133.119 127.691 1.00 105.64 ? 805  ALA A CA    1 
ATOM   5686  C  C     . ALA A 1 805 ? 130.217 132.363 126.422 1.00 107.57 ? 805  ALA A C     1 
ATOM   5687  O  O     . ALA A 1 805 ? 130.097 132.901 125.317 1.00 109.31 ? 805  ALA A O     1 
ATOM   5688  C  CB    . ALA A 1 805 ? 131.113 133.647 128.377 1.00 98.52  ? 805  ALA A CB    1 
ATOM   5689  N  N     . PHE A 1 806 ? 130.648 131.108 126.553 1.00 104.94 ? 806  PHE A N     1 
ATOM   5690  C  CA    . PHE A 1 806 ? 131.054 130.356 125.376 1.00 105.92 ? 806  PHE A CA    1 
ATOM   5691  C  C     . PHE A 1 806 ? 129.858 129.901 124.557 1.00 107.04 ? 806  PHE A C     1 
ATOM   5692  O  O     . PHE A 1 806 ? 129.961 129.814 123.332 1.00 110.35 ? 806  PHE A O     1 
ATOM   5693  C  CB    . PHE A 1 806 ? 131.920 129.169 125.788 1.00 107.59 ? 806  PHE A CB    1 
ATOM   5694  C  CG    . PHE A 1 806 ? 133.376 129.506 125.904 1.00 111.22 ? 806  PHE A CG    1 
ATOM   5695  C  CD1   . PHE A 1 806 ? 133.823 130.365 126.891 1.00 113.88 ? 806  PHE A CD1   1 
ATOM   5696  C  CD2   . PHE A 1 806 ? 134.296 128.973 125.022 1.00 113.26 ? 806  PHE A CD2   1 
ATOM   5697  C  CE1   . PHE A 1 806 ? 135.159 130.682 126.999 1.00 115.09 ? 806  PHE A CE1   1 
ATOM   5698  C  CE2   . PHE A 1 806 ? 135.634 129.286 125.127 1.00 115.60 ? 806  PHE A CE2   1 
ATOM   5699  C  CZ    . PHE A 1 806 ? 136.065 130.142 126.116 1.00 115.22 ? 806  PHE A CZ    1 
ATOM   5700  N  N     . SER A 1 807 ? 128.715 129.629 125.190 1.00 103.62 ? 807  SER A N     1 
ATOM   5701  C  CA    . SER A 1 807 ? 127.508 129.350 124.423 1.00 102.26 ? 807  SER A CA    1 
ATOM   5702  C  C     . SER A 1 807 ? 127.107 130.563 123.600 1.00 103.24 ? 807  SER A C     1 
ATOM   5703  O  O     . SER A 1 807 ? 126.790 130.443 122.411 1.00 105.66 ? 807  SER A O     1 
ATOM   5704  C  CB    . SER A 1 807 ? 126.376 128.933 125.359 1.00 102.50 ? 807  SER A CB    1 
ATOM   5705  O  OG    . SER A 1 807 ? 126.687 127.723 126.024 1.00 111.58 ? 807  SER A OG    1 
ATOM   5706  N  N     . ASN A 1 808 ? 127.140 131.750 124.211 1.00 99.95  ? 808  ASN A N     1 
ATOM   5707  C  CA    . ASN A 1 808 ? 126.811 132.961 123.467 1.00 98.18  ? 808  ASN A CA    1 
ATOM   5708  C  C     . ASN A 1 808 ? 127.797 133.197 122.330 1.00 101.80 ? 808  ASN A C     1 
ATOM   5709  O  O     . ASN A 1 808 ? 127.393 133.512 121.205 1.00 103.66 ? 808  ASN A O     1 
ATOM   5710  C  CB    . ASN A 1 808 ? 126.778 134.162 124.409 1.00 100.17 ? 808  ASN A CB    1 
ATOM   5711  C  CG    . ASN A 1 808 ? 125.502 134.231 125.216 1.00 102.30 ? 808  ASN A CG    1 
ATOM   5712  O  OD1   . ASN A 1 808 ? 124.672 135.113 125.011 1.00 98.85  ? 808  ASN A OD1   1 
ATOM   5713  N  ND2   . ASN A 1 808 ? 125.339 133.298 126.142 1.00 108.43 ? 808  ASN A ND2   1 
ATOM   5714  N  N     . LEU A 1 809 ? 129.095 133.034 122.598 1.00 101.64 ? 809  LEU A N     1 
ATOM   5715  C  CA    . LEU A 1 809 ? 130.100 133.266 121.566 1.00 103.43 ? 809  LEU A CA    1 
ATOM   5716  C  C     . LEU A 1 809 ? 129.971 132.268 120.423 1.00 105.05 ? 809  LEU A C     1 
ATOM   5717  O  O     . LEU A 1 809 ? 130.064 132.645 119.250 1.00 105.93 ? 809  LEU A O     1 
ATOM   5718  C  CB    . LEU A 1 809 ? 131.500 133.200 122.171 1.00 103.18 ? 809  LEU A CB    1 
ATOM   5719  C  CG    . LEU A 1 809 ? 132.114 134.535 122.579 1.00 106.12 ? 809  LEU A CG    1 
ATOM   5720  C  CD1   . LEU A 1 809 ? 133.484 134.320 123.185 1.00 112.19 ? 809  LEU A CD1   1 
ATOM   5721  C  CD2   . LEU A 1 809 ? 132.199 135.455 121.380 1.00 108.39 ? 809  LEU A CD2   1 
ATOM   5722  N  N     . ILE A 1 810 ? 129.762 130.990 120.742 1.00 103.36 ? 810  ILE A N     1 
ATOM   5723  C  CA    . ILE A 1 810 ? 129.648 129.972 119.705 1.00 102.73 ? 810  ILE A CA    1 
ATOM   5724  C  C     . ILE A 1 810 ? 128.384 130.188 118.887 1.00 102.89 ? 810  ILE A C     1 
ATOM   5725  O  O     . ILE A 1 810 ? 128.395 130.047 117.659 1.00 106.95 ? 810  ILE A O     1 
ATOM   5726  C  CB    . ILE A 1 810 ? 129.695 128.568 120.333 1.00 103.26 ? 810  ILE A CB    1 
ATOM   5727  C  CG1   . ILE A 1 810 ? 131.119 128.246 120.787 1.00 105.41 ? 810  ILE A CG1   1 
ATOM   5728  C  CG2   . ILE A 1 810 ? 129.204 127.522 119.353 1.00 104.27 ? 810  ILE A CG2   1 
ATOM   5729  C  CD1   . ILE A 1 810 ? 131.276 126.859 121.358 1.00 113.61 ? 810  ILE A CD1   1 
ATOM   5730  N  N     . PHE A 1 811 ? 127.278 130.541 119.545 1.00 97.49  ? 811  PHE A N     1 
ATOM   5731  C  CA    . PHE A 1 811 ? 126.051 130.838 118.815 1.00 96.90  ? 811  PHE A CA    1 
ATOM   5732  C  C     . PHE A 1 811 ? 126.249 132.023 117.878 1.00 100.35 ? 811  PHE A C     1 
ATOM   5733  O  O     . PHE A 1 811 ? 125.848 131.978 116.708 1.00 102.49 ? 811  PHE A O     1 
ATOM   5734  C  CB    . PHE A 1 811 ? 124.917 131.106 119.803 1.00 96.87  ? 811  PHE A CB    1 
ATOM   5735  C  CG    . PHE A 1 811 ? 123.595 131.374 119.154 1.00 93.12  ? 811  PHE A CG    1 
ATOM   5736  C  CD1   . PHE A 1 811 ? 122.864 130.345 118.594 1.00 91.98  ? 811  PHE A CD1   1 
ATOM   5737  C  CD2   . PHE A 1 811 ? 123.075 132.653 119.118 1.00 97.55  ? 811  PHE A CD2   1 
ATOM   5738  C  CE1   . PHE A 1 811 ? 121.644 130.588 118.002 1.00 97.95  ? 811  PHE A CE1   1 
ATOM   5739  C  CE2   . PHE A 1 811 ? 121.856 132.902 118.528 1.00 99.78  ? 811  PHE A CE2   1 
ATOM   5740  C  CZ    . PHE A 1 811 ? 121.140 131.869 117.969 1.00 99.66  ? 811  PHE A CZ    1 
ATOM   5741  N  N     . ALA A 1 812 ? 126.888 133.088 118.369 1.00 98.82  ? 812  ALA A N     1 
ATOM   5742  C  CA    . ALA A 1 812 ? 127.113 134.261 117.534 1.00 96.46  ? 812  ALA A CA    1 
ATOM   5743  C  C     . ALA A 1 812 ? 128.008 133.934 116.347 1.00 102.08 ? 812  ALA A C     1 
ATOM   5744  O  O     . ALA A 1 812 ? 127.726 134.347 115.217 1.00 104.64 ? 812  ALA A O     1 
ATOM   5745  C  CB    . ALA A 1 812 ? 127.720 135.390 118.365 1.00 95.13  ? 812  ALA A CB    1 
ATOM   5746  N  N     . LEU A 1 813 ? 129.088 133.185 116.580 1.00 102.39 ? 813  LEU A N     1 
ATOM   5747  C  CA    . LEU A 1 813 ? 129.996 132.845 115.489 1.00 102.23 ? 813  LEU A CA    1 
ATOM   5748  C  C     . LEU A 1 813 ? 129.321 131.940 114.467 1.00 100.74 ? 813  LEU A C     1 
ATOM   5749  O  O     . LEU A 1 813 ? 129.476 132.141 113.257 1.00 104.36 ? 813  LEU A O     1 
ATOM   5750  C  CB    . LEU A 1 813 ? 131.258 132.185 116.039 1.00 99.62  ? 813  LEU A CB    1 
ATOM   5751  C  CG    . LEU A 1 813 ? 132.191 133.090 116.839 1.00 103.49 ? 813  LEU A CG    1 
ATOM   5752  C  CD1   . LEU A 1 813 ? 133.431 132.331 117.266 1.00 109.64 ? 813  LEU A CD1   1 
ATOM   5753  C  CD2   . LEU A 1 813 ? 132.563 134.317 116.031 1.00 105.97 ? 813  LEU A CD2   1 
ATOM   5754  N  N     . PHE A 1 814 ? 128.570 130.939 114.930 1.00 95.77  ? 814  PHE A N     1 
ATOM   5755  C  CA    . PHE A 1 814 ? 127.910 130.028 114.007 1.00 98.82  ? 814  PHE A CA    1 
ATOM   5756  C  C     . PHE A 1 814 ? 126.794 130.705 113.231 1.00 101.29 ? 814  PHE A C     1 
ATOM   5757  O  O     . PHE A 1 814 ? 126.523 130.306 112.095 1.00 107.26 ? 814  PHE A O     1 
ATOM   5758  C  CB    . PHE A 1 814 ? 127.360 128.816 114.759 1.00 99.69  ? 814  PHE A CB    1 
ATOM   5759  C  CG    . PHE A 1 814 ? 128.374 127.734 114.982 1.00 109.15 ? 814  PHE A CG    1 
ATOM   5760  C  CD1   . PHE A 1 814 ? 129.641 127.831 114.435 1.00 112.20 ? 814  PHE A CD1   1 
ATOM   5761  C  CD2   . PHE A 1 814 ? 128.060 126.615 115.732 1.00 112.16 ? 814  PHE A CD2   1 
ATOM   5762  C  CE1   . PHE A 1 814 ? 130.576 126.839 114.637 1.00 114.46 ? 814  PHE A CE1   1 
ATOM   5763  C  CE2   . PHE A 1 814 ? 128.992 125.618 115.937 1.00 113.78 ? 814  PHE A CE2   1 
ATOM   5764  C  CZ    . PHE A 1 814 ? 130.251 125.731 115.388 1.00 116.72 ? 814  PHE A CZ    1 
ATOM   5765  N  N     . VAL A 1 815 ? 126.144 131.712 113.804 1.00 96.93  ? 815  VAL A N     1 
ATOM   5766  C  CA    . VAL A 1 815 ? 125.164 132.470 113.037 1.00 95.99  ? 815  VAL A CA    1 
ATOM   5767  C  C     . VAL A 1 815 ? 125.844 133.387 112.030 1.00 101.80 ? 815  VAL A C     1 
ATOM   5768  O  O     . VAL A 1 815 ? 125.438 133.443 110.869 1.00 105.18 ? 815  VAL A O     1 
ATOM   5769  C  CB    . VAL A 1 815 ? 124.237 133.257 113.980 1.00 95.39  ? 815  VAL A CB    1 
ATOM   5770  C  CG1   . VAL A 1 815 ? 123.420 134.258 113.192 1.00 98.27  ? 815  VAL A CG1   1 
ATOM   5771  C  CG2   . VAL A 1 815 ? 123.325 132.308 114.727 1.00 96.88  ? 815  VAL A CG2   1 
ATOM   5772  N  N     . VAL A 1 816 ? 126.904 134.085 112.444 1.00 100.41 ? 816  VAL A N     1 
ATOM   5773  C  CA    . VAL A 1 816 ? 127.574 135.028 111.553 1.00 95.80  ? 816  VAL A CA    1 
ATOM   5774  C  C     . VAL A 1 816 ? 128.177 134.303 110.356 1.00 101.07 ? 816  VAL A C     1 
ATOM   5775  O  O     . VAL A 1 816 ? 128.026 134.736 109.208 1.00 101.44 ? 816  VAL A O     1 
ATOM   5776  C  CB    . VAL A 1 816 ? 128.642 135.823 112.323 1.00 88.37  ? 816  VAL A CB    1 
ATOM   5777  C  CG1   . VAL A 1 816 ? 129.646 136.431 111.365 1.00 92.54  ? 816  VAL A CG1   1 
ATOM   5778  C  CG2   . VAL A 1 816 ? 127.993 136.904 113.160 1.00 98.92  ? 816  VAL A CG2   1 
ATOM   5779  N  N     . TYR A 1 817 ? 128.862 133.186 110.601 1.00 103.18 ? 817  TYR A N     1 
ATOM   5780  C  CA    . TYR A 1 817 ? 129.600 132.526 109.530 1.00 103.96 ? 817  TYR A CA    1 
ATOM   5781  C  C     . TYR A 1 817 ? 128.700 131.664 108.654 1.00 104.27 ? 817  TYR A C     1 
ATOM   5782  O  O     . TYR A 1 817 ? 128.972 131.499 107.461 1.00 112.83 ? 817  TYR A O     1 
ATOM   5783  C  CB    . TYR A 1 817 ? 130.730 131.687 110.123 1.00 104.31 ? 817  TYR A CB    1 
ATOM   5784  C  CG    . TYR A 1 817 ? 131.946 132.501 110.485 1.00 106.38 ? 817  TYR A CG    1 
ATOM   5785  C  CD1   . TYR A 1 817 ? 132.289 133.630 109.758 1.00 110.60 ? 817  TYR A CD1   1 
ATOM   5786  C  CD2   . TYR A 1 817 ? 132.740 132.155 111.565 1.00 106.85 ? 817  TYR A CD2   1 
ATOM   5787  C  CE1   . TYR A 1 817 ? 133.395 134.382 110.087 1.00 110.98 ? 817  TYR A CE1   1 
ATOM   5788  C  CE2   . TYR A 1 817 ? 133.846 132.902 111.902 1.00 113.23 ? 817  TYR A CE2   1 
ATOM   5789  C  CZ    . TYR A 1 817 ? 134.169 134.014 111.160 1.00 113.39 ? 817  TYR A CZ    1 
ATOM   5790  O  OH    . TYR A 1 817 ? 135.272 134.762 111.492 1.00 116.25 ? 817  TYR A OH    1 
ATOM   5791  N  N     . PHE A 1 818 ? 127.631 131.106 109.218 1.00 99.64  ? 818  PHE A N     1 
ATOM   5792  C  CA    . PHE A 1 818 ? 126.809 130.135 108.511 1.00 104.70 ? 818  PHE A CA    1 
ATOM   5793  C  C     . PHE A 1 818 ? 125.378 130.595 108.272 1.00 105.61 ? 818  PHE A C     1 
ATOM   5794  O  O     . PHE A 1 818 ? 124.536 129.771 107.902 1.00 107.19 ? 818  PHE A O     1 
ATOM   5795  C  CB    . PHE A 1 818 ? 126.794 128.807 109.275 1.00 105.01 ? 818  PHE A CB    1 
ATOM   5796  C  CG    . PHE A 1 818 ? 128.138 128.151 109.373 1.00 109.83 ? 818  PHE A CG    1 
ATOM   5797  C  CD1   . PHE A 1 818 ? 129.067 128.293 108.361 1.00 110.01 ? 818  PHE A CD1   1 
ATOM   5798  C  CD2   . PHE A 1 818 ? 128.474 127.394 110.480 1.00 112.59 ? 818  PHE A CD2   1 
ATOM   5799  C  CE1   . PHE A 1 818 ? 130.304 127.690 108.448 1.00 110.29 ? 818  PHE A CE1   1 
ATOM   5800  C  CE2   . PHE A 1 818 ? 129.710 126.790 110.573 1.00 112.46 ? 818  PHE A CE2   1 
ATOM   5801  C  CZ    . PHE A 1 818 ? 130.626 126.939 109.556 1.00 113.27 ? 818  PHE A CZ    1 
ATOM   5802  N  N     . ALA A 1 819 ? 125.070 131.875 108.470 1.00 104.17 ? 819  ALA A N     1 
ATOM   5803  C  CA    . ALA A 1 819 ? 123.721 132.369 108.250 1.00 102.89 ? 819  ALA A CA    1 
ATOM   5804  C  C     . ALA A 1 819 ? 123.774 133.792 107.721 1.00 107.11 ? 819  ALA A C     1 
ATOM   5805  O  O     . ALA A 1 819 ? 124.607 134.598 108.142 1.00 108.89 ? 819  ALA A O     1 
ATOM   5806  C  CB    . ALA A 1 819 ? 122.887 132.320 109.535 1.00 101.05 ? 819  ALA A CB    1 
ATOM   5807  N  N     . SER A 1 820 ? 122.875 134.091 106.794 1.00 110.25 ? 820  SER A N     1 
ATOM   5808  C  CA    . SER A 1 820 ? 122.724 135.429 106.249 1.00 114.91 ? 820  SER A CA    1 
ATOM   5809  C  C     . SER A 1 820 ? 121.589 136.156 106.960 1.00 111.49 ? 820  SER A C     1 
ATOM   5810  O  O     . SER A 1 820 ? 120.800 135.562 107.697 1.00 111.00 ? 820  SER A O     1 
ATOM   5811  C  CB    . SER A 1 820 ? 122.463 135.370 104.741 1.00 120.13 ? 820  SER A CB    1 
ATOM   5812  O  OG    . SER A 1 820 ? 122.605 136.649 104.149 1.00 125.96 ? 820  SER A OG    1 
ATOM   5813  N  N     . SER A 1 821 ? 121.515 137.467 106.729 1.00 109.64 ? 821  SER A N     1 
ATOM   5814  C  CA    . SER A 1 821 ? 120.454 138.256 107.341 1.00 108.54 ? 821  SER A CA    1 
ATOM   5815  C  C     . SER A 1 821 ? 119.079 137.834 106.845 1.00 110.98 ? 821  SER A C     1 
ATOM   5816  O  O     . SER A 1 821 ? 118.083 138.022 107.552 1.00 115.38 ? 821  SER A O     1 
ATOM   5817  C  CB    . SER A 1 821 ? 120.676 139.741 107.070 1.00 115.41 ? 821  SER A CB    1 
ATOM   5818  O  OG    . SER A 1 821 ? 119.572 140.507 107.518 1.00 119.56 ? 821  SER A OG    1 
ATOM   5819  N  N     . SER A 1 822 ? 118.998 137.271 105.641 1.00 110.58 ? 822  SER A N     1 
ATOM   5820  C  CA    . SER A 1 822 ? 117.717 136.840 105.101 1.00 113.88 ? 822  SER A CA    1 
ATOM   5821  C  C     . SER A 1 822 ? 117.258 135.498 105.656 1.00 111.01 ? 822  SER A C     1 
ATOM   5822  O  O     . SER A 1 822 ? 116.069 135.180 105.555 1.00 112.93 ? 822  SER A O     1 
ATOM   5823  C  CB    . SER A 1 822 ? 117.789 136.761 103.576 1.00 120.45 ? 822  SER A CB    1 
ATOM   5824  O  OG    . SER A 1 822 ? 117.979 135.425 103.144 1.00 122.55 ? 822  SER A OG    1 
ATOM   5825  N  N     . THR A 1 823 ? 118.161 134.709 106.237 1.00 106.42 ? 823  THR A N     1 
ATOM   5826  C  CA    . THR A 1 823 ? 117.827 133.376 106.722 1.00 108.60 ? 823  THR A CA    1 
ATOM   5827  C  C     . THR A 1 823 ? 117.875 133.270 108.240 1.00 106.55 ? 823  THR A C     1 
ATOM   5828  O  O     . THR A 1 823 ? 117.609 132.194 108.784 1.00 108.30 ? 823  THR A O     1 
ATOM   5829  C  CB    . THR A 1 823 ? 118.761 132.336 106.101 1.00 113.27 ? 823  THR A CB    1 
ATOM   5830  O  OG1   . THR A 1 823 ? 120.045 132.409 106.731 1.00 113.23 ? 823  THR A OG1   1 
ATOM   5831  C  CG2   . THR A 1 823 ? 118.920 132.585 104.611 1.00 115.33 ? 823  THR A CG2   1 
ATOM   5832  N  N     . TYR A 1 824 ? 118.206 134.350 108.933 1.00 103.78 ? 824  TYR A N     1 
ATOM   5833  C  CA    . TYR A 1 824 ? 118.201 134.383 110.390 1.00 101.25 ? 824  TYR A CA    1 
ATOM   5834  C  C     . TYR A 1 824 ? 117.264 135.428 110.966 1.00 102.58 ? 824  TYR A C     1 
ATOM   5835  O  O     . TYR A 1 824 ? 116.556 135.146 111.937 1.00 103.93 ? 824  TYR A O     1 
ATOM   5836  C  CB    . TYR A 1 824 ? 119.614 134.640 110.923 1.00 95.82  ? 824  TYR A CB    1 
ATOM   5837  C  CG    . TYR A 1 824 ? 119.668 134.793 112.425 1.00 93.25  ? 824  TYR A CG    1 
ATOM   5838  C  CD1   . TYR A 1 824 ? 119.681 133.686 113.258 1.00 91.98  ? 824  TYR A CD1   1 
ATOM   5839  C  CD2   . TYR A 1 824 ? 119.703 136.051 113.009 1.00 96.89  ? 824  TYR A CD2   1 
ATOM   5840  C  CE1   . TYR A 1 824 ? 119.727 133.829 114.630 1.00 94.16  ? 824  TYR A CE1   1 
ATOM   5841  C  CE2   . TYR A 1 824 ? 119.748 136.202 114.377 1.00 99.69  ? 824  TYR A CE2   1 
ATOM   5842  C  CZ    . TYR A 1 824 ? 119.761 135.090 115.182 1.00 98.77  ? 824  TYR A CZ    1 
ATOM   5843  O  OH    . TYR A 1 824 ? 119.808 135.242 116.547 1.00 100.55 ? 824  TYR A OH    1 
ATOM   5844  N  N     . MET A 1 825 ? 117.254 136.633 110.407 1.00 100.87 ? 825  MET A N     1 
ATOM   5845  C  CA    . MET A 1 825 ? 116.396 137.680 110.952 1.00 97.59  ? 825  MET A CA    1 
ATOM   5846  C  C     . MET A 1 825 ? 114.912 137.347 110.877 1.00 98.30  ? 825  MET A C     1 
ATOM   5847  O  O     . MET A 1 825 ? 114.186 137.718 111.814 1.00 100.59 ? 825  MET A O     1 
ATOM   5848  C  CB    . MET A 1 825 ? 116.703 139.018 110.275 1.00 96.31  ? 825  MET A CB    1 
ATOM   5849  C  CG    . MET A 1 825 ? 118.067 139.549 110.648 1.00 100.60 ? 825  MET A CG    1 
ATOM   5850  S  SD    . MET A 1 825 ? 118.253 139.651 112.436 1.00 105.48 ? 825  MET A SD    1 
ATOM   5851  C  CE    . MET A 1 825 ? 117.192 141.035 112.812 1.00 98.57  ? 825  MET A CE    1 
ATOM   5852  N  N     . PRO A 1 826 ? 114.385 136.719 109.819 1.00 98.31  ? 826  PRO A N     1 
ATOM   5853  C  CA    . PRO A 1 826 ? 112.996 136.243 109.908 1.00 97.84  ? 826  PRO A CA    1 
ATOM   5854  C  C     . PRO A 1 826 ? 112.764 135.320 111.091 1.00 98.32  ? 826  PRO A C     1 
ATOM   5855  O  O     . PRO A 1 826 ? 111.724 135.419 111.755 1.00 103.19 ? 826  PRO A O     1 
ATOM   5856  C  CB    . PRO A 1 826 ? 112.790 135.526 108.568 1.00 103.15 ? 826  PRO A CB    1 
ATOM   5857  C  CG    . PRO A 1 826 ? 113.709 136.225 107.642 1.00 104.59 ? 826  PRO A CG    1 
ATOM   5858  C  CD    . PRO A 1 826 ? 114.924 136.559 108.456 1.00 102.65 ? 826  PRO A CD    1 
ATOM   5859  N  N     . VAL A 1 827 ? 113.725 134.446 111.398 1.00 96.93  ? 827  VAL A N     1 
ATOM   5860  C  CA    . VAL A 1 827 ? 113.584 133.555 112.547 1.00 97.22  ? 827  VAL A CA    1 
ATOM   5861  C  C     . VAL A 1 827 ? 113.567 134.351 113.846 1.00 97.75  ? 827  VAL A C     1 
ATOM   5862  O  O     . VAL A 1 827 ? 112.758 134.084 114.744 1.00 102.47 ? 827  VAL A O     1 
ATOM   5863  C  CB    . VAL A 1 827 ? 114.704 132.499 112.545 1.00 94.56  ? 827  VAL A CB    1 
ATOM   5864  C  CG1   . VAL A 1 827 ? 114.700 131.716 113.843 1.00 87.52  ? 827  VAL A CG1   1 
ATOM   5865  C  CG2   . VAL A 1 827 ? 114.541 131.565 111.361 1.00 97.15  ? 827  VAL A CG2   1 
ATOM   5866  N  N     . LEU A 1 828 ? 114.464 135.331 113.975 1.00 93.42  ? 828  LEU A N     1 
ATOM   5867  C  CA    . LEU A 1 828 ? 114.496 136.137 115.192 1.00 94.24  ? 828  LEU A CA    1 
ATOM   5868  C  C     . LEU A 1 828 ? 113.210 136.935 115.362 1.00 97.70  ? 828  LEU A C     1 
ATOM   5869  O  O     . LEU A 1 828 ? 112.667 137.029 116.471 1.00 100.70 ? 828  LEU A O     1 
ATOM   5870  C  CB    . LEU A 1 828 ? 115.700 137.073 115.177 1.00 93.28  ? 828  LEU A CB    1 
ATOM   5871  C  CG    . LEU A 1 828 ? 115.992 137.741 116.518 1.00 87.68  ? 828  LEU A CG    1 
ATOM   5872  C  CD1   . LEU A 1 828 ? 116.407 136.702 117.536 1.00 87.75  ? 828  LEU A CD1   1 
ATOM   5873  C  CD2   . LEU A 1 828 ? 117.065 138.801 116.364 1.00 91.61  ? 828  LEU A CD2   1 
ATOM   5874  N  N     . TYR A 1 829 ? 112.711 137.523 114.273 1.00 95.06  ? 829  TYR A N     1 
ATOM   5875  C  CA    . TYR A 1 829 ? 111.452 138.251 114.338 1.00 93.09  ? 829  TYR A CA    1 
ATOM   5876  C  C     . TYR A 1 829 ? 110.312 137.331 114.740 1.00 98.25  ? 829  TYR A C     1 
ATOM   5877  O  O     . TYR A 1 829 ? 109.476 137.703 115.564 1.00 103.55 ? 829  TYR A O     1 
ATOM   5878  C  CB    . TYR A 1 829 ? 111.151 138.922 112.999 1.00 92.75  ? 829  TYR A CB    1 
ATOM   5879  C  CG    . TYR A 1 829 ? 112.108 140.030 112.625 1.00 97.99  ? 829  TYR A CG    1 
ATOM   5880  C  CD1   . TYR A 1 829 ? 112.887 140.655 113.585 1.00 93.47  ? 829  TYR A CD1   1 
ATOM   5881  C  CD2   . TYR A 1 829 ? 112.226 140.452 111.310 1.00 101.11 ? 829  TYR A CD2   1 
ATOM   5882  C  CE1   . TYR A 1 829 ? 113.757 141.670 113.246 1.00 94.40  ? 829  TYR A CE1   1 
ATOM   5883  C  CE2   . TYR A 1 829 ? 113.095 141.463 110.961 1.00 99.62  ? 829  TYR A CE2   1 
ATOM   5884  C  CZ    . TYR A 1 829 ? 113.858 142.068 111.932 1.00 101.76 ? 829  TYR A CZ    1 
ATOM   5885  O  OH    . TYR A 1 829 ? 114.724 143.077 111.586 1.00 112.12 ? 829  TYR A OH    1 
ATOM   5886  N  N     . ILE A 1 830 ? 110.269 136.119 114.183 1.00 96.40  ? 830  ILE A N     1 
ATOM   5887  C  CA    . ILE A 1 830 ? 109.206 135.185 114.539 1.00 91.48  ? 830  ILE A CA    1 
ATOM   5888  C  C     . ILE A 1 830 ? 109.283 134.818 116.016 1.00 98.28  ? 830  ILE A C     1 
ATOM   5889  O  O     . ILE A 1 830 ? 108.263 134.782 116.713 1.00 104.86 ? 830  ILE A O     1 
ATOM   5890  C  CB    . ILE A 1 830 ? 109.265 133.939 113.637 1.00 90.28  ? 830  ILE A CB    1 
ATOM   5891  C  CG1   . ILE A 1 830 ? 108.736 134.274 112.242 1.00 96.19  ? 830  ILE A CG1   1 
ATOM   5892  C  CG2   . ILE A 1 830 ? 108.483 132.792 114.249 1.00 95.54  ? 830  ILE A CG2   1 
ATOM   5893  C  CD1   . ILE A 1 830 ? 108.856 133.138 111.251 1.00 99.39  ? 830  ILE A CD1   1 
ATOM   5894  N  N     . PHE A 1 831 ? 110.489 134.551 116.520 1.00 98.20  ? 831  PHE A N     1 
ATOM   5895  C  CA    . PHE A 1 831 ? 110.630 134.145 117.916 1.00 101.92 ? 831  PHE A CA    1 
ATOM   5896  C  C     . PHE A 1 831 ? 110.208 135.266 118.862 1.00 104.74 ? 831  PHE A C     1 
ATOM   5897  O  O     . PHE A 1 831 ? 109.416 135.051 119.794 1.00 106.97 ? 831  PHE A O     1 
ATOM   5898  C  CB    . PHE A 1 831 ? 112.073 133.719 118.191 1.00 99.00  ? 831  PHE A CB    1 
ATOM   5899  C  CG    . PHE A 1 831 ? 112.226 132.816 119.382 1.00 105.35 ? 831  PHE A CG    1 
ATOM   5900  C  CD1   . PHE A 1 831 ? 112.176 133.320 120.669 1.00 107.79 ? 831  PHE A CD1   1 
ATOM   5901  C  CD2   . PHE A 1 831 ? 112.420 131.457 119.208 1.00 108.55 ? 831  PHE A CD2   1 
ATOM   5902  C  CE1   . PHE A 1 831 ? 112.316 132.483 121.758 1.00 113.52 ? 831  PHE A CE1   1 
ATOM   5903  C  CE2   . PHE A 1 831 ? 112.562 130.618 120.293 1.00 116.12 ? 831  PHE A CE2   1 
ATOM   5904  C  CZ    . PHE A 1 831 ? 112.511 131.131 121.569 1.00 117.14 ? 831  PHE A CZ    1 
ATOM   5905  N  N     . VAL A 1 832 ? 110.725 136.477 118.636 1.00 101.59 ? 832  VAL A N     1 
ATOM   5906  C  CA    . VAL A 1 832 ? 110.379 137.599 119.505 1.00 98.10  ? 832  VAL A CA    1 
ATOM   5907  C  C     . VAL A 1 832 ? 108.900 137.936 119.374 1.00 98.85  ? 832  VAL A C     1 
ATOM   5908  O  O     . VAL A 1 832 ? 108.241 138.296 120.356 1.00 105.48 ? 832  VAL A O     1 
ATOM   5909  C  CB    . VAL A 1 832 ? 111.272 138.815 119.196 1.00 96.74  ? 832  VAL A CB    1 
ATOM   5910  C  CG1   . VAL A 1 832 ? 110.760 140.043 119.912 1.00 97.79  ? 832  VAL A CG1   1 
ATOM   5911  C  CG2   . VAL A 1 832 ? 112.704 138.534 119.592 1.00 99.47  ? 832  VAL A CG2   1 
ATOM   5912  N  N     . ALA A 1 833 ? 108.354 137.818 118.162 1.00 96.33  ? 833  ALA A N     1 
ATOM   5913  C  CA    . ALA A 1 833 ? 106.935 138.062 117.953 1.00 98.38  ? 833  ALA A CA    1 
ATOM   5914  C  C     . ALA A 1 833 ? 106.090 137.066 118.727 1.00 100.73 ? 833  ALA A C     1 
ATOM   5915  O  O     . ALA A 1 833 ? 105.054 137.431 119.285 1.00 105.50 ? 833  ALA A O     1 
ATOM   5916  C  CB    . ALA A 1 833 ? 106.609 137.999 116.460 1.00 99.41  ? 833  ALA A CB    1 
ATOM   5917  N  N     . SER A 1 834 ? 106.516 135.803 118.772 1.00 95.87  ? 834  SER A N     1 
ATOM   5918  C  CA    . SER A 1 834 ? 105.788 134.795 119.537 1.00 98.97  ? 834  SER A CA    1 
ATOM   5919  C  C     . SER A 1 834 ? 105.827 135.105 121.028 1.00 104.05 ? 834  SER A C     1 
ATOM   5920  O  O     . SER A 1 834 ? 104.804 135.024 121.723 1.00 110.64 ? 834  SER A O     1 
ATOM   5921  C  CB    . SER A 1 834 ? 106.370 133.410 119.254 1.00 102.34 ? 834  SER A CB    1 
ATOM   5922  O  OG    . SER A 1 834 ? 105.820 132.437 120.120 1.00 119.46 ? 834  SER A OG    1 
ATOM   5923  N  N     . LEU A 1 835 ? 107.002 135.475 121.537 1.00 100.71 ? 835  LEU A N     1 
ATOM   5924  C  CA    . LEU A 1 835 ? 107.103 135.815 122.954 1.00 101.65 ? 835  LEU A CA    1 
ATOM   5925  C  C     . LEU A 1 835 ? 106.219 137.010 123.299 1.00 104.40 ? 835  LEU A C     1 
ATOM   5926  O  O     . LEU A 1 835 ? 105.490 136.998 124.301 1.00 109.12 ? 835  LEU A O     1 
ATOM   5927  C  CB    . LEU A 1 835 ? 108.557 136.093 123.323 1.00 97.64  ? 835  LEU A CB    1 
ATOM   5928  C  CG    . LEU A 1 835 ? 109.428 134.856 123.511 1.00 101.68 ? 835  LEU A CG    1 
ATOM   5929  C  CD1   . LEU A 1 835 ? 110.794 135.252 124.045 1.00 105.49 ? 835  LEU A CD1   1 
ATOM   5930  C  CD2   . LEU A 1 835 ? 108.740 133.867 124.440 1.00 100.74 ? 835  LEU A CD2   1 
ATOM   5931  N  N     . ASN A 1 836 ? 106.261 138.052 122.472 1.00 100.07 ? 836  ASN A N     1 
ATOM   5932  C  CA    . ASN A 1 836 ? 105.441 139.223 122.750 1.00 95.82  ? 836  ASN A CA    1 
ATOM   5933  C  C     . ASN A 1 836 ? 103.961 138.946 122.518 1.00 97.65  ? 836  ASN A C     1 
ATOM   5934  O  O     . ASN A 1 836 ? 103.119 139.573 123.158 1.00 101.08 ? 836  ASN A O     1 
ATOM   5935  C  CB    . ASN A 1 836 ? 105.917 140.414 121.923 1.00 98.58  ? 836  ASN A CB    1 
ATOM   5936  C  CG    . ASN A 1 836 ? 107.127 141.088 122.533 1.00 100.21 ? 836  ASN A CG    1 
ATOM   5937  O  OD1   . ASN A 1 836 ? 107.754 140.558 123.446 1.00 100.24 ? 836  ASN A OD1   1 
ATOM   5938  N  ND2   . ASN A 1 836 ? 107.462 142.268 122.026 1.00 105.42 ? 836  ASN A ND2   1 
ATOM   5939  N  N     . THR A 1 837 ? 103.622 138.005 121.638 1.00 94.33  ? 837  THR A N     1 
ATOM   5940  C  CA    . THR A 1 837 ? 102.231 137.607 121.492 1.00 92.81  ? 837  THR A CA    1 
ATOM   5941  C  C     . THR A 1 837 ? 101.735 136.952 122.768 1.00 97.92  ? 837  THR A C     1 
ATOM   5942  O  O     . THR A 1 837 ? 100.631 137.249 123.244 1.00 102.31 ? 837  THR A O     1 
ATOM   5943  C  CB    . THR A 1 837 ? 102.072 136.647 120.315 1.00 98.02  ? 837  THR A CB    1 
ATOM   5944  O  OG1   . THR A 1 837 ? 102.552 137.252 119.128 1.00 105.76 ? 837  THR A OG1   1 
ATOM   5945  C  CG2   . THR A 1 837 ? 100.603 136.274 120.141 1.00 100.56 ? 837  THR A CG2   1 
ATOM   5946  N  N     . CYS A 1 838 ? 102.545 136.057 123.340 1.00 97.84  ? 838  CYS A N     1 
ATOM   5947  C  CA    . CYS A 1 838 ? 102.160 135.415 124.591 1.00 95.74  ? 838  CYS A CA    1 
ATOM   5948  C  C     . CYS A 1 838 ? 102.011 136.441 125.706 1.00 97.14  ? 838  CYS A C     1 
ATOM   5949  O  O     . CYS A 1 838 ? 101.039 136.401 126.468 1.00 103.49 ? 838  CYS A O     1 
ATOM   5950  C  CB    . CYS A 1 838 ? 103.181 134.344 124.971 1.00 97.61  ? 838  CYS A CB    1 
ATOM   5951  S  SG    . CYS A 1 838 ? 102.604 133.231 126.279 1.00 129.30 ? 838  CYS A SG    1 
ATOM   5952  N  N     . ARG A 1 839 ? 102.946 137.391 125.798 1.00 92.99  ? 839  ARG A N     1 
ATOM   5953  C  CA    . ARG A 1 839 ? 102.857 138.392 126.860 1.00 91.28  ? 839  ARG A CA    1 
ATOM   5954  C  C     . ARG A 1 839 ? 101.673 139.335 126.652 1.00 93.41  ? 839  ARG A C     1 
ATOM   5955  O  O     . ARG A 1 839 ? 101.007 139.727 127.618 1.00 96.84  ? 839  ARG A O     1 
ATOM   5956  C  CB    . ARG A 1 839 ? 104.167 139.169 126.963 1.00 95.26  ? 839  ARG A CB    1 
ATOM   5957  C  CG    . ARG A 1 839 ? 105.306 138.331 127.516 1.00 101.39 ? 839  ARG A CG    1 
ATOM   5958  C  CD    . ARG A 1 839 ? 106.660 138.874 127.119 1.00 108.82 ? 839  ARG A CD    1 
ATOM   5959  N  NE    . ARG A 1 839 ? 107.010 140.060 127.889 1.00 111.82 ? 839  ARG A NE    1 
ATOM   5960  C  CZ    . ARG A 1 839 ? 108.119 140.764 127.715 1.00 109.29 ? 839  ARG A CZ    1 
ATOM   5961  N  NH1   . ARG A 1 839 ? 109.010 140.434 126.796 1.00 111.19 ? 839  ARG A NH1   1 
ATOM   5962  N  NH2   . ARG A 1 839 ? 108.341 141.825 128.486 1.00 112.95 ? 839  ARG A NH2   1 
ATOM   5963  N  N     . LEU A 1 840 ? 101.387 139.706 125.403 1.00 93.93  ? 840  LEU A N     1 
ATOM   5964  C  CA    . LEU A 1 840 ? 100.232 140.551 125.125 1.00 91.70  ? 840  LEU A CA    1 
ATOM   5965  C  C     . LEU A 1 840 ? 98.933  139.835 125.456 1.00 97.58  ? 840  LEU A C     1 
ATOM   5966  O  O     . LEU A 1 840 ? 98.013  140.437 126.023 1.00 102.49 ? 840  LEU A O     1 
ATOM   5967  C  CB    . LEU A 1 840 ? 100.235 140.974 123.661 1.00 91.87  ? 840  LEU A CB    1 
ATOM   5968  C  CG    . LEU A 1 840 ? 99.067  141.845 123.211 1.00 93.98  ? 840  LEU A CG    1 
ATOM   5969  C  CD1   . LEU A 1 840 ? 98.985  143.085 124.076 1.00 95.35  ? 840  LEU A CD1   1 
ATOM   5970  C  CD2   . LEU A 1 840 ? 99.201  142.215 121.743 1.00 95.78  ? 840  LEU A CD2   1 
ATOM   5971  N  N     . LEU A 1 841 ? 98.831  138.556 125.092 1.00 95.62  ? 841  LEU A N     1 
ATOM   5972  C  CA    . LEU A 1 841 ? 97.640  137.790 125.429 1.00 92.85  ? 841  LEU A CA    1 
ATOM   5973  C  C     . LEU A 1 841 ? 97.489  137.669 126.937 1.00 98.74  ? 841  LEU A C     1 
ATOM   5974  O  O     . LEU A 1 841 ? 96.373  137.740 127.462 1.00 107.84 ? 841  LEU A O     1 
ATOM   5975  C  CB    . LEU A 1 841 ? 97.698  136.412 124.775 1.00 89.17  ? 841  LEU A CB    1 
ATOM   5976  C  CG    . LEU A 1 841 ? 97.408  136.413 123.276 1.00 90.17  ? 841  LEU A CG    1 
ATOM   5977  C  CD1   . LEU A 1 841 ? 97.469  135.004 122.712 1.00 94.31  ? 841  LEU A CD1   1 
ATOM   5978  C  CD2   . LEU A 1 841 ? 96.059  137.051 122.999 1.00 89.60  ? 841  LEU A CD2   1 
ATOM   5979  N  N     . GLY A 1 842 ? 98.602  137.501 127.651 1.00 94.66  ? 842  GLY A N     1 
ATOM   5980  C  CA    . GLY A 1 842 ? 98.535  137.479 129.101 1.00 95.86  ? 842  GLY A CA    1 
ATOM   5981  C  C     . GLY A 1 842 ? 98.027  138.783 129.686 1.00 98.47  ? 842  GLY A C     1 
ATOM   5982  O  O     . GLY A 1 842 ? 97.189  138.784 130.589 1.00 105.40 ? 842  GLY A O     1 
ATOM   5983  N  N     . SER A 1 843 ? 98.528  139.913 129.183 1.00 95.99  ? 843  SER A N     1 
ATOM   5984  C  CA    . SER A 1 843 ? 98.066  141.201 129.693 1.00 99.70  ? 843  SER A CA    1 
ATOM   5985  C  C     . SER A 1 843 ? 96.588  141.421 129.387 1.00 104.06 ? 843  SER A C     1 
ATOM   5986  O  O     . SER A 1 843 ? 95.836  141.916 130.238 1.00 111.16 ? 843  SER A O     1 
ATOM   5987  C  CB    . SER A 1 843 ? 98.908  142.334 129.115 1.00 102.25 ? 843  SER A CB    1 
ATOM   5988  O  OG    . SER A 1 843 ? 98.431  143.587 129.569 1.00 101.06 ? 843  SER A OG    1 
ATOM   5989  N  N     . ILE A 1 844 ? 96.152  141.054 128.179 1.00 98.36  ? 844  ILE A N     1 
ATOM   5990  C  CA    . ILE A 1 844 ? 94.739  141.182 127.830 1.00 98.88  ? 844  ILE A CA    1 
ATOM   5991  C  C     . ILE A 1 844 ? 93.888  140.312 128.742 1.00 105.90 ? 844  ILE A C     1 
ATOM   5992  O  O     . ILE A 1 844 ? 92.825  140.734 129.216 1.00 112.57 ? 844  ILE A O     1 
ATOM   5993  C  CB    . ILE A 1 844 ? 94.511  140.830 126.348 1.00 102.11 ? 844  ILE A CB    1 
ATOM   5994  C  CG1   . ILE A 1 844 ? 95.043  141.934 125.437 1.00 99.11  ? 844  ILE A CG1   1 
ATOM   5995  C  CG2   . ILE A 1 844 ? 93.038  140.593 126.074 1.00 107.21 ? 844  ILE A CG2   1 
ATOM   5996  C  CD1   . ILE A 1 844 ? 95.622  141.423 124.146 1.00 96.30  ? 844  ILE A CD1   1 
ATOM   5997  N  N     . GLY A 1 845 ? 94.337  139.081 128.996 1.00 103.04 ? 845  GLY A N     1 
ATOM   5998  C  CA    . GLY A 1 845 ? 93.594  138.200 129.878 1.00 107.60 ? 845  GLY A CA    1 
ATOM   5999  C  C     . GLY A 1 845 ? 93.501  138.737 131.291 1.00 111.66 ? 845  GLY A C     1 
ATOM   6000  O  O     . GLY A 1 845 ? 92.453  138.647 131.930 1.00 118.76 ? 845  GLY A O     1 
ATOM   6001  N  N     . HIS A 1 846 ? 94.595  139.308 131.797 1.00 105.33 ? 846  HIS A N     1 
ATOM   6002  C  CA    . HIS A 1 846 ? 94.563  139.891 133.134 1.00 106.51 ? 846  HIS A CA    1 
ATOM   6003  C  C     . HIS A 1 846 ? 93.592  141.063 133.201 1.00 113.71 ? 846  HIS A C     1 
ATOM   6004  O  O     . HIS A 1 846 ? 92.808  141.177 134.153 1.00 121.68 ? 846  HIS A O     1 
ATOM   6005  C  CB    . HIS A 1 846 ? 95.969  140.321 133.543 1.00 105.43 ? 846  HIS A CB    1 
ATOM   6006  C  CG    . HIS A 1 846 ? 96.074  140.800 134.956 1.00 107.09 ? 846  HIS A CG    1 
ATOM   6007  N  ND1   . HIS A 1 846 ? 96.725  140.085 135.937 1.00 105.32 ? 846  HIS A ND1   1 
ATOM   6008  C  CD2   . HIS A 1 846 ? 95.634  141.935 135.548 1.00 112.22 ? 846  HIS A CD2   1 
ATOM   6009  C  CE1   . HIS A 1 846 ? 96.668  140.749 137.076 1.00 106.60 ? 846  HIS A CE1   1 
ATOM   6010  N  NE2   . HIS A 1 846 ? 96.013  141.876 136.867 1.00 109.37 ? 846  HIS A NE2   1 
ATOM   6011  N  N     . TRP A 1 847 ? 93.620  141.938 132.193 1.00 110.70 ? 847  TRP A N     1 
ATOM   6012  C  CA    . TRP A 1 847 ? 92.697  143.069 132.182 1.00 111.55 ? 847  TRP A CA    1 
ATOM   6013  C  C     . TRP A 1 847 ? 91.247  142.606 132.135 1.00 118.17 ? 847  TRP A C     1 
ATOM   6014  O  O     . TRP A 1 847 ? 90.402  143.108 132.890 1.00 123.06 ? 847  TRP A O     1 
ATOM   6015  C  CB    . TRP A 1 847 ? 93.000  143.986 130.998 1.00 112.83 ? 847  TRP A CB    1 
ATOM   6016  C  CG    . TRP A 1 847 ? 92.116  145.189 130.938 1.00 114.38 ? 847  TRP A CG    1 
ATOM   6017  C  CD1   . TRP A 1 847 ? 92.353  146.409 131.496 1.00 113.85 ? 847  TRP A CD1   1 
ATOM   6018  C  CD2   . TRP A 1 847 ? 90.849  145.287 130.280 1.00 118.88 ? 847  TRP A CD2   1 
ATOM   6019  N  NE1   . TRP A 1 847 ? 91.311  147.262 131.227 1.00 114.59 ? 847  TRP A NE1   1 
ATOM   6020  C  CE2   . TRP A 1 847 ? 90.375  146.596 130.482 1.00 119.34 ? 847  TRP A CE2   1 
ATOM   6021  C  CE3   . TRP A 1 847 ? 90.069  144.395 129.540 1.00 120.75 ? 847  TRP A CE3   1 
ATOM   6022  C  CZ2   . TRP A 1 847 ? 89.156  147.035 129.971 1.00 123.07 ? 847  TRP A CZ2   1 
ATOM   6023  C  CZ3   . TRP A 1 847 ? 88.861  144.830 129.035 1.00 120.10 ? 847  TRP A CZ3   1 
ATOM   6024  C  CH2   . TRP A 1 847 ? 88.416  146.138 129.252 1.00 122.16 ? 847  TRP A CH2   1 
ATOM   6025  N  N     . VAL A 1 848 ? 90.934  141.652 131.252 1.00 115.03 ? 848  VAL A N     1 
ATOM   6026  C  CA    . VAL A 1 848 ? 89.548  141.212 131.126 1.00 115.63 ? 848  VAL A CA    1 
ATOM   6027  C  C     . VAL A 1 848 ? 89.111  140.483 132.388 1.00 118.80 ? 848  VAL A C     1 
ATOM   6028  O  O     . VAL A 1 848 ? 87.964  140.609 132.824 1.00 126.30 ? 848  VAL A O     1 
ATOM   6029  C  CB    . VAL A 1 848 ? 89.346  140.355 129.860 1.00 115.98 ? 848  VAL A CB    1 
ATOM   6030  C  CG1   . VAL A 1 848 ? 90.156  139.081 129.914 1.00 115.19 ? 848  VAL A CG1   1 
ATOM   6031  C  CG2   . VAL A 1 848 ? 87.872  140.046 129.661 1.00 124.23 ? 848  VAL A CG2   1 
ATOM   6032  N  N     . TYR A 1 849 ? 90.020  139.729 133.012 1.00 118.58 ? 849  TYR A N     1 
ATOM   6033  C  CA    . TYR A 1 849 ? 89.692  139.085 134.277 1.00 126.28 ? 849  TYR A CA    1 
ATOM   6034  C  C     . TYR A 1 849 ? 89.351  140.113 135.345 1.00 129.02 ? 849  TYR A C     1 
ATOM   6035  O  O     . TYR A 1 849 ? 88.334  139.983 136.037 1.00 137.13 ? 849  TYR A O     1 
ATOM   6036  C  CB    . TYR A 1 849 ? 90.852  138.204 134.734 1.00 121.66 ? 849  TYR A CB    1 
ATOM   6037  C  CG    . TYR A 1 849 ? 90.776  137.816 136.189 1.00 122.29 ? 849  TYR A CG    1 
ATOM   6038  C  CD1   . TYR A 1 849 ? 89.813  136.928 136.642 1.00 126.82 ? 849  TYR A CD1   1 
ATOM   6039  C  CD2   . TYR A 1 849 ? 91.671  138.337 137.111 1.00 119.81 ? 849  TYR A CD2   1 
ATOM   6040  C  CE1   . TYR A 1 849 ? 89.740  136.572 137.973 1.00 126.81 ? 849  TYR A CE1   1 
ATOM   6041  C  CE2   . TYR A 1 849 ? 91.607  137.986 138.441 1.00 122.33 ? 849  TYR A CE2   1 
ATOM   6042  C  CZ    . TYR A 1 849 ? 90.640  137.103 138.867 1.00 125.68 ? 849  TYR A CZ    1 
ATOM   6043  O  OH    . TYR A 1 849 ? 90.570  136.750 140.193 1.00 124.23 ? 849  TYR A OH    1 
ATOM   6044  N  N     . ILE A 1 850 ? 90.175  141.155 135.477 1.00 121.60 ? 850  ILE A N     1 
ATOM   6045  C  CA    . ILE A 1 850 ? 89.914  142.162 136.501 1.00 122.32 ? 850  ILE A CA    1 
ATOM   6046  C  C     . ILE A 1 850 ? 88.591  142.872 136.242 1.00 130.93 ? 850  ILE A C     1 
ATOM   6047  O  O     . ILE A 1 850 ? 87.794  143.065 137.168 1.00 135.06 ? 850  ILE A O     1 
ATOM   6048  C  CB    . ILE A 1 850 ? 91.081  143.162 136.587 1.00 119.15 ? 850  ILE A CB    1 
ATOM   6049  C  CG1   . ILE A 1 850 ? 92.141  142.658 137.559 1.00 114.59 ? 850  ILE A CG1   1 
ATOM   6050  C  CG2   . ILE A 1 850 ? 90.595  144.519 137.057 1.00 124.35 ? 850  ILE A CG2   1 
ATOM   6051  C  CD1   . ILE A 1 850 ? 93.336  143.569 137.659 1.00 112.06 ? 850  ILE A CD1   1 
ATOM   6052  N  N     . HIS A 1 851 ? 88.318  143.252 134.995 1.00 128.76 ? 851  HIS A N     1 
ATOM   6053  C  CA    . HIS A 1 851 ? 87.132  144.039 134.685 1.00 129.00 ? 851  HIS A CA    1 
ATOM   6054  C  C     . HIS A 1 851 ? 85.883  143.194 134.454 1.00 137.03 ? 851  HIS A C     1 
ATOM   6055  O  O     . HIS A 1 851 ? 84.801  143.755 134.259 1.00 144.03 ? 851  HIS A O     1 
ATOM   6056  C  CB    . HIS A 1 851 ? 87.391  144.927 133.469 1.00 127.22 ? 851  HIS A CB    1 
ATOM   6057  C  CG    . HIS A 1 851 ? 88.186  146.155 133.780 1.00 127.35 ? 851  HIS A CG    1 
ATOM   6058  N  ND1   . HIS A 1 851 ? 89.328  146.127 134.549 1.00 124.49 ? 851  HIS A ND1   1 
ATOM   6059  C  CD2   . HIS A 1 851 ? 88.001  147.450 133.430 1.00 131.68 ? 851  HIS A CD2   1 
ATOM   6060  C  CE1   . HIS A 1 851 ? 89.814  147.350 134.659 1.00 125.54 ? 851  HIS A CE1   1 
ATOM   6061  N  NE2   . HIS A 1 851 ? 89.028  148.171 133.988 1.00 132.05 ? 851  HIS A NE2   1 
ATOM   6062  N  N     . THR A 1 852 ? 85.998  141.871 134.473 1.00 136.43 ? 852  THR A N     1 
ATOM   6063  C  CA    . THR A 1 852 ? 84.851  141.009 134.221 1.00 141.87 ? 852  THR A CA    1 
ATOM   6064  C  C     . THR A 1 852 ? 84.467  140.149 135.412 1.00 152.25 ? 852  THR A C     1 
ATOM   6065  O  O     . THR A 1 852 ? 83.281  139.858 135.594 1.00 164.33 ? 852  THR A O     1 
ATOM   6066  C  CB    . THR A 1 852 ? 85.141  140.106 133.010 1.00 139.52 ? 852  THR A CB    1 
ATOM   6067  O  OG1   . THR A 1 852 ? 85.509  140.917 131.888 1.00 139.79 ? 852  THR A OG1   1 
ATOM   6068  C  CG2   . THR A 1 852 ? 83.921  139.276 132.640 1.00 147.00 ? 852  THR A CG2   1 
ATOM   6069  N  N     . GLU A 1 853 ? 85.433  139.744 136.241 1.00 149.30 ? 853  GLU A N     1 
ATOM   6070  C  CA    . GLU A 1 853 ? 85.131  138.821 137.329 1.00 159.25 ? 853  GLU A CA    1 
ATOM   6071  C  C     . GLU A 1 853 ? 84.122  139.395 138.316 1.00 164.50 ? 853  GLU A C     1 
ATOM   6072  O  O     . GLU A 1 853 ? 83.393  138.628 138.955 1.00 165.68 ? 853  GLU A O     1 
ATOM   6073  C  CB    . GLU A 1 853 ? 86.420  138.431 138.056 1.00 150.70 ? 853  GLU A CB    1 
ATOM   6074  C  CG    . GLU A 1 853 ? 86.275  137.219 138.960 1.00 151.87 ? 853  GLU A CG    1 
ATOM   6075  C  CD    . GLU A 1 853 ? 85.865  135.974 138.197 1.00 149.63 ? 853  GLU A CD    1 
ATOM   6076  O  OE1   . GLU A 1 853 ? 86.272  135.830 137.026 1.00 144.90 ? 853  GLU A OE1   1 
ATOM   6077  O  OE2   . GLU A 1 853 ? 85.128  135.142 138.766 1.00 153.17 ? 853  GLU A OE2   1 
ATOM   6078  N  N     . GLY A 1 854 ? 84.056  140.720 138.449 1.00 162.34 ? 854  GLY A N     1 
ATOM   6079  C  CA    . GLY A 1 854 ? 83.075  141.312 139.344 1.00 167.07 ? 854  GLY A CA    1 
ATOM   6080  C  C     . GLY A 1 854 ? 81.646  141.039 138.916 1.00 173.38 ? 854  GLY A C     1 
ATOM   6081  O  O     . GLY A 1 854 ? 80.804  140.662 139.735 1.00 172.55 ? 854  GLY A O     1 
ATOM   6082  N  N     . LEU A 1 855 ? 81.351  141.220 137.626 1.00 177.63 ? 855  LEU A N     1 
ATOM   6083  C  CA    . LEU A 1 855 ? 79.988  141.013 137.148 1.00 183.35 ? 855  LEU A CA    1 
ATOM   6084  C  C     . LEU A 1 855 ? 79.633  139.532 137.106 1.00 185.47 ? 855  LEU A C     1 
ATOM   6085  O  O     . LEU A 1 855 ? 78.488  139.154 137.380 1.00 190.00 ? 855  LEU A O     1 
ATOM   6086  C  CB    . LEU A 1 855 ? 79.808  141.652 135.770 1.00 183.61 ? 855  LEU A CB    1 
ATOM   6087  C  CG    . LEU A 1 855 ? 78.404  141.608 135.158 1.00 186.92 ? 855  LEU A CG    1 
ATOM   6088  C  CD1   . LEU A 1 855 ? 78.060  142.939 134.510 1.00 179.04 ? 855  LEU A CD1   1 
ATOM   6089  C  CD2   . LEU A 1 855 ? 78.280  140.477 134.145 1.00 189.63 ? 855  LEU A CD2   1 
ATOM   6090  N  N     . ARG A 1 856 ? 80.599  138.676 136.766 1.00 181.48 ? 856  ARG A N     1 
ATOM   6091  C  CA    . ARG A 1 856 ? 80.374  137.239 136.686 1.00 185.40 ? 856  ARG A CA    1 
ATOM   6092  C  C     . ARG A 1 856 ? 80.766  136.521 137.973 1.00 184.59 ? 856  ARG A C     1 
ATOM   6093  O  O     . ARG A 1 856 ? 81.185  135.359 137.936 1.00 183.35 ? 856  ARG A O     1 
ATOM   6094  C  CB    . ARG A 1 856 ? 81.125  136.643 135.495 1.00 184.30 ? 856  ARG A CB    1 
ATOM   6095  C  CG    . ARG A 1 856 ? 80.389  135.489 134.829 1.00 195.22 ? 856  ARG A CG    1 
ATOM   6096  C  CD    . ARG A 1 856 ? 81.302  134.670 133.932 1.00 200.48 ? 856  ARG A CD    1 
ATOM   6097  N  NE    . ARG A 1 856 ? 80.687  133.401 133.558 1.00 204.44 ? 856  ARG A NE    1 
ATOM   6098  C  CZ    . ARG A 1 856 ? 81.322  132.407 132.954 1.00 202.67 ? 856  ARG A CZ    1 
ATOM   6099  N  NH1   . ARG A 1 856 ? 82.605  132.494 132.642 1.00 197.22 ? 856  ARG A NH1   1 
ATOM   6100  N  NH2   . ARG A 1 856 ? 80.654  131.296 132.656 1.00 204.12 ? 856  ARG A NH2   1 
ATOM   6101  N  N     . GLY A 1 857 ? 80.646  137.198 139.117 1.00 187.15 ? 857  GLY A N     1 
ATOM   6102  C  CA    . GLY A 1 857 ? 80.922  136.556 140.389 1.00 189.65 ? 857  GLY A CA    1 
ATOM   6103  C  C     . GLY A 1 857 ? 79.862  135.565 140.821 1.00 194.93 ? 857  GLY A C     1 
ATOM   6104  O  O     . GLY A 1 857 ? 80.165  134.649 141.592 1.00 194.46 ? 857  GLY A O     1 
ATOM   6105  N  N     . ARG A 1 858 ? 78.624  135.730 140.347 1.00 195.08 ? 858  ARG A N     1 
ATOM   6106  C  CA    . ARG A 1 858 ? 77.573  134.776 140.687 1.00 195.49 ? 858  ARG A CA    1 
ATOM   6107  C  C     . ARG A 1 858 ? 77.864  133.403 140.094 1.00 195.38 ? 858  ARG A C     1 
ATOM   6108  O  O     . ARG A 1 858 ? 77.619  132.377 140.739 1.00 194.18 ? 858  ARG A O     1 
ATOM   6109  C  CB    . ARG A 1 858 ? 76.214  135.288 140.206 1.00 195.81 ? 858  ARG A CB    1 
ATOM   6110  C  CG    . ARG A 1 858 ? 76.234  135.938 138.833 1.00 195.27 ? 858  ARG A CG    1 
ATOM   6111  C  CD    . ARG A 1 858 ? 74.915  136.634 138.537 1.00 199.41 ? 858  ARG A CD    1 
ATOM   6112  N  NE    . ARG A 1 858 ? 75.000  137.504 137.370 1.00 202.91 ? 858  ARG A NE    1 
ATOM   6113  C  CZ    . ARG A 1 858 ? 74.006  138.261 136.926 1.00 205.85 ? 858  ARG A CZ    1 
ATOM   6114  N  NH1   . ARG A 1 858 ? 72.829  138.282 137.531 1.00 208.19 ? 858  ARG A NH1   1 
ATOM   6115  N  NH2   . ARG A 1 858 ? 74.197  139.015 135.848 1.00 203.48 ? 858  ARG A NH2   1 
ATOM   6116  N  N     . VAL A 1 859 ? 78.382  133.365 138.871 1.00 195.49 ? 859  VAL A N     1 
ATOM   6117  C  CA    . VAL A 1 859 ? 78.683  132.107 138.203 1.00 196.05 ? 859  VAL A CA    1 
ATOM   6118  C  C     . VAL A 1 859 ? 80.183  131.839 138.228 1.00 192.21 ? 859  VAL A C     1 
ATOM   6119  O  O     . VAL A 1 859 ? 80.637  130.844 138.793 1.00 185.91 ? 859  VAL A O     1 
ATOM   6120  C  CB    . VAL A 1 859 ? 78.156  132.108 136.760 1.00 198.62 ? 859  VAL A CB    1 
ATOM   6121  C  CG1   . VAL A 1 859 ? 78.473  130.785 136.079 1.00 200.70 ? 859  VAL A CG1   1 
ATOM   6122  C  CG2   . VAL A 1 859 ? 76.659  132.383 136.742 1.00 197.03 ? 859  VAL A CG2   1 
ATOM   6123  N  N     . HIS B 1 23  ? 86.942  129.547 164.865 1.00 191.67 ? 23   HIS B N     1 
ATOM   6124  C  CA    . HIS B 1 23  ? 87.489  130.258 166.014 1.00 189.79 ? 23   HIS B CA    1 
ATOM   6125  C  C     . HIS B 1 23  ? 87.904  129.280 167.105 1.00 187.19 ? 23   HIS B C     1 
ATOM   6126  O  O     . HIS B 1 23  ? 88.642  129.636 168.022 1.00 184.82 ? 23   HIS B O     1 
ATOM   6127  C  CB    . HIS B 1 23  ? 86.471  131.258 166.564 1.00 194.08 ? 23   HIS B CB    1 
ATOM   6128  C  CG    . HIS B 1 23  ? 85.943  132.210 165.536 1.00 199.83 ? 23   HIS B CG    1 
ATOM   6129  N  ND1   . HIS B 1 23  ? 86.522  133.437 165.290 1.00 201.38 ? 23   HIS B ND1   1 
ATOM   6130  C  CD2   . HIS B 1 23  ? 84.888  132.116 164.692 1.00 200.57 ? 23   HIS B CD2   1 
ATOM   6131  C  CE1   . HIS B 1 23  ? 85.847  134.056 164.338 1.00 200.65 ? 23   HIS B CE1   1 
ATOM   6132  N  NE2   . HIS B 1 23  ? 84.851  133.277 163.958 1.00 199.38 ? 23   HIS B NE2   1 
ATOM   6133  N  N     . ALA B 1 24  ? 87.412  128.045 167.002 1.00 188.53 ? 24   ALA B N     1 
ATOM   6134  C  CA    . ALA B 1 24  ? 87.759  127.022 167.987 1.00 183.94 ? 24   ALA B CA    1 
ATOM   6135  C  C     . ALA B 1 24  ? 89.256  126.739 168.050 1.00 184.26 ? 24   ALA B C     1 
ATOM   6136  O  O     . ALA B 1 24  ? 89.792  126.645 169.168 1.00 183.14 ? 24   ALA B O     1 
ATOM   6137  C  CB    . ALA B 1 24  ? 86.955  125.747 167.710 1.00 179.83 ? 24   ALA B CB    1 
ATOM   6138  N  N     . PRO B 1 25  ? 89.982  126.572 166.933 1.00 184.03 ? 25   PRO B N     1 
ATOM   6139  C  CA    . PRO B 1 25  ? 91.440  126.389 167.055 1.00 182.22 ? 25   PRO B CA    1 
ATOM   6140  C  C     . PRO B 1 25  ? 92.142  127.553 167.730 1.00 180.09 ? 25   PRO B C     1 
ATOM   6141  O  O     . PRO B 1 25  ? 93.094  127.342 168.491 1.00 179.90 ? 25   PRO B O     1 
ATOM   6142  C  CB    . PRO B 1 25  ? 91.894  126.222 165.597 1.00 177.40 ? 25   PRO B CB    1 
ATOM   6143  C  CG    . PRO B 1 25  ? 90.695  125.727 164.887 1.00 178.61 ? 25   PRO B CG    1 
ATOM   6144  C  CD    . PRO B 1 25  ? 89.541  126.425 165.534 1.00 180.47 ? 25   PRO B CD    1 
ATOM   6145  N  N     . ARG B 1 26  ? 91.692  128.783 167.476 1.00 176.36 ? 26   ARG B N     1 
ATOM   6146  C  CA    . ARG B 1 26  ? 92.314  129.947 168.099 1.00 168.87 ? 26   ARG B CA    1 
ATOM   6147  C  C     . ARG B 1 26  ? 92.119  129.932 169.608 1.00 171.67 ? 26   ARG B C     1 
ATOM   6148  O  O     . ARG B 1 26  ? 93.071  130.137 170.372 1.00 171.32 ? 26   ARG B O     1 
ATOM   6149  C  CB    . ARG B 1 26  ? 91.735  131.225 167.499 1.00 162.06 ? 26   ARG B CB    1 
ATOM   6150  C  CG    . ARG B 1 26  ? 91.881  131.323 165.996 1.00 160.41 ? 26   ARG B CG    1 
ATOM   6151  C  CD    . ARG B 1 26  ? 93.310  131.030 165.549 1.00 155.30 ? 26   ARG B CD    1 
ATOM   6152  N  NE    . ARG B 1 26  ? 94.333  131.756 166.299 1.00 146.02 ? 26   ARG B NE    1 
ATOM   6153  C  CZ    . ARG B 1 26  ? 94.364  133.068 166.496 1.00 143.24 ? 26   ARG B CZ    1 
ATOM   6154  N  NH1   . ARG B 1 26  ? 93.446  133.873 165.984 1.00 140.56 ? 26   ARG B NH1   1 
ATOM   6155  N  NH2   . ARG B 1 26  ? 95.350  133.591 167.219 1.00 142.62 ? 26   ARG B NH2   1 
ATOM   6156  N  N     . SER B 1 27  ? 90.883  129.699 170.053 1.00 174.19 ? 27   SER B N     1 
ATOM   6157  C  CA    . SER B 1 27  ? 90.616  129.622 171.483 1.00 175.33 ? 27   SER B CA    1 
ATOM   6158  C  C     . SER B 1 27  ? 91.397  128.483 172.120 1.00 179.59 ? 27   SER B C     1 
ATOM   6159  O  O     . SER B 1 27  ? 91.928  128.630 173.225 1.00 184.21 ? 27   SER B O     1 
ATOM   6160  C  CB    . SER B 1 27  ? 89.117  129.452 171.728 1.00 178.26 ? 27   SER B CB    1 
ATOM   6161  O  OG    . SER B 1 27  ? 88.827  129.410 173.114 1.00 179.03 ? 27   SER B OG    1 
ATOM   6162  N  N     . SER B 1 28  ? 91.490  127.343 171.430 1.00 179.30 ? 28   SER B N     1 
ATOM   6163  C  CA    . SER B 1 28  ? 92.247  126.216 171.965 1.00 179.87 ? 28   SER B CA    1 
ATOM   6164  C  C     . SER B 1 28  ? 93.722  126.566 172.129 1.00 180.60 ? 28   SER B C     1 
ATOM   6165  O  O     . SER B 1 28  ? 94.314  126.312 173.185 1.00 182.75 ? 28   SER B O     1 
ATOM   6166  C  CB    . SER B 1 28  ? 92.081  124.998 171.057 1.00 179.88 ? 28   SER B CB    1 
ATOM   6167  O  OG    . SER B 1 28  ? 92.732  123.861 171.598 1.00 182.41 ? 28   SER B OG    1 
ATOM   6168  N  N     . MET B 1 29  ? 94.327  127.167 171.101 1.00 177.91 ? 29   MET B N     1 
ATOM   6169  C  CA    . MET B 1 29  ? 95.741  127.524 171.176 1.00 176.66 ? 29   MET B CA    1 
ATOM   6170  C  C     . MET B 1 29  ? 95.998  128.556 172.267 1.00 177.47 ? 29   MET B C     1 
ATOM   6171  O  O     . MET B 1 29  ? 96.985  128.458 173.009 1.00 177.54 ? 29   MET B O     1 
ATOM   6172  C  CB    . MET B 1 29  ? 96.221  128.051 169.825 1.00 165.02 ? 29   MET B CB    1 
ATOM   6173  C  CG    . MET B 1 29  ? 97.591  128.705 169.870 1.00 157.97 ? 29   MET B CG    1 
ATOM   6174  S  SD    . MET B 1 29  ? 97.948  129.688 168.405 1.00 141.66 ? 29   MET B SD    1 
ATOM   6175  C  CE    . MET B 1 29  ? 99.735  129.721 168.455 1.00 120.80 ? 29   MET B CE    1 
ATOM   6176  N  N     . MET B 1 30  ? 95.122  129.553 172.387 1.00 175.77 ? 30   MET B N     1 
ATOM   6177  C  CA    . MET B 1 30  ? 95.358  130.600 173.373 1.00 173.73 ? 30   MET B CA    1 
ATOM   6178  C  C     . MET B 1 30  ? 95.104  130.095 174.787 1.00 180.56 ? 30   MET B C     1 
ATOM   6179  O  O     . MET B 1 30  ? 95.776  130.520 175.732 1.00 183.38 ? 30   MET B O     1 
ATOM   6180  C  CB    . MET B 1 30  ? 94.502  131.819 173.052 1.00 168.00 ? 30   MET B CB    1 
ATOM   6181  C  CG    . MET B 1 30  ? 94.951  132.515 171.784 1.00 162.87 ? 30   MET B CG    1 
ATOM   6182  S  SD    . MET B 1 30  ? 96.696  132.963 171.823 1.00 162.90 ? 30   MET B SD    1 
ATOM   6183  C  CE    . MET B 1 30  ? 96.827  133.944 170.330 1.00 131.06 ? 30   MET B CE    1 
ATOM   6184  N  N     . SER B 1 31  ? 94.153  129.173 174.956 1.00 182.58 ? 31   SER B N     1 
ATOM   6185  C  CA    . SER B 1 31  ? 93.985  128.527 176.253 1.00 185.26 ? 31   SER B CA    1 
ATOM   6186  C  C     . SER B 1 31  ? 95.194  127.665 176.589 1.00 189.77 ? 31   SER B C     1 
ATOM   6187  O  O     . SER B 1 31  ? 95.590  127.566 177.756 1.00 194.82 ? 31   SER B O     1 
ATOM   6188  C  CB    . SER B 1 31  ? 92.704  127.693 176.263 1.00 185.98 ? 31   SER B CB    1 
ATOM   6189  O  OG    . SER B 1 31  ? 91.564  128.511 176.064 1.00 188.02 ? 31   SER B OG    1 
ATOM   6190  N  N     . VAL B 1 32  ? 95.796  127.036 175.578 1.00 189.18 ? 32   VAL B N     1 
ATOM   6191  C  CA    . VAL B 1 32  ? 97.030  126.288 175.798 1.00 192.47 ? 32   VAL B CA    1 
ATOM   6192  C  C     . VAL B 1 32  ? 98.139  127.216 176.280 1.00 194.69 ? 32   VAL B C     1 
ATOM   6193  O  O     . VAL B 1 32  ? 98.868  126.898 177.228 1.00 197.31 ? 32   VAL B O     1 
ATOM   6194  C  CB    . VAL B 1 32  ? 97.433  125.538 174.514 1.00 189.37 ? 32   VAL B CB    1 
ATOM   6195  C  CG1   . VAL B 1 32  ? 98.908  125.171 174.548 1.00 187.75 ? 32   VAL B CG1   1 
ATOM   6196  C  CG2   . VAL B 1 32  ? 96.572  124.295 174.339 1.00 189.97 ? 32   VAL B CG2   1 
ATOM   6197  N  N     . GLU B 1 33  ? 98.280  128.378 175.641 1.00 190.06 ? 33   GLU B N     1 
ATOM   6198  C  CA    . GLU B 1 33  ? 99.295  129.335 176.082 1.00 187.56 ? 33   GLU B CA    1 
ATOM   6199  C  C     . GLU B 1 33  ? 98.999  129.853 177.487 1.00 193.20 ? 33   GLU B C     1 
ATOM   6200  O  O     . GLU B 1 33  ? 99.918  130.047 178.292 1.00 194.07 ? 33   GLU B O     1 
ATOM   6201  C  CB    . GLU B 1 33  ? 99.403  130.495 175.094 1.00 174.22 ? 33   GLU B CB    1 
ATOM   6202  C  CG    . GLU B 1 33  ? 100.227 130.176 173.859 1.00 166.15 ? 33   GLU B CG    1 
ATOM   6203  C  CD    . GLU B 1 33  ? 100.578 131.413 173.061 1.00 153.86 ? 33   GLU B CD    1 
ATOM   6204  O  OE1   . GLU B 1 33  ? 100.091 132.506 173.414 1.00 152.60 ? 33   GLU B OE1   1 
ATOM   6205  O  OE2   . GLU B 1 33  ? 101.343 131.295 172.082 1.00 144.48 ? 33   GLU B OE2   1 
ATOM   6206  N  N     . TYR B 1 34  ? 97.722  130.086 177.797 1.00 196.70 ? 34   TYR B N     1 
ATOM   6207  C  CA    . TYR B 1 34  ? 97.345  130.526 179.137 1.00 202.64 ? 34   TYR B CA    1 
ATOM   6208  C  C     . TYR B 1 34  ? 97.690  129.473 180.183 1.00 204.98 ? 34   TYR B C     1 
ATOM   6209  O  O     . TYR B 1 34  ? 98.157  129.805 181.278 1.00 206.09 ? 34   TYR B O     1 
ATOM   6210  C  CB    . TYR B 1 34  ? 95.851  130.853 179.180 1.00 205.23 ? 34   TYR B CB    1 
ATOM   6211  C  CG    . TYR B 1 34  ? 95.358  131.322 180.532 1.00 212.18 ? 34   TYR B CG    1 
ATOM   6212  C  CD1   . TYR B 1 34  ? 95.573  132.626 180.958 1.00 214.97 ? 34   TYR B CD1   1 
ATOM   6213  C  CD2   . TYR B 1 34  ? 94.673  130.460 181.380 1.00 213.11 ? 34   TYR B CD2   1 
ATOM   6214  C  CE1   . TYR B 1 34  ? 95.122  133.058 182.193 1.00 218.82 ? 34   TYR B CE1   1 
ATOM   6215  C  CE2   . TYR B 1 34  ? 94.219  130.883 182.616 1.00 217.48 ? 34   TYR B CE2   1 
ATOM   6216  C  CZ    . TYR B 1 34  ? 94.446  132.183 183.017 1.00 222.32 ? 34   TYR B CZ    1 
ATOM   6217  O  OH    . TYR B 1 34  ? 93.996  132.608 184.246 1.00 227.42 ? 34   TYR B OH    1 
ATOM   6218  N  N     . ASP B 1 35  ? 97.454  128.198 179.868 1.00 204.68 ? 35   ASP B N     1 
ATOM   6219  C  CA    . ASP B 1 35  ? 97.802  127.131 180.799 1.00 206.46 ? 35   ASP B CA    1 
ATOM   6220  C  C     . ASP B 1 35  ? 99.310  126.949 180.904 1.00 205.85 ? 35   ASP B C     1 
ATOM   6221  O  O     . ASP B 1 35  ? 99.808  126.504 181.945 1.00 207.80 ? 35   ASP B O     1 
ATOM   6222  C  CB    . ASP B 1 35  ? 97.136  125.822 180.373 1.00 206.88 ? 35   ASP B CB    1 
ATOM   6223  C  CG    . ASP B 1 35  ? 96.986  124.845 181.522 1.00 210.60 ? 35   ASP B CG    1 
ATOM   6224  O  OD1   . ASP B 1 35  ? 97.223  125.247 182.680 1.00 211.89 ? 35   ASP B OD1   1 
ATOM   6225  O  OD2   . ASP B 1 35  ? 96.630  123.676 181.267 1.00 211.23 ? 35   ASP B OD2   1 
ATOM   6226  N  N     . GLY B 1 36  ? 100.048 127.273 179.843 1.00 201.18 ? 36   GLY B N     1 
ATOM   6227  C  CA    . GLY B 1 36  ? 101.497 127.223 179.897 1.00 202.21 ? 36   GLY B CA    1 
ATOM   6228  C  C     . GLY B 1 36  ? 102.157 128.425 180.536 1.00 206.27 ? 36   GLY B C     1 
ATOM   6229  O  O     . GLY B 1 36  ? 103.350 128.368 180.847 1.00 206.89 ? 36   GLY B O     1 
ATOM   6230  N  N     . ILE B 1 37  ? 101.409 129.514 180.727 1.00 206.18 ? 37   ILE B N     1 
ATOM   6231  C  CA    . ILE B 1 37  ? 101.980 130.704 181.363 1.00 204.76 ? 37   ILE B CA    1 
ATOM   6232  C  C     . ILE B 1 37  ? 102.442 130.447 182.792 1.00 204.78 ? 37   ILE B C     1 
ATOM   6233  O  O     . ILE B 1 37  ? 103.584 130.813 183.122 1.00 204.78 ? 37   ILE B O     1 
ATOM   6234  C  CB    . ILE B 1 37  ? 100.988 131.881 181.264 1.00 204.83 ? 37   ILE B CB    1 
ATOM   6235  C  CG1   . ILE B 1 37  ? 101.175 132.618 179.939 1.00 201.77 ? 37   ILE B CG1   1 
ATOM   6236  C  CG2   . ILE B 1 37  ? 101.166 132.840 182.433 1.00 203.82 ? 37   ILE B CG2   1 
ATOM   6237  C  CD1   . ILE B 1 37  ? 102.543 133.252 179.787 1.00 184.12 ? 37   ILE B CD1   1 
ATOM   6238  N  N     . PRO B 1 38  ? 101.642 129.850 183.686 1.00 207.56 ? 38   PRO B N     1 
ATOM   6239  C  CA    . PRO B 1 38  ? 102.077 129.733 185.084 1.00 209.63 ? 38   PRO B CA    1 
ATOM   6240  C  C     . PRO B 1 38  ? 103.357 128.921 185.219 1.00 209.84 ? 38   PRO B C     1 
ATOM   6241  O  O     . PRO B 1 38  ? 103.569 127.936 184.508 1.00 204.54 ? 38   PRO B O     1 
ATOM   6242  C  CB    . PRO B 1 38  ? 100.894 129.037 185.770 1.00 210.37 ? 38   PRO B CB    1 
ATOM   6243  C  CG    . PRO B 1 38  ? 100.146 128.380 184.672 1.00 209.63 ? 38   PRO B CG    1 
ATOM   6244  C  CD    . PRO B 1 38  ? 100.284 129.304 183.512 1.00 208.95 ? 38   PRO B CD    1 
ATOM   6245  N  N     . LEU B 1 39  ? 104.205 129.353 186.151 1.00 212.21 ? 39   LEU B N     1 
ATOM   6246  C  CA    . LEU B 1 39  ? 105.503 128.734 186.413 1.00 209.09 ? 39   LEU B CA    1 
ATOM   6247  C  C     . LEU B 1 39  ? 106.339 128.602 185.144 1.00 204.83 ? 39   LEU B C     1 
ATOM   6248  O  O     . LEU B 1 39  ? 106.367 127.547 184.512 1.00 204.13 ? 39   LEU B O     1 
ATOM   6249  C  CB    . LEU B 1 39  ? 105.325 127.364 187.069 1.00 207.56 ? 39   LEU B CB    1 
ATOM   6250  C  CG    . LEU B 1 39  ? 106.567 126.820 187.775 1.00 202.86 ? 39   LEU B CG    1 
ATOM   6251  C  CD1   . LEU B 1 39  ? 106.998 127.756 188.894 1.00 196.89 ? 39   LEU B CD1   1 
ATOM   6252  C  CD2   . LEU B 1 39  ? 106.310 125.421 188.310 1.00 203.33 ? 39   LEU B CD2   1 
ATOM   6253  N  N     . ILE B 1 91  ? 140.522 125.935 196.205 1.00 205.09 ? 91   ILE B N     1 
ATOM   6254  C  CA    . ILE B 1 91  ? 141.589 125.402 195.361 1.00 197.50 ? 91   ILE B CA    1 
ATOM   6255  C  C     . ILE B 1 91  ? 141.572 126.156 194.034 1.00 192.63 ? 91   ILE B C     1 
ATOM   6256  O  O     . ILE B 1 91  ? 140.497 126.303 193.432 1.00 194.13 ? 91   ILE B O     1 
ATOM   6257  C  CB    . ILE B 1 91  ? 141.458 123.880 195.166 1.00 194.87 ? 91   ILE B CB    1 
ATOM   6258  C  CG1   . ILE B 1 91  ? 140.459 123.505 194.065 1.00 195.45 ? 91   ILE B CG1   1 
ATOM   6259  C  CG2   . ILE B 1 91  ? 141.071 123.210 196.481 1.00 195.74 ? 91   ILE B CG2   1 
ATOM   6260  C  CD1   . ILE B 1 91  ? 140.087 122.038 194.040 1.00 196.56 ? 91   ILE B CD1   1 
ATOM   6261  N  N     . PRO B 1 92  ? 142.687 126.731 193.605 1.00 187.90 ? 92   PRO B N     1 
ATOM   6262  C  CA    . PRO B 1 92  ? 142.758 127.356 192.282 1.00 179.82 ? 92   PRO B CA    1 
ATOM   6263  C  C     . PRO B 1 92  ? 142.938 126.302 191.192 1.00 176.60 ? 92   PRO B C     1 
ATOM   6264  O  O     . PRO B 1 92  ? 142.921 125.098 191.444 1.00 178.82 ? 92   PRO B O     1 
ATOM   6265  C  CB    . PRO B 1 92  ? 143.988 128.257 192.385 1.00 175.85 ? 92   PRO B CB    1 
ATOM   6266  C  CG    . PRO B 1 92  ? 144.137 128.532 193.841 1.00 180.10 ? 92   PRO B CG    1 
ATOM   6267  C  CD    . PRO B 1 92  ? 143.716 127.257 194.514 1.00 188.18 ? 92   PRO B CD    1 
ATOM   6268  N  N     . SER B 1 93  ? 143.116 126.781 189.962 1.00 170.33 ? 93   SER B N     1 
ATOM   6269  C  CA    . SER B 1 93  ? 143.398 125.918 188.823 1.00 164.29 ? 93   SER B CA    1 
ATOM   6270  C  C     . SER B 1 93  ? 144.484 126.555 187.968 1.00 164.00 ? 93   SER B C     1 
ATOM   6271  O  O     . SER B 1 93  ? 144.587 127.780 187.870 1.00 166.66 ? 93   SER B O     1 
ATOM   6272  C  CB    . SER B 1 93  ? 142.143 125.663 187.981 1.00 159.35 ? 93   SER B CB    1 
ATOM   6273  O  OG    . SER B 1 93  ? 142.444 124.855 186.857 1.00 157.06 ? 93   SER B OG    1 
ATOM   6274  N  N     . VAL B 1 94  ? 145.299 125.703 187.342 1.00 160.20 ? 94   VAL B N     1 
ATOM   6275  C  CA    . VAL B 1 94  ? 146.382 126.205 186.498 1.00 154.63 ? 94   VAL B CA    1 
ATOM   6276  C  C     . VAL B 1 94  ? 145.820 126.883 185.254 1.00 154.41 ? 94   VAL B C     1 
ATOM   6277  O  O     . VAL B 1 94  ? 146.371 127.880 184.770 1.00 157.34 ? 94   VAL B O     1 
ATOM   6278  C  CB    . VAL B 1 94  ? 147.375 125.074 186.155 1.00 150.01 ? 94   VAL B CB    1 
ATOM   6279  C  CG1   . VAL B 1 94  ? 146.917 124.265 184.952 1.00 151.53 ? 94   VAL B CG1   1 
ATOM   6280  C  CG2   . VAL B 1 94  ? 148.762 125.646 185.916 1.00 146.73 ? 94   VAL B CG2   1 
ATOM   6281  N  N     . GLU B 1 95  ? 144.709 126.366 184.722 1.00 152.93 ? 95   GLU B N     1 
ATOM   6282  C  CA    . GLU B 1 95  ? 144.066 127.021 183.588 1.00 152.77 ? 95   GLU B CA    1 
ATOM   6283  C  C     . GLU B 1 95  ? 143.530 128.390 183.985 1.00 156.24 ? 95   GLU B C     1 
ATOM   6284  O  O     . GLU B 1 95  ? 143.642 129.357 183.221 1.00 153.82 ? 95   GLU B O     1 
ATOM   6285  C  CB    . GLU B 1 95  ? 142.946 126.140 183.039 1.00 151.65 ? 95   GLU B CB    1 
ATOM   6286  C  CG    . GLU B 1 95  ? 142.784 126.211 181.531 1.00 156.33 ? 95   GLU B CG    1 
ATOM   6287  C  CD    . GLU B 1 95  ? 142.253 127.549 181.060 1.00 160.32 ? 95   GLU B CD    1 
ATOM   6288  O  OE1   . GLU B 1 95  ? 141.450 128.163 181.793 1.00 161.74 ? 95   GLU B OE1   1 
ATOM   6289  O  OE2   . GLU B 1 95  ? 142.638 127.988 179.956 1.00 161.67 ? 95   GLU B OE2   1 
ATOM   6290  N  N     . GLU B 1 96  ? 142.943 128.488 185.179 1.00 157.65 ? 96   GLU B N     1 
ATOM   6291  C  CA    . GLU B 1 96  ? 142.492 129.781 185.681 1.00 156.68 ? 96   GLU B CA    1 
ATOM   6292  C  C     . GLU B 1 96  ? 143.659 130.744 185.838 1.00 151.48 ? 96   GLU B C     1 
ATOM   6293  O  O     . GLU B 1 96  ? 143.545 131.928 185.503 1.00 151.51 ? 96   GLU B O     1 
ATOM   6294  C  CB    . GLU B 1 96  ? 141.764 129.601 187.013 1.00 161.14 ? 96   GLU B CB    1 
ATOM   6295  C  CG    . GLU B 1 96  ? 141.226 130.891 187.608 1.00 162.46 ? 96   GLU B CG    1 
ATOM   6296  C  CD    . GLU B 1 96  ? 141.311 130.910 189.123 1.00 165.68 ? 96   GLU B CD    1 
ATOM   6297  O  OE1   . GLU B 1 96  ? 141.224 129.827 189.739 1.00 167.12 ? 96   GLU B OE1   1 
ATOM   6298  O  OE2   . GLU B 1 96  ? 141.470 132.008 189.698 1.00 163.24 ? 96   GLU B OE2   1 
ATOM   6299  N  N     . ALA B 1 97  ? 144.791 130.256 186.351 1.00 147.05 ? 97   ALA B N     1 
ATOM   6300  C  CA    . ALA B 1 97  ? 145.963 131.112 186.496 1.00 147.06 ? 97   ALA B CA    1 
ATOM   6301  C  C     . ALA B 1 97  ? 146.448 131.613 185.142 1.00 149.03 ? 97   ALA B C     1 
ATOM   6302  O  O     . ALA B 1 97  ? 146.765 132.799 184.988 1.00 152.68 ? 97   ALA B O     1 
ATOM   6303  C  CB    . ALA B 1 97  ? 147.076 130.359 187.221 1.00 148.06 ? 97   ALA B CB    1 
ATOM   6304  N  N     . LEU B 1 98  ? 146.507 130.725 184.147 1.00 148.47 ? 98   LEU B N     1 
ATOM   6305  C  CA    . LEU B 1 98  ? 146.937 131.133 182.813 1.00 146.07 ? 98   LEU B CA    1 
ATOM   6306  C  C     . LEU B 1 98  ? 145.986 132.162 182.214 1.00 147.57 ? 98   LEU B C     1 
ATOM   6307  O  O     . LEU B 1 98  ? 146.429 133.155 181.626 1.00 149.64 ? 98   LEU B O     1 
ATOM   6308  C  CB    . LEU B 1 98  ? 147.049 129.913 181.900 1.00 142.39 ? 98   LEU B CB    1 
ATOM   6309  C  CG    . LEU B 1 98  ? 148.189 128.937 182.186 1.00 138.45 ? 98   LEU B CG    1 
ATOM   6310  C  CD1   . LEU B 1 98  ? 148.177 127.793 181.190 1.00 139.44 ? 98   LEU B CD1   1 
ATOM   6311  C  CD2   . LEU B 1 98  ? 149.517 129.660 182.139 1.00 132.52 ? 98   LEU B CD2   1 
ATOM   6312  N  N     . SER B 1 99  ? 144.677 131.946 182.358 1.00 146.66 ? 99   SER B N     1 
ATOM   6313  C  CA    . SER B 1 99  ? 143.712 132.895 181.811 1.00 148.38 ? 99   SER B CA    1 
ATOM   6314  C  C     . SER B 1 99  ? 143.807 134.249 182.504 1.00 148.00 ? 99   SER B C     1 
ATOM   6315  O  O     . SER B 1 99  ? 143.741 135.297 181.849 1.00 147.70 ? 99   SER B O     1 
ATOM   6316  C  CB    . SER B 1 99  ? 142.297 132.332 181.925 1.00 149.70 ? 99   SER B CB    1 
ATOM   6317  O  OG    . SER B 1 99  ? 141.474 132.817 180.879 1.00 147.71 ? 99   SER B OG    1 
ATOM   6318  N  N     . THR B 1 100 ? 143.958 134.251 183.831 1.00 146.47 ? 100  THR B N     1 
ATOM   6319  C  CA    . THR B 1 100 ? 144.083 135.511 184.555 1.00 145.66 ? 100  THR B CA    1 
ATOM   6320  C  C     . THR B 1 100 ? 145.351 136.253 184.158 1.00 146.20 ? 100  THR B C     1 
ATOM   6321  O  O     . THR B 1 100 ? 145.334 137.478 184.001 1.00 148.49 ? 100  THR B O     1 
ATOM   6322  C  CB    . THR B 1 100 ? 144.057 135.264 186.063 1.00 149.14 ? 100  THR B CB    1 
ATOM   6323  O  OG1   . THR B 1 100 ? 144.978 134.218 186.394 1.00 152.78 ? 100  THR B OG1   1 
ATOM   6324  C  CG2   . THR B 1 100 ? 142.659 134.876 186.519 1.00 149.82 ? 100  THR B CG2   1 
ATOM   6325  N  N     . LEU B 1 101 ? 146.464 135.533 183.994 1.00 144.23 ? 101  LEU B N     1 
ATOM   6326  C  CA    . LEU B 1 101 ? 147.693 136.189 183.556 1.00 139.02 ? 101  LEU B CA    1 
ATOM   6327  C  C     . LEU B 1 101 ? 147.558 136.736 182.141 1.00 142.19 ? 101  LEU B C     1 
ATOM   6328  O  O     . LEU B 1 101 ? 148.098 137.802 181.829 1.00 144.83 ? 101  LEU B O     1 
ATOM   6329  C  CB    . LEU B 1 101 ? 148.873 135.227 183.646 1.00 133.50 ? 101  LEU B CB    1 
ATOM   6330  C  CG    . LEU B 1 101 ? 149.454 135.090 185.047 1.00 137.29 ? 101  LEU B CG    1 
ATOM   6331  C  CD1   . LEU B 1 101 ? 150.651 134.172 185.022 1.00 141.55 ? 101  LEU B CD1   1 
ATOM   6332  C  CD2   . LEU B 1 101 ? 149.831 136.451 185.592 1.00 139.94 ? 101  LEU B CD2   1 
ATOM   6333  N  N     . ASP B 1 102 ? 146.856 136.015 181.267 1.00 143.36 ? 102  ASP B N     1 
ATOM   6334  C  CA    . ASP B 1 102 ? 146.630 136.505 179.910 1.00 144.43 ? 102  ASP B CA    1 
ATOM   6335  C  C     . ASP B 1 102 ? 145.796 137.785 179.942 1.00 146.32 ? 102  ASP B C     1 
ATOM   6336  O  O     . ASP B 1 102 ? 146.091 138.753 179.226 1.00 147.55 ? 102  ASP B O     1 
ATOM   6337  C  CB    . ASP B 1 102 ? 145.980 135.374 179.089 1.00 143.84 ? 102  ASP B CB    1 
ATOM   6338  C  CG    . ASP B 1 102 ? 145.315 135.828 177.773 1.00 152.04 ? 102  ASP B CG    1 
ATOM   6339  O  OD1   . ASP B 1 102 ? 144.931 136.998 177.582 1.00 156.69 ? 102  ASP B OD1   1 
ATOM   6340  O  OD2   . ASP B 1 102 ? 145.159 134.956 176.889 1.00 154.58 ? 102  ASP B OD2   1 
ATOM   6341  N  N     . ARG B 1 103 ? 144.758 137.812 180.781 1.00 145.35 ? 103  ARG B N     1 
ATOM   6342  C  CA    . ARG B 1 103 ? 143.961 139.026 180.942 1.00 145.71 ? 103  ARG B CA    1 
ATOM   6343  C  C     . ARG B 1 103 ? 144.799 140.170 181.499 1.00 143.51 ? 103  ARG B C     1 
ATOM   6344  O  O     . ARG B 1 103 ? 144.629 141.326 181.097 1.00 143.73 ? 103  ARG B O     1 
ATOM   6345  C  CB    . ARG B 1 103 ? 142.765 138.754 181.854 1.00 148.47 ? 103  ARG B CB    1 
ATOM   6346  C  CG    . ARG B 1 103 ? 141.667 137.923 181.221 1.00 147.09 ? 103  ARG B CG    1 
ATOM   6347  C  CD    . ARG B 1 103 ? 140.657 137.490 182.266 1.00 147.53 ? 103  ARG B CD    1 
ATOM   6348  N  NE    . ARG B 1 103 ? 140.264 138.596 183.129 1.00 150.23 ? 103  ARG B NE    1 
ATOM   6349  C  CZ    . ARG B 1 103 ? 139.751 138.453 184.342 1.00 151.97 ? 103  ARG B CZ    1 
ATOM   6350  N  NH1   . ARG B 1 103 ? 139.572 137.257 184.879 1.00 149.46 ? 103  ARG B NH1   1 
ATOM   6351  N  NH2   . ARG B 1 103 ? 139.414 139.535 185.035 1.00 153.53 ? 103  ARG B NH2   1 
ATOM   6352  N  N     . ALA B 1 104 ? 145.690 139.871 182.446 1.00 142.34 ? 104  ALA B N     1 
ATOM   6353  C  CA    . ALA B 1 104 ? 146.568 140.902 182.991 1.00 142.53 ? 104  ALA B CA    1 
ATOM   6354  C  C     . ALA B 1 104 ? 147.492 141.456 181.918 1.00 140.49 ? 104  ALA B C     1 
ATOM   6355  O  O     . ALA B 1 104 ? 147.756 142.662 181.874 1.00 144.92 ? 104  ALA B O     1 
ATOM   6356  C  CB    . ALA B 1 104 ? 147.381 140.342 184.155 1.00 143.72 ? 104  ALA B CB    1 
ATOM   6357  N  N     . ALA B 1 105 ? 148.009 140.581 181.056 1.00 137.63 ? 105  ALA B N     1 
ATOM   6358  C  CA    . ALA B 1 105 ? 148.829 141.036 179.940 1.00 139.39 ? 105  ALA B CA    1 
ATOM   6359  C  C     . ALA B 1 105 ? 148.032 141.943 179.014 1.00 142.18 ? 105  ALA B C     1 
ATOM   6360  O  O     . ALA B 1 105 ? 148.540 142.970 178.553 1.00 144.99 ? 105  ALA B O     1 
ATOM   6361  C  CB    . ALA B 1 105 ? 149.383 139.839 179.171 1.00 137.52 ? 105  ALA B CB    1 
ATOM   6362  N  N     . ALA B 1 106 ? 146.780 141.582 178.733 1.00 141.23 ? 106  ALA B N     1 
ATOM   6363  C  CA    . ALA B 1 106 ? 145.948 142.440 177.893 1.00 142.56 ? 106  ALA B CA    1 
ATOM   6364  C  C     . ALA B 1 106 ? 145.714 143.799 178.547 1.00 143.58 ? 106  ALA B C     1 
ATOM   6365  O  O     . ALA B 1 106 ? 145.792 144.842 177.884 1.00 143.86 ? 106  ALA B O     1 
ATOM   6366  C  CB    . ALA B 1 106 ? 144.618 141.752 177.590 1.00 144.30 ? 106  ALA B CB    1 
ATOM   6367  N  N     . ALA B 1 107 ? 145.432 143.807 179.852 1.00 143.15 ? 107  ALA B N     1 
ATOM   6368  C  CA    . ALA B 1 107 ? 145.199 145.065 180.554 1.00 142.41 ? 107  ALA B CA    1 
ATOM   6369  C  C     . ALA B 1 107 ? 146.447 145.938 180.548 1.00 142.36 ? 107  ALA B C     1 
ATOM   6370  O  O     . ALA B 1 107 ? 146.361 147.155 180.349 1.00 146.57 ? 107  ALA B O     1 
ATOM   6371  C  CB    . ALA B 1 107 ? 144.740 144.794 181.985 1.00 146.45 ? 107  ALA B CB    1 
ATOM   6372  N  N     . LEU B 1 108 ? 147.616 145.335 180.769 1.00 139.04 ? 108  LEU B N     1 
ATOM   6373  C  CA    . LEU B 1 108 ? 148.864 146.084 180.694 1.00 136.84 ? 108  LEU B CA    1 
ATOM   6374  C  C     . LEU B 1 108 ? 149.113 146.605 179.286 1.00 139.53 ? 108  LEU B C     1 
ATOM   6375  O  O     . LEU B 1 108 ? 149.668 147.696 179.118 1.00 142.80 ? 108  LEU B O     1 
ATOM   6376  C  CB    . LEU B 1 108 ? 150.026 145.206 181.152 1.00 135.38 ? 108  LEU B CB    1 
ATOM   6377  C  CG    . LEU B 1 108 ? 151.408 145.851 181.216 1.00 136.71 ? 108  LEU B CG    1 
ATOM   6378  C  CD1   . LEU B 1 108 ? 151.335 147.208 181.889 1.00 138.63 ? 108  LEU B CD1   1 
ATOM   6379  C  CD2   . LEU B 1 108 ? 152.377 144.940 181.943 1.00 139.06 ? 108  LEU B CD2   1 
ATOM   6380  N  N     . ASN B 1 109 ? 148.712 145.840 178.268 1.00 141.34 ? 109  ASN B N     1 
ATOM   6381  C  CA    . ASN B 1 109 ? 148.809 146.319 176.895 1.00 143.25 ? 109  ASN B CA    1 
ATOM   6382  C  C     . ASN B 1 109 ? 147.920 147.533 176.671 1.00 144.34 ? 109  ASN B C     1 
ATOM   6383  O  O     . ASN B 1 109 ? 148.287 148.441 175.917 1.00 145.46 ? 109  ASN B O     1 
ATOM   6384  C  CB    . ASN B 1 109 ? 148.430 145.202 175.925 1.00 145.54 ? 109  ASN B CB    1 
ATOM   6385  C  CG    . ASN B 1 109 ? 149.629 144.615 175.216 1.00 147.68 ? 109  ASN B CG    1 
ATOM   6386  O  OD1   . ASN B 1 109 ? 150.732 144.580 175.760 1.00 146.18 ? 109  ASN B OD1   1 
ATOM   6387  N  ND2   . ASN B 1 109 ? 149.420 144.143 173.993 1.00 151.17 ? 109  ASN B ND2   1 
ATOM   6388  N  N     . ALA B 1 110 ? 146.756 147.567 177.312 1.00 144.09 ? 110  ALA B N     1 
ATOM   6389  C  CA    . ALA B 1 110 ? 145.844 148.697 177.196 1.00 143.59 ? 110  ALA B CA    1 
ATOM   6390  C  C     . ALA B 1 110 ? 146.142 149.810 178.194 1.00 145.92 ? 110  ALA B C     1 
ATOM   6391  O  O     . ALA B 1 110 ? 145.390 150.788 178.247 1.00 145.73 ? 110  ALA B O     1 
ATOM   6392  C  CB    . ALA B 1 110 ? 144.396 148.228 177.368 1.00 144.40 ? 110  ALA B CB    1 
ATOM   6393  N  N     . ARG B 1 111 ? 147.210 149.679 178.984 1.00 150.87 ? 111  ARG B N     1 
ATOM   6394  C  CA    . ARG B 1 111 ? 147.611 150.688 179.967 1.00 153.39 ? 111  ARG B CA    1 
ATOM   6395  C  C     . ARG B 1 111 ? 146.510 150.944 180.996 1.00 153.03 ? 111  ARG B C     1 
ATOM   6396  O  O     . ARG B 1 111 ? 145.993 152.055 181.130 1.00 155.55 ? 111  ARG B O     1 
ATOM   6397  C  CB    . ARG B 1 111 ? 148.041 151.990 179.286 1.00 152.50 ? 111  ARG B CB    1 
ATOM   6398  C  CG    . ARG B 1 111 ? 149.310 151.867 178.465 1.00 154.77 ? 111  ARG B CG    1 
ATOM   6399  C  CD    . ARG B 1 111 ? 149.559 153.119 177.645 1.00 162.03 ? 111  ARG B CD    1 
ATOM   6400  N  NE    . ARG B 1 111 ? 150.971 153.479 177.618 1.00 170.01 ? 111  ARG B NE    1 
ATOM   6401  C  CZ    . ARG B 1 111 ? 151.651 153.762 176.515 1.00 171.90 ? 111  ARG B CZ    1 
ATOM   6402  N  NH1   . ARG B 1 111 ? 151.082 153.719 175.322 1.00 172.53 ? 111  ARG B NH1   1 
ATOM   6403  N  NH2   . ARG B 1 111 ? 152.935 154.095 176.613 1.00 170.44 ? 111  ARG B NH2   1 
ATOM   6404  N  N     . ARG B 1 112 ? 146.152 149.893 181.727 1.00 151.08 ? 112  ARG B N     1 
ATOM   6405  C  CA    . ARG B 1 112 ? 145.269 149.976 182.888 1.00 153.53 ? 112  ARG B CA    1 
ATOM   6406  C  C     . ARG B 1 112 ? 146.040 149.343 184.040 1.00 156.99 ? 112  ARG B C     1 
ATOM   6407  O  O     . ARG B 1 112 ? 145.900 148.149 184.311 1.00 157.99 ? 112  ARG B O     1 
ATOM   6408  C  CB    . ARG B 1 112 ? 143.946 149.272 182.641 1.00 152.72 ? 112  ARG B CB    1 
ATOM   6409  C  CG    . ARG B 1 112 ? 143.395 149.443 181.241 1.00 148.94 ? 112  ARG B CG    1 
ATOM   6410  C  CD    . ARG B 1 112 ? 141.955 148.975 181.172 1.00 152.63 ? 112  ARG B CD    1 
ATOM   6411  N  NE    . ARG B 1 112 ? 141.477 148.890 179.798 1.00 158.97 ? 112  ARG B NE    1 
ATOM   6412  C  CZ    . ARG B 1 112 ? 140.775 147.875 179.314 1.00 158.43 ? 112  ARG B CZ    1 
ATOM   6413  N  NH1   . ARG B 1 112 ? 140.454 146.835 180.066 1.00 155.75 ? 112  ARG B NH1   1 
ATOM   6414  N  NH2   . ARG B 1 112 ? 140.387 147.903 178.042 1.00 156.86 ? 112  ARG B NH2   1 
ATOM   6415  N  N     . TYR B 1 113 ? 146.853 150.151 184.719 1.00 154.64 ? 113  TYR B N     1 
ATOM   6416  C  CA    . TYR B 1 113 ? 147.839 149.603 185.641 1.00 157.98 ? 113  TYR B CA    1 
ATOM   6417  C  C     . TYR B 1 113 ? 147.220 149.044 186.915 1.00 159.96 ? 113  TYR B C     1 
ATOM   6418  O  O     . TYR B 1 113 ? 147.731 148.059 187.452 1.00 161.83 ? 113  TYR B O     1 
ATOM   6419  C  CB    . TYR B 1 113 ? 148.887 150.664 185.965 1.00 159.29 ? 113  TYR B CB    1 
ATOM   6420  C  CG    . TYR B 1 113 ? 149.687 151.069 184.751 1.00 159.71 ? 113  TYR B CG    1 
ATOM   6421  C  CD1   . TYR B 1 113 ? 150.739 150.285 184.300 1.00 159.34 ? 113  TYR B CD1   1 
ATOM   6422  C  CD2   . TYR B 1 113 ? 149.379 152.219 184.042 1.00 160.02 ? 113  TYR B CD2   1 
ATOM   6423  C  CE1   . TYR B 1 113 ? 151.469 150.642 183.187 1.00 160.47 ? 113  TYR B CE1   1 
ATOM   6424  C  CE2   . TYR B 1 113 ? 150.104 152.585 182.927 1.00 159.77 ? 113  TYR B CE2   1 
ATOM   6425  C  CZ    . TYR B 1 113 ? 151.148 151.793 182.504 1.00 158.89 ? 113  TYR B CZ    1 
ATOM   6426  O  OH    . TYR B 1 113 ? 151.874 152.152 181.393 1.00 157.02 ? 113  TYR B OH    1 
ATOM   6427  N  N     . ARG B 1 114 ? 146.128 149.628 187.411 1.00 160.65 ? 114  ARG B N     1 
ATOM   6428  C  CA    . ARG B 1 114 ? 145.488 149.075 188.602 1.00 165.80 ? 114  ARG B CA    1 
ATOM   6429  C  C     . ARG B 1 114 ? 144.967 147.665 188.342 1.00 163.26 ? 114  ARG B C     1 
ATOM   6430  O  O     . ARG B 1 114 ? 145.268 146.727 189.093 1.00 164.01 ? 114  ARG B O     1 
ATOM   6431  C  CB    . ARG B 1 114 ? 144.359 149.994 189.069 1.00 175.44 ? 114  ARG B CB    1 
ATOM   6432  C  CG    . ARG B 1 114 ? 144.740 150.898 190.230 1.00 180.11 ? 114  ARG B CG    1 
ATOM   6433  C  CD    . ARG B 1 114 ? 145.722 151.974 189.807 1.00 176.42 ? 114  ARG B CD    1 
ATOM   6434  N  NE    . ARG B 1 114 ? 146.192 152.751 190.947 1.00 180.96 ? 114  ARG B NE    1 
ATOM   6435  C  CZ    . ARG B 1 114 ? 145.582 153.828 191.423 1.00 183.67 ? 114  ARG B CZ    1 
ATOM   6436  N  NH1   . ARG B 1 114 ? 144.466 154.286 190.879 1.00 186.54 ? 114  ARG B NH1   1 
ATOM   6437  N  NH2   . ARG B 1 114 ? 146.103 154.459 192.471 1.00 181.60 ? 114  ARG B NH2   1 
ATOM   6438  N  N     . ASP B 1 115 ? 144.192 147.494 187.268 1.00 161.56 ? 115  ASP B N     1 
ATOM   6439  C  CA    . ASP B 1 115 ? 143.679 146.171 186.933 1.00 161.34 ? 115  ASP B CA    1 
ATOM   6440  C  C     . ASP B 1 115 ? 144.809 145.218 186.568 1.00 158.90 ? 115  ASP B C     1 
ATOM   6441  O  O     . ASP B 1 115 ? 144.757 144.027 186.897 1.00 158.17 ? 115  ASP B O     1 
ATOM   6442  C  CB    . ASP B 1 115 ? 142.669 146.270 185.792 1.00 160.53 ? 115  ASP B CB    1 
ATOM   6443  C  CG    . ASP B 1 115 ? 141.857 147.544 185.847 1.00 165.49 ? 115  ASP B CG    1 
ATOM   6444  O  OD1   . ASP B 1 115 ? 141.235 147.807 186.897 1.00 174.27 ? 115  ASP B OD1   1 
ATOM   6445  O  OD2   . ASP B 1 115 ? 141.837 148.281 184.841 1.00 160.96 ? 115  ASP B OD2   1 
ATOM   6446  N  N     . ALA B 1 116 ? 145.834 145.722 185.877 1.00 154.40 ? 116  ALA B N     1 
ATOM   6447  C  CA    . ALA B 1 116 ? 146.974 144.881 185.540 1.00 148.76 ? 116  ALA B CA    1 
ATOM   6448  C  C     . ALA B 1 116 ? 147.652 144.354 186.796 1.00 149.68 ? 116  ALA B C     1 
ATOM   6449  O  O     . ALA B 1 116 ? 147.949 143.160 186.890 1.00 152.22 ? 116  ALA B O     1 
ATOM   6450  C  CB    . ALA B 1 116 ? 147.966 145.659 184.679 1.00 148.77 ? 116  ALA B CB    1 
ATOM   6451  N  N     . LEU B 1 117 ? 147.881 145.225 187.780 1.00 148.63 ? 117  LEU B N     1 
ATOM   6452  C  CA    . LEU B 1 117 ? 148.480 144.789 189.035 1.00 147.71 ? 117  LEU B CA    1 
ATOM   6453  C  C     . LEU B 1 117 ? 147.588 143.783 189.746 1.00 154.41 ? 117  LEU B C     1 
ATOM   6454  O  O     . LEU B 1 117 ? 148.075 142.776 190.274 1.00 160.02 ? 117  LEU B O     1 
ATOM   6455  C  CB    . LEU B 1 117 ? 148.748 145.994 189.934 1.00 148.43 ? 117  LEU B CB    1 
ATOM   6456  C  CG    . LEU B 1 117 ? 149.264 145.682 191.338 1.00 155.79 ? 117  LEU B CG    1 
ATOM   6457  C  CD1   . LEU B 1 117 ? 150.565 144.902 191.267 1.00 157.12 ? 117  LEU B CD1   1 
ATOM   6458  C  CD2   . LEU B 1 117 ? 149.446 146.960 192.136 1.00 163.84 ? 117  LEU B CD2   1 
ATOM   6459  N  N     . LYS B 1 118 ? 146.275 144.028 189.755 1.00 155.02 ? 118  LYS B N     1 
ATOM   6460  C  CA    . LYS B 1 118 ? 145.364 143.112 190.436 1.00 155.51 ? 118  LYS B CA    1 
ATOM   6461  C  C     . LYS B 1 118 ? 145.418 141.719 189.819 1.00 152.50 ? 118  LYS B C     1 
ATOM   6462  O  O     . LYS B 1 118 ? 145.617 140.720 190.524 1.00 153.14 ? 118  LYS B O     1 
ATOM   6463  C  CB    . LYS B 1 118 ? 143.939 143.661 190.398 1.00 156.92 ? 118  LYS B CB    1 
ATOM   6464  C  CG    . LYS B 1 118 ? 142.941 142.804 191.154 1.00 158.86 ? 118  LYS B CG    1 
ATOM   6465  C  CD    . LYS B 1 118 ? 141.579 143.468 191.228 1.00 166.02 ? 118  LYS B CD    1 
ATOM   6466  C  CE    . LYS B 1 118 ? 140.971 143.627 189.847 1.00 160.77 ? 118  LYS B CE    1 
ATOM   6467  N  NZ    . LYS B 1 118 ? 139.630 144.267 189.908 1.00 165.96 ? 118  LYS B NZ    1 
ATOM   6468  N  N     . LEU B 1 119 ? 145.255 141.631 188.497 1.00 149.59 ? 119  LEU B N     1 
ATOM   6469  C  CA    . LEU B 1 119 ? 145.230 140.319 187.855 1.00 148.34 ? 119  LEU B CA    1 
ATOM   6470  C  C     . LEU B 1 119 ? 146.601 139.654 187.879 1.00 148.91 ? 119  LEU B C     1 
ATOM   6471  O  O     . LEU B 1 119 ? 146.694 138.426 187.989 1.00 152.39 ? 119  LEU B O     1 
ATOM   6472  C  CB    . LEU B 1 119 ? 144.704 140.428 186.425 1.00 143.25 ? 119  LEU B CB    1 
ATOM   6473  C  CG    . LEU B 1 119 ? 143.467 141.294 186.205 1.00 146.86 ? 119  LEU B CG    1 
ATOM   6474  C  CD1   . LEU B 1 119 ? 143.435 141.836 184.788 1.00 144.08 ? 119  LEU B CD1   1 
ATOM   6475  C  CD2   . LEU B 1 119 ? 142.209 140.504 186.506 1.00 151.78 ? 119  LEU B CD2   1 
ATOM   6476  N  N     . TYR B 1 120 ? 147.679 140.436 187.783 1.00 146.18 ? 120  TYR B N     1 
ATOM   6477  C  CA    . TYR B 1 120 ? 149.011 139.854 187.883 1.00 144.47 ? 120  TYR B CA    1 
ATOM   6478  C  C     . TYR B 1 120 ? 149.249 139.259 189.264 1.00 147.79 ? 120  TYR B C     1 
ATOM   6479  O  O     . TYR B 1 120 ? 149.806 138.163 189.385 1.00 154.54 ? 120  TYR B O     1 
ATOM   6480  C  CB    . TYR B 1 120 ? 150.068 140.906 187.552 1.00 143.06 ? 120  TYR B CB    1 
ATOM   6481  C  CG    . TYR B 1 120 ? 150.395 141.008 186.079 1.00 139.67 ? 120  TYR B CG    1 
ATOM   6482  C  CD1   . TYR B 1 120 ? 150.614 139.872 185.318 1.00 141.04 ? 120  TYR B CD1   1 
ATOM   6483  C  CD2   . TYR B 1 120 ? 150.477 142.241 185.451 1.00 139.38 ? 120  TYR B CD2   1 
ATOM   6484  C  CE1   . TYR B 1 120 ? 150.909 139.961 183.975 1.00 140.21 ? 120  TYR B CE1   1 
ATOM   6485  C  CE2   . TYR B 1 120 ? 150.770 142.339 184.110 1.00 136.55 ? 120  TYR B CE2   1 
ATOM   6486  C  CZ    . TYR B 1 120 ? 150.985 141.197 183.376 1.00 136.03 ? 120  TYR B CZ    1 
ATOM   6487  O  OH    . TYR B 1 120 ? 151.279 141.292 182.037 1.00 133.93 ? 120  TYR B OH    1 
ATOM   6488  N  N     . LEU B 1 121 ? 148.827 139.960 190.321 1.00 146.88 ? 121  LEU B N     1 
ATOM   6489  C  CA    . LEU B 1 121 ? 148.950 139.405 191.665 1.00 149.61 ? 121  LEU B CA    1 
ATOM   6490  C  C     . LEU B 1 121 ? 148.103 138.148 191.818 1.00 153.40 ? 121  LEU B C     1 
ATOM   6491  O  O     . LEU B 1 121 ? 148.536 137.162 192.431 1.00 156.30 ? 121  LEU B O     1 
ATOM   6492  C  CB    . LEU B 1 121 ? 148.552 140.450 192.706 1.00 149.22 ? 121  LEU B CB    1 
ATOM   6493  C  CG    . LEU B 1 121 ? 149.698 141.318 193.220 1.00 155.95 ? 121  LEU B CG    1 
ATOM   6494  C  CD1   . LEU B 1 121 ? 149.178 142.402 194.142 1.00 171.39 ? 121  LEU B CD1   1 
ATOM   6495  C  CD2   . LEU B 1 121 ? 150.729 140.459 193.928 1.00 158.90 ? 121  LEU B CD2   1 
ATOM   6496  N  N     . GLY B 1 123 ? 147.235 135.992 189.468 1.00 150.89 ? 123  GLY B N     1 
ATOM   6497  C  CA    . GLY B 1 123 ? 147.904 134.900 188.780 1.00 147.70 ? 123  GLY B CA    1 
ATOM   6498  C  C     . GLY B 1 123 ? 149.144 134.420 189.510 1.00 148.43 ? 123  GLY B C     1 
ATOM   6499  O  O     . GLY B 1 123 ? 149.412 133.215 189.573 1.00 152.20 ? 123  GLY B O     1 
ATOM   6500  N  N     . GLY B 1 124 ? 149.921 135.352 190.066 1.00 147.84 ? 124  GLY B N     1 
ATOM   6501  C  CA    . GLY B 1 124 ? 151.112 134.961 190.798 1.00 149.43 ? 124  GLY B CA    1 
ATOM   6502  C  C     . GLY B 1 124 ? 150.794 134.093 191.999 1.00 154.04 ? 124  GLY B C     1 
ATOM   6503  O  O     . GLY B 1 124 ? 151.391 133.030 192.187 1.00 157.37 ? 124  GLY B O     1 
ATOM   6504  N  N     . ALA B 1 128 ? 151.623 130.141 192.572 1.00 150.53 ? 128  ALA B N     1 
ATOM   6505  C  CA    . ALA B 1 128 ? 152.367 129.801 193.779 1.00 154.52 ? 128  ALA B CA    1 
ATOM   6506  C  C     . ALA B 1 128 ? 151.645 128.726 194.580 1.00 158.35 ? 128  ALA B C     1 
ATOM   6507  O  O     . ALA B 1 128 ? 152.281 127.837 195.158 1.00 160.39 ? 128  ALA B O     1 
ATOM   6508  C  CB    . ALA B 1 128 ? 152.593 131.050 194.630 1.00 157.27 ? 128  ALA B CB    1 
ATOM   6509  N  N     . ASN B 1 129 ? 150.313 128.789 194.622 1.00 158.99 ? 129  ASN B N     1 
ATOM   6510  C  CA    . ASN B 1 129 ? 149.549 127.770 195.335 1.00 161.00 ? 129  ASN B CA    1 
ATOM   6511  C  C     . ASN B 1 129 ? 149.461 126.475 194.534 1.00 161.51 ? 129  ASN B C     1 
ATOM   6512  O  O     . ASN B 1 129 ? 149.474 125.381 195.111 1.00 163.97 ? 129  ASN B O     1 
ATOM   6513  C  CB    . ASN B 1 129 ? 148.153 128.298 195.658 1.00 159.45 ? 129  ASN B CB    1 
ATOM   6514  C  CG    . ASN B 1 129 ? 148.159 129.291 196.804 1.00 162.90 ? 129  ASN B CG    1 
ATOM   6515  O  OD1   . ASN B 1 129 ? 149.012 129.229 197.690 1.00 164.45 ? 129  ASN B OD1   1 
ATOM   6516  N  ND2   . ASN B 1 129 ? 147.207 130.216 196.791 1.00 163.77 ? 129  ASN B ND2   1 
ATOM   6517  N  N     . VAL B 1 130 ? 149.367 126.577 193.206 1.00 158.27 ? 130  VAL B N     1 
ATOM   6518  C  CA    . VAL B 1 130 ? 149.183 125.394 192.369 1.00 156.59 ? 130  VAL B CA    1 
ATOM   6519  C  C     . VAL B 1 130 ? 150.449 124.544 192.333 1.00 159.61 ? 130  VAL B C     1 
ATOM   6520  O  O     . VAL B 1 130 ? 150.381 123.308 192.334 1.00 160.58 ? 130  VAL B O     1 
ATOM   6521  C  CB    . VAL B 1 130 ? 148.735 125.813 190.956 1.00 147.22 ? 130  VAL B CB    1 
ATOM   6522  C  CG1   . VAL B 1 130 ? 149.070 124.737 189.938 1.00 144.75 ? 130  VAL B CG1   1 
ATOM   6523  C  CG2   . VAL B 1 130 ? 147.247 126.108 190.943 1.00 151.79 ? 130  VAL B CG2   1 
ATOM   6524  N  N     . ALA B 1 131 ? 151.621 125.187 192.313 1.00 157.56 ? 131  ALA B N     1 
ATOM   6525  C  CA    . ALA B 1 131 ? 152.866 124.468 192.054 1.00 156.30 ? 131  ALA B CA    1 
ATOM   6526  C  C     . ALA B 1 131 ? 153.109 123.338 193.047 1.00 162.70 ? 131  ALA B C     1 
ATOM   6527  O  O     . ALA B 1 131 ? 153.711 122.320 192.686 1.00 164.53 ? 131  ALA B O     1 
ATOM   6528  C  CB    . ALA B 1 131 ? 154.042 125.443 192.071 1.00 153.43 ? 131  ALA B CB    1 
ATOM   6529  N  N     . ARG B 1 133 ? 150.929 121.349 194.245 1.00 166.44 ? 133  ARG B N     1 
ATOM   6530  C  CA    . ARG B 1 133 ? 150.067 120.214 193.937 1.00 167.07 ? 133  ARG B CA    1 
ATOM   6531  C  C     . ARG B 1 133 ? 150.616 119.358 192.802 1.00 167.60 ? 133  ARG B C     1 
ATOM   6532  O  O     . ARG B 1 133 ? 150.403 118.139 192.794 1.00 170.76 ? 133  ARG B O     1 
ATOM   6533  C  CB    . ARG B 1 133 ? 148.659 120.713 193.605 1.00 166.15 ? 133  ARG B CB    1 
ATOM   6534  C  CG    . ARG B 1 133 ? 147.767 119.705 192.902 1.00 169.50 ? 133  ARG B CG    1 
ATOM   6535  C  CD    . ARG B 1 133 ? 146.286 120.055 193.031 1.00 173.19 ? 133  ARG B CD    1 
ATOM   6536  N  NE    . ARG B 1 133 ? 146.037 121.488 193.136 1.00 175.60 ? 133  ARG B NE    1 
ATOM   6537  C  CZ    . ARG B 1 133 ? 145.796 122.127 194.274 1.00 176.21 ? 133  ARG B CZ    1 
ATOM   6538  N  NH1   . ARG B 1 133 ? 145.766 121.489 195.432 1.00 173.94 ? 133  ARG B NH1   1 
ATOM   6539  N  NH2   . ARG B 1 133 ? 145.582 123.439 194.248 1.00 176.15 ? 133  ARG B NH2   1 
ATOM   6540  N  N     . GLN B 1 134 ? 151.329 119.960 191.853 1.00 164.75 ? 134  GLN B N     1 
ATOM   6541  C  CA    . GLN B 1 134 ? 151.856 119.205 190.723 1.00 164.72 ? 134  GLN B CA    1 
ATOM   6542  C  C     . GLN B 1 134 ? 152.887 118.183 191.185 1.00 166.88 ? 134  GLN B C     1 
ATOM   6543  O  O     . GLN B 1 134 ? 153.780 118.488 191.980 1.00 166.16 ? 134  GLN B O     1 
ATOM   6544  C  CB    . GLN B 1 134 ? 152.484 120.152 189.700 1.00 161.09 ? 134  GLN B CB    1 
ATOM   6545  C  CG    . GLN B 1 134 ? 151.490 121.016 188.947 1.00 155.55 ? 134  GLN B CG    1 
ATOM   6546  C  CD    . GLN B 1 134 ? 150.560 120.206 188.072 1.00 149.32 ? 134  GLN B CD    1 
ATOM   6547  O  OE1   . GLN B 1 134 ? 150.910 119.118 187.615 1.00 151.75 ? 134  GLN B OE1   1 
ATOM   6548  N  NE2   . GLN B 1 134 ? 149.369 120.735 187.826 1.00 145.29 ? 134  GLN B NE2   1 
ATOM   6549  N  N     . ALA B 1 135 ? 152.756 116.956 190.677 1.00 165.81 ? 135  ALA B N     1 
ATOM   6550  C  CA    . ALA B 1 135 ? 153.710 115.905 191.012 1.00 167.89 ? 135  ALA B CA    1 
ATOM   6551  C  C     . ALA B 1 135 ? 154.897 115.887 190.060 1.00 170.87 ? 135  ALA B C     1 
ATOM   6552  O  O     . ALA B 1 135 ? 155.958 115.360 190.412 1.00 173.25 ? 135  ALA B O     1 
ATOM   6553  C  CB    . ALA B 1 135 ? 153.017 114.542 191.012 1.00 167.56 ? 135  ALA B CB    1 
ATOM   6554  N  N     . ASN B 1 136 ? 154.741 116.442 188.865 1.00 166.82 ? 136  ASN B N     1 
ATOM   6555  C  CA    . ASN B 1 136 ? 155.840 116.497 187.909 1.00 162.40 ? 136  ASN B CA    1 
ATOM   6556  C  C     . ASN B 1 136 ? 156.893 117.479 188.401 1.00 159.66 ? 136  ASN B C     1 
ATOM   6557  O  O     . ASN B 1 136 ? 156.578 118.660 188.598 1.00 159.88 ? 136  ASN B O     1 
ATOM   6558  C  CB    . ASN B 1 136 ? 155.322 116.911 186.535 1.00 155.45 ? 136  ASN B CB    1 
ATOM   6559  C  CG    . ASN B 1 136 ? 156.302 116.601 185.423 1.00 154.80 ? 136  ASN B CG    1 
ATOM   6560  O  OD1   . ASN B 1 136 ? 157.515 116.717 185.595 1.00 155.56 ? 136  ASN B OD1   1 
ATOM   6561  N  ND2   . ASN B 1 136 ? 155.779 116.204 184.269 1.00 153.29 ? 136  ASN B ND2   1 
ATOM   6562  N  N     . PRO B 1 137 ? 158.136 117.045 188.628 1.00 158.43 ? 137  PRO B N     1 
ATOM   6563  C  CA    . PRO B 1 137 ? 159.153 117.987 189.126 1.00 160.04 ? 137  PRO B CA    1 
ATOM   6564  C  C     . PRO B 1 137 ? 159.396 119.162 188.198 1.00 158.48 ? 137  PRO B C     1 
ATOM   6565  O  O     . PRO B 1 137 ? 159.555 120.295 188.670 1.00 159.06 ? 137  PRO B O     1 
ATOM   6566  C  CB    . PRO B 1 137 ? 160.402 117.105 189.268 1.00 170.21 ? 137  PRO B CB    1 
ATOM   6567  C  CG    . PRO B 1 137 ? 159.876 115.711 189.382 1.00 167.46 ? 137  PRO B CG    1 
ATOM   6568  C  CD    . PRO B 1 137 ? 158.654 115.672 188.520 1.00 160.97 ? 137  PRO B CD    1 
ATOM   6569  N  N     . LYS B 1 138 ? 159.403 118.932 186.883 1.00 156.79 ? 138  LYS B N     1 
ATOM   6570  C  CA    . LYS B 1 138 ? 159.696 120.017 185.952 1.00 154.54 ? 138  LYS B CA    1 
ATOM   6571  C  C     . LYS B 1 138 ? 158.584 121.057 185.949 1.00 148.64 ? 138  LYS B C     1 
ATOM   6572  O  O     . LYS B 1 138 ? 158.854 122.262 186.001 1.00 149.03 ? 138  LYS B O     1 
ATOM   6573  C  CB    . LYS B 1 138 ? 159.920 119.464 184.546 1.00 150.87 ? 138  LYS B CB    1 
ATOM   6574  C  CG    . LYS B 1 138 ? 160.003 120.537 183.473 1.00 145.01 ? 138  LYS B CG    1 
ATOM   6575  C  CD    . LYS B 1 138 ? 160.091 119.930 182.083 1.00 143.94 ? 138  LYS B CD    1 
ATOM   6576  C  CE    . LYS B 1 138 ? 161.409 119.193 181.896 1.00 151.80 ? 138  LYS B CE    1 
ATOM   6577  N  NZ    . LYS B 1 138 ? 161.557 118.636 180.524 1.00 147.77 ? 138  LYS B NZ    1 
ATOM   6578  N  N     . ILE B 1 139 ? 157.327 120.612 185.900 1.00 146.83 ? 139  ILE B N     1 
ATOM   6579  C  CA    . ILE B 1 139 ? 156.212 121.555 185.915 1.00 144.38 ? 139  ILE B CA    1 
ATOM   6580  C  C     . ILE B 1 139 ? 156.136 122.269 187.258 1.00 144.84 ? 139  ILE B C     1 
ATOM   6581  O  O     . ILE B 1 139 ? 155.837 123.466 187.322 1.00 144.01 ? 139  ILE B O     1 
ATOM   6582  C  CB    . ILE B 1 139 ? 154.894 120.839 185.576 1.00 144.91 ? 139  ILE B CB    1 
ATOM   6583  C  CG1   . ILE B 1 139 ? 154.947 120.284 184.155 1.00 142.42 ? 139  ILE B CG1   1 
ATOM   6584  C  CG2   . ILE B 1 139 ? 153.720 121.790 185.714 1.00 142.12 ? 139  ILE B CG2   1 
ATOM   6585  C  CD1   . ILE B 1 139 ? 155.105 121.352 183.102 1.00 135.05 ? 139  ILE B CD1   1 
ATOM   6586  N  N     . CYS B 1 140 ? 156.408 121.552 188.350 1.00 146.24 ? 140  CYS B N     1 
ATOM   6587  C  CA    . CYS B 1 140 ? 156.404 122.186 189.663 1.00 146.84 ? 140  CYS B CA    1 
ATOM   6588  C  C     . CYS B 1 140 ? 157.452 123.290 189.738 1.00 146.61 ? 140  CYS B C     1 
ATOM   6589  O  O     . CYS B 1 140 ? 157.168 124.402 190.199 1.00 144.97 ? 140  CYS B O     1 
ATOM   6590  C  CB    . CYS B 1 140 ? 156.639 121.138 190.751 1.00 154.29 ? 140  CYS B CB    1 
ATOM   6591  S  SG    . CYS B 1 140 ? 156.921 121.815 192.403 1.00 159.73 ? 140  CYS B SG    1 
ATOM   6592  N  N     . ASN B 1 141 ? 158.670 123.005 189.268 1.00 149.43 ? 141  ASN B N     1 
ATOM   6593  C  CA    . ASN B 1 141 ? 159.724 124.015 189.285 1.00 148.11 ? 141  ASN B CA    1 
ATOM   6594  C  C     . ASN B 1 141 ? 159.382 125.189 188.378 1.00 142.98 ? 141  ASN B C     1 
ATOM   6595  O  O     . ASN B 1 141 ? 159.598 126.350 188.748 1.00 145.09 ? 141  ASN B O     1 
ATOM   6596  C  CB    . ASN B 1 141 ? 161.057 123.390 188.878 1.00 155.23 ? 141  ASN B CB    1 
ATOM   6597  C  CG    . ASN B 1 141 ? 161.531 122.338 189.860 1.00 170.03 ? 141  ASN B CG    1 
ATOM   6598  O  OD1   . ASN B 1 141 ? 160.833 122.010 190.818 1.00 174.28 ? 141  ASN B OD1   1 
ATOM   6599  N  ND2   . ASN B 1 141 ? 162.723 121.803 189.626 1.00 182.40 ? 141  ASN B ND2   1 
ATOM   6600  N  N     . LEU B 1 142 ? 158.845 124.912 187.187 1.00 137.65 ? 142  LEU B N     1 
ATOM   6601  C  CA    . LEU B 1 142 ? 158.494 125.993 186.271 1.00 135.47 ? 142  LEU B CA    1 
ATOM   6602  C  C     . LEU B 1 142 ? 157.411 126.888 186.855 1.00 137.22 ? 142  LEU B C     1 
ATOM   6603  O  O     . LEU B 1 142 ? 157.500 128.116 186.764 1.00 137.63 ? 142  LEU B O     1 
ATOM   6604  C  CB    . LEU B 1 142 ? 158.045 125.428 184.925 1.00 132.69 ? 142  LEU B CB    1 
ATOM   6605  C  CG    . LEU B 1 142 ? 159.140 124.876 184.015 1.00 135.29 ? 142  LEU B CG    1 
ATOM   6606  C  CD1   . LEU B 1 142 ? 158.572 124.547 182.648 1.00 125.07 ? 142  LEU B CD1   1 
ATOM   6607  C  CD2   . LEU B 1 142 ? 160.283 125.866 183.902 1.00 136.07 ? 142  LEU B CD2   1 
ATOM   6608  N  N     . LEU B 1 143 ? 156.383 126.295 187.464 1.00 138.70 ? 143  LEU B N     1 
ATOM   6609  C  CA    . LEU B 1 143 ? 155.306 127.103 188.026 1.00 135.43 ? 143  LEU B CA    1 
ATOM   6610  C  C     . LEU B 1 143 ? 155.774 127.875 189.251 1.00 135.71 ? 143  LEU B C     1 
ATOM   6611  O  O     . LEU B 1 143 ? 155.373 129.026 189.452 1.00 134.67 ? 143  LEU B O     1 
ATOM   6612  C  CB    . LEU B 1 143 ? 154.103 126.223 188.361 1.00 137.55 ? 143  LEU B CB    1 
ATOM   6613  C  CG    . LEU B 1 143 ? 153.387 125.619 187.152 1.00 131.79 ? 143  LEU B CG    1 
ATOM   6614  C  CD1   . LEU B 1 143 ? 152.132 124.885 187.581 1.00 140.43 ? 143  LEU B CD1   1 
ATOM   6615  C  CD2   . LEU B 1 143 ? 153.053 126.701 186.144 1.00 123.65 ? 143  LEU B CD2   1 
ATOM   6616  N  N     . THR B 1 144 ? 156.628 127.270 190.081 1.00 136.80 ? 144  THR B N     1 
ATOM   6617  C  CA    . THR B 1 144 ? 157.177 128.000 191.218 1.00 133.54 ? 144  THR B CA    1 
ATOM   6618  C  C     . THR B 1 144 ? 157.998 129.196 190.752 1.00 139.13 ? 144  THR B C     1 
ATOM   6619  O  O     . THR B 1 144 ? 157.857 130.306 191.281 1.00 146.54 ? 144  THR B O     1 
ATOM   6620  C  CB    . THR B 1 144 ? 158.026 127.069 192.083 1.00 135.42 ? 144  THR B CB    1 
ATOM   6621  O  OG1   . THR B 1 144 ? 157.237 125.950 192.502 1.00 138.69 ? 144  THR B OG1   1 
ATOM   6622  C  CG2   . THR B 1 144 ? 158.539 127.803 193.309 1.00 141.33 ? 144  THR B CG2   1 
ATOM   6623  N  N     . SER B 1 145 ? 158.853 128.990 189.747 1.00 138.80 ? 145  SER B N     1 
ATOM   6624  C  CA    . SER B 1 145 ? 159.668 130.086 189.234 1.00 137.96 ? 145  SER B CA    1 
ATOM   6625  C  C     . SER B 1 145 ? 158.803 131.166 188.599 1.00 138.40 ? 145  SER B C     1 
ATOM   6626  O  O     . SER B 1 145 ? 159.059 132.362 188.782 1.00 144.61 ? 145  SER B O     1 
ATOM   6627  C  CB    . SER B 1 145 ? 160.689 129.555 188.230 1.00 140.56 ? 145  SER B CB    1 
ATOM   6628  O  OG    . SER B 1 145 ? 161.576 130.578 187.818 1.00 145.03 ? 145  SER B OG    1 
ATOM   6629  N  N     . LYS B 1 146 ? 157.776 130.766 187.846 1.00 133.60 ? 146  LYS B N     1 
ATOM   6630  C  CA    . LYS B 1 146 ? 156.885 131.740 187.227 1.00 132.32 ? 146  LYS B CA    1 
ATOM   6631  C  C     . LYS B 1 146 ? 156.131 132.546 188.275 1.00 136.41 ? 146  LYS B C     1 
ATOM   6632  O  O     . LYS B 1 146 ? 155.983 133.764 188.140 1.00 138.63 ? 146  LYS B O     1 
ATOM   6633  C  CB    . LYS B 1 146 ? 155.908 131.037 186.290 1.00 127.26 ? 146  LYS B CB    1 
ATOM   6634  C  CG    . LYS B 1 146 ? 155.796 131.683 184.926 1.00 123.03 ? 146  LYS B CG    1 
ATOM   6635  C  CD    . LYS B 1 146 ? 155.223 133.083 185.017 1.00 120.10 ? 146  LYS B CD    1 
ATOM   6636  C  CE    . LYS B 1 146 ? 155.197 133.751 183.655 1.00 119.26 ? 146  LYS B CE    1 
ATOM   6637  N  NZ    . LYS B 1 146 ? 154.723 135.158 183.733 1.00 122.66 ? 146  LYS B NZ    1 
ATOM   6638  N  N     . GLY B 1 147 ? 155.642 131.885 189.325 1.00 138.58 ? 147  GLY B N     1 
ATOM   6639  C  CA    . GLY B 1 147 ? 154.970 132.610 190.388 1.00 139.35 ? 147  GLY B CA    1 
ATOM   6640  C  C     . GLY B 1 147 ? 155.893 133.579 191.097 1.00 141.41 ? 147  GLY B C     1 
ATOM   6641  O  O     . GLY B 1 147 ? 155.512 134.716 191.382 1.00 148.04 ? 147  GLY B O     1 
ATOM   6642  N  N     . PHE B 1 148 ? 157.124 133.148 191.382 1.00 140.48 ? 148  PHE B N     1 
ATOM   6643  C  CA    . PHE B 1 148 ? 158.077 134.031 192.044 1.00 143.45 ? 148  PHE B CA    1 
ATOM   6644  C  C     . PHE B 1 148 ? 158.390 135.244 191.177 1.00 143.39 ? 148  PHE B C     1 
ATOM   6645  O  O     . PHE B 1 148 ? 158.412 136.384 191.664 1.00 149.52 ? 148  PHE B O     1 
ATOM   6646  C  CB    . PHE B 1 148 ? 159.354 133.257 192.368 1.00 147.73 ? 148  PHE B CB    1 
ATOM   6647  C  CG    . PHE B 1 148 ? 159.286 132.482 193.653 1.00 158.55 ? 148  PHE B CG    1 
ATOM   6648  C  CD1   . PHE B 1 148 ? 158.084 132.332 194.327 1.00 159.28 ? 148  PHE B CD1   1 
ATOM   6649  C  CD2   . PHE B 1 148 ? 160.418 131.875 194.170 1.00 166.07 ? 148  PHE B CD2   1 
ATOM   6650  C  CE1   . PHE B 1 148 ? 158.017 131.610 195.503 1.00 170.59 ? 148  PHE B CE1   1 
ATOM   6651  C  CE2   . PHE B 1 148 ? 160.356 131.149 195.343 1.00 176.67 ? 148  PHE B CE2   1 
ATOM   6652  C  CZ    . PHE B 1 148 ? 159.155 131.019 196.012 1.00 181.94 ? 148  PHE B CZ    1 
ATOM   6653  N  N     . GLU B 1 149 ? 158.618 135.018 189.880 1.00 140.85 ? 149  GLU B N     1 
ATOM   6654  C  CA    . GLU B 1 149 ? 158.915 136.118 188.970 1.00 142.75 ? 149  GLU B CA    1 
ATOM   6655  C  C     . GLU B 1 149 ? 157.728 137.062 188.833 1.00 143.07 ? 149  GLU B C     1 
ATOM   6656  O  O     . GLU B 1 149 ? 157.900 138.286 188.794 1.00 147.92 ? 149  GLU B O     1 
ATOM   6657  C  CB    . GLU B 1 149 ? 159.326 135.566 187.606 1.00 140.03 ? 149  GLU B CB    1 
ATOM   6658  C  CG    . GLU B 1 149 ? 159.370 136.603 186.500 1.00 138.82 ? 149  GLU B CG    1 
ATOM   6659  C  CD    . GLU B 1 149 ? 159.512 135.979 185.127 1.00 145.65 ? 149  GLU B CD    1 
ATOM   6660  O  OE1   . GLU B 1 149 ? 159.827 134.773 185.049 1.00 144.03 ? 149  GLU B OE1   1 
ATOM   6661  O  OE2   . GLU B 1 149 ? 159.304 136.693 184.124 1.00 148.81 ? 149  GLU B OE2   1 
ATOM   6662  N  N     . THR B 1 150 ? 156.513 136.515 188.759 1.00 140.60 ? 150  THR B N     1 
ATOM   6663  C  CA    . THR B 1 150 ? 155.334 137.361 188.637 1.00 141.17 ? 150  THR B CA    1 
ATOM   6664  C  C     . THR B 1 150 ? 155.111 138.180 189.901 1.00 146.16 ? 150  THR B C     1 
ATOM   6665  O  O     . THR B 1 150 ? 154.694 139.337 189.828 1.00 148.19 ? 150  THR B O     1 
ATOM   6666  C  CB    . THR B 1 150 ? 154.104 136.513 188.322 1.00 140.55 ? 150  THR B CB    1 
ATOM   6667  O  OG1   . THR B 1 150 ? 154.390 135.654 187.213 1.00 143.42 ? 150  THR B OG1   1 
ATOM   6668  C  CG2   . THR B 1 150 ? 152.928 137.402 187.962 1.00 139.66 ? 150  THR B CG2   1 
ATOM   6669  N  N     . LEU B 1 151 ? 155.389 137.602 191.072 1.00 147.30 ? 151  LEU B N     1 
ATOM   6670  C  CA    . LEU B 1 151 ? 155.274 138.373 192.306 1.00 149.06 ? 151  LEU B CA    1 
ATOM   6671  C  C     . LEU B 1 151 ? 156.317 139.484 192.364 1.00 155.33 ? 151  LEU B C     1 
ATOM   6672  O  O     . LEU B 1 151 ? 156.022 140.600 192.809 1.00 160.10 ? 151  LEU B O     1 
ATOM   6673  C  CB    . LEU B 1 151 ? 155.394 137.454 193.520 1.00 156.60 ? 151  LEU B CB    1 
ATOM   6674  C  CG    . LEU B 1 151 ? 154.239 136.471 193.716 1.00 156.78 ? 151  LEU B CG    1 
ATOM   6675  C  CD1   . LEU B 1 151 ? 154.416 135.682 195.004 1.00 163.97 ? 151  LEU B CD1   1 
ATOM   6676  C  CD2   . LEU B 1 151 ? 152.908 137.199 193.703 1.00 154.87 ? 151  LEU B CD2   1 
ATOM   6677  N  N     . ASN B 1 152 ? 157.546 139.199 191.921 1.00 150.59 ? 152  ASN B N     1 
ATOM   6678  C  CA    . ASN B 1 152 ? 158.558 140.251 191.861 1.00 146.46 ? 152  ASN B CA    1 
ATOM   6679  C  C     . ASN B 1 152 ? 158.133 141.366 190.913 1.00 147.90 ? 152  ASN B C     1 
ATOM   6680  O  O     . ASN B 1 152 ? 158.300 142.554 191.218 1.00 157.21 ? 152  ASN B O     1 
ATOM   6681  C  CB    . ASN B 1 152 ? 159.904 139.668 191.435 1.00 146.77 ? 152  ASN B CB    1 
ATOM   6682  C  CG    . ASN B 1 152 ? 160.482 138.723 192.467 1.00 154.26 ? 152  ASN B CG    1 
ATOM   6683  O  OD1   . ASN B 1 152 ? 159.913 138.538 193.542 1.00 159.04 ? 152  ASN B OD1   1 
ATOM   6684  N  ND2   . ASN B 1 152 ? 161.621 138.121 192.146 1.00 155.49 ? 152  ASN B ND2   1 
ATOM   6685  N  N     . TRP B 1 153 ? 157.570 141.001 189.760 1.00 143.24 ? 153  TRP B N     1 
ATOM   6686  C  CA    . TRP B 1 153 ? 157.093 142.005 188.816 1.00 144.74 ? 153  TRP B CA    1 
ATOM   6687  C  C     . TRP B 1 153 ? 155.926 142.799 189.392 1.00 148.20 ? 153  TRP B C     1 
ATOM   6688  O  O     . TRP B 1 153 ? 155.806 144.004 189.146 1.00 151.62 ? 153  TRP B O     1 
ATOM   6689  C  CB    . TRP B 1 153 ? 156.698 141.340 187.500 1.00 140.73 ? 153  TRP B CB    1 
ATOM   6690  C  CG    . TRP B 1 153 ? 155.611 142.053 186.771 1.00 135.17 ? 153  TRP B CG    1 
ATOM   6691  C  CD1   . TRP B 1 153 ? 154.343 141.608 186.558 1.00 138.30 ? 153  TRP B CD1   1 
ATOM   6692  C  CD2   . TRP B 1 153 ? 155.690 143.344 186.161 1.00 136.68 ? 153  TRP B CD2   1 
ATOM   6693  N  NE1   . TRP B 1 153 ? 153.627 142.538 185.849 1.00 135.76 ? 153  TRP B NE1   1 
ATOM   6694  C  CE2   . TRP B 1 153 ? 154.432 143.615 185.594 1.00 135.66 ? 153  TRP B CE2   1 
ATOM   6695  C  CE3   . TRP B 1 153 ? 156.703 144.299 186.040 1.00 144.78 ? 153  TRP B CE3   1 
ATOM   6696  C  CZ2   . TRP B 1 153 ? 154.159 144.798 184.917 1.00 138.82 ? 153  TRP B CZ2   1 
ATOM   6697  C  CZ3   . TRP B 1 153 ? 156.430 145.473 185.366 1.00 144.78 ? 153  TRP B CZ3   1 
ATOM   6698  C  CH2   . TRP B 1 153 ? 155.169 145.712 184.812 1.00 141.74 ? 153  TRP B CH2   1 
ATOM   6699  N  N     . CYS B 1 154 ? 155.045 142.139 190.146 1.00 148.15 ? 154  CYS B N     1 
ATOM   6700  C  CA    . CYS B 1 154 ? 153.952 142.848 190.801 1.00 148.89 ? 154  CYS B CA    1 
ATOM   6701  C  C     . CYS B 1 154 ? 154.480 143.853 191.811 1.00 151.90 ? 154  CYS B C     1 
ATOM   6702  O  O     . CYS B 1 154 ? 153.960 144.967 191.916 1.00 155.85 ? 154  CYS B O     1 
ATOM   6703  C  CB    . CYS B 1 154 ? 153.012 141.860 191.487 1.00 154.99 ? 154  CYS B CB    1 
ATOM   6704  S  SG    . CYS B 1 154 ? 152.049 140.835 190.371 1.00 162.14 ? 154  CYS B SG    1 
ATOM   6705  N  N     . ALA B 1 155 ? 155.502 143.469 192.577 1.00 153.05 ? 155  ALA B N     1 
ATOM   6706  C  CA    . ALA B 1 155 ? 156.119 144.409 193.507 1.00 154.51 ? 155  ALA B CA    1 
ATOM   6707  C  C     . ALA B 1 155 ? 156.723 145.591 192.760 1.00 156.16 ? 155  ALA B C     1 
ATOM   6708  O  O     . ALA B 1 155 ? 156.585 146.747 193.181 1.00 160.88 ? 155  ALA B O     1 
ATOM   6709  C  CB    . ALA B 1 155 ? 157.180 143.699 194.346 1.00 162.78 ? 155  ALA B CB    1 
ATOM   6710  N  N     . ARG B 1 156 ? 157.391 145.316 191.636 1.00 156.66 ? 156  ARG B N     1 
ATOM   6711  C  CA    . ARG B 1 156 ? 157.973 146.392 190.839 1.00 159.27 ? 156  ARG B CA    1 
ATOM   6712  C  C     . ARG B 1 156 ? 156.898 147.341 190.321 1.00 160.34 ? 156  ARG B C     1 
ATOM   6713  O  O     . ARG B 1 156 ? 157.064 148.564 190.368 1.00 168.17 ? 156  ARG B O     1 
ATOM   6714  C  CB    . ARG B 1 156 ? 158.779 145.811 189.678 1.00 158.64 ? 156  ARG B CB    1 
ATOM   6715  C  CG    . ARG B 1 156 ? 160.237 145.533 190.005 1.00 167.10 ? 156  ARG B CG    1 
ATOM   6716  C  CD    . ARG B 1 156 ? 160.984 146.811 190.345 1.00 175.20 ? 156  ARG B CD    1 
ATOM   6717  N  NE    . ARG B 1 156 ? 161.245 147.623 189.163 1.00 181.87 ? 156  ARG B NE    1 
ATOM   6718  C  CZ    . ARG B 1 156 ? 162.421 147.706 188.555 1.00 184.20 ? 156  ARG B CZ    1 
ATOM   6719  N  NH1   . ARG B 1 156 ? 163.475 147.037 188.994 1.00 185.13 ? 156  ARG B NH1   1 
ATOM   6720  N  NH2   . ARG B 1 156 ? 162.543 148.482 187.482 1.00 183.17 ? 156  ARG B NH2   1 
ATOM   6721  N  N     . LEU B 1 157 ? 155.781 146.796 189.837 1.00 153.21 ? 157  LEU B N     1 
ATOM   6722  C  CA    . LEU B 1 157 ? 154.717 147.642 189.300 1.00 153.05 ? 157  LEU B CA    1 
ATOM   6723  C  C     . LEU B 1 157 ? 154.009 148.419 190.405 1.00 158.89 ? 157  LEU B C     1 
ATOM   6724  O  O     . LEU B 1 157 ? 153.601 149.568 190.199 1.00 163.15 ? 157  LEU B O     1 
ATOM   6725  C  CB    . LEU B 1 157 ? 153.719 146.795 188.514 1.00 148.47 ? 157  LEU B CB    1 
ATOM   6726  C  CG    . LEU B 1 157 ? 152.616 147.570 187.795 1.00 145.28 ? 157  LEU B CG    1 
ATOM   6727  C  CD1   . LEU B 1 157 ? 153.223 148.591 186.858 1.00 148.82 ? 157  LEU B CD1   1 
ATOM   6728  C  CD2   . LEU B 1 157 ? 151.708 146.626 187.033 1.00 143.08 ? 157  LEU B CD2   1 
ATOM   6729  N  N     . CYS B 1 158 ? 153.845 147.808 191.580 1.00 160.39 ? 158  CYS B N     1 
ATOM   6730  C  CA    . CYS B 1 158 ? 153.268 148.527 192.710 1.00 164.17 ? 158  CYS B CA    1 
ATOM   6731  C  C     . CYS B 1 158 ? 154.156 149.690 193.125 1.00 167.85 ? 158  CYS B C     1 
ATOM   6732  O  O     . CYS B 1 158 ? 153.663 150.791 193.394 1.00 172.72 ? 158  CYS B O     1 
ATOM   6733  C  CB    . CYS B 1 158 ? 153.046 147.572 193.882 1.00 169.52 ? 158  CYS B CB    1 
ATOM   6734  S  SG    . CYS B 1 158 ? 152.366 148.348 195.364 1.00 182.66 ? 158  CYS B SG    1 
ATOM   6735  N  N     . ASP B 1 159 ? 155.472 149.468 193.175 1.00 167.97 ? 159  ASP B N     1 
ATOM   6736  C  CA    . ASP B 1 159 ? 156.388 150.567 193.466 1.00 169.21 ? 159  ASP B CA    1 
ATOM   6737  C  C     . ASP B 1 159 ? 156.329 151.631 192.378 1.00 169.82 ? 159  ASP B C     1 
ATOM   6738  O  O     . ASP B 1 159 ? 156.405 152.831 192.667 1.00 177.15 ? 159  ASP B O     1 
ATOM   6739  C  CB    . ASP B 1 159 ? 157.813 150.037 193.627 1.00 171.01 ? 159  ASP B CB    1 
ATOM   6740  C  CG    . ASP B 1 159 ? 158.011 149.287 194.929 1.00 175.64 ? 159  ASP B CG    1 
ATOM   6741  O  OD1   . ASP B 1 159 ? 157.291 149.586 195.904 1.00 177.82 ? 159  ASP B OD1   1 
ATOM   6742  O  OD2   . ASP B 1 159 ? 158.889 148.400 194.979 1.00 177.07 ? 159  ASP B OD2   1 
ATOM   6743  N  N     . TRP B 1 160 ? 156.189 151.209 191.121 1.00 163.99 ? 160  TRP B N     1 
ATOM   6744  C  CA    . TRP B 1 160 ? 156.092 152.157 190.016 1.00 166.54 ? 160  TRP B CA    1 
ATOM   6745  C  C     . TRP B 1 160 ? 154.856 153.038 190.144 1.00 167.15 ? 160  TRP B C     1 
ATOM   6746  O  O     . TRP B 1 160 ? 154.922 154.249 189.908 1.00 168.73 ? 160  TRP B O     1 
ATOM   6747  C  CB    . TRP B 1 160 ? 156.084 151.397 188.690 1.00 163.84 ? 160  TRP B CB    1 
ATOM   6748  C  CG    . TRP B 1 160 ? 156.055 152.267 187.477 1.00 163.71 ? 160  TRP B CG    1 
ATOM   6749  C  CD1   . TRP B 1 160 ? 157.121 152.848 186.861 1.00 167.98 ? 160  TRP B CD1   1 
ATOM   6750  C  CD2   . TRP B 1 160 ? 154.901 152.631 186.711 1.00 161.17 ? 160  TRP B CD2   1 
ATOM   6751  N  NE1   . TRP B 1 160 ? 156.703 153.564 185.767 1.00 168.31 ? 160  TRP B NE1   1 
ATOM   6752  C  CE2   . TRP B 1 160 ? 155.344 153.445 185.653 1.00 161.85 ? 160  TRP B CE2   1 
ATOM   6753  C  CE3   . TRP B 1 160 ? 153.537 152.352 186.822 1.00 161.46 ? 160  TRP B CE3   1 
ATOM   6754  C  CZ2   . TRP B 1 160 ? 154.472 153.985 184.712 1.00 156.31 ? 160  TRP B CZ2   1 
ATOM   6755  C  CZ3   . TRP B 1 160 ? 152.673 152.887 185.886 1.00 161.39 ? 160  TRP B CZ3   1 
ATOM   6756  C  CH2   . TRP B 1 160 ? 153.144 153.694 184.845 1.00 155.97 ? 160  TRP B CH2   1 
ATOM   6757  N  N     . ILE B 1 161 ? 153.719 152.447 190.512 1.00 167.67 ? 161  ILE B N     1 
ATOM   6758  C  CA    . ILE B 1 161 ? 152.505 153.235 190.709 1.00 169.87 ? 161  ILE B CA    1 
ATOM   6759  C  C     . ILE B 1 161 ? 152.649 154.144 191.924 1.00 172.82 ? 161  ILE B C     1 
ATOM   6760  O  O     . ILE B 1 161 ? 152.228 155.307 191.899 1.00 170.70 ? 161  ILE B O     1 
ATOM   6761  C  CB    . ILE B 1 161 ? 151.278 152.314 190.825 1.00 170.52 ? 161  ILE B CB    1 
ATOM   6762  C  CG1   . ILE B 1 161 ? 150.986 151.646 189.482 1.00 165.75 ? 161  ILE B CG1   1 
ATOM   6763  C  CG2   . ILE B 1 161 ? 150.064 153.094 191.296 1.00 170.90 ? 161  ILE B CG2   1 
ATOM   6764  C  CD1   . ILE B 1 161 ? 149.793 150.724 189.510 1.00 162.49 ? 161  ILE B CD1   1 
ATOM   6765  N  N     . GLU B 1 162 ? 153.248 153.635 193.005 1.00 175.80 ? 162  GLU B N     1 
ATOM   6766  C  CA    . GLU B 1 162 ? 153.497 154.468 194.178 1.00 175.45 ? 162  GLU B CA    1 
ATOM   6767  C  C     . GLU B 1 162 ? 154.418 155.635 193.851 1.00 178.44 ? 162  GLU B C     1 
ATOM   6768  O  O     . GLU B 1 162 ? 154.378 156.668 194.529 1.00 184.15 ? 162  GLU B O     1 
ATOM   6769  C  CB    . GLU B 1 162 ? 154.094 153.625 195.307 1.00 175.16 ? 162  GLU B CB    1 
ATOM   6770  C  CG    . GLU B 1 162 ? 153.113 152.668 195.967 1.00 179.36 ? 162  GLU B CG    1 
ATOM   6771  C  CD    . GLU B 1 162 ? 152.030 153.385 196.747 1.00 183.92 ? 162  GLU B CD    1 
ATOM   6772  O  OE1   . GLU B 1 162 ? 152.291 154.501 197.243 1.00 185.51 ? 162  GLU B OE1   1 
ATOM   6773  O  OE2   . GLU B 1 162 ? 150.917 152.830 196.867 1.00 186.06 ? 162  GLU B OE2   1 
ATOM   6774  N  N     . GLY B 1 163 ? 155.252 155.492 192.823 1.00 176.03 ? 163  GLY B N     1 
ATOM   6775  C  CA    . GLY B 1 163 ? 156.121 156.561 192.385 1.00 175.27 ? 163  GLY B CA    1 
ATOM   6776  C  C     . GLY B 1 163 ? 157.502 156.575 193.000 1.00 179.68 ? 163  GLY B C     1 
ATOM   6777  O  O     . GLY B 1 163 ? 158.336 157.387 192.580 1.00 179.23 ? 163  GLY B O     1 
ATOM   6778  N  N     . ARG B 1 164 ? 157.775 155.710 193.980 1.00 182.81 ? 164  ARG B N     1 
ATOM   6779  C  CA    . ARG B 1 164 ? 159.118 155.651 194.549 1.00 183.33 ? 164  ARG B CA    1 
ATOM   6780  C  C     . ARG B 1 164 ? 160.133 155.202 193.506 1.00 182.38 ? 164  ARG B C     1 
ATOM   6781  O  O     . ARG B 1 164 ? 161.326 155.508 193.616 1.00 183.31 ? 164  ARG B O     1 
ATOM   6782  C  CB    . ARG B 1 164 ? 159.142 154.721 195.762 1.00 180.97 ? 164  ARG B CB    1 
ATOM   6783  C  CG    . ARG B 1 164 ? 158.308 153.464 195.608 1.00 179.07 ? 164  ARG B CG    1 
ATOM   6784  C  CD    . ARG B 1 164 ? 158.058 152.805 196.955 1.00 179.67 ? 164  ARG B CD    1 
ATOM   6785  N  NE    . ARG B 1 164 ? 159.282 152.252 197.524 1.00 184.62 ? 164  ARG B NE    1 
ATOM   6786  C  CZ    . ARG B 1 164 ? 159.317 151.367 198.511 1.00 184.33 ? 164  ARG B CZ    1 
ATOM   6787  N  NH1   . ARG B 1 164 ? 158.209 150.901 199.063 1.00 180.68 ? 164  ARG B NH1   1 
ATOM   6788  N  NH2   . ARG B 1 164 ? 160.495 150.936 198.954 1.00 185.46 ? 164  ARG B NH2   1 
ATOM   6789  N  N     . ILE B 1 165 ? 159.679 154.474 192.490 1.00 180.36 ? 165  ILE B N     1 
ATOM   6790  C  CA    . ILE B 1 165 ? 160.503 154.089 191.352 1.00 182.67 ? 165  ILE B CA    1 
ATOM   6791  C  C     . ILE B 1 165 ? 159.883 154.688 190.099 1.00 182.14 ? 165  ILE B C     1 
ATOM   6792  O  O     . ILE B 1 165 ? 158.736 154.376 189.757 1.00 178.86 ? 165  ILE B O     1 
ATOM   6793  C  CB    . ILE B 1 165 ? 160.624 152.560 191.233 1.00 181.90 ? 165  ILE B CB    1 
ATOM   6794  C  CG1   . ILE B 1 165 ? 161.500 152.007 192.359 1.00 184.53 ? 165  ILE B CG1   1 
ATOM   6795  C  CG2   . ILE B 1 165 ? 161.181 152.173 189.871 1.00 177.54 ? 165  ILE B CG2   1 
ATOM   6796  C  CD1   . ILE B 1 165 ? 161.719 150.511 192.290 1.00 180.72 ? 165  ILE B CD1   1 
ATOM   6797  N  N     . LYS B 1 166 ? 160.635 155.547 189.420 1.00 185.54 ? 166  LYS B N     1 
ATOM   6798  C  CA    . LYS B 1 166 ? 160.179 156.204 188.203 1.00 181.83 ? 166  LYS B CA    1 
ATOM   6799  C  C     . LYS B 1 166 ? 160.818 155.529 186.999 1.00 178.37 ? 166  LYS B C     1 
ATOM   6800  O  O     . LYS B 1 166 ? 162.046 155.413 186.926 1.00 179.06 ? 166  LYS B O     1 
ATOM   6801  C  CB    . LYS B 1 166 ? 160.515 157.697 188.219 1.00 183.82 ? 166  LYS B CB    1 
ATOM   6802  C  CG    . LYS B 1 166 ? 159.859 158.471 189.354 1.00 188.09 ? 166  LYS B CG    1 
ATOM   6803  C  CD    . LYS B 1 166 ? 160.273 159.934 189.340 1.00 187.49 ? 166  LYS B CD    1 
ATOM   6804  C  CE    . LYS B 1 166 ? 159.670 160.689 190.513 1.00 186.68 ? 166  LYS B CE    1 
ATOM   6805  N  NZ    . LYS B 1 166 ? 160.158 162.096 190.574 1.00 183.97 ? 166  LYS B NZ    1 
ATOM   6806  N  N     . GLU B 1 167 ? 159.985 155.087 186.060 1.00 176.80 ? 167  GLU B N     1 
ATOM   6807  C  CA    . GLU B 1 167 ? 160.466 154.382 184.882 1.00 177.39 ? 167  GLU B CA    1 
ATOM   6808  C  C     . GLU B 1 167 ? 159.423 154.522 183.784 1.00 174.26 ? 167  GLU B C     1 
ATOM   6809  O  O     . GLU B 1 167 ? 158.220 154.594 184.047 1.00 174.97 ? 167  GLU B O     1 
ATOM   6810  C  CB    . GLU B 1 167 ? 160.777 152.913 185.210 1.00 180.29 ? 167  GLU B CB    1 
ATOM   6811  C  CG    . GLU B 1 167 ? 161.400 152.081 184.087 1.00 180.62 ? 167  GLU B CG    1 
ATOM   6812  C  CD    . GLU B 1 167 ? 160.392 151.517 183.104 1.00 176.47 ? 167  GLU B CD    1 
ATOM   6813  O  OE1   . GLU B 1 167 ? 160.820 150.856 182.134 1.00 175.73 ? 167  GLU B OE1   1 
ATOM   6814  O  OE2   . GLU B 1 167 ? 159.177 151.710 183.306 1.00 173.87 ? 167  GLU B OE2   1 
ATOM   6815  N  N     . LYS B 1 168 ? 159.902 154.562 182.545 1.00 171.06 ? 168  LYS B N     1 
ATOM   6816  C  CA    . LYS B 1 168 ? 159.078 154.864 181.383 1.00 170.56 ? 168  LYS B CA    1 
ATOM   6817  C  C     . LYS B 1 168 ? 158.606 153.539 180.791 1.00 170.11 ? 168  LYS B C     1 
ATOM   6818  O  O     . LYS B 1 168 ? 159.430 152.683 180.455 1.00 172.40 ? 168  LYS B O     1 
ATOM   6819  C  CB    . LYS B 1 168 ? 159.898 155.680 180.376 1.00 170.24 ? 168  LYS B CB    1 
ATOM   6820  C  CG    . LYS B 1 168 ? 159.458 155.768 178.897 1.00 167.81 ? 168  LYS B CG    1 
ATOM   6821  C  CD    . LYS B 1 168 ? 157.955 155.707 178.653 1.00 167.96 ? 168  LYS B CD    1 
ATOM   6822  C  CE    . LYS B 1 168 ? 157.641 155.426 177.194 1.00 167.34 ? 168  LYS B CE    1 
ATOM   6823  N  NZ    . LYS B 1 168 ? 156.239 154.970 177.023 1.00 167.17 ? 168  LYS B NZ    1 
ATOM   6824  N  N     . HIS B 1 169 ? 157.280 153.378 180.662 1.00 168.92 ? 169  HIS B N     1 
ATOM   6825  C  CA    . HIS B 1 169 ? 156.672 152.209 180.031 1.00 168.38 ? 169  HIS B CA    1 
ATOM   6826  C  C     . HIS B 1 169 ? 157.074 150.916 180.730 1.00 169.17 ? 169  HIS B C     1 
ATOM   6827  O  O     . HIS B 1 169 ? 157.846 150.126 180.171 1.00 171.22 ? 169  HIS B O     1 
ATOM   6828  C  CB    . HIS B 1 169 ? 157.056 152.138 178.551 1.00 169.30 ? 169  HIS B CB    1 
ATOM   6829  C  CG    . HIS B 1 169 ? 155.991 151.551 177.677 1.00 174.29 ? 169  HIS B CG    1 
ATOM   6830  N  ND1   . HIS B 1 169 ? 155.416 152.243 176.633 1.00 176.00 ? 169  HIS B ND1   1 
ATOM   6831  C  CD2   . HIS B 1 169 ? 155.395 150.335 177.696 1.00 173.91 ? 169  HIS B CD2   1 
ATOM   6832  C  CE1   . HIS B 1 169 ? 154.515 151.477 176.044 1.00 177.03 ? 169  HIS B CE1   1 
ATOM   6833  N  NE2   . HIS B 1 169 ? 154.482 150.314 176.670 1.00 177.07 ? 169  HIS B NE2   1 
ATOM   6834  N  N     . PRO B 1 170 ? 156.592 150.667 181.945 1.00 166.29 ? 170  PRO B N     1 
ATOM   6835  C  CA    . PRO B 1 170 ? 157.011 149.461 182.662 1.00 160.45 ? 170  PRO B CA    1 
ATOM   6836  C  C     . PRO B 1 170 ? 156.494 148.199 181.992 1.00 154.42 ? 170  PRO B C     1 
ATOM   6837  O  O     . PRO B 1 170 ? 155.396 148.163 181.433 1.00 150.30 ? 170  PRO B O     1 
ATOM   6838  C  CB    . PRO B 1 170 ? 156.397 149.647 184.052 1.00 162.86 ? 170  PRO B CB    1 
ATOM   6839  C  CG    . PRO B 1 170 ? 155.180 150.459 183.806 1.00 164.16 ? 170  PRO B CG    1 
ATOM   6840  C  CD    . PRO B 1 170 ? 155.467 151.343 182.612 1.00 166.11 ? 170  PRO B CD    1 
ATOM   6841  N  N     . ARG B 1 171 ? 157.319 147.161 182.046 1.00 153.82 ? 171  ARG B N     1 
ATOM   6842  C  CA    . ARG B 1 171 ? 157.044 145.867 181.446 1.00 147.31 ? 171  ARG B CA    1 
ATOM   6843  C  C     . ARG B 1 171 ? 157.682 144.788 182.307 1.00 147.40 ? 171  ARG B C     1 
ATOM   6844  O  O     . ARG B 1 171 ? 158.654 145.062 183.022 1.00 151.24 ? 171  ARG B O     1 
ATOM   6845  C  CB    . ARG B 1 171 ? 157.590 145.793 180.013 1.00 140.79 ? 171  ARG B CB    1 
ATOM   6846  C  CG    . ARG B 1 171 ? 156.586 146.208 178.957 1.00 139.00 ? 171  ARG B CG    1 
ATOM   6847  C  CD    . ARG B 1 171 ? 155.538 145.134 178.756 1.00 134.55 ? 171  ARG B CD    1 
ATOM   6848  N  NE    . ARG B 1 171 ? 154.327 145.648 178.133 1.00 137.13 ? 171  ARG B NE    1 
ATOM   6849  C  CZ    . ARG B 1 171 ? 153.262 144.910 177.852 1.00 136.26 ? 171  ARG B CZ    1 
ATOM   6850  N  NH1   . ARG B 1 171 ? 153.232 143.613 178.113 1.00 134.18 ? 171  ARG B NH1   1 
ATOM   6851  N  NH2   . ARG B 1 171 ? 152.206 145.484 177.286 1.00 138.81 ? 171  ARG B NH2   1 
ATOM   6852  N  N     . PRO B 1 172 ? 157.156 143.563 182.274 1.00 142.01 ? 172  PRO B N     1 
ATOM   6853  C  CA    . PRO B 1 172 ? 157.749 142.493 183.083 1.00 141.11 ? 172  PRO B CA    1 
ATOM   6854  C  C     . PRO B 1 172 ? 159.208 142.270 182.716 1.00 138.61 ? 172  PRO B C     1 
ATOM   6855  O  O     . PRO B 1 172 ? 159.597 142.366 181.550 1.00 138.84 ? 172  PRO B O     1 
ATOM   6856  C  CB    . PRO B 1 172 ? 156.887 141.270 182.746 1.00 136.98 ? 172  PRO B CB    1 
ATOM   6857  C  CG    . PRO B 1 172 ? 156.158 141.633 181.496 1.00 134.65 ? 172  PRO B CG    1 
ATOM   6858  C  CD    . PRO B 1 172 ? 155.949 143.105 181.570 1.00 136.36 ? 172  PRO B CD    1 
ATOM   6859  N  N     . GLY B 1 173 ? 160.015 141.982 183.731 1.00 141.64 ? 173  GLY B N     1 
ATOM   6860  C  CA    . GLY B 1 173 ? 161.438 141.828 183.516 1.00 148.27 ? 173  GLY B CA    1 
ATOM   6861  C  C     . GLY B 1 173 ? 161.755 140.670 182.590 1.00 150.36 ? 173  GLY B C     1 
ATOM   6862  O  O     . GLY B 1 173 ? 161.076 139.645 182.575 1.00 151.94 ? 173  GLY B O     1 
ATOM   6863  N  N     . VAL B 1 174 ? 162.810 140.849 181.797 1.00 149.43 ? 174  VAL B N     1 
ATOM   6864  C  CA    . VAL B 1 174 ? 163.235 139.806 180.875 1.00 146.69 ? 174  VAL B CA    1 
ATOM   6865  C  C     . VAL B 1 174 ? 163.891 138.681 181.662 1.00 151.11 ? 174  VAL B C     1 
ATOM   6866  O  O     . VAL B 1 174 ? 164.877 138.894 182.379 1.00 159.04 ? 174  VAL B O     1 
ATOM   6867  C  CB    . VAL B 1 174 ? 164.190 140.377 179.819 1.00 146.77 ? 174  VAL B CB    1 
ATOM   6868  C  CG1   . VAL B 1 174 ? 164.679 139.274 178.901 1.00 143.51 ? 174  VAL B CG1   1 
ATOM   6869  C  CG2   . VAL B 1 174 ? 163.501 141.471 179.030 1.00 141.85 ? 174  VAL B CG2   1 
ATOM   6870  N  N     . HIS B 1 175 ? 163.345 137.476 181.530 1.00 144.21 ? 175  HIS B N     1 
ATOM   6871  C  CA    . HIS B 1 175 ? 163.848 136.313 182.249 1.00 143.29 ? 175  HIS B CA    1 
ATOM   6872  C  C     . HIS B 1 175 ? 163.903 135.138 181.289 1.00 138.89 ? 175  HIS B C     1 
ATOM   6873  O  O     . HIS B 1 175 ? 162.864 134.690 180.796 1.00 135.15 ? 175  HIS B O     1 
ATOM   6874  C  CB    . HIS B 1 175 ? 162.963 135.983 183.454 1.00 142.71 ? 175  HIS B CB    1 
ATOM   6875  C  CG    . HIS B 1 175 ? 163.574 134.997 184.400 1.00 147.27 ? 175  HIS B CG    1 
ATOM   6876  N  ND1   . HIS B 1 175 ? 162.879 133.918 184.900 1.00 147.67 ? 175  HIS B ND1   1 
ATOM   6877  C  CD2   . HIS B 1 175 ? 164.815 134.927 184.936 1.00 153.43 ? 175  HIS B CD2   1 
ATOM   6878  C  CE1   . HIS B 1 175 ? 163.665 133.224 185.704 1.00 154.01 ? 175  HIS B CE1   1 
ATOM   6879  N  NE2   . HIS B 1 175 ? 164.846 133.816 185.743 1.00 158.48 ? 175  HIS B NE2   1 
ATOM   6880  N  N     . LYS B 1 176 ? 165.108 134.646 181.022 1.00 134.59 ? 176  LYS B N     1 
ATOM   6881  C  CA    . LYS B 1 176 ? 165.309 133.477 180.181 1.00 125.90 ? 176  LYS B CA    1 
ATOM   6882  C  C     . LYS B 1 176 ? 165.578 132.264 181.058 1.00 129.45 ? 176  LYS B C     1 
ATOM   6883  O  O     . LYS B 1 176 ? 166.376 132.326 181.999 1.00 138.61 ? 176  LYS B O     1 
ATOM   6884  C  CB    . LYS B 1 176 ? 166.455 133.692 179.192 1.00 125.10 ? 176  LYS B CB    1 
ATOM   6885  C  CG    . LYS B 1 176 ? 167.786 134.060 179.816 1.00 137.02 ? 176  LYS B CG    1 
ATOM   6886  C  CD    . LYS B 1 176 ? 168.930 133.747 178.867 1.00 139.18 ? 176  LYS B CD    1 
ATOM   6887  C  CE    . LYS B 1 176 ? 168.614 134.198 177.452 1.00 133.77 ? 176  LYS B CE    1 
ATOM   6888  N  NZ    . LYS B 1 176 ? 169.752 133.938 176.534 1.00 132.91 ? 176  LYS B NZ    1 
ATOM   6889  N  N     . VAL B 1 177 ? 164.901 131.163 180.752 1.00 120.01 ? 177  VAL B N     1 
ATOM   6890  C  CA    . VAL B 1 177 ? 164.935 129.960 181.572 1.00 120.58 ? 177  VAL B CA    1 
ATOM   6891  C  C     . VAL B 1 177 ? 165.625 128.858 180.785 1.00 125.35 ? 177  VAL B C     1 
ATOM   6892  O  O     . VAL B 1 177 ? 165.238 128.566 179.649 1.00 124.26 ? 177  VAL B O     1 
ATOM   6893  C  CB    . VAL B 1 177 ? 163.519 129.532 181.998 1.00 120.83 ? 177  VAL B CB    1 
ATOM   6894  C  CG1   . VAL B 1 177 ? 163.076 130.317 183.219 1.00 126.45 ? 177  VAL B CG1   1 
ATOM   6895  C  CG2   . VAL B 1 177 ? 162.548 129.746 180.856 1.00 121.34 ? 177  VAL B CG2   1 
ATOM   6896  N  N     . GLY B 1 178 ? 166.649 128.260 181.384 1.00 131.31 ? 178  GLY B N     1 
ATOM   6897  C  CA    . GLY B 1 178 ? 167.360 127.145 180.789 1.00 130.40 ? 178  GLY B CA    1 
ATOM   6898  C  C     . GLY B 1 178 ? 166.976 125.847 181.476 1.00 138.55 ? 178  GLY B C     1 
ATOM   6899  O  O     . GLY B 1 178 ? 167.267 125.651 182.657 1.00 150.09 ? 178  GLY B O     1 
ATOM   6900  N  N     . ILE B 1 179 ? 166.326 124.969 180.720 1.00 131.76 ? 179  ILE B N     1 
ATOM   6901  C  CA    . ILE B 1 179 ? 165.912 123.672 181.244 1.00 139.42 ? 179  ILE B CA    1 
ATOM   6902  C  C     . ILE B 1 179 ? 166.805 122.598 180.638 1.00 137.54 ? 179  ILE B C     1 
ATOM   6903  O  O     . ILE B 1 179 ? 167.282 122.762 179.506 1.00 136.24 ? 179  ILE B O     1 
ATOM   6904  C  CB    . ILE B 1 179 ? 164.428 123.391 180.953 1.00 136.06 ? 179  ILE B CB    1 
ATOM   6905  C  CG1   . ILE B 1 179 ? 164.178 123.286 179.448 1.00 127.92 ? 179  ILE B CG1   1 
ATOM   6906  C  CG2   . ILE B 1 179 ? 163.549 124.461 181.570 1.00 136.70 ? 179  ILE B CG2   1 
ATOM   6907  C  CD1   . ILE B 1 179 ? 162.789 122.798 179.098 1.00 133.72 ? 179  ILE B CD1   1 
ATOM   6908  N  N     . PRO B 1 180 ? 167.087 121.509 181.352 1.00 138.16 ? 180  PRO B N     1 
ATOM   6909  C  CA    . PRO B 1 180 ? 167.848 120.419 180.740 1.00 137.42 ? 180  PRO B CA    1 
ATOM   6910  C  C     . PRO B 1 180 ? 167.096 119.852 179.550 1.00 138.56 ? 180  PRO B C     1 
ATOM   6911  O  O     . PRO B 1 180 ? 165.871 119.719 179.566 1.00 136.91 ? 180  PRO B O     1 
ATOM   6912  C  CB    . PRO B 1 180 ? 167.978 119.392 181.870 1.00 138.98 ? 180  PRO B CB    1 
ATOM   6913  C  CG    . PRO B 1 180 ? 167.752 120.169 183.122 1.00 148.65 ? 180  PRO B CG    1 
ATOM   6914  C  CD    . PRO B 1 180 ? 166.765 121.233 182.761 1.00 146.75 ? 180  PRO B CD    1 
ATOM   6915  N  N     . VAL B 1 181 ? 167.848 119.523 178.501 1.00 139.88 ? 181  VAL B N     1 
ATOM   6916  C  CA    . VAL B 1 181 ? 167.232 119.040 177.275 1.00 134.91 ? 181  VAL B CA    1 
ATOM   6917  C  C     . VAL B 1 181 ? 166.769 117.603 177.470 1.00 141.84 ? 181  VAL B C     1 
ATOM   6918  O  O     . VAL B 1 181 ? 167.362 116.834 178.241 1.00 144.93 ? 181  VAL B O     1 
ATOM   6919  C  CB    . VAL B 1 181 ? 168.207 119.178 176.094 1.00 131.93 ? 181  VAL B CB    1 
ATOM   6920  C  CG1   . VAL B 1 181 ? 169.122 117.972 175.997 1.00 141.66 ? 181  VAL B CG1   1 
ATOM   6921  C  CG2   . VAL B 1 181 ? 167.440 119.373 174.809 1.00 122.77 ? 181  VAL B CG2   1 
ATOM   6922  N  N     . SER B 1 182 ? 165.676 117.244 176.795 1.00 142.73 ? 182  SER B N     1 
ATOM   6923  C  CA    . SER B 1 182 ? 165.091 115.920 176.983 1.00 145.55 ? 182  SER B CA    1 
ATOM   6924  C  C     . SER B 1 182 ? 166.021 114.821 176.487 1.00 147.72 ? 182  SER B C     1 
ATOM   6925  O  O     . SER B 1 182 ? 166.165 113.779 177.136 1.00 145.35 ? 182  SER B O     1 
ATOM   6926  C  CB    . SER B 1 182 ? 163.741 115.839 176.272 1.00 143.88 ? 182  SER B CB    1 
ATOM   6927  O  OG    . SER B 1 182 ? 163.889 116.048 174.879 1.00 144.02 ? 182  SER B OG    1 
ATOM   6928  N  N     . ASN B 1 183 ? 166.661 115.032 175.340 1.00 147.84 ? 183  ASN B N     1 
ATOM   6929  C  CA    . ASN B 1 183 ? 167.474 114.009 174.695 1.00 145.91 ? 183  ASN B CA    1 
ATOM   6930  C  C     . ASN B 1 183 ? 168.896 114.518 174.527 1.00 147.12 ? 183  ASN B C     1 
ATOM   6931  O  O     . ASN B 1 183 ? 169.123 115.523 173.845 1.00 148.84 ? 183  ASN B O     1 
ATOM   6932  C  CB    . ASN B 1 183 ? 166.880 113.625 173.340 1.00 144.71 ? 183  ASN B CB    1 
ATOM   6933  C  CG    . ASN B 1 183 ? 165.417 113.252 173.435 1.00 148.47 ? 183  ASN B CG    1 
ATOM   6934  O  OD1   . ASN B 1 183 ? 164.970 112.697 174.439 1.00 152.10 ? 183  ASN B OD1   1 
ATOM   6935  N  ND2   . ASN B 1 183 ? 164.659 113.559 172.390 1.00 144.19 ? 183  ASN B ND2   1 
ATOM   6936  N  N     . TRP B 1 184 ? 169.848 113.821 175.139 1.00 149.61 ? 184  TRP B N     1 
ATOM   6937  C  CA    . TRP B 1 184 ? 171.264 114.089 174.950 1.00 153.76 ? 184  TRP B CA    1 
ATOM   6938  C  C     . TRP B 1 184 ? 171.963 112.774 174.642 1.00 158.96 ? 184  TRP B C     1 
ATOM   6939  O  O     . TRP B 1 184 ? 171.726 111.764 175.311 1.00 160.78 ? 184  TRP B O     1 
ATOM   6940  C  CB    . TRP B 1 184 ? 171.886 114.751 176.186 1.00 150.41 ? 184  TRP B CB    1 
ATOM   6941  C  CG    . TRP B 1 184 ? 173.351 115.017 176.044 1.00 153.69 ? 184  TRP B CG    1 
ATOM   6942  C  CD1   . TRP B 1 184 ? 173.935 115.973 175.269 1.00 151.87 ? 184  TRP B CD1   1 
ATOM   6943  C  CD2   . TRP B 1 184 ? 174.419 114.318 176.693 1.00 158.86 ? 184  TRP B CD2   1 
ATOM   6944  N  NE1   . TRP B 1 184 ? 175.301 115.915 175.394 1.00 156.71 ? 184  TRP B NE1   1 
ATOM   6945  C  CE2   . TRP B 1 184 ? 175.624 114.906 176.262 1.00 161.45 ? 184  TRP B CE2   1 
ATOM   6946  C  CE3   . TRP B 1 184 ? 174.474 113.252 177.595 1.00 159.45 ? 184  TRP B CE3   1 
ATOM   6947  C  CZ2   . TRP B 1 184 ? 176.870 114.464 176.702 1.00 164.03 ? 184  TRP B CZ2   1 
ATOM   6948  C  CZ3   . TRP B 1 184 ? 175.712 112.814 178.031 1.00 161.83 ? 184  TRP B CZ3   1 
ATOM   6949  C  CH2   . TRP B 1 184 ? 176.893 113.420 177.585 1.00 164.74 ? 184  TRP B CH2   1 
ATOM   6950  N  N     . ASP B 1 185 ? 172.821 112.789 173.627 1.00 157.92 ? 185  ASP B N     1 
ATOM   6951  C  CA    . ASP B 1 185 ? 173.468 111.569 173.163 1.00 157.25 ? 185  ASP B CA    1 
ATOM   6952  C  C     . ASP B 1 185 ? 174.727 111.309 173.979 1.00 158.98 ? 185  ASP B C     1 
ATOM   6953  O  O     . ASP B 1 185 ? 175.646 112.135 173.995 1.00 160.98 ? 185  ASP B O     1 
ATOM   6954  C  CB    . ASP B 1 185 ? 173.801 111.680 171.678 1.00 158.61 ? 185  ASP B CB    1 
ATOM   6955  C  CG    . ASP B 1 185 ? 172.588 112.017 170.836 1.00 154.98 ? 185  ASP B CG    1 
ATOM   6956  O  OD1   . ASP B 1 185 ? 172.123 113.174 170.898 1.00 149.99 ? 185  ASP B OD1   1 
ATOM   6957  O  OD2   . ASP B 1 185 ? 172.099 111.125 170.112 1.00 154.74 ? 185  ASP B OD2   1 
ATOM   6958  N  N     . GLU B 1 186 ? 174.765 110.163 174.661 1.00 161.63 ? 186  GLU B N     1 
ATOM   6959  C  CA    . GLU B 1 186 ? 175.960 109.792 175.411 1.00 167.82 ? 186  GLU B CA    1 
ATOM   6960  C  C     . GLU B 1 186 ? 177.152 109.600 174.482 1.00 169.57 ? 186  GLU B C     1 
ATOM   6961  O  O     . GLU B 1 186 ? 178.272 110.012 174.804 1.00 168.23 ? 186  GLU B O     1 
ATOM   6962  C  CB    . GLU B 1 186 ? 175.702 108.522 176.221 1.00 169.93 ? 186  GLU B CB    1 
ATOM   6963  C  CG    . GLU B 1 186 ? 174.755 108.704 177.397 1.00 169.14 ? 186  GLU B CG    1 
ATOM   6964  C  CD    . GLU B 1 186 ? 173.296 108.692 176.982 1.00 168.24 ? 186  GLU B CD    1 
ATOM   6965  O  OE1   . GLU B 1 186 ? 173.011 108.350 175.815 1.00 166.64 ? 186  GLU B OE1   1 
ATOM   6966  O  OE2   . GLU B 1 186 ? 172.434 109.023 177.822 1.00 169.12 ? 186  GLU B OE2   1 
ATOM   6967  N  N     . ASP B 1 187 ? 176.930 108.977 173.328 1.00 169.45 ? 187  ASP B N     1 
ATOM   6968  C  CA    . ASP B 1 187 ? 177.978 108.740 172.339 1.00 170.36 ? 187  ASP B CA    1 
ATOM   6969  C  C     . ASP B 1 187 ? 177.930 109.873 171.320 1.00 166.11 ? 187  ASP B C     1 
ATOM   6970  O  O     . ASP B 1 187 ? 177.073 109.892 170.433 1.00 163.19 ? 187  ASP B O     1 
ATOM   6971  C  CB    . ASP B 1 187 ? 177.800 107.378 171.678 1.00 176.71 ? 187  ASP B CB    1 
ATOM   6972  C  CG    . ASP B 1 187 ? 176.344 107.033 171.442 1.00 177.20 ? 187  ASP B CG    1 
ATOM   6973  O  OD1   . ASP B 1 187 ? 175.473 107.859 171.789 1.00 170.12 ? 187  ASP B OD1   1 
ATOM   6974  O  OD2   . ASP B 1 187 ? 176.069 105.936 170.912 1.00 181.69 ? 187  ASP B OD2   1 
ATOM   6975  N  N     . TRP B 1 188 ? 178.854 110.820 171.454 1.00 163.91 ? 188  TRP B N     1 
ATOM   6976  C  CA    . TRP B 1 188 ? 178.947 111.953 170.548 1.00 154.73 ? 188  TRP B CA    1 
ATOM   6977  C  C     . TRP B 1 188 ? 180.375 112.474 170.594 1.00 154.30 ? 188  TRP B C     1 
ATOM   6978  O  O     . TRP B 1 188 ? 181.042 112.392 171.629 1.00 159.17 ? 188  TRP B O     1 
ATOM   6979  C  CB    . TRP B 1 188 ? 177.949 113.053 170.927 1.00 149.09 ? 188  TRP B CB    1 
ATOM   6980  C  CG    . TRP B 1 188 ? 177.642 114.007 169.820 1.00 145.05 ? 188  TRP B CG    1 
ATOM   6981  C  CD1   . TRP B 1 188 ? 176.722 113.838 168.829 1.00 141.31 ? 188  TRP B CD1   1 
ATOM   6982  C  CD2   . TRP B 1 188 ? 178.250 115.283 169.592 1.00 147.86 ? 188  TRP B CD2   1 
ATOM   6983  N  NE1   . TRP B 1 188 ? 176.719 114.930 167.996 1.00 136.08 ? 188  TRP B NE1   1 
ATOM   6984  C  CE2   . TRP B 1 188 ? 177.650 115.831 168.442 1.00 139.19 ? 188  TRP B CE2   1 
ATOM   6985  C  CE3   . TRP B 1 188 ? 179.244 116.015 170.247 1.00 149.67 ? 188  TRP B CE3   1 
ATOM   6986  C  CZ2   . TRP B 1 188 ? 178.011 117.074 167.933 1.00 131.77 ? 188  TRP B CZ2   1 
ATOM   6987  C  CZ3   . TRP B 1 188 ? 179.600 117.250 169.740 1.00 144.72 ? 188  TRP B CZ3   1 
ATOM   6988  C  CH2   . TRP B 1 188 ? 178.985 117.767 168.595 1.00 137.05 ? 188  TRP B CH2   1 
ATOM   6989  N  N     . VAL B 1 189 ? 180.842 113.009 169.470 1.00 149.45 ? 189  VAL B N     1 
ATOM   6990  C  CA    . VAL B 1 189 ? 182.223 113.453 169.333 1.00 155.12 ? 189  VAL B CA    1 
ATOM   6991  C  C     . VAL B 1 189 ? 182.232 114.940 169.013 1.00 157.24 ? 189  VAL B C     1 
ATOM   6992  O  O     . VAL B 1 189 ? 181.561 115.385 168.075 1.00 156.32 ? 189  VAL B O     1 
ATOM   6993  C  CB    . VAL B 1 189 ? 182.972 112.655 168.250 1.00 157.82 ? 189  VAL B CB    1 
ATOM   6994  C  CG1   . VAL B 1 189 ? 184.404 113.149 168.122 1.00 160.91 ? 189  VAL B CG1   1 
ATOM   6995  C  CG2   . VAL B 1 189 ? 182.943 111.170 168.573 1.00 155.91 ? 189  VAL B CG2   1 
ATOM   6996  N  N     . GLY B 1 190 ? 182.995 115.702 169.793 1.00 161.31 ? 190  GLY B N     1 
ATOM   6997  C  CA    . GLY B 1 190 ? 183.170 117.116 169.566 1.00 161.80 ? 190  GLY B CA    1 
ATOM   6998  C  C     . GLY B 1 190 ? 184.552 117.568 169.993 1.00 172.66 ? 190  GLY B C     1 
ATOM   6999  O  O     . GLY B 1 190 ? 185.226 116.905 170.787 1.00 177.15 ? 190  GLY B O     1 
ATOM   7000  N  N     . PRO B 1 191 ? 185.006 118.708 169.464 1.00 175.93 ? 191  PRO B N     1 
ATOM   7001  C  CA    . PRO B 1 191 ? 186.365 119.179 169.778 1.00 181.54 ? 191  PRO B CA    1 
ATOM   7002  C  C     . PRO B 1 191 ? 186.546 119.483 171.257 1.00 183.11 ? 191  PRO B C     1 
ATOM   7003  O  O     . PRO B 1 191 ? 187.451 118.953 171.911 1.00 186.74 ? 191  PRO B O     1 
ATOM   7004  C  CB    . PRO B 1 191 ? 186.504 120.448 168.923 1.00 178.94 ? 191  PRO B CB    1 
ATOM   7005  C  CG    . PRO B 1 191 ? 185.423 120.343 167.882 1.00 174.99 ? 191  PRO B CG    1 
ATOM   7006  C  CD    . PRO B 1 191 ? 184.301 119.611 168.542 1.00 171.35 ? 191  PRO B CD    1 
ATOM   7007  N  N     . PHE B 1 192 ? 185.678 120.343 171.782 1.00 178.59 ? 192  PHE B N     1 
ATOM   7008  C  CA    . PHE B 1 192 ? 185.601 120.665 173.199 1.00 174.31 ? 192  PHE B CA    1 
ATOM   7009  C  C     . PHE B 1 192 ? 184.325 121.456 173.419 1.00 169.26 ? 192  PHE B C     1 
ATOM   7010  O  O     . PHE B 1 192 ? 183.891 122.191 172.529 1.00 166.85 ? 192  PHE B O     1 
ATOM   7011  C  CB    . PHE B 1 192 ? 186.812 121.472 173.682 1.00 176.49 ? 192  PHE B CB    1 
ATOM   7012  C  CG    . PHE B 1 192 ? 186.865 121.641 175.175 1.00 179.27 ? 192  PHE B CG    1 
ATOM   7013  C  CD1   . PHE B 1 192 ? 187.347 120.627 175.986 1.00 179.99 ? 192  PHE B CD1   1 
ATOM   7014  C  CD2   . PHE B 1 192 ? 186.410 122.807 175.768 1.00 178.63 ? 192  PHE B CD2   1 
ATOM   7015  C  CE1   . PHE B 1 192 ? 187.391 120.781 177.359 1.00 180.75 ? 192  PHE B CE1   1 
ATOM   7016  C  CE2   . PHE B 1 192 ? 186.449 122.966 177.139 1.00 179.61 ? 192  PHE B CE2   1 
ATOM   7017  C  CZ    . PHE B 1 192 ? 186.940 121.951 177.936 1.00 181.82 ? 192  PHE B CZ    1 
ATOM   7018  N  N     . MET B 1 193 ? 183.724 121.293 174.593 1.00 167.85 ? 193  MET B N     1 
ATOM   7019  C  CA    . MET B 1 193 ? 182.443 121.920 174.879 1.00 163.56 ? 193  MET B CA    1 
ATOM   7020  C  C     . MET B 1 193 ? 182.211 121.902 176.380 1.00 164.29 ? 193  MET B C     1 
ATOM   7021  O  O     . MET B 1 193 ? 182.828 121.103 177.090 1.00 166.22 ? 193  MET B O     1 
ATOM   7022  C  CB    . MET B 1 193 ? 181.316 121.185 174.150 1.00 157.25 ? 193  MET B CB    1 
ATOM   7023  C  CG    . MET B 1 193 ? 180.354 122.081 173.405 1.00 147.06 ? 193  MET B CG    1 
ATOM   7024  S  SD    . MET B 1 193 ? 179.444 121.114 172.188 1.00 144.26 ? 193  MET B SD    1 
ATOM   7025  C  CE    . MET B 1 193 ? 178.134 122.244 171.749 1.00 129.82 ? 193  MET B CE    1 
ATOM   7026  N  N     . ASP B 1 194 ? 181.339 122.782 176.862 1.00 160.29 ? 194  ASP B N     1 
ATOM   7027  C  CA    . ASP B 1 194 ? 180.980 122.747 178.272 1.00 156.81 ? 194  ASP B CA    1 
ATOM   7028  C  C     . ASP B 1 194 ? 179.597 122.126 178.457 1.00 151.17 ? 194  ASP B C     1 
ATOM   7029  O  O     . ASP B 1 194 ? 178.765 122.115 177.545 1.00 148.83 ? 194  ASP B O     1 
ATOM   7030  C  CB    . ASP B 1 194 ? 181.109 124.155 178.890 1.00 156.64 ? 194  ASP B CB    1 
ATOM   7031  C  CG    . ASP B 1 194 ? 179.888 125.063 178.680 1.00 155.04 ? 194  ASP B CG    1 
ATOM   7032  O  OD1   . ASP B 1 194 ? 178.744 124.609 178.502 1.00 152.22 ? 194  ASP B OD1   1 
ATOM   7033  O  OD2   . ASP B 1 194 ? 180.097 126.295 178.690 1.00 156.50 ? 194  ASP B OD2   1 
ATOM   7034  N  N     . GLU B 1 195 ? 179.373 121.575 179.652 1.00 152.30 ? 195  GLU B N     1 
ATOM   7035  C  CA    . GLU B 1 195 ? 178.131 120.855 179.914 1.00 153.37 ? 195  GLU B CA    1 
ATOM   7036  C  C     . GLU B 1 195 ? 176.927 121.792 179.914 1.00 148.63 ? 195  GLU B C     1 
ATOM   7037  O  O     . GLU B 1 195 ? 175.848 121.423 179.434 1.00 147.38 ? 195  GLU B O     1 
ATOM   7038  C  CB    . GLU B 1 195 ? 178.250 120.076 181.228 1.00 155.72 ? 195  GLU B CB    1 
ATOM   7039  C  CG    . GLU B 1 195 ? 178.494 120.899 182.486 1.00 157.11 ? 195  GLU B CG    1 
ATOM   7040  C  CD    . GLU B 1 195 ? 177.218 121.418 183.118 1.00 156.28 ? 195  GLU B CD    1 
ATOM   7041  O  OE1   . GLU B 1 195 ? 176.124 120.994 182.691 1.00 156.24 ? 195  GLU B OE1   1 
ATOM   7042  O  OE2   . GLU B 1 195 ? 177.311 122.234 184.059 1.00 153.43 ? 195  GLU B OE2   1 
ATOM   7043  N  N     . GLU B 1 196 ? 177.092 123.010 180.436 1.00 147.57 ? 196  GLU B N     1 
ATOM   7044  C  CA    . GLU B 1 196 ? 175.978 123.953 180.479 1.00 148.80 ? 196  GLU B CA    1 
ATOM   7045  C  C     . GLU B 1 196 ? 175.495 124.315 179.079 1.00 145.83 ? 196  GLU B C     1 
ATOM   7046  O  O     . GLU B 1 196 ? 174.287 124.403 178.836 1.00 145.26 ? 196  GLU B O     1 
ATOM   7047  C  CB    . GLU B 1 196 ? 176.382 125.209 181.253 1.00 152.79 ? 196  GLU B CB    1 
ATOM   7048  C  CG    . GLU B 1 196 ? 175.306 126.282 181.301 1.00 149.04 ? 196  GLU B CG    1 
ATOM   7049  C  CD    . GLU B 1 196 ? 175.731 127.493 182.107 1.00 153.10 ? 196  GLU B CD    1 
ATOM   7050  O  OE1   . GLU B 1 196 ? 176.904 127.539 182.532 1.00 154.20 ? 196  GLU B OE1   1 
ATOM   7051  O  OE2   . GLU B 1 196 ? 174.893 128.394 182.322 1.00 153.72 ? 196  GLU B OE2   1 
ATOM   7052  N  N     . GLU B 1 197 ? 176.421 124.543 178.147 1.00 145.80 ? 197  GLU B N     1 
ATOM   7053  C  CA    . GLU B 1 197 ? 176.020 124.856 176.778 1.00 142.63 ? 197  GLU B CA    1 
ATOM   7054  C  C     . GLU B 1 197 ? 175.533 123.624 176.027 1.00 142.32 ? 197  GLU B C     1 
ATOM   7055  O  O     . GLU B 1 197 ? 174.574 123.713 175.253 1.00 135.96 ? 197  GLU B O     1 
ATOM   7056  C  CB    . GLU B 1 197 ? 177.179 125.505 176.023 1.00 146.03 ? 197  GLU B CB    1 
ATOM   7057  C  CG    . GLU B 1 197 ? 176.835 125.945 174.619 1.00 144.23 ? 197  GLU B CG    1 
ATOM   7058  C  CD    . GLU B 1 197 ? 178.027 126.513 173.882 1.00 146.74 ? 197  GLU B CD    1 
ATOM   7059  O  OE1   . GLU B 1 197 ? 179.169 126.333 174.357 1.00 149.23 ? 197  GLU B OE1   1 
ATOM   7060  O  OE2   . GLU B 1 197 ? 177.819 127.146 172.828 1.00 140.99 ? 197  GLU B OE2   1 
ATOM   7061  N  N     . ALA B 1 198 ? 176.184 122.476 176.225 1.00 147.82 ? 198  ALA B N     1 
ATOM   7062  C  CA    . ALA B 1 198 ? 175.849 121.296 175.435 1.00 141.46 ? 198  ALA B CA    1 
ATOM   7063  C  C     . ALA B 1 198 ? 174.510 120.698 175.848 1.00 134.34 ? 198  ALA B C     1 
ATOM   7064  O  O     . ALA B 1 198 ? 173.675 120.385 174.991 1.00 127.69 ? 198  ALA B O     1 
ATOM   7065  C  CB    . ALA B 1 198 ? 176.958 120.252 175.559 1.00 142.32 ? 198  ALA B CB    1 
ATOM   7066  N  N     . ARG B 1 199 ? 174.279 120.538 177.151 1.00 137.74 ? 199  ARG B N     1 
ATOM   7067  C  CA    . ARG B 1 199 ? 173.152 119.755 177.640 1.00 138.38 ? 199  ARG B CA    1 
ATOM   7068  C  C     . ARG B 1 199 ? 171.885 120.569 177.863 1.00 135.51 ? 199  ARG B C     1 
ATOM   7069  O  O     . ARG B 1 199 ? 170.799 119.985 177.919 1.00 135.47 ? 199  ARG B O     1 
ATOM   7070  C  CB    . ARG B 1 199 ? 173.536 119.056 178.952 1.00 140.51 ? 199  ARG B CB    1 
ATOM   7071  C  CG    . ARG B 1 199 ? 172.599 117.932 179.373 1.00 144.53 ? 199  ARG B CG    1 
ATOM   7072  C  CD    . ARG B 1 199 ? 173.283 116.839 180.206 1.00 150.66 ? 199  ARG B CD    1 
ATOM   7073  N  NE    . ARG B 1 199 ? 174.528 116.340 179.631 1.00 152.82 ? 199  ARG B NE    1 
ATOM   7074  C  CZ    . ARG B 1 199 ? 175.733 116.819 179.912 1.00 154.50 ? 199  ARG B CZ    1 
ATOM   7075  N  NH1   . ARG B 1 199 ? 175.901 117.797 180.785 1.00 152.63 ? 199  ARG B NH1   1 
ATOM   7076  N  NH2   . ARG B 1 199 ? 176.796 116.296 179.309 1.00 155.21 ? 199  ARG B NH2   1 
ATOM   7077  N  N     . ARG B 1 200 ? 171.987 121.888 177.975 1.00 136.26 ? 200  ARG B N     1 
ATOM   7078  C  CA    . ARG B 1 200 ? 170.887 122.718 178.446 1.00 131.43 ? 200  ARG B CA    1 
ATOM   7079  C  C     . ARG B 1 200 ? 170.383 123.611 177.320 1.00 126.02 ? 200  ARG B C     1 
ATOM   7080  O  O     . ARG B 1 200 ? 171.170 124.067 176.486 1.00 130.12 ? 200  ARG B O     1 
ATOM   7081  C  CB    . ARG B 1 200 ? 171.336 123.566 179.632 1.00 136.48 ? 200  ARG B CB    1 
ATOM   7082  C  CG    . ARG B 1 200 ? 170.213 124.148 180.463 1.00 138.51 ? 200  ARG B CG    1 
ATOM   7083  C  CD    . ARG B 1 200 ? 170.762 124.749 181.751 1.00 144.37 ? 200  ARG B CD    1 
ATOM   7084  N  NE    . ARG B 1 200 ? 171.845 123.966 182.342 1.00 147.67 ? 200  ARG B NE    1 
ATOM   7085  C  CZ    . ARG B 1 200 ? 171.752 122.704 182.745 1.00 151.04 ? 200  ARG B CZ    1 
ATOM   7086  N  NH1   . ARG B 1 200 ? 170.615 122.030 182.671 1.00 149.57 ? 200  ARG B NH1   1 
ATOM   7087  N  NH2   . ARG B 1 200 ? 172.827 122.103 183.248 1.00 154.47 ? 200  ARG B NH2   1 
ATOM   7088  N  N     . MET B 1 201 ? 169.077 123.856 177.298 1.00 123.30 ? 201  MET B N     1 
ATOM   7089  C  CA    . MET B 1 201 ? 168.447 124.672 176.270 1.00 117.30 ? 201  MET B CA    1 
ATOM   7090  C  C     . MET B 1 201 ? 167.880 125.947 176.879 1.00 125.60 ? 201  MET B C     1 
ATOM   7091  O  O     . MET B 1 201 ? 167.113 125.899 177.845 1.00 134.16 ? 201  MET B O     1 
ATOM   7092  C  CB    . MET B 1 201 ? 167.342 123.890 175.558 1.00 115.22 ? 201  MET B CB    1 
ATOM   7093  C  CG    . MET B 1 201 ? 166.468 124.727 174.642 1.00 111.57 ? 201  MET B CG    1 
ATOM   7094  S  SD    . MET B 1 201 ? 164.926 125.250 175.409 1.00 115.88 ? 201  MET B SD    1 
ATOM   7095  C  CE    . MET B 1 201 ? 163.775 124.101 174.662 1.00 110.27 ? 201  MET B CE    1 
ATOM   7096  N  N     . TRP B 1 202 ? 168.252 127.084 176.296 1.00 119.96 ? 202  TRP B N     1 
ATOM   7097  C  CA    . TRP B 1 202 ? 167.858 128.409 176.751 1.00 116.59 ? 202  TRP B CA    1 
ATOM   7098  C  C     . TRP B 1 202 ? 166.693 128.939 175.927 1.00 112.39 ? 202  TRP B C     1 
ATOM   7099  O  O     . TRP B 1 202 ? 166.616 128.715 174.717 1.00 111.52 ? 202  TRP B O     1 
ATOM   7100  C  CB    . TRP B 1 202 ? 169.042 129.372 176.654 1.00 115.10 ? 202  TRP B CB    1 
ATOM   7101  C  CG    . TRP B 1 202 ? 170.257 128.888 177.368 1.00 120.80 ? 202  TRP B CG    1 
ATOM   7102  C  CD1   . TRP B 1 202 ? 171.391 128.386 176.807 1.00 124.94 ? 202  TRP B CD1   1 
ATOM   7103  C  CD2   . TRP B 1 202 ? 170.514 128.974 178.774 1.00 127.80 ? 202  TRP B CD2   1 
ATOM   7104  N  NE1   . TRP B 1 202 ? 172.313 128.092 177.779 1.00 133.48 ? 202  TRP B NE1   1 
ATOM   7105  C  CE2   . TRP B 1 202 ? 171.800 128.451 178.997 1.00 135.69 ? 202  TRP B CE2   1 
ATOM   7106  C  CE3   . TRP B 1 202 ? 169.771 129.422 179.868 1.00 128.56 ? 202  TRP B CE3   1 
ATOM   7107  C  CZ2   . TRP B 1 202 ? 172.359 128.360 180.268 1.00 139.29 ? 202  TRP B CZ2   1 
ATOM   7108  C  CZ3   . TRP B 1 202 ? 170.326 129.327 181.130 1.00 138.59 ? 202  TRP B CZ3   1 
ATOM   7109  C  CH2   . TRP B 1 202 ? 171.608 128.801 181.319 1.00 141.05 ? 202  TRP B CH2   1 
ATOM   7110  N  N     . TYR B 1 203 ? 165.792 129.659 176.593 1.00 112.75 ? 203  TYR B N     1 
ATOM   7111  C  CA    . TYR B 1 203 ? 164.610 130.195 175.934 1.00 108.02 ? 203  TYR B CA    1 
ATOM   7112  C  C     . TYR B 1 203 ? 164.173 131.476 176.628 1.00 111.19 ? 203  TYR B C     1 
ATOM   7113  O  O     . TYR B 1 203 ? 164.201 131.562 177.857 1.00 121.18 ? 203  TYR B O     1 
ATOM   7114  C  CB    . TYR B 1 203 ? 163.462 129.184 175.947 1.00 105.58 ? 203  TYR B CB    1 
ATOM   7115  C  CG    . TYR B 1 203 ? 162.096 129.822 175.923 1.00 106.54 ? 203  TYR B CG    1 
ATOM   7116  C  CD1   . TYR B 1 203 ? 161.595 130.377 174.758 1.00 112.01 ? 203  TYR B CD1   1 
ATOM   7117  C  CD2   . TYR B 1 203 ? 161.305 129.868 177.059 1.00 107.17 ? 203  TYR B CD2   1 
ATOM   7118  C  CE1   . TYR B 1 203 ? 160.351 130.959 174.722 1.00 112.84 ? 203  TYR B CE1   1 
ATOM   7119  C  CE2   . TYR B 1 203 ? 160.056 130.452 177.030 1.00 109.41 ? 203  TYR B CE2   1 
ATOM   7120  C  CZ    . TYR B 1 203 ? 159.586 130.995 175.857 1.00 108.46 ? 203  TYR B CZ    1 
ATOM   7121  O  OH    . TYR B 1 203 ? 158.345 131.578 175.813 1.00 105.33 ? 203  TYR B OH    1 
ATOM   7122  N  N     . THR B 1 204 ? 163.750 132.462 175.832 1.00 108.44 ? 204  THR B N     1 
ATOM   7123  C  CA    . THR B 1 204 ? 163.260 133.731 176.355 1.00 115.84 ? 204  THR B CA    1 
ATOM   7124  C  C     . THR B 1 204 ? 162.170 134.291 175.457 1.00 114.57 ? 204  THR B C     1 
ATOM   7125  O  O     . THR B 1 204 ? 162.374 134.393 174.240 1.00 116.11 ? 204  THR B O     1 
ATOM   7126  C  CB    . THR B 1 204 ? 164.383 134.764 176.489 1.00 120.49 ? 204  THR B CB    1 
ATOM   7127  O  OG1   . THR B 1 204 ? 163.814 136.074 176.602 1.00 114.61 ? 204  THR B OG1   1 
ATOM   7128  C  CG2   . THR B 1 204 ? 165.313 134.717 175.288 1.00 119.44 ? 204  THR B CG2   1 
ATOM   7129  N  N     . PRO B 1 205 ? 161.016 134.661 176.013 1.00 113.81 ? 205  PRO B N     1 
ATOM   7130  C  CA    . PRO B 1 205 ? 159.995 135.344 175.215 1.00 115.20 ? 205  PRO B CA    1 
ATOM   7131  C  C     . PRO B 1 205 ? 160.235 136.844 175.189 1.00 120.61 ? 205  PRO B C     1 
ATOM   7132  O  O     . PRO B 1 205 ? 160.574 137.466 176.198 1.00 125.16 ? 205  PRO B O     1 
ATOM   7133  C  CB    . PRO B 1 205 ? 158.701 134.999 175.961 1.00 113.47 ? 205  PRO B CB    1 
ATOM   7134  C  CG    . PRO B 1 205 ? 159.128 134.908 177.383 1.00 112.87 ? 205  PRO B CG    1 
ATOM   7135  C  CD    . PRO B 1 205 ? 160.569 134.439 177.399 1.00 113.89 ? 205  PRO B CD    1 
ATOM   7136  N  N     . VAL B 1 206 ? 160.057 137.436 174.011 1.00 119.90 ? 206  VAL B N     1 
ATOM   7137  C  CA    . VAL B 1 206 ? 160.378 138.842 173.817 1.00 122.01 ? 206  VAL B CA    1 
ATOM   7138  C  C     . VAL B 1 206 ? 159.122 139.602 173.408 1.00 122.82 ? 206  VAL B C     1 
ATOM   7139  O  O     . VAL B 1 206 ? 158.310 139.132 172.605 1.00 118.21 ? 206  VAL B O     1 
ATOM   7140  C  CB    . VAL B 1 206 ? 161.521 139.043 172.792 1.00 119.78 ? 206  VAL B CB    1 
ATOM   7141  C  CG1   . VAL B 1 206 ? 162.631 138.027 173.020 1.00 121.87 ? 206  VAL B CG1   1 
ATOM   7142  C  CG2   . VAL B 1 206 ? 161.016 138.949 171.384 1.00 115.50 ? 206  VAL B CG2   1 
ATOM   7143  N  N     . TYR B 1 207 ? 158.947 140.777 174.016 1.00 126.52 ? 207  TYR B N     1 
ATOM   7144  C  CA    . TYR B 1 207 ? 157.832 141.669 173.733 1.00 125.80 ? 207  TYR B CA    1 
ATOM   7145  C  C     . TYR B 1 207 ? 158.086 142.581 172.542 1.00 129.65 ? 207  TYR B C     1 
ATOM   7146  O  O     . TYR B 1 207 ? 157.135 143.185 172.037 1.00 131.37 ? 207  TYR B O     1 
ATOM   7147  C  CB    . TYR B 1 207 ? 157.533 142.541 174.964 1.00 121.02 ? 207  TYR B CB    1 
ATOM   7148  C  CG    . TYR B 1 207 ? 156.358 143.492 174.826 1.00 126.75 ? 207  TYR B CG    1 
ATOM   7149  C  CD1   . TYR B 1 207 ? 155.218 143.140 174.109 1.00 130.33 ? 207  TYR B CD1   1 
ATOM   7150  C  CD2   . TYR B 1 207 ? 156.413 144.762 175.377 1.00 133.18 ? 207  TYR B CD2   1 
ATOM   7151  C  CE1   . TYR B 1 207 ? 154.160 144.017 173.976 1.00 135.36 ? 207  TYR B CE1   1 
ATOM   7152  C  CE2   . TYR B 1 207 ? 155.365 145.642 175.245 1.00 137.67 ? 207  TYR B CE2   1 
ATOM   7153  C  CZ    . TYR B 1 207 ? 154.242 145.266 174.549 1.00 139.52 ? 207  TYR B CZ    1 
ATOM   7154  O  OH    . TYR B 1 207 ? 153.201 146.154 174.428 1.00 148.44 ? 207  TYR B OH    1 
ATOM   7155  N  N     . CYS B 1 208 ? 159.333 142.678 172.070 1.00 127.25 ? 208  CYS B N     1 
ATOM   7156  C  CA    . CYS B 1 208 ? 159.788 143.734 171.170 1.00 125.80 ? 208  CYS B CA    1 
ATOM   7157  C  C     . CYS B 1 208 ? 158.784 144.005 170.060 1.00 130.33 ? 208  CYS B C     1 
ATOM   7158  O  O     . CYS B 1 208 ? 158.597 143.167 169.171 1.00 130.58 ? 208  CYS B O     1 
ATOM   7159  C  CB    . CYS B 1 208 ? 161.140 143.365 170.558 1.00 126.12 ? 208  CYS B CB    1 
ATOM   7160  S  SG    . CYS B 1 208 ? 162.177 144.785 170.175 1.00 134.07 ? 208  CYS B SG    1 
ATOM   7161  N  N     . PRO B 1 209 ? 158.095 145.149 170.096 1.00 132.74 ? 209  PRO B N     1 
ATOM   7162  C  CA    . PRO B 1 209 ? 157.179 145.466 168.991 1.00 133.57 ? 209  PRO B CA    1 
ATOM   7163  C  C     . PRO B 1 209 ? 157.907 145.994 167.774 1.00 134.99 ? 209  PRO B C     1 
ATOM   7164  O  O     . PRO B 1 209 ? 157.556 145.647 166.639 1.00 138.55 ? 209  PRO B O     1 
ATOM   7165  C  CB    . PRO B 1 209 ? 156.252 146.526 169.603 1.00 131.87 ? 209  PRO B CB    1 
ATOM   7166  C  CG    . PRO B 1 209 ? 157.099 147.195 170.637 1.00 132.30 ? 209  PRO B CG    1 
ATOM   7167  C  CD    . PRO B 1 209 ? 158.001 146.126 171.196 1.00 132.58 ? 209  PRO B CD    1 
ATOM   7168  N  N     . HIS B 1 210 ? 158.913 146.833 167.990 1.00 132.74 ? 210  HIS B N     1 
ATOM   7169  C  CA    . HIS B 1 210 ? 159.755 147.367 166.935 1.00 133.35 ? 210  HIS B CA    1 
ATOM   7170  C  C     . HIS B 1 210 ? 161.119 146.710 167.058 1.00 129.56 ? 210  HIS B C     1 
ATOM   7171  O  O     . HIS B 1 210 ? 161.880 147.058 167.976 1.00 130.66 ? 210  HIS B O     1 
ATOM   7172  C  CB    . HIS B 1 210 ? 159.879 148.886 167.068 1.00 139.76 ? 210  HIS B CB    1 
ATOM   7173  C  CG    . HIS B 1 210 ? 158.598 149.623 166.826 1.00 151.83 ? 210  HIS B CG    1 
ATOM   7174  N  ND1   . HIS B 1 210 ? 157.656 149.187 165.921 1.00 154.53 ? 210  HIS B ND1   1 
ATOM   7175  C  CD2   . HIS B 1 210 ? 158.102 150.764 167.366 1.00 159.74 ? 210  HIS B CD2   1 
ATOM   7176  C  CE1   . HIS B 1 210 ? 156.637 150.028 165.911 1.00 156.69 ? 210  HIS B CE1   1 
ATOM   7177  N  NE2   . HIS B 1 210 ? 156.881 150.993 166.779 1.00 161.54 ? 210  HIS B NE2   1 
ATOM   7178  N  N     . PRO B 1 211 ? 161.481 145.767 166.185 1.00 123.32 ? 211  PRO B N     1 
ATOM   7179  C  CA    . PRO B 1 211 ? 162.703 144.981 166.418 1.00 121.11 ? 211  PRO B CA    1 
ATOM   7180  C  C     . PRO B 1 211 ? 163.985 145.801 166.428 1.00 124.02 ? 211  PRO B C     1 
ATOM   7181  O  O     . PRO B 1 211 ? 165.069 145.214 166.532 1.00 124.48 ? 211  PRO B O     1 
ATOM   7182  C  CB    . PRO B 1 211 ? 162.703 143.980 165.257 1.00 115.84 ? 211  PRO B CB    1 
ATOM   7183  C  CG    . PRO B 1 211 ? 161.282 143.923 164.806 1.00 116.14 ? 211  PRO B CG    1 
ATOM   7184  C  CD    . PRO B 1 211 ? 160.735 145.296 165.011 1.00 120.43 ? 211  PRO B CD    1 
ATOM   7185  N  N     . ILE B 1 212 ? 163.910 147.127 166.296 1.00 122.26 ? 212  ILE B N     1 
ATOM   7186  C  CA    . ILE B 1 212 ? 165.118 147.943 166.367 1.00 120.63 ? 212  ILE B CA    1 
ATOM   7187  C  C     . ILE B 1 212 ? 165.647 148.020 167.795 1.00 123.63 ? 212  ILE B C     1 
ATOM   7188  O  O     . ILE B 1 212 ? 166.860 147.931 168.017 1.00 125.08 ? 212  ILE B O     1 
ATOM   7189  C  CB    . ILE B 1 212 ? 164.881 149.352 165.783 1.00 119.50 ? 212  ILE B CB    1 
ATOM   7190  C  CG1   . ILE B 1 212 ? 164.025 149.307 164.513 1.00 118.21 ? 212  ILE B CG1   1 
ATOM   7191  C  CG2   . ILE B 1 212 ? 166.207 150.043 165.508 1.00 122.20 ? 212  ILE B CG2   1 
ATOM   7192  C  CD1   . ILE B 1 212 ? 162.526 149.361 164.758 1.00 122.17 ? 212  ILE B CD1   1 
ATOM   7193  N  N     . ASP B 1 213 ? 164.768 148.193 168.786 1.00 124.19 ? 213  ASP B N     1 
ATOM   7194  C  CA    . ASP B 1 213 ? 165.209 148.286 170.172 1.00 130.38 ? 213  ASP B CA    1 
ATOM   7195  C  C     . ASP B 1 213 ? 165.247 146.934 170.864 1.00 126.24 ? 213  ASP B C     1 
ATOM   7196  O  O     . ASP B 1 213 ? 165.023 146.860 172.076 1.00 129.52 ? 213  ASP B O     1 
ATOM   7197  C  CB    . ASP B 1 213 ? 164.335 149.257 170.968 1.00 136.44 ? 213  ASP B CB    1 
ATOM   7198  C  CG    . ASP B 1 213 ? 162.887 149.221 170.560 1.00 137.11 ? 213  ASP B CG    1 
ATOM   7199  O  OD1   . ASP B 1 213 ? 162.346 148.118 170.322 1.00 132.38 ? 213  ASP B OD1   1 
ATOM   7200  O  OD2   . ASP B 1 213 ? 162.293 150.316 170.505 1.00 140.74 ? 213  ASP B OD2   1 
ATOM   7201  N  N     . PHE B 1 214 ? 165.503 145.864 170.111 1.00 120.11 ? 214  PHE B N     1 
ATOM   7202  C  CA    . PHE B 1 214 ? 165.671 144.545 170.708 1.00 119.32 ? 214  PHE B CA    1 
ATOM   7203  C  C     . PHE B 1 214 ? 166.824 144.536 171.702 1.00 124.25 ? 214  PHE B C     1 
ATOM   7204  O  O     . PHE B 1 214 ? 166.715 143.951 172.785 1.00 131.95 ? 214  PHE B O     1 
ATOM   7205  C  CB    . PHE B 1 214 ? 165.904 143.517 169.604 1.00 120.18 ? 214  PHE B CB    1 
ATOM   7206  C  CG    . PHE B 1 214 ? 165.788 142.095 170.057 1.00 117.04 ? 214  PHE B CG    1 
ATOM   7207  C  CD1   . PHE B 1 214 ? 164.560 141.474 170.134 1.00 117.11 ? 214  PHE B CD1   1 
ATOM   7208  C  CD2   . PHE B 1 214 ? 166.918 141.372 170.387 1.00 112.93 ? 214  PHE B CD2   1 
ATOM   7209  C  CE1   . PHE B 1 214 ? 164.460 140.159 170.541 1.00 113.77 ? 214  PHE B CE1   1 
ATOM   7210  C  CE2   . PHE B 1 214 ? 166.825 140.059 170.796 1.00 109.32 ? 214  PHE B CE2   1 
ATOM   7211  C  CZ    . PHE B 1 214 ? 165.594 139.453 170.873 1.00 109.56 ? 214  PHE B CZ    1 
ATOM   7212  N  N     . SER B 1 215 ? 167.940 145.175 171.351 1.00 121.81 ? 215  SER B N     1 
ATOM   7213  C  CA    . SER B 1 215 ? 169.058 145.287 172.277 1.00 125.08 ? 215  SER B CA    1 
ATOM   7214  C  C     . SER B 1 215 ? 168.813 146.324 173.364 1.00 127.89 ? 215  SER B C     1 
ATOM   7215  O  O     . SER B 1 215 ? 169.481 146.282 174.402 1.00 129.52 ? 215  SER B O     1 
ATOM   7216  C  CB    . SER B 1 215 ? 170.345 145.623 171.517 1.00 128.10 ? 215  SER B CB    1 
ATOM   7217  O  OG    . SER B 1 215 ? 170.088 146.452 170.397 1.00 127.25 ? 215  SER B OG    1 
ATOM   7218  N  N     . ASN B 1 216 ? 167.874 147.249 173.153 1.00 127.88 ? 216  ASN B N     1 
ATOM   7219  C  CA    . ASN B 1 216 ? 167.618 148.290 174.142 1.00 128.88 ? 216  ASN B CA    1 
ATOM   7220  C  C     . ASN B 1 216 ? 166.809 147.781 175.328 1.00 129.13 ? 216  ASN B C     1 
ATOM   7221  O  O     . ASN B 1 216 ? 166.993 148.268 176.448 1.00 132.86 ? 216  ASN B O     1 
ATOM   7222  C  CB    . ASN B 1 216 ? 166.900 149.474 173.492 1.00 127.10 ? 216  ASN B CB    1 
ATOM   7223  C  CG    . ASN B 1 216 ? 167.777 150.216 172.503 1.00 130.19 ? 216  ASN B CG    1 
ATOM   7224  O  OD1   . ASN B 1 216 ? 167.295 150.739 171.499 1.00 129.76 ? 216  ASN B OD1   1 
ATOM   7225  N  ND2   . ASN B 1 216 ? 169.074 150.259 172.778 1.00 130.97 ? 216  ASN B ND2   1 
ATOM   7226  N  N     . LEU B 1 217 ? 165.917 146.816 175.109 1.00 126.90 ? 217  LEU B N     1 
ATOM   7227  C  CA    . LEU B 1 217 ? 165.052 146.318 176.171 1.00 127.12 ? 217  LEU B CA    1 
ATOM   7228  C  C     . LEU B 1 217 ? 165.736 145.302 177.075 1.00 134.32 ? 217  LEU B C     1 
ATOM   7229  O  O     . LEU B 1 217 ? 165.120 144.851 178.045 1.00 141.09 ? 217  LEU B O     1 
ATOM   7230  C  CB    . LEU B 1 217 ? 163.788 145.697 175.575 1.00 121.68 ? 217  LEU B CB    1 
ATOM   7231  C  CG    . LEU B 1 217 ? 162.958 146.598 174.662 1.00 124.92 ? 217  LEU B CG    1 
ATOM   7232  C  CD1   . LEU B 1 217 ? 161.621 145.952 174.350 1.00 123.01 ? 217  LEU B CD1   1 
ATOM   7233  C  CD2   . LEU B 1 217 ? 162.760 147.959 175.297 1.00 125.28 ? 217  LEU B CD2   1 
ATOM   7234  N  N     . GLY B 1 218 ? 166.978 144.928 176.786 1.00 134.81 ? 218  GLY B N     1 
ATOM   7235  C  CA    . GLY B 1 218 ? 167.706 143.995 177.615 1.00 137.95 ? 218  GLY B CA    1 
ATOM   7236  C  C     . GLY B 1 218 ? 167.754 142.575 177.101 1.00 137.99 ? 218  GLY B C     1 
ATOM   7237  O  O     . GLY B 1 218 ? 168.273 141.701 177.804 1.00 145.17 ? 218  GLY B O     1 
ATOM   7238  N  N     . TYR B 1 219 ? 167.230 142.314 175.908 1.00 130.05 ? 219  TYR B N     1 
ATOM   7239  C  CA    . TYR B 1 219 ? 167.301 140.973 175.351 1.00 127.68 ? 219  TYR B CA    1 
ATOM   7240  C  C     . TYR B 1 219 ? 168.711 140.675 174.863 1.00 129.07 ? 219  TYR B C     1 
ATOM   7241  O  O     . TYR B 1 219 ? 169.319 141.470 174.141 1.00 131.34 ? 219  TYR B O     1 
ATOM   7242  C  CB    . TYR B 1 219 ? 166.312 140.813 174.202 1.00 123.15 ? 219  TYR B CB    1 
ATOM   7243  C  CG    . TYR B 1 219 ? 164.871 140.956 174.615 1.00 122.84 ? 219  TYR B CG    1 
ATOM   7244  C  CD1   . TYR B 1 219 ? 164.276 140.023 175.448 1.00 123.16 ? 219  TYR B CD1   1 
ATOM   7245  C  CD2   . TYR B 1 219 ? 164.110 142.029 174.185 1.00 122.92 ? 219  TYR B CD2   1 
ATOM   7246  C  CE1   . TYR B 1 219 ? 162.960 140.151 175.832 1.00 120.07 ? 219  TYR B CE1   1 
ATOM   7247  C  CE2   . TYR B 1 219 ? 162.793 142.163 174.560 1.00 122.05 ? 219  TYR B CE2   1 
ATOM   7248  C  CZ    . TYR B 1 219 ? 162.224 141.224 175.387 1.00 118.69 ? 219  TYR B CZ    1 
ATOM   7249  O  OH    . TYR B 1 219 ? 160.910 141.357 175.764 1.00 117.42 ? 219  TYR B OH    1 
ATOM   7250  N  N     . ARG B 1 220 ? 169.232 139.520 175.265 1.00 128.57 ? 220  ARG B N     1 
ATOM   7251  C  CA    . ARG B 1 220 ? 170.536 139.064 174.817 1.00 129.14 ? 220  ARG B CA    1 
ATOM   7252  C  C     . ARG B 1 220 ? 170.428 137.617 174.368 1.00 132.83 ? 220  ARG B C     1 
ATOM   7253  O  O     . ARG B 1 220 ? 169.522 136.884 174.768 1.00 133.98 ? 220  ARG B O     1 
ATOM   7254  C  CB    . ARG B 1 220 ? 171.607 139.199 175.909 1.00 134.62 ? 220  ARG B CB    1 
ATOM   7255  C  CG    . ARG B 1 220 ? 171.583 140.517 176.656 1.00 139.88 ? 220  ARG B CG    1 
ATOM   7256  C  CD    . ARG B 1 220 ? 172.052 141.654 175.766 1.00 131.96 ? 220  ARG B CD    1 
ATOM   7257  N  NE    . ARG B 1 220 ? 171.620 142.950 176.273 1.00 135.30 ? 220  ARG B NE    1 
ATOM   7258  C  CZ    . ARG B 1 220 ? 171.999 144.115 175.768 1.00 139.09 ? 220  ARG B CZ    1 
ATOM   7259  N  NH1   . ARG B 1 220 ? 172.829 144.186 174.741 1.00 144.62 ? 220  ARG B NH1   1 
ATOM   7260  N  NH2   . ARG B 1 220 ? 171.535 145.238 176.308 1.00 143.24 ? 220  ARG B NH2   1 
ATOM   7261  N  N     . LEU B 1 221 ? 171.366 137.219 173.521 1.00 133.37 ? 221  LEU B N     1 
ATOM   7262  C  CA    . LEU B 1 221 ? 171.453 135.854 173.035 1.00 131.54 ? 221  LEU B CA    1 
ATOM   7263  C  C     . LEU B 1 221 ? 172.627 135.144 173.698 1.00 133.90 ? 221  LEU B C     1 
ATOM   7264  O  O     . LEU B 1 221 ? 173.532 135.773 174.257 1.00 136.99 ? 221  LEU B O     1 
ATOM   7265  C  CB    . LEU B 1 221 ? 171.602 135.832 171.512 1.00 127.19 ? 221  LEU B CB    1 
ATOM   7266  C  CG    . LEU B 1 221 ? 170.532 136.602 170.735 1.00 116.65 ? 221  LEU B CG    1 
ATOM   7267  C  CD1   . LEU B 1 221 ? 170.708 136.420 169.239 1.00 104.17 ? 221  LEU B CD1   1 
ATOM   7268  C  CD2   . LEU B 1 221 ? 169.145 136.172 171.165 1.00 115.43 ? 221  LEU B CD2   1 
ATOM   7269  N  N     . ARG B 1 222 ? 172.595 133.812 173.637 1.00 130.55 ? 222  ARG B N     1 
ATOM   7270  C  CA    . ARG B 1 222 ? 173.626 133.024 174.302 1.00 133.01 ? 222  ARG B CA    1 
ATOM   7271  C  C     . ARG B 1 222 ? 175.005 133.323 173.735 1.00 134.36 ? 222  ARG B C     1 
ATOM   7272  O  O     . ARG B 1 222 ? 176.008 133.239 174.452 1.00 134.92 ? 222  ARG B O     1 
ATOM   7273  C  CB    . ARG B 1 222 ? 173.309 131.538 174.189 1.00 130.40 ? 222  ARG B CB    1 
ATOM   7274  C  CG    . ARG B 1 222 ? 172.391 131.054 175.277 1.00 125.06 ? 222  ARG B CG    1 
ATOM   7275  C  CD    . ARG B 1 222 ? 172.969 131.363 176.647 1.00 126.22 ? 222  ARG B CD    1 
ATOM   7276  N  NE    . ARG B 1 222 ? 174.038 130.444 177.017 1.00 130.52 ? 222  ARG B NE    1 
ATOM   7277  C  CZ    . ARG B 1 222 ? 174.756 130.540 178.127 1.00 132.66 ? 222  ARG B CZ    1 
ATOM   7278  N  NH1   . ARG B 1 222 ? 174.539 131.501 179.010 1.00 128.26 ? 222  ARG B NH1   1 
ATOM   7279  N  NH2   . ARG B 1 222 ? 175.716 129.649 178.359 1.00 139.66 ? 222  ARG B NH2   1 
ATOM   7280  N  N     . CYS B 1 223 ? 175.078 133.684 172.454 1.00 129.17 ? 223  CYS B N     1 
ATOM   7281  C  CA    . CYS B 1 223 ? 176.357 134.083 171.881 1.00 129.44 ? 223  CYS B CA    1 
ATOM   7282  C  C     . CYS B 1 223 ? 176.918 135.304 172.599 1.00 134.46 ? 223  CYS B C     1 
ATOM   7283  O  O     . CYS B 1 223 ? 178.089 135.317 173.000 1.00 134.38 ? 223  CYS B O     1 
ATOM   7284  C  CB    . CYS B 1 223 ? 176.190 134.363 170.390 1.00 120.23 ? 223  CYS B CB    1 
ATOM   7285  S  SG    . CYS B 1 223 ? 175.575 132.952 169.456 1.00 132.16 ? 223  CYS B SG    1 
ATOM   7286  N  N     . VAL B 1 224 ? 176.085 136.327 172.798 1.00 133.26 ? 224  VAL B N     1 
ATOM   7287  C  CA    . VAL B 1 224 ? 176.532 137.525 173.500 1.00 133.28 ? 224  VAL B CA    1 
ATOM   7288  C  C     . VAL B 1 224 ? 176.889 137.197 174.943 1.00 136.22 ? 224  VAL B C     1 
ATOM   7289  O  O     . VAL B 1 224 ? 177.897 137.681 175.471 1.00 140.78 ? 224  VAL B O     1 
ATOM   7290  C  CB    . VAL B 1 224 ? 175.458 138.623 173.424 1.00 130.81 ? 224  VAL B CB    1 
ATOM   7291  C  CG1   . VAL B 1 224 ? 176.002 139.929 173.972 1.00 136.88 ? 224  VAL B CG1   1 
ATOM   7292  C  CG2   . VAL B 1 224 ? 174.977 138.796 172.003 1.00 119.60 ? 224  VAL B CG2   1 
ATOM   7293  N  N     . GLU B 1 225 ? 176.070 136.378 175.606 1.00 129.91 ? 225  GLU B N     1 
ATOM   7294  C  CA    . GLU B 1 225 ? 176.313 136.078 177.014 1.00 131.35 ? 225  GLU B CA    1 
ATOM   7295  C  C     . GLU B 1 225 ? 177.617 135.312 177.201 1.00 133.63 ? 225  GLU B C     1 
ATOM   7296  O  O     . GLU B 1 225 ? 178.389 135.593 178.124 1.00 133.63 ? 225  GLU B O     1 
ATOM   7297  C  CB    . GLU B 1 225 ? 175.140 135.292 177.592 1.00 137.23 ? 225  GLU B CB    1 
ATOM   7298  C  CG    . GLU B 1 225 ? 173.813 136.012 177.496 1.00 139.66 ? 225  GLU B CG    1 
ATOM   7299  C  CD    . GLU B 1 225 ? 172.658 135.141 177.935 1.00 145.24 ? 225  GLU B CD    1 
ATOM   7300  O  OE1   . GLU B 1 225 ? 172.906 134.003 178.383 1.00 145.46 ? 225  GLU B OE1   1 
ATOM   7301  O  OE2   . GLU B 1 225 ? 171.500 135.585 177.815 1.00 146.22 ? 225  GLU B OE2   1 
ATOM   7302  N  N     . THR B 1 226 ? 177.883 134.337 176.330 1.00 131.75 ? 226  THR B N     1 
ATOM   7303  C  CA    . THR B 1 226 ? 179.115 133.568 176.414 1.00 132.90 ? 226  THR B CA    1 
ATOM   7304  C  C     . THR B 1 226 ? 180.307 134.317 175.840 1.00 135.22 ? 226  THR B C     1 
ATOM   7305  O  O     . THR B 1 226 ? 181.446 133.878 176.032 1.00 139.95 ? 226  THR B O     1 
ATOM   7306  C  CB    . THR B 1 226 ? 178.948 132.233 175.687 1.00 130.22 ? 226  THR B CB    1 
ATOM   7307  O  OG1   . THR B 1 226 ? 177.584 131.807 175.782 1.00 131.51 ? 226  THR B OG1   1 
ATOM   7308  C  CG2   . THR B 1 226 ? 179.841 131.169 176.309 1.00 131.80 ? 226  THR B CG2   1 
ATOM   7309  N  N     . GLY B 1 227 ? 180.079 135.433 175.152 1.00 133.22 ? 227  GLY B N     1 
ATOM   7310  C  CA    . GLY B 1 227 ? 181.156 136.201 174.577 1.00 129.05 ? 227  GLY B CA    1 
ATOM   7311  C  C     . GLY B 1 227 ? 181.525 135.810 173.167 1.00 124.61 ? 227  GLY B C     1 
ATOM   7312  O  O     . GLY B 1 227 ? 182.397 136.455 172.571 1.00 127.23 ? 227  GLY B O     1 
ATOM   7313  N  N     . ARG B 1 228 ? 180.901 134.772 172.617 1.00 125.20 ? 228  ARG B N     1 
ATOM   7314  C  CA    . ARG B 1 228 ? 181.131 134.425 171.224 1.00 125.82 ? 228  ARG B CA    1 
ATOM   7315  C  C     . ARG B 1 228 ? 180.590 135.524 170.324 1.00 122.13 ? 228  ARG B C     1 
ATOM   7316  O  O     . ARG B 1 228 ? 179.499 136.055 170.546 1.00 124.14 ? 228  ARG B O     1 
ATOM   7317  C  CB    . ARG B 1 228 ? 180.487 133.081 170.886 1.00 124.10 ? 228  ARG B CB    1 
ATOM   7318  C  CG    . ARG B 1 228 ? 181.119 131.915 171.631 1.00 125.83 ? 228  ARG B CG    1 
ATOM   7319  C  CD    . ARG B 1 228 ? 180.403 130.609 171.359 1.00 121.70 ? 228  ARG B CD    1 
ATOM   7320  N  NE    . ARG B 1 228 ? 181.066 129.488 172.012 1.00 129.35 ? 228  ARG B NE    1 
ATOM   7321  C  CZ    . ARG B 1 228 ? 180.575 128.258 172.067 1.00 135.09 ? 228  ARG B CZ    1 
ATOM   7322  N  NH1   . ARG B 1 228 ? 179.431 127.946 171.480 1.00 131.60 ? 228  ARG B NH1   1 
ATOM   7323  N  NH2   . ARG B 1 228 ? 181.251 127.316 172.718 1.00 140.03 ? 228  ARG B NH2   1 
ATOM   7324  N  N     . ARG B 1 229 ? 181.367 135.866 169.301 1.00 118.96 ? 229  ARG B N     1 
ATOM   7325  C  CA    . ARG B 1 229 ? 181.138 137.055 168.487 1.00 118.90 ? 229  ARG B CA    1 
ATOM   7326  C  C     . ARG B 1 229 ? 180.990 136.579 167.051 1.00 117.87 ? 229  ARG B C     1 
ATOM   7327  O  O     . ARG B 1 229 ? 181.944 136.648 166.264 1.00 121.00 ? 229  ARG B O     1 
ATOM   7328  C  CB    . ARG B 1 229 ? 182.297 138.038 168.635 1.00 126.09 ? 229  ARG B CB    1 
ATOM   7329  C  CG    . ARG B 1 229 ? 182.086 139.135 169.662 1.00 133.68 ? 229  ARG B CG    1 
ATOM   7330  C  CD    . ARG B 1 229 ? 183.430 139.729 170.057 1.00 137.48 ? 229  ARG B CD    1 
ATOM   7331  N  NE    . ARG B 1 229 ? 183.389 140.421 171.340 1.00 147.56 ? 229  ARG B NE    1 
ATOM   7332  C  CZ    . ARG B 1 229 ? 184.368 141.184 171.806 1.00 158.71 ? 229  ARG B CZ    1 
ATOM   7333  N  NH1   . ARG B 1 229 ? 185.498 141.346 171.136 1.00 160.62 ? 229  ARG B NH1   1 
ATOM   7334  N  NH2   . ARG B 1 229 ? 184.218 141.786 172.982 1.00 161.88 ? 229  ARG B NH2   1 
ATOM   7335  N  N     . PRO B 1 230 ? 179.815 136.077 166.678 1.00 111.81 ? 230  PRO B N     1 
ATOM   7336  C  CA    . PRO B 1 230 ? 179.669 135.452 165.361 1.00 107.40 ? 230  PRO B CA    1 
ATOM   7337  C  C     . PRO B 1 230 ? 179.922 136.434 164.232 1.00 108.04 ? 230  PRO B C     1 
ATOM   7338  O  O     . PRO B 1 230 ? 179.386 137.543 164.201 1.00 111.49 ? 230  PRO B O     1 
ATOM   7339  C  CB    . PRO B 1 230 ? 178.217 134.960 165.358 1.00 94.57  ? 230  PRO B CB    1 
ATOM   7340  C  CG    . PRO B 1 230 ? 177.533 135.775 166.385 1.00 102.09 ? 230  PRO B CG    1 
ATOM   7341  C  CD    . PRO B 1 230 ? 178.556 136.064 167.438 1.00 109.10 ? 230  PRO B CD    1 
ATOM   7342  N  N     . ARG B 1 231 ? 180.764 136.002 163.292 1.00 105.92 ? 231  ARG B N     1 
ATOM   7343  C  CA    . ARG B 1 231 ? 181.102 136.794 162.121 1.00 104.11 ? 231  ARG B CA    1 
ATOM   7344  C  C     . ARG B 1 231 ? 180.114 136.633 160.980 1.00 99.78  ? 231  ARG B C     1 
ATOM   7345  O  O     . ARG B 1 231 ? 179.976 137.554 160.172 1.00 104.88 ? 231  ARG B O     1 
ATOM   7346  C  CB    . ARG B 1 231 ? 182.505 136.421 161.616 1.00 110.77 ? 231  ARG B CB    1 
ATOM   7347  C  CG    . ARG B 1 231 ? 183.679 136.760 162.543 1.00 112.28 ? 231  ARG B CG    1 
ATOM   7348  C  CD    . ARG B 1 231 ? 183.491 137.974 163.455 1.00 113.94 ? 231  ARG B CD    1 
ATOM   7349  N  NE    . ARG B 1 231 ? 183.030 139.167 162.753 1.00 117.19 ? 231  ARG B NE    1 
ATOM   7350  C  CZ    . ARG B 1 231 ? 182.012 139.922 163.140 1.00 115.78 ? 231  ARG B CZ    1 
ATOM   7351  N  NH1   . ARG B 1 231 ? 181.313 139.637 164.226 1.00 110.93 ? 231  ARG B NH1   1 
ATOM   7352  N  NH2   . ARG B 1 231 ? 181.691 140.995 162.423 1.00 118.18 ? 231  ARG B NH2   1 
ATOM   7353  N  N     . LEU B 1 232 ? 179.435 135.493 160.888 1.00 92.99  ? 232  LEU B N     1 
ATOM   7354  C  CA    . LEU B 1 232 ? 178.428 135.253 159.867 1.00 88.56  ? 232  LEU B CA    1 
ATOM   7355  C  C     . LEU B 1 232 ? 177.171 134.705 160.523 1.00 88.96  ? 232  LEU B C     1 
ATOM   7356  O  O     . LEU B 1 232 ? 177.247 133.838 161.397 1.00 99.76  ? 232  LEU B O     1 
ATOM   7357  C  CB    . LEU B 1 232 ? 178.936 134.270 158.806 1.00 87.24  ? 232  LEU B CB    1 
ATOM   7358  C  CG    . LEU B 1 232 ? 177.889 133.498 157.998 1.00 85.38  ? 232  LEU B CG    1 
ATOM   7359  C  CD1   . LEU B 1 232 ? 177.088 134.430 157.112 1.00 84.02  ? 232  LEU B CD1   1 
ATOM   7360  C  CD2   . LEU B 1 232 ? 178.545 132.416 157.167 1.00 95.66  ? 232  LEU B CD2   1 
ATOM   7361  N  N     . MET B 1 233 ? 176.016 135.206 160.095 1.00 85.60  ? 233  MET B N     1 
ATOM   7362  C  CA    . MET B 1 233 ? 174.729 134.705 160.551 1.00 84.56  ? 233  MET B CA    1 
ATOM   7363  C  C     . MET B 1 233 ? 173.896 134.295 159.347 1.00 82.66  ? 233  MET B C     1 
ATOM   7364  O  O     . MET B 1 233 ? 173.997 134.900 158.277 1.00 87.39  ? 233  MET B O     1 
ATOM   7365  C  CB    . MET B 1 233 ? 173.975 135.745 161.386 1.00 88.76  ? 233  MET B CB    1 
ATOM   7366  C  CG    . MET B 1 233 ? 173.247 136.779 160.564 1.00 100.12 ? 233  MET B CG    1 
ATOM   7367  S  SD    . MET B 1 233 ? 172.482 138.081 161.539 1.00 118.82 ? 233  MET B SD    1 
ATOM   7368  C  CE    . MET B 1 233 ? 172.412 137.298 163.141 1.00 98.71  ? 233  MET B CE    1 
ATOM   7369  N  N     . ILE B 1 234 ? 173.094 133.247 159.519 1.00 86.55  ? 234  ILE B N     1 
ATOM   7370  C  CA    . ILE B 1 234 ? 172.292 132.673 158.445 1.00 82.32  ? 234  ILE B CA    1 
ATOM   7371  C  C     . ILE B 1 234 ? 170.845 132.604 158.907 1.00 88.47  ? 234  ILE B C     1 
ATOM   7372  O  O     . ILE B 1 234 ? 170.577 132.257 160.062 1.00 97.79  ? 234  ILE B O     1 
ATOM   7373  C  CB    . ILE B 1 234 ? 172.793 131.274 158.043 1.00 79.21  ? 234  ILE B CB    1 
ATOM   7374  C  CG1   . ILE B 1 234 ? 174.301 131.287 157.800 1.00 89.84  ? 234  ILE B CG1   1 
ATOM   7375  C  CG2   . ILE B 1 234 ? 172.080 130.802 156.809 1.00 83.22  ? 234  ILE B CG2   1 
ATOM   7376  C  CD1   . ILE B 1 234 ? 174.879 129.928 157.480 1.00 91.29  ? 234  ILE B CD1   1 
ATOM   7377  N  N     . CYS B 1 235 ? 169.918 132.924 158.011 1.00 86.95  ? 235  CYS B N     1 
ATOM   7378  C  CA    . CYS B 1 235 ? 168.493 132.901 158.312 1.00 89.66  ? 235  CYS B CA    1 
ATOM   7379  C  C     . CYS B 1 235 ? 167.813 131.806 157.507 1.00 91.33  ? 235  CYS B C     1 
ATOM   7380  O  O     . CYS B 1 235 ? 168.085 131.648 156.314 1.00 98.36  ? 235  CYS B O     1 
ATOM   7381  C  CB    . CYS B 1 235 ? 167.841 134.248 158.008 1.00 88.61  ? 235  CYS B CB    1 
ATOM   7382  S  SG    . CYS B 1 235 ? 166.048 134.259 158.192 1.00 100.93 ? 235  CYS B SG    1 
ATOM   7383  N  N     . ILE B 1 236 ? 166.933 131.060 158.160 1.00 88.30  ? 236  ILE B N     1 
ATOM   7384  C  CA    . ILE B 1 236 ? 166.145 130.013 157.516 1.00 91.22  ? 236  ILE B CA    1 
ATOM   7385  C  C     . ILE B 1 236 ? 164.687 130.313 157.834 1.00 97.27  ? 236  ILE B C     1 
ATOM   7386  O  O     . ILE B 1 236 ? 164.148 129.863 158.848 1.00 106.48 ? 236  ILE B O     1 
ATOM   7387  C  CB    . ILE B 1 236 ? 166.538 128.610 157.985 1.00 86.55  ? 236  ILE B CB    1 
ATOM   7388  C  CG1   . ILE B 1 236 ? 168.040 128.389 157.832 1.00 86.41  ? 236  ILE B CG1   1 
ATOM   7389  C  CG2   . ILE B 1 236 ? 165.767 127.555 157.217 1.00 92.80  ? 236  ILE B CG2   1 
ATOM   7390  C  CD1   . ILE B 1 236 ? 168.478 127.008 158.234 1.00 82.94  ? 236  ILE B CD1   1 
ATOM   7391  N  N     . THR B 1 237 ? 164.031 131.079 156.968 1.00 93.68  ? 237  THR B N     1 
ATOM   7392  C  CA    . THR B 1 237 ? 162.612 131.340 157.151 1.00 98.23  ? 237  THR B CA    1 
ATOM   7393  C  C     . THR B 1 237 ? 161.821 130.066 156.896 1.00 106.01 ? 237  THR B C     1 
ATOM   7394  O  O     . THR B 1 237 ? 161.962 129.432 155.849 1.00 111.58 ? 237  THR B O     1 
ATOM   7395  C  CB    . THR B 1 237 ? 162.139 132.443 156.207 1.00 105.77 ? 237  THR B CB    1 
ATOM   7396  O  OG1   . THR B 1 237 ? 162.338 132.029 154.852 1.00 110.70 ? 237  THR B OG1   1 
ATOM   7397  C  CG2   . THR B 1 237 ? 162.920 133.714 156.449 1.00 109.13 ? 237  THR B CG2   1 
ATOM   7398  N  N     . MET B 1 238 ? 160.982 129.693 157.858 1.00 107.96 ? 238  MET B N     1 
ATOM   7399  C  CA    . MET B 1 238 ? 160.235 128.448 157.777 1.00 107.73 ? 238  MET B CA    1 
ATOM   7400  C  C     . MET B 1 238 ? 158.782 128.708 158.141 1.00 112.02 ? 238  MET B C     1 
ATOM   7401  O  O     . MET B 1 238 ? 158.494 129.431 159.097 1.00 116.57 ? 238  MET B O     1 
ATOM   7402  C  CB    . MET B 1 238 ? 160.834 127.381 158.702 1.00 101.72 ? 238  MET B CB    1 
ATOM   7403  C  CG    . MET B 1 238 ? 159.997 126.125 158.832 1.00 106.56 ? 238  MET B CG    1 
ATOM   7404  S  SD    . MET B 1 238 ? 160.068 125.406 160.478 1.00 121.32 ? 238  MET B SD    1 
ATOM   7405  C  CE    . MET B 1 238 ? 159.493 126.781 161.464 1.00 113.88 ? 238  MET B CE    1 
ATOM   7406  N  N     . TYR B 1 239 ? 157.871 128.120 157.369 1.00 115.69 ? 239  TYR B N     1 
ATOM   7407  C  CA    . TYR B 1 239 ? 156.441 128.326 157.580 1.00 115.21 ? 239  TYR B CA    1 
ATOM   7408  C  C     . TYR B 1 239 ? 155.686 127.151 156.985 1.00 120.64 ? 239  TYR B C     1 
ATOM   7409  O  O     . TYR B 1 239 ? 155.592 127.041 155.759 1.00 126.79 ? 239  TYR B O     1 
ATOM   7410  C  CB    . TYR B 1 239 ? 155.993 129.635 156.942 1.00 119.32 ? 239  TYR B CB    1 
ATOM   7411  C  CG    . TYR B 1 239 ? 154.507 129.740 156.693 1.00 123.36 ? 239  TYR B CG    1 
ATOM   7412  C  CD1   . TYR B 1 239 ? 153.623 129.979 157.730 1.00 125.41 ? 239  TYR B CD1   1 
ATOM   7413  C  CD2   . TYR B 1 239 ? 153.993 129.616 155.411 1.00 125.76 ? 239  TYR B CD2   1 
ATOM   7414  C  CE1   . TYR B 1 239 ? 152.268 130.088 157.499 1.00 129.39 ? 239  TYR B CE1   1 
ATOM   7415  C  CE2   . TYR B 1 239 ? 152.642 129.719 155.171 1.00 128.31 ? 239  TYR B CE2   1 
ATOM   7416  C  CZ    . TYR B 1 239 ? 151.782 129.955 156.220 1.00 131.88 ? 239  TYR B CZ    1 
ATOM   7417  O  OH    . TYR B 1 239 ? 150.431 130.059 155.989 1.00 134.51 ? 239  TYR B OH    1 
ATOM   7418  N  N     . ASN B 1 240 ? 155.149 126.285 157.844 1.00 120.91 ? 240  ASN B N     1 
ATOM   7419  C  CA    . ASN B 1 240 ? 154.320 125.156 157.427 1.00 124.48 ? 240  ASN B CA    1 
ATOM   7420  C  C     . ASN B 1 240 ? 155.136 124.278 156.465 1.00 122.77 ? 240  ASN B C     1 
ATOM   7421  O  O     . ASN B 1 240 ? 154.949 124.271 155.247 1.00 124.87 ? 240  ASN B O     1 
ATOM   7422  C  CB    . ASN B 1 240 ? 152.991 125.682 156.843 1.00 124.51 ? 240  ASN B CB    1 
ATOM   7423  C  CG    . ASN B 1 240 ? 152.299 124.737 155.861 1.00 125.92 ? 240  ASN B CG    1 
ATOM   7424  O  OD1   . ASN B 1 240 ? 152.606 123.550 155.761 1.00 132.12 ? 240  ASN B OD1   1 
ATOM   7425  N  ND2   . ASN B 1 240 ? 151.352 125.287 155.115 1.00 122.66 ? 240  ASN B ND2   1 
ATOM   7426  N  N     . GLU B 1 241 ? 156.152 123.633 157.035 1.00 119.89 ? 241  GLU B N     1 
ATOM   7427  C  CA    . GLU B 1 241 ? 156.995 122.685 156.321 1.00 121.43 ? 241  GLU B CA    1 
ATOM   7428  C  C     . GLU B 1 241 ? 157.060 121.379 157.094 1.00 127.38 ? 241  GLU B C     1 
ATOM   7429  O  O     . GLU B 1 241 ? 156.897 121.355 158.315 1.00 128.50 ? 241  GLU B O     1 
ATOM   7430  C  CB    . GLU B 1 241 ? 158.425 123.212 156.121 1.00 120.86 ? 241  GLU B CB    1 
ATOM   7431  C  CG    . GLU B 1 241 ? 158.573 124.688 155.772 1.00 122.17 ? 241  GLU B CG    1 
ATOM   7432  C  CD    . GLU B 1 241 ? 157.831 125.116 154.516 1.00 126.89 ? 241  GLU B CD    1 
ATOM   7433  O  OE1   . GLU B 1 241 ? 157.341 124.248 153.766 1.00 133.54 ? 241  GLU B OE1   1 
ATOM   7434  O  OE2   . GLU B 1 241 ? 157.769 126.336 154.258 1.00 123.63 ? 241  GLU B OE2   1 
ATOM   7435  N  N     . GLY B 1 242 ? 157.309 120.292 156.374 1.00 131.74 ? 242  GLY B N     1 
ATOM   7436  C  CA    . GLY B 1 242 ? 157.506 119.010 157.001 1.00 128.96 ? 242  GLY B CA    1 
ATOM   7437  C  C     . GLY B 1 242 ? 158.884 118.925 157.619 1.00 123.75 ? 242  GLY B C     1 
ATOM   7438  O  O     . GLY B 1 242 ? 159.775 119.721 157.310 1.00 126.17 ? 242  GLY B O     1 
ATOM   7439  N  N     . PRO B 1 243 ? 159.084 117.962 158.516 1.00 120.34 ? 243  PRO B N     1 
ATOM   7440  C  CA    . PRO B 1 243 ? 160.406 117.814 159.141 1.00 124.01 ? 243  PRO B CA    1 
ATOM   7441  C  C     . PRO B 1 243 ? 161.514 117.497 158.156 1.00 128.99 ? 243  PRO B C     1 
ATOM   7442  O  O     . PRO B 1 243 ? 162.677 117.813 158.432 1.00 130.99 ? 243  PRO B O     1 
ATOM   7443  C  CB    . PRO B 1 243 ? 160.199 116.661 160.134 1.00 125.43 ? 243  PRO B CB    1 
ATOM   7444  C  CG    . PRO B 1 243 ? 158.728 116.565 160.320 1.00 128.44 ? 243  PRO B CG    1 
ATOM   7445  C  CD    . PRO B 1 243 ? 158.114 116.986 159.030 1.00 127.51 ? 243  PRO B CD    1 
ATOM   7446  N  N     . GLN B 1 244 ? 161.194 116.863 157.026 1.00 126.91 ? 244  GLN B N     1 
ATOM   7447  C  CA    . GLN B 1 244 ? 162.240 116.408 156.116 1.00 128.49 ? 244  GLN B CA    1 
ATOM   7448  C  C     . GLN B 1 244 ? 162.995 117.578 155.500 1.00 128.86 ? 244  GLN B C     1 
ATOM   7449  O  O     . GLN B 1 244 ? 164.224 117.532 155.375 1.00 130.66 ? 244  GLN B O     1 
ATOM   7450  C  CB    . GLN B 1 244 ? 161.645 115.521 155.025 1.00 129.90 ? 244  GLN B CB    1 
ATOM   7451  C  CG    . GLN B 1 244 ? 162.695 114.853 154.154 1.00 136.94 ? 244  GLN B CG    1 
ATOM   7452  C  CD    . GLN B 1 244 ? 163.588 113.907 154.935 1.00 149.40 ? 244  GLN B CD    1 
ATOM   7453  O  OE1   . GLN B 1 244 ? 163.153 113.277 155.899 1.00 153.81 ? 244  GLN B OE1   1 
ATOM   7454  N  NE2   . GLN B 1 244 ? 164.847 113.808 154.524 1.00 150.44 ? 244  GLN B NE2   1 
ATOM   7455  N  N     . GLN B 1 245 ? 162.281 118.634 155.107 1.00 125.52 ? 245  GLN B N     1 
ATOM   7456  C  CA    . GLN B 1 245 ? 162.942 119.787 154.502 1.00 123.02 ? 245  GLN B CA    1 
ATOM   7457  C  C     . GLN B 1 245 ? 163.898 120.449 155.486 1.00 122.02 ? 245  GLN B C     1 
ATOM   7458  O  O     . GLN B 1 245 ? 165.046 120.764 155.145 1.00 123.10 ? 245  GLN B O     1 
ATOM   7459  C  CB    . GLN B 1 245 ? 161.899 120.788 154.011 1.00 118.71 ? 245  GLN B CB    1 
ATOM   7460  C  CG    . GLN B 1 245 ? 160.809 120.173 153.159 1.00 125.70 ? 245  GLN B CG    1 
ATOM   7461  C  CD    . GLN B 1 245 ? 159.845 121.205 152.620 1.00 128.51 ? 245  GLN B CD    1 
ATOM   7462  O  OE1   . GLN B 1 245 ? 159.989 122.399 152.876 1.00 131.35 ? 245  GLN B OE1   1 
ATOM   7463  N  NE2   . GLN B 1 245 ? 158.853 120.751 151.865 1.00 126.22 ? 245  GLN B NE2   1 
ATOM   7464  N  N     . LEU B 1 246 ? 163.440 120.660 156.720 1.00 116.17 ? 246  LEU B N     1 
ATOM   7465  C  CA    . LEU B 1 246 ? 164.285 121.296 157.722 1.00 111.44 ? 246  LEU B CA    1 
ATOM   7466  C  C     . LEU B 1 246 ? 165.474 120.413 158.079 1.00 112.79 ? 246  LEU B C     1 
ATOM   7467  O  O     . LEU B 1 246 ? 166.592 120.909 158.264 1.00 113.10 ? 246  LEU B O     1 
ATOM   7468  C  CB    . LEU B 1 246 ? 163.459 121.629 158.962 1.00 109.58 ? 246  LEU B CB    1 
ATOM   7469  C  CG    . LEU B 1 246 ? 164.175 122.378 160.082 1.00 106.98 ? 246  LEU B CG    1 
ATOM   7470  C  CD1   . LEU B 1 246 ? 164.713 123.697 159.568 1.00 103.05 ? 246  LEU B CD1   1 
ATOM   7471  C  CD2   . LEU B 1 246 ? 163.228 122.604 161.240 1.00 109.05 ? 246  LEU B CD2   1 
ATOM   7472  N  N     . LYS B 1 247 ? 165.257 119.099 158.173 1.00 112.42 ? 247  LYS B N     1 
ATOM   7473  C  CA    . LYS B 1 247 ? 166.361 118.192 158.464 1.00 114.09 ? 247  LYS B CA    1 
ATOM   7474  C  C     . LYS B 1 247 ? 167.391 118.207 157.344 1.00 117.78 ? 247  LYS B C     1 
ATOM   7475  O  O     . LYS B 1 247 ? 168.599 118.196 157.604 1.00 117.81 ? 247  LYS B O     1 
ATOM   7476  C  CB    . LYS B 1 247 ? 165.832 116.778 158.696 1.00 116.36 ? 247  LYS B CB    1 
ATOM   7477  C  CG    . LYS B 1 247 ? 166.913 115.760 159.022 1.00 121.31 ? 247  LYS B CG    1 
ATOM   7478  C  CD    . LYS B 1 247 ? 166.360 114.601 159.834 1.00 125.92 ? 247  LYS B CD    1 
ATOM   7479  C  CE    . LYS B 1 247 ? 165.127 114.001 159.182 1.00 128.57 ? 247  LYS B CE    1 
ATOM   7480  N  NZ    . LYS B 1 247 ? 164.505 112.959 160.044 1.00 125.87 ? 247  LYS B NZ    1 
ATOM   7481  N  N     . ALA B 1 248 ? 166.933 118.238 156.090 1.00 117.87 ? 248  ALA B N     1 
ATOM   7482  C  CA    . ALA B 1 248 ? 167.860 118.318 154.967 1.00 115.71 ? 248  ALA B CA    1 
ATOM   7483  C  C     . ALA B 1 248 ? 168.652 119.617 155.000 1.00 115.36 ? 248  ALA B C     1 
ATOM   7484  O  O     . ALA B 1 248 ? 169.870 119.617 154.782 1.00 118.25 ? 248  ALA B O     1 
ATOM   7485  C  CB    . ALA B 1 248 ? 167.101 118.186 153.649 1.00 112.34 ? 248  ALA B CB    1 
ATOM   7486  N  N     . THR B 1 249 ? 167.978 120.736 155.280 1.00 110.13 ? 249  THR B N     1 
ATOM   7487  C  CA    . THR B 1 249 ? 168.677 122.017 155.341 1.00 105.47 ? 249  THR B CA    1 
ATOM   7488  C  C     . THR B 1 249 ? 169.727 122.023 156.445 1.00 108.64 ? 249  THR B C     1 
ATOM   7489  O  O     . THR B 1 249 ? 170.856 122.487 156.238 1.00 112.20 ? 249  THR B O     1 
ATOM   7490  C  CB    . THR B 1 249 ? 167.679 123.153 155.550 1.00 99.66  ? 249  THR B CB    1 
ATOM   7491  O  OG1   . THR B 1 249 ? 166.628 123.051 154.583 1.00 105.61 ? 249  THR B OG1   1 
ATOM   7492  C  CG2   . THR B 1 249 ? 168.367 124.493 155.395 1.00 99.38  ? 249  THR B CG2   1 
ATOM   7493  N  N     . LEU B 1 250 ? 169.381 121.499 157.623 1.00 106.09 ? 250  LEU B N     1 
ATOM   7494  C  CA    . LEU B 1 250 ? 170.332 121.499 158.729 1.00 105.31 ? 250  LEU B CA    1 
ATOM   7495  C  C     . LEU B 1 250 ? 171.492 120.546 158.468 1.00 110.13 ? 250  LEU B C     1 
ATOM   7496  O  O     . LEU B 1 250 ? 172.641 120.855 158.804 1.00 114.57 ? 250  LEU B O     1 
ATOM   7497  C  CB    . LEU B 1 250 ? 169.620 121.153 160.034 1.00 100.88 ? 250  LEU B CB    1 
ATOM   7498  C  CG    . LEU B 1 250 ? 168.567 122.176 160.463 1.00 94.80  ? 250  LEU B CG    1 
ATOM   7499  C  CD1   . LEU B 1 250 ? 168.020 121.849 161.839 1.00 97.59  ? 250  LEU B CD1   1 
ATOM   7500  C  CD2   . LEU B 1 250 ? 169.149 123.574 160.438 1.00 92.00  ? 250  LEU B CD2   1 
ATOM   7501  N  N     . LYS B 1 251 ? 171.221 119.388 157.860 1.00 107.36 ? 251  LYS B N     1 
ATOM   7502  C  CA    . LYS B 1 251 ? 172.305 118.483 157.498 1.00 110.63 ? 251  LYS B CA    1 
ATOM   7503  C  C     . LYS B 1 251 ? 173.243 119.132 156.490 1.00 113.24 ? 251  LYS B C     1 
ATOM   7504  O  O     . LYS B 1 251 ? 174.468 118.992 156.587 1.00 117.25 ? 251  LYS B O     1 
ATOM   7505  C  CB    . LYS B 1 251 ? 171.742 117.178 156.936 1.00 114.56 ? 251  LYS B CB    1 
ATOM   7506  C  CG    . LYS B 1 251 ? 172.810 116.222 156.426 1.00 123.30 ? 251  LYS B CG    1 
ATOM   7507  C  CD    . LYS B 1 251 ? 172.210 115.079 155.625 1.00 126.47 ? 251  LYS B CD    1 
ATOM   7508  C  CE    . LYS B 1 251 ? 173.298 114.243 154.970 1.00 125.22 ? 251  LYS B CE    1 
ATOM   7509  N  NZ    . LYS B 1 251 ? 172.735 113.138 154.147 1.00 127.78 ? 251  LYS B NZ    1 
ATOM   7510  N  N     . LYS B 1 252 ? 172.687 119.850 155.514 1.00 109.15 ? 252  LYS B N     1 
ATOM   7511  C  CA    . LYS B 1 252 ? 173.524 120.512 154.521 1.00 109.76 ? 252  LYS B CA    1 
ATOM   7512  C  C     . LYS B 1 252 ? 174.361 121.619 155.153 1.00 113.08 ? 252  LYS B C     1 
ATOM   7513  O  O     . LYS B 1 252 ? 175.532 121.800 154.798 1.00 116.46 ? 252  LYS B O     1 
ATOM   7514  C  CB    . LYS B 1 252 ? 172.654 121.057 153.393 1.00 105.04 ? 252  LYS B CB    1 
ATOM   7515  C  CG    . LYS B 1 252 ? 172.569 120.135 152.188 1.00 106.01 ? 252  LYS B CG    1 
ATOM   7516  C  CD    . LYS B 1 252 ? 172.074 118.748 152.558 1.00 110.93 ? 252  LYS B CD    1 
ATOM   7517  C  CE    . LYS B 1 252 ? 172.124 117.809 151.367 1.00 109.38 ? 252  LYS B CE    1 
ATOM   7518  N  NZ    . LYS B 1 252 ? 171.640 116.446 151.717 1.00 113.69 ? 252  LYS B NZ    1 
ATOM   7519  N  N     . LEU B 1 253 ? 173.781 122.366 156.094 1.00 107.79 ? 253  LEU B N     1 
ATOM   7520  C  CA    . LEU B 1 253 ? 174.552 123.388 156.797 1.00 105.16 ? 253  LEU B CA    1 
ATOM   7521  C  C     . LEU B 1 253 ? 175.672 122.766 157.623 1.00 108.35 ? 253  LEU B C     1 
ATOM   7522  O  O     . LEU B 1 253 ? 176.783 123.308 157.687 1.00 113.89 ? 253  LEU B O     1 
ATOM   7523  C  CB    . LEU B 1 253 ? 173.632 124.224 157.681 1.00 101.27 ? 253  LEU B CB    1 
ATOM   7524  C  CG    . LEU B 1 253 ? 172.848 125.308 156.947 1.00 95.43  ? 253  LEU B CG    1 
ATOM   7525  C  CD1   . LEU B 1 253 ? 171.973 126.067 157.915 1.00 94.93  ? 253  LEU B CD1   1 
ATOM   7526  C  CD2   . LEU B 1 253 ? 173.798 126.248 156.240 1.00 97.45  ? 253  LEU B CD2   1 
ATOM   7527  N  N     . ALA B 1 254 ? 175.398 121.633 158.270 1.00 103.92 ? 254  ALA B N     1 
ATOM   7528  C  CA    . ALA B 1 254 ? 176.444 120.945 159.018 1.00 104.99 ? 254  ALA B CA    1 
ATOM   7529  C  C     . ALA B 1 254 ? 177.552 120.461 158.091 1.00 109.34 ? 254  ALA B C     1 
ATOM   7530  O  O     . ALA B 1 254 ? 178.736 120.519 158.443 1.00 114.53 ? 254  ALA B O     1 
ATOM   7531  C  CB    . ALA B 1 254 ? 175.847 119.781 159.801 1.00 111.62 ? 254  ALA B CB    1 
ATOM   7532  N  N     . ASN B 1 255 ? 177.185 119.976 156.903 1.00 106.90 ? 255  ASN B N     1 
ATOM   7533  C  CA    . ASN B 1 255 ? 178.193 119.589 155.920 1.00 110.08 ? 255  ASN B CA    1 
ATOM   7534  C  C     . ASN B 1 255 ? 179.034 120.786 155.498 1.00 115.55 ? 255  ASN B C     1 
ATOM   7535  O  O     . ASN B 1 255 ? 180.254 120.671 155.329 1.00 119.50 ? 255  ASN B O     1 
ATOM   7536  C  CB    . ASN B 1 255 ? 177.525 118.950 154.705 1.00 110.03 ? 255  ASN B CB    1 
ATOM   7537  C  CG    . ASN B 1 255 ? 176.953 117.583 155.007 1.00 116.08 ? 255  ASN B CG    1 
ATOM   7538  O  OD1   . ASN B 1 255 ? 176.758 117.222 156.166 1.00 118.63 ? 255  ASN B OD1   1 
ATOM   7539  N  ND2   . ASN B 1 255 ? 176.677 116.813 153.963 1.00 119.01 ? 255  ASN B ND2   1 
ATOM   7540  N  N     . ASN B 1 256 ? 178.396 121.944 155.314 1.00 112.52 ? 256  ASN B N     1 
ATOM   7541  C  CA    . ASN B 1 256 ? 179.139 123.154 154.974 1.00 107.38 ? 256  ASN B CA    1 
ATOM   7542  C  C     . ASN B 1 256 ? 180.125 123.523 156.074 1.00 111.42 ? 256  ASN B C     1 
ATOM   7543  O  O     . ASN B 1 256 ? 181.275 123.884 155.794 1.00 113.55 ? 256  ASN B O     1 
ATOM   7544  C  CB    . ASN B 1 256 ? 178.174 124.309 154.721 1.00 97.33  ? 256  ASN B CB    1 
ATOM   7545  C  CG    . ASN B 1 256 ? 177.556 124.256 153.348 1.00 103.81 ? 256  ASN B CG    1 
ATOM   7546  O  OD1   . ASN B 1 256 ? 178.153 124.703 152.371 1.00 110.44 ? 256  ASN B OD1   1 
ATOM   7547  N  ND2   . ASN B 1 256 ? 176.351 123.710 153.262 1.00 103.67 ? 256  ASN B ND2   1 
ATOM   7548  N  N     . LEU B 1 257 ? 179.691 123.445 157.333 1.00 110.73 ? 257  LEU B N     1 
ATOM   7549  C  CA    . LEU B 1 257 ? 180.592 123.756 158.439 1.00 108.12 ? 257  LEU B CA    1 
ATOM   7550  C  C     . LEU B 1 257 ? 181.748 122.765 158.505 1.00 112.79 ? 257  LEU B C     1 
ATOM   7551  O  O     . LEU B 1 257 ? 182.888 123.149 158.788 1.00 117.01 ? 257  LEU B O     1 
ATOM   7552  C  CB    . LEU B 1 257 ? 179.826 123.780 159.761 1.00 103.90 ? 257  LEU B CB    1 
ATOM   7553  C  CG    . LEU B 1 257 ? 178.660 124.763 159.872 1.00 100.00 ? 257  LEU B CG    1 
ATOM   7554  C  CD1   . LEU B 1 257 ? 178.299 124.992 161.326 1.00 101.06 ? 257  LEU B CD1   1 
ATOM   7555  C  CD2   . LEU B 1 257 ? 178.999 126.077 159.197 1.00 98.52  ? 257  LEU B CD2   1 
ATOM   7556  N  N     . ALA B 1 258 ? 181.475 121.485 158.248 1.00 112.57 ? 258  ALA B N     1 
ATOM   7557  C  CA    . ALA B 1 258 ? 182.549 120.497 158.226 1.00 115.40 ? 258  ALA B CA    1 
ATOM   7558  C  C     . ALA B 1 258 ? 183.550 120.797 157.117 1.00 121.88 ? 258  ALA B C     1 
ATOM   7559  O  O     . ALA B 1 258 ? 184.768 120.701 157.322 1.00 128.12 ? 258  ALA B O     1 
ATOM   7560  C  CB    . ALA B 1 258 ? 181.970 119.092 158.063 1.00 110.82 ? 258  ALA B CB    1 
ATOM   7561  N  N     . TYR B 1 259 ? 183.054 121.170 155.935 1.00 116.73 ? 259  TYR B N     1 
ATOM   7562  C  CA    . TYR B 1 259 ? 183.946 121.526 154.837 1.00 118.82 ? 259  TYR B CA    1 
ATOM   7563  C  C     . TYR B 1 259 ? 184.789 122.744 155.184 1.00 121.76 ? 259  TYR B C     1 
ATOM   7564  O  O     . TYR B 1 259 ? 185.978 122.802 154.851 1.00 126.34 ? 259  TYR B O     1 
ATOM   7565  C  CB    . TYR B 1 259 ? 183.139 121.779 153.565 1.00 114.41 ? 259  TYR B CB    1 
ATOM   7566  C  CG    . TYR B 1 259 ? 183.989 122.093 152.357 1.00 112.44 ? 259  TYR B CG    1 
ATOM   7567  C  CD1   . TYR B 1 259 ? 184.571 121.079 151.612 1.00 117.09 ? 259  TYR B CD1   1 
ATOM   7568  C  CD2   . TYR B 1 259 ? 184.204 123.404 151.959 1.00 109.31 ? 259  TYR B CD2   1 
ATOM   7569  C  CE1   . TYR B 1 259 ? 185.348 121.362 150.508 1.00 116.25 ? 259  TYR B CE1   1 
ATOM   7570  C  CE2   . TYR B 1 259 ? 184.979 123.695 150.856 1.00 112.99 ? 259  TYR B CE2   1 
ATOM   7571  C  CZ    . TYR B 1 259 ? 185.548 122.671 150.134 1.00 117.03 ? 259  TYR B CZ    1 
ATOM   7572  O  OH    . TYR B 1 259 ? 186.321 122.956 149.033 1.00 123.35 ? 259  TYR B OH    1 
ATOM   7573  N  N     . LEU B 1 260 ? 184.188 123.732 155.849 1.00 117.42 ? 260  LEU B N     1 
ATOM   7574  C  CA    . LEU B 1 260 ? 184.950 124.899 156.277 1.00 115.73 ? 260  LEU B CA    1 
ATOM   7575  C  C     . LEU B 1 260 ? 186.003 124.517 157.310 1.00 122.40 ? 260  LEU B C     1 
ATOM   7576  O  O     . LEU B 1 260 ? 187.094 125.097 157.340 1.00 127.83 ? 260  LEU B O     1 
ATOM   7577  C  CB    . LEU B 1 260 ? 184.008 125.965 156.834 1.00 112.14 ? 260  LEU B CB    1 
ATOM   7578  C  CG    . LEU B 1 260 ? 183.376 126.892 155.798 1.00 109.08 ? 260  LEU B CG    1 
ATOM   7579  C  CD1   . LEU B 1 260 ? 182.455 127.894 156.466 1.00 113.49 ? 260  LEU B CD1   1 
ATOM   7580  C  CD2   . LEU B 1 260 ? 184.454 127.600 155.008 1.00 114.84 ? 260  LEU B CD2   1 
ATOM   7581  N  N     . LYS B 1 261 ? 185.689 123.549 158.172 1.00 121.83 ? 261  LYS B N     1 
ATOM   7582  C  CA    . LYS B 1 261 ? 186.669 123.066 159.139 1.00 123.04 ? 261  LYS B CA    1 
ATOM   7583  C  C     . LYS B 1 261 ? 187.848 122.394 158.447 1.00 127.97 ? 261  LYS B C     1 
ATOM   7584  O  O     . LYS B 1 261 ? 189.006 122.595 158.831 1.00 131.57 ? 261  LYS B O     1 
ATOM   7585  C  CB    . LYS B 1 261 ? 186.010 122.095 160.119 1.00 124.01 ? 261  LYS B CB    1 
ATOM   7586  C  CG    . LYS B 1 261 ? 186.582 122.159 161.523 1.00 127.74 ? 261  LYS B CG    1 
ATOM   7587  C  CD    . LYS B 1 261 ? 185.660 121.508 162.535 1.00 126.01 ? 261  LYS B CD    1 
ATOM   7588  C  CE    . LYS B 1 261 ? 185.647 119.998 162.374 1.00 126.28 ? 261  LYS B CE    1 
ATOM   7589  N  NZ    . LYS B 1 261 ? 186.986 119.401 162.628 1.00 125.04 ? 261  LYS B NZ    1 
ATOM   7590  N  N     . GLU B 1 262 ? 187.574 121.594 157.421 1.00 129.13 ? 262  GLU B N     1 
ATOM   7591  C  CA    . GLU B 1 262 ? 188.626 120.752 156.843 1.00 135.36 ? 262  GLU B CA    1 
ATOM   7592  C  C     . GLU B 1 262 ? 189.529 121.477 155.843 1.00 139.91 ? 262  GLU B C     1 
ATOM   7593  O  O     . GLU B 1 262 ? 190.151 120.783 155.030 1.00 145.15 ? 262  GLU B O     1 
ATOM   7594  C  CB    . GLU B 1 262 ? 188.000 119.526 156.177 1.00 138.91 ? 262  GLU B CB    1 
ATOM   7595  C  CG    . GLU B 1 262 ? 187.214 118.644 157.130 1.00 145.96 ? 262  GLU B CG    1 
ATOM   7596  C  CD    . GLU B 1 262 ? 186.678 117.396 156.461 1.00 152.88 ? 262  GLU B CD    1 
ATOM   7597  O  OE1   . GLU B 1 262 ? 186.970 117.190 155.264 1.00 156.03 ? 262  GLU B OE1   1 
ATOM   7598  O  OE2   . GLU B 1 262 ? 185.966 116.620 157.132 1.00 148.01 ? 262  GLU B OE2   1 
ATOM   7599  N  N     . GLN B 1 263 ? 189.644 122.802 155.839 1.00 140.42 ? 263  GLN B N     1 
ATOM   7600  C  CA    . GLN B 1 263 ? 190.508 123.473 154.876 1.00 143.49 ? 263  GLN B CA    1 
ATOM   7601  C  C     . GLN B 1 263 ? 191.969 123.381 155.299 1.00 151.46 ? 263  GLN B C     1 
ATOM   7602  O  O     . GLN B 1 263 ? 192.298 123.519 156.480 1.00 151.36 ? 263  GLN B O     1 
ATOM   7603  C  CB    . GLN B 1 263 ? 190.095 124.932 154.727 1.00 139.72 ? 263  GLN B CB    1 
ATOM   7604  C  CG    . GLN B 1 263 ? 188.612 125.115 154.513 1.00 132.71 ? 263  GLN B CG    1 
ATOM   7605  C  CD    . GLN B 1 263 ? 188.306 126.239 153.559 1.00 135.55 ? 263  GLN B CD    1 
ATOM   7606  O  OE1   . GLN B 1 263 ? 188.068 127.373 153.969 1.00 133.38 ? 263  GLN B OE1   1 
ATOM   7607  N  NE2   . GLN B 1 263 ? 188.318 125.932 152.269 1.00 136.71 ? 263  GLN B NE2   1 
ATOM   7608  N  N     . MET B 1 264 ? 192.844 123.145 154.326 1.00 157.32 ? 264  MET B N     1 
ATOM   7609  C  CA    . MET B 1 264 ? 194.270 123.053 154.608 1.00 163.97 ? 264  MET B CA    1 
ATOM   7610  C  C     . MET B 1 264 ? 194.853 124.443 154.858 1.00 164.88 ? 264  MET B C     1 
ATOM   7611  O  O     . MET B 1 264 ? 194.717 125.335 154.015 1.00 165.03 ? 264  MET B O     1 
ATOM   7612  C  CB    . MET B 1 264 ? 195.002 122.385 153.445 1.00 166.62 ? 264  MET B CB    1 
ATOM   7613  C  CG    . MET B 1 264 ? 194.874 120.873 153.412 1.00 168.69 ? 264  MET B CG    1 
ATOM   7614  S  SD    . MET B 1 264 ? 195.888 120.064 154.663 1.00 194.81 ? 264  MET B SD    1 
ATOM   7615  C  CE    . MET B 1 264 ? 197.525 120.306 153.979 1.00 182.43 ? 264  MET B CE    1 
ATOM   7616  N  N     . PRO B 1 265 ? 195.507 124.657 155.994 1.00 166.58 ? 265  PRO B N     1 
ATOM   7617  C  CA    . PRO B 1 265 ? 196.137 125.951 156.262 1.00 166.72 ? 265  PRO B CA    1 
ATOM   7618  C  C     . PRO B 1 265 ? 197.416 126.136 155.457 1.00 172.48 ? 265  PRO B C     1 
ATOM   7619  O  O     . PRO B 1 265 ? 197.941 125.209 154.838 1.00 172.44 ? 265  PRO B O     1 
ATOM   7620  C  CB    . PRO B 1 265 ? 196.459 125.878 157.761 1.00 165.78 ? 265  PRO B CB    1 
ATOM   7621  C  CG    . PRO B 1 265 ? 195.497 124.889 158.309 1.00 163.89 ? 265  PRO B CG    1 
ATOM   7622  C  CD    . PRO B 1 265 ? 195.342 123.863 157.223 1.00 165.66 ? 265  PRO B CD    1 
ATOM   7623  N  N     . GLY B 1 266 ? 197.913 127.369 155.485 1.00 174.55 ? 266  GLY B N     1 
ATOM   7624  C  CA    . GLY B 1 266 ? 199.204 127.672 154.884 1.00 177.84 ? 266  GLY B CA    1 
ATOM   7625  C  C     . GLY B 1 266 ? 199.275 127.458 153.388 1.00 177.36 ? 266  GLY B C     1 
ATOM   7626  O  O     . GLY B 1 266 ? 200.281 126.944 152.885 1.00 177.61 ? 266  GLY B O     1 
ATOM   7627  N  N     . ASP B 1 267 ? 198.226 127.836 152.662 1.00 176.48 ? 267  ASP B N     1 
ATOM   7628  C  CA    . ASP B 1 267 ? 198.226 127.771 151.209 1.00 175.30 ? 267  ASP B CA    1 
ATOM   7629  C  C     . ASP B 1 267 ? 197.514 128.987 150.634 1.00 174.30 ? 267  ASP B C     1 
ATOM   7630  O  O     . ASP B 1 267 ? 196.783 129.692 151.336 1.00 169.74 ? 267  ASP B O     1 
ATOM   7631  C  CB    . ASP B 1 267 ? 197.578 126.472 150.698 1.00 172.20 ? 267  ASP B CB    1 
ATOM   7632  C  CG    . ASP B 1 267 ? 196.075 126.458 150.867 1.00 170.97 ? 267  ASP B CG    1 
ATOM   7633  O  OD1   . ASP B 1 267 ? 195.565 127.177 151.750 1.00 173.60 ? 267  ASP B OD1   1 
ATOM   7634  O  OD2   . ASP B 1 267 ? 195.401 125.727 150.112 1.00 167.51 ? 267  ASP B OD2   1 
ATOM   7635  N  N     . GLU B 1 268 ? 197.746 129.226 149.342 1.00 177.30 ? 268  GLU B N     1 
ATOM   7636  C  CA    . GLU B 1 268 ? 197.224 130.427 148.698 1.00 177.15 ? 268  GLU B CA    1 
ATOM   7637  C  C     . GLU B 1 268 ? 195.708 130.374 148.548 1.00 168.87 ? 268  GLU B C     1 
ATOM   7638  O  O     . GLU B 1 268 ? 195.018 131.375 148.774 1.00 164.75 ? 268  GLU B O     1 
ATOM   7639  C  CB    . GLU B 1 268 ? 197.890 130.609 147.334 1.00 184.64 ? 268  GLU B CB    1 
ATOM   7640  C  CG    . GLU B 1 268 ? 199.409 130.528 147.371 1.00 188.69 ? 268  GLU B CG    1 
ATOM   7641  C  CD    . GLU B 1 268 ? 200.020 130.357 145.993 1.00 196.12 ? 268  GLU B CD    1 
ATOM   7642  O  OE1   . GLU B 1 268 ? 199.258 130.286 145.007 1.00 195.18 ? 268  GLU B OE1   1 
ATOM   7643  O  OE2   . GLU B 1 268 ? 201.264 130.290 145.897 1.00 200.13 ? 268  GLU B OE2   1 
ATOM   7644  N  N     . LYS B 1 269 ? 195.170 129.215 148.164 1.00 167.26 ? 269  LYS B N     1 
ATOM   7645  C  CA    . LYS B 1 269 ? 193.778 129.142 147.733 1.00 163.45 ? 269  LYS B CA    1 
ATOM   7646  C  C     . LYS B 1 269 ? 192.786 129.217 148.888 1.00 158.95 ? 269  LYS B C     1 
ATOM   7647  O  O     . LYS B 1 269 ? 191.744 129.868 148.756 1.00 148.80 ? 269  LYS B O     1 
ATOM   7648  C  CB    . LYS B 1 269 ? 193.549 127.855 146.938 1.00 162.01 ? 269  LYS B CB    1 
ATOM   7649  C  CG    . LYS B 1 269 ? 192.185 127.755 146.271 1.00 156.88 ? 269  LYS B CG    1 
ATOM   7650  C  CD    . LYS B 1 269 ? 191.906 128.942 145.357 1.00 157.48 ? 269  LYS B CD    1 
ATOM   7651  C  CE    . LYS B 1 269 ? 192.994 129.113 144.302 1.00 161.12 ? 269  LYS B CE    1 
ATOM   7652  N  NZ    . LYS B 1 269 ? 193.115 127.918 143.420 1.00 159.95 ? 269  LYS B NZ    1 
ATOM   7653  N  N     . SER B 1 270 ? 193.077 128.571 150.014 1.00 163.79 ? 270  SER B N     1 
ATOM   7654  C  CA    . SER B 1 270 ? 192.084 128.441 151.072 1.00 156.99 ? 270  SER B CA    1 
ATOM   7655  C  C     . SER B 1 270 ? 191.928 129.742 151.850 1.00 151.25 ? 270  SER B C     1 
ATOM   7656  O  O     . SER B 1 270 ? 192.757 130.651 151.765 1.00 151.78 ? 270  SER B O     1 
ATOM   7657  C  CB    . SER B 1 270 ? 192.465 127.311 152.028 1.00 160.43 ? 270  SER B CB    1 
ATOM   7658  O  OG    . SER B 1 270 ? 192.654 126.093 151.330 1.00 165.92 ? 270  SER B OG    1 
ATOM   7659  N  N     . LEU B 1 271 ? 190.844 129.820 152.617 1.00 147.43 ? 271  LEU B N     1 
ATOM   7660  C  CA    . LEU B 1 271 ? 190.570 130.991 153.435 1.00 148.94 ? 271  LEU B CA    1 
ATOM   7661  C  C     . LEU B 1 271 ? 191.540 131.072 154.606 1.00 155.12 ? 271  LEU B C     1 
ATOM   7662  O  O     . LEU B 1 271 ? 192.117 130.070 155.036 1.00 161.92 ? 271  LEU B O     1 
ATOM   7663  C  CB    . LEU B 1 271 ? 189.136 130.964 153.964 1.00 138.60 ? 271  LEU B CB    1 
ATOM   7664  C  CG    . LEU B 1 271 ? 188.006 130.893 152.941 1.00 130.75 ? 271  LEU B CG    1 
ATOM   7665  C  CD1   . LEU B 1 271 ? 186.664 131.078 153.621 1.00 112.57 ? 271  LEU B CD1   1 
ATOM   7666  C  CD2   . LEU B 1 271 ? 188.209 131.947 151.872 1.00 132.00 ? 271  LEU B CD2   1 
ATOM   7667  N  N     . THR B 1 272 ? 191.718 132.287 155.114 1.00 155.77 ? 272  THR B N     1 
ATOM   7668  C  CA    . THR B 1 272 ? 192.521 132.538 156.299 1.00 158.18 ? 272  THR B CA    1 
ATOM   7669  C  C     . THR B 1 272 ? 191.756 133.466 157.229 1.00 149.19 ? 272  THR B C     1 
ATOM   7670  O  O     . THR B 1 272 ? 190.997 134.330 156.782 1.00 144.99 ? 272  THR B O     1 
ATOM   7671  C  CB    . THR B 1 272 ? 193.887 133.161 155.952 1.00 164.92 ? 272  THR B CB    1 
ATOM   7672  O  OG1   . THR B 1 272 ? 193.692 134.361 155.193 1.00 163.64 ? 272  THR B OG1   1 
ATOM   7673  C  CG2   . THR B 1 272 ? 194.738 132.187 155.146 1.00 165.81 ? 272  THR B CG2   1 
ATOM   7674  N  N     . GLY B 1 273 ? 191.954 133.274 158.529 1.00 145.84 ? 273  GLY B N     1 
ATOM   7675  C  CA    . GLY B 1 273 ? 191.348 134.154 159.507 1.00 144.18 ? 273  GLY B CA    1 
ATOM   7676  C  C     . GLY B 1 273 ? 190.271 133.518 160.361 1.00 139.65 ? 273  GLY B C     1 
ATOM   7677  O  O     . GLY B 1 273 ? 190.466 132.438 160.927 1.00 138.87 ? 273  GLY B O     1 
ATOM   7678  N  N     . ALA B 1 274 ? 189.121 134.189 160.456 1.00 134.53 ? 274  ALA B N     1 
ATOM   7679  C  CA    . ALA B 1 274 ? 188.075 133.777 161.384 1.00 129.68 ? 274  ALA B CA    1 
ATOM   7680  C  C     . ALA B 1 274 ? 187.367 132.500 160.956 1.00 126.67 ? 274  ALA B C     1 
ATOM   7681  O  O     . ALA B 1 274 ? 186.593 131.947 161.744 1.00 121.29 ? 274  ALA B O     1 
ATOM   7682  C  CB    . ALA B 1 274 ? 187.050 134.900 161.547 1.00 128.56 ? 274  ALA B CB    1 
ATOM   7683  N  N     . PHE B 1 275 ? 187.600 132.022 159.734 1.00 127.42 ? 275  PHE B N     1 
ATOM   7684  C  CA    . PHE B 1 275 ? 186.920 130.841 159.216 1.00 124.10 ? 275  PHE B CA    1 
ATOM   7685  C  C     . PHE B 1 275 ? 187.858 129.647 159.076 1.00 127.29 ? 275  PHE B C     1 
ATOM   7686  O  O     . PHE B 1 275 ? 187.645 128.785 158.218 1.00 123.09 ? 275  PHE B O     1 
ATOM   7687  C  CB    . PHE B 1 275 ? 186.258 131.166 157.879 1.00 118.27 ? 275  PHE B CB    1 
ATOM   7688  C  CG    . PHE B 1 275 ? 185.058 132.057 158.005 1.00 117.73 ? 275  PHE B CG    1 
ATOM   7689  C  CD1   . PHE B 1 275 ? 183.866 131.572 158.509 1.00 120.71 ? 275  PHE B CD1   1 
ATOM   7690  C  CD2   . PHE B 1 275 ? 185.127 133.389 157.634 1.00 116.03 ? 275  PHE B CD2   1 
ATOM   7691  C  CE1   . PHE B 1 275 ? 182.764 132.395 158.631 1.00 117.88 ? 275  PHE B CE1   1 
ATOM   7692  C  CE2   . PHE B 1 275 ? 184.028 134.215 157.753 1.00 109.21 ? 275  PHE B CE2   1 
ATOM   7693  C  CZ    . PHE B 1 275 ? 182.846 133.718 158.252 1.00 107.69 ? 275  PHE B CZ    1 
ATOM   7694  N  N     . ALA B 1 276 ? 188.895 129.581 159.905 1.00 131.58 ? 276  ALA B N     1 
ATOM   7695  C  CA    . ALA B 1 276 ? 189.855 128.486 159.858 1.00 130.90 ? 276  ALA B CA    1 
ATOM   7696  C  C     . ALA B 1 276 ? 189.257 127.251 160.529 1.00 130.85 ? 276  ALA B C     1 
ATOM   7697  O  O     . ALA B 1 276 ? 188.104 127.244 160.968 1.00 128.77 ? 276  ALA B O     1 
ATOM   7698  C  CB    . ALA B 1 276 ? 191.172 128.910 160.502 1.00 135.60 ? 276  ALA B CB    1 
ATOM   7699  N  N     . GLY B 1 277 ? 190.046 126.183 160.619 1.00 132.41 ? 277  GLY B N     1 
ATOM   7700  C  CA    . GLY B 1 277 ? 189.555 124.934 161.152 1.00 134.60 ? 277  GLY B CA    1 
ATOM   7701  C  C     . GLY B 1 277 ? 189.497 124.893 162.669 1.00 133.77 ? 277  GLY B C     1 
ATOM   7702  O  O     . GLY B 1 277 ? 190.065 125.739 163.357 1.00 129.81 ? 277  GLY B O     1 
ATOM   7703  N  N     . ASP B 1 278 ? 188.762 123.896 163.168 1.00 133.25 ? 278  ASP B N     1 
ATOM   7704  C  CA    . ASP B 1 278 ? 188.676 123.559 164.586 1.00 133.64 ? 278  ASP B CA    1 
ATOM   7705  C  C     . ASP B 1 278 ? 187.936 124.619 165.394 1.00 135.65 ? 278  ASP B C     1 
ATOM   7706  O  O     . ASP B 1 278 ? 187.755 124.460 166.605 1.00 141.04 ? 278  ASP B O     1 
ATOM   7707  C  CB    . ASP B 1 278 ? 190.074 123.326 165.171 1.00 137.84 ? 278  ASP B CB    1 
ATOM   7708  C  CG    . ASP B 1 278 ? 190.826 122.215 164.465 1.00 144.73 ? 278  ASP B CG    1 
ATOM   7709  O  OD1   . ASP B 1 278 ? 190.179 121.231 164.047 1.00 144.77 ? 278  ASP B OD1   1 
ATOM   7710  O  OD2   . ASP B 1 278 ? 192.062 122.322 164.329 1.00 145.88 ? 278  ASP B OD2   1 
ATOM   7711  N  N     . ASP B 1 279 ? 187.504 125.703 164.743 1.00 131.92 ? 279  ASP B N     1 
ATOM   7712  C  CA    . ASP B 1 279 ? 186.789 126.763 165.443 1.00 127.58 ? 279  ASP B CA    1 
ATOM   7713  C  C     . ASP B 1 279 ? 185.753 127.465 164.572 1.00 123.54 ? 279  ASP B C     1 
ATOM   7714  O  O     . ASP B 1 279 ? 185.201 128.485 165.002 1.00 121.00 ? 279  ASP B O     1 
ATOM   7715  C  CB    . ASP B 1 279 ? 187.775 127.797 165.999 1.00 130.06 ? 279  ASP B CB    1 
ATOM   7716  C  CG    . ASP B 1 279 ? 188.367 127.380 167.329 1.00 136.69 ? 279  ASP B CG    1 
ATOM   7717  O  OD1   . ASP B 1 279 ? 187.620 126.836 168.168 1.00 138.65 ? 279  ASP B OD1   1 
ATOM   7718  O  OD2   . ASP B 1 279 ? 189.581 127.591 167.535 1.00 138.40 ? 279  ASP B OD2   1 
ATOM   7719  N  N     . VAL B 1 280 ? 185.479 126.968 163.365 1.00 124.91 ? 280  VAL B N     1 
ATOM   7720  C  CA    . VAL B 1 280 ? 184.578 127.675 162.459 1.00 117.44 ? 280  VAL B CA    1 
ATOM   7721  C  C     . VAL B 1 280 ? 183.140 127.606 162.959 1.00 115.11 ? 280  VAL B C     1 
ATOM   7722  O  O     . VAL B 1 280 ? 182.344 128.522 162.723 1.00 114.83 ? 280  VAL B O     1 
ATOM   7723  C  CB    . VAL B 1 280 ? 184.711 127.117 161.031 1.00 115.66 ? 280  VAL B CB    1 
ATOM   7724  C  CG1   . VAL B 1 280 ? 184.391 125.634 161.003 1.00 117.97 ? 280  VAL B CG1   1 
ATOM   7725  C  CG2   . VAL B 1 280 ? 183.810 127.879 160.076 1.00 113.76 ? 280  VAL B CG2   1 
ATOM   7726  N  N     . TRP B 1 281 ? 182.783 126.530 163.662 1.00 116.65 ? 281  TRP B N     1 
ATOM   7727  C  CA    . TRP B 1 281 ? 181.401 126.344 164.089 1.00 115.01 ? 281  TRP B CA    1 
ATOM   7728  C  C     . TRP B 1 281 ? 180.954 127.394 165.097 1.00 116.79 ? 281  TRP B C     1 
ATOM   7729  O  O     . TRP B 1 281 ? 179.750 127.635 165.229 1.00 114.10 ? 281  TRP B O     1 
ATOM   7730  C  CB    . TRP B 1 281 ? 181.220 124.939 164.666 1.00 115.29 ? 281  TRP B CB    1 
ATOM   7731  C  CG    . TRP B 1 281 ? 181.842 124.741 166.013 1.00 119.53 ? 281  TRP B CG    1 
ATOM   7732  C  CD1   . TRP B 1 281 ? 183.092 124.266 166.275 1.00 123.88 ? 281  TRP B CD1   1 
ATOM   7733  C  CD2   . TRP B 1 281 ? 181.234 124.991 167.285 1.00 119.13 ? 281  TRP B CD2   1 
ATOM   7734  N  NE1   . TRP B 1 281 ? 183.306 124.216 167.630 1.00 128.73 ? 281  TRP B NE1   1 
ATOM   7735  C  CE2   . TRP B 1 281 ? 182.179 124.655 168.272 1.00 124.36 ? 281  TRP B CE2   1 
ATOM   7736  C  CE3   . TRP B 1 281 ? 179.984 125.471 167.684 1.00 117.88 ? 281  TRP B CE3   1 
ATOM   7737  C  CZ2   . TRP B 1 281 ? 181.914 124.785 169.631 1.00 127.82 ? 281  TRP B CZ2   1 
ATOM   7738  C  CZ3   . TRP B 1 281 ? 179.724 125.599 169.033 1.00 121.38 ? 281  TRP B CZ3   1 
ATOM   7739  C  CH2   . TRP B 1 281 ? 180.683 125.257 169.990 1.00 126.76 ? 281  TRP B CH2   1 
ATOM   7740  N  N     . GLN B 1 282 ? 181.889 128.020 165.811 1.00 117.43 ? 282  GLN B N     1 
ATOM   7741  C  CA    . GLN B 1 282 ? 181.548 129.059 166.773 1.00 114.49 ? 282  GLN B CA    1 
ATOM   7742  C  C     . GLN B 1 282 ? 181.211 130.393 166.123 1.00 110.07 ? 282  GLN B C     1 
ATOM   7743  O  O     . GLN B 1 282 ? 180.422 131.155 166.691 1.00 111.26 ? 282  GLN B O     1 
ATOM   7744  C  CB    . GLN B 1 282 ? 182.698 129.263 167.762 1.00 117.36 ? 282  GLN B CB    1 
ATOM   7745  C  CG    . GLN B 1 282 ? 183.026 128.045 168.602 1.00 121.89 ? 282  GLN B CG    1 
ATOM   7746  C  CD    . GLN B 1 282 ? 184.112 128.322 169.618 1.00 128.14 ? 282  GLN B CD    1 
ATOM   7747  O  OE1   . GLN B 1 282 ? 184.503 129.469 169.827 1.00 131.30 ? 282  GLN B OE1   1 
ATOM   7748  N  NE2   . GLN B 1 282 ? 184.608 127.269 170.257 1.00 129.28 ? 282  GLN B NE2   1 
ATOM   7749  N  N     . ASN B 1 283 ? 181.779 130.693 164.957 1.00 107.91 ? 283  ASN B N     1 
ATOM   7750  C  CA    . ASN B 1 283 ? 181.647 132.003 164.336 1.00 103.92 ? 283  ASN B CA    1 
ATOM   7751  C  C     . ASN B 1 283 ? 180.468 132.093 163.378 1.00 98.89  ? 283  ASN B C     1 
ATOM   7752  O  O     . ASN B 1 283 ? 180.283 133.134 162.742 1.00 103.48 ? 283  ASN B O     1 
ATOM   7753  C  CB    . ASN B 1 283 ? 182.937 132.366 163.599 1.00 109.75 ? 283  ASN B CB    1 
ATOM   7754  C  CG    . ASN B 1 283 ? 184.055 132.756 164.540 1.00 119.44 ? 283  ASN B CG    1 
ATOM   7755  O  OD1   . ASN B 1 283 ? 183.847 133.504 165.494 1.00 118.70 ? 283  ASN B OD1   1 
ATOM   7756  N  ND2   . ASN B 1 283 ? 185.253 132.250 164.275 1.00 123.32 ? 283  ASN B ND2   1 
ATOM   7757  N  N     . VAL B 1 284 ? 179.670 131.037 163.258 1.00 96.07  ? 284  VAL B N     1 
ATOM   7758  C  CA    . VAL B 1 284 ? 178.521 131.012 162.362 1.00 94.06  ? 284  VAL B CA    1 
ATOM   7759  C  C     . VAL B 1 284 ? 177.280 130.692 163.178 1.00 93.12  ? 284  VAL B C     1 
ATOM   7760  O  O     . VAL B 1 284 ? 177.243 129.681 163.888 1.00 103.99 ? 284  VAL B O     1 
ATOM   7761  C  CB    . VAL B 1 284 ? 178.703 129.987 161.229 1.00 95.00  ? 284  VAL B CB    1 
ATOM   7762  C  CG1   . VAL B 1 284 ? 177.439 129.891 160.398 1.00 88.65  ? 284  VAL B CG1   1 
ATOM   7763  C  CG2   . VAL B 1 284 ? 179.889 130.365 160.359 1.00 102.08 ? 284  VAL B CG2   1 
ATOM   7764  N  N     . LEU B 1 285 ? 176.265 131.544 163.070 1.00 90.29  ? 285  LEU B N     1 
ATOM   7765  C  CA    . LEU B 1 285 ? 174.999 131.354 163.761 1.00 90.33  ? 285  LEU B CA    1 
ATOM   7766  C  C     . LEU B 1 285 ? 173.895 131.166 162.735 1.00 88.77  ? 285  LEU B C     1 
ATOM   7767  O  O     . LEU B 1 285 ? 173.771 131.953 161.793 1.00 95.31  ? 285  LEU B O     1 
ATOM   7768  C  CB    . LEU B 1 285 ? 174.685 132.545 164.684 1.00 93.34  ? 285  LEU B CB    1 
ATOM   7769  C  CG    . LEU B 1 285 ? 173.317 132.673 165.368 1.00 92.74  ? 285  LEU B CG    1 
ATOM   7770  C  CD1   . LEU B 1 285 ? 173.461 133.485 166.635 1.00 94.70  ? 285  LEU B CD1   1 
ATOM   7771  C  CD2   . LEU B 1 285 ? 172.281 133.335 164.477 1.00 94.98  ? 285  LEU B CD2   1 
ATOM   7772  N  N     . VAL B 1 286 ? 173.091 130.126 162.923 1.00 90.04  ? 286  VAL B N     1 
ATOM   7773  C  CA    . VAL B 1 286 ? 171.979 129.811 162.036 1.00 88.73  ? 286  VAL B CA    1 
ATOM   7774  C  C     . VAL B 1 286 ? 170.694 130.185 162.752 1.00 87.63  ? 286  VAL B C     1 
ATOM   7775  O  O     . VAL B 1 286 ? 170.358 129.592 163.784 1.00 92.83  ? 286  VAL B O     1 
ATOM   7776  C  CB    . VAL B 1 286 ? 171.972 128.331 161.633 1.00 91.45  ? 286  VAL B CB    1 
ATOM   7777  C  CG1   . VAL B 1 286 ? 170.737 128.020 160.824 1.00 90.15  ? 286  VAL B CG1   1 
ATOM   7778  C  CG2   . VAL B 1 286 ? 173.220 128.005 160.839 1.00 98.28  ? 286  VAL B CG2   1 
ATOM   7779  N  N     . CYS B 1 287 ? 169.971 131.154 162.204 1.00 85.40  ? 287  CYS B N     1 
ATOM   7780  C  CA    . CYS B 1 287 ? 168.792 131.714 162.848 1.00 84.62  ? 287  CYS B CA    1 
ATOM   7781  C  C     . CYS B 1 287 ? 167.548 131.263 162.096 1.00 85.88  ? 287  CYS B C     1 
ATOM   7782  O  O     . CYS B 1 287 ? 167.346 131.646 160.941 1.00 87.98  ? 287  CYS B O     1 
ATOM   7783  C  CB    . CYS B 1 287 ? 168.881 133.238 162.894 1.00 85.25  ? 287  CYS B CB    1 
ATOM   7784  S  SG    . CYS B 1 287 ? 167.298 134.072 162.983 1.00 107.12 ? 287  CYS B SG    1 
ATOM   7785  N  N     . ILE B 1 288 ? 166.716 130.460 162.752 1.00 87.60  ? 288  ILE B N     1 
ATOM   7786  C  CA    . ILE B 1 288 ? 165.501 129.915 162.158 1.00 85.96  ? 288  ILE B CA    1 
ATOM   7787  C  C     . ILE B 1 288 ? 164.340 130.786 162.608 1.00 88.90  ? 288  ILE B C     1 
ATOM   7788  O  O     . ILE B 1 288 ? 164.007 130.824 163.797 1.00 96.31  ? 288  ILE B O     1 
ATOM   7789  C  CB    . ILE B 1 288 ? 165.275 128.452 162.559 1.00 83.93  ? 288  ILE B CB    1 
ATOM   7790  C  CG1   . ILE B 1 288 ? 166.509 127.610 162.242 1.00 90.81  ? 288  ILE B CG1   1 
ATOM   7791  C  CG2   . ILE B 1 288 ? 164.051 127.895 161.860 1.00 82.61  ? 288  ILE B CG2   1 
ATOM   7792  C  CD1   . ILE B 1 288 ? 166.372 126.163 162.642 1.00 92.68  ? 288  ILE B CD1   1 
ATOM   7793  N  N     . VAL B 1 289 ? 163.716 131.484 161.669 1.00 89.49  ? 289  VAL B N     1 
ATOM   7794  C  CA    . VAL B 1 289 ? 162.599 132.371 161.968 1.00 92.14  ? 289  VAL B CA    1 
ATOM   7795  C  C     . VAL B 1 289 ? 161.338 131.707 161.433 1.00 94.53  ? 289  VAL B C     1 
ATOM   7796  O  O     . VAL B 1 289 ? 161.175 131.544 160.219 1.00 100.60 ? 289  VAL B O     1 
ATOM   7797  C  CB    . VAL B 1 289 ? 162.791 133.766 161.367 1.00 93.71  ? 289  VAL B CB    1 
ATOM   7798  C  CG1   . VAL B 1 289 ? 161.551 134.600 161.590 1.00 93.25  ? 289  VAL B CG1   1 
ATOM   7799  C  CG2   . VAL B 1 289 ? 163.991 134.444 161.982 1.00 91.67  ? 289  VAL B CG2   1 
ATOM   7800  N  N     . ALA B 1 290 ? 160.439 131.324 162.332 1.00 94.91  ? 290  ALA B N     1 
ATOM   7801  C  CA    . ALA B 1 290 ? 159.147 130.812 161.914 1.00 95.40  ? 290  ALA B CA    1 
ATOM   7802  C  C     . ALA B 1 290 ? 158.224 131.967 161.548 1.00 103.17 ? 290  ALA B C     1 
ATOM   7803  O  O     . ALA B 1 290 ? 158.580 133.141 161.665 1.00 114.70 ? 290  ALA B O     1 
ATOM   7804  C  CB    . ALA B 1 290 ? 158.518 129.958 163.012 1.00 99.41  ? 290  ALA B CB    1 
ATOM   7805  N  N     . ASP B 1 291 ? 157.022 131.623 161.093 1.00 103.46 ? 291  ASP B N     1 
ATOM   7806  C  CA    . ASP B 1 291 ? 156.061 132.636 160.680 1.00 113.27 ? 291  ASP B CA    1 
ATOM   7807  C  C     . ASP B 1 291 ? 154.817 132.685 161.551 1.00 116.84 ? 291  ASP B C     1 
ATOM   7808  O  O     . ASP B 1 291 ? 154.211 133.753 161.682 1.00 122.67 ? 291  ASP B O     1 
ATOM   7809  C  CB    . ASP B 1 291 ? 155.637 132.410 159.227 1.00 118.62 ? 291  ASP B CB    1 
ATOM   7810  C  CG    . ASP B 1 291 ? 155.316 133.702 158.511 1.00 122.22 ? 291  ASP B CG    1 
ATOM   7811  O  OD1   . ASP B 1 291 ? 155.022 134.702 159.194 1.00 119.16 ? 291  ASP B OD1   1 
ATOM   7812  O  OD2   . ASP B 1 291 ? 155.349 133.719 157.264 1.00 126.52 ? 291  ASP B OD2   1 
ATOM   7813  N  N     . GLY B 1 292 ? 154.415 131.568 162.142 1.00 115.64 ? 292  GLY B N     1 
ATOM   7814  C  CA    . GLY B 1 292 ? 153.256 131.579 163.008 1.00 121.57 ? 292  GLY B CA    1 
ATOM   7815  C  C     . GLY B 1 292 ? 153.135 130.333 163.854 1.00 129.19 ? 292  GLY B C     1 
ATOM   7816  O  O     . GLY B 1 292 ? 153.227 129.217 163.338 1.00 133.77 ? 292  GLY B O     1 
ATOM   7817  N  N     . ARG B 1 293 ? 152.917 130.509 165.158 1.00 126.40 ? 293  ARG B N     1 
ATOM   7818  C  CA    . ARG B 1 293 ? 152.725 129.364 166.038 1.00 126.07 ? 293  ARG B CA    1 
ATOM   7819  C  C     . ARG B 1 293 ? 151.485 128.565 165.667 1.00 135.51 ? 293  ARG B C     1 
ATOM   7820  O  O     . ARG B 1 293 ? 151.372 127.398 166.055 1.00 142.05 ? 293  ARG B O     1 
ATOM   7821  C  CB    . ARG B 1 293 ? 152.635 129.833 167.490 1.00 124.56 ? 293  ARG B CB    1 
ATOM   7822  C  CG    . ARG B 1 293 ? 152.926 128.757 168.515 1.00 128.66 ? 293  ARG B CG    1 
ATOM   7823  C  CD    . ARG B 1 293 ? 153.100 129.360 169.894 1.00 130.44 ? 293  ARG B CD    1 
ATOM   7824  N  NE    . ARG B 1 293 ? 151.823 129.725 170.493 1.00 133.02 ? 293  ARG B NE    1 
ATOM   7825  C  CZ    . ARG B 1 293 ? 151.144 128.954 171.330 1.00 133.47 ? 293  ARG B CZ    1 
ATOM   7826  N  NH1   . ARG B 1 293 ? 151.589 127.760 171.685 1.00 130.52 ? 293  ARG B NH1   1 
ATOM   7827  N  NH2   . ARG B 1 293 ? 149.991 129.393 171.825 1.00 136.30 ? 293  ARG B NH2   1 
ATOM   7828  N  N     . GLU B 1 294 ? 150.566 129.167 164.917 1.00 136.62 ? 294  GLU B N     1 
ATOM   7829  C  CA    . GLU B 1 294 ? 149.325 128.522 164.520 1.00 141.32 ? 294  GLU B CA    1 
ATOM   7830  C  C     . GLU B 1 294 ? 149.429 127.770 163.200 1.00 142.44 ? 294  GLU B C     1 
ATOM   7831  O  O     . GLU B 1 294 ? 148.485 127.059 162.840 1.00 146.28 ? 294  GLU B O     1 
ATOM   7832  C  CB    . GLU B 1 294 ? 148.221 129.574 164.423 1.00 147.45 ? 294  GLU B CB    1 
ATOM   7833  C  CG    . GLU B 1 294 ? 148.174 130.283 163.082 1.00 148.73 ? 294  GLU B CG    1 
ATOM   7834  C  CD    . GLU B 1 294 ? 147.481 131.628 163.157 1.00 155.64 ? 294  GLU B CD    1 
ATOM   7835  O  OE1   . GLU B 1 294 ? 147.511 132.252 164.238 1.00 160.30 ? 294  GLU B OE1   1 
ATOM   7836  O  OE2   . GLU B 1 294 ? 146.910 132.061 162.135 1.00 154.21 ? 294  GLU B OE2   1 
ATOM   7837  N  N     . GLN B 1 295 ? 150.540 127.900 162.474 1.00 137.39 ? 295  GLN B N     1 
ATOM   7838  C  CA    . GLN B 1 295 ? 150.655 127.327 161.142 1.00 136.90 ? 295  GLN B CA    1 
ATOM   7839  C  C     . GLN B 1 295 ? 151.813 126.354 160.976 1.00 131.63 ? 295  GLN B C     1 
ATOM   7840  O  O     . GLN B 1 295 ? 151.836 125.619 159.984 1.00 136.90 ? 295  GLN B O     1 
ATOM   7841  C  CB    . GLN B 1 295 ? 150.790 128.442 160.098 1.00 135.17 ? 295  GLN B CB    1 
ATOM   7842  C  CG    . GLN B 1 295 ? 149.516 129.229 159.868 1.00 136.87 ? 295  GLN B CG    1 
ATOM   7843  C  CD    . GLN B 1 295 ? 148.501 128.460 159.047 1.00 144.59 ? 295  GLN B CD    1 
ATOM   7844  O  OE1   . GLN B 1 295 ? 148.836 127.479 158.385 1.00 143.37 ? 295  GLN B OE1   1 
ATOM   7845  N  NE2   . GLN B 1 295 ? 147.250 128.904 159.086 1.00 152.96 ? 295  GLN B NE2   1 
ATOM   7846  N  N     . VAL B 1 296 ? 152.773 126.330 161.900 1.00 125.42 ? 296  VAL B N     1 
ATOM   7847  C  CA    . VAL B 1 296 ? 153.880 125.387 161.795 1.00 124.47 ? 296  VAL B CA    1 
ATOM   7848  C  C     . VAL B 1 296 ? 153.353 123.964 161.905 1.00 129.59 ? 296  VAL B C     1 
ATOM   7849  O  O     . VAL B 1 296 ? 152.339 123.705 162.566 1.00 134.99 ? 296  VAL B O     1 
ATOM   7850  C  CB    . VAL B 1 296 ? 154.946 125.681 162.860 1.00 122.95 ? 296  VAL B CB    1 
ATOM   7851  C  CG1   . VAL B 1 296 ? 155.424 127.110 162.742 1.00 119.87 ? 296  VAL B CG1   1 
ATOM   7852  C  CG2   . VAL B 1 296 ? 154.374 125.451 164.241 1.00 126.28 ? 296  VAL B CG2   1 
ATOM   7853  N  N     . HIS B 1 297 ? 154.000 123.038 161.206 1.00 128.24 ? 297  HIS B N     1 
ATOM   7854  C  CA    . HIS B 1 297 ? 153.557 121.645 161.195 1.00 128.36 ? 297  HIS B CA    1 
ATOM   7855  C  C     . HIS B 1 297 ? 153.822 120.907 162.502 1.00 131.02 ? 297  HIS B C     1 
ATOM   7856  O  O     . HIS B 1 297 ? 154.940 120.933 163.017 1.00 131.88 ? 297  HIS B O     1 
ATOM   7857  C  CB    . HIS B 1 297 ? 154.205 120.890 160.031 1.00 130.04 ? 297  HIS B CB    1 
ATOM   7858  C  CG    . HIS B 1 297 ? 153.340 119.815 159.452 1.00 131.33 ? 297  HIS B CG    1 
ATOM   7859  N  ND1   . HIS B 1 297 ? 153.288 118.540 159.974 1.00 135.08 ? 297  HIS B ND1   1 
ATOM   7860  C  CD2   . HIS B 1 297 ? 152.492 119.824 158.397 1.00 129.31 ? 297  HIS B CD2   1 
ATOM   7861  C  CE1   . HIS B 1 297 ? 152.445 117.810 159.265 1.00 134.60 ? 297  HIS B CE1   1 
ATOM   7862  N  NE2   . HIS B 1 297 ? 151.948 118.566 158.302 1.00 131.67 ? 297  HIS B NE2   1 
ATOM   7863  N  N     . PRO B 1 298 ? 152.789 120.242 163.046 1.00 129.10 ? 298  PRO B N     1 
ATOM   7864  C  CA    . PRO B 1 298 ? 153.014 119.498 164.296 1.00 132.18 ? 298  PRO B CA    1 
ATOM   7865  C  C     . PRO B 1 298 ? 154.177 118.527 164.209 1.00 133.40 ? 298  PRO B C     1 
ATOM   7866  O  O     . PRO B 1 298 ? 154.905 118.346 165.192 1.00 135.84 ? 298  PRO B O     1 
ATOM   7867  C  CB    . PRO B 1 298 ? 151.679 118.776 164.513 1.00 130.78 ? 298  PRO B CB    1 
ATOM   7868  C  CG    . PRO B 1 298 ? 150.680 119.620 163.800 1.00 126.57 ? 298  PRO B CG    1 
ATOM   7869  C  CD    . PRO B 1 298 ? 151.390 120.164 162.597 1.00 123.74 ? 298  PRO B CD    1 
ATOM   7870  N  N     . LYS B 1 299 ? 154.381 117.899 163.050 1.00 130.17 ? 299  LYS B N     1 
ATOM   7871  C  CA    . LYS B 1 299 ? 155.563 117.062 162.878 1.00 130.61 ? 299  LYS B CA    1 
ATOM   7872  C  C     . LYS B 1 299 ? 156.838 117.892 162.911 1.00 128.87 ? 299  LYS B C     1 
ATOM   7873  O  O     . LYS B 1 299 ? 157.867 117.429 163.417 1.00 130.00 ? 299  LYS B O     1 
ATOM   7874  C  CB    . LYS B 1 299 ? 155.467 116.267 161.576 1.00 133.23 ? 299  LYS B CB    1 
ATOM   7875  C  CG    . LYS B 1 299 ? 154.133 115.573 161.353 1.00 138.31 ? 299  LYS B CG    1 
ATOM   7876  C  CD    . LYS B 1 299 ? 153.696 114.799 162.588 1.00 140.61 ? 299  LYS B CD    1 
ATOM   7877  C  CE    . LYS B 1 299 ? 152.521 113.888 162.281 1.00 147.08 ? 299  LYS B CE    1 
ATOM   7878  N  NZ    . LYS B 1 299 ? 152.698 113.180 160.984 1.00 146.17 ? 299  LYS B NZ    1 
ATOM   7879  N  N     . THR B 1 300 ? 156.740 119.135 162.452 1.00 126.13 ? 300  THR B N     1 
ATOM   7880  C  CA    . THR B 1 300 ? 157.871 120.049 162.476 1.00 127.48 ? 300  THR B CA    1 
ATOM   7881  C  C     . THR B 1 300 ? 158.233 120.338 163.932 1.00 127.14 ? 300  THR B C     1 
ATOM   7882  O  O     . THR B 1 300 ? 159.409 120.334 164.298 1.00 128.11 ? 300  THR B O     1 
ATOM   7883  C  CB    . THR B 1 300 ? 157.548 121.372 161.758 1.00 123.81 ? 300  THR B CB    1 
ATOM   7884  O  OG1   . THR B 1 300 ? 158.705 121.826 161.044 1.00 128.33 ? 300  THR B OG1   1 
ATOM   7885  C  CG2   . THR B 1 300 ? 157.128 122.434 162.763 1.00 118.96 ? 300  THR B CG2   1 
ATOM   7886  N  N     . LEU B 1 301 ? 157.219 120.588 164.759 1.00 124.88 ? 301  LEU B N     1 
ATOM   7887  C  CA    . LEU B 1 301 ? 157.445 120.855 166.177 1.00 125.50 ? 301  LEU B CA    1 
ATOM   7888  C  C     . LEU B 1 301 ? 157.966 119.618 166.898 1.00 127.04 ? 301  LEU B C     1 
ATOM   7889  O  O     . LEU B 1 301 ? 158.803 119.725 167.802 1.00 128.96 ? 301  LEU B O     1 
ATOM   7890  C  CB    . LEU B 1 301 ? 156.164 121.367 166.829 1.00 127.86 ? 301  LEU B CB    1 
ATOM   7891  C  CG    . LEU B 1 301 ? 155.672 122.716 166.308 1.00 125.98 ? 301  LEU B CG    1 
ATOM   7892  C  CD1   . LEU B 1 301 ? 154.811 123.401 167.347 1.00 124.53 ? 301  LEU B CD1   1 
ATOM   7893  C  CD2   . LEU B 1 301 ? 156.857 123.597 165.950 1.00 121.71 ? 301  LEU B CD2   1 
ATOM   7894  N  N     . ASP B 1 302 ? 157.479 118.436 166.520 1.00 126.45 ? 302  ASP B N     1 
ATOM   7895  C  CA    . ASP B 1 302 ? 158.017 117.208 167.095 1.00 127.55 ? 302  ASP B CA    1 
ATOM   7896  C  C     . ASP B 1 302 ? 159.495 117.053 166.763 1.00 127.91 ? 302  ASP B C     1 
ATOM   7897  O  O     . ASP B 1 302 ? 160.301 116.694 167.629 1.00 129.05 ? 302  ASP B O     1 
ATOM   7898  C  CB    . ASP B 1 302 ? 157.222 116.001 166.600 1.00 130.73 ? 302  ASP B CB    1 
ATOM   7899  C  CG    . ASP B 1 302 ? 155.793 116.003 167.099 1.00 137.02 ? 302  ASP B CG    1 
ATOM   7900  O  OD1   . ASP B 1 302 ? 155.412 116.961 167.802 1.00 139.51 ? 302  ASP B OD1   1 
ATOM   7901  O  OD2   . ASP B 1 302 ? 155.051 115.049 166.789 1.00 140.08 ? 302  ASP B OD2   1 
ATOM   7902  N  N     . TYR B 1 303 ? 159.874 117.335 165.515 1.00 124.05 ? 303  TYR B N     1 
ATOM   7903  C  CA    . TYR B 1 303 ? 161.286 117.296 165.146 1.00 119.74 ? 303  TYR B CA    1 
ATOM   7904  C  C     . TYR B 1 303 ? 162.093 118.315 165.938 1.00 119.84 ? 303  TYR B C     1 
ATOM   7905  O  O     . TYR B 1 303 ? 163.205 118.020 166.394 1.00 121.29 ? 303  TYR B O     1 
ATOM   7906  C  CB    . TYR B 1 303 ? 161.451 117.539 163.648 1.00 115.62 ? 303  TYR B CB    1 
ATOM   7907  C  CG    . TYR B 1 303 ? 162.893 117.592 163.206 1.00 114.36 ? 303  TYR B CG    1 
ATOM   7908  C  CD1   . TYR B 1 303 ? 163.693 116.461 163.243 1.00 117.62 ? 303  TYR B CD1   1 
ATOM   7909  C  CD2   . TYR B 1 303 ? 163.456 118.776 162.756 1.00 111.69 ? 303  TYR B CD2   1 
ATOM   7910  C  CE1   . TYR B 1 303 ? 165.013 116.506 162.843 1.00 118.60 ? 303  TYR B CE1   1 
ATOM   7911  C  CE2   . TYR B 1 303 ? 164.773 118.831 162.353 1.00 111.36 ? 303  TYR B CE2   1 
ATOM   7912  C  CZ    . TYR B 1 303 ? 165.547 117.694 162.399 1.00 117.57 ? 303  TYR B CZ    1 
ATOM   7913  O  OH    . TYR B 1 303 ? 166.861 117.743 161.998 1.00 119.90 ? 303  TYR B OH    1 
ATOM   7914  N  N     . LEU B 1 304 ? 161.553 119.524 166.105 1.00 118.60 ? 304  LEU B N     1 
ATOM   7915  C  CA    . LEU B 1 304 ? 162.275 120.567 166.824 1.00 117.92 ? 304  LEU B CA    1 
ATOM   7916  C  C     . LEU B 1 304 ? 162.485 120.182 168.282 1.00 120.06 ? 304  LEU B C     1 
ATOM   7917  O  O     . LEU B 1 304 ? 163.550 120.444 168.854 1.00 121.83 ? 304  LEU B O     1 
ATOM   7918  C  CB    . LEU B 1 304 ? 161.529 121.895 166.713 1.00 114.48 ? 304  LEU B CB    1 
ATOM   7919  C  CG    . LEU B 1 304 ? 161.556 122.536 165.324 1.00 111.50 ? 304  LEU B CG    1 
ATOM   7920  C  CD1   . LEU B 1 304 ? 160.704 123.790 165.288 1.00 109.74 ? 304  LEU B CD1   1 
ATOM   7921  C  CD2   . LEU B 1 304 ? 162.977 122.839 164.892 1.00 106.96 ? 304  LEU B CD2   1 
ATOM   7922  N  N     . GLU B 1 305 ? 161.482 119.560 168.904 1.00 119.94 ? 305  GLU B N     1 
ATOM   7923  C  CA    . GLU B 1 305 ? 161.677 119.025 170.246 1.00 120.62 ? 305  GLU B CA    1 
ATOM   7924  C  C     . GLU B 1 305 ? 162.696 117.895 170.246 1.00 122.14 ? 305  GLU B C     1 
ATOM   7925  O  O     . GLU B 1 305 ? 163.458 117.747 171.207 1.00 123.77 ? 305  GLU B O     1 
ATOM   7926  C  CB    . GLU B 1 305 ? 160.351 118.534 170.827 1.00 124.31 ? 305  GLU B CB    1 
ATOM   7927  C  CG    . GLU B 1 305 ? 159.331 119.626 171.079 1.00 128.40 ? 305  GLU B CG    1 
ATOM   7928  C  CD    . GLU B 1 305 ? 158.026 119.082 171.630 1.00 134.53 ? 305  GLU B CD    1 
ATOM   7929  O  OE1   . GLU B 1 305 ? 156.955 119.434 171.090 1.00 135.22 ? 305  GLU B OE1   1 
ATOM   7930  O  OE2   . GLU B 1 305 ? 158.070 118.304 172.605 1.00 136.25 ? 305  GLU B OE2   1 
ATOM   7931  N  N     . ALA B 1 306 ? 162.720 117.089 169.183 1.00 122.29 ? 306  ALA B N     1 
ATOM   7932  C  CA    . ALA B 1 306 ? 163.675 115.988 169.109 1.00 125.50 ? 306  ALA B CA    1 
ATOM   7933  C  C     . ALA B 1 306 ? 165.109 116.497 169.064 1.00 125.48 ? 306  ALA B C     1 
ATOM   7934  O  O     . ALA B 1 306 ? 165.997 115.923 169.704 1.00 133.59 ? 306  ALA B O     1 
ATOM   7935  C  CB    . ALA B 1 306 ? 163.377 115.116 167.891 1.00 126.26 ? 306  ALA B CB    1 
ATOM   7936  N  N     . ILE B 1 307 ? 165.358 117.573 168.318 1.00 119.28 ? 307  ILE B N     1 
ATOM   7937  C  CA    . ILE B 1 307 ? 166.713 118.107 168.208 1.00 117.07 ? 307  ILE B CA    1 
ATOM   7938  C  C     . ILE B 1 307 ? 166.995 118.999 169.409 1.00 118.17 ? 307  ILE B C     1 
ATOM   7939  O  O     . ILE B 1 307 ? 168.068 119.605 169.508 1.00 118.46 ? 307  ILE B O     1 
ATOM   7940  C  CB    . ILE B 1 307 ? 166.926 118.878 166.893 1.00 111.51 ? 307  ILE B CB    1 
ATOM   7941  C  CG1   . ILE B 1 307 ? 165.741 119.790 166.603 1.00 114.06 ? 307  ILE B CG1   1 
ATOM   7942  C  CG2   . ILE B 1 307 ? 167.113 117.911 165.744 1.00 114.80 ? 307  ILE B CG2   1 
ATOM   7943  C  CD1   . ILE B 1 307 ? 166.085 120.973 165.736 1.00 111.14 ? 307  ILE B CD1   1 
ATOM   7944  N  N     . GLY B 1 308 ? 166.036 119.084 170.327 1.00 120.79 ? 308  GLY B N     1 
ATOM   7945  C  CA    . GLY B 1 308 ? 166.223 119.832 171.553 1.00 122.95 ? 308  GLY B CA    1 
ATOM   7946  C  C     . GLY B 1 308 ? 166.230 121.332 171.361 1.00 116.47 ? 308  GLY B C     1 
ATOM   7947  O  O     . GLY B 1 308 ? 167.209 122.006 171.690 1.00 115.46 ? 308  GLY B O     1 
ATOM   7948  N  N     . LEU B 1 309 ? 165.139 121.866 170.818 1.00 113.66 ? 309  LEU B N     1 
ATOM   7949  C  CA    . LEU B 1 309 ? 165.059 123.293 170.542 1.00 108.69 ? 309  LEU B CA    1 
ATOM   7950  C  C     . LEU B 1 309 ? 163.653 123.847 170.763 1.00 113.26 ? 309  LEU B C     1 
ATOM   7951  O  O     . LEU B 1 309 ? 163.418 125.031 170.499 1.00 113.74 ? 309  LEU B O     1 
ATOM   7952  C  CB    . LEU B 1 309 ? 165.560 123.543 169.110 1.00 110.04 ? 309  LEU B CB    1 
ATOM   7953  C  CG    . LEU B 1 309 ? 165.525 124.883 168.386 1.00 104.34 ? 309  LEU B CG    1 
ATOM   7954  C  CD1   . LEU B 1 309 ? 166.784 125.069 167.573 1.00 102.32 ? 309  LEU B CD1   1 
ATOM   7955  C  CD2   . LEU B 1 309 ? 164.325 124.873 167.483 1.00 104.31 ? 309  LEU B CD2   1 
ATOM   7956  N  N     . TYR B 1 310 ? 162.725 123.046 171.279 1.00 120.35 ? 310  TYR B N     1 
ATOM   7957  C  CA    . TYR B 1 310 ? 161.342 123.471 171.449 1.00 117.42 ? 310  TYR B CA    1 
ATOM   7958  C  C     . TYR B 1 310 ? 160.758 122.776 172.670 1.00 125.47 ? 310  TYR B C     1 
ATOM   7959  O  O     . TYR B 1 310 ? 161.118 121.638 172.980 1.00 131.73 ? 310  TYR B O     1 
ATOM   7960  C  CB    . TYR B 1 310 ? 160.521 123.152 170.197 1.00 114.59 ? 310  TYR B CB    1 
ATOM   7961  C  CG    . TYR B 1 310 ? 159.115 123.694 170.206 1.00 119.17 ? 310  TYR B CG    1 
ATOM   7962  C  CD1   . TYR B 1 310 ? 158.834 124.957 169.714 1.00 121.24 ? 310  TYR B CD1   1 
ATOM   7963  C  CD2   . TYR B 1 310 ? 158.063 122.931 170.686 1.00 120.18 ? 310  TYR B CD2   1 
ATOM   7964  C  CE1   . TYR B 1 310 ? 157.549 125.450 169.713 1.00 124.26 ? 310  TYR B CE1   1 
ATOM   7965  C  CE2   . TYR B 1 310 ? 156.776 123.416 170.688 1.00 120.72 ? 310  TYR B CE2   1 
ATOM   7966  C  CZ    . TYR B 1 310 ? 156.524 124.676 170.200 1.00 122.53 ? 310  TYR B CZ    1 
ATOM   7967  O  OH    . TYR B 1 310 ? 155.238 125.163 170.202 1.00 124.36 ? 310  TYR B OH    1 
ATOM   7968  N  N     . ASP B 1 311 ? 159.857 123.473 173.362 1.00 123.53 ? 311  ASP B N     1 
ATOM   7969  C  CA    . ASP B 1 311 ? 159.213 122.908 174.547 1.00 122.90 ? 311  ASP B CA    1 
ATOM   7970  C  C     . ASP B 1 311 ? 157.889 123.620 174.777 1.00 122.62 ? 311  ASP B C     1 
ATOM   7971  O  O     . ASP B 1 311 ? 157.876 124.790 175.176 1.00 124.64 ? 311  ASP B O     1 
ATOM   7972  C  CB    . ASP B 1 311 ? 160.115 123.036 175.772 1.00 121.72 ? 311  ASP B CB    1 
ATOM   7973  C  CG    . ASP B 1 311 ? 159.904 121.914 176.768 1.00 127.28 ? 311  ASP B CG    1 
ATOM   7974  O  OD1   . ASP B 1 311 ? 160.309 120.772 176.469 1.00 128.97 ? 311  ASP B OD1   1 
ATOM   7975  O  OD2   . ASP B 1 311 ? 159.333 122.171 177.847 1.00 133.77 ? 311  ASP B OD2   1 
ATOM   7976  N  N     . GLU B 1 312 ? 156.782 122.912 174.536 1.00 122.54 ? 312  GLU B N     1 
ATOM   7977  C  CA    . GLU B 1 312 ? 155.457 123.507 174.694 1.00 121.00 ? 312  GLU B CA    1 
ATOM   7978  C  C     . GLU B 1 312 ? 155.183 123.901 176.139 1.00 123.51 ? 312  GLU B C     1 
ATOM   7979  O  O     . GLU B 1 312 ? 154.619 124.971 176.398 1.00 124.35 ? 312  GLU B O     1 
ATOM   7980  C  CB    . GLU B 1 312 ? 154.386 122.535 174.199 1.00 121.90 ? 312  GLU B CB    1 
ATOM   7981  C  CG    . GLU B 1 312 ? 153.048 123.178 173.849 1.00 125.99 ? 312  GLU B CG    1 
ATOM   7982  C  CD    . GLU B 1 312 ? 153.048 123.911 172.519 1.00 134.96 ? 312  GLU B CD    1 
ATOM   7983  O  OE1   . GLU B 1 312 ? 151.948 124.132 171.971 1.00 140.71 ? 312  GLU B OE1   1 
ATOM   7984  O  OE2   . GLU B 1 312 ? 154.133 124.260 172.013 1.00 135.41 ? 312  GLU B OE2   1 
ATOM   7985  N  N     . ASP B 1 313 ? 155.548 123.040 177.092 1.00 124.59 ? 313  ASP B N     1 
ATOM   7986  C  CA    . ASP B 1 313 ? 155.322 123.360 178.498 1.00 123.30 ? 313  ASP B CA    1 
ATOM   7987  C  C     . ASP B 1 313 ? 156.097 124.603 178.909 1.00 121.33 ? 313  ASP B C     1 
ATOM   7988  O  O     . ASP B 1 313 ? 155.554 125.492 179.576 1.00 120.44 ? 313  ASP B O     1 
ATOM   7989  C  CB    . ASP B 1 313 ? 155.714 122.172 179.376 1.00 126.58 ? 313  ASP B CB    1 
ATOM   7990  C  CG    . ASP B 1 313 ? 155.064 120.880 178.930 1.00 131.86 ? 313  ASP B CG    1 
ATOM   7991  O  OD1   . ASP B 1 313 ? 154.336 120.899 177.917 1.00 133.29 ? 313  ASP B OD1   1 
ATOM   7992  O  OD2   . ASP B 1 313 ? 155.283 119.843 179.591 1.00 135.93 ? 313  ASP B OD2   1 
ATOM   7993  N  N     . LEU B 1 314 ? 157.370 124.682 178.516 1.00 122.32 ? 314  LEU B N     1 
ATOM   7994  C  CA    . LEU B 1 314 ? 158.175 125.853 178.839 1.00 118.62 ? 314  LEU B CA    1 
ATOM   7995  C  C     . LEU B 1 314 ? 157.588 127.107 178.212 1.00 114.57 ? 314  LEU B C     1 
ATOM   7996  O  O     . LEU B 1 314 ? 157.505 128.154 178.863 1.00 116.26 ? 314  LEU B O     1 
ATOM   7997  C  CB    . LEU B 1 314 ? 159.614 125.643 178.374 1.00 117.39 ? 314  LEU B CB    1 
ATOM   7998  C  CG    . LEU B 1 314 ? 160.641 126.666 178.847 1.00 115.19 ? 314  LEU B CG    1 
ATOM   7999  C  CD1   . LEU B 1 314 ? 160.792 126.589 180.350 1.00 119.02 ? 314  LEU B CD1   1 
ATOM   8000  C  CD2   . LEU B 1 314 ? 161.972 126.425 178.164 1.00 115.92 ? 314  LEU B CD2   1 
ATOM   8001  N  N     . LEU B 1 315 ? 157.167 127.017 176.948 1.00 114.77 ? 315  LEU B N     1 
ATOM   8002  C  CA    . LEU B 1 315 ? 156.566 128.171 176.288 1.00 115.84 ? 315  LEU B CA    1 
ATOM   8003  C  C     . LEU B 1 315 ? 155.323 128.643 177.028 1.00 117.88 ? 315  LEU B C     1 
ATOM   8004  O  O     . LEU B 1 315 ? 155.188 129.834 177.334 1.00 118.79 ? 315  LEU B O     1 
ATOM   8005  C  CB    . LEU B 1 315 ? 156.227 127.823 174.838 1.00 115.66 ? 315  LEU B CB    1 
ATOM   8006  C  CG    . LEU B 1 315 ? 155.516 128.882 173.994 1.00 112.95 ? 315  LEU B CG    1 
ATOM   8007  C  CD1   . LEU B 1 315 ? 156.108 128.921 172.600 1.00 116.33 ? 315  LEU B CD1   1 
ATOM   8008  C  CD2   . LEU B 1 315 ? 154.025 128.611 173.920 1.00 115.75 ? 315  LEU B CD2   1 
ATOM   8009  N  N     . THR B 1 316 ? 154.413 127.719 177.343 1.00 120.29 ? 316  THR B N     1 
ATOM   8010  C  CA    . THR B 1 316 ? 153.152 128.102 177.969 1.00 120.98 ? 316  THR B CA    1 
ATOM   8011  C  C     . THR B 1 316 ? 153.369 128.668 179.367 1.00 122.16 ? 316  THR B C     1 
ATOM   8012  O  O     . THR B 1 316 ? 152.722 129.651 179.748 1.00 122.43 ? 316  THR B O     1 
ATOM   8013  C  CB    . THR B 1 316 ? 152.204 126.906 178.014 1.00 124.68 ? 316  THR B CB    1 
ATOM   8014  O  OG1   . THR B 1 316 ? 152.027 126.388 176.691 1.00 125.59 ? 316  THR B OG1   1 
ATOM   8015  C  CG2   . THR B 1 316 ? 150.854 127.323 178.560 1.00 128.05 ? 316  THR B CG2   1 
ATOM   8016  N  N     . ILE B 1 317 ? 154.269 128.071 180.149 1.00 120.00 ? 317  ILE B N     1 
ATOM   8017  C  CA    . ILE B 1 317 ? 154.515 128.585 181.494 1.00 114.03 ? 317  ILE B CA    1 
ATOM   8018  C  C     . ILE B 1 317 ? 155.189 129.949 181.442 1.00 114.36 ? 317  ILE B C     1 
ATOM   8019  O  O     . ILE B 1 317 ? 154.725 130.904 182.073 1.00 119.66 ? 317  ILE B O     1 
ATOM   8020  C  CB    . ILE B 1 317 ? 155.344 127.586 182.327 1.00 119.57 ? 317  ILE B CB    1 
ATOM   8021  C  CG1   . ILE B 1 317 ? 154.637 126.235 182.472 1.00 120.40 ? 317  ILE B CG1   1 
ATOM   8022  C  CG2   . ILE B 1 317 ? 155.648 128.165 183.699 1.00 123.30 ? 317  ILE B CG2   1 
ATOM   8023  C  CD1   . ILE B 1 317 ? 153.135 126.305 182.413 1.00 123.89 ? 317  ILE B CD1   1 
ATOM   8024  N  N     . ASN B 1 318 ? 156.276 130.078 180.679 1.00 111.62 ? 318  ASN B N     1 
ATOM   8025  C  CA    . ASN B 1 318 ? 157.090 131.282 180.761 1.00 112.24 ? 318  ASN B CA    1 
ATOM   8026  C  C     . ASN B 1 318 ? 156.599 132.409 179.863 1.00 118.40 ? 318  ASN B C     1 
ATOM   8027  O  O     . ASN B 1 318 ? 157.157 133.509 179.926 1.00 122.52 ? 318  ASN B O     1 
ATOM   8028  C  CB    . ASN B 1 318 ? 158.544 130.949 180.428 1.00 109.14 ? 318  ASN B CB    1 
ATOM   8029  C  CG    . ASN B 1 318 ? 159.349 130.590 181.657 1.00 113.74 ? 318  ASN B CG    1 
ATOM   8030  O  OD1   . ASN B 1 318 ? 160.061 131.425 182.214 1.00 120.83 ? 318  ASN B OD1   1 
ATOM   8031  N  ND2   . ASN B 1 318 ? 159.233 129.345 182.095 1.00 116.88 ? 318  ASN B ND2   1 
ATOM   8032  N  N     . SER B 1 319 ? 155.579 132.177 179.039 1.00 117.42 ? 319  SER B N     1 
ATOM   8033  C  CA    . SER B 1 319 ? 154.999 133.227 178.215 1.00 116.33 ? 319  SER B CA    1 
ATOM   8034  C  C     . SER B 1 319 ? 153.562 133.544 178.607 1.00 121.71 ? 319  SER B C     1 
ATOM   8035  O  O     . SER B 1 319 ? 152.798 134.048 177.779 1.00 124.13 ? 319  SER B O     1 
ATOM   8036  C  CB    . SER B 1 319 ? 155.066 132.837 176.740 1.00 116.72 ? 319  SER B CB    1 
ATOM   8037  O  OG    . SER B 1 319 ? 154.260 133.697 175.956 1.00 121.04 ? 319  SER B OG    1 
ATOM   8038  N  N     . ALA B 1 320 ? 153.180 133.250 179.852 1.00 122.99 ? 320  ALA B N     1 
ATOM   8039  C  CA    . ALA B 1 320 ? 151.789 133.407 180.262 1.00 123.89 ? 320  ALA B CA    1 
ATOM   8040  C  C     . ALA B 1 320 ? 151.368 134.871 180.273 1.00 126.80 ? 320  ALA B C     1 
ATOM   8041  O  O     . ALA B 1 320 ? 150.344 135.236 179.686 1.00 130.03 ? 320  ALA B O     1 
ATOM   8042  C  CB    . ALA B 1 320 ? 151.576 132.777 181.637 1.00 125.10 ? 320  ALA B CB    1 
ATOM   8043  N  N     . GLY B 1 321 ? 152.144 135.725 180.932 1.00 126.87 ? 321  GLY B N     1 
ATOM   8044  C  CA    . GLY B 1 321 ? 151.741 137.107 181.106 1.00 128.41 ? 321  GLY B CA    1 
ATOM   8045  C  C     . GLY B 1 321 ? 152.606 138.116 180.384 1.00 125.58 ? 321  GLY B C     1 
ATOM   8046  O  O     . GLY B 1 321 ? 152.286 139.308 180.359 1.00 125.15 ? 321  GLY B O     1 
ATOM   8047  N  N     . ILE B 1 322 ? 153.713 137.657 179.801 1.00 127.14 ? 322  ILE B N     1 
ATOM   8048  C  CA    . ILE B 1 322 ? 154.617 138.571 179.111 1.00 123.13 ? 322  ILE B CA    1 
ATOM   8049  C  C     . ILE B 1 322 ? 153.968 139.113 177.844 1.00 118.43 ? 322  ILE B C     1 
ATOM   8050  O  O     . ILE B 1 322 ? 154.218 140.256 177.444 1.00 121.59 ? 322  ILE B O     1 
ATOM   8051  C  CB    . ILE B 1 322 ? 155.957 137.874 178.822 1.00 125.98 ? 322  ILE B CB    1 
ATOM   8052  C  CG1   . ILE B 1 322 ? 156.483 137.211 180.098 1.00 132.93 ? 322  ILE B CG1   1 
ATOM   8053  C  CG2   . ILE B 1 322 ? 156.966 138.872 178.281 1.00 120.65 ? 322  ILE B CG2   1 
ATOM   8054  C  CD1   . ILE B 1 322 ? 157.985 137.029 180.138 1.00 135.06 ? 322  ILE B CD1   1 
ATOM   8055  N  N     . GLY B 1 323 ? 153.120 138.316 177.201 1.00 114.77 ? 323  GLY B N     1 
ATOM   8056  C  CA    . GLY B 1 323 ? 152.463 138.742 175.980 1.00 113.51 ? 323  GLY B CA    1 
ATOM   8057  C  C     . GLY B 1 323 ? 153.435 138.929 174.836 1.00 119.93 ? 323  GLY B C     1 
ATOM   8058  O  O     . GLY B 1 323 ? 153.362 139.916 174.098 1.00 124.91 ? 323  GLY B O     1 
ATOM   8059  N  N     . ALA B 1 324 ? 154.349 137.977 174.682 1.00 121.46 ? 324  ALA B N     1 
ATOM   8060  C  CA    . ALA B 1 324 ? 155.420 138.098 173.706 1.00 121.22 ? 324  ALA B CA    1 
ATOM   8061  C  C     . ALA B 1 324 ? 154.885 138.030 172.280 1.00 121.52 ? 324  ALA B C     1 
ATOM   8062  O  O     . ALA B 1 324 ? 153.961 137.275 171.972 1.00 120.48 ? 324  ALA B O     1 
ATOM   8063  C  CB    . ALA B 1 324 ? 156.456 136.996 173.923 1.00 120.31 ? 324  ALA B CB    1 
ATOM   8064  N  N     . GLN B 1 325 ? 155.483 138.843 171.405 1.00 122.21 ? 325  GLN B N     1 
ATOM   8065  C  CA    . GLN B 1 325 ? 155.182 138.759 169.980 1.00 121.28 ? 325  GLN B CA    1 
ATOM   8066  C  C     . GLN B 1 325 ? 155.833 137.536 169.349 1.00 118.41 ? 325  GLN B C     1 
ATOM   8067  O  O     . GLN B 1 325 ? 155.219 136.864 168.513 1.00 118.64 ? 325  GLN B O     1 
ATOM   8068  C  CB    . GLN B 1 325 ? 155.645 140.026 169.263 1.00 125.23 ? 325  GLN B CB    1 
ATOM   8069  C  CG    . GLN B 1 325 ? 155.446 141.303 170.052 1.00 130.74 ? 325  GLN B CG    1 
ATOM   8070  C  CD    . GLN B 1 325 ? 154.004 141.763 170.052 1.00 139.12 ? 325  GLN B CD    1 
ATOM   8071  O  OE1   . GLN B 1 325 ? 153.217 141.369 169.193 1.00 144.29 ? 325  GLN B OE1   1 
ATOM   8072  N  NE2   . GLN B 1 325 ? 153.651 142.603 171.017 1.00 137.74 ? 325  GLN B NE2   1 
ATOM   8073  N  N     . CYS B 1 326 ? 157.071 137.236 169.733 1.00 116.97 ? 326  CYS B N     1 
ATOM   8074  C  CA    . CYS B 1 326 ? 157.757 136.055 169.236 1.00 114.84 ? 326  CYS B CA    1 
ATOM   8075  C  C     . CYS B 1 326 ? 158.535 135.422 170.377 1.00 116.20 ? 326  CYS B C     1 
ATOM   8076  O  O     . CYS B 1 326 ? 158.987 136.108 171.297 1.00 119.74 ? 326  CYS B O     1 
ATOM   8077  C  CB    . CYS B 1 326 ? 158.698 136.391 168.074 1.00 115.52 ? 326  CYS B CB    1 
ATOM   8078  S  SG    . CYS B 1 326 ? 160.251 137.169 168.539 1.00 126.00 ? 326  CYS B SG    1 
ATOM   8079  N  N     . HIS B 1 327 ? 158.695 134.106 170.302 1.00 109.62 ? 327  HIS B N     1 
ATOM   8080  C  CA    . HIS B 1 327 ? 159.434 133.340 171.293 1.00 107.00 ? 327  HIS B CA    1 
ATOM   8081  C  C     . HIS B 1 327 ? 160.665 132.751 170.625 1.00 106.35 ? 327  HIS B C     1 
ATOM   8082  O  O     . HIS B 1 327 ? 160.545 132.036 169.626 1.00 111.44 ? 327  HIS B O     1 
ATOM   8083  C  CB    . HIS B 1 327 ? 158.579 132.215 171.876 1.00 106.19 ? 327  HIS B CB    1 
ATOM   8084  C  CG    . HIS B 1 327 ? 157.114 132.518 171.908 1.00 108.85 ? 327  HIS B CG    1 
ATOM   8085  N  ND1   . HIS B 1 327 ? 156.485 133.035 173.019 1.00 115.56 ? 327  HIS B ND1   1 
ATOM   8086  C  CD2   . HIS B 1 327 ? 156.153 132.363 170.969 1.00 111.32 ? 327  HIS B CD2   1 
ATOM   8087  C  CE1   . HIS B 1 327 ? 155.199 133.192 172.759 1.00 116.97 ? 327  HIS B CE1   1 
ATOM   8088  N  NE2   . HIS B 1 327 ? 154.971 132.791 171.522 1.00 116.92 ? 327  HIS B NE2   1 
ATOM   8089  N  N     . LEU B 1 328 ? 161.840 133.038 171.173 1.00 100.92 ? 328  LEU B N     1 
ATOM   8090  C  CA    . LEU B 1 328 ? 163.085 132.551 170.600 1.00 99.28  ? 328  LEU B CA    1 
ATOM   8091  C  C     . LEU B 1 328 ? 163.717 131.530 171.534 1.00 99.96  ? 328  LEU B C     1 
ATOM   8092  O  O     . LEU B 1 328 ? 163.866 131.783 172.733 1.00 104.04 ? 328  LEU B O     1 
ATOM   8093  C  CB    . LEU B 1 328 ? 164.057 133.701 170.305 1.00 97.54  ? 328  LEU B CB    1 
ATOM   8094  C  CG    . LEU B 1 328 ? 164.691 134.522 171.424 1.00 99.25  ? 328  LEU B CG    1 
ATOM   8095  C  CD1   . LEU B 1 328 ? 166.068 133.988 171.778 1.00 101.63 ? 328  LEU B CD1   1 
ATOM   8096  C  CD2   . LEU B 1 328 ? 164.785 135.966 170.990 1.00 101.52 ? 328  LEU B CD2   1 
ATOM   8097  N  N     . PHE B 1 329 ? 164.072 130.377 170.979 1.00 97.57  ? 329  PHE B N     1 
ATOM   8098  C  CA    . PHE B 1 329 ? 164.804 129.344 171.690 1.00 97.21  ? 329  PHE B CA    1 
ATOM   8099  C  C     . PHE B 1 329 ? 166.215 129.255 171.126 1.00 99.45  ? 329  PHE B C     1 
ATOM   8100  O  O     . PHE B 1 329 ? 166.423 129.335 169.914 1.00 107.30 ? 329  PHE B O     1 
ATOM   8101  C  CB    . PHE B 1 329 ? 164.128 127.974 171.570 1.00 98.24  ? 329  PHE B CB    1 
ATOM   8102  C  CG    . PHE B 1 329 ? 162.648 127.978 171.848 1.00 103.08 ? 329  PHE B CG    1 
ATOM   8103  C  CD1   . PHE B 1 329 ? 161.746 128.482 170.927 1.00 103.82 ? 329  PHE B CD1   1 
ATOM   8104  C  CD2   . PHE B 1 329 ? 162.156 127.415 173.011 1.00 105.99 ? 329  PHE B CD2   1 
ATOM   8105  C  CE1   . PHE B 1 329 ? 160.391 128.463 171.181 1.00 102.81 ? 329  PHE B CE1   1 
ATOM   8106  C  CE2   . PHE B 1 329 ? 160.803 127.395 173.269 1.00 106.63 ? 329  PHE B CE2   1 
ATOM   8107  C  CZ    . PHE B 1 329 ? 159.920 127.918 172.353 1.00 105.89 ? 329  PHE B CZ    1 
ATOM   8108  N  N     . GLU B 1 330 ? 167.185 129.088 172.016 1.00 97.72  ? 330  GLU B N     1 
ATOM   8109  C  CA    . GLU B 1 330 ? 168.580 128.998 171.619 1.00 99.84  ? 330  GLU B CA    1 
ATOM   8110  C  C     . GLU B 1 330 ? 169.149 127.659 172.056 1.00 105.95 ? 330  GLU B C     1 
ATOM   8111  O  O     . GLU B 1 330 ? 169.045 127.284 173.226 1.00 116.72 ? 330  GLU B O     1 
ATOM   8112  C  CB    . GLU B 1 330 ? 169.406 130.134 172.224 1.00 104.22 ? 330  GLU B CB    1 
ATOM   8113  C  CG    . GLU B 1 330 ? 168.745 131.495 172.147 1.00 108.71 ? 330  GLU B CG    1 
ATOM   8114  C  CD    . GLU B 1 330 ? 169.583 132.582 172.788 1.00 127.62 ? 330  GLU B CD    1 
ATOM   8115  O  OE1   . GLU B 1 330 ? 170.803 132.625 172.527 1.00 129.41 ? 330  GLU B OE1   1 
ATOM   8116  O  OE2   . GLU B 1 330 ? 169.022 133.394 173.553 1.00 131.04 ? 330  GLU B OE2   1 
ATOM   8117  N  N     . HIS B 1 331 ? 169.758 126.949 171.113 1.00 102.57 ? 331  HIS B N     1 
ATOM   8118  C  CA    . HIS B 1 331 ? 170.426 125.694 171.419 1.00 102.41 ? 331  HIS B CA    1 
ATOM   8119  C  C     . HIS B 1 331 ? 171.434 125.397 170.323 1.00 112.08 ? 331  HIS B C     1 
ATOM   8120  O  O     . HIS B 1 331 ? 171.083 125.324 169.144 1.00 116.87 ? 331  HIS B O     1 
ATOM   8121  C  CB    . HIS B 1 331 ? 169.433 124.536 171.545 1.00 100.11 ? 331  HIS B CB    1 
ATOM   8122  C  CG    . HIS B 1 331 ? 170.051 123.263 172.033 1.00 105.68 ? 331  HIS B CG    1 
ATOM   8123  N  ND1   . HIS B 1 331 ? 169.450 122.035 171.872 1.00 111.73 ? 331  HIS B ND1   1 
ATOM   8124  C  CD2   . HIS B 1 331 ? 171.217 123.030 172.680 1.00 110.58 ? 331  HIS B CD2   1 
ATOM   8125  C  CE1   . HIS B 1 331 ? 170.219 121.098 172.396 1.00 114.53 ? 331  HIS B CE1   1 
ATOM   8126  N  NE2   . HIS B 1 331 ? 171.297 121.675 172.894 1.00 115.85 ? 331  HIS B NE2   1 
ATOM   8127  N  N     . THR B 1 332 ? 172.691 125.221 170.727 1.00 111.91 ? 332  THR B N     1 
ATOM   8128  C  CA    . THR B 1 332 ? 173.749 124.805 169.811 1.00 109.04 ? 332  THR B CA    1 
ATOM   8129  C  C     . THR B 1 332 ? 173.579 123.307 169.585 1.00 112.15 ? 332  THR B C     1 
ATOM   8130  O  O     . THR B 1 332 ? 174.281 122.474 170.157 1.00 117.85 ? 332  THR B O     1 
ATOM   8131  C  CB    . THR B 1 332 ? 175.122 125.149 170.370 1.00 117.37 ? 332  THR B CB    1 
ATOM   8132  O  OG1   . THR B 1 332 ? 175.588 124.069 171.183 1.00 131.36 ? 332  THR B OG1   1 
ATOM   8133  C  CG2   . THR B 1 332 ? 175.045 126.408 171.211 1.00 120.58 ? 332  THR B CG2   1 
ATOM   8134  N  N     . LEU B 1 333 ? 172.620 122.976 168.728 1.00 111.28 ? 333  LEU B N     1 
ATOM   8135  C  CA    . LEU B 1 333 ? 172.156 121.605 168.581 1.00 111.95 ? 333  LEU B CA    1 
ATOM   8136  C  C     . LEU B 1 333 ? 173.237 120.698 168.002 1.00 114.35 ? 333  LEU B C     1 
ATOM   8137  O  O     . LEU B 1 333 ? 174.041 121.101 167.159 1.00 116.74 ? 333  LEU B O     1 
ATOM   8138  C  CB    . LEU B 1 333 ? 170.891 121.577 167.720 1.00 104.69 ? 333  LEU B CB    1 
ATOM   8139  C  CG    . LEU B 1 333 ? 170.788 122.445 166.460 1.00 95.24  ? 333  LEU B CG    1 
ATOM   8140  C  CD1   . LEU B 1 333 ? 171.730 122.017 165.354 1.00 103.25 ? 333  LEU B CD1   1 
ATOM   8141  C  CD2   . LEU B 1 333 ? 169.361 122.482 165.955 1.00 94.64  ? 333  LEU B CD2   1 
ATOM   8142  N  N     . GLN B 1 334 ? 173.266 119.462 168.496 1.00 113.90 ? 334  GLN B N     1 
ATOM   8143  C  CA    . GLN B 1 334 ? 174.159 118.425 167.997 1.00 120.70 ? 334  GLN B CA    1 
ATOM   8144  C  C     . GLN B 1 334 ? 173.346 117.480 167.127 1.00 123.50 ? 334  GLN B C     1 
ATOM   8145  O  O     . GLN B 1 334 ? 172.295 116.990 167.554 1.00 125.67 ? 334  GLN B O     1 
ATOM   8146  C  CB    . GLN B 1 334 ? 174.833 117.651 169.135 1.00 124.80 ? 334  GLN B CB    1 
ATOM   8147  C  CG    . GLN B 1 334 ? 175.472 118.490 170.238 1.00 127.24 ? 334  GLN B CG    1 
ATOM   8148  C  CD    . GLN B 1 334 ? 174.462 119.100 171.185 1.00 121.50 ? 334  GLN B CD    1 
ATOM   8149  O  OE1   . GLN B 1 334 ? 173.327 118.637 171.280 1.00 119.29 ? 334  GLN B OE1   1 
ATOM   8150  N  NE2   . GLN B 1 334 ? 174.873 120.139 171.899 1.00 121.97 ? 334  GLN B NE2   1 
ATOM   8151  N  N     . LEU B 1 335 ? 173.828 117.226 165.916 1.00 125.19 ? 335  LEU B N     1 
ATOM   8152  C  CA    . LEU B 1 335 ? 173.136 116.376 164.959 1.00 126.07 ? 335  LEU B CA    1 
ATOM   8153  C  C     . LEU B 1 335 ? 174.021 115.200 164.579 1.00 134.24 ? 335  LEU B C     1 
ATOM   8154  O  O     . LEU B 1 335 ? 175.225 115.362 164.356 1.00 138.98 ? 335  LEU B O     1 
ATOM   8155  C  CB    . LEU B 1 335 ? 172.744 117.165 163.709 1.00 119.02 ? 335  LEU B CB    1 
ATOM   8156  C  CG    . LEU B 1 335 ? 171.594 118.147 163.916 1.00 111.13 ? 335  LEU B CG    1 
ATOM   8157  C  CD1   . LEU B 1 335 ? 171.243 118.854 162.625 1.00 105.88 ? 335  LEU B CD1   1 
ATOM   8158  C  CD2   . LEU B 1 335 ? 170.395 117.408 164.462 1.00 111.28 ? 335  LEU B CD2   1 
ATOM   8159  N  N     . SER B 1 336 ? 173.421 114.015 164.513 1.00 134.27 ? 336  SER B N     1 
ATOM   8160  C  CA    . SER B 1 336 ? 174.130 112.800 164.138 1.00 139.67 ? 336  SER B CA    1 
ATOM   8161  C  C     . SER B 1 336 ? 173.432 112.167 162.946 1.00 143.28 ? 336  SER B C     1 
ATOM   8162  O  O     . SER B 1 336 ? 172.200 112.080 162.919 1.00 141.58 ? 336  SER B O     1 
ATOM   8163  C  CB    . SER B 1 336 ? 174.193 111.808 165.305 1.00 141.33 ? 336  SER B CB    1 
ATOM   8164  O  OG    . SER B 1 336 ? 172.899 111.523 165.804 1.00 143.78 ? 336  SER B OG    1 
ATOM   8165  N  N     . VAL B 1 337 ? 174.217 111.740 161.961 1.00 146.95 ? 337  VAL B N     1 
ATOM   8166  C  CA    . VAL B 1 337 ? 173.712 111.029 160.792 1.00 150.99 ? 337  VAL B CA    1 
ATOM   8167  C  C     . VAL B 1 337 ? 174.496 109.731 160.661 1.00 154.90 ? 337  VAL B C     1 
ATOM   8168  O  O     . VAL B 1 337 ? 175.694 109.754 160.350 1.00 153.84 ? 337  VAL B O     1 
ATOM   8169  C  CB    . VAL B 1 337 ? 173.822 111.871 159.513 1.00 144.74 ? 337  VAL B CB    1 
ATOM   8170  C  CG1   . VAL B 1 337 ? 173.424 111.045 158.303 1.00 143.65 ? 337  VAL B CG1   1 
ATOM   8171  C  CG2   . VAL B 1 337 ? 172.949 113.109 159.621 1.00 136.31 ? 337  VAL B CG2   1 
ATOM   8172  N  N     . ASN B 1 338 ? 173.820 108.608 160.891 1.00 156.41 ? 338  ASN B N     1 
ATOM   8173  C  CA    . ASN B 1 338 ? 174.413 107.266 160.814 1.00 159.30 ? 338  ASN B CA    1 
ATOM   8174  C  C     . ASN B 1 338 ? 175.575 107.220 161.805 1.00 158.86 ? 338  ASN B C     1 
ATOM   8175  O  O     . ASN B 1 338 ? 175.406 107.651 162.957 1.00 154.63 ? 338  ASN B O     1 
ATOM   8176  C  CB    . ASN B 1 338 ? 174.767 106.958 159.365 1.00 161.78 ? 338  ASN B CB    1 
ATOM   8177  C  CG    . ASN B 1 338 ? 173.709 107.438 158.393 1.00 160.61 ? 338  ASN B CG    1 
ATOM   8178  O  OD1   . ASN B 1 338 ? 172.551 107.629 158.763 1.00 156.57 ? 338  ASN B OD1   1 
ATOM   8179  N  ND2   . ASN B 1 338 ? 174.103 107.639 157.141 1.00 158.57 ? 338  ASN B ND2   1 
ATOM   8180  N  N     . GLY B 1 339 ? 176.746 106.722 161.421 1.00 161.77 ? 339  GLY B N     1 
ATOM   8181  C  CA    . GLY B 1 339 ? 177.898 106.685 162.292 1.00 161.07 ? 339  GLY B CA    1 
ATOM   8182  C  C     . GLY B 1 339 ? 178.733 107.941 162.301 1.00 161.71 ? 339  GLY B C     1 
ATOM   8183  O  O     . GLY B 1 339 ? 179.770 107.983 162.971 1.00 162.45 ? 339  GLY B O     1 
ATOM   8184  N  N     . LYS B 1 340 ? 178.316 108.972 161.573 1.00 160.00 ? 340  LYS B N     1 
ATOM   8185  C  CA    . LYS B 1 340 ? 179.032 110.237 161.522 1.00 159.19 ? 340  LYS B CA    1 
ATOM   8186  C  C     . LYS B 1 340 ? 178.243 111.309 162.260 1.00 154.45 ? 340  LYS B C     1 
ATOM   8187  O  O     . LYS B 1 340 ? 177.072 111.555 161.957 1.00 151.33 ? 340  LYS B O     1 
ATOM   8188  C  CB    . LYS B 1 340 ? 179.277 110.667 160.074 1.00 157.82 ? 340  LYS B CB    1 
ATOM   8189  C  CG    . LYS B 1 340 ? 180.263 109.785 159.327 1.00 159.72 ? 340  LYS B CG    1 
ATOM   8190  C  CD    . LYS B 1 340 ? 180.525 110.306 157.924 1.00 164.67 ? 340  LYS B CD    1 
ATOM   8191  C  CE    . LYS B 1 340 ? 181.523 109.427 157.188 1.00 160.63 ? 340  LYS B CE    1 
ATOM   8192  N  NZ    . LYS B 1 340 ? 181.777 109.909 155.802 1.00 156.19 ? 340  LYS B NZ    1 
ATOM   8193  N  N     . CYS B 1 341 ? 178.893 111.945 163.228 1.00 148.77 ? 341  CYS B N     1 
ATOM   8194  C  CA    . CYS B 1 341 ? 178.279 112.991 164.032 1.00 139.40 ? 341  CYS B CA    1 
ATOM   8195  C  C     . CYS B 1 341 ? 178.606 114.343 163.412 1.00 136.03 ? 341  CYS B C     1 
ATOM   8196  O  O     . CYS B 1 341 ? 179.781 114.693 163.259 1.00 136.60 ? 341  CYS B O     1 
ATOM   8197  C  CB    . CYS B 1 341 ? 178.774 112.921 165.475 1.00 144.42 ? 341  CYS B CB    1 
ATOM   8198  S  SG    . CYS B 1 341 ? 180.540 112.583 165.627 1.00 163.43 ? 341  CYS B SG    1 
ATOM   8199  N  N     . LEU B 1 342 ? 177.569 115.096 163.057 1.00 133.10 ? 342  LEU B N     1 
ATOM   8200  C  CA    . LEU B 1 342 ? 177.762 116.375 162.396 1.00 128.81 ? 342  LEU B CA    1 
ATOM   8201  C  C     . LEU B 1 342 ? 178.323 117.412 163.364 1.00 129.85 ? 342  LEU B C     1 
ATOM   8202  O  O     . LEU B 1 342 ? 178.288 117.250 164.586 1.00 134.04 ? 342  LEU B O     1 
ATOM   8203  C  CB    . LEU B 1 342 ? 176.447 116.875 161.802 1.00 123.39 ? 342  LEU B CB    1 
ATOM   8204  C  CG    . LEU B 1 342 ? 175.780 115.959 160.778 1.00 128.93 ? 342  LEU B CG    1 
ATOM   8205  C  CD1   . LEU B 1 342 ? 174.402 116.480 160.413 1.00 123.85 ? 342  LEU B CD1   1 
ATOM   8206  C  CD2   . LEU B 1 342 ? 176.649 115.829 159.541 1.00 125.54 ? 342  LEU B CD2   1 
ATOM   8207  N  N     . LEU B 1 343 ? 178.855 118.487 162.791 1.00 121.22 ? 343  LEU B N     1 
ATOM   8208  C  CA    . LEU B 1 343 ? 179.379 119.580 163.589 1.00 116.08 ? 343  LEU B CA    1 
ATOM   8209  C  C     . LEU B 1 343 ? 178.236 120.287 164.317 1.00 115.82 ? 343  LEU B C     1 
ATOM   8210  O  O     . LEU B 1 343 ? 177.145 120.445 163.763 1.00 118.39 ? 343  LEU B O     1 
ATOM   8211  C  CB    . LEU B 1 343 ? 180.115 120.576 162.700 1.00 109.85 ? 343  LEU B CB    1 
ATOM   8212  C  CG    . LEU B 1 343 ? 181.645 120.591 162.676 1.00 113.43 ? 343  LEU B CG    1 
ATOM   8213  C  CD1   . LEU B 1 343 ? 182.137 121.973 162.284 1.00 112.70 ? 343  LEU B CD1   1 
ATOM   8214  C  CD2   . LEU B 1 343 ? 182.254 120.150 163.993 1.00 119.63 ? 343  LEU B CD2   1 
ATOM   8215  N  N     . PRO B 1 344 ? 178.452 120.710 165.561 1.00 112.27 ? 344  PRO B N     1 
ATOM   8216  C  CA    . PRO B 1 344 ? 177.412 121.469 166.260 1.00 108.29 ? 344  PRO B CA    1 
ATOM   8217  C  C     . PRO B 1 344 ? 177.130 122.783 165.552 1.00 108.60 ? 344  PRO B C     1 
ATOM   8218  O  O     . PRO B 1 344 ? 178.033 123.442 165.036 1.00 115.12 ? 344  PRO B O     1 
ATOM   8219  C  CB    . PRO B 1 344 ? 178.009 121.694 167.651 1.00 114.57 ? 344  PRO B CB    1 
ATOM   8220  C  CG    . PRO B 1 344 ? 179.475 121.641 167.436 1.00 118.44 ? 344  PRO B CG    1 
ATOM   8221  C  CD    . PRO B 1 344 ? 179.692 120.628 166.349 1.00 116.31 ? 344  PRO B CD    1 
ATOM   8222  N  N     . ILE B 1 345 ? 175.856 123.162 165.533 1.00 106.68 ? 345  ILE B N     1 
ATOM   8223  C  CA    . ILE B 1 345 ? 175.400 124.358 164.836 1.00 105.15 ? 345  ILE B CA    1 
ATOM   8224  C  C     . ILE B 1 345 ? 174.822 125.315 165.865 1.00 107.41 ? 345  ILE B C     1 
ATOM   8225  O  O     . ILE B 1 345 ? 173.904 124.949 166.608 1.00 112.37 ? 345  ILE B O     1 
ATOM   8226  C  CB    . ILE B 1 345 ? 174.352 124.033 163.761 1.00 99.03  ? 345  ILE B CB    1 
ATOM   8227  C  CG1   . ILE B 1 345 ? 174.786 122.825 162.935 1.00 103.65 ? 345  ILE B CG1   1 
ATOM   8228  C  CG2   . ILE B 1 345 ? 174.128 125.226 162.865 1.00 93.12  ? 345  ILE B CG2   1 
ATOM   8229  C  CD1   . ILE B 1 345 ? 173.718 122.327 161.993 1.00 102.94 ? 345  ILE B CD1   1 
ATOM   8230  N  N     . GLN B 1 346 ? 175.342 126.537 165.901 1.00 101.87 ? 346  GLN B N     1 
ATOM   8231  C  CA    . GLN B 1 346 ? 174.825 127.555 166.804 1.00 101.09 ? 346  GLN B CA    1 
ATOM   8232  C  C     . GLN B 1 346 ? 173.505 128.072 166.251 1.00 99.50  ? 346  GLN B C     1 
ATOM   8233  O  O     . GLN B 1 346 ? 173.488 128.788 165.245 1.00 104.35 ? 346  GLN B O     1 
ATOM   8234  C  CB    . GLN B 1 346 ? 175.837 128.686 166.959 1.00 97.26  ? 346  GLN B CB    1 
ATOM   8235  C  CG    . GLN B 1 346 ? 175.902 129.274 168.350 1.00 103.81 ? 346  GLN B CG    1 
ATOM   8236  C  CD    . GLN B 1 346 ? 177.179 130.045 168.587 1.00 111.79 ? 346  GLN B CD    1 
ATOM   8237  O  OE1   . GLN B 1 346 ? 177.782 129.955 169.655 1.00 118.81 ? 346  GLN B OE1   1 
ATOM   8238  N  NE2   . GLN B 1 346 ? 177.606 130.803 167.587 1.00 110.05 ? 346  GLN B NE2   1 
ATOM   8239  N  N     . THR B 1 347 ? 172.402 127.718 166.903 1.00 95.27  ? 347  THR B N     1 
ATOM   8240  C  CA    . THR B 1 347 ? 171.076 127.926 166.341 1.00 94.91  ? 347  THR B CA    1 
ATOM   8241  C  C     . THR B 1 347 ? 170.225 128.781 167.266 1.00 91.93  ? 347  THR B C     1 
ATOM   8242  O  O     . THR B 1 347 ? 170.267 128.622 168.488 1.00 97.00  ? 347  THR B O     1 
ATOM   8243  C  CB    . THR B 1 347 ? 170.370 126.592 166.088 1.00 100.23 ? 347  THR B CB    1 
ATOM   8244  O  OG1   . THR B 1 347 ? 171.238 125.726 165.348 1.00 110.73 ? 347  THR B OG1   1 
ATOM   8245  C  CG2   . THR B 1 347 ? 169.095 126.807 165.292 1.00 97.15  ? 347  THR B CG2   1 
ATOM   8246  N  N     . VAL B 1 348 ? 169.462 129.693 166.669 1.00 93.19  ? 348  VAL B N     1 
ATOM   8247  C  CA    . VAL B 1 348 ? 168.467 130.496 167.368 1.00 89.12  ? 348  VAL B CA    1 
ATOM   8248  C  C     . VAL B 1 348 ? 167.172 130.358 166.583 1.00 86.93  ? 348  VAL B C     1 
ATOM   8249  O  O     . VAL B 1 348 ? 167.140 130.633 165.378 1.00 90.62  ? 348  VAL B O     1 
ATOM   8250  C  CB    . VAL B 1 348 ? 168.888 131.967 167.486 1.00 89.80  ? 348  VAL B CB    1 
ATOM   8251  C  CG1   . VAL B 1 348 ? 167.667 132.867 167.572 1.00 87.34  ? 348  VAL B CG1   1 
ATOM   8252  C  CG2   . VAL B 1 348 ? 169.789 132.164 168.690 1.00 96.66  ? 348  VAL B CG2   1 
ATOM   8253  N  N     . PHE B 1 349 ? 166.110 129.921 167.250 1.00 90.44  ? 349  PHE B N     1 
ATOM   8254  C  CA    . PHE B 1 349 ? 164.829 129.668 166.599 1.00 90.80  ? 349  PHE B CA    1 
ATOM   8255  C  C     . PHE B 1 349 ? 163.784 130.615 167.169 1.00 91.06  ? 349  PHE B C     1 
ATOM   8256  O  O     . PHE B 1 349 ? 163.364 130.462 168.319 1.00 95.85  ? 349  PHE B O     1 
ATOM   8257  C  CB    . PHE B 1 349 ? 164.409 128.216 166.790 1.00 93.19  ? 349  PHE B CB    1 
ATOM   8258  C  CG    . PHE B 1 349 ? 162.972 127.946 166.451 1.00 94.59  ? 349  PHE B CG    1 
ATOM   8259  C  CD1   . PHE B 1 349 ? 162.536 127.981 165.141 1.00 98.89  ? 349  PHE B CD1   1 
ATOM   8260  C  CD2   . PHE B 1 349 ? 162.061 127.634 167.442 1.00 97.44  ? 349  PHE B CD2   1 
ATOM   8261  C  CE1   . PHE B 1 349 ? 161.218 127.723 164.827 1.00 96.07  ? 349  PHE B CE1   1 
ATOM   8262  C  CE2   . PHE B 1 349 ? 160.742 127.375 167.133 1.00 96.84  ? 349  PHE B CE2   1 
ATOM   8263  C  CZ    . PHE B 1 349 ? 160.321 127.420 165.824 1.00 93.96  ? 349  PHE B CZ    1 
ATOM   8264  N  N     . ALA B 1 350 ? 163.343 131.568 166.356 1.00 93.05  ? 350  ALA B N     1 
ATOM   8265  C  CA    . ALA B 1 350 ? 162.388 132.585 166.777 1.00 94.07  ? 350  ALA B CA    1 
ATOM   8266  C  C     . ALA B 1 350 ? 161.023 132.236 166.203 1.00 97.15  ? 350  ALA B C     1 
ATOM   8267  O  O     . ALA B 1 350 ? 160.730 132.554 165.047 1.00 102.31 ? 350  ALA B O     1 
ATOM   8268  C  CB    . ALA B 1 350 ? 162.833 133.973 166.326 1.00 93.29  ? 350  ALA B CB    1 
ATOM   8269  N  N     . LEU B 1 351 ? 160.191 131.589 167.011 1.00 100.68 ? 351  LEU B N     1 
ATOM   8270  C  CA    . LEU B 1 351 ? 158.818 131.268 166.649 1.00 99.46  ? 351  LEU B CA    1 
ATOM   8271  C  C     . LEU B 1 351 ? 157.951 132.461 167.017 1.00 106.62 ? 351  LEU B C     1 
ATOM   8272  O  O     . LEU B 1 351 ? 157.879 132.837 168.191 1.00 114.10 ? 351  LEU B O     1 
ATOM   8273  C  CB    . LEU B 1 351 ? 158.341 130.010 167.372 1.00 99.39  ? 351  LEU B CB    1 
ATOM   8274  C  CG    . LEU B 1 351 ? 156.844 129.707 167.344 1.00 104.13 ? 351  LEU B CG    1 
ATOM   8275  C  CD1   . LEU B 1 351 ? 156.330 129.679 165.921 1.00 112.35 ? 351  LEU B CD1   1 
ATOM   8276  C  CD2   . LEU B 1 351 ? 156.556 128.395 168.041 1.00 110.27 ? 351  LEU B CD2   1 
ATOM   8277  N  N     . LYS B 1 352 ? 157.296 133.051 166.025 1.00 106.77 ? 352  LYS B N     1 
ATOM   8278  C  CA    . LYS B 1 352 ? 156.531 134.267 166.248 1.00 114.01 ? 352  LYS B CA    1 
ATOM   8279  C  C     . LYS B 1 352 ? 155.038 133.965 166.286 1.00 119.66 ? 352  LYS B C     1 
ATOM   8280  O  O     . LYS B 1 352 ? 154.526 133.174 165.490 1.00 122.84 ? 352  LYS B O     1 
ATOM   8281  C  CB    . LYS B 1 352 ? 156.878 135.317 165.189 1.00 111.79 ? 352  LYS B CB    1 
ATOM   8282  C  CG    . LYS B 1 352 ? 156.123 135.259 163.885 1.00 112.94 ? 352  LYS B CG    1 
ATOM   8283  C  CD    . LYS B 1 352 ? 156.465 136.484 163.055 1.00 109.36 ? 352  LYS B CD    1 
ATOM   8284  C  CE    . LYS B 1 352 ? 156.492 136.164 161.576 1.00 114.29 ? 352  LYS B CE    1 
ATOM   8285  N  NZ    . LYS B 1 352 ? 157.159 137.239 160.793 1.00 117.50 ? 352  LYS B NZ    1 
ATOM   8286  N  N     . GLU B 1 353 ? 154.354 134.586 167.250 1.00 118.95 ? 353  GLU B N     1 
ATOM   8287  C  CA    . GLU B 1 353 ? 153.012 134.151 167.623 1.00 123.35 ? 353  GLU B CA    1 
ATOM   8288  C  C     . GLU B 1 353 ? 151.998 134.435 166.523 1.00 129.52 ? 353  GLU B C     1 
ATOM   8289  O  O     . GLU B 1 353 ? 151.221 133.553 166.139 1.00 137.40 ? 353  GLU B O     1 
ATOM   8290  C  CB    . GLU B 1 353 ? 152.595 134.830 168.926 1.00 126.16 ? 353  GLU B CB    1 
ATOM   8291  C  CG    . GLU B 1 353 ? 151.328 134.274 169.541 1.00 131.94 ? 353  GLU B CG    1 
ATOM   8292  C  CD    . GLU B 1 353 ? 151.386 134.250 171.054 1.00 142.35 ? 353  GLU B CD    1 
ATOM   8293  O  OE1   . GLU B 1 353 ? 150.754 135.120 171.688 1.00 149.20 ? 353  GLU B OE1   1 
ATOM   8294  O  OE2   . GLU B 1 353 ? 152.067 133.363 171.610 1.00 138.18 ? 353  GLU B OE2   1 
ATOM   8295  N  N     . ASN B 1 354 ? 151.986 135.657 166.004 1.00 125.37 ? 354  ASN B N     1 
ATOM   8296  C  CA    . ASN B 1 354 ? 151.005 136.068 165.014 1.00 127.07 ? 354  ASN B CA    1 
ATOM   8297  C  C     . ASN B 1 354 ? 151.570 135.888 163.612 1.00 128.82 ? 354  ASN B C     1 
ATOM   8298  O  O     . ASN B 1 354 ? 152.715 136.253 163.334 1.00 130.52 ? 354  ASN B O     1 
ATOM   8299  C  CB    . ASN B 1 354 ? 150.585 137.524 165.224 1.00 128.49 ? 354  ASN B CB    1 
ATOM   8300  C  CG    . ASN B 1 354 ? 149.628 137.691 166.385 1.00 136.36 ? 354  ASN B CG    1 
ATOM   8301  O  OD1   . ASN B 1 354 ? 148.595 137.027 166.453 1.00 138.80 ? 354  ASN B OD1   1 
ATOM   8302  N  ND2   . ASN B 1 354 ? 149.968 138.583 167.309 1.00 143.37 ? 354  ASN B ND2   1 
ATOM   8303  N  N     . LYS B 1 355 ? 150.751 135.318 162.733 1.00 128.54 ? 355  LYS B N     1 
ATOM   8304  C  CA    . LYS B 1 355 ? 151.177 135.087 161.361 1.00 123.95 ? 355  LYS B CA    1 
ATOM   8305  C  C     . LYS B 1 355 ? 151.451 136.408 160.657 1.00 124.94 ? 355  LYS B C     1 
ATOM   8306  O  O     . LYS B 1 355 ? 150.719 137.387 160.824 1.00 129.84 ? 355  LYS B O     1 
ATOM   8307  C  CB    . LYS B 1 355 ? 150.116 134.301 160.593 1.00 128.32 ? 355  LYS B CB    1 
ATOM   8308  C  CG    . LYS B 1 355 ? 150.519 133.982 159.164 1.00 128.74 ? 355  LYS B CG    1 
ATOM   8309  C  CD    . LYS B 1 355 ? 149.363 133.416 158.365 1.00 136.30 ? 355  LYS B CD    1 
ATOM   8310  C  CE    . LYS B 1 355 ? 149.775 133.168 156.926 1.00 129.63 ? 355  LYS B CE    1 
ATOM   8311  N  NZ    . LYS B 1 355 ? 150.375 134.386 156.315 1.00 124.46 ? 355  LYS B NZ    1 
ATOM   8312  N  N     . ALA B 1 356 ? 152.519 136.429 159.868 1.00 123.24 ? 356  ALA B N     1 
ATOM   8313  C  CA    . ALA B 1 356 ? 152.899 137.607 159.108 1.00 122.39 ? 356  ALA B CA    1 
ATOM   8314  C  C     . ALA B 1 356 ? 153.550 137.146 157.812 1.00 125.12 ? 356  ALA B C     1 
ATOM   8315  O  O     . ALA B 1 356 ? 153.397 135.996 157.391 1.00 129.67 ? 356  ALA B O     1 
ATOM   8316  C  CB    . ALA B 1 356 ? 153.822 138.513 159.924 1.00 119.30 ? 356  ALA B CB    1 
ATOM   8317  N  N     . SER B 1 357 ? 154.272 138.055 157.170 1.00 121.27 ? 357  SER B N     1 
ATOM   8318  C  CA    . SER B 1 357 ? 154.880 137.737 155.891 1.00 121.22 ? 357  SER B CA    1 
ATOM   8319  C  C     . SER B 1 357 ? 156.359 137.395 156.053 1.00 119.81 ? 357  SER B C     1 
ATOM   8320  O  O     . SER B 1 357 ? 156.974 137.633 157.098 1.00 119.37 ? 357  SER B O     1 
ATOM   8321  C  CB    . SER B 1 357 ? 154.715 138.904 154.919 1.00 124.03 ? 357  SER B CB    1 
ATOM   8322  O  OG    . SER B 1 357 ? 154.760 140.142 155.605 1.00 126.37 ? 357  SER B OG    1 
ATOM   8323  N  N     . LYS B 1 358 ? 156.925 136.818 154.990 1.00 117.30 ? 358  LYS B N     1 
ATOM   8324  C  CA    . LYS B 1 358 ? 158.368 136.616 154.941 1.00 112.45 ? 358  LYS B CA    1 
ATOM   8325  C  C     . LYS B 1 358 ? 159.106 137.934 155.099 1.00 115.81 ? 358  LYS B C     1 
ATOM   8326  O  O     . LYS B 1 358 ? 160.211 137.969 155.653 1.00 119.74 ? 358  LYS B O     1 
ATOM   8327  C  CB    . LYS B 1 358 ? 158.756 135.940 153.626 1.00 114.46 ? 358  LYS B CB    1 
ATOM   8328  C  CG    . LYS B 1 358 ? 160.246 135.713 153.449 1.00 112.65 ? 358  LYS B CG    1 
ATOM   8329  C  CD    . LYS B 1 358 ? 160.554 135.181 152.061 1.00 119.28 ? 358  LYS B CD    1 
ATOM   8330  C  CE    . LYS B 1 358 ? 162.038 134.920 151.885 1.00 121.45 ? 358  LYS B CE    1 
ATOM   8331  N  NZ    . LYS B 1 358 ? 162.349 134.382 150.534 1.00 129.53 ? 358  LYS B NZ    1 
ATOM   8332  N  N     . LEU B 1 359 ? 158.504 139.030 154.636 1.00 116.68 ? 359  LEU B N     1 
ATOM   8333  C  CA    . LEU B 1 359 ? 159.083 140.344 154.875 1.00 113.05 ? 359  LEU B CA    1 
ATOM   8334  C  C     . LEU B 1 359 ? 159.150 140.653 156.363 1.00 114.54 ? 359  LEU B C     1 
ATOM   8335  O  O     . LEU B 1 359 ? 160.142 141.214 156.831 1.00 117.31 ? 359  LEU B O     1 
ATOM   8336  C  CB    . LEU B 1 359 ? 158.278 141.415 154.144 1.00 113.90 ? 359  LEU B CB    1 
ATOM   8337  C  CG    . LEU B 1 359 ? 158.899 142.809 154.140 1.00 113.40 ? 359  LEU B CG    1 
ATOM   8338  C  CD1   . LEU B 1 359 ? 160.352 142.714 153.735 1.00 111.80 ? 359  LEU B CD1   1 
ATOM   8339  C  CD2   . LEU B 1 359 ? 158.141 143.731 153.205 1.00 125.46 ? 359  LEU B CD2   1 
ATOM   8340  N  N     . ASP B 1 360 ? 158.119 140.281 157.124 1.00 114.39 ? 360  ASP B N     1 
ATOM   8341  C  CA    . ASP B 1 360 ? 158.151 140.502 158.568 1.00 114.80 ? 360  ASP B CA    1 
ATOM   8342  C  C     . ASP B 1 360 ? 159.158 139.582 159.248 1.00 113.18 ? 360  ASP B C     1 
ATOM   8343  O  O     . ASP B 1 360 ? 159.812 139.978 160.222 1.00 114.33 ? 360  ASP B O     1 
ATOM   8344  C  CB    . ASP B 1 360 ? 156.758 140.305 159.159 1.00 118.78 ? 360  ASP B CB    1 
ATOM   8345  C  CG    . ASP B 1 360 ? 156.545 141.101 160.430 1.00 121.38 ? 360  ASP B CG    1 
ATOM   8346  O  OD1   . ASP B 1 360 ? 157.519 141.300 161.183 1.00 119.72 ? 360  ASP B OD1   1 
ATOM   8347  O  OD2   . ASP B 1 360 ? 155.399 141.531 160.676 1.00 125.83 ? 360  ASP B OD2   1 
ATOM   8348  N  N     . SER B 1 361 ? 159.285 138.347 158.763 1.00 113.84 ? 361  SER B N     1 
ATOM   8349  C  CA    . SER B 1 361 ? 160.308 137.456 159.301 1.00 111.06 ? 361  SER B CA    1 
ATOM   8350  C  C     . SER B 1 361 ? 161.699 138.038 159.091 1.00 108.82 ? 361  SER B C     1 
ATOM   8351  O  O     . SER B 1 361 ? 162.532 138.030 160.007 1.00 112.37 ? 361  SER B O     1 
ATOM   8352  C  CB    . SER B 1 361 ? 160.198 136.077 158.654 1.00 111.81 ? 361  SER B CB    1 
ATOM   8353  O  OG    . SER B 1 361 ? 158.914 135.521 158.861 1.00 114.69 ? 361  SER B OG    1 
ATOM   8354  N  N     . HIS B 1 362 ? 161.964 138.560 157.892 1.00 106.20 ? 362  HIS B N     1 
ATOM   8355  C  CA    . HIS B 1 362 ? 163.239 139.222 157.643 1.00 104.09 ? 362  HIS B CA    1 
ATOM   8356  C  C     . HIS B 1 362 ? 163.375 140.490 158.471 1.00 106.41 ? 362  HIS B C     1 
ATOM   8357  O  O     . HIS B 1 362 ? 164.481 140.842 158.885 1.00 108.43 ? 362  HIS B O     1 
ATOM   8358  C  CB    . HIS B 1 362 ? 163.399 139.535 156.158 1.00 105.67 ? 362  HIS B CB    1 
ATOM   8359  C  CG    . HIS B 1 362 ? 163.758 138.346 155.329 1.00 104.43 ? 362  HIS B CG    1 
ATOM   8360  N  ND1   . HIS B 1 362 ? 163.738 138.366 153.952 1.00 107.65 ? 362  HIS B ND1   1 
ATOM   8361  C  CD2   . HIS B 1 362 ? 164.146 137.099 155.682 1.00 101.01 ? 362  HIS B CD2   1 
ATOM   8362  C  CE1   . HIS B 1 362 ? 164.100 137.182 153.492 1.00 109.29 ? 362  HIS B CE1   1 
ATOM   8363  N  NE2   . HIS B 1 362 ? 164.350 136.394 154.522 1.00 107.58 ? 362  HIS B NE2   1 
ATOM   8364  N  N     . HIS B 1 363 ? 162.270 141.194 158.716 1.00 109.18 ? 363  HIS B N     1 
ATOM   8365  C  CA    . HIS B 1 363 ? 162.316 142.358 159.593 1.00 111.23 ? 363  HIS B CA    1 
ATOM   8366  C  C     . HIS B 1 363 ? 162.840 141.971 160.963 1.00 109.62 ? 363  HIS B C     1 
ATOM   8367  O  O     . HIS B 1 363 ? 163.824 142.541 161.452 1.00 110.28 ? 363  HIS B O     1 
ATOM   8368  C  CB    . HIS B 1 363 ? 160.924 142.981 159.706 1.00 111.35 ? 363  HIS B CB    1 
ATOM   8369  C  CG    . HIS B 1 363 ? 160.905 144.314 160.386 1.00 112.12 ? 363  HIS B CG    1 
ATOM   8370  N  ND1   . HIS B 1 363 ? 162.047 144.938 160.841 1.00 114.71 ? 363  HIS B ND1   1 
ATOM   8371  C  CD2   . HIS B 1 363 ? 159.879 145.143 160.689 1.00 114.70 ? 363  HIS B CD2   1 
ATOM   8372  C  CE1   . HIS B 1 363 ? 161.724 146.093 161.393 1.00 118.14 ? 363  HIS B CE1   1 
ATOM   8373  N  NE2   . HIS B 1 363 ? 160.415 146.242 161.314 1.00 119.63 ? 363  HIS B NE2   1 
ATOM   8374  N  N     . TRP B 1 364 ? 162.222 140.961 161.574 1.00 108.71 ? 364  TRP B N     1 
ATOM   8375  C  CA    . TRP B 1 364 ? 162.675 140.500 162.879 1.00 106.24 ? 364  TRP B CA    1 
ATOM   8376  C  C     . TRP B 1 364 ? 164.137 140.087 162.820 1.00 106.30 ? 364  TRP B C     1 
ATOM   8377  O  O     . TRP B 1 364 ? 164.979 140.633 163.545 1.00 110.35 ? 364  TRP B O     1 
ATOM   8378  C  CB    . TRP B 1 364 ? 161.814 139.332 163.353 1.00 103.82 ? 364  TRP B CB    1 
ATOM   8379  C  CG    . TRP B 1 364 ? 160.746 139.743 164.291 1.00 110.79 ? 364  TRP B CG    1 
ATOM   8380  C  CD1   . TRP B 1 364 ? 159.436 139.965 163.993 1.00 117.58 ? 364  TRP B CD1   1 
ATOM   8381  C  CD2   . TRP B 1 364 ? 160.897 140.034 165.681 1.00 113.27 ? 364  TRP B CD2   1 
ATOM   8382  N  NE1   . TRP B 1 364 ? 158.754 140.352 165.118 1.00 117.61 ? 364  TRP B NE1   1 
ATOM   8383  C  CE2   . TRP B 1 364 ? 159.631 140.405 166.168 1.00 117.81 ? 364  TRP B CE2   1 
ATOM   8384  C  CE3   . TRP B 1 364 ? 161.979 140.007 166.564 1.00 113.51 ? 364  TRP B CE3   1 
ATOM   8385  C  CZ2   . TRP B 1 364 ? 159.417 140.745 167.497 1.00 121.18 ? 364  TRP B CZ2   1 
ATOM   8386  C  CZ3   . TRP B 1 364 ? 161.764 140.346 167.882 1.00 118.72 ? 364  TRP B CZ3   1 
ATOM   8387  C  CH2   . TRP B 1 364 ? 160.494 140.711 168.336 1.00 122.72 ? 364  TRP B CH2   1 
ATOM   8388  N  N     . TYR B 1 365 ? 164.464 139.186 161.892 1.00 103.56 ? 365  TYR B N     1 
ATOM   8389  C  CA    . TYR B 1 365 ? 165.817 138.656 161.779 1.00 100.72 ? 365  TYR B CA    1 
ATOM   8390  C  C     . TYR B 1 365 ? 166.836 139.776 161.636 1.00 101.36 ? 365  TYR B C     1 
ATOM   8391  O  O     . TYR B 1 365 ? 167.637 140.025 162.546 1.00 107.39 ? 365  TYR B O     1 
ATOM   8392  C  CB    . TYR B 1 365 ? 165.873 137.703 160.585 1.00 101.47 ? 365  TYR B CB    1 
ATOM   8393  C  CG    . TYR B 1 365 ? 167.248 137.404 160.048 1.00 99.04  ? 365  TYR B CG    1 
ATOM   8394  C  CD1   . TYR B 1 365 ? 168.189 136.740 160.815 1.00 99.45  ? 365  TYR B CD1   1 
ATOM   8395  C  CD2   . TYR B 1 365 ? 167.596 137.770 158.758 1.00 99.68  ? 365  TYR B CD2   1 
ATOM   8396  C  CE1   . TYR B 1 365 ? 169.439 136.459 160.314 1.00 93.61  ? 365  TYR B CE1   1 
ATOM   8397  C  CE2   . TYR B 1 365 ? 168.840 137.497 158.252 1.00 96.91  ? 365  TYR B CE2   1 
ATOM   8398  C  CZ    . TYR B 1 365 ? 169.756 136.841 159.033 1.00 91.62  ? 365  TYR B CZ    1 
ATOM   8399  O  OH    . TYR B 1 365 ? 170.996 136.560 158.526 1.00 92.84  ? 365  TYR B OH    1 
ATOM   8400  N  N     . PHE B 1 366 ? 166.765 140.512 160.526 1.00 100.77 ? 366  PHE B N     1 
ATOM   8401  C  CA    . PHE B 1 366 ? 167.706 141.579 160.232 1.00 104.13 ? 366  PHE B CA    1 
ATOM   8402  C  C     . PHE B 1 366 ? 167.756 142.564 161.383 1.00 110.04 ? 366  PHE B C     1 
ATOM   8403  O  O     . PHE B 1 366 ? 168.753 142.589 162.108 1.00 115.10 ? 366  PHE B O     1 
ATOM   8404  C  CB    . PHE B 1 366 ? 167.312 142.302 158.943 1.00 100.97 ? 366  PHE B CB    1 
ATOM   8405  C  CG    . PHE B 1 366 ? 167.857 141.669 157.702 1.00 99.92  ? 366  PHE B CG    1 
ATOM   8406  C  CD1   . PHE B 1 366 ? 169.208 141.724 157.418 1.00 102.84 ? 366  PHE B CD1   1 
ATOM   8407  C  CD2   . PHE B 1 366 ? 167.019 141.018 156.816 1.00 103.10 ? 366  PHE B CD2   1 
ATOM   8408  C  CE1   . PHE B 1 366 ? 169.710 141.145 156.277 1.00 102.60 ? 366  PHE B CE1   1 
ATOM   8409  C  CE2   . PHE B 1 366 ? 167.519 140.434 155.674 1.00 104.51 ? 366  PHE B CE2   1 
ATOM   8410  C  CZ    . PHE B 1 366 ? 168.866 140.498 155.404 1.00 103.47 ? 366  PHE B CZ    1 
ATOM   8411  N  N     . ASN B 1 367 ? 166.664 143.294 161.629 1.00 107.75 ? 367  ASN B N     1 
ATOM   8412  C  CA    . ASN B 1 367 ? 166.721 144.372 162.603 1.00 107.79 ? 367  ASN B CA    1 
ATOM   8413  C  C     . ASN B 1 367 ? 167.218 143.854 163.945 1.00 113.41 ? 367  ASN B C     1 
ATOM   8414  O  O     . ASN B 1 367 ? 168.342 144.176 164.338 1.00 120.76 ? 367  ASN B O     1 
ATOM   8415  C  CB    . ASN B 1 367 ? 165.352 145.034 162.746 1.00 108.29 ? 367  ASN B CB    1 
ATOM   8416  C  CG    . ASN B 1 367 ? 165.128 146.127 161.723 1.00 111.08 ? 367  ASN B CG    1 
ATOM   8417  O  OD1   . ASN B 1 367 ? 164.698 145.862 160.602 1.00 112.47 ? 367  ASN B OD1   1 
ATOM   8418  N  ND2   . ASN B 1 367 ? 165.425 147.362 162.101 1.00 112.84 ? 367  ASN B ND2   1 
ATOM   8419  N  N     . ALA B 1 368 ? 166.459 142.973 164.603 1.00 107.87 ? 368  ALA B N     1 
ATOM   8420  C  CA    . ALA B 1 368 ? 166.827 142.565 165.953 1.00 106.39 ? 368  ALA B CA    1 
ATOM   8421  C  C     . ALA B 1 368 ? 168.210 141.922 165.984 1.00 111.76 ? 368  ALA B C     1 
ATOM   8422  O  O     . ALA B 1 368 ? 169.154 142.473 166.569 1.00 118.24 ? 368  ALA B O     1 
ATOM   8423  C  CB    . ALA B 1 368 ? 165.773 141.609 166.509 1.00 106.35 ? 368  ALA B CB    1 
ATOM   8424  N  N     . PHE B 1 369 ? 168.360 140.761 165.341 1.00 108.10 ? 369  PHE B N     1 
ATOM   8425  C  CA    . PHE B 1 369 ? 169.555 139.965 165.583 1.00 107.43 ? 369  PHE B CA    1 
ATOM   8426  C  C     . PHE B 1 369 ? 170.786 140.598 164.944 1.00 110.18 ? 369  PHE B C     1 
ATOM   8427  O  O     . PHE B 1 369 ? 171.872 140.596 165.542 1.00 112.51 ? 369  PHE B O     1 
ATOM   8428  C  CB    . PHE B 1 369 ? 169.333 138.545 165.071 1.00 108.45 ? 369  PHE B CB    1 
ATOM   8429  C  CG    . PHE B 1 369 ? 168.055 137.921 165.562 1.00 107.70 ? 369  PHE B CG    1 
ATOM   8430  C  CD1   . PHE B 1 369 ? 167.574 138.195 166.829 1.00 106.39 ? 369  PHE B CD1   1 
ATOM   8431  C  CD2   . PHE B 1 369 ? 167.325 137.074 164.749 1.00 104.75 ? 369  PHE B CD2   1 
ATOM   8432  C  CE1   . PHE B 1 369 ? 166.397 137.631 167.275 1.00 107.82 ? 369  PHE B CE1   1 
ATOM   8433  C  CE2   . PHE B 1 369 ? 166.147 136.506 165.193 1.00 98.33  ? 369  PHE B CE2   1 
ATOM   8434  C  CZ    . PHE B 1 369 ? 165.684 136.786 166.457 1.00 100.87 ? 369  PHE B CZ    1 
ATOM   8435  N  N     . ALA B 1 370 ? 170.656 141.113 163.715 1.00 108.39 ? 370  ALA B N     1 
ATOM   8436  C  CA    . ALA B 1 370 ? 171.785 141.773 163.082 1.00 112.39 ? 370  ALA B CA    1 
ATOM   8437  C  C     . ALA B 1 370 ? 172.204 143.017 163.854 1.00 117.96 ? 370  ALA B C     1 
ATOM   8438  O  O     . ALA B 1 370 ? 173.399 143.233 164.067 1.00 122.08 ? 370  ALA B O     1 
ATOM   8439  C  CB    . ALA B 1 370 ? 171.437 142.123 161.638 1.00 109.67 ? 370  ALA B CB    1 
ATOM   8440  N  N     . GLU B 1 371 ? 171.252 143.843 164.303 1.00 115.73 ? 371  GLU B N     1 
ATOM   8441  C  CA    . GLU B 1 371 ? 171.633 145.026 165.062 1.00 117.22 ? 371  GLU B CA    1 
ATOM   8442  C  C     . GLU B 1 371 ? 172.258 144.643 166.395 1.00 119.88 ? 371  GLU B C     1 
ATOM   8443  O  O     . GLU B 1 371 ? 173.036 145.415 166.966 1.00 127.56 ? 371  GLU B O     1 
ATOM   8444  C  CB    . GLU B 1 371 ? 170.416 145.925 165.275 1.00 115.60 ? 371  GLU B CB    1 
ATOM   8445  C  CG    . GLU B 1 371 ? 170.105 146.836 164.102 1.00 120.99 ? 371  GLU B CG    1 
ATOM   8446  C  CD    . GLU B 1 371 ? 171.106 147.962 163.952 1.00 130.65 ? 371  GLU B CD    1 
ATOM   8447  O  OE1   . GLU B 1 371 ? 171.845 148.239 164.919 1.00 135.94 ? 371  GLU B OE1   1 
ATOM   8448  O  OE2   . GLU B 1 371 ? 171.152 148.574 162.865 1.00 131.71 ? 371  GLU B OE2   1 
ATOM   8449  N  N     . GLN B 1 372 ? 171.935 143.455 166.910 1.00 113.84 ? 372  GLN B N     1 
ATOM   8450  C  CA    . GLN B 1 372 ? 172.545 143.037 168.167 1.00 114.27 ? 372  GLN B CA    1 
ATOM   8451  C  C     . GLN B 1 372 ? 173.980 142.564 167.970 1.00 118.18 ? 372  GLN B C     1 
ATOM   8452  O  O     . GLN B 1 372 ? 174.919 143.168 168.499 1.00 126.60 ? 372  GLN B O     1 
ATOM   8453  C  CB    . GLN B 1 372 ? 171.719 141.940 168.829 1.00 111.35 ? 372  GLN B CB    1 
ATOM   8454  C  CG    . GLN B 1 372 ? 172.162 141.681 170.249 1.00 112.86 ? 372  GLN B CG    1 
ATOM   8455  C  CD    . GLN B 1 372 ? 171.018 141.360 171.163 1.00 123.03 ? 372  GLN B CD    1 
ATOM   8456  O  OE1   . GLN B 1 372 ? 169.858 141.502 170.792 1.00 121.45 ? 372  GLN B OE1   1 
ATOM   8457  N  NE2   . GLN B 1 372 ? 171.335 140.933 172.374 1.00 131.00 ? 372  GLN B NE2   1 
ATOM   8458  N  N     . ILE B 1 373 ? 174.177 141.483 167.212 1.00 112.98 ? 373  ILE B N     1 
ATOM   8459  C  CA    . ILE B 1 373 ? 175.503 140.862 167.212 1.00 112.32 ? 373  ILE B CA    1 
ATOM   8460  C  C     . ILE B 1 373 ? 176.387 141.447 166.117 1.00 113.80 ? 373  ILE B C     1 
ATOM   8461  O  O     . ILE B 1 373 ? 177.613 141.287 166.148 1.00 117.64 ? 373  ILE B O     1 
ATOM   8462  C  CB    . ILE B 1 373 ? 175.412 139.329 167.110 1.00 106.18 ? 373  ILE B CB    1 
ATOM   8463  C  CG1   . ILE B 1 373 ? 174.309 138.890 166.162 1.00 104.29 ? 373  ILE B CG1   1 
ATOM   8464  C  CG2   . ILE B 1 373 ? 175.191 138.713 168.477 1.00 112.97 ? 373  ILE B CG2   1 
ATOM   8465  C  CD1   . ILE B 1 373 ? 174.140 137.397 166.135 1.00 100.94 ? 373  ILE B CD1   1 
ATOM   8466  N  N     . GLN B 1 374 ? 175.792 142.127 165.141 1.00 113.36 ? 374  GLN B N     1 
ATOM   8467  C  CA    . GLN B 1 374 ? 176.504 142.837 164.087 1.00 113.45 ? 374  GLN B CA    1 
ATOM   8468  C  C     . GLN B 1 374 ? 177.437 141.898 163.333 1.00 109.40 ? 374  GLN B C     1 
ATOM   8469  O  O     . GLN B 1 374 ? 178.662 141.980 163.488 1.00 108.63 ? 374  GLN B O     1 
ATOM   8470  C  CB    . GLN B 1 374 ? 177.279 144.020 164.665 1.00 118.64 ? 374  GLN B CB    1 
ATOM   8471  C  CG    . GLN B 1 374 ? 177.247 145.241 163.778 1.00 119.99 ? 374  GLN B CG    1 
ATOM   8472  C  CD    . GLN B 1 374 ? 176.133 146.186 164.165 1.00 122.90 ? 374  GLN B CD    1 
ATOM   8473  O  OE1   . GLN B 1 374 ? 175.883 146.416 165.346 1.00 122.81 ? 374  GLN B OE1   1 
ATOM   8474  N  NE2   . GLN B 1 374 ? 175.437 146.716 163.171 1.00 124.29 ? 374  GLN B NE2   1 
ATOM   8475  N  N     . PRO B 1 375 ? 176.901 140.999 162.524 1.00 105.79 ? 375  PRO B N     1 
ATOM   8476  C  CA    . PRO B 1 375 ? 177.741 140.068 161.772 1.00 104.90 ? 375  PRO B CA    1 
ATOM   8477  C  C     . PRO B 1 375 ? 178.481 140.809 160.666 1.00 107.00 ? 375  PRO B C     1 
ATOM   8478  O  O     . PRO B 1 375 ? 178.154 141.938 160.312 1.00 112.53 ? 375  PRO B O     1 
ATOM   8479  C  CB    . PRO B 1 375 ? 176.727 139.078 161.206 1.00 101.15 ? 375  PRO B CB    1 
ATOM   8480  C  CG    . PRO B 1 375 ? 175.513 139.900 161.007 1.00 104.58 ? 375  PRO B CG    1 
ATOM   8481  C  CD    . PRO B 1 375 ? 175.484 140.879 162.148 1.00 106.86 ? 375  PRO B CD    1 
ATOM   8482  N  N     . GLU B 1 376 ? 179.498 140.149 160.120 1.00 105.10 ? 376  GLU B N     1 
ATOM   8483  C  CA    . GLU B 1 376 ? 180.249 140.698 159.001 1.00 100.30 ? 376  GLU B CA    1 
ATOM   8484  C  C     . GLU B 1 376 ? 179.576 140.390 157.672 1.00 99.36  ? 376  GLU B C     1 
ATOM   8485  O  O     . GLU B 1 376 ? 179.470 141.268 156.811 1.00 109.16 ? 376  GLU B O     1 
ATOM   8486  C  CB    . GLU B 1 376 ? 181.683 140.158 159.014 1.00 106.71 ? 376  GLU B CB    1 
ATOM   8487  C  CG    . GLU B 1 376 ? 182.582 140.759 157.951 1.00 113.22 ? 376  GLU B CG    1 
ATOM   8488  C  CD    . GLU B 1 376 ? 184.026 140.324 158.098 1.00 123.54 ? 376  GLU B CD    1 
ATOM   8489  O  OE1   . GLU B 1 376 ? 184.338 139.609 159.073 1.00 125.00 ? 376  GLU B OE1   1 
ATOM   8490  O  OE2   . GLU B 1 376 ? 184.851 140.696 157.236 1.00 120.29 ? 376  GLU B OE2   1 
ATOM   8491  N  N     . TYR B 1 377 ? 179.107 139.159 157.496 1.00 94.78  ? 377  TYR B N     1 
ATOM   8492  C  CA    . TYR B 1 377 ? 178.296 138.765 156.356 1.00 91.33  ? 377  TYR B CA    1 
ATOM   8493  C  C     . TYR B 1 377 ? 176.961 138.230 156.853 1.00 88.62  ? 377  TYR B C     1 
ATOM   8494  O  O     . TYR B 1 377 ? 176.881 137.608 157.914 1.00 96.38  ? 377  TYR B O     1 
ATOM   8495  C  CB    . TYR B 1 377 ? 178.996 137.702 155.503 1.00 90.55  ? 377  TYR B CB    1 
ATOM   8496  C  CG    . TYR B 1 377 ? 180.454 137.983 155.246 1.00 93.90  ? 377  TYR B CG    1 
ATOM   8497  C  CD1   . TYR B 1 377 ? 180.877 139.238 154.844 1.00 99.54  ? 377  TYR B CD1   1 
ATOM   8498  C  CD2   . TYR B 1 377 ? 181.411 136.999 155.423 1.00 102.88 ? 377  TYR B CD2   1 
ATOM   8499  C  CE1   . TYR B 1 377 ? 182.206 139.503 154.612 1.00 107.08 ? 377  TYR B CE1   1 
ATOM   8500  C  CE2   . TYR B 1 377 ? 182.746 137.254 155.195 1.00 108.41 ? 377  TYR B CE2   1 
ATOM   8501  C  CZ    . TYR B 1 377 ? 183.136 138.509 154.790 1.00 110.69 ? 377  TYR B CZ    1 
ATOM   8502  O  OH    . TYR B 1 377 ? 184.464 138.777 154.561 1.00 117.52 ? 377  TYR B OH    1 
ATOM   8503  N  N     . THR B 1 378 ? 175.910 138.483 156.080 1.00 85.77  ? 378  THR B N     1 
ATOM   8504  C  CA    . THR B 1 378 ? 174.559 138.063 156.438 1.00 84.02  ? 378  THR B CA    1 
ATOM   8505  C  C     . THR B 1 378 ? 173.978 137.282 155.270 1.00 86.87  ? 378  THR B C     1 
ATOM   8506  O  O     . THR B 1 378 ? 173.821 137.829 154.175 1.00 93.38  ? 378  THR B O     1 
ATOM   8507  C  CB    . THR B 1 378 ? 173.682 139.263 156.781 1.00 88.61  ? 378  THR B CB    1 
ATOM   8508  O  OG1   . THR B 1 378 ? 174.088 139.809 158.040 1.00 94.47  ? 378  THR B OG1   1 
ATOM   8509  C  CG2   . THR B 1 378 ? 172.233 138.854 156.858 1.00 83.69  ? 378  THR B CG2   1 
ATOM   8510  N  N     . ALA B 1 379 ? 173.655 136.014 155.502 1.00 86.28  ? 379  ALA B N     1 
ATOM   8511  C  CA    . ALA B 1 379 ? 173.142 135.126 154.471 1.00 84.43  ? 379  ALA B CA    1 
ATOM   8512  C  C     . ALA B 1 379 ? 171.682 134.800 154.744 1.00 85.44  ? 379  ALA B C     1 
ATOM   8513  O  O     . ALA B 1 379 ? 171.274 134.660 155.899 1.00 92.05  ? 379  ALA B O     1 
ATOM   8514  C  CB    . ALA B 1 379 ? 173.958 133.835 154.400 1.00 83.17  ? 379  ALA B CB    1 
ATOM   8515  N  N     . VAL B 1 380 ? 170.897 134.689 153.677 1.00 84.69  ? 380  VAL B N     1 
ATOM   8516  C  CA    . VAL B 1 380 ? 169.473 134.396 153.771 1.00 84.17  ? 380  VAL B CA    1 
ATOM   8517  C  C     . VAL B 1 380 ? 169.132 133.280 152.797 1.00 92.78  ? 380  VAL B C     1 
ATOM   8518  O  O     . VAL B 1 380 ? 169.421 133.388 151.600 1.00 99.21  ? 380  VAL B O     1 
ATOM   8519  C  CB    . VAL B 1 380 ? 168.614 135.639 153.477 1.00 85.39  ? 380  VAL B CB    1 
ATOM   8520  C  CG1   . VAL B 1 380 ? 167.152 135.261 153.454 1.00 92.07  ? 380  VAL B CG1   1 
ATOM   8521  C  CG2   . VAL B 1 380 ? 168.869 136.714 154.512 1.00 88.52  ? 380  VAL B CG2   1 
ATOM   8522  N  N     . MET B 1 381 ? 168.513 132.217 153.303 1.00 93.93  ? 381  MET B N     1 
ATOM   8523  C  CA    . MET B 1 381 ? 167.962 131.185 152.440 1.00 97.54  ? 381  MET B CA    1 
ATOM   8524  C  C     . MET B 1 381 ? 166.625 130.731 153.002 1.00 102.17 ? 381  MET B C     1 
ATOM   8525  O  O     . MET B 1 381 ? 166.347 130.877 154.193 1.00 107.75 ? 381  MET B O     1 
ATOM   8526  C  CB    . MET B 1 381 ? 168.901 129.981 152.281 1.00 96.90  ? 381  MET B CB    1 
ATOM   8527  C  CG    . MET B 1 381 ? 168.678 128.872 153.292 1.00 92.76  ? 381  MET B CG    1 
ATOM   8528  S  SD    . MET B 1 381 ? 170.027 127.681 153.366 1.00 101.02 ? 381  MET B SD    1 
ATOM   8529  C  CE    . MET B 1 381 ? 171.238 128.576 154.311 1.00 95.21  ? 381  MET B CE    1 
ATOM   8530  N  N     . ASP B 1 382 ? 165.797 130.179 152.123 1.00 105.77 ? 382  ASP B N     1 
ATOM   8531  C  CA    . ASP B 1 382 ? 164.495 129.660 152.509 1.00 108.56 ? 382  ASP B CA    1 
ATOM   8532  C  C     . ASP B 1 382 ? 164.671 128.289 153.156 1.00 110.23 ? 382  ASP B C     1 
ATOM   8533  O  O     . ASP B 1 382 ? 165.786 127.791 153.315 1.00 112.94 ? 382  ASP B O     1 
ATOM   8534  C  CB    . ASP B 1 382 ? 163.574 129.595 151.295 1.00 115.12 ? 382  ASP B CB    1 
ATOM   8535  C  CG    . ASP B 1 382 ? 163.119 130.961 150.840 1.00 127.29 ? 382  ASP B CG    1 
ATOM   8536  O  OD1   . ASP B 1 382 ? 163.633 131.967 151.371 1.00 132.34 ? 382  ASP B OD1   1 
ATOM   8537  O  OD2   . ASP B 1 382 ? 162.254 131.030 149.942 1.00 132.20 ? 382  ASP B OD2   1 
ATOM   8538  N  N     . VAL B 1 383 ? 163.567 127.659 153.530 1.00 111.55 ? 383  VAL B N     1 
ATOM   8539  C  CA    . VAL B 1 383 ? 163.585 126.331 154.128 1.00 111.75 ? 383  VAL B CA    1 
ATOM   8540  C  C     . VAL B 1 383 ? 163.444 125.305 153.015 1.00 117.20 ? 383  VAL B C     1 
ATOM   8541  O  O     . VAL B 1 383 ? 162.578 125.437 152.142 1.00 123.28 ? 383  VAL B O     1 
ATOM   8542  C  CB    . VAL B 1 383 ? 162.470 126.180 155.174 1.00 110.02 ? 383  VAL B CB    1 
ATOM   8543  C  CG1   . VAL B 1 383 ? 161.153 126.648 154.597 1.00 114.41 ? 383  VAL B CG1   1 
ATOM   8544  C  CG2   . VAL B 1 383 ? 162.372 124.741 155.639 1.00 112.03 ? 383  VAL B CG2   1 
ATOM   8545  N  N     . GLY B 1 384 ? 164.310 124.297 153.026 1.00 112.16 ? 384  GLY B N     1 
ATOM   8546  C  CA    . GLY B 1 384 ? 164.301 123.273 152.008 1.00 108.71 ? 384  GLY B CA    1 
ATOM   8547  C  C     . GLY B 1 384 ? 165.386 123.411 150.964 1.00 105.11 ? 384  GLY B C     1 
ATOM   8548  O  O     . GLY B 1 384 ? 165.460 122.569 150.062 1.00 110.48 ? 384  GLY B O     1 
ATOM   8549  N  N     . THR B 1 385 ? 166.213 124.449 151.045 1.00 101.13 ? 385  THR B N     1 
ATOM   8550  C  CA    . THR B 1 385 ? 167.310 124.621 150.100 1.00 102.66 ? 385  THR B CA    1 
ATOM   8551  C  C     . THR B 1 385 ? 168.532 123.870 150.609 1.00 101.62 ? 385  THR B C     1 
ATOM   8552  O  O     . THR B 1 385 ? 169.098 124.222 151.648 1.00 103.30 ? 385  THR B O     1 
ATOM   8553  C  CB    . THR B 1 385 ? 167.623 126.100 149.912 1.00 99.17  ? 385  THR B CB    1 
ATOM   8554  O  OG1   . THR B 1 385 ? 167.786 126.716 151.193 1.00 103.78 ? 385  THR B OG1   1 
ATOM   8555  C  CG2   . THR B 1 385 ? 166.496 126.792 149.171 1.00 100.95 ? 385  THR B CG2   1 
ATOM   8556  N  N     . MET B 1 386 ? 168.946 122.840 149.880 1.00 99.15  ? 386  MET B N     1 
ATOM   8557  C  CA    . MET B 1 386 ? 170.116 122.046 150.232 1.00 98.24  ? 386  MET B CA    1 
ATOM   8558  C  C     . MET B 1 386 ? 171.333 122.656 149.549 1.00 102.43 ? 386  MET B C     1 
ATOM   8559  O  O     . MET B 1 386 ? 171.333 122.856 148.331 1.00 108.73 ? 386  MET B O     1 
ATOM   8560  C  CB    . MET B 1 386 ? 169.931 120.589 149.818 1.00 101.42 ? 386  MET B CB    1 
ATOM   8561  C  CG    . MET B 1 386 ? 168.885 119.835 150.614 1.00 107.40 ? 386  MET B CG    1 
ATOM   8562  S  SD    . MET B 1 386 ? 167.228 120.049 149.949 1.00 114.03 ? 386  MET B SD    1 
ATOM   8563  C  CE    . MET B 1 386 ? 167.061 118.556 148.977 1.00 112.29 ? 386  MET B CE    1 
ATOM   8564  N  N     . LEU B 1 387 ? 172.366 122.946 150.329 1.00 100.66 ? 387  LEU B N     1 
ATOM   8565  C  CA    . LEU B 1 387 ? 173.598 123.498 149.791 1.00 98.80  ? 387  LEU B CA    1 
ATOM   8566  C  C     . LEU B 1 387 ? 174.649 122.405 149.665 1.00 102.78 ? 387  LEU B C     1 
ATOM   8567  O  O     . LEU B 1 387 ? 174.716 121.485 150.482 1.00 107.44 ? 387  LEU B O     1 
ATOM   8568  C  CB    . LEU B 1 387 ? 174.131 124.619 150.686 1.00 92.71  ? 387  LEU B CB    1 
ATOM   8569  C  CG    . LEU B 1 387 ? 173.130 125.551 151.368 1.00 88.91  ? 387  LEU B CG    1 
ATOM   8570  C  CD1   . LEU B 1 387 ? 173.865 126.608 152.167 1.00 93.23  ? 387  LEU B CD1   1 
ATOM   8571  C  CD2   . LEU B 1 387 ? 172.217 126.200 150.356 1.00 92.44  ? 387  LEU B CD2   1 
ATOM   8572  N  N     . THR B 1 388 ? 175.487 122.520 148.642 1.00 99.86  ? 388  THR B N     1 
ATOM   8573  C  CA    . THR B 1 388 ? 176.581 121.576 148.493 1.00 104.53 ? 388  THR B CA    1 
ATOM   8574  C  C     . THR B 1 388 ? 177.612 121.804 149.596 1.00 107.85 ? 388  THR B C     1 
ATOM   8575  O  O     . THR B 1 388 ? 177.481 122.701 150.433 1.00 108.75 ? 388  THR B O     1 
ATOM   8576  C  CB    . THR B 1 388 ? 177.212 121.702 147.111 1.00 106.76 ? 388  THR B CB    1 
ATOM   8577  O  OG1   . THR B 1 388 ? 177.200 123.075 146.704 1.00 106.22 ? 388  THR B OG1   1 
ATOM   8578  C  CG2   . THR B 1 388 ? 176.443 120.868 146.101 1.00 109.47 ? 388  THR B CG2   1 
ATOM   8579  N  N     . LYS B 1 389 ? 178.658 120.978 149.604 1.00 111.56 ? 389  LYS B N     1 
ATOM   8580  C  CA    . LYS B 1 389 ? 179.696 121.125 150.615 1.00 112.52 ? 389  LYS B CA    1 
ATOM   8581  C  C     . LYS B 1 389 ? 180.427 122.456 150.522 1.00 115.85 ? 389  LYS B C     1 
ATOM   8582  O  O     . LYS B 1 389 ? 181.028 122.880 151.513 1.00 117.81 ? 389  LYS B O     1 
ATOM   8583  C  CB    . LYS B 1 389 ? 180.714 119.990 150.505 1.00 112.57 ? 389  LYS B CB    1 
ATOM   8584  C  CG    . LYS B 1 389 ? 180.205 118.635 150.962 1.00 113.15 ? 389  LYS B CG    1 
ATOM   8585  C  CD    . LYS B 1 389 ? 181.333 117.609 151.052 1.00 120.54 ? 389  LYS B CD    1 
ATOM   8586  C  CE    . LYS B 1 389 ? 182.318 117.700 149.890 1.00 122.44 ? 389  LYS B CE    1 
ATOM   8587  N  NZ    . LYS B 1 389 ? 181.661 117.707 148.551 1.00 118.23 ? 389  LYS B NZ    1 
ATOM   8588  N  N     . SER B 1 390 ? 180.389 123.125 149.371 1.00 109.66 ? 390  SER B N     1 
ATOM   8589  C  CA    . SER B 1 390 ? 181.217 124.302 149.146 1.00 108.94 ? 390  SER B CA    1 
ATOM   8590  C  C     . SER B 1 390 ? 180.418 125.558 148.830 1.00 111.47 ? 390  SER B C     1 
ATOM   8591  O  O     . SER B 1 390 ? 180.995 126.527 148.328 1.00 119.56 ? 390  SER B O     1 
ATOM   8592  C  CB    . SER B 1 390 ? 182.215 124.030 148.019 1.00 111.09 ? 390  SER B CB    1 
ATOM   8593  O  OG    . SER B 1 390 ? 183.070 122.950 148.347 1.00 114.87 ? 390  SER B OG    1 
ATOM   8594  N  N     . ALA B 1 391 ? 179.113 125.580 149.106 1.00 104.89 ? 391  ALA B N     1 
ATOM   8595  C  CA    . ALA B 1 391 ? 178.336 126.788 148.846 1.00 107.41 ? 391  ALA B CA    1 
ATOM   8596  C  C     . ALA B 1 391 ? 178.787 127.936 149.741 1.00 107.38 ? 391  ALA B C     1 
ATOM   8597  O  O     . ALA B 1 391 ? 179.117 129.028 149.255 1.00 110.85 ? 391  ALA B O     1 
ATOM   8598  C  CB    . ALA B 1 391 ? 176.848 126.508 149.042 1.00 105.62 ? 391  ALA B CB    1 
ATOM   8599  N  N     . LEU B 1 392 ? 178.817 127.703 151.054 1.00 102.15 ? 392  LEU B N     1 
ATOM   8600  C  CA    . LEU B 1 392 ? 179.262 128.741 151.974 1.00 101.07 ? 392  LEU B CA    1 
ATOM   8601  C  C     . LEU B 1 392 ? 180.726 129.081 151.747 1.00 103.59 ? 392  LEU B C     1 
ATOM   8602  O  O     . LEU B 1 392 ? 181.117 130.250 151.834 1.00 105.68 ? 392  LEU B O     1 
ATOM   8603  C  CB    . LEU B 1 392 ? 179.028 128.308 153.420 1.00 95.81  ? 392  LEU B CB    1 
ATOM   8604  C  CG    . LEU B 1 392 ? 177.598 128.455 153.936 1.00 92.80  ? 392  LEU B CG    1 
ATOM   8605  C  CD1   . LEU B 1 392 ? 177.517 128.065 155.399 1.00 93.39  ? 392  LEU B CD1   1 
ATOM   8606  C  CD2   . LEU B 1 392 ? 177.108 129.873 153.731 1.00 96.49  ? 392  LEU B CD2   1 
ATOM   8607  N  N     . TYR B 1 393 ? 181.552 128.076 151.451 1.00 104.11 ? 393  TYR B N     1 
ATOM   8608  C  CA    . TYR B 1 393 ? 182.958 128.351 151.180 1.00 103.51 ? 393  TYR B CA    1 
ATOM   8609  C  C     . TYR B 1 393 ? 183.119 129.263 149.975 1.00 104.68 ? 393  TYR B C     1 
ATOM   8610  O  O     . TYR B 1 393 ? 183.911 130.207 150.005 1.00 111.15 ? 393  TYR B O     1 
ATOM   8611  C  CB    . TYR B 1 393 ? 183.738 127.061 150.958 1.00 107.02 ? 393  TYR B CB    1 
ATOM   8612  C  CG    . TYR B 1 393 ? 185.082 127.332 150.325 1.00 109.08 ? 393  TYR B CG    1 
ATOM   8613  C  CD1   . TYR B 1 393 ? 186.080 127.987 151.027 1.00 110.35 ? 393  TYR B CD1   1 
ATOM   8614  C  CD2   . TYR B 1 393 ? 185.342 126.958 149.015 1.00 111.88 ? 393  TYR B CD2   1 
ATOM   8615  C  CE1   . TYR B 1 393 ? 187.302 128.252 150.447 1.00 118.95 ? 393  TYR B CE1   1 
ATOM   8616  C  CE2   . TYR B 1 393 ? 186.564 127.216 148.429 1.00 115.52 ? 393  TYR B CE2   1 
ATOM   8617  C  CZ    . TYR B 1 393 ? 187.540 127.863 149.150 1.00 123.43 ? 393  TYR B CZ    1 
ATOM   8618  O  OH    . TYR B 1 393 ? 188.760 128.123 148.574 1.00 135.60 ? 393  TYR B OH    1 
ATOM   8619  N  N     . HIS B 1 394 ? 182.384 128.992 148.897 1.00 101.32 ? 394  HIS B N     1 
ATOM   8620  C  CA    . HIS B 1 394 ? 182.509 129.825 147.707 1.00 102.66 ? 394  HIS B CA    1 
ATOM   8621  C  C     . HIS B 1 394 ? 181.989 131.232 147.960 1.00 106.00 ? 394  HIS B C     1 
ATOM   8622  O  O     . HIS B 1 394 ? 182.598 132.212 147.513 1.00 111.65 ? 394  HIS B O     1 
ATOM   8623  C  CB    . HIS B 1 394 ? 181.787 129.176 146.529 1.00 101.74 ? 394  HIS B CB    1 
ATOM   8624  C  CG    . HIS B 1 394 ? 182.559 128.062 145.897 1.00 108.49 ? 394  HIS B CG    1 
ATOM   8625  N  ND1   . HIS B 1 394 ? 182.193 126.739 146.018 1.00 110.07 ? 394  HIS B ND1   1 
ATOM   8626  C  CD2   . HIS B 1 394 ? 183.689 128.073 145.152 1.00 112.01 ? 394  HIS B CD2   1 
ATOM   8627  C  CE1   . HIS B 1 394 ? 183.059 125.984 145.366 1.00 111.85 ? 394  HIS B CE1   1 
ATOM   8628  N  NE2   . HIS B 1 394 ? 183.977 126.769 144.832 1.00 118.27 ? 394  HIS B NE2   1 
ATOM   8629  N  N     . LEU B 1 395 ? 180.874 131.357 148.683 1.00 104.70 ? 395  LEU B N     1 
ATOM   8630  C  CA    . LEU B 1 395 ? 180.360 132.688 148.997 1.00 103.05 ? 395  LEU B CA    1 
ATOM   8631  C  C     . LEU B 1 395 ? 181.368 133.487 149.815 1.00 103.42 ? 395  LEU B C     1 
ATOM   8632  O  O     . LEU B 1 395 ? 181.660 134.650 149.504 1.00 106.35 ? 395  LEU B O     1 
ATOM   8633  C  CB    . LEU B 1 395 ? 179.031 132.577 149.738 1.00 94.15  ? 395  LEU B CB    1 
ATOM   8634  C  CG    . LEU B 1 395 ? 177.795 132.771 148.867 1.00 89.92  ? 395  LEU B CG    1 
ATOM   8635  C  CD1   . LEU B 1 395 ? 176.583 132.967 149.732 1.00 88.11  ? 395  LEU B CD1   1 
ATOM   8636  C  CD2   . LEU B 1 395 ? 177.988 133.965 147.959 1.00 98.81  ? 395  LEU B CD2   1 
ATOM   8637  N  N     . LEU B 1 396 ? 181.930 132.870 150.855 1.00 102.29 ? 396  LEU B N     1 
ATOM   8638  C  CA    . LEU B 1 396 ? 182.889 133.582 151.689 1.00 102.48 ? 396  LEU B CA    1 
ATOM   8639  C  C     . LEU B 1 396 ? 184.170 133.881 150.923 1.00 105.55 ? 396  LEU B C     1 
ATOM   8640  O  O     . LEU B 1 396 ? 184.772 134.941 151.111 1.00 111.77 ? 396  LEU B O     1 
ATOM   8641  C  CB    . LEU B 1 396 ? 183.186 132.778 152.952 1.00 106.44 ? 396  LEU B CB    1 
ATOM   8642  C  CG    . LEU B 1 396 ? 181.967 132.499 153.830 1.00 102.16 ? 396  LEU B CG    1 
ATOM   8643  C  CD1   . LEU B 1 396 ? 182.385 131.875 155.146 1.00 108.08 ? 396  LEU B CD1   1 
ATOM   8644  C  CD2   . LEU B 1 396 ? 181.166 133.763 154.057 1.00 93.01  ? 396  LEU B CD2   1 
ATOM   8645  N  N     . PHE B 1 397 ? 184.604 132.965 150.055 1.00 103.54 ? 397  PHE B N     1 
ATOM   8646  C  CA    . PHE B 1 397 ? 185.788 133.215 149.244 1.00 107.42 ? 397  PHE B CA    1 
ATOM   8647  C  C     . PHE B 1 397 ? 185.583 134.423 148.347 1.00 110.06 ? 397  PHE B C     1 
ATOM   8648  O  O     . PHE B 1 397 ? 186.455 135.294 148.248 1.00 117.53 ? 397  PHE B O     1 
ATOM   8649  C  CB    . PHE B 1 397 ? 186.123 131.979 148.412 1.00 110.40 ? 397  PHE B CB    1 
ATOM   8650  C  CG    . PHE B 1 397 ? 187.386 132.109 147.616 1.00 113.91 ? 397  PHE B CG    1 
ATOM   8651  C  CD1   . PHE B 1 397 ? 188.614 131.844 148.191 1.00 120.30 ? 397  PHE B CD1   1 
ATOM   8652  C  CD2   . PHE B 1 397 ? 187.343 132.490 146.287 1.00 120.11 ? 397  PHE B CD2   1 
ATOM   8653  C  CE1   . PHE B 1 397 ? 189.775 131.961 147.457 1.00 130.61 ? 397  PHE B CE1   1 
ATOM   8654  C  CE2   . PHE B 1 397 ? 188.502 132.610 145.549 1.00 126.29 ? 397  PHE B CE2   1 
ATOM   8655  C  CZ    . PHE B 1 397 ? 189.720 132.345 146.134 1.00 131.14 ? 397  PHE B CZ    1 
ATOM   8656  N  N     . ALA B 1 398 ? 184.424 134.499 147.691 1.00 104.95 ? 398  ALA B N     1 
ATOM   8657  C  CA    . ALA B 1 398 ? 184.125 135.666 146.871 1.00 106.98 ? 398  ALA B CA    1 
ATOM   8658  C  C     . ALA B 1 398 ? 184.140 136.933 147.713 1.00 109.53 ? 398  ALA B C     1 
ATOM   8659  O  O     . ALA B 1 398 ? 184.758 137.936 147.337 1.00 114.33 ? 398  ALA B O     1 
ATOM   8660  C  CB    . ALA B 1 398 ? 182.772 135.491 146.181 1.00 104.44 ? 398  ALA B CB    1 
ATOM   8661  N  N     . PHE B 1 399 ? 183.500 136.886 148.885 1.00 106.79 ? 399  PHE B N     1 
ATOM   8662  C  CA    . PHE B 1 399 ? 183.395 138.081 149.717 1.00 104.75 ? 399  PHE B CA    1 
ATOM   8663  C  C     . PHE B 1 399 ? 184.763 138.573 150.177 1.00 109.81 ? 399  PHE B C     1 
ATOM   8664  O  O     . PHE B 1 399 ? 185.041 139.776 150.133 1.00 118.01 ? 399  PHE B O     1 
ATOM   8665  C  CB    . PHE B 1 399 ? 182.496 137.801 150.919 1.00 103.00 ? 399  PHE B CB    1 
ATOM   8666  C  CG    . PHE B 1 399 ? 181.052 138.120 150.680 1.00 100.51 ? 399  PHE B CG    1 
ATOM   8667  C  CD1   . PHE B 1 399 ? 180.658 139.401 150.355 1.00 98.62  ? 399  PHE B CD1   1 
ATOM   8668  C  CD2   . PHE B 1 399 ? 180.087 137.138 150.786 1.00 104.79 ? 399  PHE B CD2   1 
ATOM   8669  C  CE1   . PHE B 1 399 ? 179.332 139.694 150.137 1.00 100.62 ? 399  PHE B CE1   1 
ATOM   8670  C  CE2   . PHE B 1 399 ? 178.760 137.427 150.570 1.00 96.82  ? 399  PHE B CE2   1 
ATOM   8671  C  CZ    . PHE B 1 399 ? 178.383 138.706 150.245 1.00 95.81  ? 399  PHE B CZ    1 
ATOM   8672  N  N     . GLU B 1 400 ? 185.632 137.663 150.629 1.00 105.93 ? 400  GLU B N     1 
ATOM   8673  C  CA    . GLU B 1 400 ? 186.955 138.088 151.083 1.00 109.36 ? 400  GLU B CA    1 
ATOM   8674  C  C     . GLU B 1 400 ? 187.832 138.544 149.924 1.00 116.09 ? 400  GLU B C     1 
ATOM   8675  O  O     . GLU B 1 400 ? 188.497 139.582 150.021 1.00 121.26 ? 400  GLU B O     1 
ATOM   8676  C  CB    . GLU B 1 400 ? 187.660 136.976 151.864 1.00 111.78 ? 400  GLU B CB    1 
ATOM   8677  C  CG    . GLU B 1 400 ? 186.798 136.192 152.831 1.00 117.60 ? 400  GLU B CG    1 
ATOM   8678  C  CD    . GLU B 1 400 ? 186.683 136.854 154.188 1.00 124.29 ? 400  GLU B CD    1 
ATOM   8679  O  OE1   . GLU B 1 400 ? 187.124 138.013 154.329 1.00 127.19 ? 400  GLU B OE1   1 
ATOM   8680  O  OE2   . GLU B 1 400 ? 186.150 136.214 155.118 1.00 123.90 ? 400  GLU B OE2   1 
ATOM   8681  N  N     . ARG B 1 401 ? 187.863 137.789 148.824 1.00 113.80 ? 401  ARG B N     1 
ATOM   8682  C  CA    . ARG B 1 401 ? 188.818 138.103 147.767 1.00 115.57 ? 401  ARG B CA    1 
ATOM   8683  C  C     . ARG B 1 401 ? 188.401 139.328 146.964 1.00 117.80 ? 401  ARG B C     1 
ATOM   8684  O  O     . ARG B 1 401 ? 189.250 139.982 146.349 1.00 124.21 ? 401  ARG B O     1 
ATOM   8685  C  CB    . ARG B 1 401 ? 189.017 136.897 146.850 1.00 113.76 ? 401  ARG B CB    1 
ATOM   8686  C  CG    . ARG B 1 401 ? 189.496 135.647 147.570 1.00 119.71 ? 401  ARG B CG    1 
ATOM   8687  C  CD    . ARG B 1 401 ? 191.002 135.475 147.414 1.00 125.54 ? 401  ARG B CD    1 
ATOM   8688  N  NE    . ARG B 1 401 ? 191.541 134.420 148.265 1.00 131.58 ? 401  ARG B NE    1 
ATOM   8689  C  CZ    . ARG B 1 401 ? 191.638 134.489 149.586 1.00 134.59 ? 401  ARG B CZ    1 
ATOM   8690  N  NH1   . ARG B 1 401 ? 191.257 135.566 150.254 1.00 128.12 ? 401  ARG B NH1   1 
ATOM   8691  N  NH2   . ARG B 1 401 ? 192.135 133.453 150.255 1.00 140.27 ? 401  ARG B NH2   1 
ATOM   8692  N  N     . ASN B 1 402 ? 187.109 139.665 146.946 1.00 114.80 ? 402  ASN B N     1 
ATOM   8693  C  CA    . ASN B 1 402 ? 186.703 140.821 146.155 1.00 114.82 ? 402  ASN B CA    1 
ATOM   8694  C  C     . ASN B 1 402 ? 186.776 142.112 146.962 1.00 115.92 ? 402  ASN B C     1 
ATOM   8695  O  O     . ASN B 1 402 ? 187.249 143.136 146.459 1.00 122.77 ? 402  ASN B O     1 
ATOM   8696  C  CB    . ASN B 1 402 ? 185.297 140.613 145.599 1.00 110.23 ? 402  ASN B CB    1 
ATOM   8697  C  CG    . ASN B 1 402 ? 185.039 141.433 144.354 1.00 110.26 ? 402  ASN B CG    1 
ATOM   8698  O  OD1   . ASN B 1 402 ? 185.495 142.569 144.239 1.00 113.51 ? 402  ASN B OD1   1 
ATOM   8699  N  ND2   . ASN B 1 402 ? 184.317 140.854 143.403 1.00 112.57 ? 402  ASN B ND2   1 
ATOM   8700  N  N     . HIS B 1 403 ? 186.293 142.088 148.204 1.00 114.63 ? 403  HIS B N     1 
ATOM   8701  C  CA    . HIS B 1 403 ? 186.272 143.218 149.130 1.00 118.53 ? 403  HIS B CA    1 
ATOM   8702  C  C     . HIS B 1 403 ? 185.378 144.353 148.651 1.00 112.79 ? 403  HIS B C     1 
ATOM   8703  O  O     . HIS B 1 403 ? 185.327 145.399 149.307 1.00 111.89 ? 403  HIS B O     1 
ATOM   8704  C  CB    . HIS B 1 403 ? 187.676 143.777 149.411 1.00 125.87 ? 403  HIS B CB    1 
ATOM   8705  C  CG    . HIS B 1 403 ? 188.289 143.263 150.677 1.00 136.50 ? 403  HIS B CG    1 
ATOM   8706  N  ND1   . HIS B 1 403 ? 187.749 143.513 151.920 1.00 138.31 ? 403  HIS B ND1   1 
ATOM   8707  C  CD2   . HIS B 1 403 ? 189.395 142.512 150.890 1.00 139.56 ? 403  HIS B CD2   1 
ATOM   8708  C  CE1   . HIS B 1 403 ? 188.496 142.937 152.845 1.00 144.75 ? 403  HIS B CE1   1 
ATOM   8709  N  NE2   . HIS B 1 403 ? 189.501 142.323 152.247 1.00 143.84 ? 403  HIS B NE2   1 
ATOM   8710  N  N     . GLN B 1 404 ? 184.677 144.188 147.533 1.00 111.16 ? 404  GLN B N     1 
ATOM   8711  C  CA    . GLN B 1 404 ? 183.806 145.214 146.981 1.00 109.40 ? 404  GLN B CA    1 
ATOM   8712  C  C     . GLN B 1 404 ? 182.360 144.756 146.863 1.00 108.80 ? 404  GLN B C     1 
ATOM   8713  O  O     . GLN B 1 404 ? 181.464 145.598 146.750 1.00 105.15 ? 404  GLN B O     1 
ATOM   8714  C  CB    . GLN B 1 404 ? 184.322 145.647 145.605 1.00 110.81 ? 404  GLN B CB    1 
ATOM   8715  C  CG    . GLN B 1 404 ? 183.723 146.934 145.068 1.00 108.57 ? 404  GLN B CG    1 
ATOM   8716  C  CD    . GLN B 1 404 ? 183.998 147.121 143.591 1.00 112.04 ? 404  GLN B CD    1 
ATOM   8717  O  OE1   . GLN B 1 404 ? 184.890 146.486 143.030 1.00 111.62 ? 404  GLN B OE1   1 
ATOM   8718  N  NE2   . GLN B 1 404 ? 183.249 148.012 142.958 1.00 112.97 ? 404  GLN B NE2   1 
ATOM   8719  N  N     . ILE B 1 405 ? 182.113 143.452 146.895 1.00 109.44 ? 405  ILE B N     1 
ATOM   8720  C  CA    . ILE B 1 405 ? 180.779 142.900 146.694 1.00 100.30 ? 405  ILE B CA    1 
ATOM   8721  C  C     . ILE B 1 405 ? 179.895 143.325 147.856 1.00 99.82  ? 405  ILE B C     1 
ATOM   8722  O  O     . ILE B 1 405 ? 180.245 143.117 149.022 1.00 102.16 ? 405  ILE B O     1 
ATOM   8723  C  CB    . ILE B 1 405 ? 180.825 141.371 146.575 1.00 99.73  ? 405  ILE B CB    1 
ATOM   8724  C  CG1   . ILE B 1 405 ? 181.718 140.949 145.413 1.00 101.43 ? 405  ILE B CG1   1 
ATOM   8725  C  CG2   . ILE B 1 405 ? 179.434 140.816 146.385 1.00 99.74  ? 405  ILE B CG2   1 
ATOM   8726  C  CD1   . ILE B 1 405 ? 181.934 139.460 145.343 1.00 106.93 ? 405  ILE B CD1   1 
ATOM   8727  N  N     . GLY B 1 406 ? 178.751 143.919 147.540 1.00 100.68 ? 406  GLY B N     1 
ATOM   8728  C  CA    . GLY B 1 406 ? 177.809 144.329 148.560 1.00 104.81 ? 406  GLY B CA    1 
ATOM   8729  C  C     . GLY B 1 406 ? 176.748 143.281 148.804 1.00 97.46  ? 406  GLY B C     1 
ATOM   8730  O  O     . GLY B 1 406 ? 175.882 143.448 149.666 1.00 101.95 ? 406  GLY B O     1 
ATOM   8731  N  N     . GLY B 1 407 ? 176.805 142.195 148.042 1.00 92.44  ? 407  GLY B N     1 
ATOM   8732  C  CA    . GLY B 1 407 ? 175.851 141.114 148.178 1.00 92.79  ? 407  GLY B CA    1 
ATOM   8733  C  C     . GLY B 1 407 ? 175.948 140.126 147.037 1.00 97.39  ? 407  GLY B C     1 
ATOM   8734  O  O     . GLY B 1 407 ? 176.267 140.508 145.908 1.00 106.59 ? 407  GLY B O     1 
ATOM   8735  N  N     . ALA B 1 408 ? 175.662 138.857 147.307 1.00 92.65  ? 408  ALA B N     1 
ATOM   8736  C  CA    . ALA B 1 408 ? 175.760 137.821 146.292 1.00 91.48  ? 408  ALA B CA    1 
ATOM   8737  C  C     . ALA B 1 408 ? 174.705 136.762 146.554 1.00 92.25  ? 408  ALA B C     1 
ATOM   8738  O  O     . ALA B 1 408 ? 174.198 136.623 147.669 1.00 101.31 ? 408  ALA B O     1 
ATOM   8739  C  CB    . ALA B 1 408 ? 177.155 137.185 146.270 1.00 90.52  ? 408  ALA B CB    1 
ATOM   8740  N  N     . CYS B 1 409 ? 174.376 136.010 145.509 1.00 86.61  ? 409  CYS B N     1 
ATOM   8741  C  CA    . CYS B 1 409 ? 173.418 134.923 145.624 1.00 94.09  ? 409  CYS B CA    1 
ATOM   8742  C  C     . CYS B 1 409 ? 173.938 133.721 144.858 1.00 99.15  ? 409  CYS B C     1 
ATOM   8743  O  O     . CYS B 1 409 ? 174.572 133.869 143.811 1.00 104.26 ? 409  CYS B O     1 
ATOM   8744  C  CB    . CYS B 1 409 ? 172.038 135.323 145.095 1.00 102.50 ? 409  CYS B CB    1 
ATOM   8745  S  SG    . CYS B 1 409 ? 172.021 135.818 143.374 1.00 119.74 ? 409  CYS B SG    1 
ATOM   8746  N  N     . GLY B 1 410 ? 173.664 132.530 145.387 1.00 100.53 ? 410  GLY B N     1 
ATOM   8747  C  CA    . GLY B 1 410 ? 174.130 131.306 144.779 1.00 97.89  ? 410  GLY B CA    1 
ATOM   8748  C  C     . GLY B 1 410 ? 173.209 130.819 143.680 1.00 97.66  ? 410  GLY B C     1 
ATOM   8749  O  O     . GLY B 1 410 ? 172.096 131.305 143.489 1.00 98.12  ? 410  GLY B O     1 
ATOM   8750  N  N     . GLN B 1 411 ? 173.702 129.834 142.941 1.00 103.93 ? 411  GLN B N     1 
ATOM   8751  C  CA    . GLN B 1 411 ? 172.927 129.224 141.875 1.00 102.57 ? 411  GLN B CA    1 
ATOM   8752  C  C     . GLN B 1 411 ? 171.760 128.441 142.458 1.00 101.72 ? 411  GLN B C     1 
ATOM   8753  O  O     . GLN B 1 411 ? 171.900 127.756 143.474 1.00 103.69 ? 411  GLN B O     1 
ATOM   8754  C  CB    . GLN B 1 411 ? 173.817 128.305 141.039 1.00 104.94 ? 411  GLN B CB    1 
ATOM   8755  C  CG    . GLN B 1 411 ? 173.104 127.606 139.906 1.00 108.46 ? 411  GLN B CG    1 
ATOM   8756  C  CD    . GLN B 1 411 ? 174.051 126.808 139.041 1.00 116.20 ? 411  GLN B CD    1 
ATOM   8757  O  OE1   . GLN B 1 411 ? 175.225 126.652 139.372 1.00 118.78 ? 411  GLN B OE1   1 
ATOM   8758  N  NE2   . GLN B 1 411 ? 173.549 126.304 137.923 1.00 118.19 ? 411  GLN B NE2   1 
ATOM   8759  N  N     . LEU B 1 412 ? 170.605 128.547 141.812 1.00 100.65 ? 412  LEU B N     1 
ATOM   8760  C  CA    . LEU B 1 412 ? 169.404 127.833 142.219 1.00 100.90 ? 412  LEU B CA    1 
ATOM   8761  C  C     . LEU B 1 412 ? 169.207 126.638 141.298 1.00 105.60 ? 412  LEU B C     1 
ATOM   8762  O  O     . LEU B 1 412 ? 169.154 126.796 140.074 1.00 113.51 ? 412  LEU B O     1 
ATOM   8763  C  CB    . LEU B 1 412 ? 168.182 128.750 142.176 1.00 103.67 ? 412  LEU B CB    1 
ATOM   8764  C  CG    . LEU B 1 412 ? 166.992 128.337 143.038 1.00 104.04 ? 412  LEU B CG    1 
ATOM   8765  C  CD1   . LEU B 1 412 ? 167.384 128.326 144.502 1.00 100.65 ? 412  LEU B CD1   1 
ATOM   8766  C  CD2   . LEU B 1 412 ? 165.820 129.271 142.802 1.00 114.09 ? 412  LEU B CD2   1 
ATOM   8767  N  N     . THR B 1 413 ? 169.106 125.448 141.883 1.00 99.88  ? 413  THR B N     1 
ATOM   8768  C  CA    . THR B 1 413 ? 169.055 124.212 141.119 1.00 101.31 ? 413  THR B CA    1 
ATOM   8769  C  C     . THR B 1 413 ? 167.960 123.322 141.692 1.00 110.18 ? 413  THR B C     1 
ATOM   8770  O  O     . THR B 1 413 ? 167.700 123.320 142.896 1.00 116.77 ? 413  THR B O     1 
ATOM   8771  C  CB    . THR B 1 413 ? 170.425 123.513 141.135 1.00 109.73 ? 413  THR B CB    1 
ATOM   8772  O  OG1   . THR B 1 413 ? 171.285 124.132 140.172 1.00 112.84 ? 413  THR B OG1   1 
ATOM   8773  C  CG2   . THR B 1 413 ? 170.310 122.032 140.810 1.00 116.20 ? 413  THR B CG2   1 
ATOM   8774  N  N     . VAL B 1 414 ? 167.300 122.572 140.812 1.00 110.57 ? 414  VAL B N     1 
ATOM   8775  C  CA    . VAL B 1 414 ? 166.281 121.605 141.203 1.00 114.98 ? 414  VAL B CA    1 
ATOM   8776  C  C     . VAL B 1 414 ? 166.974 120.301 141.570 1.00 126.31 ? 414  VAL B C     1 
ATOM   8777  O  O     . VAL B 1 414 ? 167.792 119.787 140.796 1.00 129.09 ? 414  VAL B O     1 
ATOM   8778  C  CB    . VAL B 1 414 ? 165.261 121.389 140.074 1.00 110.44 ? 414  VAL B CB    1 
ATOM   8779  C  CG1   . VAL B 1 414 ? 164.288 120.288 140.445 1.00 119.18 ? 414  VAL B CG1   1 
ATOM   8780  C  CG2   . VAL B 1 414 ? 164.534 122.681 139.769 1.00 107.14 ? 414  VAL B CG2   1 
ATOM   8781  N  N     . ASP B 1 415 ? 166.659 119.767 142.749 1.00 129.10 ? 415  ASP B N     1 
ATOM   8782  C  CA    . ASP B 1 415 ? 167.324 118.558 143.218 1.00 133.76 ? 415  ASP B CA    1 
ATOM   8783  C  C     . ASP B 1 415 ? 166.864 117.361 142.399 1.00 138.25 ? 415  ASP B C     1 
ATOM   8784  O  O     . ASP B 1 415 ? 165.702 117.289 141.986 1.00 136.71 ? 415  ASP B O     1 
ATOM   8785  C  CB    . ASP B 1 415 ? 167.029 118.319 144.696 1.00 132.89 ? 415  ASP B CB    1 
ATOM   8786  C  CG    . ASP B 1 415 ? 165.578 118.554 145.041 1.00 137.80 ? 415  ASP B CG    1 
ATOM   8787  O  OD1   . ASP B 1 415 ? 164.884 119.236 144.263 1.00 136.90 ? 415  ASP B OD1   1 
ATOM   8788  O  OD2   . ASP B 1 415 ? 165.132 118.057 146.096 1.00 141.63 ? 415  ASP B OD2   1 
ATOM   8789  N  N     . ASN B 1 416 ? 167.775 116.413 142.183 1.00 142.99 ? 416  ASN B N     1 
ATOM   8790  C  CA    . ASN B 1 416 ? 167.521 115.221 141.382 1.00 145.24 ? 416  ASN B CA    1 
ATOM   8791  C  C     . ASN B 1 416 ? 166.934 115.587 140.025 1.00 144.61 ? 416  ASN B C     1 
ATOM   8792  O  O     . ASN B 1 416 ? 165.784 115.234 139.733 1.00 145.85 ? 416  ASN B O     1 
ATOM   8793  C  CB    . ASN B 1 416 ? 166.587 114.262 142.122 1.00 146.06 ? 416  ASN B CB    1 
ATOM   8794  C  CG    . ASN B 1 416 ? 167.249 113.616 143.319 1.00 152.04 ? 416  ASN B CG    1 
ATOM   8795  O  OD1   . ASN B 1 416 ? 168.252 114.111 143.832 1.00 154.21 ? 416  ASN B OD1   1 
ATOM   8796  N  ND2   . ASN B 1 416 ? 166.692 112.498 143.771 1.00 156.50 ? 416  ASN B ND2   1 
ATOM   8797  N  N     . PRO B 1 417 ? 167.673 116.302 139.173 1.00 143.07 ? 417  PRO B N     1 
ATOM   8798  C  CA    . PRO B 1 417 ? 167.131 116.589 137.838 1.00 139.69 ? 417  PRO B CA    1 
ATOM   8799  C  C     . PRO B 1 417 ? 167.197 115.392 136.909 1.00 148.17 ? 417  PRO B C     1 
ATOM   8800  O  O     . PRO B 1 417 ? 166.284 115.193 136.098 1.00 148.99 ? 417  PRO B O     1 
ATOM   8801  C  CB    . PRO B 1 417 ? 168.010 117.746 137.352 1.00 135.55 ? 417  PRO B CB    1 
ATOM   8802  C  CG    . PRO B 1 417 ? 169.314 117.525 138.037 1.00 139.96 ? 417  PRO B CG    1 
ATOM   8803  C  CD    . PRO B 1 417 ? 169.006 116.901 139.371 1.00 142.99 ? 417  PRO B CD    1 
ATOM   8804  N  N     . PHE B 1 418 ? 168.257 114.586 137.001 1.00 150.14 ? 418  PHE B N     1 
ATOM   8805  C  CA    . PHE B 1 418 ? 168.346 113.386 136.176 1.00 150.52 ? 418  PHE B CA    1 
ATOM   8806  C  C     . PHE B 1 418 ? 167.240 112.400 136.526 1.00 149.93 ? 418  PHE B C     1 
ATOM   8807  O  O     . PHE B 1 418 ? 166.599 111.831 135.636 1.00 149.89 ? 418  PHE B O     1 
ATOM   8808  C  CB    . PHE B 1 418 ? 169.715 112.728 136.346 1.00 152.45 ? 418  PHE B CB    1 
ATOM   8809  C  CG    . PHE B 1 418 ? 170.852 113.532 135.783 1.00 155.61 ? 418  PHE B CG    1 
ATOM   8810  C  CD1   . PHE B 1 418 ? 170.631 114.490 134.811 1.00 152.72 ? 418  PHE B CD1   1 
ATOM   8811  C  CD2   . PHE B 1 418 ? 172.148 113.322 136.225 1.00 158.21 ? 418  PHE B CD2   1 
ATOM   8812  C  CE1   . PHE B 1 418 ? 171.678 115.228 134.292 1.00 153.39 ? 418  PHE B CE1   1 
ATOM   8813  C  CE2   . PHE B 1 418 ? 173.200 114.056 135.710 1.00 159.44 ? 418  PHE B CE2   1 
ATOM   8814  C  CZ    . PHE B 1 418 ? 172.964 115.010 134.742 1.00 156.15 ? 418  PHE B CZ    1 
ATOM   8815  N  N     . GLU B 1 419 ? 167.002 112.190 137.816 1.00 148.62 ? 419  GLU B N     1 
ATOM   8816  C  CA    . GLU B 1 419 ? 165.955 111.281 138.251 1.00 150.38 ? 419  GLU B CA    1 
ATOM   8817  C  C     . GLU B 1 419 ? 164.594 111.934 138.037 1.00 149.46 ? 419  GLU B C     1 
ATOM   8818  O  O     . GLU B 1 419 ? 164.456 113.160 138.070 1.00 149.74 ? 419  GLU B O     1 
ATOM   8819  C  CB    . GLU B 1 419 ? 166.207 110.867 139.713 1.00 151.36 ? 419  GLU B CB    1 
ATOM   8820  C  CG    . GLU B 1 419 ? 165.076 110.226 140.556 1.00 155.24 ? 419  GLU B CG    1 
ATOM   8821  C  CD    . GLU B 1 419 ? 163.889 111.130 140.845 1.00 155.50 ? 419  GLU B CD    1 
ATOM   8822  O  OE1   . GLU B 1 419 ? 162.804 110.600 141.165 1.00 157.18 ? 419  GLU B OE1   1 
ATOM   8823  O  OE2   . GLU B 1 419 ? 164.049 112.367 140.793 1.00 154.75 ? 419  GLU B OE2   1 
ATOM   8824  N  N     . ASN B 1 420 ? 163.590 111.093 137.788 1.00 148.75 ? 420  ASN B N     1 
ATOM   8825  C  CA    . ASN B 1 420 ? 162.230 111.543 137.488 1.00 150.38 ? 420  ASN B CA    1 
ATOM   8826  C  C     . ASN B 1 420 ? 162.217 112.448 136.260 1.00 149.11 ? 420  ASN B C     1 
ATOM   8827  O  O     . ASN B 1 420 ? 161.789 113.603 136.318 1.00 143.32 ? 420  ASN B O     1 
ATOM   8828  C  CB    . ASN B 1 420 ? 161.596 112.244 138.690 1.00 152.14 ? 420  ASN B CB    1 
ATOM   8829  C  CG    . ASN B 1 420 ? 160.085 112.191 138.664 1.00 153.13 ? 420  ASN B CG    1 
ATOM   8830  O  OD1   . ASN B 1 420 ? 159.495 111.277 138.087 1.00 151.67 ? 420  ASN B OD1   1 
ATOM   8831  N  ND2   . ASN B 1 420 ? 159.448 113.168 139.297 1.00 148.17 ? 420  ASN B ND2   1 
ATOM   8832  N  N     . LEU B 1 421 ? 162.699 111.917 135.135 1.00 150.23 ? 421  LEU B N     1 
ATOM   8833  C  CA    . LEU B 1 421 ? 162.705 112.680 133.893 1.00 145.74 ? 421  LEU B CA    1 
ATOM   8834  C  C     . LEU B 1 421 ? 161.376 112.572 133.159 1.00 140.73 ? 421  LEU B C     1 
ATOM   8835  O  O     . LEU B 1 421 ? 161.158 113.295 132.182 1.00 137.45 ? 421  LEU B O     1 
ATOM   8836  C  CB    . LEU B 1 421 ? 163.853 112.204 133.000 1.00 145.28 ? 421  LEU B CB    1 
ATOM   8837  C  CG    . LEU B 1 421 ? 164.311 113.113 131.858 1.00 142.39 ? 421  LEU B CG    1 
ATOM   8838  C  CD1   . LEU B 1 421 ? 164.502 114.535 132.351 1.00 137.72 ? 421  LEU B CD1   1 
ATOM   8839  C  CD2   . LEU B 1 421 ? 165.594 112.581 131.245 1.00 143.27 ? 421  LEU B CD2   1 
ATOM   8840  N  N     . SER B 1 422 ? 160.482 111.694 133.616 1.00 140.26 ? 422  SER B N     1 
ATOM   8841  C  CA    . SER B 1 422 ? 159.180 111.548 132.981 1.00 140.99 ? 422  SER B CA    1 
ATOM   8842  C  C     . SER B 1 422 ? 158.277 112.750 133.220 1.00 138.06 ? 422  SER B C     1 
ATOM   8843  O  O     . SER B 1 422 ? 157.340 112.967 132.446 1.00 135.63 ? 422  SER B O     1 
ATOM   8844  C  CB    . SER B 1 422 ? 158.493 110.277 133.483 1.00 142.81 ? 422  SER B CB    1 
ATOM   8845  O  OG    . SER B 1 422 ? 157.213 110.123 132.897 1.00 142.40 ? 422  SER B OG    1 
ATOM   8846  N  N     . ASN B 1 423 ? 158.532 113.530 134.267 1.00 135.99 ? 423  ASN B N     1 
ATOM   8847  C  CA    . ASN B 1 423 ? 157.706 114.691 134.573 1.00 130.68 ? 423  ASN B CA    1 
ATOM   8848  C  C     . ASN B 1 423 ? 158.141 115.866 133.708 1.00 129.02 ? 423  ASN B C     1 
ATOM   8849  O  O     . ASN B 1 423 ? 159.310 116.264 133.733 1.00 131.93 ? 423  ASN B O     1 
ATOM   8850  C  CB    . ASN B 1 423 ? 157.811 115.044 136.054 1.00 128.84 ? 423  ASN B CB    1 
ATOM   8851  C  CG    . ASN B 1 423 ? 156.655 115.895 136.533 1.00 127.40 ? 423  ASN B CG    1 
ATOM   8852  O  OD1   . ASN B 1 423 ? 155.918 116.468 135.732 1.00 126.46 ? 423  ASN B OD1   1 
ATOM   8853  N  ND2   . ASN B 1 423 ? 156.489 115.983 137.846 1.00 127.37 ? 423  ASN B ND2   1 
ATOM   8854  N  N     . TRP B 1 424 ? 157.201 116.420 132.941 1.00 126.87 ? 424  TRP B N     1 
ATOM   8855  C  CA    . TRP B 1 424 ? 157.528 117.530 132.055 1.00 124.46 ? 424  TRP B CA    1 
ATOM   8856  C  C     . TRP B 1 424 ? 157.678 118.845 132.805 1.00 120.19 ? 424  TRP B C     1 
ATOM   8857  O  O     . TRP B 1 424 ? 158.548 119.649 132.460 1.00 120.26 ? 424  TRP B O     1 
ATOM   8858  C  CB    . TRP B 1 424 ? 156.465 117.658 130.963 1.00 124.07 ? 424  TRP B CB    1 
ATOM   8859  C  CG    . TRP B 1 424 ? 156.493 116.526 129.980 1.00 126.92 ? 424  TRP B CG    1 
ATOM   8860  C  CD1   . TRP B 1 424 ? 156.154 115.228 130.217 1.00 131.92 ? 424  TRP B CD1   1 
ATOM   8861  C  CD2   . TRP B 1 424 ? 156.878 116.595 128.603 1.00 125.57 ? 424  TRP B CD2   1 
ATOM   8862  N  NE1   . TRP B 1 424 ? 156.309 114.482 129.075 1.00 130.78 ? 424  TRP B NE1   1 
ATOM   8863  C  CE2   . TRP B 1 424 ? 156.751 115.299 128.069 1.00 126.69 ? 424  TRP B CE2   1 
ATOM   8864  C  CE3   . TRP B 1 424 ? 157.317 117.626 127.769 1.00 124.67 ? 424  TRP B CE3   1 
ATOM   8865  C  CZ2   . TRP B 1 424 ? 157.048 115.007 126.741 1.00 124.21 ? 424  TRP B CZ2   1 
ATOM   8866  C  CZ3   . TRP B 1 424 ? 157.611 117.333 126.452 1.00 125.40 ? 424  TRP B CZ3   1 
ATOM   8867  C  CH2   . TRP B 1 424 ? 157.475 116.035 125.951 1.00 126.54 ? 424  TRP B CH2   1 
ATOM   8868  N  N     . VAL B 1 425 ? 156.858 119.080 133.831 1.00 113.85 ? 425  VAL B N     1 
ATOM   8869  C  CA    . VAL B 1 425 ? 156.943 120.333 134.576 1.00 110.72 ? 425  VAL B CA    1 
ATOM   8870  C  C     . VAL B 1 425 ? 158.268 120.431 135.323 1.00 115.56 ? 425  VAL B C     1 
ATOM   8871  O  O     . VAL B 1 425 ? 158.900 121.493 135.355 1.00 119.98 ? 425  VAL B O     1 
ATOM   8872  C  CB    . VAL B 1 425 ? 155.742 120.467 135.527 1.00 112.07 ? 425  VAL B CB    1 
ATOM   8873  C  CG1   . VAL B 1 425 ? 155.926 121.657 136.442 1.00 115.51 ? 425  VAL B CG1   1 
ATOM   8874  C  CG2   . VAL B 1 425 ? 154.459 120.598 134.731 1.00 113.48 ? 425  VAL B CG2   1 
ATOM   8875  N  N     . ILE B 1 426 ? 158.708 119.332 135.940 1.00 116.29 ? 426  ILE B N     1 
ATOM   8876  C  CA    . ILE B 1 426 ? 159.969 119.347 136.676 1.00 113.75 ? 426  ILE B CA    1 
ATOM   8877  C  C     . ILE B 1 426 ? 161.135 119.626 135.735 1.00 113.14 ? 426  ILE B C     1 
ATOM   8878  O  O     . ILE B 1 426 ? 162.016 120.440 136.037 1.00 115.01 ? 426  ILE B O     1 
ATOM   8879  C  CB    . ILE B 1 426 ? 160.156 118.019 137.432 1.00 116.03 ? 426  ILE B CB    1 
ATOM   8880  C  CG1   . ILE B 1 426 ? 159.382 118.041 138.751 1.00 120.84 ? 426  ILE B CG1   1 
ATOM   8881  C  CG2   . ILE B 1 426 ? 161.632 117.733 137.670 1.00 113.19 ? 426  ILE B CG2   1 
ATOM   8882  C  CD1   . ILE B 1 426 ? 160.152 118.642 139.902 1.00 123.97 ? 426  ILE B CD1   1 
ATOM   8883  N  N     . SER B 1 427 ? 161.152 118.966 134.576 1.00 110.29 ? 427  SER B N     1 
ATOM   8884  C  CA    . SER B 1 427 ? 162.226 119.187 133.614 1.00 107.73 ? 427  SER B CA    1 
ATOM   8885  C  C     . SER B 1 427 ? 162.192 120.604 133.056 1.00 108.91 ? 427  SER B C     1 
ATOM   8886  O  O     . SER B 1 427 ? 163.244 121.219 132.846 1.00 112.54 ? 427  SER B O     1 
ATOM   8887  C  CB    . SER B 1 427 ? 162.137 118.161 132.486 1.00 114.22 ? 427  SER B CB    1 
ATOM   8888  O  OG    . SER B 1 427 ? 162.254 116.842 132.989 1.00 123.26 ? 427  SER B OG    1 
ATOM   8889  N  N     . ALA B 1 428 ? 160.997 121.137 132.796 1.00 104.65 ? 428  ALA B N     1 
ATOM   8890  C  CA    . ALA B 1 428 ? 160.893 122.503 132.299 1.00 99.87  ? 428  ALA B CA    1 
ATOM   8891  C  C     . ALA B 1 428 ? 161.388 123.503 133.332 1.00 99.34  ? 428  ALA B C     1 
ATOM   8892  O  O     . ALA B 1 428 ? 162.064 124.478 132.988 1.00 103.85 ? 428  ALA B O     1 
ATOM   8893  C  CB    . ALA B 1 428 ? 159.452 122.810 131.904 1.00 104.20 ? 428  ALA B CB    1 
ATOM   8894  N  N     . GLN B 1 429 ? 161.061 123.279 134.605 1.00 101.70 ? 429  GLN B N     1 
ATOM   8895  C  CA    . GLN B 1 429 ? 161.578 124.141 135.662 1.00 103.21 ? 429  GLN B CA    1 
ATOM   8896  C  C     . GLN B 1 429 ? 163.092 124.037 135.769 1.00 104.26 ? 429  GLN B C     1 
ATOM   8897  O  O     . GLN B 1 429 ? 163.773 125.043 135.992 1.00 108.16 ? 429  GLN B O     1 
ATOM   8898  C  CB    . GLN B 1 429 ? 160.915 123.790 136.991 1.00 103.83 ? 429  GLN B CB    1 
ATOM   8899  C  CG    . GLN B 1 429 ? 159.533 124.380 137.147 1.00 106.40 ? 429  GLN B CG    1 
ATOM   8900  C  CD    . GLN B 1 429 ? 159.090 124.421 138.588 1.00 119.74 ? 429  GLN B CD    1 
ATOM   8901  O  OE1   . GLN B 1 429 ? 159.058 125.481 139.209 1.00 123.88 ? 429  GLN B OE1   1 
ATOM   8902  N  NE2   . GLN B 1 429 ? 158.719 123.266 139.123 1.00 124.23 ? 429  GLN B NE2   1 
ATOM   8903  N  N     . HIS B 1 430 ? 163.638 122.830 135.612 1.00 101.94 ? 430  HIS B N     1 
ATOM   8904  C  CA    . HIS B 1 430 ? 165.089 122.674 135.627 1.00 100.53 ? 430  HIS B CA    1 
ATOM   8905  C  C     . HIS B 1 430 ? 165.736 123.461 134.496 1.00 101.59 ? 430  HIS B C     1 
ATOM   8906  O  O     . HIS B 1 430 ? 166.734 124.164 134.700 1.00 103.68 ? 430  HIS B O     1 
ATOM   8907  C  CB    . HIS B 1 430 ? 165.456 121.196 135.521 1.00 103.99 ? 430  HIS B CB    1 
ATOM   8908  C  CG    . HIS B 1 430 ? 166.922 120.935 135.633 1.00 104.77 ? 430  HIS B CG    1 
ATOM   8909  N  ND1   . HIS B 1 430 ? 167.718 121.562 136.566 1.00 108.25 ? 430  HIS B ND1   1 
ATOM   8910  C  CD2   . HIS B 1 430 ? 167.742 120.128 134.921 1.00 111.27 ? 430  HIS B CD2   1 
ATOM   8911  C  CE1   . HIS B 1 430 ? 168.963 121.144 136.432 1.00 114.80 ? 430  HIS B CE1   1 
ATOM   8912  N  NE2   . HIS B 1 430 ? 169.005 120.275 135.439 1.00 118.05 ? 430  HIS B NE2   1 
ATOM   8913  N  N     . PHE B 1 431 ? 165.176 123.354 133.289 1.00 100.44 ? 431  PHE B N     1 
ATOM   8914  C  CA    . PHE B 1 431 ? 165.717 124.098 132.157 1.00 95.50  ? 431  PHE B CA    1 
ATOM   8915  C  C     . PHE B 1 431 ? 165.618 125.596 132.393 1.00 97.48  ? 431  PHE B C     1 
ATOM   8916  O  O     . PHE B 1 431 ? 166.559 126.341 132.095 1.00 101.13 ? 431  PHE B O     1 
ATOM   8917  C  CB    . PHE B 1 431 ? 164.984 123.720 130.871 1.00 99.64  ? 431  PHE B CB    1 
ATOM   8918  C  CG    . PHE B 1 431 ? 165.510 124.414 129.643 1.00 99.62  ? 431  PHE B CG    1 
ATOM   8919  C  CD1   . PHE B 1 431 ? 165.069 125.678 129.295 1.00 96.36  ? 431  PHE B CD1   1 
ATOM   8920  C  CD2   . PHE B 1 431 ? 166.448 123.799 128.839 1.00 105.41 ? 431  PHE B CD2   1 
ATOM   8921  C  CE1   . PHE B 1 431 ? 165.552 126.309 128.170 1.00 97.10  ? 431  PHE B CE1   1 
ATOM   8922  C  CE2   . PHE B 1 431 ? 166.930 124.428 127.712 1.00 105.01 ? 431  PHE B CE2   1 
ATOM   8923  C  CZ    . PHE B 1 431 ? 166.482 125.683 127.379 1.00 101.31 ? 431  PHE B CZ    1 
ATOM   8924  N  N     . GLU B 1 432 ? 164.477 126.058 132.908 1.00 99.71  ? 432  GLU B N     1 
ATOM   8925  C  CA    . GLU B 1 432 ? 164.312 127.483 133.153 1.00 97.96  ? 432  GLU B CA    1 
ATOM   8926  C  C     . GLU B 1 432 ? 165.329 127.979 134.163 1.00 100.25 ? 432  GLU B C     1 
ATOM   8927  O  O     . GLU B 1 432 ? 165.947 129.027 133.962 1.00 101.60 ? 432  GLU B O     1 
ATOM   8928  C  CB    . GLU B 1 432 ? 162.900 127.788 133.645 1.00 99.56  ? 432  GLU B CB    1 
ATOM   8929  C  CG    . GLU B 1 432 ? 162.716 129.244 134.031 1.00 103.99 ? 432  GLU B CG    1 
ATOM   8930  C  CD    . GLU B 1 432 ? 161.517 129.468 134.922 1.00 113.16 ? 432  GLU B CD    1 
ATOM   8931  O  OE1   . GLU B 1 432 ? 160.814 128.485 135.228 1.00 116.29 ? 432  GLU B OE1   1 
ATOM   8932  O  OE2   . GLU B 1 432 ? 161.276 130.627 135.318 1.00 115.62 ? 432  GLU B OE2   1 
ATOM   8933  N  N     . TYR B 1 433 ? 165.532 127.232 135.248 1.00 99.00  ? 433  TYR B N     1 
ATOM   8934  C  CA    . TYR B 1 433 ? 166.512 127.644 136.245 1.00 96.99  ? 433  TYR B CA    1 
ATOM   8935  C  C     . TYR B 1 433 ? 167.908 127.695 135.648 1.00 99.22  ? 433  TYR B C     1 
ATOM   8936  O  O     . TYR B 1 433 ? 168.643 128.667 135.850 1.00 101.71 ? 433  TYR B O     1 
ATOM   8937  C  CB    . TYR B 1 433 ? 166.490 126.699 137.443 1.00 96.49  ? 433  TYR B CB    1 
ATOM   8938  C  CG    . TYR B 1 433 ? 165.341 126.922 138.389 1.00 97.43  ? 433  TYR B CG    1 
ATOM   8939  C  CD1   . TYR B 1 433 ? 164.365 127.868 138.120 1.00 100.54 ? 433  TYR B CD1   1 
ATOM   8940  C  CD2   . TYR B 1 433 ? 165.241 126.195 139.560 1.00 101.93 ? 433  TYR B CD2   1 
ATOM   8941  C  CE1   . TYR B 1 433 ? 163.316 128.070 138.988 1.00 106.83 ? 433  TYR B CE1   1 
ATOM   8942  C  CE2   . TYR B 1 433 ? 164.204 126.393 140.431 1.00 104.48 ? 433  TYR B CE2   1 
ATOM   8943  C  CZ    . TYR B 1 433 ? 163.243 127.328 140.143 1.00 107.30 ? 433  TYR B CZ    1 
ATOM   8944  O  OH    . TYR B 1 433 ? 162.204 127.518 141.020 1.00 115.62 ? 433  TYR B OH    1 
ATOM   8945  N  N     . LYS B 1 434 ? 168.293 126.659 134.901 1.00 99.19  ? 434  LYS B N     1 
ATOM   8946  C  CA    . LYS B 1 434 ? 169.655 126.609 134.384 1.00 97.08  ? 434  LYS B CA    1 
ATOM   8947  C  C     . LYS B 1 434 ? 169.904 127.736 133.389 1.00 98.43  ? 434  LYS B C     1 
ATOM   8948  O  O     . LYS B 1 434 ? 170.923 128.433 133.465 1.00 105.62 ? 434  LYS B O     1 
ATOM   8949  C  CB    . LYS B 1 434 ? 169.923 125.248 133.747 1.00 96.31  ? 434  LYS B CB    1 
ATOM   8950  C  CG    . LYS B 1 434 ? 170.134 124.148 134.769 1.00 106.91 ? 434  LYS B CG    1 
ATOM   8951  C  CD    . LYS B 1 434 ? 171.518 124.201 135.382 1.00 113.05 ? 434  LYS B CD    1 
ATOM   8952  C  CE    . LYS B 1 434 ? 171.624 123.237 136.551 1.00 119.22 ? 434  LYS B CE    1 
ATOM   8953  N  NZ    . LYS B 1 434 ? 171.647 123.948 137.857 1.00 117.73 ? 434  LYS B NZ    1 
ATOM   8954  N  N     . ILE B 1 435 ? 168.967 127.947 132.462 1.00 96.20  ? 435  ILE B N     1 
ATOM   8955  C  CA    . ILE B 1 435 ? 169.139 129.003 131.470 1.00 96.79  ? 435  ILE B CA    1 
ATOM   8956  C  C     . ILE B 1 435 ? 169.098 130.375 132.125 1.00 103.28 ? 435  ILE B C     1 
ATOM   8957  O  O     . ILE B 1 435 ? 169.935 131.237 131.832 1.00 107.67 ? 435  ILE B O     1 
ATOM   8958  C  CB    . ILE B 1 435 ? 168.086 128.873 130.357 1.00 94.03  ? 435  ILE B CB    1 
ATOM   8959  C  CG1   . ILE B 1 435 ? 168.498 127.775 129.380 1.00 100.54 ? 435  ILE B CG1   1 
ATOM   8960  C  CG2   . ILE B 1 435 ? 167.906 130.193 129.634 1.00 92.10  ? 435  ILE B CG2   1 
ATOM   8961  C  CD1   . ILE B 1 435 ? 169.903 127.942 128.848 1.00 100.71 ? 435  ILE B CD1   1 
ATOM   8962  N  N     . SER B 1 436 ? 168.131 130.606 133.018 1.00 103.06 ? 436  SER B N     1 
ATOM   8963  C  CA    . SER B 1 436 ? 168.049 131.891 133.697 1.00 103.05 ? 436  SER B CA    1 
ATOM   8964  C  C     . SER B 1 436 ? 169.340 132.187 134.438 1.00 100.41 ? 436  SER B C     1 
ATOM   8965  O  O     . SER B 1 436 ? 169.977 133.219 134.199 1.00 106.23 ? 436  SER B O     1 
ATOM   8966  C  CB    . SER B 1 436 ? 166.861 131.899 134.658 1.00 100.11 ? 436  SER B CB    1 
ATOM   8967  O  OG    . SER B 1 436 ? 166.787 133.123 135.364 1.00 101.44 ? 436  SER B OG    1 
ATOM   8968  N  N     . ASN B 1 437 ? 169.777 131.255 135.292 1.00 94.03  ? 437  ASN B N     1 
ATOM   8969  C  CA    . ASN B 1 437 ? 171.047 131.404 135.987 1.00 96.03  ? 437  ASN B CA    1 
ATOM   8970  C  C     . ASN B 1 437 ? 172.154 131.759 135.011 1.00 101.39 ? 437  ASN B C     1 
ATOM   8971  O  O     . ASN B 1 437 ? 172.630 132.896 134.998 1.00 112.96 ? 437  ASN B O     1 
ATOM   8972  C  CB    . ASN B 1 437 ? 171.388 130.120 136.743 1.00 99.02  ? 437  ASN B CB    1 
ATOM   8973  C  CG    . ASN B 1 437 ? 170.592 129.968 138.016 1.00 108.49 ? 437  ASN B CG    1 
ATOM   8974  O  OD1   . ASN B 1 437 ? 170.201 130.953 138.639 1.00 112.06 ? 437  ASN B OD1   1 
ATOM   8975  N  ND2   . ASN B 1 437 ? 170.343 128.727 138.410 1.00 109.87 ? 437  ASN B ND2   1 
ATOM   8976  N  N     . ILE B 1 438 ? 172.485 130.838 134.104 1.00 97.40  ? 438  ILE B N     1 
ATOM   8977  C  CA    . ILE B 1 438 ? 173.647 131.014 133.244 1.00 100.23 ? 438  ILE B CA    1 
ATOM   8978  C  C     . ILE B 1 438 ? 173.546 132.351 132.524 1.00 105.82 ? 438  ILE B C     1 
ATOM   8979  O  O     . ILE B 1 438 ? 174.265 133.298 132.866 1.00 112.00 ? 438  ILE B O     1 
ATOM   8980  C  CB    . ILE B 1 438 ? 173.766 129.854 132.240 1.00 96.76  ? 438  ILE B CB    1 
ATOM   8981  C  CG1   . ILE B 1 438 ? 174.149 128.564 132.964 1.00 104.89 ? 438  ILE B CG1   1 
ATOM   8982  C  CG2   . ILE B 1 438 ? 174.793 130.175 131.172 1.00 97.66  ? 438  ILE B CG2   1 
ATOM   8983  C  CD1   . ILE B 1 438 ? 174.295 127.375 132.050 1.00 110.19 ? 438  ILE B CD1   1 
ATOM   8984  N  N     . LEU B 1 439 ? 172.558 132.488 131.639 1.00 99.38  ? 439  LEU B N     1 
ATOM   8985  C  CA    . LEU B 1 439 ? 172.494 133.662 130.776 1.00 99.31  ? 439  LEU B CA    1 
ATOM   8986  C  C     . LEU B 1 439 ? 172.297 134.940 131.585 1.00 104.79 ? 439  LEU B C     1 
ATOM   8987  O  O     . LEU B 1 439 ? 173.179 135.809 131.624 1.00 111.86 ? 439  LEU B O     1 
ATOM   8988  C  CB    . LEU B 1 439 ? 171.371 133.488 129.753 1.00 100.46 ? 439  LEU B CB    1 
ATOM   8989  C  CG    . LEU B 1 439 ? 171.765 132.954 128.374 1.00 101.13 ? 439  LEU B CG    1 
ATOM   8990  C  CD1   . LEU B 1 439 ? 172.473 131.622 128.493 1.00 106.56 ? 439  LEU B CD1   1 
ATOM   8991  C  CD2   . LEU B 1 439 ? 170.544 132.823 127.486 1.00 102.35 ? 439  LEU B CD2   1 
ATOM   8992  N  N     . ASP B 1 440 ? 171.143 135.069 132.247 1.00 99.18  ? 440  ASP B N     1 
ATOM   8993  C  CA    . ASP B 1 440 ? 170.799 136.345 132.859 1.00 100.47 ? 440  ASP B CA    1 
ATOM   8994  C  C     . ASP B 1 440 ? 171.743 136.683 134.002 1.00 103.80 ? 440  ASP B C     1 
ATOM   8995  O  O     . ASP B 1 440 ? 172.223 137.816 134.100 1.00 108.80 ? 440  ASP B O     1 
ATOM   8996  C  CB    . ASP B 1 440 ? 169.352 136.323 133.348 1.00 104.51 ? 440  ASP B CB    1 
ATOM   8997  C  CG    . ASP B 1 440 ? 168.362 136.121 132.223 1.00 110.78 ? 440  ASP B CG    1 
ATOM   8998  O  OD1   . ASP B 1 440 ? 168.799 135.830 131.092 1.00 108.36 ? 440  ASP B OD1   1 
ATOM   8999  O  OD2   . ASP B 1 440 ? 167.145 136.255 132.468 1.00 116.88 ? 440  ASP B OD2   1 
ATOM   9000  N  N     . LYS B 1 441 ? 172.007 135.725 134.895 1.00 101.70 ? 441  LYS B N     1 
ATOM   9001  C  CA    . LYS B 1 441 ? 172.826 136.034 136.054 1.00 100.32 ? 441  LYS B CA    1 
ATOM   9002  C  C     . LYS B 1 441 ? 174.269 136.305 135.657 1.00 102.49 ? 441  LYS B C     1 
ATOM   9003  O  O     . LYS B 1 441 ? 174.919 137.163 136.256 1.00 108.68 ? 441  LYS B O     1 
ATOM   9004  C  CB    . LYS B 1 441 ? 172.745 134.897 137.067 1.00 101.49 ? 441  LYS B CB    1 
ATOM   9005  C  CG    . LYS B 1 441 ? 171.342 134.655 137.586 1.00 100.42 ? 441  LYS B CG    1 
ATOM   9006  C  CD    . LYS B 1 441 ? 170.680 135.944 138.024 1.00 101.99 ? 441  LYS B CD    1 
ATOM   9007  C  CE    . LYS B 1 441 ? 169.380 135.665 138.751 1.00 114.83 ? 441  LYS B CE    1 
ATOM   9008  N  NZ    . LYS B 1 441 ? 169.598 134.772 139.920 1.00 113.08 ? 441  LYS B NZ    1 
ATOM   9009  N  N     . SER B 1 442 ? 174.798 135.604 134.646 1.00 96.26  ? 442  SER B N     1 
ATOM   9010  C  CA    . SER B 1 442 ? 176.147 135.914 134.191 1.00 101.04 ? 442  SER B CA    1 
ATOM   9011  C  C     . SER B 1 442 ? 176.209 137.311 133.590 1.00 106.06 ? 442  SER B C     1 
ATOM   9012  O  O     . SER B 1 442 ? 177.128 138.088 133.884 1.00 108.67 ? 442  SER B O     1 
ATOM   9013  C  CB    . SER B 1 442 ? 176.603 134.864 133.182 1.00 102.46 ? 442  SER B CB    1 
ATOM   9014  O  OG    . SER B 1 442 ? 176.584 133.571 133.760 1.00 109.88 ? 442  SER B OG    1 
ATOM   9015  N  N     . LEU B 1 443 ? 175.220 137.661 132.763 1.00 105.35 ? 443  LEU B N     1 
ATOM   9016  C  CA    . LEU B 1 443 ? 175.202 138.994 132.171 1.00 101.77 ? 443  LEU B CA    1 
ATOM   9017  C  C     . LEU B 1 443 ? 175.092 140.073 133.241 1.00 101.60 ? 443  LEU B C     1 
ATOM   9018  O  O     . LEU B 1 443 ? 175.742 141.120 133.149 1.00 103.20 ? 443  LEU B O     1 
ATOM   9019  C  CB    . LEU B 1 443 ? 174.054 139.105 131.173 1.00 95.22  ? 443  LEU B CB    1 
ATOM   9020  C  CG    . LEU B 1 443 ? 173.762 140.496 130.618 1.00 95.02  ? 443  LEU B CG    1 
ATOM   9021  C  CD1   . LEU B 1 443 ? 174.965 141.052 129.887 1.00 98.52  ? 443  LEU B CD1   1 
ATOM   9022  C  CD2   . LEU B 1 443 ? 172.578 140.416 129.691 1.00 96.66  ? 443  LEU B CD2   1 
ATOM   9023  N  N     . GLU B 1 444 ? 174.275 139.834 134.266 1.00 98.47  ? 444  GLU B N     1 
ATOM   9024  C  CA    . GLU B 1 444 ? 174.064 140.842 135.298 1.00 100.14 ? 444  GLU B CA    1 
ATOM   9025  C  C     . GLU B 1 444 ? 175.255 140.932 136.246 1.00 102.30 ? 444  GLU B C     1 
ATOM   9026  O  O     . GLU B 1 444 ? 175.584 142.019 136.733 1.00 107.55 ? 444  GLU B O     1 
ATOM   9027  C  CB    . GLU B 1 444 ? 172.776 140.533 136.056 1.00 102.72 ? 444  GLU B CB    1 
ATOM   9028  C  CG    . GLU B 1 444 ? 171.528 140.744 135.217 1.00 106.22 ? 444  GLU B CG    1 
ATOM   9029  C  CD    . GLU B 1 444 ? 170.249 140.580 136.008 1.00 117.84 ? 444  GLU B CD    1 
ATOM   9030  O  OE1   . GLU B 1 444 ? 170.318 140.149 137.175 1.00 120.65 ? 444  GLU B OE1   1 
ATOM   9031  O  OE2   . GLU B 1 444 ? 169.169 140.878 135.457 1.00 120.89 ? 444  GLU B OE2   1 
ATOM   9032  N  N     . SER B 1 445 ? 175.913 139.805 136.523 1.00 96.02  ? 445  SER B N     1 
ATOM   9033  C  CA    . SER B 1 445 ? 177.107 139.815 137.357 1.00 96.13  ? 445  SER B CA    1 
ATOM   9034  C  C     . SER B 1 445 ? 178.304 140.416 136.642 1.00 99.01  ? 445  SER B C     1 
ATOM   9035  O  O     . SER B 1 445 ? 179.231 140.888 137.307 1.00 96.34  ? 445  SER B O     1 
ATOM   9036  C  CB    . SER B 1 445 ? 177.442 138.398 137.813 1.00 101.33 ? 445  SER B CB    1 
ATOM   9037  O  OG    . SER B 1 445 ? 178.743 138.345 138.367 1.00 106.80 ? 445  SER B OG    1 
ATOM   9038  N  N     . CYS B 1 446 ? 178.318 140.393 135.307 1.00 100.21 ? 446  CYS B N     1 
ATOM   9039  C  CA    . CYS B 1 446 ? 179.358 141.117 134.586 1.00 100.12 ? 446  CYS B CA    1 
ATOM   9040  C  C     . CYS B 1 446 ? 179.276 142.610 134.868 1.00 104.54 ? 446  CYS B C     1 
ATOM   9041  O  O     . CYS B 1 446 ? 180.303 143.277 135.038 1.00 106.96 ? 446  CYS B O     1 
ATOM   9042  C  CB    . CYS B 1 446 ? 179.247 140.850 133.088 1.00 93.65  ? 446  CYS B CB    1 
ATOM   9043  S  SG    . CYS B 1 446 ? 179.994 139.304 132.570 1.00 104.24 ? 446  CYS B SG    1 
ATOM   9044  N  N     . PHE B 1 447 ? 178.064 143.149 134.930 1.00 102.36 ? 447  PHE B N     1 
ATOM   9045  C  CA    . PHE B 1 447 ? 177.842 144.569 135.153 1.00 97.32  ? 447  PHE B CA    1 
ATOM   9046  C  C     . PHE B 1 447 ? 177.668 144.920 136.622 1.00 98.80  ? 447  PHE B C     1 
ATOM   9047  O  O     . PHE B 1 447 ? 177.397 146.082 136.938 1.00 103.96 ? 447  PHE B O     1 
ATOM   9048  C  CB    . PHE B 1 447 ? 176.620 145.029 134.356 1.00 96.62  ? 447  PHE B CB    1 
ATOM   9049  C  CG    . PHE B 1 447 ? 176.847 145.054 132.876 1.00 101.65 ? 447  PHE B CG    1 
ATOM   9050  C  CD1   . PHE B 1 447 ? 178.095 145.354 132.360 1.00 108.02 ? 447  PHE B CD1   1 
ATOM   9051  C  CD2   . PHE B 1 447 ? 175.815 144.789 131.999 1.00 99.94  ? 447  PHE B CD2   1 
ATOM   9052  C  CE1   . PHE B 1 447 ? 178.307 145.380 130.999 1.00 109.36 ? 447  PHE B CE1   1 
ATOM   9053  C  CE2   . PHE B 1 447 ? 176.021 144.815 130.640 1.00 102.10 ? 447  PHE B CE2   1 
ATOM   9054  C  CZ    . PHE B 1 447 ? 177.268 145.111 130.139 1.00 107.04 ? 447  PHE B CZ    1 
ATOM   9055  N  N     . GLY B 1 448 ? 177.821 143.955 137.521 1.00 100.85 ? 448  GLY B N     1 
ATOM   9056  C  CA    . GLY B 1 448 ? 177.773 144.228 138.947 1.00 105.25 ? 448  GLY B CA    1 
ATOM   9057  C  C     . GLY B 1 448 ? 176.430 144.676 139.479 1.00 102.48 ? 448  GLY B C     1 
ATOM   9058  O  O     . GLY B 1 448 ? 176.378 145.504 140.396 1.00 108.63 ? 448  GLY B O     1 
ATOM   9059  N  N     . PHE B 1 449 ? 175.340 144.154 138.926 1.00 97.35  ? 449  PHE B N     1 
ATOM   9060  C  CA    . PHE B 1 449 ? 174.007 144.406 139.460 1.00 102.41 ? 449  PHE B CA    1 
ATOM   9061  C  C     . PHE B 1 449 ? 173.130 143.237 139.054 1.00 110.26 ? 449  PHE B C     1 
ATOM   9062  O  O     . PHE B 1 449 ? 172.876 143.047 137.862 1.00 113.03 ? 449  PHE B O     1 
ATOM   9063  C  CB    . PHE B 1 449 ? 173.429 145.720 138.937 1.00 100.82 ? 449  PHE B CB    1 
ATOM   9064  C  CG    . PHE B 1 449 ? 171.936 145.828 139.079 1.00 105.56 ? 449  PHE B CG    1 
ATOM   9065  C  CD1   . PHE B 1 449 ? 171.370 146.204 140.281 1.00 105.14 ? 449  PHE B CD1   1 
ATOM   9066  C  CD2   . PHE B 1 449 ? 171.101 145.564 138.009 1.00 107.53 ? 449  PHE B CD2   1 
ATOM   9067  C  CE1   . PHE B 1 449 ? 170.001 146.308 140.416 1.00 107.91 ? 449  PHE B CE1   1 
ATOM   9068  C  CE2   . PHE B 1 449 ? 169.731 145.664 138.140 1.00 105.92 ? 449  PHE B CE2   1 
ATOM   9069  C  CZ    . PHE B 1 449 ? 169.181 146.037 139.345 1.00 105.90 ? 449  PHE B CZ    1 
ATOM   9070  N  N     . ILE B 1 450 ? 172.666 142.463 140.028 1.00 111.44 ? 450  ILE B N     1 
ATOM   9071  C  CA    . ILE B 1 450 ? 171.926 141.240 139.755 1.00 108.93 ? 450  ILE B CA    1 
ATOM   9072  C  C     . ILE B 1 450 ? 170.611 141.270 140.516 1.00 113.24 ? 450  ILE B C     1 
ATOM   9073  O  O     . ILE B 1 450 ? 170.584 141.521 141.725 1.00 116.90 ? 450  ILE B O     1 
ATOM   9074  C  CB    . ILE B 1 450 ? 172.749 139.987 140.120 1.00 106.52 ? 450  ILE B CB    1 
ATOM   9075  C  CG1   . ILE B 1 450 ? 171.874 138.743 140.120 1.00 111.83 ? 450  ILE B CG1   1 
ATOM   9076  C  CG2   . ILE B 1 450 ? 173.386 140.135 141.477 1.00 105.92 ? 450  ILE B CG2   1 
ATOM   9077  C  CD1   . ILE B 1 450 ? 172.643 137.504 140.465 1.00 115.70 ? 450  ILE B CD1   1 
ATOM   9078  N  N     . SER B 1 451 ? 169.518 141.024 139.800 1.00 118.97 ? 451  SER B N     1 
ATOM   9079  C  CA    . SER B 1 451 ? 168.194 140.904 140.395 1.00 125.22 ? 451  SER B CA    1 
ATOM   9080  C  C     . SER B 1 451 ? 168.045 139.469 140.883 1.00 126.07 ? 451  SER B C     1 
ATOM   9081  O  O     . SER B 1 451 ? 167.812 138.557 140.084 1.00 125.52 ? 451  SER B O     1 
ATOM   9082  C  CB    . SER B 1 451 ? 167.104 141.262 139.388 1.00 127.99 ? 451  SER B CB    1 
ATOM   9083  O  OG    . SER B 1 451 ? 167.241 142.599 138.941 1.00 126.56 ? 451  SER B OG    1 
ATOM   9084  N  N     . VAL B 1 452 ? 168.184 139.274 142.193 1.00 128.50 ? 452  VAL B N     1 
ATOM   9085  C  CA    . VAL B 1 452 ? 168.247 137.930 142.751 1.00 129.58 ? 452  VAL B CA    1 
ATOM   9086  C  C     . VAL B 1 452 ? 166.924 137.215 142.524 1.00 134.17 ? 452  VAL B C     1 
ATOM   9087  O  O     . VAL B 1 452 ? 165.848 137.825 142.579 1.00 135.00 ? 452  VAL B O     1 
ATOM   9088  C  CB    . VAL B 1 452 ? 168.613 137.986 144.242 1.00 121.81 ? 452  VAL B CB    1 
ATOM   9089  C  CG1   . VAL B 1 452 ? 169.912 138.748 144.438 1.00 116.53 ? 452  VAL B CG1   1 
ATOM   9090  C  CG2   . VAL B 1 452 ? 167.507 138.645 145.031 1.00 123.76 ? 452  VAL B CG2   1 
ATOM   9091  N  N     . LEU B 1 453 ? 167.002 135.923 142.228 1.00 135.08 ? 453  LEU B N     1 
ATOM   9092  C  CA    . LEU B 1 453 ? 165.797 135.122 142.096 1.00 136.68 ? 453  LEU B CA    1 
ATOM   9093  C  C     . LEU B 1 453 ? 165.126 134.975 143.458 1.00 137.43 ? 453  LEU B C     1 
ATOM   9094  O  O     . LEU B 1 453 ? 165.811 134.823 144.475 1.00 134.54 ? 453  LEU B O     1 
ATOM   9095  C  CB    . LEU B 1 453 ? 166.127 133.742 141.527 1.00 134.55 ? 453  LEU B CB    1 
ATOM   9096  C  CG    . LEU B 1 453 ? 166.374 133.640 140.022 1.00 129.61 ? 453  LEU B CG    1 
ATOM   9097  C  CD1   . LEU B 1 453 ? 166.826 132.236 139.653 1.00 117.73 ? 453  LEU B CD1   1 
ATOM   9098  C  CD2   . LEU B 1 453 ? 165.126 134.025 139.249 1.00 125.79 ? 453  LEU B CD2   1 
ATOM   9099  N  N     . PRO B 1 454 ? 163.797 135.028 143.518 1.00 138.37 ? 454  PRO B N     1 
ATOM   9100  C  CA    . PRO B 1 454 ? 163.117 134.819 144.800 1.00 134.71 ? 454  PRO B CA    1 
ATOM   9101  C  C     . PRO B 1 454 ? 163.338 133.404 145.310 1.00 130.75 ? 454  PRO B C     1 
ATOM   9102  O  O     . PRO B 1 454 ? 163.271 132.432 144.556 1.00 122.85 ? 454  PRO B O     1 
ATOM   9103  C  CB    . PRO B 1 454 ? 161.645 135.084 144.469 1.00 130.48 ? 454  PRO B CB    1 
ATOM   9104  C  CG    . PRO B 1 454 ? 161.540 134.851 143.004 1.00 132.72 ? 454  PRO B CG    1 
ATOM   9105  C  CD    . PRO B 1 454 ? 162.851 135.280 142.421 1.00 135.40 ? 454  PRO B CD    1 
ATOM   9106  N  N     . GLY B 1 455 ? 163.610 133.299 146.608 1.00 131.81 ? 455  GLY B N     1 
ATOM   9107  C  CA    . GLY B 1 455 ? 163.920 132.030 147.228 1.00 130.01 ? 455  GLY B CA    1 
ATOM   9108  C  C     . GLY B 1 455 ? 165.348 131.565 147.059 1.00 129.78 ? 455  GLY B C     1 
ATOM   9109  O  O     . GLY B 1 455 ? 165.712 130.523 147.619 1.00 126.75 ? 455  GLY B O     1 
ATOM   9110  N  N     . ALA B 1 456 ? 166.171 132.300 146.316 1.00 127.53 ? 456  ALA B N     1 
ATOM   9111  C  CA    . ALA B 1 456 ? 167.558 131.916 146.125 1.00 118.09 ? 456  ALA B CA    1 
ATOM   9112  C  C     . ALA B 1 456 ? 168.350 132.137 147.409 1.00 108.79 ? 456  ALA B C     1 
ATOM   9113  O  O     . ALA B 1 456 ? 168.029 132.996 148.233 1.00 106.79 ? 456  ALA B O     1 
ATOM   9114  C  CB    . ALA B 1 456 ? 168.182 132.702 144.972 1.00 113.62 ? 456  ALA B CB    1 
ATOM   9115  N  N     . PHE B 1 457 ? 169.401 131.342 147.575 1.00 102.95 ? 457  PHE B N     1 
ATOM   9116  C  CA    . PHE B 1 457 ? 170.282 131.443 148.730 1.00 96.76  ? 457  PHE B CA    1 
ATOM   9117  C  C     . PHE B 1 457 ? 171.197 132.641 148.506 1.00 97.59  ? 457  PHE B C     1 
ATOM   9118  O  O     . PHE B 1 457 ? 172.250 132.518 147.872 1.00 102.59 ? 457  PHE B O     1 
ATOM   9119  C  CB    . PHE B 1 457 ? 171.072 130.152 148.923 1.00 90.95  ? 457  PHE B CB    1 
ATOM   9120  C  CG    . PHE B 1 457 ? 172.285 130.302 149.788 1.00 93.85  ? 457  PHE B CG    1 
ATOM   9121  C  CD1   . PHE B 1 457 ? 172.161 130.669 151.116 1.00 96.70  ? 457  PHE B CD1   1 
ATOM   9122  C  CD2   . PHE B 1 457 ? 173.545 130.055 149.282 1.00 98.09  ? 457  PHE B CD2   1 
ATOM   9123  C  CE1   . PHE B 1 457 ? 173.273 130.802 151.917 1.00 101.42 ? 457  PHE B CE1   1 
ATOM   9124  C  CE2   . PHE B 1 457 ? 174.658 130.183 150.079 1.00 103.93 ? 457  PHE B CE2   1 
ATOM   9125  C  CZ    . PHE B 1 457 ? 174.522 130.559 151.399 1.00 106.35 ? 457  PHE B CZ    1 
ATOM   9126  N  N     . SER B 1 458 ? 170.782 133.799 149.006 1.00 91.52  ? 458  SER B N     1 
ATOM   9127  C  CA    . SER B 1 458 ? 171.498 135.049 148.811 1.00 89.77  ? 458  SER B CA    1 
ATOM   9128  C  C     . SER B 1 458 ? 172.142 135.486 150.117 1.00 89.03  ? 458  SER B C     1 
ATOM   9129  O  O     . SER B 1 458 ? 171.620 135.245 151.207 1.00 94.42  ? 458  SER B O     1 
ATOM   9130  C  CB    . SER B 1 458 ? 170.561 136.143 148.290 1.00 94.65  ? 458  SER B CB    1 
ATOM   9131  O  OG    . SER B 1 458 ? 169.446 136.303 149.145 1.00 99.07  ? 458  SER B OG    1 
ATOM   9132  N  N     . ALA B 1 459 ? 173.291 136.141 149.995 1.00 87.59  ? 459  ALA B N     1 
ATOM   9133  C  CA    . ALA B 1 459 ? 174.013 136.624 151.160 1.00 83.75  ? 459  ALA B CA    1 
ATOM   9134  C  C     . ALA B 1 459 ? 174.499 138.037 150.894 1.00 90.85  ? 459  ALA B C     1 
ATOM   9135  O  O     . ALA B 1 459 ? 174.822 138.396 149.760 1.00 100.94 ? 459  ALA B O     1 
ATOM   9136  C  CB    . ALA B 1 459 ? 175.200 135.722 151.508 1.00 86.69  ? 459  ALA B CB    1 
ATOM   9137  N  N     . TYR B 1 460 ? 174.552 138.835 151.956 1.00 91.17  ? 460  TYR B N     1 
ATOM   9138  C  CA    . TYR B 1 460 ? 175.056 140.195 151.886 1.00 92.91  ? 460  TYR B CA    1 
ATOM   9139  C  C     . TYR B 1 460 ? 176.102 140.373 152.974 1.00 93.09  ? 460  TYR B C     1 
ATOM   9140  O  O     . TYR B 1 460 ? 176.253 139.530 153.862 1.00 100.47 ? 460  TYR B O     1 
ATOM   9141  C  CB    . TYR B 1 460 ? 173.936 141.224 152.058 1.00 87.98  ? 460  TYR B CB    1 
ATOM   9142  C  CG    . TYR B 1 460 ? 172.711 140.979 151.213 1.00 89.86  ? 460  TYR B CG    1 
ATOM   9143  C  CD1   . TYR B 1 460 ? 171.693 140.150 151.657 1.00 91.65  ? 460  TYR B CD1   1 
ATOM   9144  C  CD2   . TYR B 1 460 ? 172.558 141.602 149.984 1.00 95.43  ? 460  TYR B CD2   1 
ATOM   9145  C  CE1   . TYR B 1 460 ? 170.567 139.933 150.894 1.00 100.60 ? 460  TYR B CE1   1 
ATOM   9146  C  CE2   . TYR B 1 460 ? 171.436 141.391 149.214 1.00 99.50  ? 460  TYR B CE2   1 
ATOM   9147  C  CZ    . TYR B 1 460 ? 170.444 140.556 149.673 1.00 106.13 ? 460  TYR B CZ    1 
ATOM   9148  O  OH    . TYR B 1 460 ? 169.322 140.342 148.909 1.00 112.76 ? 460  TYR B OH    1 
ATOM   9149  N  N     . ARG B 1 461 ? 176.826 141.482 152.910 1.00 88.22  ? 461  ARG B N     1 
ATOM   9150  C  CA    . ARG B 1 461 ? 177.719 141.881 153.984 1.00 95.67  ? 461  ARG B CA    1 
ATOM   9151  C  C     . ARG B 1 461 ? 177.072 143.027 154.747 1.00 101.49 ? 461  ARG B C     1 
ATOM   9152  O  O     . ARG B 1 461 ? 176.481 143.930 154.147 1.00 107.30 ? 461  ARG B O     1 
ATOM   9153  C  CB    . ARG B 1 461 ? 179.106 142.270 153.454 1.00 94.72  ? 461  ARG B CB    1 
ATOM   9154  C  CG    . ARG B 1 461 ? 179.260 143.703 152.998 1.00 98.51  ? 461  ARG B CG    1 
ATOM   9155  C  CD    . ARG B 1 461 ? 180.718 144.063 152.774 1.00 100.97 ? 461  ARG B CD    1 
ATOM   9156  N  NE    . ARG B 1 461 ? 181.340 143.258 151.731 1.00 98.41  ? 461  ARG B NE    1 
ATOM   9157  C  CZ    . ARG B 1 461 ? 182.410 142.498 151.915 1.00 100.41 ? 461  ARG B CZ    1 
ATOM   9158  N  NH1   . ARG B 1 461 ? 183.005 142.418 153.093 1.00 101.28 ? 461  ARG B NH1   1 
ATOM   9159  N  NH2   . ARG B 1 461 ? 182.898 141.805 150.891 1.00 103.06 ? 461  ARG B NH2   1 
ATOM   9160  N  N     . TYR B 1 462 ? 177.144 142.965 156.074 1.00 102.89 ? 462  TYR B N     1 
ATOM   9161  C  CA    . TYR B 1 462 ? 176.430 143.933 156.896 1.00 103.38 ? 462  TYR B CA    1 
ATOM   9162  C  C     . TYR B 1 462 ? 177.218 145.228 157.027 1.00 106.35 ? 462  TYR B C     1 
ATOM   9163  O  O     . TYR B 1 462 ? 177.473 145.704 158.137 1.00 114.52 ? 462  TYR B O     1 
ATOM   9164  C  CB    . TYR B 1 462 ? 176.133 143.350 158.275 1.00 106.48 ? 462  TYR B CB    1 
ATOM   9165  C  CG    . TYR B 1 462 ? 174.869 143.894 158.886 1.00 105.68 ? 462  TYR B CG    1 
ATOM   9166  C  CD1   . TYR B 1 462 ? 173.633 143.607 158.332 1.00 103.72 ? 462  TYR B CD1   1 
ATOM   9167  C  CD2   . TYR B 1 462 ? 174.911 144.704 160.009 1.00 111.31 ? 462  TYR B CD2   1 
ATOM   9168  C  CE1   . TYR B 1 462 ? 172.475 144.105 158.882 1.00 111.63 ? 462  TYR B CE1   1 
ATOM   9169  C  CE2   . TYR B 1 462 ? 173.758 145.208 160.566 1.00 117.24 ? 462  TYR B CE2   1 
ATOM   9170  C  CZ    . TYR B 1 462 ? 172.542 144.906 159.997 1.00 119.68 ? 462  TYR B CZ    1 
ATOM   9171  O  OH    . TYR B 1 462 ? 171.385 145.404 160.548 1.00 124.21 ? 462  TYR B OH    1 
ATOM   9172  N  N     . GLU B 1 463 ? 177.610 145.796 155.891 1.00 105.06 ? 463  GLU B N     1 
ATOM   9173  C  CA    . GLU B 1 463 ? 178.233 147.109 155.836 1.00 107.67 ? 463  GLU B CA    1 
ATOM   9174  C  C     . GLU B 1 463 ? 177.565 147.888 154.715 1.00 112.97 ? 463  GLU B C     1 
ATOM   9175  O  O     . GLU B 1 463 ? 177.544 149.123 154.721 1.00 122.18 ? 463  GLU B O     1 
ATOM   9176  C  CB    . GLU B 1 463 ? 179.740 146.986 155.610 1.00 112.64 ? 463  GLU B CB    1 
ATOM   9177  C  CG    . GLU B 1 463 ? 180.528 148.256 155.869 1.00 122.64 ? 463  GLU B CG    1 
ATOM   9178  C  CD    . GLU B 1 463 ? 182.019 148.060 155.675 1.00 133.37 ? 463  GLU B CD    1 
ATOM   9179  O  OE1   . GLU B 1 463 ? 182.447 146.903 155.483 1.00 131.10 ? 463  GLU B OE1   1 
ATOM   9180  O  OE2   . GLU B 1 463 ? 182.765 149.061 155.711 1.00 140.02 ? 463  GLU B OE2   1 
ATOM   9181  N  N     . ALA B 1 464 ? 177.012 147.154 153.751 1.00 110.12 ? 464  ALA B N     1 
ATOM   9182  C  CA    . ALA B 1 464 ? 176.277 147.727 152.634 1.00 112.91 ? 464  ALA B CA    1 
ATOM   9183  C  C     . ALA B 1 464 ? 174.773 147.650 152.819 1.00 114.18 ? 464  ALA B C     1 
ATOM   9184  O  O     . ALA B 1 464 ? 174.028 147.997 151.899 1.00 122.31 ? 464  ALA B O     1 
ATOM   9185  C  CB    . ALA B 1 464 ? 176.650 147.012 151.335 1.00 110.09 ? 464  ALA B CB    1 
ATOM   9186  N  N     . ILE B 1 465 ? 174.317 147.188 153.975 1.00 107.92 ? 465  ILE B N     1 
ATOM   9187  C  CA    . ILE B 1 465 ? 172.909 146.953 154.239 1.00 108.69 ? 465  ILE B CA    1 
ATOM   9188  C  C     . ILE B 1 465 ? 172.474 147.616 155.548 1.00 116.37 ? 465  ILE B C     1 
ATOM   9189  O  O     . ILE B 1 465 ? 171.281 147.751 155.812 1.00 116.55 ? 465  ILE B O     1 
ATOM   9190  C  CB    . ILE B 1 465 ? 172.610 145.441 154.194 1.00 105.47 ? 465  ILE B CB    1 
ATOM   9191  C  CG1   . ILE B 1 465 ? 171.987 145.064 152.852 1.00 101.99 ? 465  ILE B CG1   1 
ATOM   9192  C  CG2   . ILE B 1 465 ? 171.805 144.935 155.372 1.00 110.64 ? 465  ILE B CG2   1 
ATOM   9193  C  CD1   . ILE B 1 465 ? 171.457 143.667 152.821 1.00 103.73 ? 465  ILE B CD1   1 
ATOM   9194  N  N     . ARG B 1 466 ? 173.441 148.139 156.306 1.00 117.97 ? 466  ARG B N     1 
ATOM   9195  C  CA    . ARG B 1 466 ? 173.199 148.621 157.663 1.00 115.80 ? 466  ARG B CA    1 
ATOM   9196  C  C     . ARG B 1 466 ? 172.021 149.586 157.735 1.00 117.81 ? 466  ARG B C     1 
ATOM   9197  O  O     . ARG B 1 466 ? 171.115 149.411 158.558 1.00 118.44 ? 466  ARG B O     1 
ATOM   9198  C  CB    . ARG B 1 466 ? 174.466 149.291 158.192 1.00 119.64 ? 466  ARG B CB    1 
ATOM   9199  C  CG    . ARG B 1 466 ? 174.358 149.842 159.599 1.00 123.99 ? 466  ARG B CG    1 
ATOM   9200  C  CD    . ARG B 1 466 ? 174.358 148.749 160.642 1.00 120.51 ? 466  ARG B CD    1 
ATOM   9201  N  NE    . ARG B 1 466 ? 174.911 149.230 161.901 1.00 125.43 ? 466  ARG B NE    1 
ATOM   9202  C  CZ    . ARG B 1 466 ? 174.220 149.896 162.816 1.00 127.10 ? 466  ARG B CZ    1 
ATOM   9203  N  NH1   . ARG B 1 466 ? 172.939 150.175 162.645 1.00 127.95 ? 466  ARG B NH1   1 
ATOM   9204  N  NH2   . ARG B 1 466 ? 174.830 150.292 163.929 1.00 127.19 ? 466  ARG B NH2   1 
ATOM   9205  N  N     . GLY B 1 467 ? 172.006 150.605 156.882 1.00 119.31 ? 467  GLY B N     1 
ATOM   9206  C  CA    . GLY B 1 467 ? 171.042 151.679 157.046 1.00 120.92 ? 467  GLY B CA    1 
ATOM   9207  C  C     . GLY B 1 467 ? 169.986 151.813 155.970 1.00 119.67 ? 467  GLY B C     1 
ATOM   9208  O  O     . GLY B 1 467 ? 168.960 151.124 155.995 1.00 118.81 ? 467  GLY B O     1 
ATOM   9209  N  N     . ALA B 1 468 ? 170.230 152.730 155.033 1.00 121.04 ? 468  ALA B N     1 
ATOM   9210  C  CA    . ALA B 1 468 ? 169.235 153.050 154.014 1.00 118.35 ? 468  ALA B CA    1 
ATOM   9211  C  C     . ALA B 1 468 ? 168.750 151.847 153.212 1.00 117.82 ? 468  ALA B C     1 
ATOM   9212  O  O     . ALA B 1 468 ? 167.543 151.793 152.917 1.00 121.79 ? 468  ALA B O     1 
ATOM   9213  C  CB    . ALA B 1 468 ? 169.789 154.134 153.080 1.00 116.38 ? 468  ALA B CB    1 
ATOM   9214  N  N     . PRO B 1 469 ? 169.595 150.894 152.794 1.00 114.57 ? 469  PRO B N     1 
ATOM   9215  C  CA    . PRO B 1 469 ? 169.048 149.719 152.098 1.00 112.34 ? 469  PRO B CA    1 
ATOM   9216  C  C     . PRO B 1 469 ? 168.007 148.965 152.906 1.00 117.11 ? 469  PRO B C     1 
ATOM   9217  O  O     . PRO B 1 469 ? 166.931 148.662 152.378 1.00 119.24 ? 469  PRO B O     1 
ATOM   9218  C  CB    . PRO B 1 469 ? 170.292 148.865 151.833 1.00 111.87 ? 469  PRO B CB    1 
ATOM   9219  C  CG    . PRO B 1 469 ? 171.384 149.847 151.727 1.00 114.20 ? 469  PRO B CG    1 
ATOM   9220  C  CD    . PRO B 1 469 ? 171.068 150.913 152.732 1.00 115.82 ? 469  PRO B CD    1 
ATOM   9221  N  N     . LEU B 1 470 ? 168.280 148.666 154.180 1.00 117.94 ? 470  LEU B N     1 
ATOM   9222  C  CA    . LEU B 1 470 ? 167.287 147.949 154.973 1.00 114.35 ? 470  LEU B CA    1 
ATOM   9223  C  C     . LEU B 1 470 ? 166.065 148.813 155.245 1.00 119.89 ? 470  LEU B C     1 
ATOM   9224  O  O     . LEU B 1 470 ? 164.944 148.296 155.312 1.00 120.03 ? 470  LEU B O     1 
ATOM   9225  C  CB    . LEU B 1 470 ? 167.864 147.485 156.308 1.00 109.94 ? 470  LEU B CB    1 
ATOM   9226  C  CG    . LEU B 1 470 ? 168.484 146.092 156.412 1.00 109.64 ? 470  LEU B CG    1 
ATOM   9227  C  CD1   . LEU B 1 470 ? 169.448 146.052 157.592 1.00 116.86 ? 470  LEU B CD1   1 
ATOM   9228  C  CD2   . LEU B 1 470 ? 167.465 144.986 156.481 1.00 112.01 ? 470  LEU B CD2   1 
ATOM   9229  N  N     . ASP B 1 471 ? 166.265 150.119 155.438 1.00 123.20 ? 471  ASP B N     1 
ATOM   9230  C  CA    . ASP B 1 471 ? 165.130 151.010 155.654 1.00 122.15 ? 471  ASP B CA    1 
ATOM   9231  C  C     . ASP B 1 471 ? 164.192 150.993 154.456 1.00 123.95 ? 471  ASP B C     1 
ATOM   9232  O  O     . ASP B 1 471 ? 162.970 150.881 154.612 1.00 126.37 ? 471  ASP B O     1 
ATOM   9233  C  CB    . ASP B 1 471 ? 165.627 152.428 155.931 1.00 123.98 ? 471  ASP B CB    1 
ATOM   9234  C  CG    . ASP B 1 471 ? 165.436 152.840 157.376 1.00 133.18 ? 471  ASP B CG    1 
ATOM   9235  O  OD1   . ASP B 1 471 ? 165.163 151.956 158.214 1.00 134.07 ? 471  ASP B OD1   1 
ATOM   9236  O  OD2   . ASP B 1 471 ? 165.564 154.046 157.674 1.00 139.61 ? 471  ASP B OD2   1 
ATOM   9237  N  N     . ALA B 1 472 ? 164.747 151.083 153.246 1.00 123.66 ? 472  ALA B N     1 
ATOM   9238  C  CA    . ALA B 1 472 ? 163.924 150.963 152.048 1.00 120.28 ? 472  ALA B CA    1 
ATOM   9239  C  C     . ALA B 1 472 ? 163.284 149.585 151.962 1.00 118.48 ? 472  ALA B C     1 
ATOM   9240  O  O     . ALA B 1 472 ? 162.111 149.461 151.599 1.00 126.63 ? 472  ALA B O     1 
ATOM   9241  C  CB    . ALA B 1 472 ? 164.761 151.245 150.802 1.00 118.61 ? 472  ALA B CB    1 
ATOM   9242  N  N     . TYR B 1 473 ? 164.040 148.541 152.310 1.00 115.09 ? 473  TYR B N     1 
ATOM   9243  C  CA    . TYR B 1 473 ? 163.524 147.176 152.264 1.00 116.51 ? 473  TYR B CA    1 
ATOM   9244  C  C     . TYR B 1 473 ? 162.272 147.023 153.121 1.00 119.12 ? 473  TYR B C     1 
ATOM   9245  O  O     . TYR B 1 473 ? 161.277 146.438 152.679 1.00 117.20 ? 473  TYR B O     1 
ATOM   9246  C  CB    . TYR B 1 473 ? 164.624 146.217 152.725 1.00 117.45 ? 473  TYR B CB    1 
ATOM   9247  C  CG    . TYR B 1 473 ? 164.343 144.739 152.572 1.00 114.38 ? 473  TYR B CG    1 
ATOM   9248  C  CD1   . TYR B 1 473 ? 163.345 144.274 151.734 1.00 115.73 ? 473  TYR B CD1   1 
ATOM   9249  C  CD2   . TYR B 1 473 ? 165.089 143.805 153.277 1.00 112.64 ? 473  TYR B CD2   1 
ATOM   9250  C  CE1   . TYR B 1 473 ? 163.101 142.921 151.603 1.00 115.73 ? 473  TYR B CE1   1 
ATOM   9251  C  CE2   . TYR B 1 473 ? 164.850 142.455 153.152 1.00 112.25 ? 473  TYR B CE2   1 
ATOM   9252  C  CZ    . TYR B 1 473 ? 163.855 142.018 152.315 1.00 111.70 ? 473  TYR B CZ    1 
ATOM   9253  O  OH    . TYR B 1 473 ? 163.613 140.671 152.187 1.00 113.87 ? 473  TYR B OH    1 
ATOM   9254  N  N     . PHE B 1 474 ? 162.299 147.549 154.344 1.00 122.78 ? 474  PHE B N     1 
ATOM   9255  C  CA    . PHE B 1 474 ? 161.191 147.410 155.282 1.00 121.15 ? 474  PHE B CA    1 
ATOM   9256  C  C     . PHE B 1 474 ? 160.293 148.638 155.331 1.00 126.52 ? 474  PHE B C     1 
ATOM   9257  O  O     . PHE B 1 474 ? 159.538 148.802 156.296 1.00 129.16 ? 474  PHE B O     1 
ATOM   9258  C  CB    . PHE B 1 474 ? 161.714 147.102 156.683 1.00 118.14 ? 474  PHE B CB    1 
ATOM   9259  C  CG    . PHE B 1 474 ? 162.510 145.842 156.759 1.00 110.13 ? 474  PHE B CG    1 
ATOM   9260  C  CD1   . PHE B 1 474 ? 162.096 144.712 156.085 1.00 111.56 ? 474  PHE B CD1   1 
ATOM   9261  C  CD2   . PHE B 1 474 ? 163.662 145.781 157.512 1.00 108.44 ? 474  PHE B CD2   1 
ATOM   9262  C  CE1   . PHE B 1 474 ? 162.826 143.549 156.150 1.00 112.57 ? 474  PHE B CE1   1 
ATOM   9263  C  CE2   . PHE B 1 474 ? 164.385 144.618 157.587 1.00 109.17 ? 474  PHE B CE2   1 
ATOM   9264  C  CZ    . PHE B 1 474 ? 163.975 143.504 156.897 1.00 108.68 ? 474  PHE B CZ    1 
ATOM   9265  N  N     . GLN B 1 475 ? 160.408 149.530 154.346 1.00 129.93 ? 475  GLN B N     1 
ATOM   9266  C  CA    . GLN B 1 475 ? 159.493 150.662 154.243 1.00 129.19 ? 475  GLN B CA    1 
ATOM   9267  C  C     . GLN B 1 475 ? 158.035 150.218 154.243 1.00 130.29 ? 475  GLN B C     1 
ATOM   9268  O  O     . GLN B 1 475 ? 157.171 150.909 154.794 1.00 136.16 ? 475  GLN B O     1 
ATOM   9269  C  CB    . GLN B 1 475 ? 159.822 151.460 152.981 1.00 130.21 ? 475  GLN B CB    1 
ATOM   9270  C  CG    . GLN B 1 475 ? 158.958 152.676 152.739 1.00 137.29 ? 475  GLN B CG    1 
ATOM   9271  C  CD    . GLN B 1 475 ? 159.464 153.501 151.574 1.00 146.05 ? 475  GLN B CD    1 
ATOM   9272  O  OE1   . GLN B 1 475 ? 158.698 154.219 150.932 1.00 152.66 ? 475  GLN B OE1   1 
ATOM   9273  N  NE2   . GLN B 1 475 ? 160.754 153.401 151.290 1.00 142.46 ? 475  GLN B NE2   1 
ATOM   9274  N  N     . THR B 1 476 ? 157.738 149.066 153.637 1.00 128.74 ? 476  THR B N     1 
ATOM   9275  C  CA    . THR B 1 476 ? 156.358 148.586 153.607 1.00 131.44 ? 476  THR B CA    1 
ATOM   9276  C  C     . THR B 1 476 ? 155.839 148.290 155.009 1.00 132.44 ? 476  THR B C     1 
ATOM   9277  O  O     . THR B 1 476 ? 154.686 148.597 155.330 1.00 133.58 ? 476  THR B O     1 
ATOM   9278  C  CB    . THR B 1 476 ? 156.251 147.345 152.723 1.00 133.10 ? 476  THR B CB    1 
ATOM   9279  O  OG1   . THR B 1 476 ? 156.467 147.718 151.360 1.00 139.55 ? 476  THR B OG1   1 
ATOM   9280  C  CG2   . THR B 1 476 ? 154.876 146.710 152.849 1.00 129.21 ? 476  THR B CG2   1 
ATOM   9281  N  N     . LEU B 1 477 ? 156.672 147.686 155.857 1.00 132.75 ? 477  LEU B N     1 
ATOM   9282  C  CA    . LEU B 1 477 ? 156.248 147.410 157.224 1.00 129.32 ? 477  LEU B CA    1 
ATOM   9283  C  C     . LEU B 1 477 ? 156.223 148.672 158.072 1.00 132.32 ? 477  LEU B C     1 
ATOM   9284  O  O     . LEU B 1 477 ? 155.309 148.855 158.883 1.00 133.41 ? 477  LEU B O     1 
ATOM   9285  C  CB    . LEU B 1 477 ? 157.168 146.370 157.856 1.00 123.72 ? 477  LEU B CB    1 
ATOM   9286  C  CG    . LEU B 1 477 ? 157.051 144.963 157.281 1.00 120.64 ? 477  LEU B CG    1 
ATOM   9287  C  CD1   . LEU B 1 477 ? 157.842 144.006 158.131 1.00 120.16 ? 477  LEU B CD1   1 
ATOM   9288  C  CD2   . LEU B 1 477 ? 155.598 144.538 157.208 1.00 122.10 ? 477  LEU B CD2   1 
ATOM   9289  N  N     . ASN B 1 478 ? 157.215 149.546 157.905 1.00 133.92 ? 478  ASN B N     1 
ATOM   9290  C  CA    . ASN B 1 478 ? 157.291 150.742 158.737 1.00 132.99 ? 478  ASN B CA    1 
ATOM   9291  C  C     . ASN B 1 478 ? 156.157 151.714 158.429 1.00 134.43 ? 478  ASN B C     1 
ATOM   9292  O  O     . ASN B 1 478 ? 155.589 152.321 159.344 1.00 137.04 ? 478  ASN B O     1 
ATOM   9293  C  CB    . ASN B 1 478 ? 158.647 151.420 158.556 1.00 132.49 ? 478  ASN B CB    1 
ATOM   9294  C  CG    . ASN B 1 478 ? 159.793 150.564 159.053 1.00 134.11 ? 478  ASN B CG    1 
ATOM   9295  O  OD1   . ASN B 1 478 ? 159.632 149.762 159.972 1.00 131.10 ? 478  ASN B OD1   1 
ATOM   9296  N  ND2   . ASN B 1 478 ? 160.960 150.731 158.445 1.00 136.53 ? 478  ASN B ND2   1 
ATOM   9297  N  N     . ILE B 1 479 ? 155.813 151.877 157.155 1.00 135.23 ? 479  ILE B N     1 
ATOM   9298  C  CA    . ILE B 1 479 ? 154.781 152.812 156.721 1.00 138.88 ? 479  ILE B CA    1 
ATOM   9299  C  C     . ILE B 1 479 ? 153.630 152.013 156.129 1.00 145.67 ? 479  ILE B C     1 
ATOM   9300  O  O     . ILE B 1 479 ? 153.839 151.194 155.229 1.00 148.14 ? 479  ILE B O     1 
ATOM   9301  C  CB    . ILE B 1 479 ? 155.331 153.823 155.700 1.00 137.36 ? 479  ILE B CB    1 
ATOM   9302  C  CG1   . ILE B 1 479 ? 156.485 154.615 156.314 1.00 135.51 ? 479  ILE B CG1   1 
ATOM   9303  C  CG2   . ILE B 1 479 ? 154.232 154.755 155.232 1.00 140.01 ? 479  ILE B CG2   1 
ATOM   9304  C  CD1   . ILE B 1 479 ? 157.106 155.615 155.371 1.00 136.06 ? 479  ILE B CD1   1 
ATOM   9305  N  N     . GLU B 1 480 ? 152.419 152.261 156.625 1.00 151.39 ? 480  GLU B N     1 
ATOM   9306  C  CA    . GLU B 1 480 ? 151.260 151.485 156.210 1.00 154.13 ? 480  GLU B CA    1 
ATOM   9307  C  C     . GLU B 1 480 ? 150.984 151.666 154.720 1.00 155.26 ? 480  GLU B C     1 
ATOM   9308  O  O     . GLU B 1 480 ? 151.328 152.682 154.110 1.00 153.46 ? 480  GLU B O     1 
ATOM   9309  C  CB    . GLU B 1 480 ? 150.027 151.869 157.034 1.00 155.45 ? 480  GLU B CB    1 
ATOM   9310  C  CG    . GLU B 1 480 ? 149.430 153.245 156.749 1.00 158.30 ? 480  GLU B CG    1 
ATOM   9311  C  CD    . GLU B 1 480 ? 150.250 154.391 157.322 1.00 159.01 ? 480  GLU B CD    1 
ATOM   9312  O  OE1   . GLU B 1 480 ? 149.635 155.352 157.831 1.00 161.42 ? 480  GLU B OE1   1 
ATOM   9313  O  OE2   . GLU B 1 480 ? 151.495 154.350 157.260 1.00 156.27 ? 480  GLU B OE2   1 
ATOM   9314  N  N     . LEU B 1 481 ? 150.348 150.646 154.138 1.00 157.63 ? 481  LEU B N     1 
ATOM   9315  C  CA    . LEU B 1 481 ? 150.189 150.563 152.690 1.00 158.21 ? 481  LEU B CA    1 
ATOM   9316  C  C     . LEU B 1 481 ? 149.347 151.696 152.123 1.00 159.47 ? 481  LEU B C     1 
ATOM   9317  O  O     . LEU B 1 481 ? 149.374 151.927 150.911 1.00 155.66 ? 481  LEU B O     1 
ATOM   9318  C  CB    . LEU B 1 481 ? 149.566 149.217 152.320 1.00 157.22 ? 481  LEU B CB    1 
ATOM   9319  C  CG    . LEU B 1 481 ? 150.559 148.181 151.794 1.00 156.53 ? 481  LEU B CG    1 
ATOM   9320  C  CD1   . LEU B 1 481 ? 149.944 146.796 151.778 1.00 158.47 ? 481  LEU B CD1   1 
ATOM   9321  C  CD2   . LEU B 1 481 ? 151.026 148.573 150.415 1.00 157.11 ? 481  LEU B CD2   1 
ATOM   9322  N  N     . ASP B 1 482 ? 148.588 152.399 152.963 1.00 163.25 ? 482  ASP B N     1 
ATOM   9323  C  CA    . ASP B 1 482 ? 147.725 153.467 152.467 1.00 164.86 ? 482  ASP B CA    1 
ATOM   9324  C  C     . ASP B 1 482 ? 148.532 154.637 151.918 1.00 160.10 ? 482  ASP B C     1 
ATOM   9325  O  O     . ASP B 1 482 ? 148.181 155.211 150.882 1.00 159.44 ? 482  ASP B O     1 
ATOM   9326  C  CB    . ASP B 1 482 ? 146.789 153.929 153.581 1.00 166.24 ? 482  ASP B CB    1 
ATOM   9327  C  CG    . ASP B 1 482 ? 145.806 152.864 153.982 1.00 168.94 ? 482  ASP B CG    1 
ATOM   9328  O  OD1   . ASP B 1 482 ? 145.440 152.032 153.118 1.00 167.61 ? 482  ASP B OD1   1 
ATOM   9329  O  OD2   . ASP B 1 482 ? 145.403 152.839 155.164 1.00 169.31 ? 482  ASP B OD2   1 
ATOM   9330  N  N     . VAL B 1 483 ? 149.602 155.021 152.611 1.00 158.15 ? 483  VAL B N     1 
ATOM   9331  C  CA    . VAL B 1 483 ? 150.417 156.147 152.168 1.00 156.46 ? 483  VAL B CA    1 
ATOM   9332  C  C     . VAL B 1 483 ? 151.216 155.779 150.924 1.00 157.18 ? 483  VAL B C     1 
ATOM   9333  O  O     . VAL B 1 483 ? 151.321 156.571 149.979 1.00 156.70 ? 483  VAL B O     1 
ATOM   9334  C  CB    . VAL B 1 483 ? 151.330 156.610 153.315 1.00 155.78 ? 483  VAL B CB    1 
ATOM   9335  C  CG1   . VAL B 1 483 ? 152.512 157.391 152.769 1.00 153.84 ? 483  VAL B CG1   1 
ATOM   9336  C  CG2   . VAL B 1 483 ? 150.536 157.429 154.318 1.00 154.34 ? 483  VAL B CG2   1 
ATOM   9337  N  N     . LEU B 1 484 ? 151.809 154.583 150.912 1.00 156.76 ? 484  LEU B N     1 
ATOM   9338  C  CA    . LEU B 1 484 ? 152.655 154.177 149.794 1.00 154.26 ? 484  LEU B CA    1 
ATOM   9339  C  C     . LEU B 1 484 ? 151.846 154.013 148.514 1.00 158.06 ? 484  LEU B C     1 
ATOM   9340  O  O     . LEU B 1 484 ? 152.226 154.530 147.458 1.00 158.67 ? 484  LEU B O     1 
ATOM   9341  C  CB    . LEU B 1 484 ? 153.384 152.878 150.133 1.00 150.94 ? 484  LEU B CB    1 
ATOM   9342  C  CG    . LEU B 1 484 ? 154.303 152.916 151.350 1.00 148.05 ? 484  LEU B CG    1 
ATOM   9343  C  CD1   . LEU B 1 484 ? 154.913 151.546 151.622 1.00 143.89 ? 484  LEU B CD1   1 
ATOM   9344  C  CD2   . LEU B 1 484 ? 155.373 153.973 151.150 1.00 145.93 ? 484  LEU B CD2   1 
ATOM   9345  N  N     . GLY B 1 485 ? 150.729 153.296 148.590 1.00 157.28 ? 485  GLY B N     1 
ATOM   9346  C  CA    . GLY B 1 485 ? 149.922 153.010 147.429 1.00 155.35 ? 485  GLY B CA    1 
ATOM   9347  C  C     . GLY B 1 485 ? 150.025 151.560 146.999 1.00 157.87 ? 485  GLY B C     1 
ATOM   9348  O  O     . GLY B 1 485 ? 150.676 150.740 147.654 1.00 160.73 ? 485  GLY B O     1 
ATOM   9349  N  N     . PRO B 1 486 ? 149.384 151.215 145.876 1.00 156.42 ? 486  PRO B N     1 
ATOM   9350  C  CA    . PRO B 1 486 ? 149.437 149.829 145.387 1.00 157.26 ? 486  PRO B CA    1 
ATOM   9351  C  C     . PRO B 1 486 ? 150.702 149.537 144.601 1.00 153.16 ? 486  PRO B C     1 
ATOM   9352  O  O     . PRO B 1 486 ? 151.196 148.404 144.559 1.00 151.02 ? 486  PRO B O     1 
ATOM   9353  C  CB    . PRO B 1 486 ? 148.195 149.728 144.496 1.00 151.80 ? 486  PRO B CB    1 
ATOM   9354  C  CG    . PRO B 1 486 ? 147.879 151.151 144.089 1.00 150.55 ? 486  PRO B CG    1 
ATOM   9355  C  CD    . PRO B 1 486 ? 148.679 152.105 144.939 1.00 151.14 ? 486  PRO B CD    1 
ATOM   9356  N  N     . PHE B 1 487 ? 151.218 150.585 143.967 1.00 151.07 ? 487  PHE B N     1 
ATOM   9357  C  CA    . PHE B 1 487 ? 152.441 150.483 143.183 1.00 150.41 ? 487  PHE B CA    1 
ATOM   9358  C  C     . PHE B 1 487 ? 153.606 150.030 144.062 1.00 152.62 ? 487  PHE B C     1 
ATOM   9359  O  O     . PHE B 1 487 ? 154.280 149.034 143.764 1.00 152.24 ? 487  PHE B O     1 
ATOM   9360  C  CB    . PHE B 1 487 ? 152.668 151.852 142.535 1.00 149.58 ? 487  PHE B CB    1 
ATOM   9361  C  CG    . PHE B 1 487 ? 153.862 151.953 141.639 1.00 150.47 ? 487  PHE B CG    1 
ATOM   9362  C  CD1   . PHE B 1 487 ? 155.125 152.144 142.153 1.00 152.51 ? 487  PHE B CD1   1 
ATOM   9363  C  CD2   . PHE B 1 487 ? 153.698 151.996 140.265 1.00 150.86 ? 487  PHE B CD2   1 
ATOM   9364  C  CE1   . PHE B 1 487 ? 156.201 152.314 141.311 1.00 153.56 ? 487  PHE B CE1   1 
ATOM   9365  C  CE2   . PHE B 1 487 ? 154.787 152.133 139.419 1.00 150.60 ? 487  PHE B CE2   1 
ATOM   9366  C  CZ    . PHE B 1 487 ? 156.038 152.282 139.947 1.00 150.59 ? 487  PHE B CZ    1 
ATOM   9367  N  N     . ILE B 1 488 ? 153.787 150.691 145.208 1.00 152.82 ? 488  ILE B N     1 
ATOM   9368  C  CA    . ILE B 1 488 ? 154.850 150.323 146.138 1.00 147.54 ? 488  ILE B CA    1 
ATOM   9369  C  C     . ILE B 1 488 ? 154.603 148.943 146.739 1.00 147.31 ? 488  ILE B C     1 
ATOM   9370  O  O     . ILE B 1 488 ? 155.545 148.171 146.953 1.00 149.31 ? 488  ILE B O     1 
ATOM   9371  C  CB    . ILE B 1 488 ? 154.978 151.398 147.230 1.00 150.60 ? 488  ILE B CB    1 
ATOM   9372  C  CG1   . ILE B 1 488 ? 154.936 152.796 146.615 1.00 156.75 ? 488  ILE B CG1   1 
ATOM   9373  C  CG2   . ILE B 1 488 ? 156.257 151.214 148.014 1.00 147.23 ? 488  ILE B CG2   1 
ATOM   9374  C  CD1   . ILE B 1 488 ? 156.103 153.105 145.712 1.00 154.29 ? 488  ILE B CD1   1 
ATOM   9375  N  N     . GLY B 1 489 ? 153.348 148.617 147.052 1.00 146.58 ? 489  GLY B N     1 
ATOM   9376  C  CA    . GLY B 1 489 ? 153.069 147.324 147.662 1.00 148.57 ? 489  GLY B CA    1 
ATOM   9377  C  C     . GLY B 1 489 ? 153.359 146.157 146.736 1.00 150.80 ? 489  GLY B C     1 
ATOM   9378  O  O     . GLY B 1 489 ? 154.026 145.189 147.123 1.00 150.51 ? 489  GLY B O     1 
ATOM   9379  N  N     . ASN B 1 490 ? 152.865 146.231 145.498 1.00 149.31 ? 490  ASN B N     1 
ATOM   9380  C  CA    . ASN B 1 490 ? 153.198 145.215 144.508 1.00 145.48 ? 490  ASN B CA    1 
ATOM   9381  C  C     . ASN B 1 490 ? 154.698 145.177 144.266 1.00 142.64 ? 490  ASN B C     1 
ATOM   9382  O  O     . ASN B 1 490 ? 155.268 144.114 143.990 1.00 142.32 ? 490  ASN B O     1 
ATOM   9383  C  CB    . ASN B 1 490 ? 152.452 145.493 143.204 1.00 146.00 ? 490  ASN B CB    1 
ATOM   9384  C  CG    . ASN B 1 490 ? 150.971 145.207 143.310 1.00 151.63 ? 490  ASN B CG    1 
ATOM   9385  O  OD1   . ASN B 1 490 ? 150.135 146.082 143.071 1.00 151.51 ? 490  ASN B OD1   1 
ATOM   9386  N  ND2   . ASN B 1 490 ? 150.635 143.981 143.679 1.00 153.34 ? 490  ASN B ND2   1 
ATOM   9387  N  N     . MET B 1 491 ? 155.355 146.331 144.381 1.00 145.18 ? 491  MET B N     1 
ATOM   9388  C  CA    . MET B 1 491 ? 156.803 146.385 144.249 1.00 145.57 ? 491  MET B CA    1 
ATOM   9389  C  C     . MET B 1 491 ? 157.493 145.596 145.354 1.00 147.53 ? 491  MET B C     1 
ATOM   9390  O  O     . MET B 1 491 ? 158.491 144.911 145.111 1.00 143.05 ? 491  MET B O     1 
ATOM   9391  C  CB    . MET B 1 491 ? 157.227 147.845 144.276 1.00 144.69 ? 491  MET B CB    1 
ATOM   9392  C  CG    . MET B 1 491 ? 158.602 148.139 143.816 1.00 140.07 ? 491  MET B CG    1 
ATOM   9393  S  SD    . MET B 1 491 ? 158.505 149.866 143.354 1.00 159.87 ? 491  MET B SD    1 
ATOM   9394  C  CE    . MET B 1 491 ? 158.016 149.684 141.646 1.00 143.65 ? 491  MET B CE    1 
ATOM   9395  N  N     . TYR B 1 492 ? 156.975 145.692 146.575 1.00 150.48 ? 492  TYR B N     1 
ATOM   9396  C  CA    . TYR B 1 492 ? 157.548 145.029 147.738 1.00 149.95 ? 492  TYR B CA    1 
ATOM   9397  C  C     . TYR B 1 492 ? 156.997 143.630 147.976 1.00 150.27 ? 492  TYR B C     1 
ATOM   9398  O  O     . TYR B 1 492 ? 157.338 143.020 148.997 1.00 150.06 ? 492  TYR B O     1 
ATOM   9399  C  CB    . TYR B 1 492 ? 157.339 145.884 148.984 1.00 146.79 ? 492  TYR B CB    1 
ATOM   9400  C  CG    . TYR B 1 492 ? 158.337 147.004 149.120 1.00 146.50 ? 492  TYR B CG    1 
ATOM   9401  C  CD1   . TYR B 1 492 ? 159.579 146.766 149.673 1.00 141.84 ? 492  TYR B CD1   1 
ATOM   9402  C  CD2   . TYR B 1 492 ? 158.044 148.291 148.694 1.00 148.15 ? 492  TYR B CD2   1 
ATOM   9403  C  CE1   . TYR B 1 492 ? 160.504 147.768 149.805 1.00 140.12 ? 492  TYR B CE1   1 
ATOM   9404  C  CE2   . TYR B 1 492 ? 158.969 149.309 148.823 1.00 146.74 ? 492  TYR B CE2   1 
ATOM   9405  C  CZ    . TYR B 1 492 ? 160.197 149.042 149.379 1.00 141.96 ? 492  TYR B CZ    1 
ATOM   9406  O  OH    . TYR B 1 492 ? 161.124 150.052 149.510 1.00 141.64 ? 492  TYR B OH    1 
ATOM   9407  N  N     . LEU B 1 493 ? 156.144 143.115 147.084 1.00 148.55 ? 493  LEU B N     1 
ATOM   9408  C  CA    . LEU B 1 493 ? 155.794 141.698 147.151 1.00 148.57 ? 493  LEU B CA    1 
ATOM   9409  C  C     . LEU B 1 493 ? 157.029 140.807 147.156 1.00 148.30 ? 493  LEU B C     1 
ATOM   9410  O  O     . LEU B 1 493 ? 157.139 139.900 147.988 1.00 145.33 ? 493  LEU B O     1 
ATOM   9411  C  CB    . LEU B 1 493 ? 154.888 141.314 145.983 1.00 150.08 ? 493  LEU B CB    1 
ATOM   9412  C  CG    . LEU B 1 493 ? 153.408 141.215 146.326 1.00 151.35 ? 493  LEU B CG    1 
ATOM   9413  C  CD1   . LEU B 1 493 ? 152.599 140.724 145.139 1.00 149.37 ? 493  LEU B CD1   1 
ATOM   9414  C  CD2   . LEU B 1 493 ? 153.231 140.288 147.518 1.00 147.38 ? 493  LEU B CD2   1 
ATOM   9415  N  N     . ALA B 1 494 ? 157.962 141.041 146.234 1.00 144.57 ? 494  ALA B N     1 
ATOM   9416  C  CA    . ALA B 1 494 ? 159.267 140.378 146.224 1.00 140.49 ? 494  ALA B CA    1 
ATOM   9417  C  C     . ALA B 1 494 ? 160.298 141.498 146.293 1.00 137.64 ? 494  ALA B C     1 
ATOM   9418  O  O     . ALA B 1 494 ? 160.723 142.030 145.265 1.00 133.14 ? 494  ALA B O     1 
ATOM   9419  C  CB    . ALA B 1 494 ? 159.451 139.500 144.995 1.00 132.98 ? 494  ALA B CB    1 
ATOM   9420  N  N     . GLU B 1 495 ? 160.685 141.860 147.513 1.00 130.24 ? 495  GLU B N     1 
ATOM   9421  C  CA    . GLU B 1 495 ? 161.506 143.034 147.759 1.00 124.75 ? 495  GLU B CA    1 
ATOM   9422  C  C     . GLU B 1 495 ? 162.993 142.720 147.868 1.00 124.59 ? 495  GLU B C     1 
ATOM   9423  O  O     . GLU B 1 495 ? 163.782 143.620 148.168 1.00 127.08 ? 495  GLU B O     1 
ATOM   9424  C  CB    . GLU B 1 495 ? 161.029 143.744 149.024 1.00 124.85 ? 495  GLU B CB    1 
ATOM   9425  N  N     . ASP B 1 496 ? 163.397 141.469 147.640 1.00 123.82 ? 496  ASP B N     1 
ATOM   9426  C  CA    . ASP B 1 496 ? 164.824 141.167 147.628 1.00 122.98 ? 496  ASP B CA    1 
ATOM   9427  C  C     . ASP B 1 496 ? 165.513 141.873 146.467 1.00 120.10 ? 496  ASP B C     1 
ATOM   9428  O  O     . ASP B 1 496 ? 166.669 142.297 146.584 1.00 121.91 ? 496  ASP B O     1 
ATOM   9429  C  CB    . ASP B 1 496 ? 165.044 139.657 147.566 1.00 125.11 ? 496  ASP B CB    1 
ATOM   9430  C  CG    . ASP B 1 496 ? 166.361 139.237 148.192 1.00 132.57 ? 496  ASP B CG    1 
ATOM   9431  O  OD1   . ASP B 1 496 ? 167.021 140.090 148.819 1.00 127.59 ? 496  ASP B OD1   1 
ATOM   9432  O  OD2   . ASP B 1 496 ? 166.729 138.049 148.071 1.00 137.70 ? 496  ASP B OD2   1 
ATOM   9433  N  N     . ARG B 1 497 ? 164.807 142.033 145.345 1.00 119.38 ? 497  ARG B N     1 
ATOM   9434  C  CA    . ARG B 1 497 ? 165.324 142.851 144.255 1.00 123.50 ? 497  ARG B CA    1 
ATOM   9435  C  C     . ARG B 1 497 ? 165.462 144.308 144.675 1.00 122.40 ? 497  ARG B C     1 
ATOM   9436  O  O     . ARG B 1 497 ? 166.407 144.989 144.262 1.00 123.81 ? 497  ARG B O     1 
ATOM   9437  C  CB    . ARG B 1 497 ? 164.407 142.740 143.040 1.00 125.67 ? 497  ARG B CB    1 
ATOM   9438  C  CG    . ARG B 1 497 ? 164.149 141.321 142.577 1.00 127.81 ? 497  ARG B CG    1 
ATOM   9439  C  CD    . ARG B 1 497 ? 163.631 141.298 141.151 1.00 132.18 ? 497  ARG B CD    1 
ATOM   9440  N  NE    . ARG B 1 497 ? 163.599 139.948 140.604 1.00 138.66 ? 497  ARG B NE    1 
ATOM   9441  C  CZ    . ARG B 1 497 ? 163.468 139.666 139.315 1.00 144.26 ? 497  ARG B CZ    1 
ATOM   9442  N  NH1   . ARG B 1 497 ? 163.349 140.621 138.408 1.00 143.35 ? 497  ARG B NH1   1 
ATOM   9443  N  NH2   . ARG B 1 497 ? 163.456 138.394 138.927 1.00 149.71 ? 497  ARG B NH2   1 
ATOM   9444  N  N     . ILE B 1 498 ? 164.527 144.804 145.488 1.00 115.73 ? 498  ILE B N     1 
ATOM   9445  C  CA    . ILE B 1 498 ? 164.616 146.172 145.991 1.00 115.46 ? 498  ILE B CA    1 
ATOM   9446  C  C     . ILE B 1 498 ? 165.840 146.327 146.886 1.00 116.81 ? 498  ILE B C     1 
ATOM   9447  O  O     . ILE B 1 498 ? 166.562 147.328 146.815 1.00 118.58 ? 498  ILE B O     1 
ATOM   9448  C  CB    . ILE B 1 498 ? 163.319 146.553 146.725 1.00 119.49 ? 498  ILE B CB    1 
ATOM   9449  C  CG1   . ILE B 1 498 ? 162.307 147.126 145.736 1.00 125.39 ? 498  ILE B CG1   1 
ATOM   9450  C  CG2   . ILE B 1 498 ? 163.594 147.546 147.836 1.00 120.91 ? 498  ILE B CG2   1 
ATOM   9451  C  CD1   . ILE B 1 498 ? 161.033 147.599 146.379 1.00 132.11 ? 498  ILE B CD1   1 
ATOM   9452  N  N     . LEU B 1 499 ? 166.091 145.334 147.741 1.00 113.47 ? 499  LEU B N     1 
ATOM   9453  C  CA    . LEU B 1 499 ? 167.289 145.364 148.572 1.00 108.44 ? 499  LEU B CA    1 
ATOM   9454  C  C     . LEU B 1 499 ? 168.551 145.329 147.720 1.00 112.72 ? 499  LEU B C     1 
ATOM   9455  O  O     . LEU B 1 499 ? 169.525 146.033 148.009 1.00 115.07 ? 499  LEU B O     1 
ATOM   9456  C  CB    . LEU B 1 499 ? 167.271 144.197 149.556 1.00 107.67 ? 499  LEU B CB    1 
ATOM   9457  C  CG    . LEU B 1 499 ? 168.370 144.172 150.615 1.00 108.16 ? 499  LEU B CG    1 
ATOM   9458  C  CD1   . LEU B 1 499 ? 168.373 145.460 151.407 1.00 113.59 ? 499  LEU B CD1   1 
ATOM   9459  C  CD2   . LEU B 1 499 ? 168.166 142.981 151.531 1.00 110.48 ? 499  LEU B CD2   1 
ATOM   9460  N  N     . SER B 1 500 ? 168.549 144.516 146.662 1.00 114.54 ? 500  SER B N     1 
ATOM   9461  C  CA    . SER B 1 500 ? 169.692 144.466 145.756 1.00 109.52 ? 500  SER B CA    1 
ATOM   9462  C  C     . SER B 1 500 ? 169.946 145.824 145.114 1.00 108.07 ? 500  SER B C     1 
ATOM   9463  O  O     . SER B 1 500 ? 171.086 146.306 145.072 1.00 111.16 ? 500  SER B O     1 
ATOM   9464  C  CB    . SER B 1 500 ? 169.454 143.404 144.686 1.00 110.50 ? 500  SER B CB    1 
ATOM   9465  O  OG    . SER B 1 500 ? 169.222 142.138 145.276 1.00 120.13 ? 500  SER B OG    1 
ATOM   9466  N  N     . PHE B 1 501 ? 168.887 146.463 144.614 1.00 107.35 ? 501  PHE B N     1 
ATOM   9467  C  CA    . PHE B 1 501 ? 169.054 147.770 143.988 1.00 108.76 ? 501  PHE B CA    1 
ATOM   9468  C  C     . PHE B 1 501 ? 169.538 148.809 144.988 1.00 110.52 ? 501  PHE B C     1 
ATOM   9469  O  O     . PHE B 1 501 ? 170.380 149.649 144.658 1.00 113.43 ? 501  PHE B O     1 
ATOM   9470  C  CB    . PHE B 1 501 ? 167.753 148.239 143.346 1.00 109.65 ? 501  PHE B CB    1 
ATOM   9471  C  CG    . PHE B 1 501 ? 167.903 149.517 142.579 1.00 110.39 ? 501  PHE B CG    1 
ATOM   9472  C  CD1   . PHE B 1 501 ? 168.637 149.556 141.410 1.00 109.45 ? 501  PHE B CD1   1 
ATOM   9473  C  CD2   . PHE B 1 501 ? 167.329 150.684 143.041 1.00 111.84 ? 501  PHE B CD2   1 
ATOM   9474  C  CE1   . PHE B 1 501 ? 168.784 150.734 140.712 1.00 110.66 ? 501  PHE B CE1   1 
ATOM   9475  C  CE2   . PHE B 1 501 ? 167.472 151.863 142.348 1.00 110.71 ? 501  PHE B CE2   1 
ATOM   9476  C  CZ    . PHE B 1 501 ? 168.200 151.889 141.182 1.00 112.59 ? 501  PHE B CZ    1 
ATOM   9477  N  N     . GLU B 1 502 ? 169.009 148.782 146.212 1.00 108.30 ? 502  GLU B N     1 
ATOM   9478  C  CA    . GLU B 1 502 ? 169.433 149.759 147.207 1.00 108.70 ? 502  GLU B CA    1 
ATOM   9479  C  C     . GLU B 1 502 ? 170.885 149.539 147.606 1.00 109.45 ? 502  GLU B C     1 
ATOM   9480  O  O     . GLU B 1 502 ? 171.607 150.498 147.902 1.00 111.24 ? 502  GLU B O     1 
ATOM   9481  C  CB    . GLU B 1 502 ? 168.521 149.696 148.429 1.00 112.61 ? 502  GLU B CB    1 
ATOM   9482  C  CG    . GLU B 1 502 ? 167.111 150.190 148.171 1.00 116.43 ? 502  GLU B CG    1 
ATOM   9483  C  CD    . GLU B 1 502 ? 167.057 151.673 147.879 1.00 121.02 ? 502  GLU B CD    1 
ATOM   9484  O  OE1   . GLU B 1 502 ? 167.975 152.402 148.308 1.00 120.11 ? 502  GLU B OE1   1 
ATOM   9485  O  OE2   . GLU B 1 502 ? 166.093 152.115 147.221 1.00 125.38 ? 502  GLU B OE2   1 
ATOM   9486  N  N     . VAL B 1 503 ? 171.331 148.282 147.627 1.00 107.77 ? 503  VAL B N     1 
ATOM   9487  C  CA    . VAL B 1 503 ? 172.742 147.999 147.870 1.00 102.89 ? 503  VAL B CA    1 
ATOM   9488  C  C     . VAL B 1 503 ? 173.593 148.563 146.740 1.00 106.66 ? 503  VAL B C     1 
ATOM   9489  O  O     . VAL B 1 503 ? 174.660 149.143 146.970 1.00 110.81 ? 503  VAL B O     1 
ATOM   9490  C  CB    . VAL B 1 503 ? 172.963 146.487 148.044 1.00 102.27 ? 503  VAL B CB    1 
ATOM   9491  C  CG1   . VAL B 1 503 ? 174.429 146.140 147.881 1.00 100.47 ? 503  VAL B CG1   1 
ATOM   9492  C  CG2   . VAL B 1 503 ? 172.462 146.037 149.397 1.00 107.52 ? 503  VAL B CG2   1 
ATOM   9493  N  N     . VAL B 1 504 ? 173.128 148.403 145.499 1.00 108.58 ? 504  VAL B N     1 
ATOM   9494  C  CA    . VAL B 1 504 ? 173.901 148.881 144.354 1.00 107.26 ? 504  VAL B CA    1 
ATOM   9495  C  C     . VAL B 1 504 ? 173.984 150.403 144.346 1.00 110.21 ? 504  VAL B C     1 
ATOM   9496  O  O     . VAL B 1 504 ? 175.046 150.978 144.082 1.00 114.99 ? 504  VAL B O     1 
ATOM   9497  C  CB    . VAL B 1 504 ? 173.307 148.342 143.042 1.00 101.65 ? 504  VAL B CB    1 
ATOM   9498  C  CG1   . VAL B 1 504 ? 173.996 148.979 141.854 1.00 99.99  ? 504  VAL B CG1   1 
ATOM   9499  C  CG2   . VAL B 1 504 ? 173.462 146.842 142.982 1.00 105.76 ? 504  VAL B CG2   1 
ATOM   9500  N  N     . ALA B 1 505 ? 172.875 151.081 144.637 1.00 108.66 ? 505  ALA B N     1 
ATOM   9501  C  CA    . ALA B 1 505 ? 172.788 152.532 144.529 1.00 108.56 ? 505  ALA B CA    1 
ATOM   9502  C  C     . ALA B 1 505 ? 172.791 153.224 145.887 1.00 113.12 ? 505  ALA B C     1 
ATOM   9503  O  O     . ALA B 1 505 ? 172.118 154.244 146.063 1.00 116.93 ? 505  ALA B O     1 
ATOM   9504  C  CB    . ALA B 1 505 ? 171.542 152.927 143.740 1.00 108.47 ? 505  ALA B CB    1 
ATOM   9505  N  N     . ARG B 1 506 ? 173.532 152.691 146.854 1.00 113.07 ? 506  ARG B N     1 
ATOM   9506  C  CA    . ARG B 1 506 ? 173.630 153.341 148.152 1.00 115.78 ? 506  ARG B CA    1 
ATOM   9507  C  C     . ARG B 1 506 ? 174.457 154.614 148.038 1.00 123.78 ? 506  ARG B C     1 
ATOM   9508  O  O     . ARG B 1 506 ? 175.479 154.649 147.349 1.00 127.90 ? 506  ARG B O     1 
ATOM   9509  C  CB    . ARG B 1 506 ? 174.254 152.395 149.177 1.00 118.25 ? 506  ARG B CB    1 
ATOM   9510  C  CG    . ARG B 1 506 ? 173.910 152.739 150.613 1.00 117.30 ? 506  ARG B CG    1 
ATOM   9511  C  CD    . ARG B 1 506 ? 174.725 151.920 151.592 1.00 109.52 ? 506  ARG B CD    1 
ATOM   9512  N  NE    . ARG B 1 506 ? 174.253 152.095 152.959 1.00 114.39 ? 506  ARG B NE    1 
ATOM   9513  C  CZ    . ARG B 1 506 ? 174.936 151.738 154.037 1.00 123.64 ? 506  ARG B CZ    1 
ATOM   9514  N  NH1   . ARG B 1 506 ? 176.132 151.183 153.944 1.00 128.25 ? 506  ARG B NH1   1 
ATOM   9515  N  NH2   . ARG B 1 506 ? 174.406 151.944 155.239 1.00 125.24 ? 506  ARG B NH2   1 
ATOM   9516  N  N     . LYS B 1 507 ? 174.009 155.666 148.718 1.00 121.95 ? 507  LYS B N     1 
ATOM   9517  C  CA    . LYS B 1 507 ? 174.668 156.960 148.608 1.00 122.96 ? 507  LYS B CA    1 
ATOM   9518  C  C     . LYS B 1 507 ? 176.063 156.918 149.218 1.00 125.50 ? 507  LYS B C     1 
ATOM   9519  O  O     . LYS B 1 507 ? 176.282 156.313 150.271 1.00 126.83 ? 507  LYS B O     1 
ATOM   9520  C  CB    . LYS B 1 507 ? 173.830 158.042 149.289 1.00 125.28 ? 507  LYS B CB    1 
ATOM   9521  C  CG    . LYS B 1 507 ? 174.504 159.404 149.338 1.00 129.69 ? 507  LYS B CG    1 
ATOM   9522  C  CD    . LYS B 1 507 ? 173.490 160.531 149.440 1.00 132.37 ? 507  LYS B CD    1 
ATOM   9523  C  CE    . LYS B 1 507 ? 172.515 160.298 150.579 1.00 137.33 ? 507  LYS B CE    1 
ATOM   9524  N  NZ    . LYS B 1 507 ? 171.436 161.321 150.594 1.00 133.25 ? 507  LYS B NZ    1 
ATOM   9525  N  N     . ASN B 1 508 ? 177.014 157.555 148.532 1.00 127.40 ? 508  ASN B N     1 
ATOM   9526  C  CA    . ASN B 1 508 ? 178.390 157.725 148.995 1.00 131.04 ? 508  ASN B CA    1 
ATOM   9527  C  C     . ASN B 1 508 ? 179.137 156.402 149.131 1.00 131.84 ? 508  ASN B C     1 
ATOM   9528  O  O     . ASN B 1 508 ? 180.216 156.357 149.730 1.00 133.91 ? 508  ASN B O     1 
ATOM   9529  C  CB    . ASN B 1 508 ? 178.443 158.498 150.317 1.00 132.11 ? 508  ASN B CB    1 
ATOM   9530  C  CG    . ASN B 1 508 ? 177.892 159.902 150.191 1.00 133.26 ? 508  ASN B CG    1 
ATOM   9531  O  OD1   . ASN B 1 508 ? 177.855 160.469 149.100 1.00 133.54 ? 508  ASN B OD1   1 
ATOM   9532  N  ND2   . ASN B 1 508 ? 177.463 160.472 151.310 1.00 136.91 ? 508  ASN B ND2   1 
ATOM   9533  N  N     . CYS B 1 509 ? 178.591 155.319 148.585 1.00 124.29 ? 509  CYS B N     1 
ATOM   9534  C  CA    . CYS B 1 509 ? 179.253 154.024 148.616 1.00 121.03 ? 509  CYS B CA    1 
ATOM   9535  C  C     . CYS B 1 509 ? 179.032 153.314 147.290 1.00 119.04 ? 509  CYS B C     1 
ATOM   9536  O  O     . CYS B 1 509 ? 177.957 153.403 146.693 1.00 120.01 ? 509  CYS B O     1 
ATOM   9537  C  CB    . CYS B 1 509 ? 178.742 153.157 149.772 1.00 123.58 ? 509  CYS B CB    1 
ATOM   9538  S  SG    . CYS B 1 509 ? 179.813 153.152 151.229 1.00 141.61 ? 509  CYS B SG    1 
ATOM   9539  N  N     . ASN B 1 510 ? 180.061 152.604 146.834 1.00 118.52 ? 510  ASN B N     1 
ATOM   9540  C  CA    . ASN B 1 510 ? 180.010 151.857 145.580 1.00 115.37 ? 510  ASN B CA    1 
ATOM   9541  C  C     . ASN B 1 510 ? 180.020 150.366 145.903 1.00 115.89 ? 510  ASN B C     1 
ATOM   9542  O  O     . ASN B 1 510 ? 181.071 149.723 145.926 1.00 119.94 ? 510  ASN B O     1 
ATOM   9543  C  CB    . ASN B 1 510 ? 181.172 152.247 144.657 1.00 116.73 ? 510  ASN B CB    1 
ATOM   9544  C  CG    . ASN B 1 510 ? 182.525 152.115 145.325 1.00 120.33 ? 510  ASN B CG    1 
ATOM   9545  O  OD1   . ASN B 1 510 ? 182.616 151.935 146.538 1.00 122.41 ? 510  ASN B OD1   1 
ATOM   9546  N  ND2   . ASN B 1 510 ? 183.586 152.200 144.533 1.00 121.94 ? 510  ASN B ND2   1 
ATOM   9547  N  N     . TRP B 1 511 ? 178.838 149.811 146.144 1.00 111.22 ? 511  TRP B N     1 
ATOM   9548  C  CA    . TRP B 1 511 ? 178.676 148.379 146.342 1.00 105.56 ? 511  TRP B CA    1 
ATOM   9549  C  C     . TRP B 1 511 ? 178.085 147.765 145.085 1.00 108.44 ? 511  TRP B C     1 
ATOM   9550  O  O     . TRP B 1 511 ? 176.955 148.088 144.706 1.00 111.26 ? 511  TRP B O     1 
ATOM   9551  C  CB    . TRP B 1 511 ? 177.779 148.072 147.541 1.00 100.06 ? 511  TRP B CB    1 
ATOM   9552  C  CG    . TRP B 1 511 ? 178.261 148.645 148.823 1.00 104.31 ? 511  TRP B CG    1 
ATOM   9553  C  CD1   . TRP B 1 511 ? 177.817 149.777 149.431 1.00 114.41 ? 511  TRP B CD1   1 
ATOM   9554  C  CD2   . TRP B 1 511 ? 179.304 148.125 149.653 1.00 103.38 ? 511  TRP B CD2   1 
ATOM   9555  N  NE1   . TRP B 1 511 ? 178.506 149.988 150.599 1.00 116.63 ? 511  TRP B NE1   1 
ATOM   9556  C  CE2   . TRP B 1 511 ? 179.428 148.987 150.756 1.00 108.40 ? 511  TRP B CE2   1 
ATOM   9557  C  CE3   . TRP B 1 511 ? 180.139 147.009 149.575 1.00 105.23 ? 511  TRP B CE3   1 
ATOM   9558  C  CZ2   . TRP B 1 511 ? 180.353 148.772 151.769 1.00 109.83 ? 511  TRP B CZ2   1 
ATOM   9559  C  CZ3   . TRP B 1 511 ? 181.057 146.798 150.581 1.00 105.80 ? 511  TRP B CZ3   1 
ATOM   9560  C  CH2   . TRP B 1 511 ? 181.157 147.673 151.664 1.00 107.76 ? 511  TRP B CH2   1 
ATOM   9561  N  N     . THR B 1 512 ? 178.843 146.888 144.444 1.00 105.30 ? 512  THR B N     1 
ATOM   9562  C  CA    . THR B 1 512 ? 178.334 146.097 143.339 1.00 103.63 ? 512  THR B CA    1 
ATOM   9563  C  C     . THR B 1 512 ? 177.855 144.758 143.874 1.00 104.35 ? 512  THR B C     1 
ATOM   9564  O  O     . THR B 1 512 ? 178.023 144.434 145.051 1.00 106.26 ? 512  THR B O     1 
ATOM   9565  C  CB    . THR B 1 512 ? 179.395 145.890 142.254 1.00 109.24 ? 512  THR B CB    1 
ATOM   9566  O  OG1   . THR B 1 512 ? 180.167 144.721 142.554 1.00 115.98 ? 512  THR B OG1   1 
ATOM   9567  C  CG2   . THR B 1 512 ? 180.308 147.091 142.174 1.00 112.34 ? 512  THR B CG2   1 
ATOM   9568  N  N     . MET B 1 513 ? 177.253 143.977 142.991 1.00 101.92 ? 513  MET B N     1 
ATOM   9569  C  CA    . MET B 1 513 ? 176.725 142.671 143.337 1.00 97.64  ? 513  MET B CA    1 
ATOM   9570  C  C     . MET B 1 513 ? 177.483 141.599 142.567 1.00 98.85  ? 513  MET B C     1 
ATOM   9571  O  O     . MET B 1 513 ? 178.299 141.890 141.690 1.00 104.54 ? 513  MET B O     1 
ATOM   9572  C  CB    . MET B 1 513 ? 175.228 142.608 143.038 1.00 93.02  ? 513  MET B CB    1 
ATOM   9573  C  CG    . MET B 1 513 ? 174.391 143.479 143.948 1.00 101.50 ? 513  MET B CG    1 
ATOM   9574  S  SD    . MET B 1 513 ? 172.796 142.746 144.326 1.00 125.09 ? 513  MET B SD    1 
ATOM   9575  C  CE    . MET B 1 513 ? 173.196 141.755 145.757 1.00 111.37 ? 513  MET B CE    1 
ATOM   9576  N  N     . HIS B 1 514 ? 177.216 140.344 142.910 1.00 91.99  ? 514  HIS B N     1 
ATOM   9577  C  CA    . HIS B 1 514 ? 177.956 139.254 142.302 1.00 96.61  ? 514  HIS B CA    1 
ATOM   9578  C  C     . HIS B 1 514 ? 177.086 138.010 142.289 1.00 103.01 ? 514  HIS B C     1 
ATOM   9579  O  O     . HIS B 1 514 ? 176.148 137.874 143.077 1.00 109.65 ? 514  HIS B O     1 
ATOM   9580  C  CB    . HIS B 1 514 ? 179.268 138.999 143.050 1.00 94.83  ? 514  HIS B CB    1 
ATOM   9581  C  CG    . HIS B 1 514 ? 180.185 138.039 142.362 1.00 101.72 ? 514  HIS B CG    1 
ATOM   9582  N  ND1   . HIS B 1 514 ? 180.400 138.061 141.002 1.00 107.68 ? 514  HIS B ND1   1 
ATOM   9583  C  CD2   . HIS B 1 514 ? 180.961 137.043 142.849 1.00 104.13 ? 514  HIS B CD2   1 
ATOM   9584  C  CE1   . HIS B 1 514 ? 181.260 137.113 140.678 1.00 110.54 ? 514  HIS B CE1   1 
ATOM   9585  N  NE2   . HIS B 1 514 ? 181.616 136.480 141.781 1.00 109.39 ? 514  HIS B NE2   1 
ATOM   9586  N  N     . TYR B 1 515 ? 177.405 137.103 141.373 1.00 100.25 ? 515  TYR B N     1 
ATOM   9587  C  CA    . TYR B 1 515 ? 176.707 135.832 141.243 1.00 101.20 ? 515  TYR B CA    1 
ATOM   9588  C  C     . TYR B 1 515 ? 177.746 134.724 141.268 1.00 106.00 ? 515  TYR B C     1 
ATOM   9589  O  O     . TYR B 1 515 ? 178.641 134.691 140.416 1.00 110.77 ? 515  TYR B O     1 
ATOM   9590  C  CB    . TYR B 1 515 ? 175.890 135.789 139.952 1.00 99.92  ? 515  TYR B CB    1 
ATOM   9591  C  CG    . TYR B 1 515 ? 175.533 134.398 139.494 1.00 103.92 ? 515  TYR B CG    1 
ATOM   9592  C  CD1   . TYR B 1 515 ? 174.489 133.704 140.081 1.00 105.32 ? 515  TYR B CD1   1 
ATOM   9593  C  CD2   . TYR B 1 515 ? 176.236 133.782 138.472 1.00 106.40 ? 515  TYR B CD2   1 
ATOM   9594  C  CE1   . TYR B 1 515 ? 174.157 132.435 139.665 1.00 109.18 ? 515  TYR B CE1   1 
ATOM   9595  C  CE2   . TYR B 1 515 ? 175.911 132.513 138.050 1.00 108.85 ? 515  TYR B CE2   1 
ATOM   9596  C  CZ    . TYR B 1 515 ? 174.872 131.845 138.650 1.00 112.13 ? 515  TYR B CZ    1 
ATOM   9597  O  OH    . TYR B 1 515 ? 174.547 130.578 138.228 1.00 113.85 ? 515  TYR B OH    1 
ATOM   9598  N  N     . VAL B 1 516 ? 177.630 133.824 142.236 1.00 106.36 ? 516  VAL B N     1 
ATOM   9599  C  CA    . VAL B 1 516 ? 178.599 132.754 142.433 1.00 107.49 ? 516  VAL B CA    1 
ATOM   9600  C  C     . VAL B 1 516 ? 178.089 131.504 141.729 1.00 108.05 ? 516  VAL B C     1 
ATOM   9601  O  O     . VAL B 1 516 ? 177.038 130.959 142.087 1.00 106.75 ? 516  VAL B O     1 
ATOM   9602  C  CB    . VAL B 1 516 ? 178.855 132.499 143.925 1.00 107.17 ? 516  VAL B CB    1 
ATOM   9603  C  CG1   . VAL B 1 516 ? 179.771 133.568 144.481 1.00 101.37 ? 516  VAL B CG1   1 
ATOM   9604  C  CG2   . VAL B 1 516 ? 177.550 132.513 144.684 1.00 107.33 ? 516  VAL B CG2   1 
ATOM   9605  N  N     . LYS B 1 517 ? 178.829 131.059 140.716 1.00 111.84 ? 517  LYS B N     1 
ATOM   9606  C  CA    . LYS B 1 517 ? 178.417 129.898 139.939 1.00 112.74 ? 517  LYS B CA    1 
ATOM   9607  C  C     . LYS B 1 517 ? 178.518 128.607 140.737 1.00 113.18 ? 517  LYS B C     1 
ATOM   9608  O  O     . LYS B 1 517 ? 177.610 127.771 140.672 1.00 112.35 ? 517  LYS B O     1 
ATOM   9609  C  CB    . LYS B 1 517 ? 179.262 129.804 138.666 1.00 114.79 ? 517  LYS B CB    1 
ATOM   9610  C  CG    . LYS B 1 517 ? 179.120 128.501 137.899 1.00 116.63 ? 517  LYS B CG    1 
ATOM   9611  C  CD    . LYS B 1 517 ? 177.931 128.539 136.957 1.00 119.77 ? 517  LYS B CD    1 
ATOM   9612  C  CE    . LYS B 1 517 ? 177.798 127.231 136.194 1.00 121.68 ? 517  LYS B CE    1 
ATOM   9613  N  NZ    . LYS B 1 517 ? 178.256 126.069 137.004 1.00 119.73 ? 517  LYS B NZ    1 
ATOM   9614  N  N     . ASP B 1 518 ? 179.593 128.432 141.499 1.00 111.90 ? 518  ASP B N     1 
ATOM   9615  C  CA    . ASP B 1 518 ? 179.886 127.169 142.160 1.00 112.21 ? 518  ASP B CA    1 
ATOM   9616  C  C     . ASP B 1 518 ? 179.113 126.963 143.457 1.00 113.95 ? 518  ASP B C     1 
ATOM   9617  O  O     . ASP B 1 518 ? 179.074 125.837 143.960 1.00 116.68 ? 518  ASP B O     1 
ATOM   9618  C  CB    . ASP B 1 518 ? 181.389 127.065 142.438 1.00 113.59 ? 518  ASP B CB    1 
ATOM   9619  C  CG    . ASP B 1 518 ? 182.223 127.198 141.179 1.00 119.54 ? 518  ASP B CG    1 
ATOM   9620  O  OD1   . ASP B 1 518 ? 181.954 126.463 140.206 1.00 122.84 ? 518  ASP B OD1   1 
ATOM   9621  O  OD2   . ASP B 1 518 ? 183.146 128.039 141.160 1.00 120.05 ? 518  ASP B OD2   1 
ATOM   9622  N  N     . ALA B 1 519 ? 178.497 128.009 144.009 1.00 110.92 ? 519  ALA B N     1 
ATOM   9623  C  CA    . ALA B 1 519 ? 177.762 127.891 145.269 1.00 105.67 ? 519  ALA B CA    1 
ATOM   9624  C  C     . ALA B 1 519 ? 176.321 127.499 144.961 1.00 107.74 ? 519  ALA B C     1 
ATOM   9625  O  O     . ALA B 1 519 ? 175.374 128.262 145.158 1.00 107.27 ? 519  ALA B O     1 
ATOM   9626  C  CB    . ALA B 1 519 ? 177.838 129.189 146.060 1.00 105.31 ? 519  ALA B CB    1 
ATOM   9627  N  N     . VAL B 1 520 ? 176.161 126.273 144.479 1.00 107.43 ? 520  VAL B N     1 
ATOM   9628  C  CA    . VAL B 1 520 ? 174.866 125.768 144.040 1.00 103.64 ? 520  VAL B CA    1 
ATOM   9629  C  C     . VAL B 1 520 ? 174.005 125.452 145.254 1.00 99.83  ? 520  VAL B C     1 
ATOM   9630  O  O     . VAL B 1 520 ? 174.438 124.747 146.172 1.00 100.58 ? 520  VAL B O     1 
ATOM   9631  C  CB    . VAL B 1 520 ? 175.037 124.533 143.140 1.00 105.01 ? 520  VAL B CB    1 
ATOM   9632  C  CG1   . VAL B 1 520 ? 176.031 123.565 143.747 1.00 106.72 ? 520  VAL B CG1   1 
ATOM   9633  C  CG2   . VAL B 1 520 ? 173.702 123.849 142.923 1.00 106.84 ? 520  VAL B CG2   1 
ATOM   9634  N  N     . ALA B 1 521 ? 172.785 125.982 145.261 1.00 97.21  ? 521  ALA B N     1 
ATOM   9635  C  CA    . ALA B 1 521 ? 171.817 125.742 146.323 1.00 96.40  ? 521  ALA B CA    1 
ATOM   9636  C  C     . ALA B 1 521 ? 170.623 125.016 145.728 1.00 100.63 ? 521  ALA B C     1 
ATOM   9637  O  O     . ALA B 1 521 ? 169.855 125.608 144.965 1.00 103.98 ? 521  ALA B O     1 
ATOM   9638  C  CB    . ALA B 1 521 ? 171.376 127.054 146.975 1.00 97.65  ? 521  ALA B CB    1 
ATOM   9639  N  N     . ARG B 1 522 ? 170.458 123.746 146.086 1.00 105.26 ? 522  ARG B N     1 
ATOM   9640  C  CA    . ARG B 1 522 ? 169.437 122.891 145.496 1.00 106.43 ? 522  ARG B CA    1 
ATOM   9641  C  C     . ARG B 1 522 ? 168.144 123.021 146.289 1.00 105.21 ? 522  ARG B C     1 
ATOM   9642  O  O     . ARG B 1 522 ? 168.124 122.757 147.495 1.00 108.67 ? 522  ARG B O     1 
ATOM   9643  C  CB    . ARG B 1 522 ? 169.902 121.436 145.462 1.00 108.86 ? 522  ARG B CB    1 
ATOM   9644  C  CG    . ARG B 1 522 ? 171.316 121.254 144.947 1.00 109.29 ? 522  ARG B CG    1 
ATOM   9645  C  CD    . ARG B 1 522 ? 171.707 119.790 144.914 1.00 112.68 ? 522  ARG B CD    1 
ATOM   9646  N  NE    . ARG B 1 522 ? 173.128 119.616 144.645 1.00 122.03 ? 522  ARG B NE    1 
ATOM   9647  C  CZ    . ARG B 1 522 ? 173.664 119.606 143.432 1.00 124.69 ? 522  ARG B CZ    1 
ATOM   9648  N  NH1   . ARG B 1 522 ? 172.922 119.758 142.348 1.00 117.16 ? 522  ARG B NH1   1 
ATOM   9649  N  NH2   . ARG B 1 522 ? 174.978 119.440 143.305 1.00 124.99 ? 522  ARG B NH2   1 
ATOM   9650  N  N     . THR B 1 523 ? 167.074 123.422 145.613 1.00 105.09 ? 523  THR B N     1 
ATOM   9651  C  CA    . THR B 1 523 ? 165.757 123.540 146.213 1.00 110.51 ? 523  THR B CA    1 
ATOM   9652  C  C     . THR B 1 523 ? 164.831 122.493 145.604 1.00 118.23 ? 523  THR B C     1 
ATOM   9653  O  O     . THR B 1 523 ? 165.189 121.800 144.651 1.00 121.61 ? 523  THR B O     1 
ATOM   9654  C  CB    . THR B 1 523 ? 165.207 124.950 146.014 1.00 113.32 ? 523  THR B CB    1 
ATOM   9655  O  OG1   . THR B 1 523 ? 163.834 124.990 146.420 1.00 123.63 ? 523  THR B OG1   1 
ATOM   9656  C  CG2   . THR B 1 523 ? 165.295 125.341 144.552 1.00 109.44 ? 523  THR B CG2   1 
ATOM   9657  N  N     . ASP B 1 524 ? 163.614 122.388 146.138 1.00 122.45 ? 524  ASP B N     1 
ATOM   9658  C  CA    . ASP B 1 524 ? 162.631 121.401 145.687 1.00 129.07 ? 524  ASP B CA    1 
ATOM   9659  C  C     . ASP B 1 524 ? 161.427 122.157 145.135 1.00 130.98 ? 524  ASP B C     1 
ATOM   9660  O  O     . ASP B 1 524 ? 160.601 122.673 145.891 1.00 134.70 ? 524  ASP B O     1 
ATOM   9661  C  CB    . ASP B 1 524 ? 162.237 120.461 146.818 1.00 132.15 ? 524  ASP B CB    1 
ATOM   9662  C  CG    . ASP B 1 524 ? 161.559 119.203 146.317 1.00 141.75 ? 524  ASP B CG    1 
ATOM   9663  O  OD1   . ASP B 1 524 ? 162.233 118.389 145.651 1.00 144.25 ? 524  ASP B OD1   1 
ATOM   9664  O  OD2   . ASP B 1 524 ? 160.354 119.026 146.593 1.00 146.41 ? 524  ASP B OD2   1 
ATOM   9665  N  N     . VAL B 1 525 ? 161.332 122.213 143.811 1.00 130.92 ? 525  VAL B N     1 
ATOM   9666  C  CA    . VAL B 1 525 ? 160.281 122.951 143.118 1.00 128.48 ? 525  VAL B CA    1 
ATOM   9667  C  C     . VAL B 1 525 ? 159.002 122.126 143.044 1.00 130.76 ? 525  VAL B C     1 
ATOM   9668  O  O     . VAL B 1 525 ? 159.058 120.891 143.123 1.00 135.24 ? 525  VAL B O     1 
ATOM   9669  C  CB    . VAL B 1 525 ? 160.755 123.359 141.719 1.00 124.61 ? 525  VAL B CB    1 
ATOM   9670  C  CG1   . VAL B 1 525 ? 161.880 124.353 141.846 1.00 124.45 ? 525  VAL B CG1   1 
ATOM   9671  C  CG2   . VAL B 1 525 ? 161.200 122.132 140.948 1.00 123.83 ? 525  VAL B CG2   1 
ATOM   9672  N  N     . PRO B 1 526 ? 157.836 122.756 142.895 1.00 130.40 ? 526  PRO B N     1 
ATOM   9673  C  CA    . PRO B 1 526 ? 156.591 121.988 142.785 1.00 134.13 ? 526  PRO B CA    1 
ATOM   9674  C  C     . PRO B 1 526 ? 156.571 121.111 141.545 1.00 135.26 ? 526  PRO B C     1 
ATOM   9675  O  O     . PRO B 1 526 ? 157.076 121.479 140.482 1.00 134.31 ? 526  PRO B O     1 
ATOM   9676  C  CB    . PRO B 1 526 ? 155.510 123.072 142.711 1.00 127.01 ? 526  PRO B CB    1 
ATOM   9677  C  CG    . PRO B 1 526 ? 156.224 124.288 142.247 1.00 123.96 ? 526  PRO B CG    1 
ATOM   9678  C  CD    . PRO B 1 526 ? 157.584 124.204 142.860 1.00 129.14 ? 526  PRO B CD    1 
ATOM   9679  N  N     . HIS B 1 527 ? 155.966 119.936 141.695 1.00 134.63 ? 527  HIS B N     1 
ATOM   9680  C  CA    . HIS B 1 527 ? 155.875 118.955 140.625 1.00 133.80 ? 527  HIS B CA    1 
ATOM   9681  C  C     . HIS B 1 527 ? 154.545 119.001 139.887 1.00 134.59 ? 527  HIS B C     1 
ATOM   9682  O  O     . HIS B 1 527 ? 154.320 118.178 138.995 1.00 132.56 ? 527  HIS B O     1 
ATOM   9683  C  CB    . HIS B 1 527 ? 156.099 117.550 141.190 1.00 138.63 ? 527  HIS B CB    1 
ATOM   9684  C  CG    . HIS B 1 527 ? 155.474 117.336 142.533 1.00 147.93 ? 527  HIS B CG    1 
ATOM   9685  N  ND1   . HIS B 1 527 ? 154.194 117.750 142.832 1.00 148.55 ? 527  HIS B ND1   1 
ATOM   9686  C  CD2   . HIS B 1 527 ? 155.953 116.752 143.657 1.00 151.38 ? 527  HIS B CD2   1 
ATOM   9687  C  CE1   . HIS B 1 527 ? 153.911 117.430 144.082 1.00 149.54 ? 527  HIS B CE1   1 
ATOM   9688  N  NE2   . HIS B 1 527 ? 154.962 116.823 144.605 1.00 153.12 ? 527  HIS B NE2   1 
ATOM   9689  N  N     . ASP B 1 528 ? 153.666 119.938 140.230 1.00 135.96 ? 528  ASP B N     1 
ATOM   9690  C  CA    . ASP B 1 528 ? 152.355 120.043 139.611 1.00 138.12 ? 528  ASP B CA    1 
ATOM   9691  C  C     . ASP B 1 528 ? 152.216 121.395 138.928 1.00 133.92 ? 528  ASP B C     1 
ATOM   9692  O  O     . ASP B 1 528 ? 152.785 122.401 139.363 1.00 136.87 ? 528  ASP B O     1 
ATOM   9693  C  CB    . ASP B 1 528 ? 151.224 119.863 140.633 1.00 143.74 ? 528  ASP B CB    1 
ATOM   9694  C  CG    . ASP B 1 528 ? 150.901 118.407 140.895 1.00 154.19 ? 528  ASP B CG    1 
ATOM   9695  O  OD1   . ASP B 1 528 ? 151.035 117.590 139.960 1.00 158.65 ? 528  ASP B OD1   1 
ATOM   9696  O  OD2   . ASP B 1 528 ? 150.507 118.080 142.034 1.00 153.42 ? 528  ASP B OD2   1 
ATOM   9697  N  N     . LEU B 1 529 ? 151.436 121.402 137.846 1.00 127.63 ? 529  LEU B N     1 
ATOM   9698  C  CA    . LEU B 1 529 ? 151.234 122.633 137.094 1.00 123.76 ? 529  LEU B CA    1 
ATOM   9699  C  C     . LEU B 1 529 ? 150.551 123.702 137.934 1.00 127.37 ? 529  LEU B C     1 
ATOM   9700  O  O     . LEU B 1 529 ? 150.845 124.886 137.771 1.00 130.85 ? 529  LEU B O     1 
ATOM   9701  C  CB    . LEU B 1 529 ? 150.423 122.356 135.830 1.00 120.09 ? 529  LEU B CB    1 
ATOM   9702  C  CG    . LEU B 1 529 ? 150.307 123.531 134.858 1.00 119.98 ? 529  LEU B CG    1 
ATOM   9703  C  CD1   . LEU B 1 529 ? 151.678 123.942 134.356 1.00 120.81 ? 529  LEU B CD1   1 
ATOM   9704  C  CD2   . LEU B 1 529 ? 149.397 123.185 133.696 1.00 124.00 ? 529  LEU B CD2   1 
ATOM   9705  N  N     . VAL B 1 530 ? 149.659 123.315 138.847 1.00 126.80 ? 530  VAL B N     1 
ATOM   9706  C  CA    . VAL B 1 530 ? 148.954 124.308 139.654 1.00 130.08 ? 530  VAL B CA    1 
ATOM   9707  C  C     . VAL B 1 530 ? 149.901 124.977 140.649 1.00 134.06 ? 530  VAL B C     1 
ATOM   9708  O  O     . VAL B 1 530 ? 149.885 126.208 140.821 1.00 135.91 ? 530  VAL B O     1 
ATOM   9709  C  CB    . VAL B 1 530 ? 147.747 123.655 140.351 1.00 132.07 ? 530  VAL B CB    1 
ATOM   9710  C  CG1   . VAL B 1 530 ? 146.648 123.390 139.340 1.00 130.59 ? 530  VAL B CG1   1 
ATOM   9711  C  CG2   . VAL B 1 530 ? 148.156 122.354 141.021 1.00 133.67 ? 530  VAL B CG2   1 
ATOM   9712  N  N     . GLY B 1 531 ? 150.738 124.185 141.323 1.00 131.55 ? 531  GLY B N     1 
ATOM   9713  C  CA    . GLY B 1 531 ? 151.737 124.767 142.201 1.00 129.88 ? 531  GLY B CA    1 
ATOM   9714  C  C     . GLY B 1 531 ? 152.722 125.632 141.444 1.00 128.02 ? 531  GLY B C     1 
ATOM   9715  O  O     . GLY B 1 531 ? 153.116 126.704 141.916 1.00 129.32 ? 531  GLY B O     1 
ATOM   9716  N  N     . LEU B 1 532 ? 153.124 125.183 140.252 1.00 124.24 ? 532  LEU B N     1 
ATOM   9717  C  CA    . LEU B 1 532 ? 153.978 126.007 139.405 1.00 122.62 ? 532  LEU B CA    1 
ATOM   9718  C  C     . LEU B 1 532 ? 153.291 127.317 139.052 1.00 125.46 ? 532  LEU B C     1 
ATOM   9719  O  O     . LEU B 1 532 ? 153.932 128.371 139.013 1.00 129.73 ? 532  LEU B O     1 
ATOM   9720  C  CB    . LEU B 1 532 ? 154.354 125.244 138.137 1.00 116.57 ? 532  LEU B CB    1 
ATOM   9721  C  CG    . LEU B 1 532 ? 155.224 126.017 137.147 1.00 114.33 ? 532  LEU B CG    1 
ATOM   9722  C  CD1   . LEU B 1 532 ? 156.450 126.573 137.836 1.00 117.70 ? 532  LEU B CD1   1 
ATOM   9723  C  CD2   . LEU B 1 532 ? 155.614 125.162 135.957 1.00 115.88 ? 532  LEU B CD2   1 
ATOM   9724  N  N     . ILE B 1 533 ? 151.984 127.268 138.796 1.00 124.12 ? 533  ILE B N     1 
ATOM   9725  C  CA    . ILE B 1 533 ? 151.239 128.468 138.426 1.00 123.31 ? 533  ILE B CA    1 
ATOM   9726  C  C     . ILE B 1 533 ? 151.252 129.472 139.569 1.00 127.05 ? 533  ILE B C     1 
ATOM   9727  O  O     . ILE B 1 533 ? 151.528 130.659 139.370 1.00 132.16 ? 533  ILE B O     1 
ATOM   9728  C  CB    . ILE B 1 533 ? 149.804 128.097 138.016 1.00 118.11 ? 533  ILE B CB    1 
ATOM   9729  C  CG1   . ILE B 1 533 ? 149.778 127.593 136.577 1.00 116.49 ? 533  ILE B CG1   1 
ATOM   9730  C  CG2   . ILE B 1 533 ? 148.881 129.289 138.163 1.00 118.34 ? 533  ILE B CG2   1 
ATOM   9731  C  CD1   . ILE B 1 533 ? 148.417 127.170 136.119 1.00 118.86 ? 533  ILE B CD1   1 
ATOM   9732  N  N     . SER B 1 534 ? 150.968 129.008 140.787 1.00 125.59 ? 534  SER B N     1 
ATOM   9733  C  CA    . SER B 1 534 ? 150.968 129.920 141.933 1.00 129.37 ? 534  SER B CA    1 
ATOM   9734  C  C     . SER B 1 534 ? 152.361 130.498 142.182 1.00 131.46 ? 534  SER B C     1 
ATOM   9735  O  O     . SER B 1 534 ? 152.528 131.720 142.372 1.00 131.82 ? 534  SER B O     1 
ATOM   9736  C  CB    . SER B 1 534 ? 150.455 129.196 143.177 1.00 130.07 ? 534  SER B CB    1 
ATOM   9737  O  OG    . SER B 1 534 ? 149.172 128.640 142.951 1.00 128.18 ? 534  SER B OG    1 
ATOM   9738  N  N     . GLN B 1 535 ? 153.376 129.629 142.180 1.00 129.29 ? 535  GLN B N     1 
ATOM   9739  C  CA    . GLN B 1 535 ? 154.741 130.079 142.409 1.00 130.72 ? 535  GLN B CA    1 
ATOM   9740  C  C     . GLN B 1 535 ? 155.144 131.128 141.384 1.00 129.65 ? 535  GLN B C     1 
ATOM   9741  O  O     . GLN B 1 535 ? 155.634 132.205 141.741 1.00 132.53 ? 535  GLN B O     1 
ATOM   9742  C  CB    . GLN B 1 535 ? 155.694 128.886 142.358 1.00 128.34 ? 535  GLN B CB    1 
ATOM   9743  C  CG    . GLN B 1 535 ? 157.122 129.208 142.739 1.00 130.33 ? 535  GLN B CG    1 
ATOM   9744  C  CD    . GLN B 1 535 ? 158.054 128.037 142.523 1.00 129.80 ? 535  GLN B CD    1 
ATOM   9745  O  OE1   . GLN B 1 535 ? 157.750 127.127 141.755 1.00 127.63 ? 535  GLN B OE1   1 
ATOM   9746  N  NE2   . GLN B 1 535 ? 159.194 128.050 143.201 1.00 132.99 ? 535  GLN B NE2   1 
ATOM   9747  N  N     . ARG B 1 536 ? 154.912 130.843 140.101 1.00 125.06 ? 536  ARG B N     1 
ATOM   9748  C  CA    . ARG B 1 536 ? 155.313 131.775 139.061 1.00 126.13 ? 536  ARG B CA    1 
ATOM   9749  C  C     . ARG B 1 536 ? 154.465 133.034 139.086 1.00 130.72 ? 536  ARG B C     1 
ATOM   9750  O  O     . ARG B 1 536 ? 154.936 134.092 138.670 1.00 131.99 ? 536  ARG B O     1 
ATOM   9751  C  CB    . ARG B 1 536 ? 155.240 131.101 137.694 1.00 121.54 ? 536  ARG B CB    1 
ATOM   9752  C  CG    . ARG B 1 536 ? 156.379 130.135 137.449 1.00 117.08 ? 536  ARG B CG    1 
ATOM   9753  C  CD    . ARG B 1 536 ? 157.718 130.767 137.760 1.00 116.89 ? 536  ARG B CD    1 
ATOM   9754  N  NE    . ARG B 1 536 ? 158.825 129.936 137.305 1.00 118.56 ? 536  ARG B NE    1 
ATOM   9755  C  CZ    . ARG B 1 536 ? 159.342 128.940 138.009 1.00 124.82 ? 536  ARG B CZ    1 
ATOM   9756  N  NH1   . ARG B 1 536 ? 158.865 128.616 139.200 1.00 127.13 ? 536  ARG B NH1   1 
ATOM   9757  N  NH2   . ARG B 1 536 ? 160.362 128.251 137.508 1.00 122.61 ? 536  ARG B NH2   1 
ATOM   9758  N  N     . LYS B 1 537 ? 153.232 132.955 139.589 1.00 129.99 ? 537  LYS B N     1 
ATOM   9759  C  CA    . LYS B 1 537 ? 152.453 134.170 139.797 1.00 133.01 ? 537  LYS B CA    1 
ATOM   9760  C  C     . LYS B 1 537 ? 153.178 135.117 140.739 1.00 134.85 ? 537  LYS B C     1 
ATOM   9761  O  O     . LYS B 1 537 ? 153.395 136.293 140.416 1.00 137.99 ? 537  LYS B O     1 
ATOM   9762  C  CB    . LYS B 1 537 ? 151.074 133.825 140.357 1.00 132.51 ? 537  LYS B CB    1 
ATOM   9763  C  CG    . LYS B 1 537 ? 150.441 134.958 141.151 1.00 131.20 ? 537  LYS B CG    1 
ATOM   9764  C  CD    . LYS B 1 537 ? 149.535 134.435 142.248 1.00 132.61 ? 537  LYS B CD    1 
ATOM   9765  C  CE    . LYS B 1 537 ? 148.546 135.497 142.696 1.00 140.57 ? 537  LYS B CE    1 
ATOM   9766  N  NZ    . LYS B 1 537 ? 147.934 135.167 144.012 1.00 143.75 ? 537  LYS B NZ    1 
ATOM   9767  N  N     . ARG B 1 538 ? 153.576 134.614 141.909 1.00 130.93 ? 538  ARG B N     1 
ATOM   9768  C  CA    . ARG B 1 538 ? 154.249 135.486 142.872 1.00 131.01 ? 538  ARG B CA    1 
ATOM   9769  C  C     . ARG B 1 538 ? 155.605 135.957 142.344 1.00 129.70 ? 538  ARG B C     1 
ATOM   9770  O  O     . ARG B 1 538 ? 155.958 137.145 142.455 1.00 129.74 ? 538  ARG B O     1 
ATOM   9771  C  CB    . ARG B 1 538 ? 154.387 134.774 144.214 1.00 128.12 ? 538  ARG B CB    1 
ATOM   9772  C  CG    . ARG B 1 538 ? 153.043 134.537 144.879 1.00 131.33 ? 538  ARG B CG    1 
ATOM   9773  C  CD    . ARG B 1 538 ? 153.190 134.077 146.313 1.00 131.75 ? 538  ARG B CD    1 
ATOM   9774  N  NE    . ARG B 1 538 ? 153.000 132.638 146.436 1.00 132.09 ? 538  ARG B NE    1 
ATOM   9775  C  CZ    . ARG B 1 538 ? 151.843 132.008 146.285 1.00 138.08 ? 538  ARG B CZ    1 
ATOM   9776  N  NH1   . ARG B 1 538 ? 150.723 132.667 146.042 1.00 141.26 ? 538  ARG B NH1   1 
ATOM   9777  N  NH2   . ARG B 1 538 ? 151.808 130.683 146.390 1.00 140.45 ? 538  ARG B NH2   1 
ATOM   9778  N  N     . TRP B 1 539 ? 156.368 135.040 141.741 1.00 128.87 ? 539  TRP B N     1 
ATOM   9779  C  CA    . TRP B 1 539 ? 157.649 135.401 141.139 1.00 128.60 ? 539  TRP B CA    1 
ATOM   9780  C  C     . TRP B 1 539 ? 157.493 136.511 140.110 1.00 130.15 ? 539  TRP B C     1 
ATOM   9781  O  O     . TRP B 1 539 ? 158.235 137.497 140.135 1.00 131.91 ? 539  TRP B O     1 
ATOM   9782  C  CB    . TRP B 1 539 ? 158.294 134.171 140.500 1.00 130.78 ? 539  TRP B CB    1 
ATOM   9783  C  CG    . TRP B 1 539 ? 158.806 133.146 141.461 1.00 127.94 ? 539  TRP B CG    1 
ATOM   9784  C  CD1   . TRP B 1 539 ? 158.248 132.765 142.642 1.00 128.48 ? 539  TRP B CD1   1 
ATOM   9785  C  CD2   . TRP B 1 539 ? 159.961 132.322 141.280 1.00 127.64 ? 539  TRP B CD2   1 
ATOM   9786  N  NE1   . TRP B 1 539 ? 159.003 131.782 143.228 1.00 130.92 ? 539  TRP B NE1   1 
ATOM   9787  C  CE2   . TRP B 1 539 ? 160.059 131.488 142.407 1.00 130.66 ? 539  TRP B CE2   1 
ATOM   9788  C  CE3   . TRP B 1 539 ? 160.931 132.222 140.281 1.00 125.02 ? 539  TRP B CE3   1 
ATOM   9789  C  CZ2   . TRP B 1 539 ? 161.087 130.565 142.563 1.00 130.88 ? 539  TRP B CZ2   1 
ATOM   9790  C  CZ3   . TRP B 1 539 ? 161.949 131.306 140.437 1.00 128.90 ? 539  TRP B CZ3   1 
ATOM   9791  C  CH2   . TRP B 1 539 ? 162.020 130.491 141.569 1.00 132.32 ? 539  TRP B CH2   1 
ATOM   9792  N  N     . LEU B 1 540 ? 156.534 136.370 139.192 1.00 127.59 ? 540  LEU B N     1 
ATOM   9793  C  CA    . LEU B 1 540 ? 156.388 137.346 138.121 1.00 130.43 ? 540  LEU B CA    1 
ATOM   9794  C  C     . LEU B 1 540 ? 155.878 138.677 138.646 1.00 135.83 ? 540  LEU B C     1 
ATOM   9795  O  O     . LEU B 1 540 ? 156.291 139.733 138.160 1.00 140.27 ? 540  LEU B O     1 
ATOM   9796  C  CB    . LEU B 1 540 ? 155.464 136.805 137.036 1.00 128.56 ? 540  LEU B CB    1 
ATOM   9797  C  CG    . LEU B 1 540 ? 156.086 135.733 136.146 1.00 131.97 ? 540  LEU B CG    1 
ATOM   9798  C  CD1   . LEU B 1 540 ? 155.034 135.130 135.251 1.00 130.11 ? 540  LEU B CD1   1 
ATOM   9799  C  CD2   . LEU B 1 540 ? 157.218 136.319 135.323 1.00 138.90 ? 540  LEU B CD2   1 
ATOM   9800  N  N     . ASN B 1 541 ? 154.981 138.655 139.634 1.00 133.23 ? 541  ASN B N     1 
ATOM   9801  C  CA    . ASN B 1 541 ? 154.523 139.908 140.225 1.00 130.74 ? 541  ASN B CA    1 
ATOM   9802  C  C     . ASN B 1 541 ? 155.699 140.694 140.787 1.00 129.48 ? 541  ASN B C     1 
ATOM   9803  O  O     . ASN B 1 541 ? 155.920 141.871 140.438 1.00 125.55 ? 541  ASN B O     1 
ATOM   9804  C  CB    . ASN B 1 541 ? 153.508 139.619 141.328 1.00 127.50 ? 541  ASN B CB    1 
ATOM   9805  C  CG    . ASN B 1 541 ? 152.131 140.092 140.971 1.00 131.72 ? 541  ASN B CG    1 
ATOM   9806  O  OD1   . ASN B 1 541 ? 151.927 140.650 139.900 1.00 134.67 ? 541  ASN B OD1   1 
ATOM   9807  N  ND2   . ASN B 1 541 ? 151.174 139.886 141.871 1.00 134.45 ? 541  ASN B ND2   1 
ATOM   9808  N  N     . GLY B 1 542 ? 156.488 140.036 141.640 1.00 133.77 ? 542  GLY B N     1 
ATOM   9809  C  CA    . GLY B 1 542 ? 157.633 140.708 142.226 1.00 134.82 ? 542  GLY B CA    1 
ATOM   9810  C  C     . GLY B 1 542 ? 158.635 141.152 141.182 1.00 133.90 ? 542  GLY B C     1 
ATOM   9811  O  O     . GLY B 1 542 ? 159.151 142.269 141.237 1.00 137.48 ? 542  GLY B O     1 
ATOM   9812  N  N     . ALA B 1 543 ? 158.915 140.285 140.206 1.00 132.56 ? 543  ALA B N     1 
ATOM   9813  C  CA    . ALA B 1 543 ? 159.907 140.609 139.188 1.00 133.17 ? 543  ALA B CA    1 
ATOM   9814  C  C     . ALA B 1 543 ? 159.480 141.812 138.362 1.00 131.78 ? 543  ALA B C     1 
ATOM   9815  O  O     . ALA B 1 543 ? 160.280 142.724 138.130 1.00 132.13 ? 543  ALA B O     1 
ATOM   9816  C  CB    . ALA B 1 543 ? 160.147 139.398 138.288 1.00 135.31 ? 543  ALA B CB    1 
ATOM   9817  N  N     . PHE B 1 544 ? 158.218 141.846 137.930 1.00 130.06 ? 544  PHE B N     1 
ATOM   9818  C  CA    . PHE B 1 544 ? 157.749 142.953 137.105 1.00 130.59 ? 544  PHE B CA    1 
ATOM   9819  C  C     . PHE B 1 544 ? 157.820 144.270 137.859 1.00 131.82 ? 544  PHE B C     1 
ATOM   9820  O  O     . PHE B 1 544 ? 158.349 145.266 137.345 1.00 132.08 ? 544  PHE B O     1 
ATOM   9821  C  CB    . PHE B 1 544 ? 156.322 142.695 136.628 1.00 129.13 ? 544  PHE B CB    1 
ATOM   9822  C  CG    . PHE B 1 544 ? 155.804 143.748 135.693 1.00 126.93 ? 544  PHE B CG    1 
ATOM   9823  C  CD1   . PHE B 1 544 ? 156.391 143.944 134.456 1.00 123.75 ? 544  PHE B CD1   1 
ATOM   9824  C  CD2   . PHE B 1 544 ? 154.736 144.550 136.055 1.00 127.07 ? 544  PHE B CD2   1 
ATOM   9825  C  CE1   . PHE B 1 544 ? 155.920 144.914 133.595 1.00 121.63 ? 544  PHE B CE1   1 
ATOM   9826  C  CE2   . PHE B 1 544 ? 154.260 145.522 135.198 1.00 123.34 ? 544  PHE B CE2   1 
ATOM   9827  C  CZ    . PHE B 1 544 ? 154.853 145.703 133.967 1.00 119.87 ? 544  PHE B CZ    1 
ATOM   9828  N  N     . PHE B 1 545 ? 157.298 144.305 139.086 1.00 133.19 ? 545  PHE B N     1 
ATOM   9829  C  CA    . PHE B 1 545 ? 157.296 145.612 139.733 1.00 132.07 ? 545  PHE B CA    1 
ATOM   9830  C  C     . PHE B 1 545 ? 158.672 146.014 140.256 1.00 130.74 ? 545  PHE B C     1 
ATOM   9831  O  O     . PHE B 1 545 ? 158.989 147.205 140.269 1.00 129.81 ? 545  PHE B O     1 
ATOM   9832  C  CB    . PHE B 1 545 ? 156.227 145.670 140.817 1.00 137.19 ? 545  PHE B CB    1 
ATOM   9833  C  CG    . PHE B 1 545 ? 154.891 146.106 140.292 1.00 138.25 ? 545  PHE B CG    1 
ATOM   9834  C  CD1   . PHE B 1 545 ? 154.621 147.449 140.100 1.00 141.17 ? 545  PHE B CD1   1 
ATOM   9835  C  CD2   . PHE B 1 545 ? 153.931 145.181 139.937 1.00 136.25 ? 545  PHE B CD2   1 
ATOM   9836  C  CE1   . PHE B 1 545 ? 153.404 147.860 139.599 1.00 141.76 ? 545  PHE B CE1   1 
ATOM   9837  C  CE2   . PHE B 1 545 ? 152.716 145.590 139.432 1.00 133.77 ? 545  PHE B CE2   1 
ATOM   9838  C  CZ    . PHE B 1 545 ? 152.451 146.928 139.265 1.00 134.46 ? 545  PHE B CZ    1 
ATOM   9839  N  N     . ALA B 1 546 ? 159.530 145.064 140.628 1.00 130.17 ? 546  ALA B N     1 
ATOM   9840  C  CA    . ALA B 1 546 ? 160.900 145.433 140.961 1.00 129.01 ? 546  ALA B CA    1 
ATOM   9841  C  C     . ALA B 1 546 ? 161.645 145.933 139.731 1.00 128.62 ? 546  ALA B C     1 
ATOM   9842  O  O     . ALA B 1 546 ? 162.490 146.832 139.827 1.00 129.37 ? 546  ALA B O     1 
ATOM   9843  C  CB    . ALA B 1 546 ? 161.625 144.246 141.587 1.00 129.95 ? 546  ALA B CB    1 
ATOM   9844  N  N     . THR B 1 547 ? 161.348 145.359 138.562 1.00 125.04 ? 547  THR B N     1 
ATOM   9845  C  CA    . THR B 1 547 ? 161.918 145.864 137.320 1.00 123.21 ? 547  THR B CA    1 
ATOM   9846  C  C     . THR B 1 547 ? 161.471 147.293 137.058 1.00 123.85 ? 547  THR B C     1 
ATOM   9847  O  O     . THR B 1 547 ? 162.272 148.137 136.642 1.00 126.24 ? 547  THR B O     1 
ATOM   9848  C  CB    . THR B 1 547 ? 161.515 144.960 136.159 1.00 121.35 ? 547  THR B CB    1 
ATOM   9849  O  OG1   . THR B 1 547 ? 162.032 143.642 136.376 1.00 124.38 ? 547  THR B OG1   1 
ATOM   9850  C  CG2   . THR B 1 547 ? 162.056 145.505 134.860 1.00 118.86 ? 547  THR B CG2   1 
ATOM   9851  N  N     . LEU B 1 548 ? 160.190 147.581 137.291 1.00 122.89 ? 548  LEU B N     1 
ATOM   9852  C  CA    . LEU B 1 548 ? 159.717 148.955 137.150 1.00 121.87 ? 548  LEU B CA    1 
ATOM   9853  C  C     . LEU B 1 548 ? 160.424 149.885 138.128 1.00 122.79 ? 548  LEU B C     1 
ATOM   9854  O  O     . LEU B 1 548 ? 160.779 151.016 137.775 1.00 124.15 ? 548  LEU B O     1 
ATOM   9855  C  CB    . LEU B 1 548 ? 158.203 149.020 137.344 1.00 123.41 ? 548  LEU B CB    1 
ATOM   9856  C  CG    . LEU B 1 548 ? 157.368 148.677 136.112 1.00 119.46 ? 548  LEU B CG    1 
ATOM   9857  C  CD1   . LEU B 1 548 ? 155.916 149.055 136.333 1.00 125.26 ? 548  LEU B CD1   1 
ATOM   9858  C  CD2   . LEU B 1 548 ? 157.922 149.374 134.883 1.00 112.72 ? 548  LEU B CD2   1 
ATOM   9859  N  N     . PHE B 1 549 ? 160.634 149.427 139.365 1.00 120.58 ? 549  PHE B N     1 
ATOM   9860  C  CA    . PHE B 1 549 ? 161.359 150.237 140.340 1.00 118.51 ? 549  PHE B CA    1 
ATOM   9861  C  C     . PHE B 1 549 ? 162.761 150.556 139.845 1.00 117.92 ? 549  PHE B C     1 
ATOM   9862  O  O     . PHE B 1 549 ? 163.190 151.715 139.871 1.00 120.00 ? 549  PHE B O     1 
ATOM   9863  C  CB    . PHE B 1 549 ? 161.424 149.509 141.684 1.00 122.65 ? 549  PHE B CB    1 
ATOM   9864  C  CG    . PHE B 1 549 ? 162.194 150.242 142.746 1.00 119.26 ? 549  PHE B CG    1 
ATOM   9865  C  CD1   . PHE B 1 549 ? 161.631 151.308 143.428 1.00 115.26 ? 549  PHE B CD1   1 
ATOM   9866  C  CD2   . PHE B 1 549 ? 163.476 149.848 143.079 1.00 121.94 ? 549  PHE B CD2   1 
ATOM   9867  C  CE1   . PHE B 1 549 ? 162.340 151.972 144.410 1.00 117.48 ? 549  PHE B CE1   1 
ATOM   9868  C  CE2   . PHE B 1 549 ? 164.186 150.508 144.058 1.00 122.81 ? 549  PHE B CE2   1 
ATOM   9869  C  CZ    . PHE B 1 549 ? 163.620 151.570 144.723 1.00 121.65 ? 549  PHE B CZ    1 
ATOM   9870  N  N     . SER B 1 550 ? 163.485 149.537 139.378 1.00 114.64 ? 550  SER B N     1 
ATOM   9871  C  CA    . SER B 1 550 ? 164.844 149.753 138.895 1.00 114.69 ? 550  SER B CA    1 
ATOM   9872  C  C     . SER B 1 550 ? 164.860 150.692 137.696 1.00 117.16 ? 550  SER B C     1 
ATOM   9873  O  O     . SER B 1 550 ? 165.714 151.581 137.606 1.00 118.16 ? 550  SER B O     1 
ATOM   9874  C  CB    . SER B 1 550 ? 165.490 148.417 138.540 1.00 117.08 ? 550  SER B CB    1 
ATOM   9875  O  OG    . SER B 1 550 ? 166.735 148.614 137.897 1.00 126.13 ? 550  SER B OG    1 
ATOM   9876  N  N     . ILE B 1 551 ? 163.915 150.518 136.772 1.00 116.45 ? 551  ILE B N     1 
ATOM   9877  C  CA    . ILE B 1 551 ? 163.872 151.359 135.579 1.00 114.52 ? 551  ILE B CA    1 
ATOM   9878  C  C     . ILE B 1 551 ? 163.615 152.812 135.954 1.00 117.01 ? 551  ILE B C     1 
ATOM   9879  O  O     . ILE B 1 551 ? 164.271 153.726 135.441 1.00 117.31 ? 551  ILE B O     1 
ATOM   9880  C  CB    . ILE B 1 551 ? 162.812 150.830 134.596 1.00 113.24 ? 551  ILE B CB    1 
ATOM   9881  C  CG1   . ILE B 1 551 ? 163.321 149.573 133.892 1.00 112.28 ? 551  ILE B CG1   1 
ATOM   9882  C  CG2   . ILE B 1 551 ? 162.444 151.893 133.581 1.00 110.19 ? 551  ILE B CG2   1 
ATOM   9883  C  CD1   . ILE B 1 551 ? 162.293 148.925 132.999 1.00 112.90 ? 551  ILE B CD1   1 
ATOM   9884  N  N     . TRP B 1 552 ? 162.665 153.051 136.860 1.00 118.10 ? 552  TRP B N     1 
ATOM   9885  C  CA    . TRP B 1 552 ? 162.303 154.426 137.187 1.00 118.47 ? 552  TRP B CA    1 
ATOM   9886  C  C     . TRP B 1 552 ? 163.353 155.093 138.067 1.00 117.36 ? 552  TRP B C     1 
ATOM   9887  O  O     . TRP B 1 552 ? 163.535 156.314 138.002 1.00 122.84 ? 552  TRP B O     1 
ATOM   9888  C  CB    . TRP B 1 552 ? 160.933 154.467 137.863 1.00 121.17 ? 552  TRP B CB    1 
ATOM   9889  C  CG    . TRP B 1 552 ? 160.477 155.854 138.200 1.00 130.13 ? 552  TRP B CG    1 
ATOM   9890  C  CD1   . TRP B 1 552 ? 160.156 156.333 139.436 1.00 132.17 ? 552  TRP B CD1   1 
ATOM   9891  C  CD2   . TRP B 1 552 ? 160.298 156.946 137.288 1.00 133.77 ? 552  TRP B CD2   1 
ATOM   9892  N  NE1   . TRP B 1 552 ? 159.785 157.653 139.351 1.00 135.04 ? 552  TRP B NE1   1 
ATOM   9893  C  CE2   . TRP B 1 552 ? 159.864 158.053 138.043 1.00 136.87 ? 552  TRP B CE2   1 
ATOM   9894  C  CE3   . TRP B 1 552 ? 160.460 157.095 135.907 1.00 129.10 ? 552  TRP B CE3   1 
ATOM   9895  C  CZ2   . TRP B 1 552 ? 159.590 159.289 137.465 1.00 136.01 ? 552  TRP B CZ2   1 
ATOM   9896  C  CZ3   . TRP B 1 552 ? 160.189 158.322 135.335 1.00 128.83 ? 552  TRP B CZ3   1 
ATOM   9897  C  CH2   . TRP B 1 552 ? 159.759 159.403 136.112 1.00 134.92 ? 552  TRP B CH2   1 
ATOM   9898  N  N     . ASN B 1 553 ? 164.054 154.321 138.896 1.00 112.92 ? 553  ASN B N     1 
ATOM   9899  C  CA    . ASN B 1 553 ? 165.011 154.880 139.839 1.00 113.63 ? 553  ASN B CA    1 
ATOM   9900  C  C     . ASN B 1 553 ? 166.458 154.649 139.430 1.00 112.94 ? 553  ASN B C     1 
ATOM   9901  O  O     . ASN B 1 553 ? 167.357 154.829 140.256 1.00 115.12 ? 553  ASN B O     1 
ATOM   9902  C  CB    . ASN B 1 553 ? 164.770 154.302 141.232 1.00 112.17 ? 553  ASN B CB    1 
ATOM   9903  C  CG    . ASN B 1 553 ? 163.406 154.655 141.777 1.00 115.12 ? 553  ASN B CG    1 
ATOM   9904  O  OD1   . ASN B 1 553 ? 162.424 154.694 141.039 1.00 118.36 ? 553  ASN B OD1   1 
ATOM   9905  N  ND2   . ASN B 1 553 ? 163.335 154.912 143.075 1.00 117.44 ? 553  ASN B ND2   1 
ATOM   9906  N  N     . TRP B 1 554 ? 166.707 154.251 138.181 1.00 110.18 ? 554  TRP B N     1 
ATOM   9907  C  CA    . TRP B 1 554 ? 168.079 153.992 137.759 1.00 109.83 ? 554  TRP B CA    1 
ATOM   9908  C  C     . TRP B 1 554 ? 168.932 155.252 137.788 1.00 114.06 ? 554  TRP B C     1 
ATOM   9909  O  O     . TRP B 1 554 ? 170.164 155.163 137.822 1.00 117.82 ? 554  TRP B O     1 
ATOM   9910  C  CB    . TRP B 1 554 ? 168.093 153.380 136.362 1.00 109.08 ? 554  TRP B CB    1 
ATOM   9911  C  CG    . TRP B 1 554 ? 169.393 152.741 136.018 1.00 107.72 ? 554  TRP B CG    1 
ATOM   9912  C  CD1   . TRP B 1 554 ? 170.464 153.333 135.422 1.00 110.01 ? 554  TRP B CD1   1 
ATOM   9913  C  CD2   . TRP B 1 554 ? 169.764 151.380 136.251 1.00 108.41 ? 554  TRP B CD2   1 
ATOM   9914  N  NE1   . TRP B 1 554 ? 171.482 152.425 135.269 1.00 112.11 ? 554  TRP B NE1   1 
ATOM   9915  C  CE2   . TRP B 1 554 ? 171.076 151.218 135.771 1.00 111.37 ? 554  TRP B CE2   1 
ATOM   9916  C  CE3   . TRP B 1 554 ? 169.114 150.284 136.819 1.00 109.70 ? 554  TRP B CE3   1 
ATOM   9917  C  CZ2   . TRP B 1 554 ? 171.749 150.003 135.841 1.00 112.41 ? 554  TRP B CZ2   1 
ATOM   9918  C  CZ3   . TRP B 1 554 ? 169.783 149.081 136.889 1.00 109.13 ? 554  TRP B CZ3   1 
ATOM   9919  C  CH2   . TRP B 1 554 ? 171.086 148.950 136.404 1.00 109.59 ? 554  TRP B CH2   1 
ATOM   9920  N  N     . GLY B 1 555 ? 168.306 156.429 137.776 1.00 111.89 ? 555  GLY B N     1 
ATOM   9921  C  CA    . GLY B 1 555 ? 169.068 157.662 137.854 1.00 114.41 ? 555  GLY B CA    1 
ATOM   9922  C  C     . GLY B 1 555 ? 169.793 157.851 139.168 1.00 117.44 ? 555  GLY B C     1 
ATOM   9923  O  O     . GLY B 1 555 ? 170.748 158.633 139.231 1.00 121.57 ? 555  GLY B O     1 
ATOM   9924  N  N     . ARG B 1 556 ? 169.367 157.146 140.217 1.00 111.94 ? 556  ARG B N     1 
ATOM   9925  C  CA    . ARG B 1 556 ? 170.006 157.284 141.518 1.00 114.96 ? 556  ARG B CA    1 
ATOM   9926  C  C     . ARG B 1 556 ? 171.453 156.813 141.506 1.00 117.13 ? 556  ARG B C     1 
ATOM   9927  O  O     . ARG B 1 556 ? 172.264 157.334 142.276 1.00 121.81 ? 556  ARG B O     1 
ATOM   9928  C  CB    . ARG B 1 556 ? 169.221 156.513 142.577 1.00 113.02 ? 556  ARG B CB    1 
ATOM   9929  C  CG    . ARG B 1 556 ? 169.613 156.864 143.998 1.00 113.93 ? 556  ARG B CG    1 
ATOM   9930  C  CD    . ARG B 1 556 ? 168.891 155.995 145.006 1.00 114.99 ? 556  ARG B CD    1 
ATOM   9931  N  NE    . ARG B 1 556 ? 167.446 156.044 144.836 1.00 118.32 ? 556  ARG B NE    1 
ATOM   9932  C  CZ    . ARG B 1 556 ? 166.591 155.283 145.504 1.00 120.05 ? 556  ARG B CZ    1 
ATOM   9933  N  NH1   . ARG B 1 556 ? 167.006 154.396 146.392 1.00 120.64 ? 556  ARG B NH1   1 
ATOM   9934  N  NH2   . ARG B 1 556 ? 165.288 155.419 145.279 1.00 120.65 ? 556  ARG B NH2   1 
ATOM   9935  N  N     . ILE B 1 557 ? 171.797 155.854 140.644 1.00 111.95 ? 557  ILE B N     1 
ATOM   9936  C  CA    . ILE B 1 557 ? 173.168 155.353 140.599 1.00 111.91 ? 557  ILE B CA    1 
ATOM   9937  C  C     . ILE B 1 557 ? 174.135 156.472 140.239 1.00 115.90 ? 557  ILE B C     1 
ATOM   9938  O  O     . ILE B 1 557 ? 175.212 156.598 140.833 1.00 119.84 ? 557  ILE B O     1 
ATOM   9939  C  CB    . ILE B 1 557 ? 173.274 154.174 139.616 1.00 107.81 ? 557  ILE B CB    1 
ATOM   9940  C  CG1   . ILE B 1 557 ? 172.322 153.053 140.026 1.00 110.25 ? 557  ILE B CG1   1 
ATOM   9941  C  CG2   . ILE B 1 557 ? 174.698 153.663 139.552 1.00 109.37 ? 557  ILE B CG2   1 
ATOM   9942  C  CD1   . ILE B 1 557 ? 172.442 151.816 139.177 1.00 104.98 ? 557  ILE B CD1   1 
ATOM   9943  N  N     . TYR B 1 558 ? 173.770 157.301 139.260 1.00 113.70 ? 558  TYR B N     1 
ATOM   9944  C  CA    . TYR B 1 558 ? 174.623 158.419 138.875 1.00 115.11 ? 558  TYR B CA    1 
ATOM   9945  C  C     . TYR B 1 558 ? 174.409 159.626 139.779 1.00 115.84 ? 558  TYR B C     1 
ATOM   9946  O  O     . TYR B 1 558 ? 175.341 160.406 140.007 1.00 115.99 ? 558  TYR B O     1 
ATOM   9947  C  CB    . TYR B 1 558 ? 174.363 158.795 137.417 1.00 112.29 ? 558  TYR B CB    1 
ATOM   9948  C  CG    . TYR B 1 558 ? 174.014 157.614 136.545 1.00 112.85 ? 558  TYR B CG    1 
ATOM   9949  C  CD1   . TYR B 1 558 ? 175.002 156.781 136.045 1.00 114.48 ? 558  TYR B CD1   1 
ATOM   9950  C  CD2   . TYR B 1 558 ? 172.695 157.325 136.234 1.00 112.02 ? 558  TYR B CD2   1 
ATOM   9951  C  CE1   . TYR B 1 558 ? 174.689 155.699 135.255 1.00 112.77 ? 558  TYR B CE1   1 
ATOM   9952  C  CE2   . TYR B 1 558 ? 172.372 156.245 135.445 1.00 112.63 ? 558  TYR B CE2   1 
ATOM   9953  C  CZ    . TYR B 1 558 ? 173.372 155.436 134.959 1.00 110.39 ? 558  TYR B CZ    1 
ATOM   9954  O  OH    . TYR B 1 558 ? 173.052 154.358 134.173 1.00 105.91 ? 558  TYR B OH    1 
ATOM   9955  N  N     . SER B 1 559 ? 173.194 159.798 140.303 1.00 114.51 ? 559  SER B N     1 
ATOM   9956  C  CA    . SER B 1 559 ? 172.888 160.999 141.071 1.00 119.10 ? 559  SER B CA    1 
ATOM   9957  C  C     . SER B 1 559 ? 173.519 160.964 142.458 1.00 121.77 ? 559  SER B C     1 
ATOM   9958  O  O     . SER B 1 559 ? 174.022 161.985 142.940 1.00 123.94 ? 559  SER B O     1 
ATOM   9959  C  CB    . SER B 1 559 ? 171.375 161.178 141.178 1.00 120.79 ? 559  SER B CB    1 
ATOM   9960  O  OG    . SER B 1 559 ? 171.020 161.770 142.414 1.00 126.98 ? 559  SER B OG    1 
ATOM   9961  N  N     . GLU B 1 560 ? 173.504 159.807 143.117 1.00 120.76 ? 560  GLU B N     1 
ATOM   9962  C  CA    . GLU B 1 560 ? 173.903 159.704 144.516 1.00 122.28 ? 560  GLU B CA    1 
ATOM   9963  C  C     . GLU B 1 560 ? 175.153 158.870 144.744 1.00 121.87 ? 560  GLU B C     1 
ATOM   9964  O  O     . GLU B 1 560 ? 176.067 159.323 145.434 1.00 126.99 ? 560  GLU B O     1 
ATOM   9965  C  CB    . GLU B 1 560 ? 172.756 159.118 145.344 1.00 120.90 ? 560  GLU B CB    1 
ATOM   9966  C  CG    . GLU B 1 560 ? 171.490 159.953 145.312 1.00 121.26 ? 560  GLU B CG    1 
ATOM   9967  C  CD    . GLU B 1 560 ? 170.407 159.403 146.216 1.00 128.93 ? 560  GLU B CD    1 
ATOM   9968  O  OE1   . GLU B 1 560 ? 170.673 158.415 146.932 1.00 133.32 ? 560  GLU B OE1   1 
ATOM   9969  O  OE2   . GLU B 1 560 ? 169.290 159.959 146.212 1.00 131.41 ? 560  GLU B OE2   1 
ATOM   9970  N  N     . SER B 1 561 ? 175.217 157.665 144.187 1.00 117.95 ? 561  SER B N     1 
ATOM   9971  C  CA    . SER B 1 561 ? 176.350 156.786 144.422 1.00 118.11 ? 561  SER B CA    1 
ATOM   9972  C  C     . SER B 1 561 ? 177.628 157.381 143.838 1.00 122.10 ? 561  SER B C     1 
ATOM   9973  O  O     . SER B 1 561 ? 177.602 158.258 142.970 1.00 127.86 ? 561  SER B O     1 
ATOM   9974  C  CB    . SER B 1 561 ? 176.092 155.410 143.814 1.00 115.89 ? 561  SER B CB    1 
ATOM   9975  O  OG    . SER B 1 561 ? 177.291 154.661 143.745 1.00 116.92 ? 561  SER B OG    1 
ATOM   9976  N  N     . LYS B 1 562 ? 178.769 156.892 144.330 1.00 120.78 ? 562  LYS B N     1 
ATOM   9977  C  CA    . LYS B 1 562 ? 180.078 157.279 143.803 1.00 121.38 ? 562  LYS B CA    1 
ATOM   9978  C  C     . LYS B 1 562 ? 180.731 156.022 143.239 1.00 117.72 ? 562  LYS B C     1 
ATOM   9979  O  O     . LYS B 1 562 ? 181.539 155.370 143.900 1.00 115.12 ? 562  LYS B O     1 
ATOM   9980  C  CB    . LYS B 1 562 ? 180.948 157.939 144.872 1.00 122.04 ? 562  LYS B CB    1 
ATOM   9981  C  CG    . LYS B 1 562 ? 180.765 157.379 146.268 1.00 126.63 ? 562  LYS B CG    1 
ATOM   9982  C  CD    . LYS B 1 562 ? 181.787 157.958 147.239 1.00 133.57 ? 562  LYS B CD    1 
ATOM   9983  C  CE    . LYS B 1 562 ? 181.966 159.457 147.052 1.00 136.22 ? 562  LYS B CE    1 
ATOM   9984  N  NZ    . LYS B 1 562 ? 180.709 160.211 147.308 1.00 132.37 ? 562  LYS B NZ    1 
ATOM   9985  N  N     . HIS B 1 563 ? 180.383 155.697 142.001 1.00 115.50 ? 563  HIS B N     1 
ATOM   9986  C  CA    . HIS B 1 563 ? 181.011 154.615 141.266 1.00 112.14 ? 563  HIS B CA    1 
ATOM   9987  C  C     . HIS B 1 563 ? 182.116 155.182 140.382 1.00 113.40 ? 563  HIS B C     1 
ATOM   9988  O  O     . HIS B 1 563 ? 182.217 156.390 140.163 1.00 116.25 ? 563  HIS B O     1 
ATOM   9989  C  CB    . HIS B 1 563 ? 179.980 153.862 140.423 1.00 116.68 ? 563  HIS B CB    1 
ATOM   9990  C  CG    . HIS B 1 563 ? 179.243 152.794 141.167 1.00 118.85 ? 563  HIS B CG    1 
ATOM   9991  N  ND1   . HIS B 1 563 ? 178.006 153.002 141.737 1.00 117.32 ? 563  HIS B ND1   1 
ATOM   9992  C  CD2   . HIS B 1 563 ? 179.562 151.504 141.423 1.00 118.58 ? 563  HIS B CD2   1 
ATOM   9993  C  CE1   . HIS B 1 563 ? 177.597 151.887 142.315 1.00 113.39 ? 563  HIS B CE1   1 
ATOM   9994  N  NE2   . HIS B 1 563 ? 178.524 150.963 142.140 1.00 113.57 ? 563  HIS B NE2   1 
ATOM   9995  N  N     . THR B 1 564 ? 182.954 154.293 139.864 1.00 112.94 ? 564  THR B N     1 
ATOM   9996  C  CA    . THR B 1 564 ? 183.918 154.703 138.860 1.00 118.26 ? 564  THR B CA    1 
ATOM   9997  C  C     . THR B 1 564 ? 183.183 155.114 137.587 1.00 119.83 ? 564  THR B C     1 
ATOM   9998  O  O     . THR B 1 564 ? 182.039 154.722 137.348 1.00 121.12 ? 564  THR B O     1 
ATOM   9999  C  CB    . THR B 1 564 ? 184.903 153.572 138.567 1.00 121.08 ? 564  THR B CB    1 
ATOM   10000 O  OG1   . THR B 1 564 ? 185.119 152.808 139.759 1.00 122.50 ? 564  THR B OG1   1 
ATOM   10001 C  CG2   . THR B 1 564 ? 186.236 154.133 138.096 1.00 120.58 ? 564  THR B CG2   1 
ATOM   10002 N  N     . PHE B 1 565 ? 183.843 155.943 136.776 1.00 117.71 ? 565  PHE B N     1 
ATOM   10003 C  CA    . PHE B 1 565 ? 183.240 156.368 135.516 1.00 116.16 ? 565  PHE B CA    1 
ATOM   10004 C  C     . PHE B 1 565 ? 182.970 155.173 134.611 1.00 119.94 ? 565  PHE B C     1 
ATOM   10005 O  O     . PHE B 1 565 ? 181.936 155.113 133.931 1.00 123.33 ? 565  PHE B O     1 
ATOM   10006 C  CB    . PHE B 1 565 ? 184.151 157.380 134.821 1.00 114.92 ? 565  PHE B CB    1 
ATOM   10007 C  CG    . PHE B 1 565 ? 183.553 157.989 133.588 1.00 120.33 ? 565  PHE B CG    1 
ATOM   10008 C  CD1   . PHE B 1 565 ? 182.545 158.930 133.686 1.00 119.31 ? 565  PHE B CD1   1 
ATOM   10009 C  CD2   . PHE B 1 565 ? 184.004 157.626 132.331 1.00 123.87 ? 565  PHE B CD2   1 
ATOM   10010 C  CE1   . PHE B 1 565 ? 181.997 159.497 132.556 1.00 124.37 ? 565  PHE B CE1   1 
ATOM   10011 C  CE2   . PHE B 1 565 ? 183.457 158.188 131.196 1.00 122.51 ? 565  PHE B CE2   1 
ATOM   10012 C  CZ    . PHE B 1 565 ? 182.451 159.124 131.310 1.00 125.27 ? 565  PHE B CZ    1 
ATOM   10013 N  N     . VAL B 1 566 ? 183.890 154.206 134.597 1.00 115.11 ? 566  VAL B N     1 
ATOM   10014 C  CA    . VAL B 1 566 ? 183.678 152.982 133.833 1.00 112.09 ? 566  VAL B CA    1 
ATOM   10015 C  C     . VAL B 1 566 ? 182.451 152.242 134.345 1.00 113.02 ? 566  VAL B C     1 
ATOM   10016 O  O     . VAL B 1 566 ? 181.651 151.720 133.561 1.00 118.67 ? 566  VAL B O     1 
ATOM   10017 C  CB    . VAL B 1 566 ? 184.934 152.096 133.887 1.00 113.42 ? 566  VAL B CB    1 
ATOM   10018 C  CG1   . VAL B 1 566 ? 184.845 150.994 132.848 1.00 120.22 ? 566  VAL B CG1   1 
ATOM   10019 C  CG2   . VAL B 1 566 ? 186.181 152.935 133.678 1.00 117.63 ? 566  VAL B CG2   1 
ATOM   10020 N  N     . ARG B 1 567 ? 182.288 152.178 135.668 1.00 110.45 ? 567  ARG B N     1 
ATOM   10021 C  CA    . ARG B 1 567 ? 181.119 151.515 136.236 1.00 111.97 ? 567  ARG B CA    1 
ATOM   10022 C  C     . ARG B 1 567 ? 179.835 152.240 135.860 1.00 111.38 ? 567  ARG B C     1 
ATOM   10023 O  O     . ARG B 1 567 ? 178.817 151.602 135.576 1.00 114.92 ? 567  ARG B O     1 
ATOM   10024 C  CB    . ARG B 1 567 ? 181.251 151.418 137.754 1.00 116.75 ? 567  ARG B CB    1 
ATOM   10025 C  CG    . ARG B 1 567 ? 182.004 150.190 138.221 1.00 120.30 ? 567  ARG B CG    1 
ATOM   10026 C  CD    . ARG B 1 567 ? 181.170 148.941 138.029 1.00 112.08 ? 567  ARG B CD    1 
ATOM   10027 N  NE    . ARG B 1 567 ? 181.899 147.740 138.413 1.00 114.60 ? 567  ARG B NE    1 
ATOM   10028 C  CZ    . ARG B 1 567 ? 181.419 146.510 138.303 1.00 118.17 ? 567  ARG B CZ    1 
ATOM   10029 N  NH1   . ARG B 1 567 ? 180.205 146.283 137.834 1.00 113.89 ? 567  ARG B NH1   1 
ATOM   10030 N  NH2   . ARG B 1 567 ? 182.177 145.483 138.674 1.00 124.02 ? 567  ARG B NH2   1 
ATOM   10031 N  N     . LYS B 1 568 ? 179.860 153.573 135.858 1.00 110.87 ? 568  LYS B N     1 
ATOM   10032 C  CA    . LYS B 1 568 ? 178.676 154.333 135.468 1.00 110.93 ? 568  LYS B CA    1 
ATOM   10033 C  C     . LYS B 1 568 ? 178.307 154.071 134.013 1.00 113.12 ? 568  LYS B C     1 
ATOM   10034 O  O     . LYS B 1 568 ? 177.128 153.892 133.688 1.00 113.07 ? 568  LYS B O     1 
ATOM   10035 C  CB    . LYS B 1 568 ? 178.907 155.824 135.703 1.00 112.42 ? 568  LYS B CB    1 
ATOM   10036 C  CG    . LYS B 1 568 ? 179.220 156.191 137.143 1.00 114.85 ? 568  LYS B CG    1 
ATOM   10037 C  CD    . LYS B 1 568 ? 178.015 156.796 137.838 1.00 114.51 ? 568  LYS B CD    1 
ATOM   10038 C  CE    . LYS B 1 568 ? 178.390 157.371 139.191 1.00 111.70 ? 568  LYS B CE    1 
ATOM   10039 N  NZ    . LYS B 1 568 ? 178.549 158.849 139.144 1.00 105.39 ? 568  LYS B NZ    1 
ATOM   10040 N  N     . MET B 1 569 ? 179.300 154.047 133.121 1.00 112.65 ? 569  MET B N     1 
ATOM   10041 C  CA    . MET B 1 569 ? 179.014 153.758 131.717 1.00 111.59 ? 569  MET B CA    1 
ATOM   10042 C  C     . MET B 1 569 ? 178.506 152.333 131.528 1.00 108.13 ? 569  MET B C     1 
ATOM   10043 O  O     . MET B 1 569 ? 177.585 152.094 130.735 1.00 111.64 ? 569  MET B O     1 
ATOM   10044 C  CB    . MET B 1 569 ? 180.254 154.018 130.866 1.00 112.94 ? 569  MET B CB    1 
ATOM   10045 C  CG    . MET B 1 569 ? 180.505 155.494 130.635 1.00 119.49 ? 569  MET B CG    1 
ATOM   10046 S  SD    . MET B 1 569 ? 178.958 156.421 130.690 1.00 139.03 ? 569  MET B SD    1 
ATOM   10047 C  CE    . MET B 1 569 ? 179.240 157.500 132.086 1.00 121.27 ? 569  MET B CE    1 
ATOM   10048 N  N     . ALA B 1 570 ? 179.093 151.370 132.242 1.00 104.04 ? 570  ALA B N     1 
ATOM   10049 C  CA    . ALA B 1 570 ? 178.603 149.999 132.162 1.00 101.87 ? 570  ALA B CA    1 
ATOM   10050 C  C     . ALA B 1 570 ? 177.166 149.907 132.655 1.00 103.77 ? 570  ALA B C     1 
ATOM   10051 O  O     . ALA B 1 570 ? 176.343 149.191 132.072 1.00 107.41 ? 570  ALA B O     1 
ATOM   10052 C  CB    . ALA B 1 570 ? 179.508 149.066 132.964 1.00 102.90 ? 570  ALA B CB    1 
ATOM   10053 N  N     . PHE B 1 571 ? 176.846 150.633 133.726 1.00 104.49 ? 571  PHE B N     1 
ATOM   10054 C  CA    . PHE B 1 571 ? 175.483 150.641 134.239 1.00 103.11 ? 571  PHE B CA    1 
ATOM   10055 C  C     . PHE B 1 571 ? 174.524 151.280 133.246 1.00 105.23 ? 571  PHE B C     1 
ATOM   10056 O  O     . PHE B 1 571 ? 173.380 150.843 133.116 1.00 104.52 ? 571  PHE B O     1 
ATOM   10057 C  CB    . PHE B 1 571 ? 175.438 151.368 135.579 1.00 105.59 ? 571  PHE B CB    1 
ATOM   10058 C  CG    . PHE B 1 571 ? 175.652 150.469 136.757 1.00 104.20 ? 571  PHE B CG    1 
ATOM   10059 C  CD1   . PHE B 1 571 ? 175.237 149.153 136.718 1.00 98.71  ? 571  PHE B CD1   1 
ATOM   10060 C  CD2   . PHE B 1 571 ? 176.287 150.932 137.892 1.00 112.82 ? 571  PHE B CD2   1 
ATOM   10061 C  CE1   . PHE B 1 571 ? 175.436 148.324 137.795 1.00 105.02 ? 571  PHE B CE1   1 
ATOM   10062 C  CE2   . PHE B 1 571 ? 176.490 150.104 138.972 1.00 111.34 ? 571  PHE B CE2   1 
ATOM   10063 C  CZ    . PHE B 1 571 ? 176.065 148.798 138.923 1.00 110.45 ? 571  PHE B CZ    1 
ATOM   10064 N  N     . LEU B 1 572 ? 174.968 152.323 132.541 1.00 106.00 ? 572  LEU B N     1 
ATOM   10065 C  CA    . LEU B 1 572 ? 174.117 152.936 131.523 1.00 104.66 ? 572  LEU B CA    1 
ATOM   10066 C  C     . LEU B 1 572 ? 173.843 151.971 130.375 1.00 101.19 ? 572  LEU B C     1 
ATOM   10067 O  O     . LEU B 1 572 ? 172.706 151.868 129.891 1.00 103.25 ? 572  LEU B O     1 
ATOM   10068 C  CB    . LEU B 1 572 ? 174.765 154.217 131.004 1.00 104.64 ? 572  LEU B CB    1 
ATOM   10069 C  CG    . LEU B 1 572 ? 173.879 155.139 130.169 1.00 102.73 ? 572  LEU B CG    1 
ATOM   10070 C  CD1   . LEU B 1 572 ? 172.495 155.246 130.781 1.00 96.98  ? 572  LEU B CD1   1 
ATOM   10071 C  CD2   . LEU B 1 572 ? 174.517 156.509 130.045 1.00 109.49 ? 572  LEU B CD2   1 
ATOM   10072 N  N     . VAL B 1 573 ? 174.876 151.255 129.927 1.00 97.51  ? 573  VAL B N     1 
ATOM   10073 C  CA    . VAL B 1 573 ? 174.690 150.264 128.868 1.00 93.23  ? 573  VAL B CA    1 
ATOM   10074 C  C     . VAL B 1 573 ? 173.722 149.181 129.327 1.00 97.40  ? 573  VAL B C     1 
ATOM   10075 O  O     . VAL B 1 573 ? 172.809 148.776 128.591 1.00 100.97 ? 573  VAL B O     1 
ATOM   10076 C  CB    . VAL B 1 573 ? 176.045 149.668 128.448 1.00 90.72  ? 573  VAL B CB    1 
ATOM   10077 C  CG1   . VAL B 1 573 ? 175.838 148.469 127.543 1.00 92.42  ? 573  VAL B CG1   1 
ATOM   10078 C  CG2   . VAL B 1 573 ? 176.893 150.719 127.760 1.00 95.99  ? 573  VAL B CG2   1 
ATOM   10079 N  N     . PHE B 1 574 ? 173.899 148.703 130.561 1.00 100.79 ? 574  PHE B N     1 
ATOM   10080 C  CA    . PHE B 1 574 ? 172.995 147.686 131.078 1.00 99.43  ? 574  PHE B CA    1 
ATOM   10081 C  C     . PHE B 1 574 ? 171.586 148.226 131.242 1.00 98.55  ? 574  PHE B C     1 
ATOM   10082 O  O     . PHE B 1 574 ? 170.624 147.474 131.107 1.00 99.51  ? 574  PHE B O     1 
ATOM   10083 C  CB    . PHE B 1 574 ? 173.493 147.138 132.411 1.00 100.11 ? 574  PHE B CB    1 
ATOM   10084 C  CG    . PHE B 1 574 ? 172.532 146.185 133.059 1.00 96.72  ? 574  PHE B CG    1 
ATOM   10085 C  CD1   . PHE B 1 574 ? 172.462 144.870 132.641 1.00 101.24 ? 574  PHE B CD1   1 
ATOM   10086 C  CD2   . PHE B 1 574 ? 171.693 146.603 134.071 1.00 96.94  ? 574  PHE B CD2   1 
ATOM   10087 C  CE1   . PHE B 1 574 ? 171.579 143.991 133.225 1.00 103.83 ? 574  PHE B CE1   1 
ATOM   10088 C  CE2   . PHE B 1 574 ? 170.807 145.728 134.657 1.00 97.84  ? 574  PHE B CE2   1 
ATOM   10089 C  CZ    . PHE B 1 574 ? 170.751 144.421 134.234 1.00 101.37 ? 574  PHE B CZ    1 
ATOM   10090 N  N     . TYR B 1 575 ? 171.440 149.513 131.551 1.00 98.50  ? 575  TYR B N     1 
ATOM   10091 C  CA    . TYR B 1 575 ? 170.106 150.089 131.674 1.00 100.51 ? 575  TYR B CA    1 
ATOM   10092 C  C     . TYR B 1 575 ? 169.409 150.141 130.326 1.00 101.83 ? 575  TYR B C     1 
ATOM   10093 O  O     . TYR B 1 575 ? 168.206 149.872 130.232 1.00 104.15 ? 575  TYR B O     1 
ATOM   10094 C  CB    . TYR B 1 575 ? 170.188 151.483 132.288 1.00 101.03 ? 575  TYR B CB    1 
ATOM   10095 C  CG    . TYR B 1 575 ? 168.861 152.197 132.352 1.00 103.34 ? 575  TYR B CG    1 
ATOM   10096 C  CD1   . TYR B 1 575 ? 167.850 151.741 133.183 1.00 108.07 ? 575  TYR B CD1   1 
ATOM   10097 C  CD2   . TYR B 1 575 ? 168.622 153.330 131.592 1.00 105.27 ? 575  TYR B CD2   1 
ATOM   10098 C  CE1   . TYR B 1 575 ? 166.637 152.390 133.250 1.00 110.59 ? 575  TYR B CE1   1 
ATOM   10099 C  CE2   . TYR B 1 575 ? 167.412 153.986 131.654 1.00 110.80 ? 575  TYR B CE2   1 
ATOM   10100 C  CZ    . TYR B 1 575 ? 166.423 153.511 132.485 1.00 111.49 ? 575  TYR B CZ    1 
ATOM   10101 O  OH    . TYR B 1 575 ? 165.213 154.159 132.553 1.00 116.31 ? 575  TYR B OH    1 
ATOM   10102 N  N     . VAL B 1 576 ? 170.148 150.482 129.269 1.00 101.51 ? 576  VAL B N     1 
ATOM   10103 C  CA    . VAL B 1 576 ? 169.572 150.442 127.926 1.00 98.07  ? 576  VAL B CA    1 
ATOM   10104 C  C     . VAL B 1 576 ? 169.139 149.021 127.583 1.00 98.80  ? 576  VAL B C     1 
ATOM   10105 O  O     . VAL B 1 576 ? 168.024 148.787 127.088 1.00 100.33 ? 576  VAL B O     1 
ATOM   10106 C  CB    . VAL B 1 576 ? 170.573 150.991 126.895 1.00 95.08  ? 576  VAL B CB    1 
ATOM   10107 C  CG1   . VAL B 1 576 ? 170.201 150.531 125.499 1.00 88.84  ? 576  VAL B CG1   1 
ATOM   10108 C  CG2   . VAL B 1 576 ? 170.620 152.506 126.964 1.00 101.51 ? 576  VAL B CG2   1 
ATOM   10109 N  N     . TYR B 1 577 ? 170.010 148.046 127.860 1.00 101.28 ? 577  TYR B N     1 
ATOM   10110 C  CA    . TYR B 1 577 ? 169.657 146.655 127.589 1.00 99.88  ? 577  TYR B CA    1 
ATOM   10111 C  C     . TYR B 1 577 ? 168.447 146.221 128.404 1.00 100.03 ? 577  TYR B C     1 
ATOM   10112 O  O     . TYR B 1 577 ? 167.585 145.493 127.906 1.00 103.31 ? 577  TYR B O     1 
ATOM   10113 C  CB    . TYR B 1 577 ? 170.835 145.729 127.880 1.00 97.61  ? 577  TYR B CB    1 
ATOM   10114 C  CG    . TYR B 1 577 ? 170.400 144.296 128.081 1.00 96.60  ? 577  TYR B CG    1 
ATOM   10115 C  CD1   . TYR B 1 577 ? 170.120 143.480 126.998 1.00 100.47 ? 577  TYR B CD1   1 
ATOM   10116 C  CD2   . TYR B 1 577 ? 170.251 143.767 129.355 1.00 95.06  ? 577  TYR B CD2   1 
ATOM   10117 C  CE1   . TYR B 1 577 ? 169.714 142.175 127.175 1.00 101.20 ? 577  TYR B CE1   1 
ATOM   10118 C  CE2   . TYR B 1 577 ? 169.841 142.466 129.541 1.00 91.77  ? 577  TYR B CE2   1 
ATOM   10119 C  CZ    . TYR B 1 577 ? 169.577 141.674 128.449 1.00 97.55  ? 577  TYR B CZ    1 
ATOM   10120 O  OH    . TYR B 1 577 ? 169.173 140.373 128.633 1.00 104.05 ? 577  TYR B OH    1 
ATOM   10121 N  N     . HIS B 1 578 ? 168.387 146.632 129.670 1.00 96.42  ? 578  HIS B N     1 
ATOM   10122 C  CA    . HIS B 1 578 ? 167.286 146.248 130.542 1.00 94.61  ? 578  HIS B CA    1 
ATOM   10123 C  C     . HIS B 1 578 ? 165.976 146.844 130.058 1.00 101.66 ? 578  HIS B C     1 
ATOM   10124 O  O     . HIS B 1 578 ? 164.936 146.179 130.086 1.00 103.01 ? 578  HIS B O     1 
ATOM   10125 C  CB    . HIS B 1 578 ? 167.589 146.693 131.971 1.00 95.99  ? 578  HIS B CB    1 
ATOM   10126 C  CG    . HIS B 1 578 ? 166.708 146.066 133.004 1.00 100.59 ? 578  HIS B CG    1 
ATOM   10127 N  ND1   . HIS B 1 578 ? 166.387 144.726 132.994 1.00 107.31 ? 578  HIS B ND1   1 
ATOM   10128 C  CD2   . HIS B 1 578 ? 166.097 146.592 134.091 1.00 104.65 ? 578  HIS B CD2   1 
ATOM   10129 C  CE1   . HIS B 1 578 ? 165.607 144.456 134.025 1.00 113.01 ? 578  HIS B CE1   1 
ATOM   10130 N  NE2   . HIS B 1 578 ? 165.416 145.570 134.707 1.00 113.98 ? 578  HIS B NE2   1 
ATOM   10131 N  N     . LEU B 1 579 ? 166.006 148.100 129.610 1.00 105.78 ? 579  LEU B N     1 
ATOM   10132 C  CA    . LEU B 1 579 ? 164.810 148.714 129.047 1.00 103.34 ? 579  LEU B CA    1 
ATOM   10133 C  C     . LEU B 1 579 ? 164.334 147.948 127.822 1.00 102.96 ? 579  LEU B C     1 
ATOM   10134 O  O     . LEU B 1 579 ? 163.144 147.633 127.697 1.00 106.14 ? 579  LEU B O     1 
ATOM   10135 C  CB    . LEU B 1 579 ? 165.090 150.173 128.694 1.00 101.47 ? 579  LEU B CB    1 
ATOM   10136 C  CG    . LEU B 1 579 ? 164.641 151.208 129.720 1.00 103.41 ? 579  LEU B CG    1 
ATOM   10137 C  CD1   . LEU B 1 579 ? 164.908 152.611 129.210 1.00 108.47 ? 579  LEU B CD1   1 
ATOM   10138 C  CD2   . LEU B 1 579 ? 163.171 151.020 130.032 1.00 102.20 ? 579  LEU B CD2   1 
ATOM   10139 N  N     . LEU B 1 580 ? 165.256 147.619 126.911 1.00 100.84 ? 580  LEU B N     1 
ATOM   10140 C  CA    . LEU B 1 580 ? 164.861 146.877 125.716 1.00 99.59  ? 580  LEU B CA    1 
ATOM   10141 C  C     . LEU B 1 580 ? 164.309 145.501 126.073 1.00 100.92 ? 580  LEU B C     1 
ATOM   10142 O  O     . LEU B 1 580 ? 163.284 145.072 125.528 1.00 105.14 ? 580  LEU B O     1 
ATOM   10143 C  CB    . LEU B 1 580 ? 166.044 146.744 124.761 1.00 100.76 ? 580  LEU B CB    1 
ATOM   10144 C  CG    . LEU B 1 580 ? 166.519 148.031 124.088 1.00 114.61 ? 580  LEU B CG    1 
ATOM   10145 C  CD1   . LEU B 1 580 ? 167.464 147.708 122.946 1.00 121.16 ? 580  LEU B CD1   1 
ATOM   10146 C  CD2   . LEU B 1 580 ? 165.336 148.843 123.594 1.00 114.62 ? 580  LEU B CD2   1 
ATOM   10147 N  N     . TYR B 1 581 ? 164.971 144.799 126.993 1.00 100.92 ? 581  TYR B N     1 
ATOM   10148 C  CA    . TYR B 1 581 ? 164.545 143.455 127.365 1.00 101.26 ? 581  TYR B CA    1 
ATOM   10149 C  C     . TYR B 1 581 ? 163.185 143.474 128.045 1.00 102.83 ? 581  TYR B C     1 
ATOM   10150 O  O     . TYR B 1 581 ? 162.337 142.618 127.774 1.00 108.88 ? 581  TYR B O     1 
ATOM   10151 C  CB    . TYR B 1 581 ? 165.592 142.815 128.274 1.00 102.53 ? 581  TYR B CB    1 
ATOM   10152 C  CG    . TYR B 1 581 ? 165.269 141.403 128.695 1.00 101.16 ? 581  TYR B CG    1 
ATOM   10153 C  CD1   . TYR B 1 581 ? 165.478 140.338 127.834 1.00 102.83 ? 581  TYR B CD1   1 
ATOM   10154 C  CD2   . TYR B 1 581 ? 164.764 141.134 129.958 1.00 102.86 ? 581  TYR B CD2   1 
ATOM   10155 C  CE1   . TYR B 1 581 ? 165.189 139.046 128.215 1.00 108.46 ? 581  TYR B CE1   1 
ATOM   10156 C  CE2   . TYR B 1 581 ? 164.472 139.844 130.348 1.00 105.96 ? 581  TYR B CE2   1 
ATOM   10157 C  CZ    . TYR B 1 581 ? 164.686 138.805 129.472 1.00 108.58 ? 581  TYR B CZ    1 
ATOM   10158 O  OH    . TYR B 1 581 ? 164.396 137.517 129.856 1.00 112.24 ? 581  TYR B OH    1 
ATOM   10159 N  N     . THR B 1 582 ? 162.958 144.440 128.936 1.00 99.07  ? 582  THR B N     1 
ATOM   10160 C  CA    . THR B 1 582 ? 161.669 144.538 129.609 1.00 98.31  ? 582  THR B CA    1 
ATOM   10161 C  C     . THR B 1 582 ? 160.566 144.907 128.628 1.00 101.40 ? 582  THR B C     1 
ATOM   10162 O  O     . THR B 1 582 ? 159.454 144.372 128.704 1.00 102.63 ? 582  THR B O     1 
ATOM   10163 C  CB    . THR B 1 582 ? 161.755 145.560 130.741 1.00 98.69  ? 582  THR B CB    1 
ATOM   10164 O  OG1   . THR B 1 582 ? 162.464 144.980 131.839 1.00 107.22 ? 582  THR B OG1   1 
ATOM   10165 C  CG2   . THR B 1 582 ? 160.369 145.964 131.210 1.00 94.82  ? 582  THR B CG2   1 
ATOM   10166 N  N     . ALA B 1 583 ? 160.856 145.811 127.688 1.00 100.49 ? 583  ALA B N     1 
ATOM   10167 C  CA    . ALA B 1 583 ? 159.867 146.149 126.672 1.00 96.69  ? 583  ALA B CA    1 
ATOM   10168 C  C     . ALA B 1 583 ? 159.512 144.934 125.829 1.00 99.65  ? 583  ALA B C     1 
ATOM   10169 O  O     . ALA B 1 583 ? 158.338 144.711 125.513 1.00 104.37 ? 583  ALA B O     1 
ATOM   10170 C  CB    . ALA B 1 583 ? 160.384 147.285 125.790 1.00 94.58  ? 583  ALA B CB    1 
ATOM   10171 N  N     . PHE B 1 584 ? 160.512 144.135 125.452 1.00 100.06 ? 584  PHE B N     1 
ATOM   10172 C  CA    . PHE B 1 584 ? 160.231 142.927 124.683 1.00 99.51  ? 584  PHE B CA    1 
ATOM   10173 C  C     . PHE B 1 584 ? 159.422 141.927 125.499 1.00 98.21  ? 584  PHE B C     1 
ATOM   10174 O  O     . PHE B 1 584 ? 158.485 141.309 124.984 1.00 103.54 ? 584  PHE B O     1 
ATOM   10175 C  CB    . PHE B 1 584 ? 161.531 142.288 124.199 1.00 98.62  ? 584  PHE B CB    1 
ATOM   10176 C  CG    . PHE B 1 584 ? 161.332 140.978 123.494 1.00 98.34  ? 584  PHE B CG    1 
ATOM   10177 C  CD1   . PHE B 1 584 ? 160.936 140.946 122.170 1.00 102.22 ? 584  PHE B CD1   1 
ATOM   10178 C  CD2   . PHE B 1 584 ? 161.541 139.781 124.153 1.00 98.45  ? 584  PHE B CD2   1 
ATOM   10179 C  CE1   . PHE B 1 584 ? 160.751 139.746 121.518 1.00 105.43 ? 584  PHE B CE1   1 
ATOM   10180 C  CE2   . PHE B 1 584 ? 161.357 138.578 123.505 1.00 101.91 ? 584  PHE B CE2   1 
ATOM   10181 C  CZ    . PHE B 1 584 ? 160.962 138.561 122.186 1.00 102.14 ? 584  PHE B CZ    1 
ATOM   10182 N  N     . GLY B 1 585 ? 159.771 141.753 126.775 1.00 96.39  ? 585  GLY B N     1 
ATOM   10183 C  CA    . GLY B 1 585 ? 159.055 140.802 127.605 1.00 98.11  ? 585  GLY B CA    1 
ATOM   10184 C  C     . GLY B 1 585 ? 157.638 141.231 127.920 1.00 100.69 ? 585  GLY B C     1 
ATOM   10185 O  O     . GLY B 1 585 ? 156.783 140.391 128.216 1.00 101.99 ? 585  GLY B O     1 
ATOM   10186 N  N     . PHE B 1 586 ? 157.368 142.536 127.876 1.00 102.00 ? 586  PHE B N     1 
ATOM   10187 C  CA    . PHE B 1 586 ? 156.008 143.013 128.098 1.00 102.79 ? 586  PHE B CA    1 
ATOM   10188 C  C     . PHE B 1 586 ? 155.084 142.572 126.971 1.00 102.04 ? 586  PHE B C     1 
ATOM   10189 O  O     . PHE B 1 586 ? 153.937 142.180 127.214 1.00 101.86 ? 586  PHE B O     1 
ATOM   10190 C  CB    . PHE B 1 586 ? 156.003 144.533 128.237 1.00 102.17 ? 586  PHE B CB    1 
ATOM   10191 C  CG    . PHE B 1 586 ? 154.675 145.103 128.633 1.00 102.05 ? 586  PHE B CG    1 
ATOM   10192 C  CD1   . PHE B 1 586 ? 154.209 144.966 129.926 1.00 103.13 ? 586  PHE B CD1   1 
ATOM   10193 C  CD2   . PHE B 1 586 ? 153.896 145.781 127.715 1.00 102.57 ? 586  PHE B CD2   1 
ATOM   10194 C  CE1   . PHE B 1 586 ? 152.990 145.491 130.295 1.00 105.62 ? 586  PHE B CE1   1 
ATOM   10195 C  CE2   . PHE B 1 586 ? 152.676 146.308 128.079 1.00 104.17 ? 586  PHE B CE2   1 
ATOM   10196 C  CZ    . PHE B 1 586 ? 152.223 146.163 129.370 1.00 104.31 ? 586  PHE B CZ    1 
ATOM   10197 N  N     . PHE B 1 587 ? 155.565 142.628 125.730 1.00 99.27  ? 587  PHE B N     1 
ATOM   10198 C  CA    . PHE B 1 587 ? 154.812 142.192 124.557 1.00 95.81  ? 587  PHE B CA    1 
ATOM   10199 C  C     . PHE B 1 587 ? 155.122 140.748 124.194 1.00 96.85  ? 587  PHE B C     1 
ATOM   10200 O  O     . PHE B 1 587 ? 155.005 140.354 123.032 1.00 98.38  ? 587  PHE B O     1 
ATOM   10201 C  CB    . PHE B 1 587 ? 155.097 143.107 123.371 1.00 93.00  ? 587  PHE B CB    1 
ATOM   10202 C  CG    . PHE B 1 587 ? 154.680 144.529 123.587 1.00 94.98  ? 587  PHE B CG    1 
ATOM   10203 C  CD1   . PHE B 1 587 ? 153.373 144.921 123.372 1.00 101.03 ? 587  PHE B CD1   1 
ATOM   10204 C  CD2   . PHE B 1 587 ? 155.598 145.477 123.998 1.00 96.17  ? 587  PHE B CD2   1 
ATOM   10205 C  CE1   . PHE B 1 587 ? 152.989 146.229 123.569 1.00 105.44 ? 587  PHE B CE1   1 
ATOM   10206 C  CE2   . PHE B 1 587 ? 155.219 146.786 124.195 1.00 100.14 ? 587  PHE B CE2   1 
ATOM   10207 C  CZ    . PHE B 1 587 ? 153.913 147.162 123.980 1.00 104.79 ? 587  PHE B CZ    1 
ATOM   10208 N  N     . LEU B 1 588 ? 155.540 139.945 125.166 1.00 96.07  ? 588  LEU B N     1 
ATOM   10209 C  CA    . LEU B 1 588 ? 155.900 138.555 124.915 1.00 95.20  ? 588  LEU B CA    1 
ATOM   10210 C  C     . LEU B 1 588 ? 154.723 137.714 124.425 1.00 97.96  ? 588  LEU B C     1 
ATOM   10211 O  O     . LEU B 1 588 ? 154.901 136.935 123.482 1.00 102.36 ? 588  LEU B O     1 
ATOM   10212 C  CB    . LEU B 1 588 ? 156.515 137.924 126.165 1.00 97.23  ? 588  LEU B CB    1 
ATOM   10213 C  CG    . LEU B 1 588 ? 157.337 136.664 125.901 1.00 98.19  ? 588  LEU B CG    1 
ATOM   10214 C  CD1   . LEU B 1 588 ? 158.278 136.882 124.733 1.00 96.79  ? 588  LEU B CD1   1 
ATOM   10215 C  CD2   . LEU B 1 588 ? 158.109 136.267 127.145 1.00 104.25 ? 588  LEU B CD2   1 
ATOM   10216 N  N     . PRO B 1 589 ? 153.529 137.793 125.031 1.00 96.86  ? 589  PRO B N     1 
ATOM   10217 C  CA    . PRO B 1 589 ? 152.409 137.007 124.482 1.00 92.75  ? 589  PRO B CA    1 
ATOM   10218 C  C     . PRO B 1 589 ? 152.062 137.377 123.053 1.00 94.33  ? 589  PRO B C     1 
ATOM   10219 O  O     . PRO B 1 589 ? 151.844 136.489 122.218 1.00 95.67  ? 589  PRO B O     1 
ATOM   10220 C  CB    . PRO B 1 589 ? 151.256 137.321 125.444 1.00 90.84  ? 589  PRO B CB    1 
ATOM   10221 C  CG    . PRO B 1 589 ? 151.913 137.717 126.698 1.00 96.39  ? 589  PRO B CG    1 
ATOM   10222 C  CD    . PRO B 1 589 ? 153.146 138.454 126.292 1.00 98.19  ? 589  PRO B CD    1 
ATOM   10223 N  N     . ALA B 1 590 ? 152.011 138.675 122.748 1.00 94.05  ? 590  ALA B N     1 
ATOM   10224 C  CA    . ALA B 1 590 ? 151.710 139.101 121.387 1.00 91.19  ? 590  ALA B CA    1 
ATOM   10225 C  C     . ALA B 1 590 ? 152.783 138.634 120.416 1.00 95.08  ? 590  ALA B C     1 
ATOM   10226 O  O     . ALA B 1 590 ? 152.470 138.156 119.321 1.00 101.82 ? 590  ALA B O     1 
ATOM   10227 C  CB    . ALA B 1 590 ? 151.561 140.619 121.332 1.00 92.79  ? 590  ALA B CB    1 
ATOM   10228 N  N     . ASN B 1 591 ? 154.055 138.758 120.801 1.00 95.49  ? 591  ASN B N     1 
ATOM   10229 C  CA    . ASN B 1 591 ? 155.135 138.324 119.922 1.00 94.47  ? 591  ASN B CA    1 
ATOM   10230 C  C     . ASN B 1 591 ? 155.102 136.818 119.700 1.00 94.27  ? 591  ASN B C     1 
ATOM   10231 O  O     . ASN B 1 591 ? 155.343 136.350 118.585 1.00 99.41  ? 591  ASN B O     1 
ATOM   10232 C  CB    . ASN B 1 591 ? 156.484 138.754 120.491 1.00 95.50  ? 591  ASN B CB    1 
ATOM   10233 C  CG    . ASN B 1 591 ? 156.780 140.212 120.234 1.00 102.28 ? 591  ASN B CG    1 
ATOM   10234 O  OD1   . ASN B 1 591 ? 156.311 140.787 119.254 1.00 102.27 ? 591  ASN B OD1   1 
ATOM   10235 N  ND2   . ASN B 1 591 ? 157.563 140.821 121.114 1.00 103.83 ? 591  ASN B ND2   1 
ATOM   10236 N  N     . LEU B 1 592 ? 154.810 136.043 120.746 1.00 93.59  ? 592  LEU B N     1 
ATOM   10237 C  CA    . LEU B 1 592 ? 154.721 134.596 120.589 1.00 91.73  ? 592  LEU B CA    1 
ATOM   10238 C  C     . LEU B 1 592 ? 153.575 134.217 119.662 1.00 95.41  ? 592  LEU B C     1 
ATOM   10239 O  O     . LEU B 1 592 ? 153.731 133.365 118.776 1.00 100.40 ? 592  LEU B O     1 
ATOM   10240 C  CB    . LEU B 1 592 ? 154.546 133.929 121.952 1.00 92.29  ? 592  LEU B CB    1 
ATOM   10241 C  CG    . LEU B 1 592 ? 154.213 132.439 121.916 1.00 87.32  ? 592  LEU B CG    1 
ATOM   10242 C  CD1   . LEU B 1 592 ? 155.402 131.639 121.426 1.00 91.10  ? 592  LEU B CD1   1 
ATOM   10243 C  CD2   . LEU B 1 592 ? 153.770 131.959 123.283 1.00 96.62  ? 592  LEU B CD2   1 
ATOM   10244 N  N     . TYR B 1 593 ? 152.411 134.842 119.851 1.00 95.90  ? 593  TYR B N     1 
ATOM   10245 C  CA    . TYR B 1 593 ? 151.278 134.554 118.981 1.00 97.26  ? 593  TYR B CA    1 
ATOM   10246 C  C     . TYR B 1 593 ? 151.601 134.908 117.539 1.00 97.18  ? 593  TYR B C     1 
ATOM   10247 O  O     . TYR B 1 593 ? 151.309 134.138 116.620 1.00 101.73 ? 593  TYR B O     1 
ATOM   10248 C  CB    . TYR B 1 593 ? 150.037 135.310 119.448 1.00 98.93  ? 593  TYR B CB    1 
ATOM   10249 C  CG    . TYR B 1 593 ? 148.974 135.420 118.380 1.00 102.82 ? 593  TYR B CG    1 
ATOM   10250 C  CD1   . TYR B 1 593 ? 148.146 134.348 118.088 1.00 105.21 ? 593  TYR B CD1   1 
ATOM   10251 C  CD2   . TYR B 1 593 ? 148.798 136.593 117.664 1.00 105.58 ? 593  TYR B CD2   1 
ATOM   10252 C  CE1   . TYR B 1 593 ? 147.176 134.440 117.114 1.00 108.35 ? 593  TYR B CE1   1 
ATOM   10253 C  CE2   . TYR B 1 593 ? 147.831 136.694 116.688 1.00 107.42 ? 593  TYR B CE2   1 
ATOM   10254 C  CZ    . TYR B 1 593 ? 147.023 135.615 116.418 1.00 111.08 ? 593  TYR B CZ    1 
ATOM   10255 O  OH    . TYR B 1 593 ? 146.056 135.710 115.447 1.00 114.14 ? 593  TYR B OH    1 
ATOM   10256 N  N     . LEU B 1 594 ? 152.213 136.074 117.321 1.00 96.46  ? 594  LEU B N     1 
ATOM   10257 C  CA    . LEU B 1 594 ? 152.546 136.489 115.964 1.00 97.01  ? 594  LEU B CA    1 
ATOM   10258 C  C     . LEU B 1 594 ? 153.566 135.553 115.333 1.00 101.23 ? 594  LEU B C     1 
ATOM   10259 O  O     . LEU B 1 594 ? 153.438 135.190 114.161 1.00 106.34 ? 594  LEU B O     1 
ATOM   10260 C  CB    . LEU B 1 594 ? 153.066 137.923 115.966 1.00 95.20  ? 594  LEU B CB    1 
ATOM   10261 C  CG    . LEU B 1 594 ? 152.017 138.981 116.290 1.00 99.34  ? 594  LEU B CG    1 
ATOM   10262 C  CD1   . LEU B 1 594 ? 152.680 140.315 116.555 1.00 100.98 ? 594  LEU B CD1   1 
ATOM   10263 C  CD2   . LEU B 1 594 ? 151.019 139.087 115.164 1.00 98.32  ? 594  LEU B CD2   1 
ATOM   10264 N  N     . ALA B 1 595 ? 154.583 135.146 116.094 1.00 97.45  ? 595  ALA B N     1 
ATOM   10265 C  CA    . ALA B 1 595 ? 155.602 134.256 115.550 1.00 95.04  ? 595  ALA B CA    1 
ATOM   10266 C  C     . ALA B 1 595 ? 155.000 132.918 115.150 1.00 99.65  ? 595  ALA B C     1 
ATOM   10267 O  O     . ALA B 1 595 ? 155.210 132.440 114.027 1.00 107.28 ? 595  ALA B O     1 
ATOM   10268 C  CB    . ALA B 1 595 ? 156.724 134.061 116.568 1.00 94.31  ? 595  ALA B CB    1 
ATOM   10269 N  N     . LEU B 1 596 ? 154.238 132.299 116.057 1.00 96.23  ? 596  LEU B N     1 
ATOM   10270 C  CA    . LEU B 1 596 ? 153.601 131.028 115.729 1.00 98.42  ? 596  LEU B CA    1 
ATOM   10271 C  C     . LEU B 1 596 ? 152.683 131.179 114.526 1.00 105.12 ? 596  LEU B C     1 
ATOM   10272 O  O     . LEU B 1 596 ? 152.805 130.441 113.538 1.00 111.46 ? 596  LEU B O     1 
ATOM   10273 C  CB    . LEU B 1 596 ? 152.820 130.501 116.931 1.00 96.57  ? 596  LEU B CB    1 
ATOM   10274 C  CG    . LEU B 1 596 ? 153.637 130.023 118.127 1.00 103.07 ? 596  LEU B CG    1 
ATOM   10275 C  CD1   . LEU B 1 596 ? 152.738 129.332 119.136 1.00 105.58 ? 596  LEU B CD1   1 
ATOM   10276 C  CD2   . LEU B 1 596 ? 154.747 129.102 117.671 1.00 101.45 ? 596  LEU B CD2   1 
ATOM   10277 N  N     . PHE B 1 597 ? 151.774 132.157 114.583 1.00 103.60 ? 597  PHE B N     1 
ATOM   10278 C  CA    . PHE B 1 597 ? 150.829 132.392 113.501 1.00 101.43 ? 597  PHE B CA    1 
ATOM   10279 C  C     . PHE B 1 597 ? 151.555 132.521 112.174 1.00 101.40 ? 597  PHE B C     1 
ATOM   10280 O  O     . PHE B 1 597 ? 151.389 131.681 111.284 1.00 108.58 ? 597  PHE B O     1 
ATOM   10281 C  CB    . PHE B 1 597 ? 150.010 133.647 113.804 1.00 102.52 ? 597  PHE B CB    1 
ATOM   10282 C  CG    . PHE B 1 597 ? 149.214 134.159 112.642 1.00 100.35 ? 597  PHE B CG    1 
ATOM   10283 C  CD1   . PHE B 1 597 ? 148.072 133.502 112.229 1.00 103.21 ? 597  PHE B CD1   1 
ATOM   10284 C  CD2   . PHE B 1 597 ? 149.587 135.315 111.985 1.00 101.55 ? 597  PHE B CD2   1 
ATOM   10285 C  CE1   . PHE B 1 597 ? 147.329 133.976 111.171 1.00 105.15 ? 597  PHE B CE1   1 
ATOM   10286 C  CE2   . PHE B 1 597 ? 148.848 135.794 110.926 1.00 96.57  ? 597  PHE B CE2   1 
ATOM   10287 C  CZ    . PHE B 1 597 ? 147.718 135.124 110.520 1.00 98.58  ? 597  PHE B CZ    1 
ATOM   10288 N  N     . PHE B 1 598 ? 152.435 133.517 112.060 1.00 97.22  ? 598  PHE B N     1 
ATOM   10289 C  CA    . PHE B 1 598 ? 153.150 133.756 110.819 1.00 100.55 ? 598  PHE B CA    1 
ATOM   10290 C  C     . PHE B 1 598 ? 153.853 132.487 110.376 1.00 106.34 ? 598  PHE B C     1 
ATOM   10291 O  O     . PHE B 1 598 ? 153.372 131.844 109.440 1.00 116.81 ? 598  PHE B O     1 
ATOM   10292 C  CB    . PHE B 1 598 ? 154.150 134.899 110.982 1.00 99.59  ? 598  PHE B CB    1 
ATOM   10293 C  CG    . PHE B 1 598 ? 153.530 136.259 110.879 1.00 104.66 ? 598  PHE B CG    1 
ATOM   10294 C  CD1   . PHE B 1 598 ? 152.343 136.439 110.196 1.00 105.20 ? 598  PHE B CD1   1 
ATOM   10295 C  CD2   . PHE B 1 598 ? 154.125 137.353 111.472 1.00 107.15 ? 598  PHE B CD2   1 
ATOM   10296 C  CE1   . PHE B 1 598 ? 151.768 137.686 110.099 1.00 101.39 ? 598  PHE B CE1   1 
ATOM   10297 C  CE2   . PHE B 1 598 ? 153.552 138.601 111.379 1.00 104.49 ? 598  PHE B CE2   1 
ATOM   10298 C  CZ    . PHE B 1 598 ? 152.373 138.767 110.692 1.00 100.47 ? 598  PHE B CZ    1 
ATOM   10299 N  N     . ILE B 1 599 ? 154.872 132.038 111.114 1.00 103.62 ? 599  ILE B N     1 
ATOM   10300 C  CA    . ILE B 1 599 ? 155.703 130.943 110.627 1.00 106.77 ? 599  ILE B CA    1 
ATOM   10301 C  C     . ILE B 1 599 ? 154.826 129.756 110.264 1.00 112.28 ? 599  ILE B C     1 
ATOM   10302 O  O     . ILE B 1 599 ? 154.608 129.484 109.078 1.00 120.13 ? 599  ILE B O     1 
ATOM   10303 C  CB    . ILE B 1 599 ? 156.758 130.523 111.665 1.00 99.89  ? 599  ILE B CB    1 
ATOM   10304 C  CG1   . ILE B 1 599 ? 157.746 131.652 111.929 1.00 99.43  ? 599  ILE B CG1   1 
ATOM   10305 C  CG2   . ILE B 1 599 ? 157.501 129.288 111.193 1.00 103.12 ? 599  ILE B CG2   1 
ATOM   10306 C  CD1   . ILE B 1 599 ? 158.792 131.290 112.949 1.00 97.92  ? 599  ILE B CD1   1 
ATOM   10307 N  N     . VAL B 1 600 ? 154.195 129.136 111.262 1.00 104.21 ? 600  VAL B N     1 
ATOM   10308 C  CA    . VAL B 1 600 ? 153.528 127.864 111.011 1.00 103.33 ? 600  VAL B CA    1 
ATOM   10309 C  C     . VAL B 1 600 ? 152.342 128.057 110.075 1.00 111.24 ? 600  VAL B C     1 
ATOM   10310 O  O     . VAL B 1 600 ? 152.299 127.494 108.975 1.00 119.28 ? 600  VAL B O     1 
ATOM   10311 C  CB    . VAL B 1 600 ? 153.100 127.208 112.332 1.00 104.71 ? 600  VAL B CB    1 
ATOM   10312 C  CG1   . VAL B 1 600 ? 152.405 125.889 112.058 1.00 111.24 ? 600  VAL B CG1   1 
ATOM   10313 C  CG2   . VAL B 1 600 ? 154.305 126.998 113.218 1.00 108.83 ? 600  VAL B CG2   1 
ATOM   10314 N  N     . PHE B 1 601 ? 151.368 128.867 110.487 1.00 108.53 ? 601  PHE B N     1 
ATOM   10315 C  CA    . PHE B 1 601 ? 150.084 128.820 109.812 1.00 111.66 ? 601  PHE B CA    1 
ATOM   10316 C  C     . PHE B 1 601 ? 150.056 129.665 108.545 1.00 113.85 ? 601  PHE B C     1 
ATOM   10317 O  O     . PHE B 1 601 ? 149.330 129.319 107.609 1.00 121.81 ? 601  PHE B O     1 
ATOM   10318 C  CB    . PHE B 1 601 ? 148.993 129.222 110.799 1.00 107.53 ? 601  PHE B CB    1 
ATOM   10319 C  CG    . PHE B 1 601 ? 148.935 128.322 112.000 1.00 109.19 ? 601  PHE B CG    1 
ATOM   10320 C  CD1   . PHE B 1 601 ? 149.700 128.590 113.121 1.00 108.93 ? 601  PHE B CD1   1 
ATOM   10321 C  CD2   . PHE B 1 601 ? 148.154 127.183 111.991 1.00 113.16 ? 601  PHE B CD2   1 
ATOM   10322 C  CE1   . PHE B 1 601 ? 149.667 127.753 114.217 1.00 105.73 ? 601  PHE B CE1   1 
ATOM   10323 C  CE2   . PHE B 1 601 ? 148.116 126.343 113.086 1.00 112.80 ? 601  PHE B CE2   1 
ATOM   10324 C  CZ    . PHE B 1 601 ? 148.873 126.630 114.201 1.00 104.13 ? 601  PHE B CZ    1 
ATOM   10325 N  N     . GLN B 1 602 ? 150.828 130.750 108.459 1.00 110.65 ? 602  GLN B N     1 
ATOM   10326 C  CA    . GLN B 1 602 ? 150.955 131.432 107.185 1.00 118.45 ? 602  GLN B CA    1 
ATOM   10327 C  C     . GLN B 1 602 ? 152.138 130.924 106.371 1.00 125.07 ? 602  GLN B C     1 
ATOM   10328 O  O     . GLN B 1 602 ? 152.486 131.545 105.362 1.00 132.82 ? 602  GLN B O     1 
ATOM   10329 C  CB    . GLN B 1 602 ? 151.068 132.943 107.390 1.00 118.15 ? 602  GLN B CB    1 
ATOM   10330 C  CG    . GLN B 1 602 ? 149.738 133.631 107.627 1.00 114.03 ? 602  GLN B CG    1 
ATOM   10331 C  CD    . GLN B 1 602 ? 149.776 135.097 107.252 1.00 114.71 ? 602  GLN B CD    1 
ATOM   10332 O  OE1   . GLN B 1 602 ? 150.720 135.561 106.615 1.00 117.02 ? 602  GLN B OE1   1 
ATOM   10333 N  NE2   . GLN B 1 602 ? 148.741 135.833 107.635 1.00 111.76 ? 602  GLN B NE2   1 
ATOM   10334 N  N     . GLY B 1 603 ? 152.776 129.828 106.787 1.00 121.16 ? 603  GLY B N     1 
ATOM   10335 C  CA    . GLY B 1 603 ? 153.566 129.068 105.848 1.00 127.93 ? 603  GLY B CA    1 
ATOM   10336 C  C     . GLY B 1 603 ? 152.730 127.950 105.271 1.00 132.05 ? 603  GLY B C     1 
ATOM   10337 O  O     . GLY B 1 603 ? 152.877 127.586 104.101 1.00 139.04 ? 603  GLY B O     1 
ATOM   10338 N  N     . PHE B 1 604 ? 151.841 127.396 106.097 1.00 127.00 ? 604  PHE B N     1 
ATOM   10339 C  CA    . PHE B 1 604 ? 150.952 126.345 105.618 1.00 126.54 ? 604  PHE B CA    1 
ATOM   10340 C  C     . PHE B 1 604 ? 149.896 126.898 104.670 1.00 128.74 ? 604  PHE B C     1 
ATOM   10341 O  O     . PHE B 1 604 ? 149.660 126.331 103.598 1.00 134.34 ? 604  PHE B O     1 
ATOM   10342 C  CB    . PHE B 1 604 ? 150.295 125.634 106.798 1.00 123.18 ? 604  PHE B CB    1 
ATOM   10343 C  CG    . PHE B 1 604 ? 149.339 124.553 106.395 1.00 126.66 ? 604  PHE B CG    1 
ATOM   10344 C  CD1   . PHE B 1 604 ? 149.806 123.333 105.942 1.00 130.44 ? 604  PHE B CD1   1 
ATOM   10345 C  CD2   . PHE B 1 604 ? 147.974 124.753 106.473 1.00 128.82 ? 604  PHE B CD2   1 
ATOM   10346 C  CE1   . PHE B 1 604 ? 148.930 122.335 105.571 1.00 131.51 ? 604  PHE B CE1   1 
ATOM   10347 C  CE2   . PHE B 1 604 ? 147.093 123.758 106.104 1.00 128.36 ? 604  PHE B CE2   1 
ATOM   10348 C  CZ    . PHE B 1 604 ? 147.572 122.548 105.653 1.00 127.00 ? 604  PHE B CZ    1 
ATOM   10349 N  N     . GLN B 1 605 ? 149.253 128.007 105.043 1.00 125.75 ? 605  GLN B N     1 
ATOM   10350 C  CA    . GLN B 1 605 ? 148.174 128.548 104.224 1.00 129.86 ? 605  GLN B CA    1 
ATOM   10351 C  C     . GLN B 1 605 ? 148.706 129.172 102.941 1.00 131.45 ? 605  GLN B C     1 
ATOM   10352 O  O     . GLN B 1 605 ? 148.118 129.003 101.867 1.00 136.73 ? 605  GLN B O     1 
ATOM   10353 C  CB    . GLN B 1 605 ? 147.370 129.573 105.025 1.00 127.98 ? 605  GLN B CB    1 
ATOM   10354 C  CG    . GLN B 1 605 ? 146.434 130.411 104.175 1.00 128.41 ? 605  GLN B CG    1 
ATOM   10355 C  CD    . GLN B 1 605 ? 145.709 131.471 104.974 1.00 130.95 ? 605  GLN B CD    1 
ATOM   10356 O  OE1   . GLN B 1 605 ? 144.804 131.168 105.748 1.00 127.25 ? 605  GLN B OE1   1 
ATOM   10357 N  NE2   . GLN B 1 605 ? 146.101 132.724 104.788 1.00 132.99 ? 605  GLN B NE2   1 
ATOM   10358 N  N     . GLN B 1 606 ? 149.825 129.888 103.027 1.00 125.84 ? 606  GLN B N     1 
ATOM   10359 C  CA    . GLN B 1 606 ? 150.351 130.631 101.893 1.00 131.48 ? 606  GLN B CA    1 
ATOM   10360 C  C     . GLN B 1 606 ? 151.514 129.919 101.215 1.00 134.61 ? 606  GLN B C     1 
ATOM   10361 O  O     . GLN B 1 606 ? 152.236 130.539 100.426 1.00 138.06 ? 606  GLN B O     1 
ATOM   10362 C  CB    . GLN B 1 606 ? 150.765 132.035 102.333 1.00 129.70 ? 606  GLN B CB    1 
ATOM   10363 C  CG    . GLN B 1 606 ? 149.657 132.795 103.039 1.00 129.74 ? 606  GLN B CG    1 
ATOM   10364 C  CD    . GLN B 1 606 ? 149.876 134.290 103.021 1.00 135.53 ? 606  GLN B CD    1 
ATOM   10365 O  OE1   . GLN B 1 606 ? 151.011 134.761 102.988 1.00 138.46 ? 606  GLN B OE1   1 
ATOM   10366 N  NE2   . GLN B 1 606 ? 148.786 135.049 103.040 1.00 135.51 ? 606  GLN B NE2   1 
ATOM   10367 N  N     . ASN B 1 607 ? 151.701 128.630 101.501 1.00 132.21 ? 607  ASN B N     1 
ATOM   10368 C  CA    . ASN B 1 607 ? 152.722 127.800 100.864 1.00 135.26 ? 607  ASN B CA    1 
ATOM   10369 C  C     . ASN B 1 607 ? 154.103 128.434 101.056 1.00 136.23 ? 607  ASN B C     1 
ATOM   10370 O  O     . ASN B 1 607 ? 154.712 128.979 100.134 1.00 139.88 ? 607  ASN B O     1 
ATOM   10371 C  CB    . ASN B 1 607 ? 152.386 127.574 99.380  1.00 141.13 ? 607  ASN B CB    1 
ATOM   10372 C  CG    . ASN B 1 607 ? 153.521 126.928 98.584  1.00 143.50 ? 607  ASN B CG    1 
ATOM   10373 O  OD1   . ASN B 1 607 ? 154.520 126.469 99.139  1.00 141.76 ? 607  ASN B OD1   1 
ATOM   10374 N  ND2   . ASN B 1 607 ? 153.365 126.901 97.267  1.00 147.11 ? 607  ASN B ND2   1 
ATOM   10375 N  N     . ARG B 1 608 ? 154.562 128.406 102.304 1.00 135.26 ? 608  ARG B N     1 
ATOM   10376 C  CA    . ARG B 1 608 ? 155.907 128.844 102.636 1.00 135.18 ? 608  ARG B CA    1 
ATOM   10377 C  C     . ARG B 1 608 ? 156.697 127.791 103.393 1.00 140.17 ? 608  ARG B C     1 
ATOM   10378 O  O     . ARG B 1 608 ? 157.886 128.001 103.657 1.00 145.28 ? 608  ARG B O     1 
ATOM   10379 C  CB    . ARG B 1 608 ? 155.860 130.145 103.442 1.00 129.20 ? 608  ARG B CB    1 
ATOM   10380 C  CG    . ARG B 1 608 ? 155.665 131.364 102.571 1.00 129.43 ? 608  ARG B CG    1 
ATOM   10381 C  CD    . ARG B 1 608 ? 155.859 132.642 103.349 1.00 125.81 ? 608  ARG B CD    1 
ATOM   10382 N  NE    . ARG B 1 608 ? 154.746 132.875 104.260 1.00 124.74 ? 608  ARG B NE    1 
ATOM   10383 C  CZ    . ARG B 1 608 ? 154.295 134.074 104.593 1.00 125.98 ? 608  ARG B CZ    1 
ATOM   10384 N  NH1   . ARG B 1 608 ? 154.823 135.176 104.086 1.00 126.83 ? 608  ARG B NH1   1 
ATOM   10385 N  NH2   . ARG B 1 608 ? 153.283 134.172 105.448 1.00 124.20 ? 608  ARG B NH2   1 
ATOM   10386 N  N     . LEU B 1 609 ? 156.077 126.672 103.753 1.00 137.18 ? 609  LEU B N     1 
ATOM   10387 C  CA    . LEU B 1 609 ? 156.817 125.547 104.303 1.00 136.12 ? 609  LEU B CA    1 
ATOM   10388 C  C     . LEU B 1 609 ? 157.617 124.895 103.183 1.00 143.82 ? 609  LEU B C     1 
ATOM   10389 O  O     . LEU B 1 609 ? 157.042 124.278 102.281 1.00 146.30 ? 609  LEU B O     1 
ATOM   10390 C  CB    . LEU B 1 609 ? 155.860 124.545 104.941 1.00 132.67 ? 609  LEU B CB    1 
ATOM   10391 C  CG    . LEU B 1 609 ? 154.766 125.125 105.838 1.00 127.38 ? 609  LEU B CG    1 
ATOM   10392 C  CD1   . LEU B 1 609 ? 153.908 124.018 106.425 1.00 127.82 ? 609  LEU B CD1   1 
ATOM   10393 C  CD2   . LEU B 1 609 ? 155.365 125.976 106.938 1.00 128.06 ? 609  LEU B CD2   1 
ATOM   10394 N  N     . GLU B 1 610 ? 158.940 125.035 103.234 1.00 143.64 ? 610  GLU B N     1 
ATOM   10395 C  CA    . GLU B 1 610 ? 159.787 124.606 102.130 1.00 146.14 ? 610  GLU B CA    1 
ATOM   10396 C  C     . GLU B 1 610 ? 159.787 123.098 101.914 1.00 148.15 ? 610  GLU B C     1 
ATOM   10397 O  O     . GLU B 1 610 ? 160.244 122.645 100.860 1.00 149.83 ? 610  GLU B O     1 
ATOM   10398 C  CB    . GLU B 1 610 ? 161.220 125.091 102.355 1.00 146.32 ? 610  GLU B CB    1 
ATOM   10399 C  CG    . GLU B 1 610 ? 161.364 126.601 102.422 1.00 151.34 ? 610  GLU B CG    1 
ATOM   10400 C  CD    . GLU B 1 610 ? 161.219 127.261 101.066 1.00 163.25 ? 610  GLU B CD    1 
ATOM   10401 O  OE1   . GLU B 1 610 ? 161.456 126.583 100.045 1.00 166.01 ? 610  GLU B OE1   1 
ATOM   10402 O  OE2   . GLU B 1 610 ? 160.870 128.459 101.019 1.00 168.95 ? 610  GLU B OE2   1 
ATOM   10403 N  N     . PHE B 1 611 ? 159.285 122.314 102.866 1.00 143.53 ? 611  PHE B N     1 
ATOM   10404 C  CA    . PHE B 1 611 ? 159.309 120.862 102.762 1.00 137.53 ? 611  PHE B CA    1 
ATOM   10405 C  C     . PHE B 1 611 ? 157.999 120.277 102.252 1.00 139.44 ? 611  PHE B C     1 
ATOM   10406 O  O     . PHE B 1 611 ? 157.855 119.051 102.221 1.00 141.42 ? 611  PHE B O     1 
ATOM   10407 C  CB    . PHE B 1 611 ? 159.662 120.239 104.115 1.00 135.10 ? 611  PHE B CB    1 
ATOM   10408 C  CG    . PHE B 1 611 ? 158.657 120.516 105.196 1.00 135.26 ? 611  PHE B CG    1 
ATOM   10409 C  CD1   . PHE B 1 611 ? 158.736 121.669 105.955 1.00 134.61 ? 611  PHE B CD1   1 
ATOM   10410 C  CD2   . PHE B 1 611 ? 157.642 119.615 105.463 1.00 137.29 ? 611  PHE B CD2   1 
ATOM   10411 C  CE1   . PHE B 1 611 ? 157.818 121.921 106.952 1.00 131.33 ? 611  PHE B CE1   1 
ATOM   10412 C  CE2   . PHE B 1 611 ? 156.721 119.863 106.459 1.00 136.44 ? 611  PHE B CE2   1 
ATOM   10413 C  CZ    . PHE B 1 611 ? 156.809 121.017 107.204 1.00 132.41 ? 611  PHE B CZ    1 
ATOM   10414 N  N     . ILE B 1 612 ? 157.043 121.114 101.853 1.00 142.40 ? 612  ILE B N     1 
ATOM   10415 C  CA    . ILE B 1 612 ? 155.758 120.632 101.360 1.00 145.11 ? 612  ILE B CA    1 
ATOM   10416 C  C     . ILE B 1 612 ? 155.197 121.670 100.400 1.00 148.17 ? 612  ILE B C     1 
ATOM   10417 O  O     . ILE B 1 612 ? 155.477 122.864 100.517 1.00 147.60 ? 612  ILE B O     1 
ATOM   10418 C  CB    . ILE B 1 612 ? 154.781 120.336 102.527 1.00 138.53 ? 612  ILE B CB    1 
ATOM   10419 C  CG1   . ILE B 1 612 ? 153.695 119.359 102.080 1.00 143.05 ? 612  ILE B CG1   1 
ATOM   10420 C  CG2   . ILE B 1 612 ? 154.162 121.615 103.058 1.00 136.68 ? 612  ILE B CG2   1 
ATOM   10421 C  CD1   . ILE B 1 612 ? 152.733 118.981 103.180 1.00 143.63 ? 612  ILE B CD1   1 
ATOM   10422 N  N     . ASP B 1 613 ? 154.418 121.209 99.426  1.00 149.18 ? 613  ASP B N     1 
ATOM   10423 C  CA    . ASP B 1 613 ? 153.789 122.075 98.436  1.00 149.96 ? 613  ASP B CA    1 
ATOM   10424 C  C     . ASP B 1 613 ? 152.288 122.090 98.693  1.00 152.11 ? 613  ASP B C     1 
ATOM   10425 O  O     . ASP B 1 613 ? 151.587 121.126 98.369  1.00 156.72 ? 613  ASP B O     1 
ATOM   10426 C  CB    . ASP B 1 613 ? 154.098 121.601 97.018  1.00 153.50 ? 613  ASP B CB    1 
ATOM   10427 C  CG    . ASP B 1 613 ? 155.328 122.267 96.437  1.00 156.89 ? 613  ASP B CG    1 
ATOM   10428 O  OD1   . ASP B 1 613 ? 155.609 123.425 96.810  1.00 152.89 ? 613  ASP B OD1   1 
ATOM   10429 O  OD2   . ASP B 1 613 ? 156.013 121.634 95.606  1.00 166.12 ? 613  ASP B OD2   1 
ATOM   10430 N  N     . THR B 1 614 ? 151.800 123.184 99.274  1.00 148.77 ? 614  THR B N     1 
ATOM   10431 C  CA    . THR B 1 614 ? 150.376 123.395 99.498  1.00 150.51 ? 614  THR B CA    1 
ATOM   10432 C  C     . THR B 1 614 ? 149.803 124.405 98.509  1.00 152.55 ? 614  THR B C     1 
ATOM   10433 O  O     . THR B 1 614 ? 148.952 125.221 98.869  1.00 152.52 ? 614  THR B O     1 
ATOM   10434 C  CB    . THR B 1 614 ? 150.119 123.852 100.932 1.00 145.33 ? 614  THR B CB    1 
ATOM   10435 O  OG1   . THR B 1 614 ? 150.749 125.119 101.150 1.00 142.91 ? 614  THR B OG1   1 
ATOM   10436 C  CG2   . THR B 1 614 ? 150.680 122.845 101.915 1.00 140.75 ? 614  THR B CG2   1 
ATOM   10437 N  N     . SER B 1 615 ? 150.275 124.364 97.261  1.00 153.94 ? 615  SER B N     1 
ATOM   10438 C  CA    . SER B 1 615 ? 149.914 125.393 96.293  1.00 157.89 ? 615  SER B CA    1 
ATOM   10439 C  C     . SER B 1 615 ? 148.416 125.396 96.012  1.00 164.02 ? 615  SER B C     1 
ATOM   10440 O  O     . SER B 1 615 ? 147.759 126.438 96.118  1.00 165.56 ? 615  SER B O     1 
ATOM   10441 C  CB    . SER B 1 615 ? 150.703 125.192 94.999  1.00 159.15 ? 615  SER B CB    1 
ATOM   10442 O  OG    . SER B 1 615 ? 152.084 125.433 95.203  1.00 156.64 ? 615  SER B OG    1 
ATOM   10443 N  N     . GLU B 1 616 ? 147.854 124.242 95.653  1.00 165.47 ? 616  GLU B N     1 
ATOM   10444 C  CA    . GLU B 1 616 ? 146.423 124.174 95.334  1.00 164.86 ? 616  GLU B CA    1 
ATOM   10445 C  C     . GLU B 1 616 ? 145.612 123.714 96.543  1.00 162.07 ? 616  GLU B C     1 
ATOM   10446 O  O     . GLU B 1 616 ? 144.787 124.468 97.066  1.00 159.32 ? 616  GLU B O     1 
ATOM   10447 C  CB    . GLU B 1 616 ? 146.183 123.278 94.111  1.00 166.57 ? 616  GLU B CB    1 
ATOM   10448 C  CG    . GLU B 1 616 ? 146.783 121.865 94.146  1.00 168.43 ? 616  GLU B CG    1 
ATOM   10449 C  CD    . GLU B 1 616 ? 148.293 121.842 93.998  1.00 168.74 ? 616  GLU B CD    1 
ATOM   10450 O  OE1   . GLU B 1 616 ? 148.869 122.874 93.596  1.00 169.62 ? 616  GLU B OE1   1 
ATOM   10451 O  OE2   . GLU B 1 616 ? 148.902 120.790 94.283  1.00 166.78 ? 616  GLU B OE2   1 
ATOM   10452 N  N     . TYR B 1 617 ? 145.859 122.486 97.007  1.00 160.53 ? 617  TYR B N     1 
ATOM   10453 C  CA    . TYR B 1 617 ? 145.100 121.871 98.092  1.00 158.04 ? 617  TYR B CA    1 
ATOM   10454 C  C     . TYR B 1 617 ? 143.598 121.985 97.851  1.00 162.57 ? 617  TYR B C     1 
ATOM   10455 O  O     . TYR B 1 617 ? 143.159 122.171 96.712  1.00 169.21 ? 617  TYR B O     1 
ATOM   10456 C  CB    . TYR B 1 617 ? 145.485 122.481 99.439  1.00 151.93 ? 617  TYR B CB    1 
ATOM   10457 C  CG    . TYR B 1 617 ? 146.399 121.584 100.242 1.00 151.51 ? 617  TYR B CG    1 
ATOM   10458 C  CD1   . TYR B 1 617 ? 147.401 120.853 99.619  1.00 151.14 ? 617  TYR B CD1   1 
ATOM   10459 C  CD2   . TYR B 1 617 ? 146.259 121.461 101.616 1.00 148.37 ? 617  TYR B CD2   1 
ATOM   10460 C  CE1   . TYR B 1 617 ? 148.241 120.030 100.341 1.00 147.00 ? 617  TYR B CE1   1 
ATOM   10461 C  CE2   . TYR B 1 617 ? 147.095 120.638 102.347 1.00 143.86 ? 617  TYR B CE2   1 
ATOM   10462 C  CZ    . TYR B 1 617 ? 148.083 119.926 101.704 1.00 143.45 ? 617  TYR B CZ    1 
ATOM   10463 O  OH    . TYR B 1 617 ? 148.918 119.107 102.425 1.00 144.43 ? 617  TYR B OH    1 
ATOM   10464 N  N     . SER B 1 618 ? 142.797 121.852 98.909  1.00 157.91 ? 618  SER B N     1 
ATOM   10465 C  CA    . SER B 1 618 ? 141.352 121.946 98.733  1.00 156.88 ? 618  SER B CA    1 
ATOM   10466 C  C     . SER B 1 618 ? 140.867 123.389 98.784  1.00 151.59 ? 618  SER B C     1 
ATOM   10467 O  O     . SER B 1 618 ? 139.745 123.676 98.352  1.00 152.77 ? 618  SER B O     1 
ATOM   10468 C  CB    . SER B 1 618 ? 140.637 121.117 99.797  1.00 156.43 ? 618  SER B CB    1 
ATOM   10469 O  OG    . SER B 1 618 ? 140.711 121.753 101.059 1.00 153.96 ? 618  SER B OG    1 
ATOM   10470 N  N     . GLN B 1 619 ? 141.684 124.297 99.317  1.00 146.40 ? 619  GLN B N     1 
ATOM   10471 C  CA    . GLN B 1 619 ? 141.432 125.717 99.540  1.00 147.22 ? 619  GLN B CA    1 
ATOM   10472 C  C     . GLN B 1 619 ? 140.459 125.893 100.715 1.00 146.00 ? 619  GLN B C     1 
ATOM   10473 O  O     . GLN B 1 619 ? 140.303 127.008 101.210 1.00 145.29 ? 619  GLN B O     1 
ATOM   10474 C  CB    . GLN B 1 619 ? 140.901 126.438 98.278  1.00 149.97 ? 619  GLN B CB    1 
ATOM   10475 C  CG    . GLN B 1 619 ? 140.337 127.861 98.400  1.00 148.86 ? 619  GLN B CG    1 
ATOM   10476 C  CD    . GLN B 1 619 ? 141.234 128.804 99.186  1.00 146.80 ? 619  GLN B CD    1 
ATOM   10477 O  OE1   . GLN B 1 619 ? 142.125 129.438 98.626  1.00 145.76 ? 619  GLN B OE1   1 
ATOM   10478 N  NE2   . GLN B 1 619 ? 140.974 128.930 100.480 1.00 144.59 ? 619  GLN B NE2   1 
ATOM   10479 N  N     . THR B 1 620 ? 139.865 124.819 101.229 1.00 146.93 ? 620  THR B N     1 
ATOM   10480 C  CA    . THR B 1 620 ? 139.122 124.881 102.477 1.00 146.27 ? 620  THR B CA    1 
ATOM   10481 C  C     . THR B 1 620 ? 140.008 124.650 103.691 1.00 142.18 ? 620  THR B C     1 
ATOM   10482 O  O     . THR B 1 620 ? 139.874 125.376 104.681 1.00 140.23 ? 620  THR B O     1 
ATOM   10483 C  CB    . THR B 1 620 ? 137.980 123.855 102.470 1.00 146.68 ? 620  THR B CB    1 
ATOM   10484 O  OG1   . THR B 1 620 ? 136.947 124.293 101.579 1.00 152.22 ? 620  THR B OG1   1 
ATOM   10485 C  CG2   . THR B 1 620 ? 137.399 123.672 103.867 1.00 140.37 ? 620  THR B CG2   1 
ATOM   10486 N  N     . VAL B 1 621 ? 140.932 123.692 103.623 1.00 141.10 ? 621  VAL B N     1 
ATOM   10487 C  CA    . VAL B 1 621 ? 141.837 123.397 104.728 1.00 139.10 ? 621  VAL B CA    1 
ATOM   10488 C  C     . VAL B 1 621 ? 142.860 124.518 104.848 1.00 136.20 ? 621  VAL B C     1 
ATOM   10489 O  O     . VAL B 1 621 ? 143.347 124.815 105.944 1.00 136.25 ? 621  VAL B O     1 
ATOM   10490 C  CB    . VAL B 1 621 ? 142.531 122.037 104.533 1.00 140.60 ? 621  VAL B CB    1 
ATOM   10491 C  CG1   . VAL B 1 621 ? 143.169 121.576 105.832 1.00 146.21 ? 621  VAL B CG1   1 
ATOM   10492 C  CG2   . VAL B 1 621 ? 141.538 121.007 104.033 1.00 142.38 ? 621  VAL B CG2   1 
ATOM   10493 N  N     . LEU B 1 622 ? 143.177 125.157 103.718 1.00 136.60 ? 622  LEU B N     1 
ATOM   10494 C  CA    . LEU B 1 622 ? 144.197 126.199 103.715 1.00 134.57 ? 622  LEU B CA    1 
ATOM   10495 C  C     . LEU B 1 622 ? 143.810 127.349 104.634 1.00 135.28 ? 622  LEU B C     1 
ATOM   10496 O  O     . LEU B 1 622 ? 144.636 127.836 105.414 1.00 132.96 ? 622  LEU B O     1 
ATOM   10497 C  CB    . LEU B 1 622 ? 144.418 126.703 102.290 1.00 136.36 ? 622  LEU B CB    1 
ATOM   10498 C  CG    . LEU B 1 622 ? 145.548 126.052 101.491 1.00 137.37 ? 622  LEU B CG    1 
ATOM   10499 C  CD1   . LEU B 1 622 ? 146.057 126.997 100.416 1.00 138.16 ? 622  LEU B CD1   1 
ATOM   10500 C  CD2   . LEU B 1 622 ? 146.679 125.607 102.399 1.00 135.54 ? 622  LEU B CD2   1 
ATOM   10501 N  N     . ASP B 1 623 ? 142.556 127.796 104.560 1.00 134.37 ? 623  ASP B N     1 
ATOM   10502 C  CA    . ASP B 1 623 ? 142.053 128.785 105.503 1.00 129.90 ? 623  ASP B CA    1 
ATOM   10503 C  C     . ASP B 1 623 ? 141.597 128.153 106.809 1.00 124.84 ? 623  ASP B C     1 
ATOM   10504 O  O     . ASP B 1 623 ? 141.559 128.841 107.837 1.00 122.20 ? 623  ASP B O     1 
ATOM   10505 C  CB    . ASP B 1 623 ? 140.896 129.567 104.881 1.00 129.19 ? 623  ASP B CB    1 
ATOM   10506 C  CG    . ASP B 1 623 ? 141.368 130.750 104.061 1.00 138.81 ? 623  ASP B CG    1 
ATOM   10507 O  OD1   . ASP B 1 623 ? 141.652 130.566 102.859 1.00 143.16 ? 623  ASP B OD1   1 
ATOM   10508 O  OD2   . ASP B 1 623 ? 141.453 131.865 104.617 1.00 142.65 ? 623  ASP B OD2   1 
ATOM   10509 N  N     . CYS B 1 624 ? 141.252 126.863 106.786 1.00 127.65 ? 624  CYS B N     1 
ATOM   10510 C  CA    . CYS B 1 624 ? 140.780 126.198 107.993 1.00 126.95 ? 624  CYS B CA    1 
ATOM   10511 C  C     . CYS B 1 624 ? 141.873 126.132 109.047 1.00 121.22 ? 624  CYS B C     1 
ATOM   10512 O  O     . CYS B 1 624 ? 141.593 126.249 110.242 1.00 119.51 ? 624  CYS B O     1 
ATOM   10513 C  CB    . CYS B 1 624 ? 140.273 124.796 107.664 1.00 131.45 ? 624  CYS B CB    1 
ATOM   10514 S  SG    . CYS B 1 624 ? 139.568 123.904 109.061 1.00 135.50 ? 624  CYS B SG    1 
ATOM   10515 N  N     . ALA B 1 625 ? 143.124 125.937 108.627 1.00 118.71 ? 625  ALA B N     1 
ATOM   10516 C  CA    . ALA B 1 625 ? 144.221 125.893 109.590 1.00 115.84 ? 625  ALA B CA    1 
ATOM   10517 C  C     . ALA B 1 625 ? 144.342 127.211 110.343 1.00 118.68 ? 625  ALA B C     1 
ATOM   10518 O  O     . ALA B 1 625 ? 144.413 127.232 111.578 1.00 120.33 ? 625  ALA B O     1 
ATOM   10519 C  CB    . ALA B 1 625 ? 145.530 125.558 108.878 1.00 118.33 ? 625  ALA B CB    1 
ATOM   10520 N  N     . VAL B 1 626 ? 144.350 128.327 109.611 1.00 119.72 ? 626  VAL B N     1 
ATOM   10521 C  CA    . VAL B 1 626 ? 144.478 129.635 110.247 1.00 115.60 ? 626  VAL B CA    1 
ATOM   10522 C  C     . VAL B 1 626 ? 143.266 129.929 111.119 1.00 116.13 ? 626  VAL B C     1 
ATOM   10523 O  O     . VAL B 1 626 ? 143.401 130.439 112.238 1.00 114.69 ? 626  VAL B O     1 
ATOM   10524 C  CB    . VAL B 1 626 ? 144.694 130.727 109.185 1.00 113.56 ? 626  VAL B CB    1 
ATOM   10525 C  CG1   . VAL B 1 626 ? 144.457 132.101 109.780 1.00 103.46 ? 626  VAL B CG1   1 
ATOM   10526 C  CG2   . VAL B 1 626 ? 146.098 130.634 108.623 1.00 120.13 ? 626  VAL B CG2   1 
ATOM   10527 N  N     . TYR B 1 627 ? 142.062 129.620 110.627 1.00 117.01 ? 627  TYR B N     1 
ATOM   10528 C  CA    . TYR B 1 627 ? 140.866 129.879 111.422 1.00 112.83 ? 627  TYR B CA    1 
ATOM   10529 C  C     . TYR B 1 627 ? 140.861 129.055 112.703 1.00 112.67 ? 627  TYR B C     1 
ATOM   10530 O  O     . TYR B 1 627 ? 140.528 129.570 113.777 1.00 114.76 ? 627  TYR B O     1 
ATOM   10531 C  CB    . TYR B 1 627 ? 139.611 129.600 110.596 1.00 114.47 ? 627  TYR B CB    1 
ATOM   10532 C  CG    . TYR B 1 627 ? 139.123 130.795 109.812 1.00 115.59 ? 627  TYR B CG    1 
ATOM   10533 C  CD1   . TYR B 1 627 ? 138.421 131.815 110.435 1.00 114.24 ? 627  TYR B CD1   1 
ATOM   10534 C  CD2   . TYR B 1 627 ? 139.368 130.906 108.452 1.00 120.24 ? 627  TYR B CD2   1 
ATOM   10535 C  CE1   . TYR B 1 627 ? 137.974 132.910 109.724 1.00 120.02 ? 627  TYR B CE1   1 
ATOM   10536 C  CE2   . TYR B 1 627 ? 138.926 131.996 107.734 1.00 120.83 ? 627  TYR B CE2   1 
ATOM   10537 C  CZ    . TYR B 1 627 ? 138.229 132.995 108.375 1.00 122.52 ? 627  TYR B CZ    1 
ATOM   10538 O  OH    . TYR B 1 627 ? 137.786 134.083 107.662 1.00 129.46 ? 627  TYR B OH    1 
ATOM   10539 N  N     . ILE B 1 628 ? 141.235 127.777 112.613 1.00 112.27 ? 628  ILE B N     1 
ATOM   10540 C  CA    . ILE B 1 628 ? 141.276 126.923 113.794 1.00 113.72 ? 628  ILE B CA    1 
ATOM   10541 C  C     . ILE B 1 628 ? 142.302 127.441 114.787 1.00 113.48 ? 628  ILE B C     1 
ATOM   10542 O  O     . ILE B 1 628 ? 142.034 127.515 115.991 1.00 115.55 ? 628  ILE B O     1 
ATOM   10543 C  CB    . ILE B 1 628 ? 141.562 125.463 113.393 1.00 114.24 ? 628  ILE B CB    1 
ATOM   10544 C  CG1   . ILE B 1 628 ? 140.257 124.713 113.138 1.00 116.54 ? 628  ILE B CG1   1 
ATOM   10545 C  CG2   . ILE B 1 628 ? 142.364 124.750 114.468 1.00 112.44 ? 628  ILE B CG2   1 
ATOM   10546 C  CD1   . ILE B 1 628 ? 140.455 123.386 112.453 1.00 120.29 ? 628  ILE B CD1   1 
ATOM   10547 N  N     . TYR B 1 629 ? 143.489 127.815 114.305 1.00 110.91 ? 629  TYR B N     1 
ATOM   10548 C  CA    . TYR B 1 629 ? 144.514 128.315 115.214 1.00 109.56 ? 629  TYR B CA    1 
ATOM   10549 C  C     . TYR B 1 629 ? 144.060 129.593 115.902 1.00 111.68 ? 629  TYR B C     1 
ATOM   10550 O  O     . TYR B 1 629 ? 144.208 129.742 117.119 1.00 115.48 ? 629  TYR B O     1 
ATOM   10551 C  CB    . TYR B 1 629 ? 145.820 128.554 114.464 1.00 107.21 ? 629  TYR B CB    1 
ATOM   10552 C  CG    . TYR B 1 629 ? 146.812 129.374 115.251 1.00 105.63 ? 629  TYR B CG    1 
ATOM   10553 C  CD1   . TYR B 1 629 ? 147.408 128.865 116.393 1.00 108.66 ? 629  TYR B CD1   1 
ATOM   10554 C  CD2   . TYR B 1 629 ? 147.150 130.657 114.854 1.00 105.88 ? 629  TYR B CD2   1 
ATOM   10555 C  CE1   . TYR B 1 629 ? 148.315 129.607 117.115 1.00 109.58 ? 629  TYR B CE1   1 
ATOM   10556 C  CE2   . TYR B 1 629 ? 148.055 131.407 115.572 1.00 104.15 ? 629  TYR B CE2   1 
ATOM   10557 C  CZ    . TYR B 1 629 ? 148.634 130.877 116.700 1.00 106.29 ? 629  TYR B CZ    1 
ATOM   10558 O  OH    . TYR B 1 629 ? 149.538 131.622 117.418 1.00 109.17 ? 629  TYR B OH    1 
ATOM   10559 N  N     . ASN B 1 630 ? 143.489 130.524 115.136 1.00 109.00 ? 630  ASN B N     1 
ATOM   10560 C  CA    . ASN B 1 630 ? 143.059 131.793 115.709 1.00 106.51 ? 630  ASN B CA    1 
ATOM   10561 C  C     . ASN B 1 630 ? 141.957 131.584 116.738 1.00 111.72 ? 630  ASN B C     1 
ATOM   10562 O  O     . ASN B 1 630 ? 142.005 132.147 117.838 1.00 112.94 ? 630  ASN B O     1 
ATOM   10563 C  CB    . ASN B 1 630 ? 142.589 132.732 114.599 1.00 108.25 ? 630  ASN B CB    1 
ATOM   10564 C  CG    . ASN B 1 630 ? 143.599 133.811 114.288 1.00 112.68 ? 630  ASN B CG    1 
ATOM   10565 O  OD1   . ASN B 1 630 ? 144.390 134.201 115.144 1.00 114.23 ? 630  ASN B OD1   1 
ATOM   10566 N  ND2   . ASN B 1 630 ? 143.579 134.300 113.055 1.00 116.60 ? 630  ASN B ND2   1 
ATOM   10567 N  N     . PHE B 1 631 ? 140.957 130.766 116.402 1.00 112.57 ? 631  PHE B N     1 
ATOM   10568 C  CA    . PHE B 1 631 ? 139.850 130.546 117.326 1.00 111.92 ? 631  PHE B CA    1 
ATOM   10569 C  C     . PHE B 1 631 ? 140.306 129.805 118.574 1.00 114.44 ? 631  PHE B C     1 
ATOM   10570 O  O     . PHE B 1 631 ? 139.893 130.149 119.686 1.00 116.14 ? 631  PHE B O     1 
ATOM   10571 C  CB    . PHE B 1 631 ? 138.724 129.790 116.626 1.00 110.35 ? 631  PHE B CB    1 
ATOM   10572 C  CG    . PHE B 1 631 ? 137.857 130.664 115.773 1.00 120.25 ? 631  PHE B CG    1 
ATOM   10573 C  CD1   . PHE B 1 631 ? 137.796 132.027 116.002 1.00 121.41 ? 631  PHE B CD1   1 
ATOM   10574 C  CD2   . PHE B 1 631 ? 137.108 130.129 114.743 1.00 125.40 ? 631  PHE B CD2   1 
ATOM   10575 C  CE1   . PHE B 1 631 ? 137.004 132.839 115.220 1.00 121.05 ? 631  PHE B CE1   1 
ATOM   10576 C  CE2   . PHE B 1 631 ? 136.313 130.937 113.958 1.00 125.05 ? 631  PHE B CE2   1 
ATOM   10577 C  CZ    . PHE B 1 631 ? 136.262 132.294 114.198 1.00 122.44 ? 631  PHE B CZ    1 
ATOM   10578 N  N     . SER B 1 632 ? 141.160 128.791 118.417 1.00 112.14 ? 632  SER B N     1 
ATOM   10579 C  CA    . SER B 1 632 ? 141.666 128.072 119.578 1.00 111.09 ? 632  SER B CA    1 
ATOM   10580 C  C     . SER B 1 632 ? 142.479 128.988 120.479 1.00 112.77 ? 632  SER B C     1 
ATOM   10581 O  O     . SER B 1 632 ? 142.304 128.976 121.702 1.00 118.23 ? 632  SER B O     1 
ATOM   10582 C  CB    . SER B 1 632 ? 142.508 126.878 119.130 1.00 111.97 ? 632  SER B CB    1 
ATOM   10583 O  OG    . SER B 1 632 ? 143.578 126.650 120.028 1.00 117.83 ? 632  SER B OG    1 
ATOM   10584 N  N     . TYR B 1 633 ? 143.359 129.804 119.896 1.00 108.86 ? 633  TYR B N     1 
ATOM   10585 C  CA    . TYR B 1 633 ? 144.176 130.705 120.700 1.00 108.13 ? 633  TYR B CA    1 
ATOM   10586 C  C     . TYR B 1 633 ? 143.313 131.729 121.424 1.00 112.42 ? 633  TYR B C     1 
ATOM   10587 O  O     . TYR B 1 633 ? 143.520 132.002 122.611 1.00 119.67 ? 633  TYR B O     1 
ATOM   10588 C  CB    . TYR B 1 633 ? 145.211 131.399 119.816 1.00 106.83 ? 633  TYR B CB    1 
ATOM   10589 C  CG    . TYR B 1 633 ? 146.494 131.741 120.531 1.00 105.45 ? 633  TYR B CG    1 
ATOM   10590 C  CD1   . TYR B 1 633 ? 147.530 130.823 120.613 1.00 105.84 ? 633  TYR B CD1   1 
ATOM   10591 C  CD2   . TYR B 1 633 ? 146.670 132.979 121.126 1.00 106.52 ? 633  TYR B CD2   1 
ATOM   10592 C  CE1   . TYR B 1 633 ? 148.705 131.130 121.267 1.00 109.09 ? 633  TYR B CE1   1 
ATOM   10593 C  CE2   . TYR B 1 633 ? 147.841 133.295 121.782 1.00 107.87 ? 633  TYR B CE2   1 
ATOM   10594 C  CZ    . TYR B 1 633 ? 148.854 132.367 121.849 1.00 109.78 ? 633  TYR B CZ    1 
ATOM   10595 O  OH    . TYR B 1 633 ? 150.022 132.680 122.503 1.00 109.70 ? 633  TYR B OH    1 
ATOM   10596 N  N     . LEU B 1 634 ? 142.326 132.297 120.728 1.00 109.71 ? 634  LEU B N     1 
ATOM   10597 C  CA    . LEU B 1 634 ? 141.490 133.320 121.346 1.00 111.90 ? 634  LEU B CA    1 
ATOM   10598 C  C     . LEU B 1 634 ? 140.614 132.734 122.446 1.00 114.51 ? 634  LEU B C     1 
ATOM   10599 O  O     . LEU B 1 634 ? 140.470 133.333 123.518 1.00 118.83 ? 634  LEU B O     1 
ATOM   10600 C  CB    . LEU B 1 634 ? 140.640 134.008 120.281 1.00 116.73 ? 634  LEU B CB    1 
ATOM   10601 C  CG    . LEU B 1 634 ? 141.321 135.188 119.585 1.00 116.40 ? 634  LEU B CG    1 
ATOM   10602 C  CD1   . LEU B 1 634 ? 140.374 135.856 118.605 1.00 124.58 ? 634  LEU B CD1   1 
ATOM   10603 C  CD2   . LEU B 1 634 ? 141.834 136.187 120.607 1.00 110.60 ? 634  LEU B CD2   1 
ATOM   10604 N  N     . PHE B 1 635 ? 140.021 131.561 122.204 1.00 109.20 ? 635  PHE B N     1 
ATOM   10605 C  CA    . PHE B 1 635 ? 139.212 130.921 123.234 1.00 112.70 ? 635  PHE B CA    1 
ATOM   10606 C  C     . PHE B 1 635 ? 140.062 130.527 124.434 1.00 114.56 ? 635  PHE B C     1 
ATOM   10607 O  O     . PHE B 1 635 ? 139.637 130.696 125.583 1.00 117.42 ? 635  PHE B O     1 
ATOM   10608 C  CB    . PHE B 1 635 ? 138.496 129.700 122.658 1.00 112.71 ? 635  PHE B CB    1 
ATOM   10609 C  CG    . PHE B 1 635 ? 137.322 130.041 121.783 1.00 115.55 ? 635  PHE B CG    1 
ATOM   10610 C  CD1   . PHE B 1 635 ? 136.837 131.335 121.723 1.00 115.54 ? 635  PHE B CD1   1 
ATOM   10611 C  CD2   . PHE B 1 635 ? 136.702 129.065 121.024 1.00 117.87 ? 635  PHE B CD2   1 
ATOM   10612 C  CE1   . PHE B 1 635 ? 135.759 131.649 120.920 1.00 117.94 ? 635  PHE B CE1   1 
ATOM   10613 C  CE2   . PHE B 1 635 ? 135.623 129.373 120.221 1.00 117.57 ? 635  PHE B CE2   1 
ATOM   10614 C  CZ    . PHE B 1 635 ? 135.153 130.666 120.169 1.00 119.26 ? 635  PHE B CZ    1 
ATOM   10615 N  N     . GLY B 1 636 ? 141.265 130.004 124.189 1.00 110.42 ? 636  GLY B N     1 
ATOM   10616 C  CA    . GLY B 1 636 ? 142.153 129.681 125.289 1.00 111.23 ? 636  GLY B CA    1 
ATOM   10617 C  C     . GLY B 1 636 ? 142.533 130.901 126.101 1.00 111.75 ? 636  GLY B C     1 
ATOM   10618 O  O     . GLY B 1 636 ? 142.544 130.856 127.330 1.00 116.67 ? 636  GLY B O     1 
ATOM   10619 N  N     . LEU B 1 637 ? 142.838 132.012 125.427 1.00 108.17 ? 637  LEU B N     1 
ATOM   10620 C  CA    . LEU B 1 637 ? 143.188 133.233 126.144 1.00 108.50 ? 637  LEU B CA    1 
ATOM   10621 C  C     . LEU B 1 637 ? 142.011 133.758 126.955 1.00 113.43 ? 637  LEU B C     1 
ATOM   10622 O  O     . LEU B 1 637 ? 142.187 134.216 128.089 1.00 118.12 ? 637  LEU B O     1 
ATOM   10623 C  CB    . LEU B 1 637 ? 143.684 134.295 125.165 1.00 107.91 ? 637  LEU B CB    1 
ATOM   10624 C  CG    . LEU B 1 637 ? 145.097 134.078 124.625 1.00 109.46 ? 637  LEU B CG    1 
ATOM   10625 C  CD1   . LEU B 1 637 ? 145.531 135.256 123.775 1.00 108.87 ? 637  LEU B CD1   1 
ATOM   10626 C  CD2   . LEU B 1 637 ? 146.069 133.852 125.767 1.00 111.73 ? 637  LEU B CD2   1 
ATOM   10627 N  N     . LEU B 1 638 ? 140.801 133.706 126.392 1.00 112.14 ? 638  LEU B N     1 
ATOM   10628 C  CA    . LEU B 1 638 ? 139.631 134.168 127.132 1.00 113.77 ? 638  LEU B CA    1 
ATOM   10629 C  C     . LEU B 1 638 ? 139.374 133.302 128.359 1.00 116.28 ? 638  LEU B C     1 
ATOM   10630 O  O     . LEU B 1 638 ? 139.109 133.820 129.453 1.00 118.72 ? 638  LEU B O     1 
ATOM   10631 C  CB    . LEU B 1 638 ? 138.406 134.183 126.220 1.00 111.07 ? 638  LEU B CB    1 
ATOM   10632 C  CG    . LEU B 1 638 ? 137.100 134.622 126.882 1.00 113.37 ? 638  LEU B CG    1 
ATOM   10633 C  CD1   . LEU B 1 638 ? 137.205 136.060 127.359 1.00 113.81 ? 638  LEU B CD1   1 
ATOM   10634 C  CD2   . LEU B 1 638 ? 135.934 134.456 125.926 1.00 112.94 ? 638  LEU B CD2   1 
ATOM   10635 N  N     . MET B 1 639 ? 139.456 131.978 128.199 1.00 111.61 ? 639  MET B N     1 
ATOM   10636 C  CA    . MET B 1 639 ? 139.271 131.085 129.337 1.00 111.02 ? 639  MET B CA    1 
ATOM   10637 C  C     . MET B 1 639 ? 140.348 131.310 130.388 1.00 115.32 ? 639  MET B C     1 
ATOM   10638 O  O     . MET B 1 639 ? 140.064 131.307 131.591 1.00 120.76 ? 639  MET B O     1 
ATOM   10639 C  CB    . MET B 1 639 ? 139.272 129.632 128.865 1.00 107.51 ? 639  MET B CB    1 
ATOM   10640 C  CG    . MET B 1 639 ? 138.889 128.634 129.939 1.00 114.67 ? 639  MET B CG    1 
ATOM   10641 S  SD    . MET B 1 639 ? 138.848 126.931 129.351 1.00 148.64 ? 639  MET B SD    1 
ATOM   10642 C  CE    . MET B 1 639 ? 138.812 127.172 127.579 1.00 119.15 ? 639  MET B CE    1 
ATOM   10643 N  N     . LEU B 1 640 ? 141.591 131.513 129.949 1.00 113.11 ? 640  LEU B N     1 
ATOM   10644 C  CA    . LEU B 1 640 ? 142.683 131.778 130.877 1.00 110.93 ? 640  LEU B CA    1 
ATOM   10645 C  C     . LEU B 1 640 ? 142.445 133.061 131.655 1.00 115.08 ? 640  LEU B C     1 
ATOM   10646 O  O     . LEU B 1 640 ? 142.664 133.104 132.868 1.00 119.03 ? 640  LEU B O     1 
ATOM   10647 C  CB    . LEU B 1 640 ? 143.999 131.863 130.110 1.00 107.87 ? 640  LEU B CB    1 
ATOM   10648 C  CG    . LEU B 1 640 ? 144.632 130.550 129.664 1.00 111.17 ? 640  LEU B CG    1 
ATOM   10649 C  CD1   . LEU B 1 640 ? 146.119 130.735 129.545 1.00 117.42 ? 640  LEU B CD1   1 
ATOM   10650 C  CD2   . LEU B 1 640 ? 144.309 129.443 130.649 1.00 110.11 ? 640  LEU B CD2   1 
ATOM   10651 N  N     . ILE B 1 641 ? 142.001 134.118 130.974 1.00 114.30 ? 641  ILE B N     1 
ATOM   10652 C  CA    . ILE B 1 641 ? 141.744 135.382 131.658 1.00 113.47 ? 641  ILE B CA    1 
ATOM   10653 C  C     . ILE B 1 641 ? 140.627 135.215 132.676 1.00 117.66 ? 641  ILE B C     1 
ATOM   10654 O  O     . ILE B 1 641 ? 140.738 135.670 133.821 1.00 122.79 ? 641  ILE B O     1 
ATOM   10655 C  CB    . ILE B 1 641 ? 141.425 136.490 130.639 1.00 112.97 ? 641  ILE B CB    1 
ATOM   10656 C  CG1   . ILE B 1 641 ? 142.703 136.947 129.935 1.00 114.80 ? 641  ILE B CG1   1 
ATOM   10657 C  CG2   . ILE B 1 641 ? 140.748 137.664 131.323 1.00 113.02 ? 641  ILE B CG2   1 
ATOM   10658 C  CD1   . ILE B 1 641 ? 142.519 138.167 129.066 1.00 112.88 ? 641  ILE B CD1   1 
ATOM   10659 N  N     . ILE B 1 642 ? 139.542 134.541 132.284 1.00 117.29 ? 642  ILE B N     1 
ATOM   10660 C  CA    . ILE B 1 642 ? 138.416 134.355 133.197 1.00 120.76 ? 642  ILE B CA    1 
ATOM   10661 C  C     . ILE B 1 642 ? 138.846 133.566 134.428 1.00 124.37 ? 642  ILE B C     1 
ATOM   10662 O  O     . ILE B 1 642 ? 138.555 133.953 135.568 1.00 127.02 ? 642  ILE B O     1 
ATOM   10663 C  CB    . ILE B 1 642 ? 137.245 133.674 132.466 1.00 117.88 ? 642  ILE B CB    1 
ATOM   10664 C  CG1   . ILE B 1 642 ? 136.555 134.666 131.531 1.00 117.90 ? 642  ILE B CG1   1 
ATOM   10665 C  CG2   . ILE B 1 642 ? 136.256 133.103 133.462 1.00 113.66 ? 642  ILE B CG2   1 
ATOM   10666 C  CD1   . ILE B 1 642 ? 135.305 134.124 130.882 1.00 115.12 ? 642  ILE B CD1   1 
ATOM   10667 N  N     . ILE B 1 643 ? 139.568 132.463 134.223 1.00 121.96 ? 643  ILE B N     1 
ATOM   10668 C  CA    . ILE B 1 643 ? 139.964 131.619 135.344 1.00 121.31 ? 643  ILE B CA    1 
ATOM   10669 C  C     . ILE B 1 643 ? 140.965 132.344 136.238 1.00 124.76 ? 643  ILE B C     1 
ATOM   10670 O  O     . ILE B 1 643 ? 140.857 132.312 137.469 1.00 126.03 ? 643  ILE B O     1 
ATOM   10671 C  CB    . ILE B 1 643 ? 140.524 130.281 134.834 1.00 118.93 ? 643  ILE B CB    1 
ATOM   10672 C  CG1   . ILE B 1 643 ? 139.425 129.476 134.146 1.00 115.87 ? 643  ILE B CG1   1 
ATOM   10673 C  CG2   . ILE B 1 643 ? 141.095 129.482 135.978 1.00 127.75 ? 643  ILE B CG2   1 
ATOM   10674 C  CD1   . ILE B 1 643 ? 139.872 128.108 133.706 1.00 119.55 ? 643  ILE B CD1   1 
ATOM   10675 N  N     . GLY B 1 644 ? 141.953 133.010 135.635 1.00 124.86 ? 644  GLY B N     1 
ATOM   10676 C  CA    . GLY B 1 644 ? 142.952 133.709 136.426 1.00 129.07 ? 644  GLY B CA    1 
ATOM   10677 C  C     . GLY B 1 644 ? 142.363 134.839 137.245 1.00 131.25 ? 644  GLY B C     1 
ATOM   10678 O  O     . GLY B 1 644 ? 142.735 135.035 138.404 1.00 135.70 ? 644  GLY B O     1 
ATOM   10679 N  N     . LEU B 1 645 ? 141.439 135.600 136.656 1.00 126.32 ? 645  LEU B N     1 
ATOM   10680 C  CA    . LEU B 1 645 ? 140.693 136.578 137.434 1.00 128.50 ? 645  LEU B CA    1 
ATOM   10681 C  C     . LEU B 1 645 ? 139.862 135.936 138.534 1.00 132.45 ? 645  LEU B C     1 
ATOM   10682 O  O     . LEU B 1 645 ? 139.738 136.523 139.613 1.00 135.63 ? 645  LEU B O     1 
ATOM   10683 C  CB    . LEU B 1 645 ? 139.767 137.391 136.531 1.00 128.24 ? 645  LEU B CB    1 
ATOM   10684 C  CG    . LEU B 1 645 ? 140.111 138.760 135.945 1.00 128.01 ? 645  LEU B CG    1 
ATOM   10685 C  CD1   . LEU B 1 645 ? 139.842 139.855 136.962 1.00 131.15 ? 645  LEU B CD1   1 
ATOM   10686 C  CD2   . LEU B 1 645 ? 141.520 138.825 135.459 1.00 127.91 ? 645  LEU B CD2   1 
ATOM   10687 N  N     . GLY B 1 646 ? 139.296 134.755 138.293 1.00 132.00 ? 646  GLY B N     1 
ATOM   10688 C  CA    . GLY B 1 646 ? 138.352 134.185 139.231 1.00 134.83 ? 646  GLY B CA    1 
ATOM   10689 C  C     . GLY B 1 646 ? 138.918 133.216 140.249 1.00 136.73 ? 646  GLY B C     1 
ATOM   10690 O  O     . GLY B 1 646 ? 139.604 133.621 141.192 1.00 138.38 ? 646  GLY B O     1 
ATOM   10691 N  N     . ASN B 1 647 ? 138.630 131.932 140.067 1.00 138.15 ? 647  ASN B N     1 
ATOM   10692 C  CA    . ASN B 1 647 ? 138.867 130.930 141.094 1.00 142.59 ? 647  ASN B CA    1 
ATOM   10693 C  C     . ASN B 1 647 ? 140.358 130.672 141.308 1.00 142.95 ? 647  ASN B C     1 
ATOM   10694 O  O     . ASN B 1 647 ? 141.193 130.883 140.425 1.00 140.86 ? 647  ASN B O     1 
ATOM   10695 C  CB    . ASN B 1 647 ? 138.163 129.623 140.734 1.00 141.68 ? 647  ASN B CB    1 
ATOM   10696 C  CG    . ASN B 1 647 ? 138.293 129.278 139.270 1.00 140.56 ? 647  ASN B CG    1 
ATOM   10697 O  OD1   . ASN B 1 647 ? 139.183 129.774 138.581 1.00 140.05 ? 647  ASN B OD1   1 
ATOM   10698 N  ND2   . ASN B 1 647 ? 137.407 128.420 138.784 1.00 140.39 ? 647  ASN B ND2   1 
ATOM   10699 N  N     . ASN B 1 648 ? 140.674 130.209 142.514 1.00 142.41 ? 648  ASN B N     1 
ATOM   10700 C  CA    . ASN B 1 648 ? 142.029 129.799 142.846 1.00 143.12 ? 648  ASN B CA    1 
ATOM   10701 C  C     . ASN B 1 648 ? 142.412 128.584 142.003 1.00 143.24 ? 648  ASN B C     1 
ATOM   10702 O  O     . ASN B 1 648 ? 141.689 127.584 141.989 1.00 144.80 ? 648  ASN B O     1 
ATOM   10703 C  CB    . ASN B 1 648 ? 142.107 129.474 144.346 1.00 147.73 ? 648  ASN B CB    1 
ATOM   10704 C  CG    . ASN B 1 648 ? 143.481 128.984 144.802 1.00 150.01 ? 648  ASN B CG    1 
ATOM   10705 O  OD1   . ASN B 1 648 ? 144.362 128.673 144.006 1.00 147.26 ? 648  ASN B OD1   1 
ATOM   10706 N  ND2   . ASN B 1 648 ? 143.658 128.915 146.116 1.00 152.85 ? 648  ASN B ND2   1 
ATOM   10707 N  N     . PRO B 1 649 ? 143.546 128.635 141.289 1.00 139.83 ? 649  PRO B N     1 
ATOM   10708 C  CA    . PRO B 1 649 ? 143.970 127.526 140.425 1.00 138.23 ? 649  PRO B CA    1 
ATOM   10709 C  C     . PRO B 1 649 ? 144.414 126.281 141.189 1.00 141.43 ? 649  PRO B C     1 
ATOM   10710 O  O     . PRO B 1 649 ? 145.559 125.843 141.087 1.00 140.47 ? 649  PRO B O     1 
ATOM   10711 C  CB    . PRO B 1 649 ? 145.128 128.140 139.633 1.00 132.47 ? 649  PRO B CB    1 
ATOM   10712 C  CG    . PRO B 1 649 ? 145.654 129.207 140.507 1.00 135.25 ? 649  PRO B CG    1 
ATOM   10713 C  CD    . PRO B 1 649 ? 144.447 129.791 141.169 1.00 138.05 ? 649  PRO B CD    1 
ATOM   10714 N  N     . LYS B 1 650 ? 143.501 125.714 141.964 1.00 142.86 ? 650  LYS B N     1 
ATOM   10715 C  CA    . LYS B 1 650 ? 143.680 124.412 142.592 1.00 143.19 ? 650  LYS B CA    1 
ATOM   10716 C  C     . LYS B 1 650 ? 142.524 123.472 142.308 1.00 143.58 ? 650  LYS B C     1 
ATOM   10717 O  O     . LYS B 1 650 ? 142.718 122.255 142.260 1.00 143.33 ? 650  LYS B O     1 
ATOM   10718 C  CB    . LYS B 1 650 ? 143.849 124.569 144.110 1.00 145.12 ? 650  LYS B CB    1 
ATOM   10719 C  CG    . LYS B 1 650 ? 144.818 123.577 144.729 1.00 147.65 ? 650  LYS B CG    1 
ATOM   10720 N  N     . HIS B 1 651 ? 141.320 124.014 142.119 1.00 145.07 ? 651  HIS B N     1 
ATOM   10721 C  CA    . HIS B 1 651 ? 140.186 123.199 141.706 1.00 147.66 ? 651  HIS B CA    1 
ATOM   10722 C  C     . HIS B 1 651 ? 140.045 123.170 140.191 1.00 149.29 ? 651  HIS B C     1 
ATOM   10723 O  O     . HIS B 1 651 ? 139.292 122.350 139.653 1.00 154.32 ? 651  HIS B O     1 
ATOM   10724 C  CB    . HIS B 1 651 ? 138.909 123.727 142.352 1.00 146.86 ? 651  HIS B CB    1 
ATOM   10725 C  CG    . HIS B 1 651 ? 138.998 125.160 142.773 1.00 147.14 ? 651  HIS B CG    1 
ATOM   10726 N  ND1   . HIS B 1 651 ? 139.625 125.555 143.936 1.00 146.00 ? 651  HIS B ND1   1 
ATOM   10727 C  CD2   . HIS B 1 651 ? 138.544 126.293 142.188 1.00 146.13 ? 651  HIS B CD2   1 
ATOM   10728 C  CE1   . HIS B 1 651 ? 139.550 126.868 144.050 1.00 147.33 ? 651  HIS B CE1   1 
ATOM   10729 N  NE2   . HIS B 1 651 ? 138.900 127.341 143.002 1.00 149.33 ? 651  HIS B NE2   1 
ATOM   10730 N  N     . MET B 1 652 ? 140.760 124.052 139.490 1.00 144.42 ? 652  MET B N     1 
ATOM   10731 C  CA    . MET B 1 652 ? 140.803 124.058 138.034 1.00 139.44 ? 652  MET B CA    1 
ATOM   10732 C  C     . MET B 1 652 ? 141.992 123.285 137.490 1.00 136.02 ? 652  MET B C     1 
ATOM   10733 O  O     . MET B 1 652 ? 142.539 123.653 136.442 1.00 135.48 ? 652  MET B O     1 
ATOM   10734 C  CB    . MET B 1 652 ? 140.821 125.494 137.511 1.00 136.09 ? 652  MET B CB    1 
ATOM   10735 C  CG    . MET B 1 652 ? 139.966 126.448 138.311 1.00 137.13 ? 652  MET B CG    1 
ATOM   10736 S  SD    . MET B 1 652 ? 138.280 125.846 138.504 1.00 151.29 ? 652  MET B SD    1 
ATOM   10737 C  CE    . MET B 1 652 ? 137.747 125.776 136.796 1.00 137.50 ? 652  MET B CE    1 
ATOM   10738 N  N     . LYS B 1 653 ? 142.421 122.234 138.191 1.00 135.83 ? 653  LYS B N     1 
ATOM   10739 C  CA    . LYS B 1 653 ? 143.566 121.458 137.733 1.00 136.29 ? 653  LYS B CA    1 
ATOM   10740 C  C     . LYS B 1 653 ? 143.301 120.848 136.365 1.00 137.79 ? 653  LYS B C     1 
ATOM   10741 O  O     . LYS B 1 653 ? 144.166 120.886 135.484 1.00 138.55 ? 653  LYS B O     1 
ATOM   10742 C  CB    . LYS B 1 653 ? 143.905 120.371 138.752 1.00 137.99 ? 653  LYS B CB    1 
ATOM   10743 C  CG    . LYS B 1 653 ? 144.818 119.281 138.217 1.00 141.76 ? 653  LYS B CG    1 
ATOM   10744 C  CD    . LYS B 1 653 ? 144.918 118.116 139.188 1.00 144.21 ? 653  LYS B CD    1 
ATOM   10745 C  CE    . LYS B 1 653 ? 145.750 116.983 138.607 1.00 144.45 ? 653  LYS B CE    1 
ATOM   10746 N  NZ    . LYS B 1 653 ? 145.835 115.821 139.534 1.00 137.89 ? 653  LYS B NZ    1 
ATOM   10747 N  N     . LEU B 1 654 ? 142.102 120.297 136.161 1.00 136.85 ? 654  LEU B N     1 
ATOM   10748 C  CA    . LEU B 1 654 ? 141.779 119.689 134.874 1.00 135.37 ? 654  LEU B CA    1 
ATOM   10749 C  C     . LEU B 1 654 ? 141.762 120.723 133.755 1.00 134.48 ? 654  LEU B C     1 
ATOM   10750 O  O     . LEU B 1 654 ? 142.312 120.481 132.675 1.00 135.89 ? 654  LEU B O     1 
ATOM   10751 C  CB    . LEU B 1 654 ? 140.437 118.965 134.958 1.00 134.29 ? 654  LEU B CB    1 
ATOM   10752 C  CG    . LEU B 1 654 ? 140.462 117.621 135.687 1.00 139.46 ? 654  LEU B CG    1 
ATOM   10753 C  CD1   . LEU B 1 654 ? 139.102 116.947 135.615 1.00 144.82 ? 654  LEU B CD1   1 
ATOM   10754 C  CD2   . LEU B 1 654 ? 141.544 116.721 135.112 1.00 136.13 ? 654  LEU B CD2   1 
ATOM   10755 N  N     . THR B 1 655 ? 141.144 121.882 133.993 1.00 132.63 ? 655  THR B N     1 
ATOM   10756 C  CA    . THR B 1 655 ? 141.081 122.907 132.955 1.00 131.36 ? 655  THR B CA    1 
ATOM   10757 C  C     . THR B 1 655 ? 142.466 123.445 132.616 1.00 130.18 ? 655  THR B C     1 
ATOM   10758 O  O     . THR B 1 655 ? 142.798 123.629 131.437 1.00 131.35 ? 655  THR B O     1 
ATOM   10759 C  CB    . THR B 1 655 ? 140.164 124.045 133.393 1.00 128.83 ? 655  THR B CB    1 
ATOM   10760 O  OG1   . THR B 1 655 ? 139.008 123.505 134.044 1.00 133.59 ? 655  THR B OG1   1 
ATOM   10761 C  CG2   . THR B 1 655 ? 139.724 124.854 132.190 1.00 121.72 ? 655  THR B CG2   1 
ATOM   10762 N  N     . TYR B 1 656 ? 143.286 123.708 133.636 1.00 130.06 ? 656  TYR B N     1 
ATOM   10763 C  CA    . TYR B 1 656 ? 144.630 124.208 133.377 1.00 126.90 ? 656  TYR B CA    1 
ATOM   10764 C  C     . TYR B 1 656 ? 145.481 123.164 132.674 1.00 127.58 ? 656  TYR B C     1 
ATOM   10765 O  O     . TYR B 1 656 ? 146.270 123.500 131.786 1.00 128.05 ? 656  TYR B O     1 
ATOM   10766 C  CB    . TYR B 1 656 ? 145.296 124.658 134.674 1.00 124.14 ? 656  TYR B CB    1 
ATOM   10767 C  CG    . TYR B 1 656 ? 145.020 126.099 135.015 1.00 119.53 ? 656  TYR B CG    1 
ATOM   10768 C  CD1   . TYR B 1 656 ? 145.531 127.122 134.233 1.00 115.95 ? 656  TYR B CD1   1 
ATOM   10769 C  CD2   . TYR B 1 656 ? 144.260 126.437 136.120 1.00 122.21 ? 656  TYR B CD2   1 
ATOM   10770 C  CE1   . TYR B 1 656 ? 145.287 128.442 134.539 1.00 115.62 ? 656  TYR B CE1   1 
ATOM   10771 C  CE2   . TYR B 1 656 ? 144.012 127.753 136.433 1.00 121.46 ? 656  TYR B CE2   1 
ATOM   10772 C  CZ    . TYR B 1 656 ? 144.526 128.752 135.641 1.00 117.99 ? 656  TYR B CZ    1 
ATOM   10773 O  OH    . TYR B 1 656 ? 144.280 130.068 135.951 1.00 118.34 ? 656  TYR B OH    1 
ATOM   10774 N  N     . TYR B 1 657 ? 145.342 121.892 133.053 1.00 126.37 ? 657  TYR B N     1 
ATOM   10775 C  CA    . TYR B 1 657 ? 146.080 120.845 132.360 1.00 128.22 ? 657  TYR B CA    1 
ATOM   10776 C  C     . TYR B 1 657 ? 145.634 120.737 130.910 1.00 129.44 ? 657  TYR B C     1 
ATOM   10777 O  O     . TYR B 1 657 ? 146.459 120.524 130.019 1.00 133.10 ? 657  TYR B O     1 
ATOM   10778 C  CB    . TYR B 1 657 ? 145.910 119.508 133.079 1.00 133.77 ? 657  TYR B CB    1 
ATOM   10779 C  CG    . TYR B 1 657 ? 146.737 118.395 132.479 1.00 143.00 ? 657  TYR B CG    1 
ATOM   10780 C  CD1   . TYR B 1 657 ? 148.086 118.268 132.781 1.00 146.82 ? 657  TYR B CD1   1 
ATOM   10781 C  CD2   . TYR B 1 657 ? 146.172 117.472 131.608 1.00 142.96 ? 657  TYR B CD2   1 
ATOM   10782 C  CE1   . TYR B 1 657 ? 148.849 117.254 132.236 1.00 152.26 ? 657  TYR B CE1   1 
ATOM   10783 C  CE2   . TYR B 1 657 ? 146.927 116.454 131.057 1.00 144.11 ? 657  TYR B CE2   1 
ATOM   10784 C  CZ    . TYR B 1 657 ? 148.265 116.349 131.375 1.00 151.55 ? 657  TYR B CZ    1 
ATOM   10785 O  OH    . TYR B 1 657 ? 149.022 115.338 130.831 1.00 153.07 ? 657  TYR B OH    1 
ATOM   10786 N  N     . PHE B 1 658 ? 144.334 120.891 130.652 1.00 126.87 ? 658  PHE B N     1 
ATOM   10787 C  CA    . PHE B 1 658 ? 143.839 120.858 129.279 1.00 129.80 ? 658  PHE B CA    1 
ATOM   10788 C  C     . PHE B 1 658 ? 144.421 121.998 128.453 1.00 128.20 ? 658  PHE B C     1 
ATOM   10789 O  O     . PHE B 1 658 ? 144.904 121.786 127.334 1.00 127.76 ? 658  PHE B O     1 
ATOM   10790 C  CB    . PHE B 1 658 ? 142.313 120.918 129.274 1.00 132.24 ? 658  PHE B CB    1 
ATOM   10791 C  CG    . PHE B 1 658 ? 141.720 121.098 127.908 1.00 133.64 ? 658  PHE B CG    1 
ATOM   10792 C  CD1   . PHE B 1 658 ? 141.794 120.088 126.965 1.00 135.57 ? 658  PHE B CD1   1 
ATOM   10793 C  CD2   . PHE B 1 658 ? 141.082 122.279 127.569 1.00 130.70 ? 658  PHE B CD2   1 
ATOM   10794 C  CE1   . PHE B 1 658 ? 141.247 120.254 125.708 1.00 136.17 ? 658  PHE B CE1   1 
ATOM   10795 C  CE2   . PHE B 1 658 ? 140.533 122.451 126.315 1.00 132.76 ? 658  PHE B CE2   1 
ATOM   10796 C  CZ    . PHE B 1 658 ? 140.616 121.438 125.383 1.00 135.04 ? 658  PHE B CZ    1 
ATOM   10797 N  N     . VAL B 1 659 ? 144.384 123.219 128.989 1.00 126.76 ? 659  VAL B N     1 
ATOM   10798 C  CA    . VAL B 1 659 ? 144.904 124.365 128.245 1.00 123.67 ? 659  VAL B CA    1 
ATOM   10799 C  C     . VAL B 1 659 ? 146.406 124.224 128.030 1.00 124.96 ? 659  VAL B C     1 
ATOM   10800 O  O     . VAL B 1 659 ? 146.923 124.489 126.935 1.00 125.70 ? 659  VAL B O     1 
ATOM   10801 C  CB    . VAL B 1 659 ? 144.555 125.680 128.965 1.00 118.16 ? 659  VAL B CB    1 
ATOM   10802 C  CG1   . VAL B 1 659 ? 145.237 126.848 128.283 1.00 114.77 ? 659  VAL B CG1   1 
ATOM   10803 C  CG2   . VAL B 1 659 ? 143.054 125.884 128.988 1.00 119.30 ? 659  VAL B CG2   1 
ATOM   10804 N  N     . GLY B 1 660 ? 147.131 123.804 129.068 1.00 124.22 ? 660  GLY B N     1 
ATOM   10805 C  CA    . GLY B 1 660 ? 148.562 123.609 128.931 1.00 121.22 ? 660  GLY B CA    1 
ATOM   10806 C  C     . GLY B 1 660 ? 148.909 122.525 127.932 1.00 123.75 ? 660  GLY B C     1 
ATOM   10807 O  O     . GLY B 1 660 ? 149.870 122.656 127.177 1.00 123.71 ? 660  GLY B O     1 
ATOM   10808 N  N     . ALA B 1 661 ? 148.132 121.440 127.911 1.00 123.71 ? 661  ALA B N     1 
ATOM   10809 C  CA    . ALA B 1 661 ? 148.374 120.374 126.948 1.00 125.36 ? 661  ALA B CA    1 
ATOM   10810 C  C     . ALA B 1 661 ? 148.089 120.838 125.528 1.00 126.52 ? 661  ALA B C     1 
ATOM   10811 O  O     . ALA B 1 661 ? 148.819 120.487 124.596 1.00 128.54 ? 661  ALA B O     1 
ATOM   10812 C  CB    . ALA B 1 661 ? 147.527 119.151 127.295 1.00 126.80 ? 661  ALA B CB    1 
ATOM   10813 N  N     . VAL B 1 662 ? 147.030 121.630 125.342 1.00 124.89 ? 662  VAL B N     1 
ATOM   10814 C  CA    . VAL B 1 662 ? 146.730 122.161 124.015 1.00 124.14 ? 662  VAL B CA    1 
ATOM   10815 C  C     . VAL B 1 662 ? 147.867 123.052 123.533 1.00 125.18 ? 662  VAL B C     1 
ATOM   10816 O  O     . VAL B 1 662 ? 148.362 122.908 122.407 1.00 128.35 ? 662  VAL B O     1 
ATOM   10817 C  CB    . VAL B 1 662 ? 145.390 122.918 124.029 1.00 121.68 ? 662  VAL B CB    1 
ATOM   10818 C  CG1   . VAL B 1 662 ? 145.244 123.756 122.773 1.00 116.81 ? 662  VAL B CG1   1 
ATOM   10819 C  CG2   . VAL B 1 662 ? 144.238 121.942 124.150 1.00 127.04 ? 662  VAL B CG2   1 
ATOM   10820 N  N     . PHE B 1 663 ? 148.312 123.975 124.388 1.00 121.83 ? 663  PHE B N     1 
ATOM   10821 C  CA    . PHE B 1 663 ? 149.409 124.860 124.010 1.00 120.00 ? 663  PHE B CA    1 
ATOM   10822 C  C     . PHE B 1 663 ? 150.697 124.080 123.775 1.00 121.43 ? 663  PHE B C     1 
ATOM   10823 O  O     . PHE B 1 663 ? 151.455 124.382 122.845 1.00 123.79 ? 663  PHE B O     1 
ATOM   10824 C  CB    . PHE B 1 663 ? 149.609 125.930 125.081 1.00 118.52 ? 663  PHE B CB    1 
ATOM   10825 C  CG    . PHE B 1 663 ? 148.621 127.057 125.003 1.00 114.74 ? 663  PHE B CG    1 
ATOM   10826 C  CD1   . PHE B 1 663 ? 147.790 127.192 123.907 1.00 114.79 ? 663  PHE B CD1   1 
ATOM   10827 C  CD2   . PHE B 1 663 ? 148.524 127.984 126.026 1.00 113.36 ? 663  PHE B CD2   1 
ATOM   10828 C  CE1   . PHE B 1 663 ? 146.883 128.228 123.833 1.00 115.89 ? 663  PHE B CE1   1 
ATOM   10829 C  CE2   . PHE B 1 663 ? 147.618 129.021 125.955 1.00 109.98 ? 663  PHE B CE2   1 
ATOM   10830 C  CZ    . PHE B 1 663 ? 146.797 129.143 124.858 1.00 111.15 ? 663  PHE B CZ    1 
ATOM   10831 N  N     . GLY B 1 664 ? 150.958 123.066 124.599 1.00 118.79 ? 664  GLY B N     1 
ATOM   10832 C  CA    . GLY B 1 664 ? 152.153 122.266 124.414 1.00 121.58 ? 664  GLY B CA    1 
ATOM   10833 C  C     . GLY B 1 664 ? 152.145 121.499 123.109 1.00 127.34 ? 664  GLY B C     1 
ATOM   10834 O  O     . GLY B 1 664 ? 153.151 121.463 122.400 1.00 130.25 ? 664  GLY B O     1 
ATOM   10835 N  N     . LEU B 1 665 ? 151.013 120.878 122.770 1.00 125.62 ? 665  LEU B N     1 
ATOM   10836 C  CA    . LEU B 1 665 ? 150.911 120.176 121.497 1.00 126.30 ? 665  LEU B CA    1 
ATOM   10837 C  C     . LEU B 1 665 ? 151.063 121.143 120.332 1.00 124.12 ? 665  LEU B C     1 
ATOM   10838 O  O     . LEU B 1 665 ? 151.715 120.825 119.328 1.00 127.82 ? 665  LEU B O     1 
ATOM   10839 C  CB    . LEU B 1 665 ? 149.580 119.430 121.415 1.00 127.21 ? 665  LEU B CB    1 
ATOM   10840 C  CG    . LEU B 1 665 ? 149.478 118.170 122.275 1.00 131.32 ? 665  LEU B CG    1 
ATOM   10841 C  CD1   . LEU B 1 665 ? 148.113 117.521 122.120 1.00 132.54 ? 665  LEU B CD1   1 
ATOM   10842 C  CD2   . LEU B 1 665 ? 150.586 117.191 121.924 1.00 133.87 ? 665  LEU B CD2   1 
ATOM   10843 N  N     . MET B 1 666 ? 150.480 122.338 120.456 1.00 118.92 ? 666  MET B N     1 
ATOM   10844 C  CA    . MET B 1 666 ? 150.636 123.340 119.409 1.00 118.61 ? 666  MET B CA    1 
ATOM   10845 C  C     . MET B 1 666 ? 152.097 123.731 119.237 1.00 122.48 ? 666  MET B C     1 
ATOM   10846 O  O     . MET B 1 666 ? 152.568 123.918 118.110 1.00 126.65 ? 666  MET B O     1 
ATOM   10847 C  CB    . MET B 1 666 ? 149.776 124.562 119.725 1.00 115.55 ? 666  MET B CB    1 
ATOM   10848 C  CG    . MET B 1 666 ? 150.172 125.822 118.985 1.00 115.22 ? 666  MET B CG    1 
ATOM   10849 S  SD    . MET B 1 666 ? 149.427 127.290 119.712 1.00 118.34 ? 666  MET B SD    1 
ATOM   10850 C  CE    . MET B 1 666 ? 147.704 126.802 119.748 1.00 109.70 ? 666  MET B CE    1 
ATOM   10851 N  N     . MET B 1 667 ? 152.845 123.832 120.337 1.00 119.28 ? 667  MET B N     1 
ATOM   10852 C  CA    . MET B 1 667 ? 154.245 124.228 120.204 1.00 116.40 ? 667  MET B CA    1 
ATOM   10853 C  C     . MET B 1 667 ? 155.133 123.078 119.746 1.00 120.52 ? 667  MET B C     1 
ATOM   10854 O  O     . MET B 1 667 ? 156.162 123.318 119.115 1.00 126.34 ? 667  MET B O     1 
ATOM   10855 C  CB    . MET B 1 667 ? 154.770 124.836 121.497 1.00 109.83 ? 667  MET B CB    1 
ATOM   10856 C  CG    . MET B 1 667 ? 154.381 126.282 121.636 1.00 111.85 ? 667  MET B CG    1 
ATOM   10857 S  SD    . MET B 1 667 ? 155.513 127.394 120.788 1.00 126.09 ? 667  MET B SD    1 
ATOM   10858 C  CE    . MET B 1 667 ? 157.081 126.855 121.453 1.00 110.72 ? 667  MET B CE    1 
ATOM   10859 N  N     . MET B 1 668 ? 154.776 121.826 120.042 1.00 118.64 ? 668  MET B N     1 
ATOM   10860 C  CA    . MET B 1 668 ? 155.502 120.728 119.403 1.00 120.73 ? 668  MET B CA    1 
ATOM   10861 C  C     . MET B 1 668 ? 155.260 120.718 117.901 1.00 122.19 ? 668  MET B C     1 
ATOM   10862 O  O     . MET B 1 668 ? 156.192 120.506 117.112 1.00 122.17 ? 668  MET B O     1 
ATOM   10863 C  CB    . MET B 1 668 ? 155.133 119.370 120.004 1.00 123.71 ? 668  MET B CB    1 
ATOM   10864 C  CG    . MET B 1 668 ? 154.941 119.341 121.497 1.00 128.17 ? 668  MET B CG    1 
ATOM   10865 S  SD    . MET B 1 668 ? 156.458 119.703 122.398 1.00 137.06 ? 668  MET B SD    1 
ATOM   10866 C  CE    . MET B 1 668 ? 157.657 118.756 121.465 1.00 131.30 ? 668  MET B CE    1 
ATOM   10867 N  N     . LEU B 1 669 ? 154.014 120.954 117.484 1.00 119.69 ? 669  LEU B N     1 
ATOM   10868 C  CA    . LEU B 1 669 ? 153.738 121.094 116.060 1.00 117.81 ? 669  LEU B CA    1 
ATOM   10869 C  C     . LEU B 1 669 ? 154.558 122.229 115.461 1.00 119.96 ? 669  LEU B C     1 
ATOM   10870 O  O     . LEU B 1 669 ? 155.174 122.071 114.400 1.00 123.08 ? 669  LEU B O     1 
ATOM   10871 C  CB    . LEU B 1 669 ? 152.245 121.329 115.843 1.00 115.55 ? 669  LEU B CB    1 
ATOM   10872 C  CG    . LEU B 1 669 ? 151.792 121.709 114.434 1.00 117.24 ? 669  LEU B CG    1 
ATOM   10873 C  CD1   . LEU B 1 669 ? 152.047 120.570 113.465 1.00 116.93 ? 669  LEU B CD1   1 
ATOM   10874 C  CD2   . LEU B 1 669 ? 150.324 122.099 114.438 1.00 117.08 ? 669  LEU B CD2   1 
ATOM   10875 N  N     . SER B 1 670 ? 154.605 123.370 116.151 1.00 116.56 ? 670  SER B N     1 
ATOM   10876 C  CA    . SER B 1 670 ? 155.368 124.513 115.665 1.00 115.66 ? 670  SER B CA    1 
ATOM   10877 C  C     . SER B 1 670 ? 156.859 124.210 115.614 1.00 119.92 ? 670  SER B C     1 
ATOM   10878 O  O     . SER B 1 670 ? 157.556 124.660 114.702 1.00 125.30 ? 670  SER B O     1 
ATOM   10879 C  CB    . SER B 1 670 ? 155.102 125.731 116.545 1.00 113.21 ? 670  SER B CB    1 
ATOM   10880 O  OG    . SER B 1 670 ? 153.720 126.034 116.594 1.00 116.10 ? 670  SER B OG    1 
ATOM   10881 N  N     . SER B 1 671 ? 157.371 123.465 116.593 1.00 118.38 ? 671  SER B N     1 
ATOM   10882 C  CA    . SER B 1 671 ? 158.794 123.151 116.628 1.00 120.30 ? 671  SER B CA    1 
ATOM   10883 C  C     . SER B 1 671 ? 159.184 122.223 115.488 1.00 123.83 ? 671  SER B C     1 
ATOM   10884 O  O     . SER B 1 671 ? 160.214 122.430 114.838 1.00 130.19 ? 671  SER B O     1 
ATOM   10885 C  CB    . SER B 1 671 ? 159.157 122.532 117.975 1.00 118.43 ? 671  SER B CB    1 
ATOM   10886 O  OG    . SER B 1 671 ? 158.439 123.157 119.023 1.00 125.22 ? 671  SER B OG    1 
ATOM   10887 N  N     . LEU B 1 672 ? 158.375 121.193 115.225 1.00 118.74 ? 672  LEU B N     1 
ATOM   10888 C  CA    . LEU B 1 672 ? 158.658 120.343 114.070 1.00 121.26 ? 672  LEU B CA    1 
ATOM   10889 C  C     . LEU B 1 672 ? 158.527 121.114 112.761 1.00 122.26 ? 672  LEU B C     1 
ATOM   10890 O  O     . LEU B 1 672 ? 159.329 120.918 111.839 1.00 125.72 ? 672  LEU B O     1 
ATOM   10891 C  CB    . LEU B 1 672 ? 157.766 119.101 114.068 1.00 123.88 ? 672  LEU B CB    1 
ATOM   10892 C  CG    . LEU B 1 672 ? 158.224 117.930 114.949 1.00 123.83 ? 672  LEU B CG    1 
ATOM   10893 C  CD1   . LEU B 1 672 ? 159.717 117.691 114.761 1.00 122.49 ? 672  LEU B CD1   1 
ATOM   10894 C  CD2   . LEU B 1 672 ? 157.908 118.115 116.417 1.00 118.51 ? 672  LEU B CD2   1 
ATOM   10895 N  N     . VAL B 1 673 ? 157.539 122.007 112.660 1.00 119.73 ? 673  VAL B N     1 
ATOM   10896 C  CA    . VAL B 1 673 ? 157.405 122.816 111.449 1.00 120.05 ? 673  VAL B CA    1 
ATOM   10897 C  C     . VAL B 1 673 ? 158.623 123.715 111.262 1.00 124.86 ? 673  VAL B C     1 
ATOM   10898 O  O     . VAL B 1 673 ? 159.155 123.842 110.152 1.00 131.40 ? 673  VAL B O     1 
ATOM   10899 C  CB    . VAL B 1 673 ? 156.097 123.627 111.489 1.00 114.47 ? 673  VAL B CB    1 
ATOM   10900 C  CG1   . VAL B 1 673 ? 156.078 124.656 110.376 1.00 116.89 ? 673  VAL B CG1   1 
ATOM   10901 C  CG2   . VAL B 1 673 ? 154.907 122.697 111.353 1.00 116.42 ? 673  VAL B CG2   1 
ATOM   10902 N  N     . GLY B 1 674 ? 159.086 124.348 112.339 1.00 121.23 ? 674  GLY B N     1 
ATOM   10903 C  CA    . GLY B 1 674 ? 160.254 125.207 112.241 1.00 122.98 ? 674  GLY B CA    1 
ATOM   10904 C  C     . GLY B 1 674 ? 161.517 124.441 111.902 1.00 129.13 ? 674  GLY B C     1 
ATOM   10905 O  O     . GLY B 1 674 ? 162.346 124.908 111.118 1.00 134.71 ? 674  GLY B O     1 
ATOM   10906 N  N     . ALA B 1 675 ? 161.684 123.256 112.493 1.00 124.85 ? 675  ALA B N     1 
ATOM   10907 C  CA    . ALA B 1 675 ? 162.831 122.422 112.155 1.00 126.07 ? 675  ALA B CA    1 
ATOM   10908 C  C     . ALA B 1 675 ? 162.796 122.016 110.689 1.00 131.51 ? 675  ALA B C     1 
ATOM   10909 O  O     . ALA B 1 675 ? 163.826 122.042 110.004 1.00 135.14 ? 675  ALA B O     1 
ATOM   10910 C  CB    . ALA B 1 675 ? 162.867 121.188 113.054 1.00 119.20 ? 675  ALA B CB    1 
ATOM   10911 N  N     . GLY B 1 676 ? 161.616 121.644 110.187 1.00 129.55 ? 676  GLY B N     1 
ATOM   10912 C  CA    . GLY B 1 676 ? 161.496 121.317 108.777 1.00 131.60 ? 676  GLY B CA    1 
ATOM   10913 C  C     . GLY B 1 676 ? 161.825 122.492 107.877 1.00 134.58 ? 676  GLY B C     1 
ATOM   10914 O  O     . GLY B 1 676 ? 162.520 122.339 106.870 1.00 138.63 ? 676  GLY B O     1 
ATOM   10915 N  N     . ILE B 1 677 ? 161.334 123.683 108.231 1.00 131.57 ? 677  ILE B N     1 
ATOM   10916 C  CA    . ILE B 1 677 ? 161.635 124.874 107.440 1.00 133.26 ? 677  ILE B CA    1 
ATOM   10917 C  C     . ILE B 1 677 ? 163.134 125.139 107.424 1.00 138.43 ? 677  ILE B C     1 
ATOM   10918 O  O     . ILE B 1 677 ? 163.727 125.388 106.366 1.00 144.87 ? 677  ILE B O     1 
ATOM   10919 C  CB    . ILE B 1 677 ? 160.860 126.089 107.979 1.00 126.58 ? 677  ILE B CB    1 
ATOM   10920 C  CG1   . ILE B 1 677 ? 159.358 125.907 107.780 1.00 126.11 ? 677  ILE B CG1   1 
ATOM   10921 C  CG2   . ILE B 1 677 ? 161.330 127.362 107.303 1.00 129.54 ? 677  ILE B CG2   1 
ATOM   10922 C  CD1   . ILE B 1 677 ? 158.538 127.030 108.368 1.00 122.89 ? 677  ILE B CD1   1 
ATOM   10923 N  N     . PHE B 1 678 ? 163.772 125.076 108.594 1.00 136.51 ? 678  PHE B N     1 
ATOM   10924 C  CA    . PHE B 1 678 ? 165.196 125.375 108.676 1.00 139.41 ? 678  PHE B CA    1 
ATOM   10925 C  C     . PHE B 1 678 ? 166.028 124.349 107.918 1.00 143.37 ? 678  PHE B C     1 
ATOM   10926 O  O     . PHE B 1 678 ? 167.033 124.699 107.288 1.00 142.93 ? 678  PHE B O     1 
ATOM   10927 C  CB    . PHE B 1 678 ? 165.633 125.453 110.137 1.00 134.00 ? 678  PHE B CB    1 
ATOM   10928 C  CG    . PHE B 1 678 ? 167.081 125.794 110.314 1.00 136.74 ? 678  PHE B CG    1 
ATOM   10929 C  CD1   . PHE B 1 678 ? 167.535 127.081 110.090 1.00 138.03 ? 678  PHE B CD1   1 
ATOM   10930 C  CD2   . PHE B 1 678 ? 167.989 124.828 110.711 1.00 138.85 ? 678  PHE B CD2   1 
ATOM   10931 C  CE1   . PHE B 1 678 ? 168.868 127.394 110.246 1.00 136.44 ? 678  PHE B CE1   1 
ATOM   10932 C  CE2   . PHE B 1 678 ? 169.323 125.138 110.874 1.00 140.99 ? 678  PHE B CE2   1 
ATOM   10933 C  CZ    . PHE B 1 678 ? 169.763 126.423 110.642 1.00 136.26 ? 678  PHE B CZ    1 
ATOM   10934 N  N     . PHE B 1 679 ? 165.632 123.075 107.965 1.00 142.45 ? 679  PHE B N     1 
ATOM   10935 C  CA    . PHE B 1 679 ? 166.406 122.050 107.272 1.00 141.96 ? 679  PHE B CA    1 
ATOM   10936 C  C     . PHE B 1 679 ? 166.182 122.089 105.765 1.00 144.75 ? 679  PHE B C     1 
ATOM   10937 O  O     . PHE B 1 679 ? 167.115 121.827 104.998 1.00 149.27 ? 679  PHE B O     1 
ATOM   10938 C  CB    . PHE B 1 679 ? 166.076 120.665 107.829 1.00 136.39 ? 679  PHE B CB    1 
ATOM   10939 C  CG    . PHE B 1 679 ? 166.519 120.455 109.255 1.00 138.61 ? 679  PHE B CG    1 
ATOM   10940 C  CD1   . PHE B 1 679 ? 167.164 121.460 109.959 1.00 135.18 ? 679  PHE B CD1   1 
ATOM   10941 C  CD2   . PHE B 1 679 ? 166.290 119.246 109.890 1.00 142.68 ? 679  PHE B CD2   1 
ATOM   10942 C  CE1   . PHE B 1 679 ? 167.568 121.265 111.263 1.00 136.45 ? 679  PHE B CE1   1 
ATOM   10943 C  CE2   . PHE B 1 679 ? 166.693 119.045 111.196 1.00 143.73 ? 679  PHE B CE2   1 
ATOM   10944 C  CZ    . PHE B 1 679 ? 167.333 120.057 111.883 1.00 142.85 ? 679  PHE B CZ    1 
ATOM   10945 N  N     . SER B 1 680 ? 164.965 122.410 105.317 1.00 140.20 ? 680  SER B N     1 
ATOM   10946 C  CA    . SER B 1 680 ? 164.704 122.487 103.885 1.00 139.57 ? 680  SER B CA    1 
ATOM   10947 C  C     . SER B 1 680 ? 165.261 123.757 103.259 1.00 147.93 ? 680  SER B C     1 
ATOM   10948 O  O     . SER B 1 680 ? 165.552 123.762 102.059 1.00 153.00 ? 680  SER B O     1 
ATOM   10949 C  CB    . SER B 1 680 ? 163.204 122.388 103.621 1.00 139.23 ? 680  SER B CB    1 
ATOM   10950 O  OG    . SER B 1 680 ? 162.695 121.153 104.089 1.00 144.16 ? 680  SER B OG    1 
ATOM   10951 N  N     . THR B 1 681 ? 165.405 124.828 104.036 1.00 150.02 ? 681  THR B N     1 
ATOM   10952 C  CA    . THR B 1 681 ? 166.024 126.040 103.526 1.00 153.51 ? 681  THR B CA    1 
ATOM   10953 C  C     . THR B 1 681 ? 167.465 125.743 103.107 1.00 158.44 ? 681  THR B C     1 
ATOM   10954 O  O     . THR B 1 681 ? 168.161 124.965 103.766 1.00 157.14 ? 681  THR B O     1 
ATOM   10955 C  CB    . THR B 1 681 ? 165.998 127.131 104.598 1.00 149.23 ? 681  THR B CB    1 
ATOM   10956 O  OG1   . THR B 1 681 ? 164.721 127.130 105.247 1.00 147.63 ? 681  THR B OG1   1 
ATOM   10957 C  CG2   . THR B 1 681 ? 166.236 128.506 103.995 1.00 149.53 ? 681  THR B CG2   1 
ATOM   10958 N  N     . PRO B 1 682 ? 167.944 126.348 102.012 1.00 159.11 ? 682  PRO B N     1 
ATOM   10959 C  CA    . PRO B 1 682 ? 169.317 126.067 101.562 1.00 158.03 ? 682  PRO B CA    1 
ATOM   10960 C  C     . PRO B 1 682 ? 170.399 126.612 102.485 1.00 159.54 ? 682  PRO B C     1 
ATOM   10961 O  O     . PRO B 1 682 ? 171.580 126.613 102.121 1.00 157.72 ? 682  PRO B O     1 
ATOM   10962 C  CB    . PRO B 1 682 ? 169.373 126.729 100.177 1.00 156.56 ? 682  PRO B CB    1 
ATOM   10963 C  CG    . PRO B 1 682 ? 168.265 127.728 100.177 1.00 152.38 ? 682  PRO B CG    1 
ATOM   10964 C  CD    . PRO B 1 682 ? 167.186 127.111 101.007 1.00 153.02 ? 682  PRO B CD    1 
ATOM   10965 N  N     . ALA B 1 683 ? 170.008 127.079 103.673 1.00 160.49 ? 683  ALA B N     1 
ATOM   10966 C  CA    . ALA B 1 683 ? 170.929 127.412 104.761 1.00 155.56 ? 683  ALA B CA    1 
ATOM   10967 C  C     . ALA B 1 683 ? 171.946 128.473 104.327 1.00 154.85 ? 683  ALA B C     1 
ATOM   10968 O  O     . ALA B 1 683 ? 173.156 128.247 104.283 1.00 156.74 ? 683  ALA B O     1 
ATOM   10969 C  CB    . ALA B 1 683 ? 171.634 126.153 105.281 1.00 155.48 ? 683  ALA B CB    1 
ATOM   10970 N  N     . THR B 1 684 ? 171.412 129.647 104.005 1.00 150.27 ? 684  THR B N     1 
ATOM   10971 C  CA    . THR B 1 684 ? 172.267 130.775 103.675 1.00 146.74 ? 684  THR B CA    1 
ATOM   10972 C  C     . THR B 1 684 ? 172.986 131.278 104.925 1.00 142.64 ? 684  THR B C     1 
ATOM   10973 O  O     . THR B 1 684 ? 172.639 130.930 106.058 1.00 139.95 ? 684  THR B O     1 
ATOM   10974 C  CB    . THR B 1 684 ? 171.456 131.901 103.035 1.00 144.22 ? 684  THR B CB    1 
ATOM   10975 O  OG1   . THR B 1 684 ? 172.231 133.107 103.025 1.00 142.75 ? 684  THR B OG1   1 
ATOM   10976 C  CG2   . THR B 1 684 ? 170.166 132.137 103.798 1.00 141.96 ? 684  THR B CG2   1 
ATOM   10977 N  N     . VAL B 1 685 ? 174.011 132.105 104.699 1.00 142.23 ? 685  VAL B N     1 
ATOM   10978 C  CA    . VAL B 1 685 ? 174.884 132.542 105.787 1.00 141.45 ? 685  VAL B CA    1 
ATOM   10979 C  C     . VAL B 1 685 ? 174.095 133.328 106.826 1.00 134.02 ? 685  VAL B C     1 
ATOM   10980 O  O     . VAL B 1 685 ? 174.251 133.127 108.037 1.00 132.29 ? 685  VAL B O     1 
ATOM   10981 C  CB    . VAL B 1 685 ? 176.060 133.364 105.232 1.00 142.88 ? 685  VAL B CB    1 
ATOM   10982 C  CG1   . VAL B 1 685 ? 176.941 133.860 106.366 1.00 134.83 ? 685  VAL B CG1   1 
ATOM   10983 C  CG2   . VAL B 1 685 ? 176.865 132.533 104.246 1.00 147.79 ? 685  VAL B CG2   1 
ATOM   10984 N  N     . HIS B 1 686 ? 173.237 134.241 106.367 1.00 133.81 ? 686  HIS B N     1 
ATOM   10985 C  CA    . HIS B 1 686 ? 172.410 135.000 107.297 1.00 133.84 ? 686  HIS B CA    1 
ATOM   10986 C  C     . HIS B 1 686 ? 171.502 134.078 108.097 1.00 129.91 ? 686  HIS B C     1 
ATOM   10987 O  O     . HIS B 1 686 ? 171.338 134.255 109.310 1.00 126.33 ? 686  HIS B O     1 
ATOM   10988 C  CB    . HIS B 1 686 ? 171.588 136.040 106.538 1.00 139.63 ? 686  HIS B CB    1 
ATOM   10989 C  CG    . HIS B 1 686 ? 170.456 136.613 107.333 1.00 141.66 ? 686  HIS B CG    1 
ATOM   10990 N  ND1   . HIS B 1 686 ? 170.603 137.712 108.151 1.00 141.61 ? 686  HIS B ND1   1 
ATOM   10991 C  CD2   . HIS B 1 686 ? 169.158 136.243 107.429 1.00 140.52 ? 686  HIS B CD2   1 
ATOM   10992 C  CE1   . HIS B 1 686 ? 169.444 137.992 108.720 1.00 140.54 ? 686  HIS B CE1   1 
ATOM   10993 N  NE2   . HIS B 1 686 ? 168.550 137.116 108.299 1.00 141.19 ? 686  HIS B NE2   1 
ATOM   10994 N  N     . SER B 1 687 ? 170.913 133.079 107.437 1.00 134.06 ? 687  SER B N     1 
ATOM   10995 C  CA    . SER B 1 687 ? 170.009 132.166 108.127 1.00 134.53 ? 687  SER B CA    1 
ATOM   10996 C  C     . SER B 1 687 ? 170.737 131.374 109.205 1.00 131.32 ? 687  SER B C     1 
ATOM   10997 O  O     . SER B 1 687 ? 170.242 131.243 110.329 1.00 127.71 ? 687  SER B O     1 
ATOM   10998 C  CB    . SER B 1 687 ? 169.347 131.221 107.126 1.00 141.45 ? 687  SER B CB    1 
ATOM   10999 O  OG    . SER B 1 687 ? 168.617 130.208 107.795 1.00 143.61 ? 687  SER B OG    1 
ATOM   11000 N  N     . ILE B 1 688 ? 171.919 130.838 108.887 1.00 131.58 ? 688  ILE B N     1 
ATOM   11001 C  CA    . ILE B 1 688 ? 172.619 130.023 109.876 1.00 127.47 ? 688  ILE B CA    1 
ATOM   11002 C  C     . ILE B 1 688 ? 173.119 130.893 111.023 1.00 120.80 ? 688  ILE B C     1 
ATOM   11003 O  O     . ILE B 1 688 ? 173.052 130.493 112.192 1.00 117.29 ? 688  ILE B O     1 
ATOM   11004 C  CB    . ILE B 1 688 ? 173.760 129.211 109.232 1.00 129.05 ? 688  ILE B CB    1 
ATOM   11005 C  CG1   . ILE B 1 688 ? 174.678 128.630 110.308 1.00 128.10 ? 688  ILE B CG1   1 
ATOM   11006 C  CG2   . ILE B 1 688 ? 174.588 130.061 108.311 1.00 128.80 ? 688  ILE B CG2   1 
ATOM   11007 C  CD1   . ILE B 1 688 ? 175.574 127.520 109.807 1.00 127.02 ? 688  ILE B CD1   1 
ATOM   11008 N  N     . VAL B 1 689 ? 173.604 132.101 110.720 1.00 121.32 ? 689  VAL B N     1 
ATOM   11009 C  CA    . VAL B 1 689 ? 174.067 132.993 111.780 1.00 115.32 ? 689  VAL B CA    1 
ATOM   11010 C  C     . VAL B 1 689 ? 172.914 133.358 112.708 1.00 112.73 ? 689  VAL B C     1 
ATOM   11011 O  O     . VAL B 1 689 ? 173.051 133.323 113.936 1.00 114.15 ? 689  VAL B O     1 
ATOM   11012 C  CB    . VAL B 1 689 ? 174.732 134.245 111.180 1.00 114.73 ? 689  VAL B CB    1 
ATOM   11013 C  CG1   . VAL B 1 689 ? 174.583 135.433 112.116 1.00 103.23 ? 689  VAL B CG1   1 
ATOM   11014 C  CG2   . VAL B 1 689 ? 176.200 133.973 110.903 1.00 121.92 ? 689  VAL B CG2   1 
ATOM   11015 N  N     . VAL B 1 690 ? 171.756 133.699 112.137 1.00 115.12 ? 690  VAL B N     1 
ATOM   11016 C  CA    . VAL B 1 690 ? 170.610 134.070 112.961 1.00 114.66 ? 690  VAL B CA    1 
ATOM   11017 C  C     . VAL B 1 690 ? 170.134 132.881 113.784 1.00 112.76 ? 690  VAL B C     1 
ATOM   11018 O  O     . VAL B 1 690 ? 169.815 133.020 114.968 1.00 111.50 ? 690  VAL B O     1 
ATOM   11019 C  CB    . VAL B 1 690 ? 169.481 134.647 112.086 1.00 120.75 ? 690  VAL B CB    1 
ATOM   11020 C  CG1   . VAL B 1 690 ? 168.124 134.391 112.721 1.00 108.58 ? 690  VAL B CG1   1 
ATOM   11021 C  CG2   . VAL B 1 690 ? 169.693 136.135 111.875 1.00 123.10 ? 690  VAL B CG2   1 
ATOM   11022 N  N     . SER B 1 691 ? 170.077 131.693 113.177 1.00 114.96 ? 691  SER B N     1 
ATOM   11023 C  CA    . SER B 1 691 ? 169.612 130.519 113.907 1.00 115.43 ? 691  SER B CA    1 
ATOM   11024 C  C     . SER B 1 691 ? 170.537 130.197 115.070 1.00 109.72 ? 691  SER B C     1 
ATOM   11025 O  O     . SER B 1 691 ? 170.078 129.934 116.188 1.00 108.41 ? 691  SER B O     1 
ATOM   11026 C  CB    . SER B 1 691 ? 169.502 129.324 112.965 1.00 125.63 ? 691  SER B CB    1 
ATOM   11027 O  OG    . SER B 1 691 ? 169.235 128.136 113.687 1.00 128.14 ? 691  SER B OG    1 
ATOM   11028 N  N     . ILE B 1 692 ? 171.850 130.221 114.827 1.00 110.43 ? 692  ILE B N     1 
ATOM   11029 C  CA    . ILE B 1 692 ? 172.809 130.021 115.908 1.00 109.28 ? 692  ILE B CA    1 
ATOM   11030 C  C     . ILE B 1 692 ? 172.572 131.054 117.000 1.00 107.14 ? 692  ILE B C     1 
ATOM   11031 O  O     . ILE B 1 692 ? 172.174 130.714 118.118 1.00 109.08 ? 692  ILE B O     1 
ATOM   11032 C  CB    . ILE B 1 692 ? 174.251 130.079 115.368 1.00 108.47 ? 692  ILE B CB    1 
ATOM   11033 C  CG1   . ILE B 1 692 ? 174.709 128.690 114.930 1.00 109.04 ? 692  ILE B CG1   1 
ATOM   11034 C  CG2   . ILE B 1 692 ? 175.216 130.592 116.424 1.00 100.08 ? 692  ILE B CG2   1 
ATOM   11035 C  CD1   . ILE B 1 692 ? 176.114 128.665 114.374 1.00 107.63 ? 692  ILE B CD1   1 
ATOM   11036 N  N     . LEU B 1 693 ? 172.683 132.335 116.642 1.00 104.58 ? 693  LEU B N     1 
ATOM   11037 C  CA    . LEU B 1 693 ? 172.643 133.448 117.576 1.00 103.77 ? 693  LEU B CA    1 
ATOM   11038 C  C     . LEU B 1 693 ? 171.304 133.580 118.284 1.00 106.94 ? 693  LEU B C     1 
ATOM   11039 O  O     . LEU B 1 693 ? 171.215 134.317 119.270 1.00 106.79 ? 693  LEU B O     1 
ATOM   11040 C  CB    . LEU B 1 693 ? 172.963 134.729 116.810 1.00 106.58 ? 693  LEU B CB    1 
ATOM   11041 C  CG    . LEU B 1 693 ? 173.913 135.762 117.395 1.00 106.51 ? 693  LEU B CG    1 
ATOM   11042 C  CD1   . LEU B 1 693 ? 175.313 135.193 117.437 1.00 106.59 ? 693  LEU B CD1   1 
ATOM   11043 C  CD2   . LEU B 1 693 ? 173.890 136.984 116.510 1.00 107.00 ? 693  LEU B CD2   1 
ATOM   11044 N  N     . THR B 1 694 ? 170.262 132.909 117.795 1.00 109.66 ? 694  THR B N     1 
ATOM   11045 C  CA    . THR B 1 694 ? 168.949 132.978 118.416 1.00 107.54 ? 694  THR B CA    1 
ATOM   11046 C  C     . THR B 1 694 ? 168.662 131.764 119.295 1.00 106.16 ? 694  THR B C     1 
ATOM   11047 O  O     . THR B 1 694 ? 168.321 131.921 120.470 1.00 108.98 ? 694  THR B O     1 
ATOM   11048 C  CB    . THR B 1 694 ? 167.871 133.124 117.337 1.00 108.90 ? 694  THR B CB    1 
ATOM   11049 O  OG1   . THR B 1 694 ? 167.810 134.489 116.908 1.00 114.15 ? 694  THR B OG1   1 
ATOM   11050 C  CG2   . THR B 1 694 ? 166.512 132.721 117.877 1.00 102.77 ? 694  THR B CG2   1 
ATOM   11051 N  N     . VAL B 1 695 ? 168.804 130.554 118.760 1.00 104.46 ? 695  VAL B N     1 
ATOM   11052 C  CA    . VAL B 1 695 ? 168.432 129.349 119.486 1.00 102.24 ? 695  VAL B CA    1 
ATOM   11053 C  C     . VAL B 1 695 ? 169.646 128.646 120.077 1.00 107.05 ? 695  VAL B C     1 
ATOM   11054 O  O     . VAL B 1 695 ? 169.621 128.239 121.238 1.00 111.69 ? 695  VAL B O     1 
ATOM   11055 C  CB    . VAL B 1 695 ? 167.634 128.394 118.574 1.00 101.92 ? 695  VAL B CB    1 
ATOM   11056 C  CG1   . VAL B 1 695 ? 167.387 127.073 119.280 1.00 100.29 ? 695  VAL B CG1   1 
ATOM   11057 C  CG2   . VAL B 1 695 ? 166.322 129.031 118.163 1.00 106.17 ? 695  VAL B CG2   1 
ATOM   11058 N  N     . GLY B 1 696 ? 170.721 128.497 119.306 1.00 107.27 ? 696  GLY B N     1 
ATOM   11059 C  CA    . GLY B 1 696 ? 171.851 127.758 119.813 1.00 109.82 ? 696  GLY B CA    1 
ATOM   11060 C  C     . GLY B 1 696 ? 172.675 128.505 120.826 1.00 109.87 ? 696  GLY B C     1 
ATOM   11061 O  O     . GLY B 1 696 ? 173.695 127.984 121.283 1.00 110.06 ? 696  GLY B O     1 
ATOM   11062 N  N     . VAL B 1 697 ? 172.270 129.729 121.170 1.00 107.14 ? 697  VAL B N     1 
ATOM   11063 C  CA    . VAL B 1 697 ? 172.956 130.478 122.216 1.00 106.75 ? 697  VAL B CA    1 
ATOM   11064 C  C     . VAL B 1 697 ? 172.855 129.743 123.545 1.00 109.83 ? 697  VAL B C     1 
ATOM   11065 O  O     . VAL B 1 697 ? 173.795 129.753 124.351 1.00 118.77 ? 697  VAL B O     1 
ATOM   11066 C  CB    . VAL B 1 697 ? 172.395 131.912 122.293 1.00 101.86 ? 697  VAL B CB    1 
ATOM   11067 C  CG1   . VAL B 1 697 ? 171.129 131.979 123.121 1.00 102.54 ? 697  VAL B CG1   1 
ATOM   11068 C  CG2   . VAL B 1 697 ? 173.416 132.822 122.869 1.00 98.43  ? 697  VAL B CG2   1 
ATOM   11069 N  N     . TYR B 1 698 ? 171.727 129.069 123.780 1.00 103.57 ? 698  TYR B N     1 
ATOM   11070 C  CA    . TYR B 1 698 ? 171.561 128.277 124.993 1.00 107.77 ? 698  TYR B CA    1 
ATOM   11071 C  C     . TYR B 1 698 ? 172.639 127.207 125.081 1.00 113.03 ? 698  TYR B C     1 
ATOM   11072 O  O     . TYR B 1 698 ? 173.338 127.086 126.095 1.00 116.75 ? 698  TYR B O     1 
ATOM   11073 C  CB    . TYR B 1 698 ? 170.173 127.634 125.003 1.00 107.67 ? 698  TYR B CB    1 
ATOM   11074 C  CG    . TYR B 1 698 ? 169.013 128.599 125.131 1.00 107.35 ? 698  TYR B CG    1 
ATOM   11075 C  CD1   . TYR B 1 698 ? 169.213 129.970 125.140 1.00 108.47 ? 698  TYR B CD1   1 
ATOM   11076 C  CD2   . TYR B 1 698 ? 167.715 128.132 125.257 1.00 105.91 ? 698  TYR B CD2   1 
ATOM   11077 C  CE1   . TYR B 1 698 ? 168.156 130.847 125.256 1.00 109.56 ? 698  TYR B CE1   1 
ATOM   11078 C  CE2   . TYR B 1 698 ? 166.651 129.002 125.374 1.00 103.27 ? 698  TYR B CE2   1 
ATOM   11079 C  CZ    . TYR B 1 698 ? 166.879 130.358 125.375 1.00 107.88 ? 698  TYR B CZ    1 
ATOM   11080 O  OH    . TYR B 1 698 ? 165.823 131.230 125.495 1.00 114.54 ? 698  TYR B OH    1 
ATOM   11081 N  N     . PHE B 1 699 ? 172.812 126.448 124.000 1.00 110.04 ? 699  PHE B N     1 
ATOM   11082 C  CA    . PHE B 1 699 ? 173.774 125.355 123.997 1.00 110.72 ? 699  PHE B CA    1 
ATOM   11083 C  C     . PHE B 1 699 ? 175.204 125.876 124.006 1.00 112.13 ? 699  PHE B C     1 
ATOM   11084 O  O     . PHE B 1 699 ? 176.086 125.263 124.613 1.00 115.87 ? 699  PHE B O     1 
ATOM   11085 C  CB    . PHE B 1 699 ? 173.531 124.460 122.784 1.00 111.72 ? 699  PHE B CB    1 
ATOM   11086 C  CG    . PHE B 1 699 ? 172.127 123.939 122.695 1.00 113.52 ? 699  PHE B CG    1 
ATOM   11087 C  CD1   . PHE B 1 699 ? 171.763 122.775 123.344 1.00 115.78 ? 699  PHE B CD1   1 
ATOM   11088 C  CD2   . PHE B 1 699 ? 171.168 124.619 121.968 1.00 113.85 ? 699  PHE B CD2   1 
ATOM   11089 C  CE1   . PHE B 1 699 ? 170.474 122.297 123.264 1.00 116.28 ? 699  PHE B CE1   1 
ATOM   11090 C  CE2   . PHE B 1 699 ? 169.877 124.146 121.887 1.00 115.41 ? 699  PHE B CE2   1 
ATOM   11091 C  CZ    . PHE B 1 699 ? 169.530 122.984 122.536 1.00 115.56 ? 699  PHE B CZ    1 
ATOM   11092 N  N     . ILE B 1 700 ? 175.453 127.012 123.352 1.00 106.78 ? 700  ILE B N     1 
ATOM   11093 C  CA    . ILE B 1 700 ? 176.798 127.583 123.342 1.00 107.17 ? 700  ILE B CA    1 
ATOM   11094 C  C     . ILE B 1 700 ? 177.203 128.009 124.747 1.00 111.53 ? 700  ILE B C     1 
ATOM   11095 O  O     . ILE B 1 700 ? 178.293 127.674 125.228 1.00 117.84 ? 700  ILE B O     1 
ATOM   11096 C  CB    . ILE B 1 700 ? 176.876 128.759 122.353 1.00 102.83 ? 700  ILE B CB    1 
ATOM   11097 C  CG1   . ILE B 1 700 ? 176.910 128.246 120.913 1.00 107.60 ? 700  ILE B CG1   1 
ATOM   11098 C  CG2   . ILE B 1 700 ? 178.099 129.610 122.636 1.00 108.07 ? 700  ILE B CG2   1 
ATOM   11099 C  CD1   . ILE B 1 700 ? 176.957 129.347 119.881 1.00 106.81 ? 700  ILE B CD1   1 
ATOM   11100 N  N     . ALA B 1 701 ? 176.322 128.741 125.435 1.00 106.82 ? 701  ALA B N     1 
ATOM   11101 C  CA    . ALA B 1 701 ? 176.624 129.165 126.797 1.00 101.52 ? 701  ALA B CA    1 
ATOM   11102 C  C     . ALA B 1 701 ? 176.735 127.970 127.735 1.00 110.02 ? 701  ALA B C     1 
ATOM   11103 O  O     . ALA B 1 701 ? 177.597 127.947 128.623 1.00 115.98 ? 701  ALA B O     1 
ATOM   11104 C  CB    . ALA B 1 701 ? 175.560 130.142 127.292 1.00 95.24  ? 701  ALA B CB    1 
ATOM   11105 N  N     . SER B 1 702 ? 175.876 126.965 127.553 1.00 109.30 ? 702  SER B N     1 
ATOM   11106 C  CA    . SER B 1 702 ? 175.946 125.777 128.396 1.00 114.11 ? 702  SER B CA    1 
ATOM   11107 C  C     . SER B 1 702 ? 177.261 125.032 128.202 1.00 116.29 ? 702  SER B C     1 
ATOM   11108 O  O     . SER B 1 702 ? 177.895 124.613 129.178 1.00 121.26 ? 702  SER B O     1 
ATOM   11109 C  CB    . SER B 1 702 ? 174.756 124.870 128.098 1.00 114.37 ? 702  SER B CB    1 
ATOM   11110 O  OG    . SER B 1 702 ? 173.550 125.610 128.141 1.00 112.07 ? 702  SER B OG    1 
ATOM   11111 N  N     . ALA B 1 703 ? 177.696 124.867 126.952 1.00 110.92 ? 703  ALA B N     1 
ATOM   11112 C  CA    . ALA B 1 703 ? 178.968 124.202 126.697 1.00 112.11 ? 703  ALA B CA    1 
ATOM   11113 C  C     . ALA B 1 703 ? 180.130 125.016 127.247 1.00 116.44 ? 703  ALA B C     1 
ATOM   11114 O  O     . ALA B 1 703 ? 181.110 124.449 127.745 1.00 118.53 ? 703  ALA B O     1 
ATOM   11115 C  CB    . ALA B 1 703 ? 179.141 123.958 125.199 1.00 111.92 ? 703  ALA B CB    1 
ATOM   11116 N  N     . LEU B 1 704 ? 180.041 126.346 127.166 1.00 113.99 ? 704  LEU B N     1 
ATOM   11117 C  CA    . LEU B 1 704 ? 181.085 127.186 127.743 1.00 109.97 ? 704  LEU B CA    1 
ATOM   11118 C  C     . LEU B 1 704 ? 181.164 127.000 129.252 1.00 113.26 ? 704  LEU B C     1 
ATOM   11119 O  O     . LEU B 1 704 ? 182.258 126.875 129.815 1.00 119.72 ? 704  LEU B O     1 
ATOM   11120 C  CB    . LEU B 1 704 ? 180.828 128.652 127.396 1.00 106.84 ? 704  LEU B CB    1 
ATOM   11121 C  CG    . LEU B 1 704 ? 181.879 129.689 127.796 1.00 108.91 ? 704  LEU B CG    1 
ATOM   11122 C  CD1   . LEU B 1 704 ? 183.281 129.101 127.781 1.00 111.45 ? 704  LEU B CD1   1 
ATOM   11123 C  CD2   . LEU B 1 704 ? 181.799 130.902 126.893 1.00 108.83 ? 704  LEU B CD2   1 
ATOM   11124 N  N     . HIS B 1 705 ? 180.016 126.954 129.921 1.00 112.44 ? 705  HIS B N     1 
ATOM   11125 C  CA    . HIS B 1 705 ? 179.979 126.765 131.365 1.00 114.02 ? 705  HIS B CA    1 
ATOM   11126 C  C     . HIS B 1 705 ? 180.202 125.319 131.776 1.00 117.72 ? 705  HIS B C     1 
ATOM   11127 O  O     . HIS B 1 705 ? 180.284 125.036 132.975 1.00 118.63 ? 705  HIS B O     1 
ATOM   11128 C  CB    . HIS B 1 705 ? 178.649 127.264 131.932 1.00 113.12 ? 705  HIS B CB    1 
ATOM   11129 C  CG    . HIS B 1 705 ? 178.622 128.737 132.187 1.00 114.48 ? 705  HIS B CG    1 
ATOM   11130 N  ND1   . HIS B 1 705 ? 177.603 129.355 132.879 1.00 118.31 ? 705  HIS B ND1   1 
ATOM   11131 C  CD2   . HIS B 1 705 ? 179.493 129.715 131.848 1.00 111.28 ? 705  HIS B CD2   1 
ATOM   11132 C  CE1   . HIS B 1 705 ? 177.847 130.651 132.951 1.00 115.05 ? 705  HIS B CE1   1 
ATOM   11133 N  NE2   . HIS B 1 705 ? 178.987 130.896 132.333 1.00 110.21 ? 705  HIS B NE2   1 
ATOM   11134 N  N     . GLY B 1 706 ? 180.288 124.400 130.818 1.00 121.70 ? 706  GLY B N     1 
ATOM   11135 C  CA    . GLY B 1 706 ? 180.611 123.024 131.115 1.00 123.84 ? 706  GLY B CA    1 
ATOM   11136 C  C     . GLY B 1 706 ? 179.430 122.142 131.441 1.00 125.21 ? 706  GLY B C     1 
ATOM   11137 O  O     . GLY B 1 706 ? 179.606 120.923 131.565 1.00 126.67 ? 706  GLY B O     1 
ATOM   11138 N  N     . GLU B 1 707 ? 178.236 122.710 131.586 1.00 123.94 ? 707  GLU B N     1 
ATOM   11139 C  CA    . GLU B 1 707 ? 177.038 121.935 131.893 1.00 126.21 ? 707  GLU B CA    1 
ATOM   11140 C  C     . GLU B 1 707 ? 176.059 122.114 130.730 1.00 125.85 ? 707  GLU B C     1 
ATOM   11141 O  O     . GLU B 1 707 ? 175.373 123.124 130.583 1.00 123.22 ? 707  GLU B O     1 
ATOM   11142 C  CB    . GLU B 1 707 ? 176.498 122.339 133.274 1.00 123.34 ? 707  GLU B CB    1 
ATOM   11143 C  CG    . GLU B 1 707 ? 175.358 123.335 133.365 1.00 125.08 ? 707  GLU B CG    1 
ATOM   11144 C  CD    . GLU B 1 707 ? 174.928 123.585 134.792 1.00 132.27 ? 707  GLU B CD    1 
ATOM   11145 O  OE1   . GLU B 1 707 ? 175.005 124.750 135.232 1.00 130.61 ? 707  GLU B OE1   1 
ATOM   11146 O  OE2   . GLU B 1 707 ? 174.537 122.620 135.480 1.00 132.85 ? 707  GLU B OE2   1 
ATOM   11147 N  N     . VAL B 1 708 ? 176.067 121.128 129.838 1.00 124.96 ? 708  VAL B N     1 
ATOM   11148 C  CA    . VAL B 1 708 ? 175.251 121.153 128.635 1.00 120.97 ? 708  VAL B CA    1 
ATOM   11149 C  C     . VAL B 1 708 ? 174.293 119.970 128.582 1.00 120.62 ? 708  VAL B C     1 
ATOM   11150 O  O     . VAL B 1 708 ? 173.288 120.016 127.869 1.00 121.43 ? 708  VAL B O     1 
ATOM   11151 C  CB    . VAL B 1 708 ? 176.142 121.204 127.374 1.00 120.66 ? 708  VAL B CB    1 
ATOM   11152 C  CG1   . VAL B 1 708 ? 176.864 119.882 127.175 1.00 130.85 ? 708  VAL B CG1   1 
ATOM   11153 C  CG2   . VAL B 1 708 ? 175.327 121.580 126.148 1.00 116.53 ? 708  VAL B CG2   1 
ATOM   11154 N  N     . HIS B 1 709 ? 174.587 118.902 129.328 1.00 121.10 ? 709  HIS B N     1 
ATOM   11155 C  CA    . HIS B 1 709 ? 173.695 117.748 129.357 1.00 125.96 ? 709  HIS B CA    1 
ATOM   11156 C  C     . HIS B 1 709 ? 172.317 118.121 129.881 1.00 128.08 ? 709  HIS B C     1 
ATOM   11157 O  O     . HIS B 1 709 ? 171.306 117.587 129.408 1.00 129.83 ? 709  HIS B O     1 
ATOM   11158 C  CB    . HIS B 1 709 ? 174.300 116.635 130.212 1.00 131.99 ? 709  HIS B CB    1 
ATOM   11159 C  CG    . HIS B 1 709 ? 175.084 117.133 131.387 1.00 134.47 ? 709  HIS B CG    1 
ATOM   11160 N  ND1   . HIS B 1 709 ? 176.409 117.497 131.295 1.00 133.97 ? 709  HIS B ND1   1 
ATOM   11161 C  CD2   . HIS B 1 709 ? 174.728 117.331 132.678 1.00 134.63 ? 709  HIS B CD2   1 
ATOM   11162 C  CE1   . HIS B 1 709 ? 176.838 117.894 132.480 1.00 134.88 ? 709  HIS B CE1   1 
ATOM   11163 N  NE2   . HIS B 1 709 ? 175.837 117.804 133.336 1.00 136.69 ? 709  HIS B NE2   1 
ATOM   11164 N  N     . HIS B 1 710 ? 172.258 119.037 130.849 1.00 125.01 ? 710  HIS B N     1 
ATOM   11165 C  CA    . HIS B 1 710 ? 170.973 119.464 131.387 1.00 121.78 ? 710  HIS B CA    1 
ATOM   11166 C  C     . HIS B 1 710 ? 170.109 120.081 130.297 1.00 121.51 ? 710  HIS B C     1 
ATOM   11167 O  O     . HIS B 1 710 ? 168.923 119.752 130.167 1.00 124.25 ? 710  HIS B O     1 
ATOM   11168 C  CB    . HIS B 1 710 ? 171.199 120.464 132.519 1.00 118.67 ? 710  HIS B CB    1 
ATOM   11169 C  CG    . HIS B 1 710 ? 171.810 119.859 133.744 1.00 128.97 ? 710  HIS B CG    1 
ATOM   11170 N  ND1   . HIS B 1 710 ? 171.264 118.773 134.392 1.00 134.99 ? 710  HIS B ND1   1 
ATOM   11171 C  CD2   . HIS B 1 710 ? 172.927 120.187 134.435 1.00 130.77 ? 710  HIS B CD2   1 
ATOM   11172 C  CE1   . HIS B 1 710 ? 172.016 118.460 135.432 1.00 135.19 ? 710  HIS B CE1   1 
ATOM   11173 N  NE2   . HIS B 1 710 ? 173.032 119.302 135.481 1.00 132.54 ? 710  HIS B NE2   1 
ATOM   11174 N  N     . ILE B 1 711 ? 170.697 120.962 129.486 1.00 116.57 ? 711  ILE B N     1 
ATOM   11175 C  CA    . ILE B 1 711 ? 169.963 121.585 128.389 1.00 111.74 ? 711  ILE B CA    1 
ATOM   11176 C  C     . ILE B 1 711 ? 169.600 120.548 127.335 1.00 114.76 ? 711  ILE B C     1 
ATOM   11177 O  O     . ILE B 1 711 ? 168.470 120.516 126.835 1.00 115.03 ? 711  ILE B O     1 
ATOM   11178 C  CB    . ILE B 1 711 ? 170.784 122.739 127.790 1.00 110.07 ? 711  ILE B CB    1 
ATOM   11179 C  CG1   . ILE B 1 711 ? 171.128 123.757 128.876 1.00 106.83 ? 711  ILE B CG1   1 
ATOM   11180 C  CG2   . ILE B 1 711 ? 170.032 123.392 126.652 1.00 111.85 ? 711  ILE B CG2   1 
ATOM   11181 C  CD1   . ILE B 1 711 ? 169.930 124.285 129.615 1.00 104.35 ? 711  ILE B CD1   1 
ATOM   11182 N  N     . PHE B 1 712 ? 170.553 119.677 126.989 1.00 117.94 ? 712  PHE B N     1 
ATOM   11183 C  CA    . PHE B 1 712 ? 170.286 118.632 126.006 1.00 117.18 ? 712  PHE B CA    1 
ATOM   11184 C  C     . PHE B 1 712 ? 169.086 117.787 126.408 1.00 118.71 ? 712  PHE B C     1 
ATOM   11185 O  O     . PHE B 1 712 ? 168.305 117.357 125.551 1.00 124.12 ? 712  PHE B O     1 
ATOM   11186 C  CB    . PHE B 1 712 ? 171.517 117.741 125.832 1.00 121.76 ? 712  PHE B CB    1 
ATOM   11187 C  CG    . PHE B 1 712 ? 172.433 118.169 124.721 1.00 127.97 ? 712  PHE B CG    1 
ATOM   11188 C  CD1   . PHE B 1 712 ? 172.141 119.277 123.946 1.00 126.36 ? 712  PHE B CD1   1 
ATOM   11189 C  CD2   . PHE B 1 712 ? 173.584 117.451 124.445 1.00 132.67 ? 712  PHE B CD2   1 
ATOM   11190 C  CE1   . PHE B 1 712 ? 172.985 119.663 122.921 1.00 130.75 ? 712  PHE B CE1   1 
ATOM   11191 C  CE2   . PHE B 1 712 ? 174.431 117.833 123.422 1.00 136.01 ? 712  PHE B CE2   1 
ATOM   11192 C  CZ    . PHE B 1 712 ? 174.131 118.941 122.660 1.00 137.17 ? 712  PHE B CZ    1 
ATOM   11193 N  N     . MET B 1 713 ? 168.918 117.543 127.707 1.00 117.07 ? 713  MET B N     1 
ATOM   11194 C  CA    . MET B 1 713 ? 167.822 116.688 128.145 1.00 117.94 ? 713  MET B CA    1 
ATOM   11195 C  C     . MET B 1 713 ? 166.518 117.465 128.288 1.00 117.35 ? 713  MET B C     1 
ATOM   11196 O  O     . MET B 1 713 ? 165.442 116.930 127.998 1.00 121.43 ? 713  MET B O     1 
ATOM   11197 C  CB    . MET B 1 713 ? 168.178 116.008 129.464 1.00 120.84 ? 713  MET B CB    1 
ATOM   11198 C  CG    . MET B 1 713 ? 169.176 114.877 129.334 1.00 129.94 ? 713  MET B CG    1 
ATOM   11199 S  SD    . MET B 1 713 ? 170.001 114.562 130.902 1.00 158.13 ? 713  MET B SD    1 
ATOM   11200 C  CE    . MET B 1 713 ? 168.704 115.027 132.048 1.00 143.75 ? 713  MET B CE    1 
ATOM   11201 N  N     . THR B 1 714 ? 166.584 118.720 128.732 1.00 113.10 ? 714  THR B N     1 
ATOM   11202 C  CA    . THR B 1 714 ? 165.382 119.454 129.102 1.00 108.73 ? 714  THR B CA    1 
ATOM   11203 C  C     . THR B 1 714 ? 164.902 120.439 128.043 1.00 110.05 ? 714  THR B C     1 
ATOM   11204 O  O     . THR B 1 714 ? 163.900 121.128 128.273 1.00 109.53 ? 714  THR B O     1 
ATOM   11205 C  CB    . THR B 1 714 ? 165.616 120.198 130.419 1.00 106.82 ? 714  THR B CB    1 
ATOM   11206 O  OG1   . THR B 1 714 ? 166.953 120.709 130.445 1.00 115.08 ? 714  THR B OG1   1 
ATOM   11207 C  CG2   . THR B 1 714 ? 165.439 119.255 131.589 1.00 109.28 ? 714  THR B CG2   1 
ATOM   11208 N  N     . PHE B 1 715 ? 165.576 120.525 126.892 1.00 112.55 ? 715  PHE B N     1 
ATOM   11209 C  CA    . PHE B 1 715 ? 165.163 121.485 125.873 1.00 110.52 ? 715  PHE B CA    1 
ATOM   11210 C  C     . PHE B 1 715 ? 163.761 121.192 125.358 1.00 111.77 ? 715  PHE B C     1 
ATOM   11211 O  O     . PHE B 1 715 ? 162.933 122.103 125.247 1.00 111.37 ? 715  PHE B O     1 
ATOM   11212 C  CB    . PHE B 1 715 ? 166.162 121.487 124.718 1.00 114.17 ? 715  PHE B CB    1 
ATOM   11213 C  CG    . PHE B 1 715 ? 165.848 122.494 123.653 1.00 119.90 ? 715  PHE B CG    1 
ATOM   11214 C  CD1   . PHE B 1 715 ? 166.092 123.841 123.862 1.00 118.53 ? 715  PHE B CD1   1 
ATOM   11215 C  CD2   . PHE B 1 715 ? 165.308 122.095 122.443 1.00 123.81 ? 715  PHE B CD2   1 
ATOM   11216 C  CE1   . PHE B 1 715 ? 165.802 124.774 122.884 1.00 116.17 ? 715  PHE B CE1   1 
ATOM   11217 C  CE2   . PHE B 1 715 ? 165.017 123.023 121.460 1.00 126.79 ? 715  PHE B CE2   1 
ATOM   11218 C  CZ    . PHE B 1 715 ? 165.264 124.364 121.682 1.00 122.18 ? 715  PHE B CZ    1 
ATOM   11219 N  N     . THR B 1 716 ? 163.478 119.931 125.025 1.00 112.45 ? 716  THR B N     1 
ATOM   11220 C  CA    . THR B 1 716 ? 162.153 119.585 124.520 1.00 112.30 ? 716  THR B CA    1 
ATOM   11221 C  C     . THR B 1 716 ? 161.085 119.790 125.585 1.00 110.41 ? 716  THR B C     1 
ATOM   11222 O  O     . THR B 1 716 ? 159.989 120.285 125.292 1.00 110.94 ? 716  THR B O     1 
ATOM   11223 C  CB    . THR B 1 716 ? 162.140 118.143 124.015 1.00 108.18 ? 716  THR B CB    1 
ATOM   11224 O  OG1   . THR B 1 716 ? 160.787 117.687 123.906 1.00 108.24 ? 716  THR B OG1   1 
ATOM   11225 C  CG2   . THR B 1 716 ? 162.908 117.233 124.961 1.00 106.35 ? 716  THR B CG2   1 
ATOM   11226 N  N     . HIS B 1 717 ? 161.390 119.424 126.832 1.00 110.74 ? 717  HIS B N     1 
ATOM   11227 C  CA    . HIS B 1 717 ? 160.423 119.592 127.909 1.00 109.23 ? 717  HIS B CA    1 
ATOM   11228 C  C     . HIS B 1 717 ? 160.088 121.060 128.124 1.00 107.98 ? 717  HIS B C     1 
ATOM   11229 O  O     . HIS B 1 717 ? 158.930 121.407 128.385 1.00 111.98 ? 717  HIS B O     1 
ATOM   11230 C  CB    . HIS B 1 717 ? 160.959 118.971 129.197 1.00 112.67 ? 717  HIS B CB    1 
ATOM   11231 C  CG    . HIS B 1 717 ? 161.247 117.507 129.088 1.00 118.62 ? 717  HIS B CG    1 
ATOM   11232 N  ND1   . HIS B 1 717 ? 160.342 116.540 129.468 1.00 120.90 ? 717  HIS B ND1   1 
ATOM   11233 C  CD2   . HIS B 1 717 ? 162.342 116.844 128.646 1.00 120.90 ? 717  HIS B CD2   1 
ATOM   11234 C  CE1   . HIS B 1 717 ? 160.865 115.345 129.262 1.00 125.22 ? 717  HIS B CE1   1 
ATOM   11235 N  NE2   . HIS B 1 717 ? 162.078 115.502 128.763 1.00 122.56 ? 717  HIS B NE2   1 
ATOM   11236 N  N     . TYR B 1 718 ? 161.086 121.941 128.027 1.00 106.27 ? 718  TYR B N     1 
ATOM   11237 C  CA    . TYR B 1 718 ? 160.806 123.362 128.208 1.00 105.52 ? 718  TYR B CA    1 
ATOM   11238 C  C     . TYR B 1 718 ? 160.082 123.945 127.003 1.00 107.17 ? 718  TYR B C     1 
ATOM   11239 O  O     . TYR B 1 718 ? 159.149 124.741 127.162 1.00 107.47 ? 718  TYR B O     1 
ATOM   11240 C  CB    . TYR B 1 718 ? 162.093 124.134 128.469 1.00 103.86 ? 718  TYR B CB    1 
ATOM   11241 C  CG    . TYR B 1 718 ? 161.873 125.621 128.620 1.00 99.72  ? 718  TYR B CG    1 
ATOM   11242 C  CD1   . TYR B 1 718 ? 161.305 126.143 129.772 1.00 104.51 ? 718  TYR B CD1   1 
ATOM   11243 C  CD2   . TYR B 1 718 ? 162.225 126.502 127.609 1.00 99.78  ? 718  TYR B CD2   1 
ATOM   11244 C  CE1   . TYR B 1 718 ? 161.101 127.498 129.916 1.00 108.13 ? 718  TYR B CE1   1 
ATOM   11245 C  CE2   . TYR B 1 718 ? 162.026 127.859 127.745 1.00 103.48 ? 718  TYR B CE2   1 
ATOM   11246 C  CZ    . TYR B 1 718 ? 161.463 128.351 128.900 1.00 110.03 ? 718  TYR B CZ    1 
ATOM   11247 O  OH    . TYR B 1 718 ? 161.261 129.703 129.039 1.00 119.33 ? 718  TYR B OH    1 
ATOM   11248 N  N     . THR B 1 719 ? 160.496 123.572 125.789 1.00 107.07 ? 719  THR B N     1 
ATOM   11249 C  CA    . THR B 1 719 ? 159.843 124.105 124.598 1.00 107.45 ? 719  THR B CA    1 
ATOM   11250 C  C     . THR B 1 719 ? 158.399 123.632 124.508 1.00 111.96 ? 719  THR B C     1 
ATOM   11251 O  O     . THR B 1 719 ? 157.568 124.273 123.856 1.00 116.50 ? 719  THR B O     1 
ATOM   11252 C  CB    . THR B 1 719 ? 160.625 123.720 123.340 1.00 110.02 ? 719  THR B CB    1 
ATOM   11253 O  OG1   . THR B 1 719 ? 160.385 124.691 122.315 1.00 115.44 ? 719  THR B OG1   1 
ATOM   11254 C  CG2   . THR B 1 719 ? 160.205 122.353 122.829 1.00 110.84 ? 719  THR B CG2   1 
ATOM   11255 N  N     . ALA B 1 720 ? 158.078 122.510 125.156 1.00 112.00 ? 720  ALA B N     1 
ATOM   11256 C  CA    . ALA B 1 720 ? 156.686 122.103 125.278 1.00 109.92 ? 720  ALA B CA    1 
ATOM   11257 C  C     . ALA B 1 720 ? 155.901 122.988 126.231 1.00 106.20 ? 720  ALA B C     1 
ATOM   11258 O  O     . ALA B 1 720 ? 154.669 122.922 126.235 1.00 109.81 ? 720  ALA B O     1 
ATOM   11259 C  CB    . ALA B 1 720 ? 156.599 120.652 125.750 1.00 113.56 ? 720  ALA B CB    1 
ATOM   11260 N  N     . LEU B 1 721 ? 156.576 123.809 127.033 1.00 104.61 ? 721  LEU B N     1 
ATOM   11261 C  CA    . LEU B 1 721 ? 155.919 124.582 128.077 1.00 106.28 ? 721  LEU B CA    1 
ATOM   11262 C  C     . LEU B 1 721 ? 156.111 126.083 127.905 1.00 107.47 ? 721  LEU B C     1 
ATOM   11263 O  O     . LEU B 1 721 ? 155.727 126.846 128.794 1.00 108.90 ? 721  LEU B O     1 
ATOM   11264 C  CB    . LEU B 1 721 ? 156.429 124.147 129.454 1.00 104.71 ? 721  LEU B CB    1 
ATOM   11265 C  CG    . LEU B 1 721 ? 155.408 124.102 130.590 1.00 102.65 ? 721  LEU B CG    1 
ATOM   11266 C  CD1   . LEU B 1 721 ? 154.081 123.584 130.079 1.00 104.51 ? 721  LEU B CD1   1 
ATOM   11267 C  CD2   . LEU B 1 721 ? 155.904 123.245 131.734 1.00 106.09 ? 721  LEU B CD2   1 
ATOM   11268 N  N     . ILE B 1 722 ? 156.701 126.526 126.800 1.00 105.63 ? 722  ILE B N     1 
ATOM   11269 C  CA    . ILE B 1 722 ? 156.898 127.949 126.523 1.00 103.39 ? 722  ILE B CA    1 
ATOM   11270 C  C     . ILE B 1 722 ? 155.567 128.699 126.473 1.00 106.79 ? 722  ILE B C     1 
ATOM   11271 O  O     . ILE B 1 722 ? 155.444 129.756 127.115 1.00 108.78 ? 722  ILE B O     1 
ATOM   11272 C  CB    . ILE B 1 722 ? 157.688 128.150 125.220 1.00 105.26 ? 722  ILE B CB    1 
ATOM   11273 C  CG1   . ILE B 1 722 ? 159.187 128.025 125.481 1.00 109.01 ? 722  ILE B CG1   1 
ATOM   11274 C  CG2   . ILE B 1 722 ? 157.383 129.505 124.610 1.00 102.38 ? 722  ILE B CG2   1 
ATOM   11275 C  CD1   . ILE B 1 722 ? 160.045 128.496 124.330 1.00 114.21 ? 722  ILE B CD1   1 
ATOM   11276 N  N     . PRO B 1 723 ? 154.551 128.227 125.737 1.00 111.42 ? 723  PRO B N     1 
ATOM   11277 C  CA    . PRO B 1 723 ? 153.310 129.011 125.676 1.00 109.69 ? 723  PRO B CA    1 
ATOM   11278 C  C     . PRO B 1 723 ? 152.555 128.992 126.983 1.00 110.33 ? 723  PRO B C     1 
ATOM   11279 O  O     . PRO B 1 723 ? 151.994 130.018 127.384 1.00 112.07 ? 723  PRO B O     1 
ATOM   11280 C  CB    . PRO B 1 723 ? 152.515 128.328 124.559 1.00 108.69 ? 723  PRO B CB    1 
ATOM   11281 C  CG    . PRO B 1 723 ? 152.962 126.937 124.615 1.00 113.59 ? 723  PRO B CG    1 
ATOM   11282 C  CD    . PRO B 1 723 ? 154.415 126.969 124.983 1.00 115.06 ? 723  PRO B CD    1 
ATOM   11283 N  N     . SER B 1 724 ? 152.516 127.842 127.656 1.00 108.13 ? 724  SER B N     1 
ATOM   11284 C  CA    . SER B 1 724 ? 151.918 127.791 128.982 1.00 109.60 ? 724  SER B CA    1 
ATOM   11285 C  C     . SER B 1 724 ? 152.599 128.785 129.907 1.00 106.62 ? 724  SER B C     1 
ATOM   11286 O  O     . SER B 1 724 ? 151.935 129.618 130.529 1.00 106.91 ? 724  SER B O     1 
ATOM   11287 C  CB    . SER B 1 724 ? 152.005 126.377 129.547 1.00 112.72 ? 724  SER B CB    1 
ATOM   11288 O  OG    . SER B 1 724 ? 151.835 126.386 130.953 1.00 115.23 ? 724  SER B OG    1 
ATOM   11289 N  N     . PHE B 1 725 ? 153.930 128.751 129.958 1.00 107.13 ? 725  PHE B N     1 
ATOM   11290 C  CA    . PHE B 1 725 ? 154.702 129.709 130.735 1.00 106.84 ? 725  PHE B CA    1 
ATOM   11291 C  C     . PHE B 1 725 ? 154.240 131.124 130.438 1.00 104.76 ? 725  PHE B C     1 
ATOM   11292 O  O     . PHE B 1 725 ? 153.597 131.753 131.284 1.00 108.66 ? 725  PHE B O     1 
ATOM   11293 C  CB    . PHE B 1 725 ? 156.194 129.580 130.425 1.00 106.96 ? 725  PHE B CB    1 
ATOM   11294 C  CG    . PHE B 1 725 ? 156.974 128.860 131.481 1.00 111.17 ? 725  PHE B CG    1 
ATOM   11295 C  CD1   . PHE B 1 725 ? 156.982 127.480 131.538 1.00 111.78 ? 725  PHE B CD1   1 
ATOM   11296 C  CD2   . PHE B 1 725 ? 157.705 129.567 132.415 1.00 111.61 ? 725  PHE B CD2   1 
ATOM   11297 C  CE1   . PHE B 1 725 ? 157.700 126.818 132.508 1.00 107.47 ? 725  PHE B CE1   1 
ATOM   11298 C  CE2   . PHE B 1 725 ? 158.423 128.912 133.386 1.00 114.62 ? 725  PHE B CE2   1 
ATOM   11299 C  CZ    . PHE B 1 725 ? 158.421 127.535 133.433 1.00 113.29 ? 725  PHE B CZ    1 
ATOM   11300 N  N     . VAL B 1 726 ? 154.560 131.611 129.245 1.00 107.04 ? 726  VAL B N     1 
ATOM   11301 C  CA    . VAL B 1 726 ? 154.219 132.968 128.823 1.00 105.57 ? 726  VAL B CA    1 
ATOM   11302 C  C     . VAL B 1 726 ? 152.774 133.418 129.055 1.00 108.15 ? 726  VAL B C     1 
ATOM   11303 O  O     . VAL B 1 726 ? 152.536 134.413 129.739 1.00 112.32 ? 726  VAL B O     1 
ATOM   11304 C  CB    . VAL B 1 726 ? 154.564 133.188 127.336 1.00 100.00 ? 726  VAL B CB    1 
ATOM   11305 C  CG1   . VAL B 1 726 ? 156.041 133.515 127.177 1.00 100.25 ? 726  VAL B CG1   1 
ATOM   11306 C  CG2   . VAL B 1 726 ? 154.191 131.961 126.519 1.00 99.74  ? 726  VAL B CG2   1 
ATOM   11307 N  N     . ASN B 1 727 ? 151.815 132.692 128.489 1.00 106.83 ? 727  ASN B N     1 
ATOM   11308 C  CA    . ASN B 1 727 ? 150.415 133.078 128.604 1.00 105.29 ? 727  ASN B CA    1 
ATOM   11309 C  C     . ASN B 1 727 ? 149.898 132.883 130.023 1.00 109.31 ? 727  ASN B C     1 
ATOM   11310 O  O     . ASN B 1 727 ? 149.500 133.847 130.685 1.00 114.47 ? 727  ASN B O     1 
ATOM   11311 C  CB    . ASN B 1 727 ? 149.576 132.280 127.606 1.00 105.21 ? 727  ASN B CB    1 
ATOM   11312 C  CG    . ASN B 1 727 ? 149.840 132.687 126.174 1.00 107.77 ? 727  ASN B CG    1 
ATOM   11313 O  OD1   . ASN B 1 727 ? 150.027 133.864 125.876 1.00 109.95 ? 727  ASN B OD1   1 
ATOM   11314 N  ND2   . ASN B 1 727 ? 149.863 131.711 125.277 1.00 106.53 ? 727  ASN B ND2   1 
ATOM   11315 N  N     . ILE B 1 728 ? 149.890 131.636 130.507 1.00 106.74 ? 728  ILE B N     1 
ATOM   11316 C  CA    . ILE B 1 728 ? 149.253 131.339 131.785 1.00 104.03 ? 728  ILE B CA    1 
ATOM   11317 C  C     . ILE B 1 728 ? 149.905 132.137 132.904 1.00 109.32 ? 728  ILE B C     1 
ATOM   11318 O  O     . ILE B 1 728 ? 149.220 132.784 133.704 1.00 114.22 ? 728  ILE B O     1 
ATOM   11319 C  CB    . ILE B 1 728 ? 149.316 129.830 132.080 1.00 104.90 ? 728  ILE B CB    1 
ATOM   11320 C  CG1   . ILE B 1 728 ? 148.753 129.018 130.917 1.00 107.30 ? 728  ILE B CG1   1 
ATOM   11321 C  CG2   . ILE B 1 728 ? 148.553 129.516 133.349 1.00 107.08 ? 728  ILE B CG2   1 
ATOM   11322 C  CD1   . ILE B 1 728 ? 148.767 127.527 131.151 1.00 115.98 ? 728  ILE B CD1   1 
ATOM   11323 N  N     . PHE B 1 729 ? 151.239 132.095 132.990 1.00 111.26 ? 729  PHE B N     1 
ATOM   11324 C  CA    . PHE B 1 729 ? 151.906 132.682 134.141 1.00 109.86 ? 729  PHE B CA    1 
ATOM   11325 C  C     . PHE B 1 729 ? 151.804 134.200 134.122 1.00 113.44 ? 729  PHE B C     1 
ATOM   11326 O  O     . PHE B 1 729 ? 151.495 134.808 135.153 1.00 120.60 ? 729  PHE B O     1 
ATOM   11327 C  CB    . PHE B 1 729 ? 153.365 132.232 134.178 1.00 111.44 ? 729  PHE B CB    1 
ATOM   11328 C  CG    . PHE B 1 729 ? 153.541 130.751 134.370 1.00 110.70 ? 729  PHE B CG    1 
ATOM   11329 C  CD1   . PHE B 1 729 ? 152.457 129.932 134.628 1.00 110.05 ? 729  PHE B CD1   1 
ATOM   11330 C  CD2   . PHE B 1 729 ? 154.793 130.176 134.270 1.00 113.80 ? 729  PHE B CD2   1 
ATOM   11331 C  CE1   . PHE B 1 729 ? 152.620 128.577 134.791 1.00 112.44 ? 729  PHE B CE1   1 
ATOM   11332 C  CE2   . PHE B 1 729 ? 154.959 128.819 134.433 1.00 113.74 ? 729  PHE B CE2   1 
ATOM   11333 C  CZ    . PHE B 1 729 ? 153.870 128.021 134.692 1.00 113.36 ? 729  PHE B CZ    1 
ATOM   11334 N  N     . THR B 1 730 ? 152.010 134.802 132.955 1.00 109.63 ? 730  THR B N     1 
ATOM   11335 C  CA    . THR B 1 730 ? 151.920 136.251 132.818 1.00 111.11 ? 730  THR B CA    1 
ATOM   11336 C  C     . THR B 1 730 ? 150.504 136.749 133.106 1.00 115.06 ? 730  THR B C     1 
ATOM   11337 O  O     . THR B 1 730 ? 150.321 137.787 133.743 1.00 118.66 ? 730  THR B O     1 
ATOM   11338 C  CB    . THR B 1 730 ? 152.339 136.710 131.409 1.00 114.28 ? 730  THR B CB    1 
ATOM   11339 O  OG1   . THR B 1 730 ? 153.762 136.613 131.274 1.00 117.31 ? 730  THR B OG1   1 
ATOM   11340 C  CG2   . THR B 1 730 ? 151.909 138.149 131.168 1.00 112.44 ? 730  THR B CG2   1 
ATOM   11341 N  N     . ILE B 1 731 ? 149.506 136.006 132.634 1.00 114.36 ? 731  ILE B N     1 
ATOM   11342 C  CA    . ILE B 1 731 ? 148.109 136.373 132.839 1.00 116.15 ? 731  ILE B CA    1 
ATOM   11343 C  C     . ILE B 1 731 ? 147.750 136.276 134.313 1.00 122.26 ? 731  ILE B C     1 
ATOM   11344 O  O     . ILE B 1 731 ? 147.226 137.226 134.899 1.00 125.96 ? 731  ILE B O     1 
ATOM   11345 C  CB    . ILE B 1 731 ? 147.189 135.495 131.972 1.00 114.76 ? 731  ILE B CB    1 
ATOM   11346 C  CG1   . ILE B 1 731 ? 147.030 136.104 130.579 1.00 115.37 ? 731  ILE B CG1   1 
ATOM   11347 C  CG2   . ILE B 1 731 ? 145.826 135.343 132.622 1.00 112.34 ? 731  ILE B CG2   1 
ATOM   11348 C  CD1   . ILE B 1 731 ? 146.221 135.253 129.630 1.00 111.51 ? 731  ILE B CD1   1 
ATOM   11349 N  N     . TYR B 1 732 ? 148.063 135.141 134.947 1.00 126.00 ? 732  TYR B N     1 
ATOM   11350 C  CA    . TYR B 1 732 ? 147.703 134.969 136.352 1.00 126.08 ? 732  TYR B CA    1 
ATOM   11351 C  C     . TYR B 1 732 ? 148.445 135.949 137.251 1.00 125.72 ? 732  TYR B C     1 
ATOM   11352 O  O     . TYR B 1 732 ? 147.862 136.483 138.201 1.00 128.19 ? 732  TYR B O     1 
ATOM   11353 C  CB    . TYR B 1 732 ? 147.956 133.533 136.805 1.00 119.95 ? 732  TYR B CB    1 
ATOM   11354 C  CG    . TYR B 1 732 ? 147.331 133.251 138.147 1.00 125.28 ? 732  TYR B CG    1 
ATOM   11355 C  CD1   . TYR B 1 732 ? 146.032 133.647 138.423 1.00 131.03 ? 732  TYR B CD1   1 
ATOM   11356 C  CD2   . TYR B 1 732 ? 148.046 132.611 139.146 1.00 127.69 ? 732  TYR B CD2   1 
ATOM   11357 C  CE1   . TYR B 1 732 ? 145.459 133.406 139.655 1.00 132.68 ? 732  TYR B CE1   1 
ATOM   11358 C  CE2   . TYR B 1 732 ? 147.481 132.364 140.380 1.00 127.67 ? 732  TYR B CE2   1 
ATOM   11359 C  CZ    . TYR B 1 732 ? 146.188 132.764 140.629 1.00 128.95 ? 732  TYR B CZ    1 
ATOM   11360 O  OH    . TYR B 1 732 ? 145.624 132.523 141.859 1.00 126.42 ? 732  TYR B OH    1 
ATOM   11361 N  N     . SER B 1 733 ? 149.730 136.194 136.983 1.00 121.16 ? 733  SER B N     1 
ATOM   11362 C  CA    . SER B 1 733 ? 150.468 137.162 137.784 1.00 124.95 ? 733  SER B CA    1 
ATOM   11363 C  C     . SER B 1 733 ? 149.856 138.549 137.665 1.00 129.75 ? 733  SER B C     1 
ATOM   11364 O  O     . SER B 1 733 ? 149.740 139.272 138.661 1.00 138.07 ? 733  SER B O     1 
ATOM   11365 C  CB    . SER B 1 733 ? 151.934 137.187 137.359 1.00 127.92 ? 733  SER B CB    1 
ATOM   11366 O  OG    . SER B 1 733 ? 152.482 138.485 137.504 1.00 131.54 ? 733  SER B OG    1 
ATOM   11367 N  N     . PHE B 1 734 ? 149.450 138.937 136.455 1.00 126.40 ? 734  PHE B N     1 
ATOM   11368 C  CA    . PHE B 1 734 ? 148.859 140.252 136.260 1.00 129.07 ? 734  PHE B CA    1 
ATOM   11369 C  C     . PHE B 1 734 ? 147.417 140.298 136.745 1.00 132.81 ? 734  PHE B C     1 
ATOM   11370 O  O     . PHE B 1 734 ? 146.858 141.388 136.900 1.00 133.73 ? 734  PHE B O     1 
ATOM   11371 C  CB    . PHE B 1 734 ? 148.934 140.626 134.782 1.00 124.44 ? 734  PHE B CB    1 
ATOM   11372 C  CG    . PHE B 1 734 ? 150.119 141.473 134.433 1.00 119.06 ? 734  PHE B CG    1 
ATOM   11373 C  CD1   . PHE B 1 734 ? 151.360 140.889 134.252 1.00 118.97 ? 734  PHE B CD1   1 
ATOM   11374 C  CD2   . PHE B 1 734 ? 150.002 142.839 134.281 1.00 119.19 ? 734  PHE B CD2   1 
ATOM   11375 C  CE1   . PHE B 1 734 ? 152.460 141.649 133.928 1.00 119.56 ? 734  PHE B CE1   1 
ATOM   11376 C  CE2   . PHE B 1 734 ? 151.103 143.605 133.954 1.00 120.87 ? 734  PHE B CE2   1 
ATOM   11377 C  CZ    . PHE B 1 734 ? 152.332 143.009 133.779 1.00 120.25 ? 734  PHE B CZ    1 
ATOM   11378 N  N     . CYS B 1 735 ? 146.813 139.136 136.987 1.00 133.81 ? 735  CYS B N     1 
ATOM   11379 C  CA    . CYS B 1 735 ? 145.419 139.004 137.387 1.00 134.35 ? 735  CYS B CA    1 
ATOM   11380 C  C     . CYS B 1 735 ? 145.174 139.377 138.840 1.00 136.70 ? 735  CYS B C     1 
ATOM   11381 O  O     . CYS B 1 735 ? 144.060 139.792 139.174 1.00 141.54 ? 735  CYS B O     1 
ATOM   11382 C  CB    . CYS B 1 735 ? 144.946 137.564 137.168 1.00 134.42 ? 735  CYS B CB    1 
ATOM   11383 S  SG    . CYS B 1 735 ? 144.368 137.155 135.509 1.00 143.00 ? 735  CYS B SG    1 
ATOM   11384 N  N     . ASN B 1 736 ? 146.170 139.233 139.708 1.00 134.26 ? 736  ASN B N     1 
ATOM   11385 C  CA    . ASN B 1 736 ? 145.982 139.357 141.149 1.00 142.94 ? 736  ASN B CA    1 
ATOM   11386 C  C     . ASN B 1 736 ? 147.035 140.276 141.752 1.00 149.01 ? 736  ASN B C     1 
ATOM   11387 O  O     . ASN B 1 736 ? 147.710 139.942 142.728 1.00 153.68 ? 736  ASN B O     1 
ATOM   11388 C  CB    . ASN B 1 736 ? 146.001 137.981 141.802 1.00 144.55 ? 736  ASN B CB    1 
ATOM   11389 C  CG    . ASN B 1 736 ? 144.832 137.120 141.370 1.00 139.01 ? 736  ASN B CG    1 
ATOM   11390 O  OD1   . ASN B 1 736 ? 144.853 136.519 140.297 1.00 132.75 ? 736  ASN B OD1   1 
ATOM   11391 N  ND2   . ASN B 1 736 ? 143.799 137.063 142.202 1.00 141.41 ? 736  ASN B ND2   1 
ATOM   11392 N  N     . LEU B 1 737 ? 147.190 141.461 141.160 1.00 145.05 ? 737  LEU B N     1 
ATOM   11393 C  CA    . LEU B 1 737 ? 148.040 142.499 141.726 1.00 145.95 ? 737  LEU B CA    1 
ATOM   11394 C  C     . LEU B 1 737 ? 147.543 143.009 143.070 1.00 152.93 ? 737  LEU B C     1 
ATOM   11395 O  O     . LEU B 1 737 ? 148.328 143.602 143.817 1.00 155.78 ? 737  LEU B O     1 
ATOM   11396 C  CB    . LEU B 1 737 ? 148.149 143.675 140.756 1.00 141.05 ? 737  LEU B CB    1 
ATOM   11397 C  CG    . LEU B 1 737 ? 149.109 143.487 139.591 1.00 142.83 ? 737  LEU B CG    1 
ATOM   11398 C  CD1   . LEU B 1 737 ? 149.142 144.721 138.723 1.00 142.83 ? 737  LEU B CD1   1 
ATOM   11399 C  CD2   . LEU B 1 737 ? 150.466 143.221 140.166 1.00 140.58 ? 737  LEU B CD2   1 
ATOM   11400 N  N     . GLN B 1 738 ? 146.270 142.795 143.393 1.00 155.79 ? 738  GLN B N     1 
ATOM   11401 C  CA    . GLN B 1 738 ? 145.698 143.252 144.651 1.00 153.38 ? 738  GLN B CA    1 
ATOM   11402 C  C     . GLN B 1 738 ? 145.886 142.258 145.787 1.00 159.98 ? 738  GLN B C     1 
ATOM   11403 O  O     . GLN B 1 738 ? 145.531 142.573 146.929 1.00 163.71 ? 738  GLN B O     1 
ATOM   11404 C  CB    . GLN B 1 738 ? 144.205 143.552 144.468 1.00 148.42 ? 738  GLN B CB    1 
ATOM   11405 C  CG    . GLN B 1 738 ? 143.294 142.356 144.693 1.00 153.41 ? 738  GLN B CG    1 
ATOM   11406 C  CD    . GLN B 1 738 ? 143.497 141.265 143.661 1.00 152.08 ? 738  GLN B CD    1 
ATOM   11407 O  OE1   . GLN B 1 738 ? 143.936 141.526 142.542 1.00 146.88 ? 738  GLN B OE1   1 
ATOM   11408 N  NE2   . GLN B 1 738 ? 143.175 140.032 144.033 1.00 155.17 ? 738  GLN B NE2   1 
ATOM   11409 N  N     . ASP B 1 739 ? 146.442 141.080 145.512 1.00 160.05 ? 739  ASP B N     1 
ATOM   11410 C  CA    . ASP B 1 739 ? 146.641 140.057 146.536 1.00 165.16 ? 739  ASP B CA    1 
ATOM   11411 C  C     . ASP B 1 739 ? 147.809 140.483 147.416 1.00 170.57 ? 739  ASP B C     1 
ATOM   11412 O  O     . ASP B 1 739 ? 148.966 140.144 147.164 1.00 170.85 ? 739  ASP B O     1 
ATOM   11413 C  CB    . ASP B 1 739 ? 146.886 138.696 145.896 1.00 162.40 ? 739  ASP B CB    1 
ATOM   11414 C  CG    . ASP B 1 739 ? 146.843 137.563 146.901 1.00 171.26 ? 739  ASP B CG    1 
ATOM   11415 O  OD1   . ASP B 1 739 ? 146.483 137.813 148.070 1.00 175.06 ? 739  ASP B OD1   1 
ATOM   11416 O  OD2   . ASP B 1 739 ? 147.166 136.418 146.519 1.00 170.71 ? 739  ASP B OD2   1 
ATOM   11417 N  N     . LEU B 1 740 ? 147.495 141.237 148.468 1.00 172.35 ? 740  LEU B N     1 
ATOM   11418 C  CA    . LEU B 1 740 ? 148.483 141.736 149.411 1.00 171.14 ? 740  LEU B CA    1 
ATOM   11419 C  C     . LEU B 1 740 ? 147.986 141.530 150.833 1.00 175.45 ? 740  LEU B C     1 
ATOM   11420 O  O     . LEU B 1 740 ? 146.780 141.481 151.087 1.00 176.49 ? 740  LEU B O     1 
ATOM   11421 C  CB    . LEU B 1 740 ? 148.793 143.225 149.174 1.00 167.04 ? 740  LEU B CB    1 
ATOM   11422 C  CG    . LEU B 1 740 ? 149.448 143.530 147.828 1.00 163.24 ? 740  LEU B CG    1 
ATOM   11423 C  CD1   . LEU B 1 740 ? 149.677 145.011 147.618 1.00 160.21 ? 740  LEU B CD1   1 
ATOM   11424 C  CD2   . LEU B 1 740 ? 150.753 142.808 147.778 1.00 161.63 ? 740  LEU B CD2   1 
ATOM   11425 N  N     . SER B 1 741 ? 148.931 141.405 151.759 1.00 179.42 ? 741  SER B N     1 
ATOM   11426 C  CA    . SER B 1 741 ? 148.602 141.202 153.164 1.00 179.33 ? 741  SER B CA    1 
ATOM   11427 C  C     . SER B 1 741 ? 148.105 142.496 153.798 1.00 177.46 ? 741  SER B C     1 
ATOM   11428 O  O     . SER B 1 741 ? 148.793 143.099 154.621 1.00 177.62 ? 741  SER B O     1 
ATOM   11429 C  CB    . SER B 1 741 ? 149.816 140.671 153.930 1.00 179.82 ? 741  SER B CB    1 
ATOM   11430 O  OG    . SER B 1 741 ? 150.882 141.603 153.906 1.00 181.11 ? 741  SER B OG    1 
ATOM   11431 N  N     . LYS B 1 762 ? 137.547 153.677 186.612 1.00 174.71 ? 762  LYS B N     1 
ATOM   11432 C  CA    . LYS B 1 762 ? 136.380 153.934 187.447 1.00 180.05 ? 762  LYS B CA    1 
ATOM   11433 C  C     . LYS B 1 762 ? 135.468 154.975 186.807 1.00 178.89 ? 762  LYS B C     1 
ATOM   11434 O  O     . LYS B 1 762 ? 135.280 156.066 187.346 1.00 179.32 ? 762  LYS B O     1 
ATOM   11435 C  CB    . LYS B 1 762 ? 136.809 154.393 188.842 1.00 183.68 ? 762  LYS B CB    1 
ATOM   11436 C  CG    . LYS B 1 762 ? 137.601 153.354 189.619 1.00 187.05 ? 762  LYS B CG    1 
ATOM   11437 C  CD    . LYS B 1 762 ? 136.766 152.116 189.894 1.00 187.03 ? 762  LYS B CD    1 
ATOM   11438 C  CE    . LYS B 1 762 ? 137.553 151.084 190.682 1.00 192.61 ? 762  LYS B CE    1 
ATOM   11439 N  NZ    . LYS B 1 762 ? 136.731 149.884 190.999 1.00 192.55 ? 762  LYS B NZ    1 
ATOM   11440 N  N     . GLY B 1 763 ? 134.902 154.630 185.651 1.00 175.24 ? 763  GLY B N     1 
ATOM   11441 C  CA    . GLY B 1 763 ? 134.009 155.512 184.938 1.00 169.22 ? 763  GLY B CA    1 
ATOM   11442 C  C     . GLY B 1 763 ? 132.550 155.162 185.161 1.00 166.79 ? 763  GLY B C     1 
ATOM   11443 O  O     . GLY B 1 763 ? 132.206 154.038 185.518 1.00 164.76 ? 763  GLY B O     1 
ATOM   11444 N  N     . ASP B 1 764 ? 131.689 156.149 184.941 1.00 166.13 ? 764  ASP B N     1 
ATOM   11445 C  CA    . ASP B 1 764 ? 130.261 155.977 185.144 1.00 162.57 ? 764  ASP B CA    1 
ATOM   11446 C  C     . ASP B 1 764 ? 129.612 155.478 183.853 1.00 160.65 ? 764  ASP B C     1 
ATOM   11447 O  O     . ASP B 1 764 ? 130.289 155.112 182.887 1.00 162.22 ? 764  ASP B O     1 
ATOM   11448 C  CB    . ASP B 1 764 ? 129.635 157.280 185.635 1.00 162.57 ? 764  ASP B CB    1 
ATOM   11449 C  CG    . ASP B 1 764 ? 130.086 158.481 184.834 1.00 162.83 ? 764  ASP B CG    1 
ATOM   11450 O  OD1   . ASP B 1 764 ? 131.262 158.508 184.416 1.00 162.81 ? 764  ASP B OD1   1 
ATOM   11451 O  OD2   . ASP B 1 764 ? 129.266 159.399 184.625 1.00 162.29 ? 764  ASP B OD2   1 
ATOM   11452 N  N     . PHE B 1 765 ? 128.278 155.458 183.829 1.00 155.45 ? 765  PHE B N     1 
ATOM   11453 C  CA    . PHE B 1 765 ? 127.581 154.874 182.691 1.00 152.91 ? 765  PHE B CA    1 
ATOM   11454 C  C     . PHE B 1 765 ? 127.702 155.759 181.457 1.00 154.91 ? 765  PHE B C     1 
ATOM   11455 O  O     . PHE B 1 765 ? 127.746 155.259 180.328 1.00 156.00 ? 765  PHE B O     1 
ATOM   11456 C  CB    . PHE B 1 765 ? 126.116 154.630 183.035 1.00 146.36 ? 765  PHE B CB    1 
ATOM   11457 C  CG    . PHE B 1 765 ? 125.431 153.707 182.081 1.00 141.15 ? 765  PHE B CG    1 
ATOM   11458 C  CD1   . PHE B 1 765 ? 126.053 152.539 181.679 1.00 142.22 ? 765  PHE B CD1   1 
ATOM   11459 C  CD2   . PHE B 1 765 ? 124.174 153.994 181.590 1.00 139.05 ? 765  PHE B CD2   1 
ATOM   11460 C  CE1   . PHE B 1 765 ? 125.439 151.677 180.802 1.00 142.12 ? 765  PHE B CE1   1 
ATOM   11461 C  CE2   . PHE B 1 765 ? 123.556 153.135 180.709 1.00 140.03 ? 765  PHE B CE2   1 
ATOM   11462 C  CZ    . PHE B 1 765 ? 124.190 151.974 180.315 1.00 137.68 ? 765  PHE B CZ    1 
ATOM   11463 N  N     . LYS B 1 766 ? 127.756 157.079 181.648 1.00 155.63 ? 766  LYS B N     1 
ATOM   11464 C  CA    . LYS B 1 766 ? 127.999 157.969 180.517 1.00 157.43 ? 766  LYS B CA    1 
ATOM   11465 C  C     . LYS B 1 766 ? 129.362 157.696 179.896 1.00 158.15 ? 766  LYS B C     1 
ATOM   11466 O  O     . LYS B 1 766 ? 129.493 157.670 178.667 1.00 158.55 ? 766  LYS B O     1 
ATOM   11467 C  CB    . LYS B 1 766 ? 127.895 159.430 180.959 1.00 159.38 ? 766  LYS B CB    1 
ATOM   11468 C  CG    . LYS B 1 766 ? 126.578 159.856 181.643 1.00 161.26 ? 766  LYS B CG    1 
ATOM   11469 C  CD    . LYS B 1 766 ? 125.283 159.245 181.084 1.00 163.91 ? 766  LYS B CD    1 
ATOM   11470 C  CE    . LYS B 1 766 ? 125.157 159.352 179.563 1.00 166.62 ? 766  LYS B CE    1 
ATOM   11471 N  NZ    . LYS B 1 766 ? 125.477 160.722 179.073 1.00 163.41 ? 766  LYS B NZ    1 
ATOM   11472 N  N     . ASP B 1 767 ? 130.382 157.483 180.730 1.00 158.13 ? 767  ASP B N     1 
ATOM   11473 C  CA    . ASP B 1 767 ? 131.703 157.124 180.224 1.00 160.07 ? 767  ASP B CA    1 
ATOM   11474 C  C     . ASP B 1 767 ? 131.676 155.779 179.509 1.00 158.10 ? 767  ASP B C     1 
ATOM   11475 O  O     . ASP B 1 767 ? 132.342 155.603 178.483 1.00 158.56 ? 767  ASP B O     1 
ATOM   11476 C  CB    . ASP B 1 767 ? 132.715 157.103 181.369 1.00 165.24 ? 767  ASP B CB    1 
ATOM   11477 C  CG    . ASP B 1 767 ? 133.996 156.377 181.003 1.00 171.03 ? 767  ASP B CG    1 
ATOM   11478 O  OD1   . ASP B 1 767 ? 134.804 156.943 180.238 1.00 173.10 ? 767  ASP B OD1   1 
ATOM   11479 O  OD2   . ASP B 1 767 ? 134.199 155.243 181.486 1.00 170.65 ? 767  ASP B OD2   1 
ATOM   11480 N  N     . VAL B 1 768 ? 130.922 154.814 180.039 1.00 153.60 ? 768  VAL B N     1 
ATOM   11481 C  CA    . VAL B 1 768 ? 130.818 153.517 179.375 1.00 153.03 ? 768  VAL B CA    1 
ATOM   11482 C  C     . VAL B 1 768 ? 130.186 153.673 177.997 1.00 154.50 ? 768  VAL B C     1 
ATOM   11483 O  O     . VAL B 1 768 ? 130.649 153.086 177.010 1.00 157.23 ? 768  VAL B O     1 
ATOM   11484 C  CB    . VAL B 1 768 ? 130.031 152.529 180.254 1.00 154.09 ? 768  VAL B CB    1 
ATOM   11485 C  CG1   . VAL B 1 768 ? 129.408 151.432 179.405 1.00 155.41 ? 768  VAL B CG1   1 
ATOM   11486 C  CG2   . VAL B 1 768 ? 130.941 151.934 181.310 1.00 154.89 ? 768  VAL B CG2   1 
ATOM   11487 N  N     . ILE B 1 769 ? 129.123 154.473 177.908 1.00 153.17 ? 769  ILE B N     1 
ATOM   11488 C  CA    . ILE B 1 769 ? 128.453 154.694 176.630 1.00 150.79 ? 769  ILE B CA    1 
ATOM   11489 C  C     . ILE B 1 769 ? 129.385 155.400 175.653 1.00 154.07 ? 769  ILE B C     1 
ATOM   11490 O  O     . ILE B 1 769 ? 129.433 155.064 174.463 1.00 155.31 ? 769  ILE B O     1 
ATOM   11491 C  CB    . ILE B 1 769 ? 127.148 155.482 176.847 1.00 147.69 ? 769  ILE B CB    1 
ATOM   11492 C  CG1   . ILE B 1 769 ? 126.046 154.549 177.346 1.00 142.14 ? 769  ILE B CG1   1 
ATOM   11493 C  CG2   . ILE B 1 769 ? 126.715 156.178 175.571 1.00 149.52 ? 769  ILE B CG2   1 
ATOM   11494 C  CD1   . ILE B 1 769 ? 125.958 153.253 176.580 1.00 138.21 ? 769  ILE B CD1   1 
ATOM   11495 N  N     . ALA B 1 770 ? 130.139 156.389 176.137 1.00 154.91 ? 770  ALA B N     1 
ATOM   11496 C  CA    . ALA B 1 770 ? 131.092 157.080 175.274 1.00 153.39 ? 770  ALA B CA    1 
ATOM   11497 C  C     . ALA B 1 770 ? 132.174 156.131 174.775 1.00 153.04 ? 770  ALA B C     1 
ATOM   11498 O  O     . ALA B 1 770 ? 132.583 156.202 173.612 1.00 154.15 ? 770  ALA B O     1 
ATOM   11499 C  CB    . ALA B 1 770 ? 131.714 158.262 176.015 1.00 154.88 ? 770  ALA B CB    1 
ATOM   11500 N  N     . LYS B 1 771 ? 132.655 155.240 175.645 1.00 154.39 ? 771  LYS B N     1 
ATOM   11501 C  CA    . LYS B 1 771 ? 133.650 154.256 175.229 1.00 157.38 ? 771  LYS B CA    1 
ATOM   11502 C  C     . LYS B 1 771 ? 133.088 153.318 174.168 1.00 158.92 ? 771  LYS B C     1 
ATOM   11503 O  O     . LYS B 1 771 ? 133.768 153.001 173.185 1.00 162.70 ? 771  LYS B O     1 
ATOM   11504 C  CB    . LYS B 1 771 ? 134.137 153.463 176.441 1.00 160.80 ? 771  LYS B CB    1 
ATOM   11505 C  CG    . LYS B 1 771 ? 135.214 152.436 176.132 1.00 160.20 ? 771  LYS B CG    1 
ATOM   11506 C  CD    . LYS B 1 771 ? 135.603 151.663 177.383 1.00 161.35 ? 771  LYS B CD    1 
ATOM   11507 C  CE    . LYS B 1 771 ? 136.114 152.592 178.472 1.00 159.28 ? 771  LYS B CE    1 
ATOM   11508 N  NZ    . LYS B 1 771 ? 136.433 151.851 179.723 1.00 156.39 ? 771  LYS B NZ    1 
ATOM   11509 N  N     . ARG B 1 772 ? 131.847 152.861 174.353 1.00 157.87 ? 772  ARG B N     1 
ATOM   11510 C  CA    . ARG B 1 772 ? 131.218 152.007 173.349 1.00 156.60 ? 772  ARG B CA    1 
ATOM   11511 C  C     . ARG B 1 772 ? 131.083 152.734 172.017 1.00 156.88 ? 772  ARG B C     1 
ATOM   11512 O  O     . ARG B 1 772 ? 131.355 152.161 170.954 1.00 159.24 ? 772  ARG B O     1 
ATOM   11513 C  CB    . ARG B 1 772 ? 129.846 151.541 173.833 1.00 157.52 ? 772  ARG B CB    1 
ATOM   11514 C  CG    . ARG B 1 772 ? 129.807 150.135 174.411 1.00 158.40 ? 772  ARG B CG    1 
ATOM   11515 C  CD    . ARG B 1 772 ? 130.133 150.131 175.893 1.00 160.37 ? 772  ARG B CD    1 
ATOM   11516 N  NE    . ARG B 1 772 ? 129.497 149.014 176.581 1.00 164.98 ? 772  ARG B NE    1 
ATOM   11517 C  CZ    . ARG B 1 772 ? 130.117 147.896 176.932 1.00 163.59 ? 772  ARG B CZ    1 
ATOM   11518 N  NH1   . ARG B 1 772 ? 131.402 147.710 176.679 1.00 164.91 ? 772  ARG B NH1   1 
ATOM   11519 N  NH2   . ARG B 1 772 ? 129.431 146.941 177.552 1.00 158.71 ? 772  ARG B NH2   1 
ATOM   11520 N  N     . ARG B 1 773 ? 130.659 153.999 172.058 1.00 155.15 ? 773  ARG B N     1 
ATOM   11521 C  CA    . ARG B 1 773 ? 130.506 154.775 170.833 1.00 156.86 ? 773  ARG B CA    1 
ATOM   11522 C  C     . ARG B 1 773 ? 131.846 154.977 170.137 1.00 159.09 ? 773  ARG B C     1 
ATOM   11523 O  O     . ARG B 1 773 ? 131.937 154.879 168.908 1.00 161.95 ? 773  ARG B O     1 
ATOM   11524 C  CB    . ARG B 1 773 ? 129.854 156.121 171.150 1.00 154.89 ? 773  ARG B CB    1 
ATOM   11525 C  CG    . ARG B 1 773 ? 129.222 156.810 169.955 1.00 156.90 ? 773  ARG B CG    1 
ATOM   11526 C  CD    . ARG B 1 773 ? 128.094 155.980 169.360 1.00 156.89 ? 773  ARG B CD    1 
ATOM   11527 N  NE    . ARG B 1 773 ? 127.265 155.345 170.378 1.00 156.12 ? 773  ARG B NE    1 
ATOM   11528 C  CZ    . ARG B 1 773 ? 126.360 155.976 171.115 1.00 154.67 ? 773  ARG B CZ    1 
ATOM   11529 N  NH1   . ARG B 1 773 ? 126.140 157.274 170.979 1.00 154.24 ? 773  ARG B NH1   1 
ATOM   11530 N  NH2   . ARG B 1 773 ? 125.655 155.287 172.007 1.00 149.43 ? 773  ARG B NH2   1 
ATOM   11531 N  N     . ALA B 1 774 ? 132.898 155.259 170.908 1.00 157.23 ? 774  ALA B N     1 
ATOM   11532 C  CA    . ALA B 1 774 ? 134.223 155.433 170.322 1.00 155.63 ? 774  ALA B CA    1 
ATOM   11533 C  C     . ALA B 1 774 ? 134.728 154.139 169.700 1.00 156.24 ? 774  ALA B C     1 
ATOM   11534 O  O     . ALA B 1 774 ? 135.329 154.156 168.620 1.00 158.85 ? 774  ALA B O     1 
ATOM   11535 C  CB    . ALA B 1 774 ? 135.203 155.938 171.379 1.00 157.05 ? 774  ALA B CB    1 
ATOM   11536 N  N     . LEU B 1 775 ? 134.503 153.005 170.369 1.00 156.78 ? 775  LEU B N     1 
ATOM   11537 C  CA    . LEU B 1 775 ? 134.912 151.726 169.797 1.00 157.56 ? 775  LEU B CA    1 
ATOM   11538 C  C     . LEU B 1 775 ? 134.163 151.437 168.503 1.00 161.72 ? 775  LEU B C     1 
ATOM   11539 O  O     . LEU B 1 775 ? 134.759 150.977 167.522 1.00 164.31 ? 775  LEU B O     1 
ATOM   11540 C  CB    . LEU B 1 775 ? 134.692 150.598 170.806 1.00 159.23 ? 775  LEU B CB    1 
ATOM   11541 C  CG    . LEU B 1 775 ? 135.628 150.568 172.016 1.00 163.51 ? 775  LEU B CG    1 
ATOM   11542 C  CD1   . LEU B 1 775 ? 135.298 149.389 172.920 1.00 163.35 ? 775  LEU B CD1   1 
ATOM   11543 C  CD2   . LEU B 1 775 ? 137.080 150.517 171.570 1.00 164.25 ? 775  LEU B CD2   1 
ATOM   11544 N  N     . GLU B 1 776 ? 132.854 151.705 168.480 1.00 163.24 ? 776  GLU B N     1 
ATOM   11545 C  CA    . GLU B 1 776 ? 132.084 151.497 167.257 1.00 163.97 ? 776  GLU B CA    1 
ATOM   11546 C  C     . GLU B 1 776 ? 132.582 152.398 166.134 1.00 164.41 ? 776  GLU B C     1 
ATOM   11547 O  O     . GLU B 1 776 ? 132.704 151.961 164.983 1.00 167.92 ? 776  GLU B O     1 
ATOM   11548 C  CB    . GLU B 1 776 ? 130.599 151.740 167.522 1.00 162.88 ? 776  GLU B CB    1 
ATOM   11549 C  CG    . GLU B 1 776 ? 129.721 150.517 167.303 1.00 162.43 ? 776  GLU B CG    1 
ATOM   11550 C  CD    . GLU B 1 776 ? 128.407 150.597 168.057 1.00 167.37 ? 776  GLU B CD    1 
ATOM   11551 O  OE1   . GLU B 1 776 ? 127.551 151.423 167.678 1.00 172.30 ? 776  GLU B OE1   1 
ATOM   11552 O  OE2   . GLU B 1 776 ? 128.228 149.831 169.027 1.00 162.58 ? 776  GLU B OE2   1 
ATOM   11553 N  N     . GLU B 1 777 ? 132.878 153.661 166.451 1.00 162.74 ? 777  GLU B N     1 
ATOM   11554 C  CA    . GLU B 1 777 ? 133.364 154.583 165.430 1.00 164.22 ? 777  GLU B CA    1 
ATOM   11555 C  C     . GLU B 1 777 ? 134.726 154.155 164.899 1.00 164.08 ? 777  GLU B C     1 
ATOM   11556 O  O     . GLU B 1 777 ? 134.981 154.237 163.693 1.00 165.35 ? 777  GLU B O     1 
ATOM   11557 C  CB    . GLU B 1 777 ? 133.429 156.003 165.994 1.00 164.87 ? 777  GLU B CB    1 
ATOM   11558 C  CG    . GLU B 1 777 ? 132.212 156.878 165.687 1.00 166.09 ? 777  GLU B CG    1 
ATOM   11559 C  CD    . GLU B 1 777 ? 131.604 156.634 164.313 1.00 169.10 ? 777  GLU B CD    1 
ATOM   11560 O  OE1   . GLU B 1 777 ? 132.356 156.461 163.330 1.00 169.21 ? 777  GLU B OE1   1 
ATOM   11561 O  OE2   . GLU B 1 777 ? 130.359 156.610 164.219 1.00 171.86 ? 777  GLU B OE2   1 
ATOM   11562 N  N     . LEU B 1 778 ? 135.618 153.701 165.783 1.00 163.55 ? 778  LEU B N     1 
ATOM   11563 C  CA    . LEU B 1 778 ? 136.924 153.227 165.335 1.00 162.49 ? 778  LEU B CA    1 
ATOM   11564 C  C     . LEU B 1 778 ? 136.791 151.981 164.471 1.00 163.49 ? 778  LEU B C     1 
ATOM   11565 O  O     . LEU B 1 778 ? 137.507 151.829 163.476 1.00 166.83 ? 778  LEU B O     1 
ATOM   11566 C  CB    . LEU B 1 778 ? 137.831 152.956 166.534 1.00 163.07 ? 778  LEU B CB    1 
ATOM   11567 C  CG    . LEU B 1 778 ? 138.349 154.188 167.278 1.00 161.06 ? 778  LEU B CG    1 
ATOM   11568 C  CD1   . LEU B 1 778 ? 139.374 153.790 168.328 1.00 158.77 ? 778  LEU B CD1   1 
ATOM   11569 C  CD2   . LEU B 1 778 ? 138.937 155.194 166.303 1.00 154.64 ? 778  LEU B CD2   1 
ATOM   11570 N  N     . ARG B 1 779 ? 135.883 151.074 164.838 1.00 162.78 ? 779  ARG B N     1 
ATOM   11571 C  CA    . ARG B 1 779 ? 135.639 149.895 164.014 1.00 163.96 ? 779  ARG B CA    1 
ATOM   11572 C  C     . ARG B 1 779 ? 135.136 150.289 162.632 1.00 164.75 ? 779  ARG B C     1 
ATOM   11573 O  O     . ARG B 1 779 ? 135.587 149.750 161.613 1.00 167.00 ? 779  ARG B O     1 
ATOM   11574 C  CB    . ARG B 1 779 ? 134.636 148.977 164.710 1.00 164.58 ? 779  ARG B CB    1 
ATOM   11575 C  CG    . ARG B 1 779 ? 134.848 147.497 164.455 1.00 166.77 ? 779  ARG B CG    1 
ATOM   11576 C  CD    . ARG B 1 779 ? 133.775 146.679 165.162 1.00 170.76 ? 779  ARG B CD    1 
ATOM   11577 N  NE    . ARG B 1 779 ? 132.433 147.187 164.898 1.00 170.74 ? 779  ARG B NE    1 
ATOM   11578 C  CZ    . ARG B 1 779 ? 131.852 147.221 163.705 1.00 167.69 ? 779  ARG B CZ    1 
ATOM   11579 N  NH1   . ARG B 1 779 ? 132.437 146.713 162.633 1.00 166.12 ? 779  ARG B NH1   1 
ATOM   11580 N  NH2   . ARG B 1 779 ? 130.648 147.773 163.586 1.00 162.87 ? 779  ARG B NH2   1 
ATOM   11581 N  N     . ARG B 1 780 ? 134.195 151.235 162.579 1.00 163.39 ? 780  ARG B N     1 
ATOM   11582 C  CA    . ARG B 1 780 ? 133.673 151.688 161.294 1.00 163.56 ? 780  ARG B CA    1 
ATOM   11583 C  C     . ARG B 1 780 ? 134.761 152.350 160.457 1.00 165.21 ? 780  ARG B C     1 
ATOM   11584 O  O     . ARG B 1 780 ? 134.842 152.126 159.243 1.00 166.50 ? 780  ARG B O     1 
ATOM   11585 C  CB    . ARG B 1 780 ? 132.505 152.649 161.512 1.00 163.59 ? 780  ARG B CB    1 
ATOM   11586 C  CG    . ARG B 1 780 ? 131.356 152.450 160.543 1.00 165.23 ? 780  ARG B CG    1 
ATOM   11587 C  CD    . ARG B 1 780 ? 130.602 151.163 160.843 1.00 166.05 ? 780  ARG B CD    1 
ATOM   11588 N  NE    . ARG B 1 780 ? 129.932 151.197 162.139 1.00 169.85 ? 780  ARG B NE    1 
ATOM   11589 C  CZ    . ARG B 1 780 ? 128.873 151.944 162.421 1.00 165.61 ? 780  ARG B CZ    1 
ATOM   11590 N  NH1   . ARG B 1 780 ? 128.317 152.729 161.513 1.00 161.88 ? 780  ARG B NH1   1 
ATOM   11591 N  NH2   . ARG B 1 780 ? 128.354 151.897 163.645 1.00 159.66 ? 780  ARG B NH2   1 
ATOM   11592 N  N     . GLU B 1 781 ? 135.607 153.166 161.089 1.00 166.04 ? 781  GLU B N     1 
ATOM   11593 C  CA    . GLU B 1 781 ? 136.691 153.817 160.362 1.00 165.93 ? 781  GLU B CA    1 
ATOM   11594 C  C     . GLU B 1 781 ? 137.694 152.801 159.834 1.00 165.22 ? 781  GLU B C     1 
ATOM   11595 O  O     . GLU B 1 781 ? 138.182 152.936 158.708 1.00 167.05 ? 781  GLU B O     1 
ATOM   11596 C  CB    . GLU B 1 781 ? 137.388 154.842 161.260 1.00 165.79 ? 781  GLU B CB    1 
ATOM   11597 C  CG    . GLU B 1 781 ? 136.579 156.106 161.575 1.00 169.06 ? 781  GLU B CG    1 
ATOM   11598 C  CD    . GLU B 1 781 ? 135.983 156.802 160.355 1.00 169.36 ? 781  GLU B CD    1 
ATOM   11599 O  OE1   . GLU B 1 781 ? 135.115 157.679 160.554 1.00 170.97 ? 781  GLU B OE1   1 
ATOM   11600 O  OE2   . GLU B 1 781 ? 136.403 156.529 159.212 1.00 167.98 ? 781  GLU B OE2   1 
ATOM   11601 N  N     . GLU B 1 782 ? 138.022 151.783 160.632 1.00 165.06 ? 782  GLU B N     1 
ATOM   11602 C  CA    . GLU B 1 782 ? 138.930 150.743 160.160 1.00 163.68 ? 782  GLU B CA    1 
ATOM   11603 C  C     . GLU B 1 782 ? 138.331 149.973 158.991 1.00 162.90 ? 782  GLU B C     1 
ATOM   11604 O  O     . GLU B 1 782 ? 139.032 149.664 158.021 1.00 165.04 ? 782  GLU B O     1 
ATOM   11605 C  CB    . GLU B 1 782 ? 139.286 149.792 161.301 1.00 164.28 ? 782  GLU B CB    1 
ATOM   11606 C  CG    . GLU B 1 782 ? 140.703 149.249 161.222 1.00 168.30 ? 782  GLU B CG    1 
ATOM   11607 C  CD    . GLU B 1 782 ? 141.744 150.281 161.600 1.00 177.22 ? 782  GLU B CD    1 
ATOM   11608 O  OE1   . GLU B 1 782 ? 141.424 151.186 162.399 1.00 181.46 ? 782  GLU B OE1   1 
ATOM   11609 O  OE2   . GLU B 1 782 ? 142.883 150.189 161.097 1.00 179.36 ? 782  GLU B OE2   1 
ATOM   11610 N  N     . LYS B 1 783 ? 137.039 149.646 159.068 1.00 160.89 ? 783  LYS B N     1 
ATOM   11611 C  CA    . LYS B 1 783 ? 136.395 148.957 157.954 1.00 157.92 ? 783  LYS B CA    1 
ATOM   11612 C  C     . LYS B 1 783 ? 136.410 149.814 156.694 1.00 160.15 ? 783  LYS B C     1 
ATOM   11613 O  O     . LYS B 1 783 ? 136.694 149.316 155.598 1.00 163.29 ? 783  LYS B O     1 
ATOM   11614 C  CB    . LYS B 1 783 ? 134.965 148.571 158.325 1.00 159.62 ? 783  LYS B CB    1 
ATOM   11615 C  CG    . LYS B 1 783 ? 134.418 147.401 157.522 1.00 161.44 ? 783  LYS B CG    1 
ATOM   11616 C  CD    . LYS B 1 783 ? 133.203 146.784 158.192 1.00 162.71 ? 783  LYS B CD    1 
ATOM   11617 C  CE    . LYS B 1 783 ? 133.537 146.285 159.587 1.00 168.57 ? 783  LYS B CE    1 
ATOM   11618 N  NZ    . LYS B 1 783 ? 134.794 145.487 159.607 1.00 172.10 ? 783  LYS B NZ    1 
ATOM   11619 N  N     . GLU B 1 784 ? 136.116 151.108 156.833 1.00 159.59 ? 784  GLU B N     1 
ATOM   11620 C  CA    . GLU B 1 784 ? 136.138 152.002 155.680 1.00 161.06 ? 784  GLU B CA    1 
ATOM   11621 C  C     . GLU B 1 784 ? 137.540 152.117 155.095 1.00 160.41 ? 784  GLU B C     1 
ATOM   11622 O  O     . GLU B 1 784 ? 137.712 152.127 153.871 1.00 161.41 ? 784  GLU B O     1 
ATOM   11623 C  CB    . GLU B 1 784 ? 135.595 153.375 156.079 1.00 162.91 ? 784  GLU B CB    1 
ATOM   11624 C  CG    . GLU B 1 784 ? 135.209 154.274 154.914 1.00 166.96 ? 784  GLU B CG    1 
ATOM   11625 C  CD    . GLU B 1 784 ? 136.317 155.228 154.505 1.00 170.55 ? 784  GLU B CD    1 
ATOM   11626 O  OE1   . GLU B 1 784 ? 136.019 156.207 153.789 1.00 171.23 ? 784  GLU B OE1   1 
ATOM   11627 O  OE2   . GLU B 1 784 ? 137.478 155.018 154.912 1.00 169.76 ? 784  GLU B OE2   1 
ATOM   11628 N  N     . ARG B 1 785 ? 138.556 152.211 155.955 1.00 158.72 ? 785  ARG B N     1 
ATOM   11629 C  CA    . ARG B 1 785 ? 139.930 152.317 155.475 1.00 156.45 ? 785  ARG B CA    1 
ATOM   11630 C  C     . ARG B 1 785 ? 140.364 151.046 154.757 1.00 156.30 ? 785  ARG B C     1 
ATOM   11631 O  O     . ARG B 1 785 ? 141.044 151.108 153.726 1.00 158.50 ? 785  ARG B O     1 
ATOM   11632 C  CB    . ARG B 1 785 ? 140.864 152.629 156.642 1.00 162.00 ? 785  ARG B CB    1 
ATOM   11633 C  CG    . ARG B 1 785 ? 141.896 153.703 156.346 1.00 163.98 ? 785  ARG B CG    1 
ATOM   11634 C  CD    . ARG B 1 785 ? 143.078 153.614 157.298 1.00 168.54 ? 785  ARG B CD    1 
ATOM   11635 N  NE    . ARG B 1 785 ? 142.658 153.531 158.692 1.00 172.87 ? 785  ARG B NE    1 
ATOM   11636 C  CZ    . ARG B 1 785 ? 142.455 154.580 159.476 1.00 176.34 ? 785  ARG B CZ    1 
ATOM   11637 N  NH1   . ARG B 1 785 ? 142.620 155.816 159.034 1.00 177.05 ? 785  ARG B NH1   1 
ATOM   11638 N  NH2   . ARG B 1 785 ? 142.077 154.385 160.736 1.00 174.87 ? 785  ARG B NH2   1 
ATOM   11639 N  N     . VAL B 1 786 ? 139.982 149.882 155.285 1.00 157.09 ? 786  VAL B N     1 
ATOM   11640 C  CA    . VAL B 1 786 ? 140.310 148.620 154.626 1.00 156.51 ? 786  VAL B CA    1 
ATOM   11641 C  C     . VAL B 1 786 ? 139.604 148.524 153.279 1.00 158.33 ? 786  VAL B C     1 
ATOM   11642 O  O     . VAL B 1 786 ? 140.185 148.066 152.285 1.00 158.97 ? 786  VAL B O     1 
ATOM   11643 C  CB    . VAL B 1 786 ? 139.959 147.434 155.544 1.00 160.53 ? 786  VAL B CB    1 
ATOM   11644 C  CG1   . VAL B 1 786 ? 139.638 146.192 154.728 1.00 161.54 ? 786  VAL B CG1   1 
ATOM   11645 C  CG2   . VAL B 1 786 ? 141.100 147.161 156.510 1.00 160.08 ? 786  VAL B CG2   1 
ATOM   11646 N  N     . GLU B 1 787 ? 138.341 148.953 153.221 1.00 159.12 ? 787  GLU B N     1 
ATOM   11647 C  CA    . GLU B 1 787 ? 137.621 148.947 151.953 1.00 158.55 ? 787  GLU B CA    1 
ATOM   11648 C  C     . GLU B 1 787 ? 138.279 149.878 150.942 1.00 155.66 ? 787  GLU B C     1 
ATOM   11649 O  O     . GLU B 1 787 ? 138.369 149.552 149.756 1.00 156.21 ? 787  GLU B O     1 
ATOM   11650 C  CB    . GLU B 1 787 ? 136.160 149.337 152.176 1.00 164.42 ? 787  GLU B CB    1 
ATOM   11651 C  CG    . GLU B 1 787 ? 135.353 149.490 150.896 1.00 169.46 ? 787  GLU B CG    1 
ATOM   11652 C  CD    . GLU B 1 787 ? 133.940 149.982 151.150 1.00 176.49 ? 787  GLU B CD    1 
ATOM   11653 O  OE1   . GLU B 1 787 ? 133.586 150.204 152.327 1.00 177.66 ? 787  GLU B OE1   1 
ATOM   11654 O  OE2   . GLU B 1 787 ? 133.182 150.141 150.170 1.00 177.06 ? 787  GLU B OE2   1 
ATOM   11655 N  N     . ASN B 1 788 ? 138.741 151.047 151.391 1.00 153.14 ? 788  ASN B N     1 
ATOM   11656 C  CA    . ASN B 1 788 ? 139.425 151.970 150.489 1.00 150.87 ? 788  ASN B CA    1 
ATOM   11657 C  C     . ASN B 1 788 ? 140.745 151.378 150.002 1.00 151.17 ? 788  ASN B C     1 
ATOM   11658 O  O     . ASN B 1 788 ? 141.106 151.527 148.827 1.00 150.80 ? 788  ASN B O     1 
ATOM   11659 C  CB    . ASN B 1 788 ? 139.635 153.313 151.195 1.00 153.31 ? 788  ASN B CB    1 
ATOM   11660 C  CG    . ASN B 1 788 ? 140.454 154.308 150.380 1.00 155.71 ? 788  ASN B CG    1 
ATOM   11661 O  OD1   . ASN B 1 788 ? 141.568 154.025 149.941 1.00 157.95 ? 788  ASN B OD1   1 
ATOM   11662 N  ND2   . ASN B 1 788 ? 139.893 155.495 150.181 1.00 154.05 ? 788  ASN B ND2   1 
ATOM   11663 N  N     . ARG B 1 789 ? 141.484 150.711 150.893 1.00 154.21 ? 789  ARG B N     1 
ATOM   11664 C  CA    . ARG B 1 789 ? 142.701 150.018 150.482 1.00 153.05 ? 789  ARG B CA    1 
ATOM   11665 C  C     . ARG B 1 789 ? 142.405 148.989 149.403 1.00 150.10 ? 789  ARG B C     1 
ATOM   11666 O  O     . ARG B 1 789 ? 143.098 148.925 148.381 1.00 151.74 ? 789  ARG B O     1 
ATOM   11667 C  CB    . ARG B 1 789 ? 143.341 149.329 151.684 1.00 156.59 ? 789  ARG B CB    1 
ATOM   11668 C  CG    . ARG B 1 789 ? 144.827 149.073 151.535 1.00 155.72 ? 789  ARG B CG    1 
ATOM   11669 C  CD    . ARG B 1 789 ? 145.457 148.673 152.865 1.00 162.33 ? 789  ARG B CD    1 
ATOM   11670 N  NE    . ARG B 1 789 ? 145.285 149.674 153.917 1.00 165.93 ? 789  ARG B NE    1 
ATOM   11671 C  CZ    . ARG B 1 789 ? 145.512 149.465 155.206 1.00 166.76 ? 789  ARG B CZ    1 
ATOM   11672 N  NH1   . ARG B 1 789 ? 145.837 148.265 155.663 1.00 165.01 ? 789  ARG B NH1   1 
ATOM   11673 N  NH2   . ARG B 1 789 ? 145.407 150.485 156.053 1.00 167.43 ? 789  ARG B NH2   1 
ATOM   11674 N  N     . LYS B 1 790 ? 141.382 148.163 149.625 1.00 149.41 ? 790  LYS B N     1 
ATOM   11675 C  CA    . LYS B 1 790 ? 141.037 147.137 148.648 1.00 147.30 ? 790  LYS B CA    1 
ATOM   11676 C  C     . LYS B 1 790 ? 140.596 147.761 147.333 1.00 146.88 ? 790  LYS B C     1 
ATOM   11677 O  O     . LYS B 1 790 ? 140.938 147.261 146.256 1.00 147.50 ? 790  LYS B O     1 
ATOM   11678 C  CB    . LYS B 1 790 ? 139.947 146.221 149.205 1.00 150.86 ? 790  LYS B CB    1 
ATOM   11679 C  CG    . LYS B 1 790 ? 140.442 144.833 149.584 1.00 154.11 ? 790  LYS B CG    1 
ATOM   11680 C  CD    . LYS B 1 790 ? 141.774 144.909 150.312 1.00 155.24 ? 790  LYS B CD    1 
ATOM   11681 C  CE    . LYS B 1 790 ? 142.403 143.536 150.463 1.00 151.94 ? 790  LYS B CE    1 
ATOM   11682 N  NZ    . LYS B 1 790 ? 143.777 143.615 151.030 1.00 148.22 ? 790  LYS B NZ    1 
ATOM   11683 N  N     . LYS B 1 791 ? 139.838 148.858 147.399 1.00 148.76 ? 791  LYS B N     1 
ATOM   11684 C  CA    . LYS B 1 791 ? 139.395 149.537 146.186 1.00 148.43 ? 791  LYS B CA    1 
ATOM   11685 C  C     . LYS B 1 791 ? 140.580 150.048 145.379 1.00 145.53 ? 791  LYS B C     1 
ATOM   11686 O  O     . LYS B 1 791 ? 140.657 149.827 144.168 1.00 146.82 ? 791  LYS B O     1 
ATOM   11687 C  CB    . LYS B 1 791 ? 138.450 150.686 146.541 1.00 148.95 ? 791  LYS B CB    1 
ATOM   11688 C  CG    . LYS B 1 791 ? 138.581 151.905 145.638 1.00 145.97 ? 791  LYS B CG    1 
ATOM   11689 C  CD    . LYS B 1 791 ? 137.723 153.057 146.125 1.00 145.71 ? 791  LYS B CD    1 
ATOM   11690 C  CE    . LYS B 1 791 ? 137.936 154.292 145.267 1.00 145.46 ? 791  LYS B CE    1 
ATOM   11691 N  NZ    . LYS B 1 791 ? 137.141 155.451 145.754 1.00 145.33 ? 791  LYS B NZ    1 
ATOM   11692 N  N     . ASN B 1 792 ? 141.522 150.728 146.037 1.00 142.51 ? 792  ASN B N     1 
ATOM   11693 C  CA    . ASN B 1 792 ? 142.682 151.245 145.316 1.00 140.17 ? 792  ASN B CA    1 
ATOM   11694 C  C     . ASN B 1 792 ? 143.526 150.112 144.747 1.00 141.23 ? 792  ASN B C     1 
ATOM   11695 O  O     . ASN B 1 792 ? 143.983 150.182 143.598 1.00 142.75 ? 792  ASN B O     1 
ATOM   11696 C  CB    . ASN B 1 792 ? 143.524 152.132 146.231 1.00 144.53 ? 792  ASN B CB    1 
ATOM   11697 C  CG    . ASN B 1 792 ? 143.049 153.569 146.241 1.00 147.62 ? 792  ASN B CG    1 
ATOM   11698 O  OD1   . ASN B 1 792 ? 141.920 153.863 145.852 1.00 147.36 ? 792  ASN B OD1   1 
ATOM   11699 N  ND2   . ASN B 1 792 ? 143.913 154.475 146.685 1.00 148.57 ? 792  ASN B ND2   1 
ATOM   11700 N  N     . PHE B 1 793 ? 143.731 149.051 145.531 1.00 143.60 ? 793  PHE B N     1 
ATOM   11701 C  CA    . PHE B 1 793 ? 144.554 147.937 145.076 1.00 143.25 ? 793  PHE B CA    1 
ATOM   11702 C  C     . PHE B 1 793 ? 143.928 147.257 143.865 1.00 142.37 ? 793  PHE B C     1 
ATOM   11703 O  O     . PHE B 1 793 ? 144.607 147.012 142.860 1.00 143.96 ? 793  PHE B O     1 
ATOM   11704 C  CB    . PHE B 1 793 ? 144.730 146.939 146.218 1.00 149.94 ? 793  PHE B CB    1 
ATOM   11705 C  CG    . PHE B 1 793 ? 145.827 147.300 147.180 1.00 155.51 ? 793  PHE B CG    1 
ATOM   11706 C  CD1   . PHE B 1 793 ? 146.437 148.540 147.123 1.00 152.22 ? 793  PHE B CD1   1 
ATOM   11707 C  CD2   . PHE B 1 793 ? 146.227 146.407 148.157 1.00 160.23 ? 793  PHE B CD2   1 
ATOM   11708 C  CE1   . PHE B 1 793 ? 147.435 148.877 148.014 1.00 155.17 ? 793  PHE B CE1   1 
ATOM   11709 C  CE2   . PHE B 1 793 ? 147.219 146.744 149.055 1.00 161.36 ? 793  PHE B CE2   1 
ATOM   11710 C  CZ    . PHE B 1 793 ? 147.829 147.978 148.977 1.00 159.13 ? 793  PHE B CZ    1 
ATOM   11711 N  N     . GLU B 1 794 ? 142.627 146.963 143.939 1.00 143.84 ? 794  GLU B N     1 
ATOM   11712 C  CA    . GLU B 1 794 ? 141.939 146.313 142.831 1.00 140.74 ? 794  GLU B CA    1 
ATOM   11713 C  C     . GLU B 1 794 ? 141.867 147.220 141.612 1.00 136.08 ? 794  GLU B C     1 
ATOM   11714 O  O     . GLU B 1 794 ? 141.963 146.746 140.476 1.00 136.58 ? 794  GLU B O     1 
ATOM   11715 C  CB    . GLU B 1 794 ? 140.537 145.890 143.266 1.00 146.26 ? 794  GLU B CB    1 
ATOM   11716 C  CG    . GLU B 1 794 ? 140.507 144.701 144.208 1.00 152.15 ? 794  GLU B CG    1 
ATOM   11717 C  CD    . GLU B 1 794 ? 139.095 144.290 144.576 1.00 156.88 ? 794  GLU B CD    1 
ATOM   11718 O  OE1   . GLU B 1 794 ? 138.188 145.146 144.506 1.00 153.46 ? 794  GLU B OE1   1 
ATOM   11719 O  OE2   . GLU B 1 794 ? 138.892 143.112 144.936 1.00 161.77 ? 794  GLU B OE2   1 
ATOM   11720 N  N     . ALA B 1 795 ? 141.676 148.525 141.821 1.00 137.11 ? 795  ALA B N     1 
ATOM   11721 C  CA    . ALA B 1 795 ? 141.632 149.447 140.694 1.00 135.18 ? 795  ALA B CA    1 
ATOM   11722 C  C     . ALA B 1 795 ? 142.970 149.495 139.974 1.00 131.37 ? 795  ALA B C     1 
ATOM   11723 O  O     . ALA B 1 795 ? 143.017 149.484 138.740 1.00 131.73 ? 795  ALA B O     1 
ATOM   11724 C  CB    . ALA B 1 795 ? 141.227 150.841 141.170 1.00 138.07 ? 795  ALA B CB    1 
ATOM   11725 N  N     . PHE B 1 796 ? 144.071 149.541 140.726 1.00 130.90 ? 796  PHE B N     1 
ATOM   11726 C  CA    . PHE B 1 796 ? 145.385 149.520 140.093 1.00 129.87 ? 796  PHE B CA    1 
ATOM   11727 C  C     . PHE B 1 796 ? 145.620 148.199 139.374 1.00 128.43 ? 796  PHE B C     1 
ATOM   11728 O  O     . PHE B 1 796 ? 146.161 148.170 138.261 1.00 129.71 ? 796  PHE B O     1 
ATOM   11729 C  CB    . PHE B 1 796 ? 146.475 149.769 141.131 1.00 134.27 ? 796  PHE B CB    1 
ATOM   11730 C  CG    . PHE B 1 796 ? 147.830 149.997 140.537 1.00 134.01 ? 796  PHE B CG    1 
ATOM   11731 C  CD1   . PHE B 1 796 ? 148.078 151.114 139.761 1.00 130.85 ? 796  PHE B CD1   1 
ATOM   11732 C  CD2   . PHE B 1 796 ? 148.859 149.099 140.757 1.00 138.12 ? 796  PHE B CD2   1 
ATOM   11733 C  CE1   . PHE B 1 796 ? 149.323 151.332 139.213 1.00 136.13 ? 796  PHE B CE1   1 
ATOM   11734 C  CE2   . PHE B 1 796 ? 150.106 149.311 140.210 1.00 139.86 ? 796  PHE B CE2   1 
ATOM   11735 C  CZ    . PHE B 1 796 ? 150.339 150.428 139.438 1.00 140.62 ? 796  PHE B CZ    1 
ATOM   11736 N  N     . ARG B 1 797 ? 145.214 147.088 139.998 1.00 128.02 ? 797  ARG B N     1 
ATOM   11737 C  CA    . ARG B 1 797 ? 145.350 145.784 139.359 1.00 128.53 ? 797  ARG B CA    1 
ATOM   11738 C  C     . ARG B 1 797 ? 144.615 145.760 138.028 1.00 126.86 ? 797  ARG B C     1 
ATOM   11739 O  O     . ARG B 1 797 ? 145.183 145.367 137.003 1.00 125.75 ? 797  ARG B O     1 
ATOM   11740 C  CB    . ARG B 1 797 ? 144.834 144.691 140.309 1.00 137.11 ? 797  ARG B CB    1 
ATOM   11741 C  CG    . ARG B 1 797 ? 144.753 143.229 139.793 1.00 138.57 ? 797  ARG B CG    1 
ATOM   11742 C  CD    . ARG B 1 797 ? 143.690 142.923 138.733 1.00 136.23 ? 797  ARG B CD    1 
ATOM   11743 N  NE    . ARG B 1 797 ? 142.331 143.202 139.183 1.00 140.58 ? 797  ARG B NE    1 
ATOM   11744 C  CZ    . ARG B 1 797 ? 141.686 142.505 140.108 1.00 143.15 ? 797  ARG B CZ    1 
ATOM   11745 N  NH1   . ARG B 1 797 ? 142.244 141.466 140.708 1.00 143.10 ? 797  ARG B NH1   1 
ATOM   11746 N  NH2   . ARG B 1 797 ? 140.444 142.851 140.433 1.00 142.95 ? 797  ARG B NH2   1 
ATOM   11747 N  N     . THR B 1 798 ? 143.349 146.176 138.028 1.00 128.84 ? 798  THR B N     1 
ATOM   11748 C  CA    . THR B 1 798 ? 142.550 146.136 136.811 1.00 125.00 ? 798  THR B CA    1 
ATOM   11749 C  C     . THR B 1 798 ? 143.100 147.085 135.757 1.00 121.19 ? 798  THR B C     1 
ATOM   11750 O  O     . THR B 1 798 ? 143.142 146.741 134.573 1.00 122.55 ? 798  THR B O     1 
ATOM   11751 C  CB    . THR B 1 798 ? 141.092 146.469 137.128 1.00 129.53 ? 798  THR B CB    1 
ATOM   11752 O  OG1   . THR B 1 798 ? 140.542 145.448 137.968 1.00 135.04 ? 798  THR B OG1   1 
ATOM   11753 C  CG2   . THR B 1 798 ? 140.277 146.556 135.854 1.00 125.59 ? 798  THR B CG2   1 
ATOM   11754 N  N     . ASN B 1 799 ? 143.536 148.280 136.162 1.00 120.47 ? 799  ASN B N     1 
ATOM   11755 C  CA    . ASN B 1 799 ? 144.075 149.227 135.191 1.00 119.42 ? 799  ASN B CA    1 
ATOM   11756 C  C     . ASN B 1 799 ? 145.334 148.685 134.530 1.00 118.24 ? 799  ASN B C     1 
ATOM   11757 O  O     . ASN B 1 799 ? 145.475 148.748 133.302 1.00 121.40 ? 799  ASN B O     1 
ATOM   11758 C  CB    . ASN B 1 799 ? 144.357 150.567 135.866 1.00 122.23 ? 799  ASN B CB    1 
ATOM   11759 C  CG    . ASN B 1 799 ? 143.093 151.321 136.209 1.00 131.83 ? 799  ASN B CG    1 
ATOM   11760 O  OD1   . ASN B 1 799 ? 141.998 150.761 136.187 1.00 132.49 ? 799  ASN B OD1   1 
ATOM   11761 N  ND2   . ASN B 1 799 ? 143.235 152.601 136.531 1.00 139.07 ? 799  ASN B ND2   1 
ATOM   11762 N  N     . VAL B 1 800 ? 146.254 148.128 135.321 1.00 114.83 ? 800  VAL B N     1 
ATOM   11763 C  CA    . VAL B 1 800 ? 147.497 147.620 134.749 1.00 111.81 ? 800  VAL B CA    1 
ATOM   11764 C  C     . VAL B 1 800 ? 147.225 146.391 133.889 1.00 111.87 ? 800  VAL B C     1 
ATOM   11765 O  O     . VAL B 1 800 ? 147.819 146.223 132.815 1.00 110.96 ? 800  VAL B O     1 
ATOM   11766 C  CB    . VAL B 1 800 ? 148.518 147.330 135.864 1.00 114.04 ? 800  VAL B CB    1 
ATOM   11767 C  CG1   . VAL B 1 800 ? 149.474 146.237 135.445 1.00 114.49 ? 800  VAL B CG1   1 
ATOM   11768 C  CG2   . VAL B 1 800 ? 149.282 148.594 136.211 1.00 121.63 ? 800  VAL B CG2   1 
ATOM   11769 N  N     . LEU B 1 801 ? 146.317 145.519 134.335 1.00 115.04 ? 801  LEU B N     1 
ATOM   11770 C  CA    . LEU B 1 801 ? 145.968 144.348 133.540 1.00 111.76 ? 801  LEU B CA    1 
ATOM   11771 C  C     . LEU B 1 801 ? 145.331 144.744 132.217 1.00 109.48 ? 801  LEU B C     1 
ATOM   11772 O  O     . LEU B 1 801 ? 145.636 144.156 131.175 1.00 111.67 ? 801  LEU B O     1 
ATOM   11773 C  CB    . LEU B 1 801 ? 145.026 143.441 134.323 1.00 111.66 ? 801  LEU B CB    1 
ATOM   11774 C  CG    . LEU B 1 801 ? 144.410 142.315 133.496 1.00 103.77 ? 801  LEU B CG    1 
ATOM   11775 C  CD1   . LEU B 1 801 ? 145.479 141.362 132.994 1.00 107.87 ? 801  LEU B CD1   1 
ATOM   11776 C  CD2   . LEU B 1 801 ? 143.370 141.583 134.305 1.00 114.07 ? 801  LEU B CD2   1 
ATOM   11777 N  N     . LEU B 1 802 ? 144.424 145.721 132.242 1.00 110.88 ? 802  LEU B N     1 
ATOM   11778 C  CA    . LEU B 1 802 ? 143.810 146.185 131.007 1.00 109.00 ? 802  LEU B CA    1 
ATOM   11779 C  C     . LEU B 1 802 ? 144.850 146.793 130.082 1.00 108.70 ? 802  LEU B C     1 
ATOM   11780 O  O     . LEU B 1 802 ? 144.842 146.529 128.877 1.00 111.67 ? 802  LEU B O     1 
ATOM   11781 C  CB    . LEU B 1 802 ? 142.703 147.192 131.311 1.00 106.42 ? 802  LEU B CB    1 
ATOM   11782 C  CG    . LEU B 1 802 ? 141.403 146.602 131.856 1.00 109.97 ? 802  LEU B CG    1 
ATOM   11783 C  CD1   . LEU B 1 802 ? 140.356 147.685 132.029 1.00 114.87 ? 802  LEU B CD1   1 
ATOM   11784 C  CD2   . LEU B 1 802 ? 140.897 145.499 130.947 1.00 107.77 ? 802  LEU B CD2   1 
ATOM   11785 N  N     . THR B 1 803 ? 145.768 147.591 130.631 1.00 104.79 ? 803  THR B N     1 
ATOM   11786 C  CA    . THR B 1 803 ? 146.833 148.154 129.810 1.00 102.97 ? 803  THR B CA    1 
ATOM   11787 C  C     . THR B 1 803 ? 147.639 147.052 129.138 1.00 106.07 ? 803  THR B C     1 
ATOM   11788 O  O     . THR B 1 803 ? 147.851 147.079 127.923 1.00 109.46 ? 803  THR B O     1 
ATOM   11789 C  CB    . THR B 1 803 ? 147.742 149.041 130.657 1.00 105.71 ? 803  THR B CB    1 
ATOM   11790 O  OG1   . THR B 1 803 ? 146.985 150.134 131.190 1.00 115.06 ? 803  THR B OG1   1 
ATOM   11791 C  CG2   . THR B 1 803 ? 148.881 149.586 129.816 1.00 101.85 ? 803  THR B CG2   1 
ATOM   11792 N  N     . TRP B 1 804 ? 148.061 146.050 129.911 1.00 106.81 ? 804  TRP B N     1 
ATOM   11793 C  CA    . TRP B 1 804 ? 148.874 144.969 129.359 1.00 107.38 ? 804  TRP B CA    1 
ATOM   11794 C  C     . TRP B 1 804 ? 148.116 144.188 128.291 1.00 107.97 ? 804  TRP B C     1 
ATOM   11795 O  O     . TRP B 1 804 ? 148.606 144.008 127.167 1.00 108.91 ? 804  TRP B O     1 
ATOM   11796 C  CB    . TRP B 1 804 ? 149.323 144.042 130.487 1.00 106.18 ? 804  TRP B CB    1 
ATOM   11797 C  CG    . TRP B 1 804 ? 150.036 142.815 130.027 1.00 106.67 ? 804  TRP B CG    1 
ATOM   11798 C  CD1   . TRP B 1 804 ? 151.277 142.748 129.474 1.00 108.99 ? 804  TRP B CD1   1 
ATOM   11799 C  CD2   . TRP B 1 804 ? 149.551 141.471 130.091 1.00 109.02 ? 804  TRP B CD2   1 
ATOM   11800 N  NE1   . TRP B 1 804 ? 151.597 141.445 129.186 1.00 111.62 ? 804  TRP B NE1   1 
ATOM   11801 C  CE2   . TRP B 1 804 ? 150.552 140.641 129.556 1.00 109.42 ? 804  TRP B CE2   1 
ATOM   11802 C  CE3   . TRP B 1 804 ? 148.367 140.889 130.547 1.00 113.20 ? 804  TRP B CE3   1 
ATOM   11803 C  CZ2   . TRP B 1 804 ? 150.406 139.263 129.464 1.00 109.15 ? 804  TRP B CZ2   1 
ATOM   11804 C  CZ3   . TRP B 1 804 ? 148.224 139.521 130.455 1.00 114.54 ? 804  TRP B CZ3   1 
ATOM   11805 C  CH2   . TRP B 1 804 ? 149.237 138.723 129.917 1.00 112.08 ? 804  TRP B CH2   1 
ATOM   11806 N  N     . ALA B 1 805 ? 146.911 143.721 128.625 1.00 107.36 ? 805  ALA B N     1 
ATOM   11807 C  CA    . ALA B 1 805 ? 146.160 142.875 127.705 1.00 105.69 ? 805  ALA B CA    1 
ATOM   11808 C  C     . ALA B 1 805 ? 145.786 143.627 126.438 1.00 108.63 ? 805  ALA B C     1 
ATOM   11809 O  O     . ALA B 1 805 ? 145.909 143.090 125.332 1.00 111.11 ? 805  ALA B O     1 
ATOM   11810 C  CB    . ALA B 1 805 ? 144.910 142.330 128.393 1.00 97.34  ? 805  ALA B CB    1 
ATOM   11811 N  N     . PHE B 1 806 ? 145.340 144.878 126.570 1.00 105.97 ? 806  PHE B N     1 
ATOM   11812 C  CA    . PHE B 1 806 ? 144.924 145.624 125.393 1.00 106.77 ? 806  PHE B CA    1 
ATOM   11813 C  C     . PHE B 1 806 ? 146.114 146.089 124.570 1.00 107.33 ? 806  PHE B C     1 
ATOM   11814 O  O     . PHE B 1 806 ? 146.008 146.172 123.345 1.00 110.99 ? 806  PHE B O     1 
ATOM   11815 C  CB    . PHE B 1 806 ? 144.049 146.803 125.804 1.00 108.08 ? 806  PHE B CB    1 
ATOM   11816 C  CG    . PHE B 1 806 ? 142.594 146.457 125.910 1.00 111.80 ? 806  PHE B CG    1 
ATOM   11817 C  CD1   . PHE B 1 806 ? 142.149 145.583 126.885 1.00 115.67 ? 806  PHE B CD1   1 
ATOM   11818 C  CD2   . PHE B 1 806 ? 141.675 146.993 125.030 1.00 114.06 ? 806  PHE B CD2   1 
ATOM   11819 C  CE1   . PHE B 1 806 ? 140.814 145.257 126.984 1.00 116.96 ? 806  PHE B CE1   1 
ATOM   11820 C  CE2   . PHE B 1 806 ? 140.338 146.671 125.126 1.00 117.29 ? 806  PHE B CE2   1 
ATOM   11821 C  CZ    . PHE B 1 806 ? 139.908 145.801 126.104 1.00 116.60 ? 806  PHE B CZ    1 
ATOM   11822 N  N     . SER B 1 807 ? 147.257 146.371 125.200 1.00 103.81 ? 807  SER B N     1 
ATOM   11823 C  CA    . SER B 1 807 ? 148.459 146.659 124.429 1.00 103.01 ? 807  SER B CA    1 
ATOM   11824 C  C     . SER B 1 807 ? 148.868 145.449 123.605 1.00 103.60 ? 807  SER B C     1 
ATOM   11825 O  O     . SER B 1 807 ? 149.180 145.570 122.415 1.00 106.20 ? 807  SER B O     1 
ATOM   11826 C  CB    . SER B 1 807 ? 149.591 147.086 125.360 1.00 103.01 ? 807  SER B CB    1 
ATOM   11827 O  OG    . SER B 1 807 ? 149.269 148.290 126.031 1.00 112.58 ? 807  SER B OG    1 
ATOM   11828 N  N     . ASN B 1 808 ? 148.845 144.262 124.217 1.00 100.11 ? 808  ASN B N     1 
ATOM   11829 C  CA    . ASN B 1 808 ? 149.181 143.053 123.472 1.00 98.37  ? 808  ASN B CA    1 
ATOM   11830 C  C     . ASN B 1 808 ? 148.194 142.811 122.336 1.00 102.09 ? 808  ASN B C     1 
ATOM   11831 O  O     . ASN B 1 808 ? 148.598 142.499 121.210 1.00 104.47 ? 808  ASN B O     1 
ATOM   11832 C  CB    . ASN B 1 808 ? 149.223 141.852 124.414 1.00 100.44 ? 808  ASN B CB    1 
ATOM   11833 C  CG    . ASN B 1 808 ? 150.509 141.782 125.206 1.00 102.25 ? 808  ASN B CG    1 
ATOM   11834 O  OD1   . ASN B 1 808 ? 151.332 140.894 124.997 1.00 100.34 ? 808  ASN B OD1   1 
ATOM   11835 N  ND2   . ASN B 1 808 ? 150.688 142.720 126.123 1.00 107.28 ? 808  ASN B ND2   1 
ATOM   11836 N  N     . LEU B 1 809 ? 146.895 142.963 122.608 1.00 101.40 ? 809  LEU B N     1 
ATOM   11837 C  CA    . LEU B 1 809 ? 145.889 142.725 121.578 1.00 102.77 ? 809  LEU B CA    1 
ATOM   11838 C  C     . LEU B 1 809 ? 146.012 143.721 120.434 1.00 105.04 ? 809  LEU B C     1 
ATOM   11839 O  O     . LEU B 1 809 ? 145.923 143.342 119.261 1.00 106.29 ? 809  LEU B O     1 
ATOM   11840 C  CB    . LEU B 1 809 ? 144.490 142.789 122.186 1.00 102.26 ? 809  LEU B CB    1 
ATOM   11841 C  CG    . LEU B 1 809 ? 143.865 141.456 122.585 1.00 105.20 ? 809  LEU B CG    1 
ATOM   11842 C  CD1   . LEU B 1 809 ? 142.504 141.680 123.209 1.00 114.91 ? 809  LEU B CD1   1 
ATOM   11843 C  CD2   . LEU B 1 809 ? 143.756 140.551 121.376 1.00 106.84 ? 809  LEU B CD2   1 
ATOM   11844 N  N     . ILE B 1 810 ? 146.212 145.001 120.751 1.00 103.54 ? 810  ILE B N     1 
ATOM   11845 C  CA    . ILE B 1 810 ? 146.317 146.020 119.714 1.00 103.07 ? 810  ILE B CA    1 
ATOM   11846 C  C     . ILE B 1 810 ? 147.579 145.813 118.892 1.00 104.03 ? 810  ILE B C     1 
ATOM   11847 O  O     . ILE B 1 810 ? 147.564 145.950 117.664 1.00 107.76 ? 810  ILE B O     1 
ATOM   11848 C  CB    . ILE B 1 810 ? 146.262 147.423 120.342 1.00 102.99 ? 810  ILE B CB    1 
ATOM   11849 C  CG1   . ILE B 1 810 ? 144.837 147.737 120.796 1.00 105.07 ? 810  ILE B CG1   1 
ATOM   11850 C  CG2   . ILE B 1 810 ? 146.746 148.472 119.360 1.00 103.50 ? 810  ILE B CG2   1 
ATOM   11851 C  CD1   . ILE B 1 810 ? 144.674 149.120 121.376 1.00 113.24 ? 810  ILE B CD1   1 
ATOM   11852 N  N     . PHE B 1 811 ? 148.690 145.470 119.547 1.00 98.64  ? 811  PHE B N     1 
ATOM   11853 C  CA    . PHE B 1 811 ? 149.918 145.186 118.815 1.00 97.58  ? 811  PHE B CA    1 
ATOM   11854 C  C     . PHE B 1 811 ? 149.732 143.999 117.879 1.00 100.44 ? 811  PHE B C     1 
ATOM   11855 O  O     . PHE B 1 811 ? 150.131 144.047 116.709 1.00 101.78 ? 811  PHE B O     1 
ATOM   11856 C  CB    . PHE B 1 811 ? 151.058 144.934 119.801 1.00 97.52  ? 811  PHE B CB    1 
ATOM   11857 C  CG    . PHE B 1 811 ? 152.375 144.648 119.149 1.00 95.25  ? 811  PHE B CG    1 
ATOM   11858 C  CD1   . PHE B 1 811 ? 153.107 145.663 118.564 1.00 94.73  ? 811  PHE B CD1   1 
ATOM   11859 C  CD2   . PHE B 1 811 ? 152.891 143.367 119.137 1.00 98.75  ? 811  PHE B CD2   1 
ATOM   11860 C  CE1   . PHE B 1 811 ? 154.322 145.403 117.970 1.00 100.62 ? 811  PHE B CE1   1 
ATOM   11861 C  CE2   . PHE B 1 811 ? 154.106 143.102 118.545 1.00 99.97  ? 811  PHE B CE2   1 
ATOM   11862 C  CZ    . PHE B 1 811 ? 154.821 144.120 117.961 1.00 101.70 ? 811  PHE B CZ    1 
ATOM   11863 N  N     . ALA B 1 812 ? 149.105 142.927 118.373 1.00 99.14  ? 812  ALA B N     1 
ATOM   11864 C  CA    . ALA B 1 812 ? 148.891 141.751 117.538 1.00 96.94  ? 812  ALA B CA    1 
ATOM   11865 C  C     . ALA B 1 812 ? 147.990 142.068 116.353 1.00 102.44 ? 812  ALA B C     1 
ATOM   11866 O  O     . ALA B 1 812 ? 148.274 141.658 115.223 1.00 104.77 ? 812  ALA B O     1 
ATOM   11867 C  CB    . ALA B 1 812 ? 148.299 140.616 118.371 1.00 94.40  ? 812  ALA B CB    1 
ATOM   11868 N  N     . LEU B 1 813 ? 146.901 142.803 116.588 1.00 102.47 ? 813  LEU B N     1 
ATOM   11869 C  CA    . LEU B 1 813 ? 145.988 143.133 115.499 1.00 101.97 ? 813  LEU B CA    1 
ATOM   11870 C  C     . LEU B 1 813 ? 146.651 144.044 114.475 1.00 101.55 ? 813  LEU B C     1 
ATOM   11871 O  O     . LEU B 1 813 ? 146.494 143.843 113.266 1.00 105.00 ? 813  LEU B O     1 
ATOM   11872 C  CB    . LEU B 1 813 ? 144.720 143.781 116.050 1.00 99.03  ? 813  LEU B CB    1 
ATOM   11873 C  CG    . LEU B 1 813 ? 143.790 142.865 116.841 1.00 104.13 ? 813  LEU B CG    1 
ATOM   11874 C  CD1   . LEU B 1 813 ? 142.543 143.615 117.266 1.00 109.78 ? 813  LEU B CD1   1 
ATOM   11875 C  CD2   . LEU B 1 813 ? 143.428 141.642 116.023 1.00 108.50 ? 813  LEU B CD2   1 
ATOM   11876 N  N     . PHE B 1 814 ? 147.396 145.051 114.936 1.00 97.14  ? 814  PHE B N     1 
ATOM   11877 C  CA    . PHE B 1 814 ? 148.045 145.967 114.011 1.00 101.10 ? 814  PHE B CA    1 
ATOM   11878 C  C     . PHE B 1 814 ? 149.165 145.300 113.232 1.00 103.25 ? 814  PHE B C     1 
ATOM   11879 O  O     . PHE B 1 814 ? 149.430 145.700 112.095 1.00 108.43 ? 814  PHE B O     1 
ATOM   11880 C  CB    . PHE B 1 814 ? 148.586 147.184 114.760 1.00 102.67 ? 814  PHE B CB    1 
ATOM   11881 C  CG    . PHE B 1 814 ? 147.565 148.260 114.979 1.00 111.17 ? 814  PHE B CG    1 
ATOM   11882 C  CD1   . PHE B 1 814 ? 146.296 148.147 114.440 1.00 114.02 ? 814  PHE B CD1   1 
ATOM   11883 C  CD2   . PHE B 1 814 ? 147.874 149.387 115.719 1.00 114.19 ? 814  PHE B CD2   1 
ATOM   11884 C  CE1   . PHE B 1 814 ? 145.353 149.134 114.639 1.00 116.65 ? 814  PHE B CE1   1 
ATOM   11885 C  CE2   . PHE B 1 814 ? 146.935 150.378 115.920 1.00 116.57 ? 814  PHE B CE2   1 
ATOM   11886 C  CZ    . PHE B 1 814 ? 145.674 150.251 115.379 1.00 119.73 ? 814  PHE B CZ    1 
ATOM   11887 N  N     . VAL B 1 815 ? 149.825 144.298 113.803 1.00 98.60  ? 815  VAL B N     1 
ATOM   11888 C  CA    . VAL B 1 815 ? 150.808 143.547 113.033 1.00 96.39  ? 815  VAL B CA    1 
ATOM   11889 C  C     . VAL B 1 815 ? 150.131 142.630 112.024 1.00 101.33 ? 815  VAL B C     1 
ATOM   11890 O  O     . VAL B 1 815 ? 150.531 142.584 110.860 1.00 105.01 ? 815  VAL B O     1 
ATOM   11891 C  CB    . VAL B 1 815 ? 151.739 142.761 113.972 1.00 95.93  ? 815  VAL B CB    1 
ATOM   11892 C  CG1   . VAL B 1 815 ? 152.553 141.761 113.180 1.00 99.14  ? 815  VAL B CG1   1 
ATOM   11893 C  CG2   . VAL B 1 815 ? 152.652 143.712 114.716 1.00 98.16  ? 815  VAL B CG2   1 
ATOM   11894 N  N     . VAL B 1 816 ? 149.079 141.921 112.440 1.00 100.10 ? 816  VAL B N     1 
ATOM   11895 C  CA    . VAL B 1 816 ? 148.414 140.975 111.549 1.00 96.32  ? 816  VAL B CA    1 
ATOM   11896 C  C     . VAL B 1 816 ? 147.801 141.697 110.355 1.00 101.75 ? 816  VAL B C     1 
ATOM   11897 O  O     . VAL B 1 816 ? 147.953 141.269 109.206 1.00 101.31 ? 816  VAL B O     1 
ATOM   11898 C  CB    . VAL B 1 816 ? 147.355 140.168 112.321 1.00 88.82  ? 816  VAL B CB    1 
ATOM   11899 C  CG1   . VAL B 1 816 ? 146.360 139.545 111.363 1.00 91.74  ? 816  VAL B CG1   1 
ATOM   11900 C  CG2   . VAL B 1 816 ? 148.017 139.098 113.160 1.00 100.72 ? 816  VAL B CG2   1 
ATOM   11901 N  N     . TYR B 1 817 ? 147.105 142.806 110.606 1.00 104.71 ? 817  TYR B N     1 
ATOM   11902 C  CA    . TYR B 1 817 ? 146.358 143.460 109.538 1.00 105.33 ? 817  TYR B CA    1 
ATOM   11903 C  C     . TYR B 1 817 ? 147.245 144.343 108.669 1.00 104.77 ? 817  TYR B C     1 
ATOM   11904 O  O     . TYR B 1 817 ? 146.976 144.505 107.474 1.00 111.99 ? 817  TYR B O     1 
ATOM   11905 C  CB    . TYR B 1 817 ? 145.214 144.277 110.134 1.00 104.47 ? 817  TYR B CB    1 
ATOM   11906 C  CG    . TYR B 1 817 ? 144.003 143.444 110.470 1.00 105.82 ? 817  TYR B CG    1 
ATOM   11907 C  CD1   . TYR B 1 817 ? 143.682 142.324 109.720 1.00 110.64 ? 817  TYR B CD1   1 
ATOM   11908 C  CD2   . TYR B 1 817 ? 143.194 143.762 111.547 1.00 106.46 ? 817  TYR B CD2   1 
ATOM   11909 C  CE1   . TYR B 1 817 ? 142.582 141.553 110.024 1.00 111.25 ? 817  TYR B CE1   1 
ATOM   11910 C  CE2   . TYR B 1 817 ? 142.094 142.996 111.860 1.00 113.50 ? 817  TYR B CE2   1 
ATOM   11911 C  CZ    . TYR B 1 817 ? 141.792 141.893 111.095 1.00 113.04 ? 817  TYR B CZ    1 
ATOM   11912 O  OH    . TYR B 1 817 ? 140.694 141.127 111.403 1.00 115.33 ? 817  TYR B OH    1 
ATOM   11913 N  N     . PHE B 1 818 ? 148.301 144.919 109.240 1.00 100.28 ? 818  PHE B N     1 
ATOM   11914 C  CA    . PHE B 1 818 ? 149.112 145.902 108.537 1.00 105.01 ? 818  PHE B CA    1 
ATOM   11915 C  C     . PHE B 1 818 ? 150.544 145.453 108.283 1.00 105.52 ? 818  PHE B C     1 
ATOM   11916 O  O     . PHE B 1 818 ? 151.378 146.287 107.917 1.00 106.26 ? 818  PHE B O     1 
ATOM   11917 C  CB    . PHE B 1 818 ? 149.124 147.222 109.314 1.00 106.07 ? 818  PHE B CB    1 
ATOM   11918 C  CG    . PHE B 1 818 ? 147.783 147.888 109.397 1.00 109.74 ? 818  PHE B CG    1 
ATOM   11919 C  CD1   . PHE B 1 818 ? 146.866 147.754 108.372 1.00 110.33 ? 818  PHE B CD1   1 
ATOM   11920 C  CD2   . PHE B 1 818 ? 147.439 148.646 110.501 1.00 111.62 ? 818  PHE B CD2   1 
ATOM   11921 C  CE1   . PHE B 1 818 ? 145.632 148.365 108.446 1.00 111.00 ? 818  PHE B CE1   1 
ATOM   11922 C  CE2   . PHE B 1 818 ? 146.206 149.258 110.580 1.00 113.69 ? 818  PHE B CE2   1 
ATOM   11923 C  CZ    . PHE B 1 818 ? 145.302 149.117 109.551 1.00 115.46 ? 818  PHE B CZ    1 
ATOM   11924 N  N     . ALA B 1 819 ? 150.861 144.173 108.465 1.00 104.66 ? 819  ALA B N     1 
ATOM   11925 C  CA    . ALA B 1 819 ? 152.212 143.691 108.227 1.00 103.82 ? 819  ALA B CA    1 
ATOM   11926 C  C     . ALA B 1 819 ? 152.166 142.258 107.725 1.00 107.07 ? 819  ALA B C     1 
ATOM   11927 O  O     . ALA B 1 819 ? 151.349 141.450 108.174 1.00 108.24 ? 819  ALA B O     1 
ATOM   11928 C  CB    . ALA B 1 819 ? 153.071 143.774 109.493 1.00 102.45 ? 819  ALA B CB    1 
ATOM   11929 N  N     . SER B 1 820 ? 153.056 141.951 106.791 1.00 110.90 ? 820  SER B N     1 
ATOM   11930 C  CA    . SER B 1 820 ? 153.205 140.607 106.258 1.00 116.42 ? 820  SER B CA    1 
ATOM   11931 C  C     . SER B 1 820 ? 154.337 139.884 106.977 1.00 112.10 ? 820  SER B C     1 
ATOM   11932 O  O     . SER B 1 820 ? 155.127 140.483 107.710 1.00 111.40 ? 820  SER B O     1 
ATOM   11933 C  CB    . SER B 1 820 ? 153.467 140.651 104.750 1.00 120.80 ? 820  SER B CB    1 
ATOM   11934 O  OG    . SER B 1 820 ? 153.333 139.365 104.172 1.00 124.17 ? 820  SER B OG    1 
ATOM   11935 N  N     . SER B 1 821 ? 154.408 138.571 106.758 1.00 109.20 ? 821  SER B N     1 
ATOM   11936 C  CA    . SER B 1 821 ? 155.461 137.782 107.387 1.00 108.35 ? 821  SER B CA    1 
ATOM   11937 C  C     . SER B 1 821 ? 156.842 138.183 106.890 1.00 110.53 ? 821  SER B C     1 
ATOM   11938 O  O     . SER B 1 821 ? 157.836 137.968 107.591 1.00 115.52 ? 821  SER B O     1 
ATOM   11939 C  CB    . SER B 1 821 ? 155.226 136.295 107.139 1.00 116.48 ? 821  SER B CB    1 
ATOM   11940 O  OG    . SER B 1 821 ? 156.328 135.528 107.588 1.00 121.99 ? 821  SER B OG    1 
ATOM   11941 N  N     . SER B 1 822 ? 156.930 138.755 105.691 1.00 109.50 ? 822  SER B N     1 
ATOM   11942 C  CA    . SER B 1 822 ? 158.217 139.171 105.152 1.00 113.43 ? 822  SER B CA    1 
ATOM   11943 C  C     . SER B 1 822 ? 158.693 140.506 105.709 1.00 109.66 ? 822  SER B C     1 
ATOM   11944 O  O     . SER B 1 822 ? 159.887 140.807 105.613 1.00 112.46 ? 822  SER B O     1 
ATOM   11945 C  CB    . SER B 1 822 ? 158.146 139.255 103.627 1.00 119.17 ? 822  SER B CB    1 
ATOM   11946 O  OG    . SER B 1 822 ? 157.973 140.594 103.199 1.00 121.76 ? 822  SER B OG    1 
ATOM   11947 N  N     . THR B 1 823 ? 157.799 141.310 106.282 1.00 104.31 ? 823  THR B N     1 
ATOM   11948 C  CA    . THR B 1 823 ? 158.145 142.643 106.756 1.00 108.05 ? 823  THR B CA    1 
ATOM   11949 C  C     . THR B 1 823 ? 158.123 142.755 108.274 1.00 105.81 ? 823  THR B C     1 
ATOM   11950 O  O     . THR B 1 823 ? 158.416 143.828 108.811 1.00 107.95 ? 823  THR B O     1 
ATOM   11951 C  CB    . THR B 1 823 ? 157.203 143.682 106.148 1.00 113.99 ? 823  THR B CB    1 
ATOM   11952 O  OG1   . THR B 1 823 ? 155.904 143.550 106.736 1.00 115.47 ? 823  THR B OG1   1 
ATOM   11953 C  CG2   . THR B 1 823 ? 157.094 143.481 104.646 1.00 115.41 ? 823  THR B CG2   1 
ATOM   11954 N  N     . TYR B 1 824 ? 157.782 141.682 108.974 1.00 102.57 ? 824  TYR B N     1 
ATOM   11955 C  CA    . TYR B 1 824 ? 157.796 141.644 110.431 1.00 101.48 ? 824  TYR B CA    1 
ATOM   11956 C  C     . TYR B 1 824 ? 158.743 140.605 110.997 1.00 102.28 ? 824  TYR B C     1 
ATOM   11957 O  O     . TYR B 1 824 ? 159.472 140.895 111.949 1.00 103.57 ? 824  TYR B O     1 
ATOM   11958 C  CB    . TYR B 1 824 ? 156.389 141.368 110.971 1.00 95.98  ? 824  TYR B CB    1 
ATOM   11959 C  CG    . TYR B 1 824 ? 156.338 141.200 112.472 1.00 91.62  ? 824  TYR B CG    1 
ATOM   11960 C  CD1   . TYR B 1 824 ? 156.345 142.296 113.318 1.00 88.43  ? 824  TYR B CD1   1 
ATOM   11961 C  CD2   . TYR B 1 824 ? 156.289 139.935 113.041 1.00 95.65  ? 824  TYR B CD2   1 
ATOM   11962 C  CE1   . TYR B 1 824 ? 156.298 142.136 114.689 1.00 91.25  ? 824  TYR B CE1   1 
ATOM   11963 C  CE2   . TYR B 1 824 ? 156.243 139.766 114.407 1.00 97.51  ? 824  TYR B CE2   1 
ATOM   11964 C  CZ    . TYR B 1 824 ? 156.247 140.869 115.227 1.00 96.95  ? 824  TYR B CZ    1 
ATOM   11965 O  OH    . TYR B 1 824 ? 156.200 140.701 116.590 1.00 100.95 ? 824  TYR B OH    1 
ATOM   11966 N  N     . MET B 1 825 ? 158.739 139.395 110.448 1.00 100.29 ? 825  MET B N     1 
ATOM   11967 C  CA    . MET B 1 825 ? 159.595 138.348 110.995 1.00 97.64  ? 825  MET B CA    1 
ATOM   11968 C  C     . MET B 1 825 ? 161.078 138.687 110.934 1.00 98.78  ? 825  MET B C     1 
ATOM   11969 O  O     . MET B 1 825 ? 161.796 138.318 111.878 1.00 100.38 ? 825  MET B O     1 
ATOM   11970 C  CB    . MET B 1 825 ? 159.301 137.013 110.308 1.00 94.93  ? 825  MET B CB    1 
ATOM   11971 C  CG    . MET B 1 825 ? 158.052 136.365 110.852 1.00 97.25  ? 825  MET B CG    1 
ATOM   11972 S  SD    . MET B 1 825 ? 158.003 136.450 112.652 1.00 106.91 ? 825  MET B SD    1 
ATOM   11973 C  CE    . MET B 1 825 ? 158.767 134.900 113.102 1.00 101.09 ? 825  MET B CE    1 
ATOM   11974 N  N     . PRO B 1 826 ? 161.614 139.312 109.880 1.00 98.50  ? 826  PRO B N     1 
ATOM   11975 C  CA    . PRO B 1 826 ? 163.007 139.778 109.972 1.00 97.60  ? 826  PRO B CA    1 
ATOM   11976 C  C     . PRO B 1 826 ? 163.239 140.711 111.147 1.00 98.80  ? 826  PRO B C     1 
ATOM   11977 O  O     . PRO B 1 826 ? 164.283 140.625 111.805 1.00 103.92 ? 826  PRO B O     1 
ATOM   11978 C  CB    . PRO B 1 826 ? 163.223 140.478 108.626 1.00 103.06 ? 826  PRO B CB    1 
ATOM   11979 C  CG    . PRO B 1 826 ? 162.299 139.776 107.702 1.00 103.35 ? 826  PRO B CG    1 
ATOM   11980 C  CD    . PRO B 1 826 ? 161.080 139.466 108.516 1.00 102.25 ? 826  PRO B CD    1 
ATOM   11981 N  N     . VAL B 1 827 ? 162.277 141.584 111.448 1.00 96.25  ? 827  VAL B N     1 
ATOM   11982 C  CA    . VAL B 1 827 ? 162.404 142.463 112.608 1.00 96.07  ? 827  VAL B CA    1 
ATOM   11983 C  C     . VAL B 1 827 ? 162.430 141.650 113.896 1.00 97.57  ? 827  VAL B C     1 
ATOM   11984 O  O     . VAL B 1 827 ? 163.242 141.908 114.794 1.00 102.31 ? 827  VAL B O     1 
ATOM   11985 C  CB    . VAL B 1 827 ? 161.266 143.500 112.619 1.00 95.28  ? 827  VAL B CB    1 
ATOM   11986 C  CG1   . VAL B 1 827 ? 161.271 144.283 113.917 1.00 90.72  ? 827  VAL B CG1   1 
ATOM   11987 C  CG2   . VAL B 1 827 ? 161.390 144.436 111.431 1.00 99.05  ? 827  VAL B CG2   1 
ATOM   11988 N  N     . LEU B 1 828 ? 161.539 140.664 114.013 1.00 93.35  ? 828  LEU B N     1 
ATOM   11989 C  CA    . LEU B 1 828 ? 161.505 139.844 115.221 1.00 94.22  ? 828  LEU B CA    1 
ATOM   11990 C  C     . LEU B 1 828 ? 162.792 139.048 115.387 1.00 97.61  ? 828  LEU B C     1 
ATOM   11991 O  O     . LEU B 1 828 ? 163.323 138.932 116.499 1.00 101.24 ? 828  LEU B O     1 
ATOM   11992 C  CB    . LEU B 1 828 ? 160.304 138.905 115.190 1.00 92.85  ? 828  LEU B CB    1 
ATOM   11993 C  CG    . LEU B 1 828 ? 160.036 138.179 116.506 1.00 88.30  ? 828  LEU B CG    1 
ATOM   11994 C  CD1   . LEU B 1 828 ? 159.657 139.170 117.588 1.00 86.48  ? 828  LEU B CD1   1 
ATOM   11995 C  CD2   . LEU B 1 828 ? 158.950 137.137 116.326 1.00 90.20  ? 828  LEU B CD2   1 
ATOM   11996 N  N     . TYR B 1 829 ? 163.302 138.483 114.293 1.00 94.35  ? 829  TYR B N     1 
ATOM   11997 C  CA    . TYR B 1 829 ? 164.560 137.752 114.353 1.00 92.60  ? 829  TYR B CA    1 
ATOM   11998 C  C     . TYR B 1 829 ? 165.704 138.668 114.755 1.00 98.36  ? 829  TYR B C     1 
ATOM   11999 O  O     . TYR B 1 829 ? 166.552 138.284 115.561 1.00 103.73 ? 829  TYR B O     1 
ATOM   12000 C  CB    . TYR B 1 829 ? 164.857 137.086 113.012 1.00 93.18  ? 829  TYR B CB    1 
ATOM   12001 C  CG    . TYR B 1 829 ? 163.906 135.974 112.646 1.00 98.24  ? 829  TYR B CG    1 
ATOM   12002 C  CD1   . TYR B 1 829 ? 163.141 135.342 113.614 1.00 93.46  ? 829  TYR B CD1   1 
ATOM   12003 C  CD2   . TYR B 1 829 ? 163.781 135.549 111.333 1.00 102.13 ? 829  TYR B CD2   1 
ATOM   12004 C  CE1   . TYR B 1 829 ? 162.275 134.322 113.283 1.00 94.59  ? 829  TYR B CE1   1 
ATOM   12005 C  CE2   . TYR B 1 829 ? 162.919 134.532 110.993 1.00 99.75  ? 829  TYR B CE2   1 
ATOM   12006 C  CZ    . TYR B 1 829 ? 162.168 133.922 111.970 1.00 100.38 ? 829  TYR B CZ    1 
ATOM   12007 O  OH    . TYR B 1 829 ? 161.308 132.907 111.629 1.00 107.92 ? 829  TYR B OH    1 
ATOM   12008 N  N     . ILE B 1 830 ? 165.740 139.886 114.212 1.00 97.31  ? 830  ILE B N     1 
ATOM   12009 C  CA    . ILE B 1 830 ? 166.796 140.823 114.583 1.00 92.13  ? 830  ILE B CA    1 
ATOM   12010 C  C     . ILE B 1 830 ? 166.716 141.160 116.065 1.00 98.50  ? 830  ILE B C     1 
ATOM   12011 O  O     . ILE B 1 830 ? 167.734 141.180 116.765 1.00 103.74 ? 830  ILE B O     1 
ATOM   12012 C  CB    . ILE B 1 830 ? 166.723 142.086 113.706 1.00 91.14  ? 830  ILE B CB    1 
ATOM   12013 C  CG1   . ILE B 1 830 ? 167.267 141.791 112.309 1.00 97.78  ? 830  ILE B CG1   1 
ATOM   12014 C  CG2   . ILE B 1 830 ? 167.491 143.226 114.346 1.00 97.35  ? 830  ILE B CG2   1 
ATOM   12015 C  CD1   . ILE B 1 830 ? 167.182 142.965 111.363 1.00 105.32 ? 830  ILE B CD1   1 
ATOM   12016 N  N     . PHE B 1 831 ? 165.508 141.410 116.572 1.00 98.59  ? 831  PHE B N     1 
ATOM   12017 C  CA    . PHE B 1 831 ? 165.358 141.773 117.979 1.00 100.93 ? 831  PHE B CA    1 
ATOM   12018 C  C     . PHE B 1 831 ? 165.778 140.626 118.896 1.00 103.30 ? 831  PHE B C     1 
ATOM   12019 O  O     . PHE B 1 831 ? 166.548 140.821 119.849 1.00 104.96 ? 831  PHE B O     1 
ATOM   12020 C  CB    . PHE B 1 831 ? 163.913 142.186 118.256 1.00 98.37  ? 831  PHE B CB    1 
ATOM   12021 C  CG    . PHE B 1 831 ? 163.758 143.097 119.436 1.00 104.14 ? 831  PHE B CG    1 
ATOM   12022 C  CD1   . PHE B 1 831 ? 163.961 142.631 120.722 1.00 105.57 ? 831  PHE B CD1   1 
ATOM   12023 C  CD2   . PHE B 1 831 ? 163.403 144.422 119.259 1.00 106.72 ? 831  PHE B CD2   1 
ATOM   12024 C  CE1   . PHE B 1 831 ? 163.818 143.470 121.807 1.00 109.77 ? 831  PHE B CE1   1 
ATOM   12025 C  CE2   . PHE B 1 831 ? 163.259 145.265 120.341 1.00 113.27 ? 831  PHE B CE2   1 
ATOM   12026 C  CZ    . PHE B 1 831 ? 163.466 144.788 121.617 1.00 114.17 ? 831  PHE B CZ    1 
ATOM   12027 N  N     . VAL B 1 832 ? 165.284 139.417 118.619 1.00 100.58 ? 832  VAL B N     1 
ATOM   12028 C  CA    . VAL B 1 832 ? 165.608 138.270 119.463 1.00 97.77  ? 832  VAL B CA    1 
ATOM   12029 C  C     . VAL B 1 832 ? 167.091 137.940 119.369 1.00 98.62  ? 832  VAL B C     1 
ATOM   12030 O  O     . VAL B 1 832 ? 167.730 137.597 120.371 1.00 105.43 ? 832  VAL B O     1 
ATOM   12031 C  CB    . VAL B 1 832 ? 164.730 137.064 119.086 1.00 97.04  ? 832  VAL B CB    1 
ATOM   12032 C  CG1   . VAL B 1 832 ? 165.212 135.813 119.790 1.00 98.96  ? 832  VAL B CG1   1 
ATOM   12033 C  CG2   . VAL B 1 832 ? 163.285 137.340 119.440 1.00 97.03  ? 832  VAL B CG2   1 
ATOM   12034 N  N     . ALA B 1 833 ? 167.665 138.038 118.167 1.00 95.53  ? 833  ALA B N     1 
ATOM   12035 C  CA    . ALA B 1 833 ? 169.090 137.795 118.001 1.00 97.58  ? 833  ALA B CA    1 
ATOM   12036 C  C     . ALA B 1 833 ? 169.912 138.816 118.768 1.00 100.66 ? 833  ALA B C     1 
ATOM   12037 O  O     . ALA B 1 833 ? 170.936 138.471 119.356 1.00 105.64 ? 833  ALA B O     1 
ATOM   12038 C  CB    . ALA B 1 833 ? 169.458 137.816 116.518 1.00 98.65  ? 833  ALA B CB    1 
ATOM   12039 N  N     . SER B 1 834 ? 169.482 140.078 118.776 1.00 95.40  ? 834  SER B N     1 
ATOM   12040 C  CA    . SER B 1 834 ? 170.200 141.098 119.532 1.00 97.73  ? 834  SER B CA    1 
ATOM   12041 C  C     . SER B 1 834 ? 170.159 140.803 121.026 1.00 102.37 ? 834  SER B C     1 
ATOM   12042 O  O     . SER B 1 834 ? 171.181 140.897 121.721 1.00 109.06 ? 834  SER B O     1 
ATOM   12043 C  CB    . SER B 1 834 ? 169.611 142.476 119.238 1.00 100.44 ? 834  SER B CB    1 
ATOM   12044 O  OG    . SER B 1 834 ? 170.150 143.451 120.111 1.00 115.65 ? 834  SER B OG    1 
ATOM   12045 N  N     . LEU B 1 835 ? 168.981 140.444 121.541 1.00 99.27  ? 835  LEU B N     1 
ATOM   12046 C  CA    . LEU B 1 835 ? 168.872 140.132 122.964 1.00 100.57 ? 835  LEU B CA    1 
ATOM   12047 C  C     . LEU B 1 835 ? 169.735 138.931 123.335 1.00 102.63 ? 835  LEU B C     1 
ATOM   12048 O  O     . LEU B 1 835 ? 170.490 138.967 124.318 1.00 106.77 ? 835  LEU B O     1 
ATOM   12049 C  CB    . LEU B 1 835 ? 167.415 139.881 123.340 1.00 97.14  ? 835  LEU B CB    1 
ATOM   12050 C  CG    . LEU B 1 835 ? 166.532 141.119 123.457 1.00 100.44 ? 835  LEU B CG    1 
ATOM   12051 C  CD1   . LEU B 1 835 ? 165.200 140.745 124.080 1.00 103.07 ? 835  LEU B CD1   1 
ATOM   12052 C  CD2   . LEU B 1 835 ? 167.233 142.202 124.263 1.00 101.11 ? 835  LEU B CD2   1 
ATOM   12053 N  N     . ASN B 1 836 ? 169.644 137.854 122.554 1.00 98.01  ? 836  ASN B N     1 
ATOM   12054 C  CA    . ASN B 1 836 ? 170.446 136.677 122.860 1.00 93.31  ? 836  ASN B CA    1 
ATOM   12055 C  C     . ASN B 1 836 ? 171.929 136.933 122.630 1.00 95.76  ? 836  ASN B C     1 
ATOM   12056 O  O     . ASN B 1 836 ? 172.764 136.308 123.283 1.00 100.60 ? 836  ASN B O     1 
ATOM   12057 C  CB    . ASN B 1 836 ? 169.961 135.478 122.049 1.00 96.12  ? 836  ASN B CB    1 
ATOM   12058 C  CG    . ASN B 1 836 ? 168.737 134.823 122.660 1.00 99.88  ? 836  ASN B CG    1 
ATOM   12059 O  OD1   . ASN B 1 836 ? 168.110 135.376 123.560 1.00 102.97 ? 836  ASN B OD1   1 
ATOM   12060 N  ND2   . ASN B 1 836 ? 168.391 133.640 122.170 1.00 103.54 ? 836  ASN B ND2   1 
ATOM   12061 N  N     . THR B 1 837 ? 172.277 137.865 121.744 1.00 93.26  ? 837  THR B N     1 
ATOM   12062 C  CA    . THR B 1 837 ? 173.674 138.226 121.557 1.00 92.02  ? 837  THR B CA    1 
ATOM   12063 C  C     . THR B 1 837 ? 174.210 138.937 122.787 1.00 95.81  ? 837  THR B C     1 
ATOM   12064 O  O     . THR B 1 837 ? 175.325 138.658 123.243 1.00 100.10 ? 837  THR B O     1 
ATOM   12065 C  CB    . THR B 1 837 ? 173.821 139.113 120.323 1.00 96.32  ? 837  THR B CB    1 
ATOM   12066 O  OG1   . THR B 1 837 ? 173.295 138.439 119.185 1.00 105.52 ? 837  THR B OG1   1 
ATOM   12067 C  CG2   . THR B 1 837 ? 175.285 139.452 120.084 1.00 98.14  ? 837  THR B CG2   1 
ATOM   12068 N  N     . CYS B 1 838 ? 173.423 139.865 123.340 1.00 95.64  ? 838  CYS B N     1 
ATOM   12069 C  CA    . CYS B 1 838 ? 173.833 140.534 124.569 1.00 93.95  ? 838  CYS B CA    1 
ATOM   12070 C  C     . CYS B 1 838 ? 173.978 139.534 125.708 1.00 95.06  ? 838  CYS B C     1 
ATOM   12071 O  O     . CYS B 1 838 ? 174.947 139.592 126.474 1.00 101.81 ? 838  CYS B O     1 
ATOM   12072 C  CB    . CYS B 1 838 ? 172.833 141.631 124.934 1.00 96.30  ? 838  CYS B CB    1 
ATOM   12073 S  SG    . CYS B 1 838 ? 173.440 142.772 126.201 1.00 125.87 ? 838  CYS B SG    1 
ATOM   12074 N  N     . ARG B 1 839 ? 173.040 138.591 125.822 1.00 90.61  ? 839  ARG B N     1 
ATOM   12075 C  CA    . ARG B 1 839 ? 173.134 137.595 126.888 1.00 88.58  ? 839  ARG B CA    1 
ATOM   12076 C  C     . ARG B 1 839 ? 174.325 136.660 126.688 1.00 91.30  ? 839  ARG B C     1 
ATOM   12077 O  O     . ARG B 1 839 ? 174.992 136.276 127.657 1.00 94.57  ? 839  ARG B O     1 
ATOM   12078 C  CB    . ARG B 1 839 ? 171.829 136.811 126.988 1.00 93.07  ? 839  ARG B CB    1 
ATOM   12079 C  CG    . ARG B 1 839 ? 170.679 137.657 127.501 1.00 97.44  ? 839  ARG B CG    1 
ATOM   12080 C  CD    . ARG B 1 839 ? 169.336 137.088 127.105 1.00 102.94 ? 839  ARG B CD    1 
ATOM   12081 N  NE    . ARG B 1 839 ? 168.978 135.924 127.905 1.00 105.52 ? 839  ARG B NE    1 
ATOM   12082 C  CZ    . ARG B 1 839 ? 167.879 135.207 127.728 1.00 104.01 ? 839  ARG B CZ    1 
ATOM   12083 N  NH1   . ARG B 1 839 ? 167.010 135.499 126.775 1.00 103.69 ? 839  ARG B NH1   1 
ATOM   12084 N  NH2   . ARG B 1 839 ? 167.644 134.171 128.527 1.00 110.46 ? 839  ARG B NH2   1 
ATOM   12085 N  N     . LEU B 1 840 ? 174.611 136.281 125.441 1.00 92.02  ? 840  LEU B N     1 
ATOM   12086 C  CA    . LEU B 1 840 ? 175.774 135.445 125.166 1.00 90.06  ? 840  LEU B CA    1 
ATOM   12087 C  C     . LEU B 1 840 ? 177.065 136.174 125.493 1.00 95.97  ? 840  LEU B C     1 
ATOM   12088 O  O     . LEU B 1 840 ? 177.994 135.583 126.054 1.00 100.93 ? 840  LEU B O     1 
ATOM   12089 C  CB    . LEU B 1 840 ? 175.778 135.018 123.703 1.00 89.56  ? 840  LEU B CB    1 
ATOM   12090 C  CG    . LEU B 1 840 ? 176.957 134.158 123.263 1.00 90.55  ? 840  LEU B CG    1 
ATOM   12091 C  CD1   . LEU B 1 840 ? 177.046 132.922 124.134 1.00 92.48  ? 840  LEU B CD1   1 
ATOM   12092 C  CD2   . LEU B 1 840 ? 176.827 133.777 121.799 1.00 93.59  ? 840  LEU B CD2   1 
ATOM   12093 N  N     . LEU B 1 841 ? 177.152 137.454 125.128 1.00 93.36  ? 841  LEU B N     1 
ATOM   12094 C  CA    . LEU B 1 841 ? 178.335 138.233 125.462 1.00 89.67  ? 841  LEU B CA    1 
ATOM   12095 C  C     . LEU B 1 841 ? 178.488 138.358 126.969 1.00 96.64  ? 841  LEU B C     1 
ATOM   12096 O  O     . LEU B 1 841 ? 179.605 138.301 127.493 1.00 104.28 ? 841  LEU B O     1 
ATOM   12097 C  CB    . LEU B 1 841 ? 178.262 139.608 124.803 1.00 84.83  ? 841  LEU B CB    1 
ATOM   12098 C  CG    . LEU B 1 841 ? 178.551 139.601 123.303 1.00 86.50  ? 841  LEU B CG    1 
ATOM   12099 C  CD1   . LEU B 1 841 ? 178.482 141.006 122.736 1.00 91.46  ? 841  LEU B CD1   1 
ATOM   12100 C  CD2   . LEU B 1 841 ? 179.903 138.970 123.030 1.00 86.61  ? 841  LEU B CD2   1 
ATOM   12101 N  N     . GLY B 1 842 ? 177.374 138.516 127.684 1.00 94.50  ? 842  GLY B N     1 
ATOM   12102 C  CA    . GLY B 1 842 ? 177.442 138.545 129.135 1.00 93.94  ? 842  GLY B CA    1 
ATOM   12103 C  C     . GLY B 1 842 ? 177.958 137.247 129.727 1.00 97.52  ? 842  GLY B C     1 
ATOM   12104 O  O     . GLY B 1 842 ? 178.800 137.257 130.627 1.00 104.70 ? 842  GLY B O     1 
ATOM   12105 N  N     . SER B 1 843 ? 177.459 136.112 129.236 1.00 94.86  ? 843  SER B N     1 
ATOM   12106 C  CA    . SER B 1 843 ? 177.931 134.829 129.750 1.00 97.59  ? 843  SER B CA    1 
ATOM   12107 C  C     . SER B 1 843 ? 179.405 134.612 129.425 1.00 102.15 ? 843  SER B C     1 
ATOM   12108 O  O     . SER B 1 843 ? 180.167 134.106 130.261 1.00 109.80 ? 843  SER B O     1 
ATOM   12109 C  CB    . SER B 1 843 ? 177.085 133.689 129.192 1.00 97.82  ? 843  SER B CB    1 
ATOM   12110 O  OG    . SER B 1 843 ? 177.572 132.441 129.647 1.00 96.97  ? 843  SER B OG    1 
ATOM   12111 N  N     . ILE B 1 844 ? 179.826 134.991 128.216 1.00 96.13  ? 844  ILE B N     1 
ATOM   12112 C  CA    . ILE B 1 844 ? 181.232 134.877 127.842 1.00 96.78  ? 844  ILE B CA    1 
ATOM   12113 C  C     . ILE B 1 844 ? 182.092 135.739 128.755 1.00 104.94 ? 844  ILE B C     1 
ATOM   12114 O  O     . ILE B 1 844 ? 183.155 135.310 129.222 1.00 111.40 ? 844  ILE B O     1 
ATOM   12115 C  CB    . ILE B 1 844 ? 181.423 135.264 126.363 1.00 99.65  ? 844  ILE B CB    1 
ATOM   12116 C  CG1   . ILE B 1 844 ? 181.104 134.086 125.447 1.00 97.75  ? 844  ILE B CG1   1 
ATOM   12117 C  CG2   . ILE B 1 844 ? 182.835 135.762 126.112 1.00 104.22 ? 844  ILE B CG2   1 
ATOM   12118 C  CD1   . ILE B 1 844 ? 180.423 134.489 124.166 1.00 95.91  ? 844  ILE B CD1   1 
ATOM   12119 N  N     . GLY B 1 845 ? 181.644 136.966 129.024 1.00 102.18 ? 845  GLY B N     1 
ATOM   12120 C  CA    . GLY B 1 845 ? 182.391 137.842 129.908 1.00 106.15 ? 845  GLY B CA    1 
ATOM   12121 C  C     . GLY B 1 845 ? 182.483 137.301 131.319 1.00 110.00 ? 845  GLY B C     1 
ATOM   12122 O  O     . GLY B 1 845 ? 183.528 137.398 131.961 1.00 116.62 ? 845  GLY B O     1 
ATOM   12123 N  N     . HIS B 1 846 ? 181.392 136.722 131.820 1.00 103.59 ? 846  HIS B N     1 
ATOM   12124 C  CA    . HIS B 1 846 ? 181.423 136.144 133.160 1.00 105.95 ? 846  HIS B CA    1 
ATOM   12125 C  C     . HIS B 1 846 ? 182.393 134.972 133.230 1.00 113.82 ? 846  HIS B C     1 
ATOM   12126 O  O     . HIS B 1 846 ? 183.179 134.861 134.181 1.00 122.80 ? 846  HIS B O     1 
ATOM   12127 C  CB    . HIS B 1 846 ? 180.015 135.718 133.569 1.00 104.00 ? 846  HIS B CB    1 
ATOM   12128 C  CG    . HIS B 1 846 ? 179.914 135.215 134.974 1.00 106.38 ? 846  HIS B CG    1 
ATOM   12129 N  ND1   . HIS B 1 846 ? 179.190 135.872 135.945 1.00 104.42 ? 846  HIS B ND1   1 
ATOM   12130 C  CD2   . HIS B 1 846 ? 180.418 134.108 135.566 1.00 110.72 ? 846  HIS B CD2   1 
ATOM   12131 C  CE1   . HIS B 1 846 ? 179.268 135.201 137.080 1.00 105.06 ? 846  HIS B CE1   1 
ATOM   12132 N  NE2   . HIS B 1 846 ? 180.006 134.125 136.877 1.00 107.94 ? 846  HIS B NE2   1 
ATOM   12133 N  N     . TRP B 1 847 ? 182.364 134.093 132.225 1.00 110.13 ? 847  TRP B N     1 
ATOM   12134 C  CA    . TRP B 1 847 ? 183.293 132.967 132.212 1.00 112.13 ? 847  TRP B CA    1 
ATOM   12135 C  C     . TRP B 1 847 ? 184.741 133.439 132.152 1.00 118.58 ? 847  TRP B C     1 
ATOM   12136 O  O     . TRP B 1 847 ? 185.596 132.942 132.901 1.00 123.30 ? 847  TRP B O     1 
ATOM   12137 C  CB    . TRP B 1 847 ? 182.985 132.045 131.034 1.00 112.42 ? 847  TRP B CB    1 
ATOM   12138 C  CG    . TRP B 1 847 ? 183.875 130.847 130.969 1.00 113.49 ? 847  TRP B CG    1 
ATOM   12139 C  CD1   . TRP B 1 847 ? 183.652 129.629 131.535 1.00 113.01 ? 847  TRP B CD1   1 
ATOM   12140 C  CD2   . TRP B 1 847 ? 185.134 130.753 130.295 1.00 117.38 ? 847  TRP B CD2   1 
ATOM   12141 N  NE1   . TRP B 1 847 ? 184.694 128.780 131.256 1.00 113.48 ? 847  TRP B NE1   1 
ATOM   12142 C  CE2   . TRP B 1 847 ? 185.618 129.447 130.496 1.00 117.17 ? 847  TRP B CE2   1 
ATOM   12143 C  CE3   . TRP B 1 847 ? 185.900 131.646 129.541 1.00 118.31 ? 847  TRP B CE3   1 
ATOM   12144 C  CZ2   . TRP B 1 847 ? 186.832 129.013 129.972 1.00 119.51 ? 847  TRP B CZ2   1 
ATOM   12145 C  CZ3   . TRP B 1 847 ? 187.104 131.214 129.023 1.00 115.98 ? 847  TRP B CZ3   1 
ATOM   12146 C  CH2   . TRP B 1 847 ? 187.559 129.910 129.240 1.00 118.07 ? 847  TRP B CH2   1 
ATOM   12147 N  N     . VAL B 1 848 ? 185.040 134.395 131.268 1.00 114.63 ? 848  VAL B N     1 
ATOM   12148 C  CA    . VAL B 1 848 ? 186.420 134.848 131.133 1.00 114.96 ? 848  VAL B CA    1 
ATOM   12149 C  C     . VAL B 1 848 ? 186.861 135.577 132.395 1.00 119.18 ? 848  VAL B C     1 
ATOM   12150 O  O     . VAL B 1 848 ? 188.014 135.461 132.818 1.00 126.56 ? 848  VAL B O     1 
ATOM   12151 C  CB    . VAL B 1 848 ? 186.603 135.710 129.868 1.00 114.19 ? 848  VAL B CB    1 
ATOM   12152 C  CG1   . VAL B 1 848 ? 185.876 137.031 129.980 1.00 113.76 ? 848  VAL B CG1   1 
ATOM   12153 C  CG2   . VAL B 1 848 ? 188.079 135.935 129.593 1.00 121.39 ? 848  VAL B CG2   1 
ATOM   12154 N  N     . TYR B 1 849 ? 185.950 136.315 133.032 1.00 119.24 ? 849  TYR B N     1 
ATOM   12155 C  CA    . TYR B 1 849 ? 186.281 136.959 134.297 1.00 126.68 ? 849  TYR B CA    1 
ATOM   12156 C  C     . TYR B 1 849 ? 186.631 135.933 135.363 1.00 128.85 ? 849  TYR B C     1 
ATOM   12157 O  O     . TYR B 1 849 ? 187.648 136.069 136.053 1.00 137.23 ? 849  TYR B O     1 
ATOM   12158 C  CB    . TYR B 1 849 ? 185.119 137.835 134.760 1.00 122.14 ? 849  TYR B CB    1 
ATOM   12159 C  CG    . TYR B 1 849 ? 185.195 138.215 136.217 1.00 124.41 ? 849  TYR B CG    1 
ATOM   12160 C  CD1   . TYR B 1 849 ? 186.151 139.110 136.673 1.00 129.65 ? 849  TYR B CD1   1 
ATOM   12161 C  CD2   . TYR B 1 849 ? 184.308 137.680 137.138 1.00 123.02 ? 849  TYR B CD2   1 
ATOM   12162 C  CE1   . TYR B 1 849 ? 186.224 139.459 138.005 1.00 128.57 ? 849  TYR B CE1   1 
ATOM   12163 C  CE2   . TYR B 1 849 ? 184.372 138.024 138.471 1.00 125.68 ? 849  TYR B CE2   1 
ATOM   12164 C  CZ    . TYR B 1 849 ? 185.331 138.914 138.899 1.00 128.61 ? 849  TYR B CZ    1 
ATOM   12165 O  OH    . TYR B 1 849 ? 185.401 139.261 140.226 1.00 129.15 ? 849  TYR B OH    1 
ATOM   12166 N  N     . ILE B 1 850 ? 185.813 134.886 135.496 1.00 121.28 ? 850  ILE B N     1 
ATOM   12167 C  CA    . ILE B 1 850 ? 186.083 133.879 136.517 1.00 123.34 ? 850  ILE B CA    1 
ATOM   12168 C  C     . ILE B 1 850 ? 187.411 133.181 136.253 1.00 130.98 ? 850  ILE B C     1 
ATOM   12169 O  O     . ILE B 1 850 ? 188.209 132.985 137.178 1.00 134.74 ? 850  ILE B O     1 
ATOM   12170 C  CB    . ILE B 1 850 ? 184.924 132.870 136.603 1.00 119.45 ? 850  ILE B CB    1 
ATOM   12171 C  CG1   . ILE B 1 850 ? 183.866 133.361 137.586 1.00 115.83 ? 850  ILE B CG1   1 
ATOM   12172 C  CG2   . ILE B 1 850 ? 185.421 131.514 137.061 1.00 123.51 ? 850  ILE B CG2   1 
ATOM   12173 C  CD1   . ILE B 1 850 ? 182.683 132.435 137.697 1.00 113.54 ? 850  ILE B CD1   1 
ATOM   12174 N  N     . HIS B 1 851 ? 187.688 132.813 135.004 1.00 129.06 ? 851  HIS B N     1 
ATOM   12175 C  CA    . HIS B 1 851 ? 188.884 132.043 134.688 1.00 128.40 ? 851  HIS B CA    1 
ATOM   12176 C  C     . HIS B 1 851 ? 190.120 132.905 134.452 1.00 136.24 ? 851  HIS B C     1 
ATOM   12177 O  O     . HIS B 1 851 ? 191.209 132.358 134.252 1.00 142.41 ? 851  HIS B O     1 
ATOM   12178 C  CB    . HIS B 1 851 ? 188.632 131.151 133.473 1.00 125.43 ? 851  HIS B CB    1 
ATOM   12179 C  CG    . HIS B 1 851 ? 187.856 129.912 133.788 1.00 124.98 ? 851  HIS B CG    1 
ATOM   12180 N  ND1   . HIS B 1 851 ? 186.717 129.924 134.563 1.00 123.03 ? 851  HIS B ND1   1 
ATOM   12181 C  CD2   . HIS B 1 851 ? 188.059 128.620 133.438 1.00 127.99 ? 851  HIS B CD2   1 
ATOM   12182 C  CE1   . HIS B 1 851 ? 186.249 128.694 134.676 1.00 122.98 ? 851  HIS B CE1   1 
ATOM   12183 N  NE2   . HIS B 1 851 ? 187.045 127.884 134.002 1.00 127.43 ? 851  HIS B NE2   1 
ATOM   12184 N  N     . THR B 1 852 ? 189.988 134.226 134.472 1.00 136.90 ? 852  THR B N     1 
ATOM   12185 C  CA    . THR B 1 852 ? 191.121 135.104 134.212 1.00 143.84 ? 852  THR B CA    1 
ATOM   12186 C  C     . THR B 1 852 ? 191.509 135.964 135.401 1.00 152.80 ? 852  THR B C     1 
ATOM   12187 O  O     . THR B 1 852 ? 192.697 136.247 135.585 1.00 164.81 ? 852  THR B O     1 
ATOM   12188 C  CB    . THR B 1 852 ? 190.809 136.009 133.008 1.00 142.03 ? 852  THR B CB    1 
ATOM   12189 O  OG1   . THR B 1 852 ? 190.443 135.199 131.884 1.00 142.21 ? 852  THR B OG1   1 
ATOM   12190 C  CG2   . THR B 1 852 ? 192.015 136.859 132.634 1.00 148.43 ? 852  THR B CG2   1 
ATOM   12191 N  N     . GLU B 1 853 ? 190.544 136.378 136.227 1.00 149.43 ? 853  GLU B N     1 
ATOM   12192 C  CA    . GLU B 1 853 ? 190.846 137.311 137.307 1.00 160.63 ? 853  GLU B CA    1 
ATOM   12193 C  C     . GLU B 1 853 ? 191.859 136.747 138.295 1.00 165.20 ? 853  GLU B C     1 
ATOM   12194 O  O     . GLU B 1 853 ? 192.576 137.522 138.940 1.00 167.09 ? 853  GLU B O     1 
ATOM   12195 C  CB    . GLU B 1 853 ? 189.558 137.703 138.033 1.00 152.17 ? 853  GLU B CB    1 
ATOM   12196 C  CG    . GLU B 1 853 ? 189.704 138.912 138.941 1.00 152.25 ? 853  GLU B CG    1 
ATOM   12197 C  CD    . GLU B 1 853 ? 190.129 140.156 138.185 1.00 151.70 ? 853  GLU B CD    1 
ATOM   12198 O  OE1   . GLU B 1 853 ? 189.728 140.309 137.013 1.00 147.98 ? 853  GLU B OE1   1 
ATOM   12199 O  OE2   . GLU B 1 853 ? 190.871 140.978 138.761 1.00 156.01 ? 853  GLU B OE2   1 
ATOM   12200 N  N     . GLY B 1 854 ? 191.945 135.422 138.422 1.00 160.40 ? 854  GLY B N     1 
ATOM   12201 C  CA    . GLY B 1 854 ? 192.944 134.841 139.303 1.00 164.72 ? 854  GLY B CA    1 
ATOM   12202 C  C     . GLY B 1 854 ? 194.364 135.131 138.855 1.00 172.54 ? 854  GLY B C     1 
ATOM   12203 O  O     . GLY B 1 854 ? 195.217 135.501 139.664 1.00 173.24 ? 854  GLY B O     1 
ATOM   12204 N  N     . LEU B 1 855 ? 194.636 134.971 137.557 1.00 176.66 ? 855  LEU B N     1 
ATOM   12205 C  CA    . LEU B 1 855 ? 195.988 135.201 137.056 1.00 183.00 ? 855  LEU B CA    1 
ATOM   12206 C  C     . LEU B 1 855 ? 196.323 136.687 137.025 1.00 185.54 ? 855  LEU B C     1 
ATOM   12207 O  O     . LEU B 1 855 ? 197.467 137.075 137.289 1.00 190.34 ? 855  LEU B O     1 
ATOM   12208 C  CB    . LEU B 1 855 ? 196.149 134.581 135.667 1.00 184.96 ? 855  LEU B CB    1 
ATOM   12209 C  CG    . LEU B 1 855 ? 197.543 134.643 135.034 1.00 189.85 ? 855  LEU B CG    1 
ATOM   12210 C  CD1   . LEU B 1 855 ? 197.886 133.324 134.361 1.00 183.92 ? 855  LEU B CD1   1 
ATOM   12211 C  CD2   . LEU B 1 855 ? 197.644 135.790 134.036 1.00 191.92 ? 855  LEU B CD2   1 
ATOM   12212 N  N     . ARG B 1 856 ? 195.343 137.533 136.706 1.00 182.26 ? 856  ARG B N     1 
ATOM   12213 C  CA    . ARG B 1 856 ? 195.550 138.974 136.635 1.00 186.79 ? 856  ARG B CA    1 
ATOM   12214 C  C     . ARG B 1 856 ? 195.159 139.677 137.931 1.00 185.62 ? 856  ARG B C     1 
ATOM   12215 O  O     . ARG B 1 856 ? 194.724 140.833 137.906 1.00 184.84 ? 856  ARG B O     1 
ATOM   12216 C  CB    . ARG B 1 856 ? 194.784 139.569 135.454 1.00 186.46 ? 856  ARG B CB    1 
ATOM   12217 C  CG    . ARG B 1 856 ? 195.504 140.736 134.791 1.00 197.06 ? 856  ARG B CG    1 
ATOM   12218 C  CD    . ARG B 1 856 ? 194.579 141.549 133.901 1.00 200.88 ? 856  ARG B CD    1 
ATOM   12219 N  NE    . ARG B 1 856 ? 195.180 142.824 133.528 1.00 202.90 ? 856  ARG B NE    1 
ATOM   12220 C  CZ    . ARG B 1 856 ? 194.533 143.814 132.928 1.00 200.64 ? 856  ARG B CZ    1 
ATOM   12221 N  NH1   . ARG B 1 856 ? 193.250 143.714 132.621 1.00 194.93 ? 856  ARG B NH1   1 
ATOM   12222 N  NH2   . ARG B 1 856 ? 195.189 144.932 132.630 1.00 203.05 ? 856  ARG B NH2   1 
ATOM   12223 N  N     . GLY B 1 857 ? 195.298 138.993 139.069 1.00 187.28 ? 857  GLY B N     1 
ATOM   12224 C  CA    . GLY B 1 857 ? 195.027 139.623 140.348 1.00 188.97 ? 857  GLY B CA    1 
ATOM   12225 C  C     . GLY B 1 857 ? 196.078 140.624 140.776 1.00 195.48 ? 857  GLY B C     1 
ATOM   12226 O  O     . GLY B 1 857 ? 195.775 141.525 141.565 1.00 194.97 ? 857  GLY B O     1 
ATOM   12227 N  N     . ARG B 1 858 ? 197.310 140.486 140.278 1.00 196.61 ? 858  ARG B N     1 
ATOM   12228 C  CA    . ARG B 1 858 ? 198.352 141.450 140.615 1.00 197.83 ? 858  ARG B CA    1 
ATOM   12229 C  C     . ARG B 1 858 ? 198.042 142.824 140.032 1.00 197.57 ? 858  ARG B C     1 
ATOM   12230 O  O     . ARG B 1 858 ? 198.277 143.848 140.683 1.00 197.63 ? 858  ARG B O     1 
ATOM   12231 C  CB    . ARG B 1 858 ? 199.713 140.955 140.124 1.00 196.77 ? 858  ARG B CB    1 
ATOM   12232 C  CG    . ARG B 1 858 ? 199.690 140.298 138.754 1.00 195.00 ? 858  ARG B CG    1 
ATOM   12233 C  CD    . ARG B 1 858 ? 201.017 139.617 138.453 1.00 199.81 ? 858  ARG B CD    1 
ATOM   12234 N  NE    . ARG B 1 858 ? 200.932 138.732 137.297 1.00 203.22 ? 858  ARG B NE    1 
ATOM   12235 C  CZ    . ARG B 1 858 ? 201.934 137.987 136.849 1.00 205.07 ? 858  ARG B CZ    1 
ATOM   12236 N  NH1   . ARG B 1 858 ? 203.118 137.996 137.438 1.00 207.04 ? 858  ARG B NH1   1 
ATOM   12237 N  NH2   . ARG B 1 858 ? 201.742 137.216 135.783 1.00 202.26 ? 858  ARG B NH2   1 
ATOM   12238 N  N     . VAL B 1 859 ? 197.517 142.865 138.812 1.00 196.88 ? 859  VAL B N     1 
ATOM   12239 C  CA    . VAL B 1 859 ? 197.186 144.125 138.162 1.00 196.89 ? 859  VAL B CA    1 
ATOM   12240 C  C     . VAL B 1 859 ? 195.677 144.333 138.147 1.00 193.51 ? 859  VAL B C     1 
ATOM   12241 O  O     . VAL B 1 859 ? 195.150 145.185 138.862 1.00 188.84 ? 859  VAL B O     1 
ATOM   12242 C  CB    . VAL B 1 859 ? 197.755 144.180 136.736 1.00 198.20 ? 859  VAL B CB    1 
ATOM   12243 C  CG1   . VAL B 1 859 ? 197.405 145.506 136.076 1.00 199.19 ? 859  VAL B CG1   1 
ATOM   12244 C  CG2   . VAL B 1 859 ? 199.262 143.966 136.757 1.00 198.44 ? 859  VAL B CG2   1 
HETATM 12245 N  N1    . UDP C 2 .   ? 118.991 144.077 154.024 1.00 124.46 ? 1001 UDP A N1    1 
HETATM 12246 C  C2    . UDP C 2 .   ? 119.215 143.121 154.993 1.00 123.56 ? 1001 UDP A C2    1 
HETATM 12247 N  N3    . UDP C 2 .   ? 120.503 142.661 155.056 1.00 121.18 ? 1001 UDP A N3    1 
HETATM 12248 C  C4    . UDP C 2 .   ? 121.584 143.029 154.276 1.00 124.82 ? 1001 UDP A C4    1 
HETATM 12249 C  C5    . UDP C 2 .   ? 121.261 144.024 153.289 1.00 122.77 ? 1001 UDP A C5    1 
HETATM 12250 C  C6    . UDP C 2 .   ? 120.007 144.492 153.211 1.00 122.61 ? 1001 UDP A C6    1 
HETATM 12251 O  O2    . UDP C 2 .   ? 118.356 142.714 155.741 1.00 124.88 ? 1001 UDP A O2    1 
HETATM 12252 O  O4    . UDP C 2 .   ? 122.676 142.525 154.454 1.00 130.77 ? 1001 UDP A O4    1 
HETATM 12253 C  "C1'" . UDP C 2 .   ? 117.670 144.650 153.841 1.00 126.76 ? 1001 UDP A "C1'" 1 
HETATM 12254 C  "C2'" . UDP C 2 .   ? 117.605 145.990 153.105 1.00 126.09 ? 1001 UDP A "C2'" 1 
HETATM 12255 O  "O2'" . UDP C 2 .   ? 117.611 147.037 154.033 1.00 123.62 ? 1001 UDP A "O2'" 1 
HETATM 12256 C  "C3'" . UDP C 2 .   ? 116.288 145.838 152.340 1.00 125.50 ? 1001 UDP A "C3'" 1 
HETATM 12257 C  "C4'" . UDP C 2 .   ? 116.364 144.370 151.970 1.00 123.79 ? 1001 UDP A "C4'" 1 
HETATM 12258 O  "O4'" . UDP C 2 .   ? 116.883 143.742 153.139 1.00 124.43 ? 1001 UDP A "O4'" 1 
HETATM 12259 O  "O3'" . UDP C 2 .   ? 115.184 146.028 153.185 1.00 124.94 ? 1001 UDP A "O3'" 1 
HETATM 12260 C  "C5'" . UDP C 2 .   ? 117.284 144.117 150.799 1.00 131.93 ? 1001 UDP A "C5'" 1 
HETATM 12261 O  "O5'" . UDP C 2 .   ? 116.948 145.003 149.756 1.00 143.62 ? 1001 UDP A "O5'" 1 
HETATM 12262 P  PA    . UDP C 2 .   ? 118.112 146.058 149.271 1.00 151.63 ? 1001 UDP A PA    1 
HETATM 12263 O  O1A   . UDP C 2 .   ? 119.439 145.373 149.229 1.00 148.02 ? 1001 UDP A O1A   1 
HETATM 12264 O  O2A   . UDP C 2 .   ? 117.944 147.348 150.008 1.00 152.29 ? 1001 UDP A O2A   1 
HETATM 12265 O  O3A   . UDP C 2 .   ? 117.501 146.156 147.753 1.00 152.55 ? 1001 UDP A O3A   1 
HETATM 12266 P  PB    . UDP C 2 .   ? 117.157 147.580 147.020 1.00 165.89 ? 1001 UDP A PB    1 
HETATM 12267 O  O1B   . UDP C 2 .   ? 117.223 147.432 145.536 1.00 160.07 ? 1001 UDP A O1B   1 
HETATM 12268 O  O2B   . UDP C 2 .   ? 115.972 148.223 147.666 1.00 156.23 ? 1001 UDP A O2B   1 
HETATM 12269 O  O3B   . UDP C 2 .   ? 118.544 148.292 147.580 1.00 164.95 ? 1001 UDP A O3B   1 
HETATM 12270 MN MN    . MN  D 3 .   ? 115.473 149.724 149.125 1.00 160.22 ? 1002 MN  A MN    1 
HETATM 12271 N  N1    . UDP E 2 .   ? 157.130 131.943 153.949 1.00 125.03 ? 1001 UDP B N1    1 
HETATM 12272 C  C2    . UDP E 2 .   ? 156.869 132.921 154.883 1.00 123.48 ? 1001 UDP B C2    1 
HETATM 12273 N  N3    . UDP E 2 .   ? 155.570 133.349 154.913 1.00 120.45 ? 1001 UDP B N3    1 
HETATM 12274 C  C4    . UDP E 2 .   ? 154.511 132.930 154.126 1.00 123.86 ? 1001 UDP B C4    1 
HETATM 12275 C  C5    . UDP E 2 .   ? 154.876 131.915 153.174 1.00 123.92 ? 1001 UDP B C5    1 
HETATM 12276 C  C6    . UDP E 2 .   ? 156.142 131.477 153.132 1.00 124.65 ? 1001 UDP B C6    1 
HETATM 12277 O  O2    . UDP E 2 .   ? 157.707 133.369 155.632 1.00 125.28 ? 1001 UDP B O2    1 
HETATM 12278 O  O4    . UDP E 2 .   ? 153.405 133.412 154.272 1.00 128.34 ? 1001 UDP B O4    1 
HETATM 12279 C  "C1'" . UDP E 2 .   ? 158.468 131.404 153.810 1.00 127.59 ? 1001 UDP B "C1'" 1 
HETATM 12280 C  "C2'" . UDP E 2 .   ? 158.579 129.995 153.231 1.00 127.30 ? 1001 UDP B "C2'" 1 
HETATM 12281 O  "O2'" . UDP E 2 .   ? 158.572 129.059 154.270 1.00 124.93 ? 1001 UDP B "O2'" 1 
HETATM 12282 C  "C3'" . UDP E 2 .   ? 159.916 130.104 152.498 1.00 126.80 ? 1001 UDP B "C3'" 1 
HETATM 12283 C  "C4'" . UDP E 2 .   ? 159.779 131.503 151.929 1.00 125.11 ? 1001 UDP B "C4'" 1 
HETATM 12284 O  "O4'" . UDP E 2 .   ? 159.202 132.256 152.991 1.00 124.93 ? 1001 UDP B "O4'" 1 
HETATM 12285 O  "O3'" . UDP E 2 .   ? 160.990 130.091 153.400 1.00 126.47 ? 1001 UDP B "O3'" 1 
HETATM 12286 C  "C5'" . UDP E 2 .   ? 158.883 131.545 150.712 1.00 135.48 ? 1001 UDP B "C5'" 1 
HETATM 12287 O  "O5'" . UDP E 2 .   ? 159.310 130.566 149.791 1.00 146.70 ? 1001 UDP B "O5'" 1 
HETATM 12288 P  PA    . UDP E 2 .   ? 158.284 129.313 149.508 1.00 159.87 ? 1001 UDP B PA    1 
HETATM 12289 O  O1A   . UDP E 2 .   ? 156.893 129.692 149.904 1.00 150.06 ? 1001 UDP B O1A   1 
HETATM 12290 O  O2A   . UDP E 2 .   ? 158.895 128.048 150.018 1.00 160.74 ? 1001 UDP B O2A   1 
HETATM 12291 O  O3A   . UDP E 2 .   ? 158.446 129.416 147.880 1.00 156.17 ? 1001 UDP B O3A   1 
HETATM 12292 P  PB    . UDP E 2 .   ? 159.085 128.200 146.985 1.00 166.69 ? 1001 UDP B PB    1 
HETATM 12293 O  O1B   . UDP E 2 .   ? 158.806 128.416 145.534 1.00 158.86 ? 1001 UDP B O1B   1 
HETATM 12294 O  O2B   . UDP E 2 .   ? 160.470 127.890 147.453 1.00 156.71 ? 1001 UDP B O2B   1 
HETATM 12295 O  O3B   . UDP E 2 .   ? 158.038 127.068 147.595 1.00 165.60 ? 1001 UDP B O3B   1 
HETATM 12296 MN MN    . MN  F 3 .   ? 160.496 126.282 149.107 1.00 162.86 ? 1002 MN  B MN    1 
# 
