data_9I1S
# 
_entry.id   9I1S 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9I1S         pdb_00009i1s 10.2210/pdb9i1s/pdb 
WWPDB D_1292144643 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-11 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9I1S 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-16 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              rficner@gwdg.de 
_pdbx_contact_author.name_first         Ficner 
_pdbx_contact_author.name_last          Ralf 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1739-6086 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Kloskowski, P.' 1 0009-0007-7077-0747 
'Neumann, P.'    2 0000-0003-0129-8112 
'Ficner, R.'     3 0000-0002-1739-6086 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acta Crystallogr D Struct Biol' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2059-7983 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            81 
_citation.language                  ? 
_citation.page_first                310 
_citation.page_last                 326 
_citation.title                     
'Myricetin-bound crystal structure of the SARS-CoV-2 helicase NSP13 facilitates the discovery of novel natural inhibitors.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1107/S2059798325004498 
_citation.pdbx_database_id_PubMed   40421686 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kloskowski, P.'  1 0009-0007-7077-0747 
primary 'Neumann, P.'     2 ?                   
primary 'Kumar, P.'       3 0009-0008-0060-1224 
primary 'Berndt, A.'      4 ?                   
primary 'Dobbelstein, M.' 5 ?                   
primary 'Ficner, R.'      6 0000-0002-1739-6086 
# 
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 'Helicase nsp13'                                               67148.805 2   3.6.4.12,3.6.4.13 ? ? ? 
2 non-polymer syn 'ZINC ION'                                                     65.409    6   ?                 ? ? ? 
3 non-polymer syn 'PHOSPHATE ION'                                                94.971    4   ?                 ? ? ? 
4 non-polymer syn '3[N-MORPHOLINO]PROPANE SULFONIC ACID'                         209.263   2   ?                 ? ? ? 
5 non-polymer syn '3,5,7-TRIHYDROXY-2-(3,4,5-TRIHYDROXYPHENYL)-4H-CHROMEN-4-ONE' 318.235   1   ?                 ? ? ? 
6 water       nat water                                                          18.015    230 ?                 ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Hel,Non-structural protein 13,nsp13' 
# 
_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       
;SMAVGACVLCNSQTSLRCGACIRRPFLCCKCCYDHVISTSHKLVLSVNPYVCNAPGCDVTDVTQLYLGGMSYYCKSHKPP
ISFPLCANGQVFGLYKNTCVGSDNVTDFNAIATCDWTNAGDYILANTCTERLKLFAAETLKATEETFKLSYGIATVREVL
SDRELHLSWEVGKPRPPLNRNYVFTGYRVTKNSKVQIGEYTFEKGDYGDAVVYRGTTTYKLNVGDYFVLTSHTVMPLSAP
TLVPQEHYVRITGLYPTLNISDEFSSNVANYQKVGMQKYSTLQGPPGTGKSHFAIGLALYYPSARIVYTACSHAAVDALC
EKALKYLPIDKCSRIIPARARVECFDKFKVNSTLEQYVFCTVNALPETTADIVVFDEISMATNYDLSVVNARLRAKHYVY
IGDPAQLPAPRTLLTKGTLEPEYFNSVCRLMKTIGPDMFLGTCRRCPAEIVDTVSALVYDNKLKAHKDKSAQCFKMFYKG
VITHDVSSAINRPQIGVVREFLTRNPAWRKAVFISPYNSQNAVASKILGLPTQTVDSSQGSEYDYVIFTQTTETAHSCNV
NRFNVAITRAKVGILCIMSDRDLYDKLQFTSLEIPRRNVATLQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMAVGACVLCNSQTSLRCGACIRRPFLCCKCCYDHVISTSHKLVLSVNPYVCNAPGCDVTDVTQLYLGGMSYYCKSHKPP
ISFPLCANGQVFGLYKNTCVGSDNVTDFNAIATCDWTNAGDYILANTCTERLKLFAAETLKATEETFKLSYGIATVREVL
SDRELHLSWEVGKPRPPLNRNYVFTGYRVTKNSKVQIGEYTFEKGDYGDAVVYRGTTTYKLNVGDYFVLTSHTVMPLSAP
TLVPQEHYVRITGLYPTLNISDEFSSNVANYQKVGMQKYSTLQGPPGTGKSHFAIGLALYYPSARIVYTACSHAAVDALC
EKALKYLPIDKCSRIIPARARVECFDKFKVNSTLEQYVFCTVNALPETTADIVVFDEISMATNYDLSVVNARLRAKHYVY
IGDPAQLPAPRTLLTKGTLEPEYFNSVCRLMKTIGPDMFLGTCRRCPAEIVDTVSALVYDNKLKAHKDKSAQCFKMFYKG
VITHDVSSAINRPQIGVVREFLTRNPAWRKAVFISPYNSQNAVASKILGLPTQTVDSSQGSEYDYVIFTQTTETAHSCNV
NRFNVAITRAKVGILCIMSDRDLYDKLQFTSLEIPRRNVATLQ
;
_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 'ZINC ION'                                                     ZN  
3 'PHOSPHATE ION'                                                PO4 
4 '3[N-MORPHOLINO]PROPANE SULFONIC ACID'                         MPO 
5 '3,5,7-TRIHYDROXY-2-(3,4,5-TRIHYDROXYPHENYL)-4H-CHROMEN-4-ONE' MYC 
6 water                                                          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   ALA n 
1 4   VAL n 
1 5   GLY n 
1 6   ALA n 
1 7   CYS n 
1 8   VAL n 
1 9   LEU n 
1 10  CYS n 
1 11  ASN n 
1 12  SER n 
1 13  GLN n 
1 14  THR n 
1 15  SER n 
1 16  LEU n 
1 17  ARG n 
1 18  CYS n 
1 19  GLY n 
1 20  ALA n 
1 21  CYS n 
1 22  ILE n 
1 23  ARG n 
1 24  ARG n 
1 25  PRO n 
1 26  PHE n 
1 27  LEU n 
1 28  CYS n 
1 29  CYS n 
1 30  LYS n 
1 31  CYS n 
1 32  CYS n 
1 33  TYR n 
1 34  ASP n 
1 35  HIS n 
1 36  VAL n 
1 37  ILE n 
1 38  SER n 
1 39  THR n 
1 40  SER n 
1 41  HIS n 
1 42  LYS n 
1 43  LEU n 
1 44  VAL n 
1 45  LEU n 
1 46  SER n 
1 47  VAL n 
1 48  ASN n 
1 49  PRO n 
1 50  TYR n 
1 51  VAL n 
1 52  CYS n 
1 53  ASN n 
1 54  ALA n 
1 55  PRO n 
1 56  GLY n 
1 57  CYS n 
1 58  ASP n 
1 59  VAL n 
1 60  THR n 
1 61  ASP n 
1 62  VAL n 
1 63  THR n 
1 64  GLN n 
1 65  LEU n 
1 66  TYR n 
1 67  LEU n 
1 68  GLY n 
1 69  GLY n 
1 70  MET n 
1 71  SER n 
1 72  TYR n 
1 73  TYR n 
1 74  CYS n 
1 75  LYS n 
1 76  SER n 
1 77  HIS n 
1 78  LYS n 
1 79  PRO n 
1 80  PRO n 
1 81  ILE n 
1 82  SER n 
1 83  PHE n 
1 84  PRO n 
1 85  LEU n 
1 86  CYS n 
1 87  ALA n 
1 88  ASN n 
1 89  GLY n 
1 90  GLN n 
1 91  VAL n 
1 92  PHE n 
1 93  GLY n 
1 94  LEU n 
1 95  TYR n 
1 96  LYS n 
1 97  ASN n 
1 98  THR n 
1 99  CYS n 
1 100 VAL n 
1 101 GLY n 
1 102 SER n 
1 103 ASP n 
1 104 ASN n 
1 105 VAL n 
1 106 THR n 
1 107 ASP n 
1 108 PHE n 
1 109 ASN n 
1 110 ALA n 
1 111 ILE n 
1 112 ALA n 
1 113 THR n 
1 114 CYS n 
1 115 ASP n 
1 116 TRP n 
1 117 THR n 
1 118 ASN n 
1 119 ALA n 
1 120 GLY n 
1 121 ASP n 
1 122 TYR n 
1 123 ILE n 
1 124 LEU n 
1 125 ALA n 
1 126 ASN n 
1 127 THR n 
1 128 CYS n 
1 129 THR n 
1 130 GLU n 
1 131 ARG n 
1 132 LEU n 
1 133 LYS n 
1 134 LEU n 
1 135 PHE n 
1 136 ALA n 
1 137 ALA n 
1 138 GLU n 
1 139 THR n 
1 140 LEU n 
1 141 LYS n 
1 142 ALA n 
1 143 THR n 
1 144 GLU n 
1 145 GLU n 
1 146 THR n 
1 147 PHE n 
1 148 LYS n 
1 149 LEU n 
1 150 SER n 
1 151 TYR n 
1 152 GLY n 
1 153 ILE n 
1 154 ALA n 
1 155 THR n 
1 156 VAL n 
1 157 ARG n 
1 158 GLU n 
1 159 VAL n 
1 160 LEU n 
1 161 SER n 
1 162 ASP n 
1 163 ARG n 
1 164 GLU n 
1 165 LEU n 
1 166 HIS n 
1 167 LEU n 
1 168 SER n 
1 169 TRP n 
1 170 GLU n 
1 171 VAL n 
1 172 GLY n 
1 173 LYS n 
1 174 PRO n 
1 175 ARG n 
1 176 PRO n 
1 177 PRO n 
1 178 LEU n 
1 179 ASN n 
1 180 ARG n 
1 181 ASN n 
1 182 TYR n 
1 183 VAL n 
1 184 PHE n 
1 185 THR n 
1 186 GLY n 
1 187 TYR n 
1 188 ARG n 
1 189 VAL n 
1 190 THR n 
1 191 LYS n 
1 192 ASN n 
1 193 SER n 
1 194 LYS n 
1 195 VAL n 
1 196 GLN n 
1 197 ILE n 
1 198 GLY n 
1 199 GLU n 
1 200 TYR n 
1 201 THR n 
1 202 PHE n 
1 203 GLU n 
1 204 LYS n 
1 205 GLY n 
1 206 ASP n 
1 207 TYR n 
1 208 GLY n 
1 209 ASP n 
1 210 ALA n 
1 211 VAL n 
1 212 VAL n 
1 213 TYR n 
1 214 ARG n 
1 215 GLY n 
1 216 THR n 
1 217 THR n 
1 218 THR n 
1 219 TYR n 
1 220 LYS n 
1 221 LEU n 
1 222 ASN n 
1 223 VAL n 
1 224 GLY n 
1 225 ASP n 
1 226 TYR n 
1 227 PHE n 
1 228 VAL n 
1 229 LEU n 
1 230 THR n 
1 231 SER n 
1 232 HIS n 
1 233 THR n 
1 234 VAL n 
1 235 MET n 
1 236 PRO n 
1 237 LEU n 
1 238 SER n 
1 239 ALA n 
1 240 PRO n 
1 241 THR n 
1 242 LEU n 
1 243 VAL n 
1 244 PRO n 
1 245 GLN n 
1 246 GLU n 
1 247 HIS n 
1 248 TYR n 
1 249 VAL n 
1 250 ARG n 
1 251 ILE n 
1 252 THR n 
1 253 GLY n 
1 254 LEU n 
1 255 TYR n 
1 256 PRO n 
1 257 THR n 
1 258 LEU n 
1 259 ASN n 
1 260 ILE n 
1 261 SER n 
1 262 ASP n 
1 263 GLU n 
1 264 PHE n 
1 265 SER n 
1 266 SER n 
1 267 ASN n 
1 268 VAL n 
1 269 ALA n 
1 270 ASN n 
1 271 TYR n 
1 272 GLN n 
1 273 LYS n 
1 274 VAL n 
1 275 GLY n 
1 276 MET n 
1 277 GLN n 
1 278 LYS n 
1 279 TYR n 
1 280 SER n 
1 281 THR n 
1 282 LEU n 
1 283 GLN n 
1 284 GLY n 
1 285 PRO n 
1 286 PRO n 
1 287 GLY n 
1 288 THR n 
1 289 GLY n 
1 290 LYS n 
1 291 SER n 
1 292 HIS n 
1 293 PHE n 
1 294 ALA n 
1 295 ILE n 
1 296 GLY n 
1 297 LEU n 
1 298 ALA n 
1 299 LEU n 
1 300 TYR n 
1 301 TYR n 
1 302 PRO n 
1 303 SER n 
1 304 ALA n 
1 305 ARG n 
1 306 ILE n 
1 307 VAL n 
1 308 TYR n 
1 309 THR n 
1 310 ALA n 
1 311 CYS n 
1 312 SER n 
1 313 HIS n 
1 314 ALA n 
1 315 ALA n 
1 316 VAL n 
1 317 ASP n 
1 318 ALA n 
1 319 LEU n 
1 320 CYS n 
1 321 GLU n 
1 322 LYS n 
1 323 ALA n 
1 324 LEU n 
1 325 LYS n 
1 326 TYR n 
1 327 LEU n 
1 328 PRO n 
1 329 ILE n 
1 330 ASP n 
1 331 LYS n 
1 332 CYS n 
1 333 SER n 
1 334 ARG n 
1 335 ILE n 
1 336 ILE n 
1 337 PRO n 
1 338 ALA n 
1 339 ARG n 
1 340 ALA n 
1 341 ARG n 
1 342 VAL n 
1 343 GLU n 
1 344 CYS n 
1 345 PHE n 
1 346 ASP n 
1 347 LYS n 
1 348 PHE n 
1 349 LYS n 
1 350 VAL n 
1 351 ASN n 
1 352 SER n 
1 353 THR n 
1 354 LEU n 
1 355 GLU n 
1 356 GLN n 
1 357 TYR n 
1 358 VAL n 
1 359 PHE n 
1 360 CYS n 
1 361 THR n 
1 362 VAL n 
1 363 ASN n 
1 364 ALA n 
1 365 LEU n 
1 366 PRO n 
1 367 GLU n 
1 368 THR n 
1 369 THR n 
1 370 ALA n 
1 371 ASP n 
1 372 ILE n 
1 373 VAL n 
1 374 VAL n 
1 375 PHE n 
1 376 ASP n 
1 377 GLU n 
1 378 ILE n 
1 379 SER n 
1 380 MET n 
1 381 ALA n 
1 382 THR n 
1 383 ASN n 
1 384 TYR n 
1 385 ASP n 
1 386 LEU n 
1 387 SER n 
1 388 VAL n 
1 389 VAL n 
1 390 ASN n 
1 391 ALA n 
1 392 ARG n 
1 393 LEU n 
1 394 ARG n 
1 395 ALA n 
1 396 LYS n 
1 397 HIS n 
1 398 TYR n 
1 399 VAL n 
1 400 TYR n 
1 401 ILE n 
1 402 GLY n 
1 403 ASP n 
1 404 PRO n 
1 405 ALA n 
1 406 GLN n 
1 407 LEU n 
1 408 PRO n 
1 409 ALA n 
1 410 PRO n 
1 411 ARG n 
1 412 THR n 
1 413 LEU n 
1 414 LEU n 
1 415 THR n 
1 416 LYS n 
1 417 GLY n 
1 418 THR n 
1 419 LEU n 
1 420 GLU n 
1 421 PRO n 
1 422 GLU n 
1 423 TYR n 
1 424 PHE n 
1 425 ASN n 
1 426 SER n 
1 427 VAL n 
1 428 CYS n 
1 429 ARG n 
1 430 LEU n 
1 431 MET n 
1 432 LYS n 
1 433 THR n 
1 434 ILE n 
1 435 GLY n 
1 436 PRO n 
1 437 ASP n 
1 438 MET n 
1 439 PHE n 
1 440 LEU n 
1 441 GLY n 
1 442 THR n 
1 443 CYS n 
1 444 ARG n 
1 445 ARG n 
1 446 CYS n 
1 447 PRO n 
1 448 ALA n 
1 449 GLU n 
1 450 ILE n 
1 451 VAL n 
1 452 ASP n 
1 453 THR n 
1 454 VAL n 
1 455 SER n 
1 456 ALA n 
1 457 LEU n 
1 458 VAL n 
1 459 TYR n 
1 460 ASP n 
1 461 ASN n 
1 462 LYS n 
1 463 LEU n 
1 464 LYS n 
1 465 ALA n 
1 466 HIS n 
1 467 LYS n 
1 468 ASP n 
1 469 LYS n 
1 470 SER n 
1 471 ALA n 
1 472 GLN n 
1 473 CYS n 
1 474 PHE n 
1 475 LYS n 
1 476 MET n 
1 477 PHE n 
1 478 TYR n 
1 479 LYS n 
1 480 GLY n 
1 481 VAL n 
1 482 ILE n 
1 483 THR n 
1 484 HIS n 
1 485 ASP n 
1 486 VAL n 
1 487 SER n 
1 488 SER n 
1 489 ALA n 
1 490 ILE n 
1 491 ASN n 
1 492 ARG n 
1 493 PRO n 
1 494 GLN n 
1 495 ILE n 
1 496 GLY n 
1 497 VAL n 
1 498 VAL n 
1 499 ARG n 
1 500 GLU n 
1 501 PHE n 
1 502 LEU n 
1 503 THR n 
1 504 ARG n 
1 505 ASN n 
1 506 PRO n 
1 507 ALA n 
1 508 TRP n 
1 509 ARG n 
1 510 LYS n 
1 511 ALA n 
1 512 VAL n 
1 513 PHE n 
1 514 ILE n 
1 515 SER n 
1 516 PRO n 
1 517 TYR n 
1 518 ASN n 
1 519 SER n 
1 520 GLN n 
1 521 ASN n 
1 522 ALA n 
1 523 VAL n 
1 524 ALA n 
1 525 SER n 
1 526 LYS n 
1 527 ILE n 
1 528 LEU n 
1 529 GLY n 
1 530 LEU n 
1 531 PRO n 
1 532 THR n 
1 533 GLN n 
1 534 THR n 
1 535 VAL n 
1 536 ASP n 
1 537 SER n 
1 538 SER n 
1 539 GLN n 
1 540 GLY n 
1 541 SER n 
1 542 GLU n 
1 543 TYR n 
1 544 ASP n 
1 545 TYR n 
1 546 VAL n 
1 547 ILE n 
1 548 PHE n 
1 549 THR n 
1 550 GLN n 
1 551 THR n 
1 552 THR n 
1 553 GLU n 
1 554 THR n 
1 555 ALA n 
1 556 HIS n 
1 557 SER n 
1 558 CYS n 
1 559 ASN n 
1 560 VAL n 
1 561 ASN n 
1 562 ARG n 
1 563 PHE n 
1 564 ASN n 
1 565 VAL n 
1 566 ALA n 
1 567 ILE n 
1 568 THR n 
1 569 ARG n 
1 570 ALA n 
1 571 LYS n 
1 572 VAL n 
1 573 GLY n 
1 574 ILE n 
1 575 LEU n 
1 576 CYS n 
1 577 ILE n 
1 578 MET n 
1 579 SER n 
1 580 ASP n 
1 581 ARG n 
1 582 ASP n 
1 583 LEU n 
1 584 TYR n 
1 585 ASP n 
1 586 LYS n 
1 587 LEU n 
1 588 GLN n 
1 589 PHE n 
1 590 THR n 
1 591 SER n 
1 592 LEU n 
1 593 GLU n 
1 594 ILE n 
1 595 PRO n 
1 596 ARG n 
1 597 ARG n 
1 598 ASN n 
1 599 VAL n 
1 600 ALA n 
1 601 THR n 
1 602 LEU n 
1 603 GLN 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                   603 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_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      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                        ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                                       ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                     ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                                                       ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                                                      ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                                        ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                                      ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                                          ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                     ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                                        ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                                         ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                                     ? 'C5 H11 N O2 S'  149.211 
MPO non-polymer         . '3[N-MORPHOLINO]PROPANE SULFONIC ACID'                         ? 'C7 H15 N O4 S'  209.263 
MYC non-polymer         . '3,5,7-TRIHYDROXY-2-(3,4,5-TRIHYDROXYPHENYL)-4H-CHROMEN-4-ONE' 
;2-(3,4,5-TRIHYDROXYPHENYL)-3,5,7-TRIHYDROXY-4H-1-BENZOPYRAN-4-ONE; 3,3',4',5,5',7-HEXAHYDROXYFLAVONE; MYRICETIN; CANNABISCETIN
;
'C15 H10 O8'     318.235 
PHE 'L-peptide linking' y PHENYLALANINE                                                  ? 'C9 H11 N O2'    165.189 
PO4 non-polymer         . 'PHOSPHATE ION'                                                ? 'O4 P -3'        94.971  
PRO 'L-peptide linking' y PROLINE                                                        ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                                         ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                                                      ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                     ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                                       ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                                         ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'                                                     ? 'Zn 2'           65.409  
# 
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   SER 1   -1  ?   ?   ?   A . n 
A 1 2   MET 2   0   ?   ?   ?   A . n 
A 1 3   ALA 3   1   1   ALA ALA A . n 
A 1 4   VAL 4   2   2   VAL VAL A . n 
A 1 5   GLY 5   3   3   GLY GLY A . n 
A 1 6   ALA 6   4   4   ALA ALA A . n 
A 1 7   CYS 7   5   5   CYS CYS A . n 
A 1 8   VAL 8   6   6   VAL VAL A . n 
A 1 9   LEU 9   7   7   LEU LEU A . n 
A 1 10  CYS 10  8   8   CYS CYS A . n 
A 1 11  ASN 11  9   9   ASN ASN A . n 
A 1 12  SER 12  10  10  SER SER A . n 
A 1 13  GLN 13  11  11  GLN GLN A . n 
A 1 14  THR 14  12  12  THR THR A . n 
A 1 15  SER 15  13  13  SER SER A . n 
A 1 16  LEU 16  14  14  LEU LEU A . n 
A 1 17  ARG 17  15  15  ARG ARG A . n 
A 1 18  CYS 18  16  16  CYS CYS A . n 
A 1 19  GLY 19  17  17  GLY GLY A . n 
A 1 20  ALA 20  18  18  ALA ALA A . n 
A 1 21  CYS 21  19  19  CYS CYS A . n 
A 1 22  ILE 22  20  20  ILE ILE A . n 
A 1 23  ARG 23  21  21  ARG ARG A . n 
A 1 24  ARG 24  22  22  ARG ARG A . n 
A 1 25  PRO 25  23  23  PRO PRO A . n 
A 1 26  PHE 26  24  24  PHE PHE A . n 
A 1 27  LEU 27  25  25  LEU LEU A . n 
A 1 28  CYS 28  26  26  CYS CYS A . n 
A 1 29  CYS 29  27  27  CYS CYS A . n 
A 1 30  LYS 30  28  28  LYS LYS A . n 
A 1 31  CYS 31  29  29  CYS CYS A . n 
A 1 32  CYS 32  30  30  CYS CYS A . n 
A 1 33  TYR 33  31  31  TYR TYR A . n 
A 1 34  ASP 34  32  32  ASP ASP A . n 
A 1 35  HIS 35  33  33  HIS HIS A . n 
A 1 36  VAL 36  34  34  VAL VAL A . n 
A 1 37  ILE 37  35  35  ILE ILE A . n 
A 1 38  SER 38  36  36  SER SER A . n 
A 1 39  THR 39  37  37  THR THR A . n 
A 1 40  SER 40  38  38  SER SER A . n 
A 1 41  HIS 41  39  39  HIS HIS A . n 
A 1 42  LYS 42  40  40  LYS LYS A . n 
A 1 43  LEU 43  41  41  LEU LEU A . n 
A 1 44  VAL 44  42  42  VAL VAL A . n 
A 1 45  LEU 45  43  43  LEU LEU A . n 
A 1 46  SER 46  44  44  SER SER A . n 
A 1 47  VAL 47  45  45  VAL VAL A . n 
A 1 48  ASN 48  46  46  ASN ASN A . n 
A 1 49  PRO 49  47  47  PRO PRO A . n 
A 1 50  TYR 50  48  48  TYR TYR A . n 
A 1 51  VAL 51  49  49  VAL VAL A . n 
A 1 52  CYS 52  50  50  CYS CYS A . n 
A 1 53  ASN 53  51  51  ASN ASN A . n 
A 1 54  ALA 54  52  52  ALA ALA A . n 
A 1 55  PRO 55  53  53  PRO PRO A . n 
A 1 56  GLY 56  54  54  GLY GLY A . n 
A 1 57  CYS 57  55  55  CYS CYS A . n 
A 1 58  ASP 58  56  56  ASP ASP A . n 
A 1 59  VAL 59  57  57  VAL VAL A . n 
A 1 60  THR 60  58  58  THR THR A . n 
A 1 61  ASP 61  59  59  ASP ASP A . n 
A 1 62  VAL 62  60  60  VAL VAL A . n 
A 1 63  THR 63  61  61  THR THR A . n 
A 1 64  GLN 64  62  62  GLN GLN A . n 
A 1 65  LEU 65  63  63  LEU LEU A . n 
A 1 66  TYR 66  64  64  TYR TYR A . n 
A 1 67  LEU 67  65  65  LEU LEU A . n 
A 1 68  GLY 68  66  66  GLY GLY A . n 
A 1 69  GLY 69  67  67  GLY GLY A . n 
A 1 70  MET 70  68  68  MET MET A . n 
A 1 71  SER 71  69  69  SER SER A . n 
A 1 72  TYR 72  70  70  TYR TYR A . n 
A 1 73  TYR 73  71  71  TYR TYR A . n 
A 1 74  CYS 74  72  72  CYS CYS A . n 
A 1 75  LYS 75  73  73  LYS LYS A . n 
A 1 76  SER 76  74  74  SER SER A . n 
A 1 77  HIS 77  75  75  HIS HIS A . n 
A 1 78  LYS 78  76  76  LYS LYS A . n 
A 1 79  PRO 79  77  77  PRO PRO A . n 
A 1 80  PRO 80  78  78  PRO PRO A . n 
A 1 81  ILE 81  79  79  ILE ILE A . n 
A 1 82  SER 82  80  80  SER SER A . n 
A 1 83  PHE 83  81  81  PHE PHE A . n 
A 1 84  PRO 84  82  82  PRO PRO A . n 
A 1 85  LEU 85  83  83  LEU LEU A . n 
A 1 86  CYS 86  84  84  CYS CYS A . n 
A 1 87  ALA 87  85  85  ALA ALA A . n 
A 1 88  ASN 88  86  86  ASN ASN A . n 
A 1 89  GLY 89  87  87  GLY GLY A . n 
A 1 90  GLN 90  88  88  GLN GLN A . n 
A 1 91  VAL 91  89  89  VAL VAL A . n 
A 1 92  PHE 92  90  90  PHE PHE A . n 
A 1 93  GLY 93  91  91  GLY GLY A . n 
A 1 94  LEU 94  92  92  LEU LEU A . n 
A 1 95  TYR 95  93  93  TYR TYR A . n 
A 1 96  LYS 96  94  94  LYS LYS A . n 
A 1 97  ASN 97  95  ?   ?   ?   A . n 
A 1 98  THR 98  96  ?   ?   ?   A . n 
A 1 99  CYS 99  97  ?   ?   ?   A . n 
A 1 100 VAL 100 98  ?   ?   ?   A . n 
A 1 101 GLY 101 99  ?   ?   ?   A . n 
A 1 102 SER 102 100 ?   ?   ?   A . n 
A 1 103 ASP 103 101 ?   ?   ?   A . n 
A 1 104 ASN 104 102 ?   ?   ?   A . n 
A 1 105 VAL 105 103 103 VAL VAL A . n 
A 1 106 THR 106 104 104 THR THR A . n 
A 1 107 ASP 107 105 105 ASP ASP A . n 
A 1 108 PHE 108 106 106 PHE PHE A . n 
A 1 109 ASN 109 107 107 ASN ASN A . n 
A 1 110 ALA 110 108 108 ALA ALA A . n 
A 1 111 ILE 111 109 109 ILE ILE A . n 
A 1 112 ALA 112 110 110 ALA ALA A . n 
A 1 113 THR 113 111 111 THR THR A . n 
A 1 114 CYS 114 112 112 CYS CYS A . n 
A 1 115 ASP 115 113 113 ASP ASP A . n 
A 1 116 TRP 116 114 114 TRP TRP A . n 
A 1 117 THR 117 115 115 THR THR A . n 
A 1 118 ASN 118 116 116 ASN ASN A . n 
A 1 119 ALA 119 117 117 ALA ALA A . n 
A 1 120 GLY 120 118 118 GLY GLY A . n 
A 1 121 ASP 121 119 119 ASP ASP A . n 
A 1 122 TYR 122 120 120 TYR TYR A . n 
A 1 123 ILE 123 121 121 ILE ILE A . n 
A 1 124 LEU 124 122 122 LEU LEU A . n 
A 1 125 ALA 125 123 123 ALA ALA A . n 
A 1 126 ASN 126 124 124 ASN ASN A . n 
A 1 127 THR 127 125 125 THR THR A . n 
A 1 128 CYS 128 126 126 CYS CYS A . n 
A 1 129 THR 129 127 127 THR THR A . n 
A 1 130 GLU 130 128 128 GLU GLU A . n 
A 1 131 ARG 131 129 129 ARG ARG A . n 
A 1 132 LEU 132 130 130 LEU LEU A . n 
A 1 133 LYS 133 131 131 LYS LYS A . n 
A 1 134 LEU 134 132 132 LEU LEU A . n 
A 1 135 PHE 135 133 133 PHE PHE A . n 
A 1 136 ALA 136 134 134 ALA ALA A . n 
A 1 137 ALA 137 135 135 ALA ALA A . n 
A 1 138 GLU 138 136 136 GLU GLU A . n 
A 1 139 THR 139 137 137 THR THR A . n 
A 1 140 LEU 140 138 138 LEU LEU A . n 
A 1 141 LYS 141 139 139 LYS LYS A . n 
A 1 142 ALA 142 140 140 ALA ALA A . n 
A 1 143 THR 143 141 141 THR THR A . n 
A 1 144 GLU 144 142 142 GLU GLU A . n 
A 1 145 GLU 145 143 143 GLU GLU A . n 
A 1 146 THR 146 144 144 THR THR A . n 
A 1 147 PHE 147 145 145 PHE PHE A . n 
A 1 148 LYS 148 146 146 LYS LYS A . n 
A 1 149 LEU 149 147 147 LEU LEU A . n 
A 1 150 SER 150 148 148 SER SER A . n 
A 1 151 TYR 151 149 149 TYR TYR A . n 
A 1 152 GLY 152 150 150 GLY GLY A . n 
A 1 153 ILE 153 151 151 ILE ILE A . n 
A 1 154 ALA 154 152 152 ALA ALA A . n 
A 1 155 THR 155 153 153 THR THR A . n 
A 1 156 VAL 156 154 154 VAL VAL A . n 
A 1 157 ARG 157 155 155 ARG ARG A . n 
A 1 158 GLU 158 156 156 GLU GLU A . n 
A 1 159 VAL 159 157 157 VAL VAL A . n 
A 1 160 LEU 160 158 158 LEU LEU A . n 
A 1 161 SER 161 159 159 SER SER A . n 
A 1 162 ASP 162 160 160 ASP ASP A . n 
A 1 163 ARG 163 161 161 ARG ARG A . n 
A 1 164 GLU 164 162 162 GLU GLU A . n 
A 1 165 LEU 165 163 163 LEU LEU A . n 
A 1 166 HIS 166 164 164 HIS HIS A . n 
A 1 167 LEU 167 165 165 LEU LEU A . n 
A 1 168 SER 168 166 166 SER SER A . n 
A 1 169 TRP 169 167 167 TRP TRP A . n 
A 1 170 GLU 170 168 168 GLU GLU A . n 
A 1 171 VAL 171 169 169 VAL VAL A . n 
A 1 172 GLY 172 170 170 GLY GLY A . n 
A 1 173 LYS 173 171 171 LYS LYS A . n 
A 1 174 PRO 174 172 172 PRO PRO A . n 
A 1 175 ARG 175 173 173 ARG ARG A . n 
A 1 176 PRO 176 174 174 PRO PRO A . n 
A 1 177 PRO 177 175 175 PRO PRO A . n 
A 1 178 LEU 178 176 176 LEU LEU A . n 
A 1 179 ASN 179 177 177 ASN ASN A . n 
A 1 180 ARG 180 178 178 ARG ARG A . n 
A 1 181 ASN 181 179 179 ASN ASN A . n 
A 1 182 TYR 182 180 180 TYR TYR A . n 
A 1 183 VAL 183 181 181 VAL VAL A . n 
A 1 184 PHE 184 182 182 PHE PHE A . n 
A 1 185 THR 185 183 183 THR THR A . n 
A 1 186 GLY 186 184 184 GLY GLY A . n 
A 1 187 TYR 187 185 185 TYR TYR A . n 
A 1 188 ARG 188 186 ?   ?   ?   A . n 
A 1 189 VAL 189 187 ?   ?   ?   A . n 
A 1 190 THR 190 188 ?   ?   ?   A . n 
A 1 191 LYS 191 189 ?   ?   ?   A . n 
A 1 192 ASN 192 190 ?   ?   ?   A . n 
A 1 193 SER 193 191 ?   ?   ?   A . n 
A 1 194 LYS 194 192 ?   ?   ?   A . n 
A 1 195 VAL 195 193 ?   ?   ?   A . n 
A 1 196 GLN 196 194 194 GLN GLN A . n 
A 1 197 ILE 197 195 195 ILE ILE A . n 
A 1 198 GLY 198 196 196 GLY GLY A . n 
A 1 199 GLU 199 197 197 GLU GLU A . n 
A 1 200 TYR 200 198 198 TYR TYR A . n 
A 1 201 THR 201 199 199 THR THR A . n 
A 1 202 PHE 202 200 200 PHE PHE A . n 
A 1 203 GLU 203 201 201 GLU GLU A . n 
A 1 204 LYS 204 202 202 LYS LYS A . n 
A 1 205 GLY 205 203 ?   ?   ?   A . n 
A 1 206 ASP 206 204 ?   ?   ?   A . n 
A 1 207 TYR 207 205 ?   ?   ?   A . n 
A 1 208 GLY 208 206 ?   ?   ?   A . n 
A 1 209 ASP 209 207 207 ASP ASP A . n 
A 1 210 ALA 210 208 208 ALA ALA A . n 
A 1 211 VAL 211 209 209 VAL VAL A . n 
A 1 212 VAL 212 210 210 VAL VAL A . n 
A 1 213 TYR 213 211 211 TYR TYR A . n 
A 1 214 ARG 214 212 212 ARG ARG A . n 
A 1 215 GLY 215 213 213 GLY GLY A . n 
A 1 216 THR 216 214 214 THR THR A . n 
A 1 217 THR 217 215 215 THR THR A . n 
A 1 218 THR 218 216 216 THR THR A . n 
A 1 219 TYR 219 217 217 TYR TYR A . n 
A 1 220 LYS 220 218 218 LYS LYS A . n 
A 1 221 LEU 221 219 219 LEU LEU A . n 
A 1 222 ASN 222 220 220 ASN ASN A . n 
A 1 223 VAL 223 221 221 VAL VAL A . n 
A 1 224 GLY 224 222 222 GLY GLY A . n 
A 1 225 ASP 225 223 223 ASP ASP A . n 
A 1 226 TYR 226 224 224 TYR TYR A . n 
A 1 227 PHE 227 225 ?   ?   ?   A . n 
A 1 228 VAL 228 226 226 VAL VAL A . n 
A 1 229 LEU 229 227 227 LEU LEU A . n 
A 1 230 THR 230 228 228 THR THR A . n 
A 1 231 SER 231 229 229 SER SER A . n 
A 1 232 HIS 232 230 230 HIS HIS A . n 
A 1 233 THR 233 231 231 THR THR A . n 
A 1 234 VAL 234 232 232 VAL VAL A . n 
A 1 235 MET 235 233 233 MET MET A . n 
A 1 236 PRO 236 234 234 PRO PRO A . n 
A 1 237 LEU 237 235 235 LEU LEU A . n 
A 1 238 SER 238 236 236 SER SER A . n 
A 1 239 ALA 239 237 237 ALA ALA A . n 
A 1 240 PRO 240 238 238 PRO PRO A . n 
A 1 241 THR 241 239 239 THR THR A . n 
A 1 242 LEU 242 240 240 LEU LEU A . n 
A 1 243 VAL 243 241 241 VAL VAL A . n 
A 1 244 PRO 244 242 242 PRO PRO A . n 
A 1 245 GLN 245 243 243 GLN GLN A . n 
A 1 246 GLU 246 244 244 GLU GLU A . n 
A 1 247 HIS 247 245 245 HIS HIS A . n 
A 1 248 TYR 248 246 246 TYR TYR A . n 
A 1 249 VAL 249 247 247 VAL VAL A . n 
A 1 250 ARG 250 248 248 ARG ARG A . n 
A 1 251 ILE 251 249 249 ILE ILE A . n 
A 1 252 THR 252 250 250 THR THR A . n 
A 1 253 GLY 253 251 251 GLY GLY A . n 
A 1 254 LEU 254 252 252 LEU LEU A . n 
A 1 255 TYR 255 253 253 TYR TYR A . n 
A 1 256 PRO 256 254 254 PRO PRO A . n 
A 1 257 THR 257 255 255 THR THR A . n 
A 1 258 LEU 258 256 256 LEU LEU A . n 
A 1 259 ASN 259 257 257 ASN ASN A . n 
A 1 260 ILE 260 258 258 ILE ILE A . n 
A 1 261 SER 261 259 259 SER SER A . n 
A 1 262 ASP 262 260 260 ASP ASP A . n 
A 1 263 GLU 263 261 261 GLU GLU A . n 
A 1 264 PHE 264 262 262 PHE PHE A . n 
A 1 265 SER 265 263 263 SER SER A . n 
A 1 266 SER 266 264 264 SER SER A . n 
A 1 267 ASN 267 265 265 ASN ASN A . n 
A 1 268 VAL 268 266 266 VAL VAL A . n 
A 1 269 ALA 269 267 267 ALA ALA A . n 
A 1 270 ASN 270 268 268 ASN ASN A . n 
A 1 271 TYR 271 269 269 TYR TYR A . n 
A 1 272 GLN 272 270 270 GLN GLN A . n 
A 1 273 LYS 273 271 271 LYS LYS A . n 
A 1 274 VAL 274 272 272 VAL VAL A . n 
A 1 275 GLY 275 273 273 GLY GLY A . n 
A 1 276 MET 276 274 274 MET MET A . n 
A 1 277 GLN 277 275 275 GLN GLN A . n 
A 1 278 LYS 278 276 276 LYS LYS A . n 
A 1 279 TYR 279 277 277 TYR TYR A . n 
A 1 280 SER 280 278 278 SER SER A . n 
A 1 281 THR 281 279 279 THR THR A . n 
A 1 282 LEU 282 280 280 LEU LEU A . n 
A 1 283 GLN 283 281 281 GLN GLN A . n 
A 1 284 GLY 284 282 282 GLY GLY A . n 
A 1 285 PRO 285 283 283 PRO PRO A . n 
A 1 286 PRO 286 284 284 PRO PRO A . n 
A 1 287 GLY 287 285 285 GLY GLY A . n 
A 1 288 THR 288 286 286 THR THR A . n 
A 1 289 GLY 289 287 287 GLY GLY A . n 
A 1 290 LYS 290 288 288 LYS LYS A . n 
A 1 291 SER 291 289 289 SER SER A . n 
A 1 292 HIS 292 290 290 HIS HIS A . n 
A 1 293 PHE 293 291 291 PHE PHE A . n 
A 1 294 ALA 294 292 292 ALA ALA A . n 
A 1 295 ILE 295 293 293 ILE ILE A . n 
A 1 296 GLY 296 294 294 GLY GLY A . n 
A 1 297 LEU 297 295 295 LEU LEU A . n 
A 1 298 ALA 298 296 296 ALA ALA A . n 
A 1 299 LEU 299 297 297 LEU LEU A . n 
A 1 300 TYR 300 298 298 TYR TYR A . n 
A 1 301 TYR 301 299 299 TYR TYR A . n 
A 1 302 PRO 302 300 300 PRO PRO A . n 
A 1 303 SER 303 301 301 SER SER A . n 
A 1 304 ALA 304 302 302 ALA ALA A . n 
A 1 305 ARG 305 303 303 ARG ARG A . n 
A 1 306 ILE 306 304 304 ILE ILE A . n 
A 1 307 VAL 307 305 305 VAL VAL A . n 
A 1 308 TYR 308 306 306 TYR TYR A . n 
A 1 309 THR 309 307 307 THR THR A . n 
A 1 310 ALA 310 308 308 ALA ALA A . n 
A 1 311 CYS 311 309 309 CYS CYS A . n 
A 1 312 SER 312 310 310 SER SER A . n 
A 1 313 HIS 313 311 311 HIS HIS A . n 
A 1 314 ALA 314 312 312 ALA ALA A . n 
A 1 315 ALA 315 313 313 ALA ALA A . n 
A 1 316 VAL 316 314 314 VAL VAL A . n 
A 1 317 ASP 317 315 315 ASP ASP A . n 
A 1 318 ALA 318 316 316 ALA ALA A . n 
A 1 319 LEU 319 317 317 LEU LEU A . n 
A 1 320 CYS 320 318 318 CYS CYS A . n 
A 1 321 GLU 321 319 319 GLU GLU A . n 
A 1 322 LYS 322 320 320 LYS LYS A . n 
A 1 323 ALA 323 321 321 ALA ALA A . n 
A 1 324 LEU 324 322 322 LEU LEU A . n 
A 1 325 LYS 325 323 323 LYS LYS A . n 
A 1 326 TYR 326 324 324 TYR TYR A . n 
A 1 327 LEU 327 325 325 LEU LEU A . n 
A 1 328 PRO 328 326 326 PRO PRO A . n 
A 1 329 ILE 329 327 327 ILE ILE A . n 
A 1 330 ASP 330 328 328 ASP ASP A . n 
A 1 331 LYS 331 329 329 LYS LYS A . n 
A 1 332 CYS 332 330 330 CYS CYS A . n 
A 1 333 SER 333 331 331 SER SER A . n 
A 1 334 ARG 334 332 332 ARG ARG A . n 
A 1 335 ILE 335 333 333 ILE ILE A . n 
A 1 336 ILE 336 334 334 ILE ILE A . n 
A 1 337 PRO 337 335 335 PRO PRO A . n 
A 1 338 ALA 338 336 336 ALA ALA A . n 
A 1 339 ARG 339 337 337 ARG ARG A . n 
A 1 340 ALA 340 338 338 ALA ALA A . n 
A 1 341 ARG 341 339 339 ARG ARG A . n 
A 1 342 VAL 342 340 340 VAL VAL A . n 
A 1 343 GLU 343 341 341 GLU GLU A . n 
A 1 344 CYS 344 342 342 CYS CYS A . n 
A 1 345 PHE 345 343 343 PHE PHE A . n 
A 1 346 ASP 346 344 344 ASP ASP A . n 
A 1 347 LYS 347 345 345 LYS LYS A . n 
A 1 348 PHE 348 346 346 PHE PHE A . n 
A 1 349 LYS 349 347 347 LYS LYS A . n 
A 1 350 VAL 350 348 348 VAL VAL A . n 
A 1 351 ASN 351 349 349 ASN ASN A . n 
A 1 352 SER 352 350 350 SER SER A . n 
A 1 353 THR 353 351 351 THR THR A . n 
A 1 354 LEU 354 352 352 LEU LEU A . n 
A 1 355 GLU 355 353 353 GLU GLU A . n 
A 1 356 GLN 356 354 354 GLN GLN A . n 
A 1 357 TYR 357 355 355 TYR TYR A . n 
A 1 358 VAL 358 356 356 VAL VAL A . n 
A 1 359 PHE 359 357 357 PHE PHE A . n 
A 1 360 CYS 360 358 358 CYS CYS A . n 
A 1 361 THR 361 359 359 THR THR A . n 
A 1 362 VAL 362 360 360 VAL VAL A . n 
A 1 363 ASN 363 361 361 ASN ASN A . n 
A 1 364 ALA 364 362 362 ALA ALA A . n 
A 1 365 LEU 365 363 363 LEU LEU A . n 
A 1 366 PRO 366 364 364 PRO PRO A . n 
A 1 367 GLU 367 365 365 GLU GLU A . n 
A 1 368 THR 368 366 366 THR THR A . n 
A 1 369 THR 369 367 367 THR THR A . n 
A 1 370 ALA 370 368 368 ALA ALA A . n 
A 1 371 ASP 371 369 369 ASP ASP A . n 
A 1 372 ILE 372 370 370 ILE ILE A . n 
A 1 373 VAL 373 371 371 VAL VAL A . n 
A 1 374 VAL 374 372 372 VAL VAL A . n 
A 1 375 PHE 375 373 373 PHE PHE A . n 
A 1 376 ASP 376 374 374 ASP ASP A . n 
A 1 377 GLU 377 375 375 GLU GLU A . n 
A 1 378 ILE 378 376 376 ILE ILE A . n 
A 1 379 SER 379 377 377 SER SER A . n 
A 1 380 MET 380 378 378 MET MET A . n 
A 1 381 ALA 381 379 379 ALA ALA A . n 
A 1 382 THR 382 380 380 THR THR A . n 
A 1 383 ASN 383 381 381 ASN ASN A . n 
A 1 384 TYR 384 382 382 TYR TYR A . n 
A 1 385 ASP 385 383 383 ASP ASP A . n 
A 1 386 LEU 386 384 384 LEU LEU A . n 
A 1 387 SER 387 385 385 SER SER A . n 
A 1 388 VAL 388 386 386 VAL VAL A . n 
A 1 389 VAL 389 387 387 VAL VAL A . n 
A 1 390 ASN 390 388 388 ASN ASN A . n 
A 1 391 ALA 391 389 389 ALA ALA A . n 
A 1 392 ARG 392 390 390 ARG ARG A . n 
A 1 393 LEU 393 391 391 LEU LEU A . n 
A 1 394 ARG 394 392 392 ARG ARG A . n 
A 1 395 ALA 395 393 393 ALA ALA A . n 
A 1 396 LYS 396 394 394 LYS LYS A . n 
A 1 397 HIS 397 395 395 HIS HIS A . n 
A 1 398 TYR 398 396 396 TYR TYR A . n 
A 1 399 VAL 399 397 397 VAL VAL A . n 
A 1 400 TYR 400 398 398 TYR TYR A . n 
A 1 401 ILE 401 399 399 ILE ILE A . n 
A 1 402 GLY 402 400 400 GLY GLY A . n 
A 1 403 ASP 403 401 401 ASP ASP A . n 
A 1 404 PRO 404 402 402 PRO PRO A . n 
A 1 405 ALA 405 403 403 ALA ALA A . n 
A 1 406 GLN 406 404 404 GLN GLN A . n 
A 1 407 LEU 407 405 405 LEU LEU A . n 
A 1 408 PRO 408 406 406 PRO PRO A . n 
A 1 409 ALA 409 407 407 ALA ALA A . n 
A 1 410 PRO 410 408 408 PRO PRO A . n 
A 1 411 ARG 411 409 409 ARG ARG A . n 
A 1 412 THR 412 410 410 THR THR A . n 
A 1 413 LEU 413 411 411 LEU LEU A . n 
A 1 414 LEU 414 412 412 LEU LEU A . n 
A 1 415 THR 415 413 413 THR THR A . n 
A 1 416 LYS 416 414 414 LYS LYS A . n 
A 1 417 GLY 417 415 415 GLY GLY A . n 
A 1 418 THR 418 416 416 THR THR A . n 
A 1 419 LEU 419 417 417 LEU LEU A . n 
A 1 420 GLU 420 418 418 GLU GLU A . n 
A 1 421 PRO 421 419 419 PRO PRO A . n 
A 1 422 GLU 422 420 420 GLU GLU A . n 
A 1 423 TYR 423 421 421 TYR TYR A . n 
A 1 424 PHE 424 422 422 PHE PHE A . n 
A 1 425 ASN 425 423 423 ASN ASN A . n 
A 1 426 SER 426 424 424 SER SER A . n 
A 1 427 VAL 427 425 425 VAL VAL A . n 
A 1 428 CYS 428 426 426 CYS CYS A . n 
A 1 429 ARG 429 427 427 ARG ARG A . n 
A 1 430 LEU 430 428 428 LEU LEU A . n 
A 1 431 MET 431 429 429 MET MET A . n 
A 1 432 LYS 432 430 430 LYS LYS A . n 
A 1 433 THR 433 431 431 THR THR A . n 
A 1 434 ILE 434 432 432 ILE ILE A . n 
A 1 435 GLY 435 433 433 GLY GLY A . n 
A 1 436 PRO 436 434 434 PRO PRO A . n 
A 1 437 ASP 437 435 435 ASP ASP A . n 
A 1 438 MET 438 436 436 MET MET A . n 
A 1 439 PHE 439 437 437 PHE PHE A . n 
A 1 440 LEU 440 438 438 LEU LEU A . n 
A 1 441 GLY 441 439 439 GLY GLY A . n 
A 1 442 THR 442 440 440 THR THR A . n 
A 1 443 CYS 443 441 441 CYS CYS A . n 
A 1 444 ARG 444 442 442 ARG ARG A . n 
A 1 445 ARG 445 443 443 ARG ARG A . n 
A 1 446 CYS 446 444 444 CYS CYS A . n 
A 1 447 PRO 447 445 445 PRO PRO A . n 
A 1 448 ALA 448 446 446 ALA ALA A . n 
A 1 449 GLU 449 447 447 GLU GLU A . n 
A 1 450 ILE 450 448 448 ILE ILE A . n 
A 1 451 VAL 451 449 449 VAL VAL A . n 
A 1 452 ASP 452 450 450 ASP ASP A . n 
A 1 453 THR 453 451 451 THR THR A . n 
A 1 454 VAL 454 452 452 VAL VAL A . n 
A 1 455 SER 455 453 453 SER SER A . n 
A 1 456 ALA 456 454 454 ALA ALA A . n 
A 1 457 LEU 457 455 455 LEU LEU A . n 
A 1 458 VAL 458 456 456 VAL VAL A . n 
A 1 459 TYR 459 457 457 TYR TYR A . n 
A 1 460 ASP 460 458 458 ASP ASP A . n 
A 1 461 ASN 461 459 459 ASN ASN A . n 
A 1 462 LYS 462 460 460 LYS LYS A . n 
A 1 463 LEU 463 461 461 LEU LEU A . n 
A 1 464 LYS 464 462 462 LYS LYS A . n 
A 1 465 ALA 465 463 463 ALA ALA A . n 
A 1 466 HIS 466 464 464 HIS HIS A . n 
A 1 467 LYS 467 465 465 LYS LYS A . n 
A 1 468 ASP 468 466 466 ASP ASP A . n 
A 1 469 LYS 469 467 467 LYS LYS A . n 
A 1 470 SER 470 468 468 SER SER A . n 
A 1 471 ALA 471 469 469 ALA ALA A . n 
A 1 472 GLN 472 470 470 GLN GLN A . n 
A 1 473 CYS 473 471 471 CYS CYS A . n 
A 1 474 PHE 474 472 472 PHE PHE A . n 
A 1 475 LYS 475 473 473 LYS LYS A . n 
A 1 476 MET 476 474 474 MET MET A . n 
A 1 477 PHE 477 475 475 PHE PHE A . n 
A 1 478 TYR 478 476 476 TYR TYR A . n 
A 1 479 LYS 479 477 477 LYS LYS A . n 
A 1 480 GLY 480 478 478 GLY GLY A . n 
A 1 481 VAL 481 479 479 VAL VAL A . n 
A 1 482 ILE 482 480 480 ILE ILE A . n 
A 1 483 THR 483 481 481 THR THR A . n 
A 1 484 HIS 484 482 482 HIS HIS A . n 
A 1 485 ASP 485 483 483 ASP ASP A . n 
A 1 486 VAL 486 484 484 VAL VAL A . n 
A 1 487 SER 487 485 485 SER SER A . n 
A 1 488 SER 488 486 486 SER SER A . n 
A 1 489 ALA 489 487 487 ALA ALA A . n 
A 1 490 ILE 490 488 488 ILE ILE A . n 
A 1 491 ASN 491 489 489 ASN ASN A . n 
A 1 492 ARG 492 490 490 ARG ARG A . n 
A 1 493 PRO 493 491 491 PRO PRO A . n 
A 1 494 GLN 494 492 492 GLN GLN A . n 
A 1 495 ILE 495 493 493 ILE ILE A . n 
A 1 496 GLY 496 494 494 GLY GLY A . n 
A 1 497 VAL 497 495 495 VAL VAL A . n 
A 1 498 VAL 498 496 496 VAL VAL A . n 
A 1 499 ARG 499 497 497 ARG ARG A . n 
A 1 500 GLU 500 498 498 GLU GLU A . n 
A 1 501 PHE 501 499 499 PHE PHE A . n 
A 1 502 LEU 502 500 500 LEU LEU A . n 
A 1 503 THR 503 501 501 THR THR A . n 
A 1 504 ARG 504 502 502 ARG ARG A . n 
A 1 505 ASN 505 503 503 ASN ASN A . n 
A 1 506 PRO 506 504 504 PRO PRO A . n 
A 1 507 ALA 507 505 505 ALA ALA A . n 
A 1 508 TRP 508 506 506 TRP TRP A . n 
A 1 509 ARG 509 507 507 ARG ARG A . n 
A 1 510 LYS 510 508 508 LYS LYS A . n 
A 1 511 ALA 511 509 509 ALA ALA A . n 
A 1 512 VAL 512 510 510 VAL VAL A . n 
A 1 513 PHE 513 511 511 PHE PHE A . n 
A 1 514 ILE 514 512 512 ILE ILE A . n 
A 1 515 SER 515 513 513 SER SER A . n 
A 1 516 PRO 516 514 514 PRO PRO A . n 
A 1 517 TYR 517 515 515 TYR TYR A . n 
A 1 518 ASN 518 516 516 ASN ASN A . n 
A 1 519 SER 519 517 517 SER SER A . n 
A 1 520 GLN 520 518 518 GLN GLN A . n 
A 1 521 ASN 521 519 519 ASN ASN A . n 
A 1 522 ALA 522 520 520 ALA ALA A . n 
A 1 523 VAL 523 521 521 VAL VAL A . n 
A 1 524 ALA 524 522 522 ALA ALA A . n 
A 1 525 SER 525 523 523 SER SER A . n 
A 1 526 LYS 526 524 524 LYS LYS A . n 
A 1 527 ILE 527 525 525 ILE ILE A . n 
A 1 528 LEU 528 526 526 LEU LEU A . n 
A 1 529 GLY 529 527 527 GLY GLY A . n 
A 1 530 LEU 530 528 528 LEU LEU A . n 
A 1 531 PRO 531 529 529 PRO PRO A . n 
A 1 532 THR 532 530 530 THR THR A . n 
A 1 533 GLN 533 531 531 GLN GLN A . n 
A 1 534 THR 534 532 532 THR THR A . n 
A 1 535 VAL 535 533 533 VAL VAL A . n 
A 1 536 ASP 536 534 534 ASP ASP A . n 
A 1 537 SER 537 535 535 SER SER A . n 
A 1 538 SER 538 536 536 SER SER A . n 
A 1 539 GLN 539 537 537 GLN GLN A . n 
A 1 540 GLY 540 538 538 GLY GLY A . n 
A 1 541 SER 541 539 539 SER SER A . n 
A 1 542 GLU 542 540 540 GLU GLU A . n 
A 1 543 TYR 543 541 541 TYR TYR A . n 
A 1 544 ASP 544 542 542 ASP ASP A . n 
A 1 545 TYR 545 543 543 TYR TYR A . n 
A 1 546 VAL 546 544 544 VAL VAL A . n 
A 1 547 ILE 547 545 545 ILE ILE A . n 
A 1 548 PHE 548 546 546 PHE PHE A . n 
A 1 549 THR 549 547 547 THR THR A . n 
A 1 550 GLN 550 548 548 GLN GLN A . n 
A 1 551 THR 551 549 549 THR THR A . n 
A 1 552 THR 552 550 550 THR THR A . n 
A 1 553 GLU 553 551 551 GLU GLU A . n 
A 1 554 THR 554 552 552 THR THR A . n 
A 1 555 ALA 555 553 553 ALA ALA A . n 
A 1 556 HIS 556 554 554 HIS HIS A . n 
A 1 557 SER 557 555 555 SER SER A . n 
A 1 558 CYS 558 556 556 CYS CYS A . n 
A 1 559 ASN 559 557 557 ASN ASN A . n 
A 1 560 VAL 560 558 558 VAL VAL A . n 
A 1 561 ASN 561 559 559 ASN ASN A . n 
A 1 562 ARG 562 560 560 ARG ARG A . n 
A 1 563 PHE 563 561 561 PHE PHE A . n 
A 1 564 ASN 564 562 562 ASN ASN A . n 
A 1 565 VAL 565 563 563 VAL VAL A . n 
A 1 566 ALA 566 564 564 ALA ALA A . n 
A 1 567 ILE 567 565 565 ILE ILE A . n 
A 1 568 THR 568 566 566 THR THR A . n 
A 1 569 ARG 569 567 567 ARG ARG A . n 
A 1 570 ALA 570 568 568 ALA ALA A . n 
A 1 571 LYS 571 569 569 LYS LYS A . n 
A 1 572 VAL 572 570 570 VAL VAL A . n 
A 1 573 GLY 573 571 571 GLY GLY A . n 
A 1 574 ILE 574 572 572 ILE ILE A . n 
A 1 575 LEU 575 573 573 LEU LEU A . n 
A 1 576 CYS 576 574 574 CYS CYS A . n 
A 1 577 ILE 577 575 575 ILE ILE A . n 
A 1 578 MET 578 576 576 MET MET A . n 
A 1 579 SER 579 577 577 SER SER A . n 
A 1 580 ASP 580 578 578 ASP ASP A . n 
A 1 581 ARG 581 579 579 ARG ARG A . n 
A 1 582 ASP 582 580 580 ASP ASP A . n 
A 1 583 LEU 583 581 581 LEU LEU A . n 
A 1 584 TYR 584 582 582 TYR TYR A . n 
A 1 585 ASP 585 583 583 ASP ASP A . n 
A 1 586 LYS 586 584 584 LYS LYS A . n 
A 1 587 LEU 587 585 585 LEU LEU A . n 
A 1 588 GLN 588 586 586 GLN GLN A . n 
A 1 589 PHE 589 587 587 PHE PHE A . n 
A 1 590 THR 590 588 588 THR THR A . n 
A 1 591 SER 591 589 589 SER SER A . n 
A 1 592 LEU 592 590 590 LEU LEU A . n 
A 1 593 GLU 593 591 591 GLU GLU A . n 
A 1 594 ILE 594 592 592 ILE ILE A . n 
A 1 595 PRO 595 593 ?   ?   ?   A . n 
A 1 596 ARG 596 594 ?   ?   ?   A . n 
A 1 597 ARG 597 595 ?   ?   ?   A . n 
A 1 598 ASN 598 596 ?   ?   ?   A . n 
A 1 599 VAL 599 597 ?   ?   ?   A . n 
A 1 600 ALA 600 598 ?   ?   ?   A . n 
A 1 601 THR 601 599 ?   ?   ?   A . n 
A 1 602 LEU 602 600 ?   ?   ?   A . n 
A 1 603 GLN 603 601 ?   ?   ?   A . n 
B 1 1   SER 1   -1  ?   ?   ?   B . n 
B 1 2   MET 2   0   ?   ?   ?   B . n 
B 1 3   ALA 3   1   ?   ?   ?   B . n 
B 1 4   VAL 4   2   2   VAL VAL B . n 
B 1 5   GLY 5   3   3   GLY GLY B . n 
B 1 6   ALA 6   4   4   ALA ALA B . n 
B 1 7   CYS 7   5   5   CYS CYS B . n 
B 1 8   VAL 8   6   6   VAL VAL B . n 
B 1 9   LEU 9   7   7   LEU LEU B . n 
B 1 10  CYS 10  8   8   CYS CYS B . n 
B 1 11  ASN 11  9   9   ASN ASN B . n 
B 1 12  SER 12  10  10  SER SER B . n 
B 1 13  GLN 13  11  11  GLN GLN B . n 
B 1 14  THR 14  12  12  THR THR B . n 
B 1 15  SER 15  13  13  SER SER B . n 
B 1 16  LEU 16  14  14  LEU LEU B . n 
B 1 17  ARG 17  15  15  ARG ARG B . n 
B 1 18  CYS 18  16  16  CYS CYS B . n 
B 1 19  GLY 19  17  17  GLY GLY B . n 
B 1 20  ALA 20  18  18  ALA ALA B . n 
B 1 21  CYS 21  19  19  CYS CYS B . n 
B 1 22  ILE 22  20  20  ILE ILE B . n 
B 1 23  ARG 23  21  21  ARG ARG B . n 
B 1 24  ARG 24  22  22  ARG ARG B . n 
B 1 25  PRO 25  23  23  PRO PRO B . n 
B 1 26  PHE 26  24  24  PHE PHE B . n 
B 1 27  LEU 27  25  25  LEU LEU B . n 
B 1 28  CYS 28  26  26  CYS CYS B . n 
B 1 29  CYS 29  27  27  CYS CYS B . n 
B 1 30  LYS 30  28  28  LYS LYS B . n 
B 1 31  CYS 31  29  29  CYS CYS B . n 
B 1 32  CYS 32  30  30  CYS CYS B . n 
B 1 33  TYR 33  31  31  TYR TYR B . n 
B 1 34  ASP 34  32  32  ASP ASP B . n 
B 1 35  HIS 35  33  33  HIS HIS B . n 
B 1 36  VAL 36  34  34  VAL VAL B . n 
B 1 37  ILE 37  35  35  ILE ILE B . n 
B 1 38  SER 38  36  36  SER SER B . n 
B 1 39  THR 39  37  37  THR THR B . n 
B 1 40  SER 40  38  38  SER SER B . n 
B 1 41  HIS 41  39  39  HIS HIS B . n 
B 1 42  LYS 42  40  40  LYS LYS B . n 
B 1 43  LEU 43  41  41  LEU LEU B . n 
B 1 44  VAL 44  42  42  VAL VAL B . n 
B 1 45  LEU 45  43  43  LEU LEU B . n 
B 1 46  SER 46  44  44  SER SER B . n 
B 1 47  VAL 47  45  45  VAL VAL B . n 
B 1 48  ASN 48  46  46  ASN ASN B . n 
B 1 49  PRO 49  47  47  PRO PRO B . n 
B 1 50  TYR 50  48  48  TYR TYR B . n 
B 1 51  VAL 51  49  49  VAL VAL B . n 
B 1 52  CYS 52  50  50  CYS CYS B . n 
B 1 53  ASN 53  51  51  ASN ASN B . n 
B 1 54  ALA 54  52  52  ALA ALA B . n 
B 1 55  PRO 55  53  53  PRO PRO B . n 
B 1 56  GLY 56  54  54  GLY GLY B . n 
B 1 57  CYS 57  55  55  CYS CYS B . n 
B 1 58  ASP 58  56  56  ASP ASP B . n 
B 1 59  VAL 59  57  57  VAL VAL B . n 
B 1 60  THR 60  58  58  THR THR B . n 
B 1 61  ASP 61  59  59  ASP ASP B . n 
B 1 62  VAL 62  60  60  VAL VAL B . n 
B 1 63  THR 63  61  61  THR THR B . n 
B 1 64  GLN 64  62  62  GLN GLN B . n 
B 1 65  LEU 65  63  63  LEU LEU B . n 
B 1 66  TYR 66  64  64  TYR TYR B . n 
B 1 67  LEU 67  65  65  LEU LEU B . n 
B 1 68  GLY 68  66  66  GLY GLY B . n 
B 1 69  GLY 69  67  67  GLY GLY B . n 
B 1 70  MET 70  68  68  MET MET B . n 
B 1 71  SER 71  69  69  SER SER B . n 
B 1 72  TYR 72  70  70  TYR TYR B . n 
B 1 73  TYR 73  71  71  TYR TYR B . n 
B 1 74  CYS 74  72  72  CYS CYS B . n 
B 1 75  LYS 75  73  73  LYS LYS B . n 
B 1 76  SER 76  74  74  SER SER B . n 
B 1 77  HIS 77  75  75  HIS HIS B . n 
B 1 78  LYS 78  76  76  LYS LYS B . n 
B 1 79  PRO 79  77  77  PRO PRO B . n 
B 1 80  PRO 80  78  78  PRO PRO B . n 
B 1 81  ILE 81  79  79  ILE ILE B . n 
B 1 82  SER 82  80  80  SER SER B . n 
B 1 83  PHE 83  81  81  PHE PHE B . n 
B 1 84  PRO 84  82  82  PRO PRO B . n 
B 1 85  LEU 85  83  83  LEU LEU B . n 
B 1 86  CYS 86  84  84  CYS CYS B . n 
B 1 87  ALA 87  85  85  ALA ALA B . n 
B 1 88  ASN 88  86  86  ASN ASN B . n 
B 1 89  GLY 89  87  87  GLY GLY B . n 
B 1 90  GLN 90  88  88  GLN GLN B . n 
B 1 91  VAL 91  89  89  VAL VAL B . n 
B 1 92  PHE 92  90  90  PHE PHE B . n 
B 1 93  GLY 93  91  91  GLY GLY B . n 
B 1 94  LEU 94  92  92  LEU LEU B . n 
B 1 95  TYR 95  93  93  TYR TYR B . n 
B 1 96  LYS 96  94  94  LYS LYS B . n 
B 1 97  ASN 97  95  95  ASN ASN B . n 
B 1 98  THR 98  96  96  THR THR B . n 
B 1 99  CYS 99  97  97  CYS CYS B . n 
B 1 100 VAL 100 98  98  VAL VAL B . n 
B 1 101 GLY 101 99  99  GLY GLY B . n 
B 1 102 SER 102 100 100 SER SER B . n 
B 1 103 ASP 103 101 101 ASP ASP B . n 
B 1 104 ASN 104 102 102 ASN ASN B . n 
B 1 105 VAL 105 103 103 VAL VAL B . n 
B 1 106 THR 106 104 104 THR THR B . n 
B 1 107 ASP 107 105 105 ASP ASP B . n 
B 1 108 PHE 108 106 106 PHE PHE B . n 
B 1 109 ASN 109 107 107 ASN ASN B . n 
B 1 110 ALA 110 108 108 ALA ALA B . n 
B 1 111 ILE 111 109 109 ILE ILE B . n 
B 1 112 ALA 112 110 110 ALA ALA B . n 
B 1 113 THR 113 111 111 THR THR B . n 
B 1 114 CYS 114 112 112 CYS CYS B . n 
B 1 115 ASP 115 113 113 ASP ASP B . n 
B 1 116 TRP 116 114 114 TRP TRP B . n 
B 1 117 THR 117 115 115 THR THR B . n 
B 1 118 ASN 118 116 116 ASN ASN B . n 
B 1 119 ALA 119 117 117 ALA ALA B . n 
B 1 120 GLY 120 118 118 GLY GLY B . n 
B 1 121 ASP 121 119 119 ASP ASP B . n 
B 1 122 TYR 122 120 120 TYR TYR B . n 
B 1 123 ILE 123 121 121 ILE ILE B . n 
B 1 124 LEU 124 122 122 LEU LEU B . n 
B 1 125 ALA 125 123 123 ALA ALA B . n 
B 1 126 ASN 126 124 124 ASN ASN B . n 
B 1 127 THR 127 125 125 THR THR B . n 
B 1 128 CYS 128 126 126 CYS CYS B . n 
B 1 129 THR 129 127 127 THR THR B . n 
B 1 130 GLU 130 128 128 GLU GLU B . n 
B 1 131 ARG 131 129 129 ARG ARG B . n 
B 1 132 LEU 132 130 130 LEU LEU B . n 
B 1 133 LYS 133 131 131 LYS LYS B . n 
B 1 134 LEU 134 132 132 LEU LEU B . n 
B 1 135 PHE 135 133 133 PHE PHE B . n 
B 1 136 ALA 136 134 134 ALA ALA B . n 
B 1 137 ALA 137 135 135 ALA ALA B . n 
B 1 138 GLU 138 136 136 GLU GLU B . n 
B 1 139 THR 139 137 137 THR THR B . n 
B 1 140 LEU 140 138 138 LEU LEU B . n 
B 1 141 LYS 141 139 139 LYS LYS B . n 
B 1 142 ALA 142 140 140 ALA ALA B . n 
B 1 143 THR 143 141 141 THR THR B . n 
B 1 144 GLU 144 142 142 GLU GLU B . n 
B 1 145 GLU 145 143 143 GLU GLU B . n 
B 1 146 THR 146 144 144 THR THR B . n 
B 1 147 PHE 147 145 145 PHE PHE B . n 
B 1 148 LYS 148 146 146 LYS LYS B . n 
B 1 149 LEU 149 147 147 LEU LEU B . n 
B 1 150 SER 150 148 148 SER SER B . n 
B 1 151 TYR 151 149 149 TYR TYR B . n 
B 1 152 GLY 152 150 150 GLY GLY B . n 
B 1 153 ILE 153 151 151 ILE ILE B . n 
B 1 154 ALA 154 152 152 ALA ALA B . n 
B 1 155 THR 155 153 153 THR THR B . n 
B 1 156 VAL 156 154 154 VAL VAL B . n 
B 1 157 ARG 157 155 155 ARG ARG B . n 
B 1 158 GLU 158 156 156 GLU GLU B . n 
B 1 159 VAL 159 157 157 VAL VAL B . n 
B 1 160 LEU 160 158 158 LEU LEU B . n 
B 1 161 SER 161 159 159 SER SER B . n 
B 1 162 ASP 162 160 160 ASP ASP B . n 
B 1 163 ARG 163 161 161 ARG ARG B . n 
B 1 164 GLU 164 162 162 GLU GLU B . n 
B 1 165 LEU 165 163 163 LEU LEU B . n 
B 1 166 HIS 166 164 164 HIS HIS B . n 
B 1 167 LEU 167 165 165 LEU LEU B . n 
B 1 168 SER 168 166 166 SER SER B . n 
B 1 169 TRP 169 167 167 TRP TRP B . n 
B 1 170 GLU 170 168 168 GLU GLU B . n 
B 1 171 VAL 171 169 169 VAL VAL B . n 
B 1 172 GLY 172 170 170 GLY GLY B . n 
B 1 173 LYS 173 171 171 LYS LYS B . n 
B 1 174 PRO 174 172 172 PRO PRO B . n 
B 1 175 ARG 175 173 173 ARG ARG B . n 
B 1 176 PRO 176 174 174 PRO PRO B . n 
B 1 177 PRO 177 175 175 PRO PRO B . n 
B 1 178 LEU 178 176 176 LEU LEU B . n 
B 1 179 ASN 179 177 177 ASN ASN B . n 
B 1 180 ARG 180 178 178 ARG ARG B . n 
B 1 181 ASN 181 179 179 ASN ASN B . n 
B 1 182 TYR 182 180 180 TYR TYR B . n 
B 1 183 VAL 183 181 181 VAL VAL B . n 
B 1 184 PHE 184 182 182 PHE PHE B . n 
B 1 185 THR 185 183 183 THR THR B . n 
B 1 186 GLY 186 184 184 GLY GLY B . n 
B 1 187 TYR 187 185 185 TYR TYR B . n 
B 1 188 ARG 188 186 186 ARG ARG B . n 
B 1 189 VAL 189 187 187 VAL VAL B . n 
B 1 190 THR 190 188 188 THR THR B . n 
B 1 191 LYS 191 189 189 LYS LYS B . n 
B 1 192 ASN 192 190 190 ASN ASN B . n 
B 1 193 SER 193 191 191 SER SER B . n 
B 1 194 LYS 194 192 192 LYS LYS B . n 
B 1 195 VAL 195 193 193 VAL VAL B . n 
B 1 196 GLN 196 194 194 GLN GLN B . n 
B 1 197 ILE 197 195 195 ILE ILE B . n 
B 1 198 GLY 198 196 196 GLY GLY B . n 
B 1 199 GLU 199 197 197 GLU GLU B . n 
B 1 200 TYR 200 198 198 TYR TYR B . n 
B 1 201 THR 201 199 199 THR THR B . n 
B 1 202 PHE 202 200 200 PHE PHE B . n 
B 1 203 GLU 203 201 201 GLU GLU B . n 
B 1 204 LYS 204 202 202 LYS LYS B . n 
B 1 205 GLY 205 203 203 GLY GLY B . n 
B 1 206 ASP 206 204 ?   ?   ?   B . n 
B 1 207 TYR 207 205 ?   ?   ?   B . n 
B 1 208 GLY 208 206 ?   ?   ?   B . n 
B 1 209 ASP 209 207 ?   ?   ?   B . n 
B 1 210 ALA 210 208 208 ALA ALA B . n 
B 1 211 VAL 211 209 209 VAL VAL B . n 
B 1 212 VAL 212 210 210 VAL VAL B . n 
B 1 213 TYR 213 211 211 TYR TYR B . n 
B 1 214 ARG 214 212 212 ARG ARG B . n 
B 1 215 GLY 215 213 213 GLY GLY B . n 
B 1 216 THR 216 214 214 THR THR B . n 
B 1 217 THR 217 215 215 THR THR B . n 
B 1 218 THR 218 216 216 THR THR B . n 
B 1 219 TYR 219 217 217 TYR TYR B . n 
B 1 220 LYS 220 218 218 LYS LYS B . n 
B 1 221 LEU 221 219 219 LEU LEU B . n 
B 1 222 ASN 222 220 220 ASN ASN B . n 
B 1 223 VAL 223 221 221 VAL VAL B . n 
B 1 224 GLY 224 222 222 GLY GLY B . n 
B 1 225 ASP 225 223 223 ASP ASP B . n 
B 1 226 TYR 226 224 224 TYR TYR B . n 
B 1 227 PHE 227 225 225 PHE PHE B . n 
B 1 228 VAL 228 226 226 VAL VAL B . n 
B 1 229 LEU 229 227 227 LEU LEU B . n 
B 1 230 THR 230 228 228 THR THR B . n 
B 1 231 SER 231 229 229 SER SER B . n 
B 1 232 HIS 232 230 230 HIS HIS B . n 
B 1 233 THR 233 231 231 THR THR B . n 
B 1 234 VAL 234 232 232 VAL VAL B . n 
B 1 235 MET 235 233 233 MET MET B . n 
B 1 236 PRO 236 234 234 PRO PRO B . n 
B 1 237 LEU 237 235 235 LEU LEU B . n 
B 1 238 SER 238 236 236 SER SER B . n 
B 1 239 ALA 239 237 237 ALA ALA B . n 
B 1 240 PRO 240 238 238 PRO PRO B . n 
B 1 241 THR 241 239 239 THR THR B . n 
B 1 242 LEU 242 240 240 LEU LEU B . n 
B 1 243 VAL 243 241 241 VAL VAL B . n 
B 1 244 PRO 244 242 242 PRO PRO B . n 
B 1 245 GLN 245 243 243 GLN GLN B . n 
B 1 246 GLU 246 244 244 GLU GLU B . n 
B 1 247 HIS 247 245 245 HIS HIS B . n 
B 1 248 TYR 248 246 246 TYR TYR B . n 
B 1 249 VAL 249 247 247 VAL VAL B . n 
B 1 250 ARG 250 248 248 ARG ARG B . n 
B 1 251 ILE 251 249 249 ILE ILE B . n 
B 1 252 THR 252 250 250 THR THR B . n 
B 1 253 GLY 253 251 251 GLY GLY B . n 
B 1 254 LEU 254 252 252 LEU LEU B . n 
B 1 255 TYR 255 253 253 TYR TYR B . n 
B 1 256 PRO 256 254 254 PRO PRO B . n 
B 1 257 THR 257 255 255 THR THR B . n 
B 1 258 LEU 258 256 256 LEU LEU B . n 
B 1 259 ASN 259 257 257 ASN ASN B . n 
B 1 260 ILE 260 258 258 ILE ILE B . n 
B 1 261 SER 261 259 259 SER SER B . n 
B 1 262 ASP 262 260 260 ASP ASP B . n 
B 1 263 GLU 263 261 261 GLU GLU B . n 
B 1 264 PHE 264 262 262 PHE PHE B . n 
B 1 265 SER 265 263 263 SER SER B . n 
B 1 266 SER 266 264 264 SER SER B . n 
B 1 267 ASN 267 265 265 ASN ASN B . n 
B 1 268 VAL 268 266 266 VAL VAL B . n 
B 1 269 ALA 269 267 267 ALA ALA B . n 
B 1 270 ASN 270 268 268 ASN ASN B . n 
B 1 271 TYR 271 269 269 TYR TYR B . n 
B 1 272 GLN 272 270 270 GLN GLN B . n 
B 1 273 LYS 273 271 271 LYS LYS B . n 
B 1 274 VAL 274 272 272 VAL VAL B . n 
B 1 275 GLY 275 273 273 GLY GLY B . n 
B 1 276 MET 276 274 274 MET MET B . n 
B 1 277 GLN 277 275 275 GLN GLN B . n 
B 1 278 LYS 278 276 276 LYS LYS B . n 
B 1 279 TYR 279 277 277 TYR TYR B . n 
B 1 280 SER 280 278 278 SER SER B . n 
B 1 281 THR 281 279 279 THR THR B . n 
B 1 282 LEU 282 280 280 LEU LEU B . n 
B 1 283 GLN 283 281 281 GLN GLN B . n 
B 1 284 GLY 284 282 282 GLY GLY B . n 
B 1 285 PRO 285 283 283 PRO PRO B . n 
B 1 286 PRO 286 284 284 PRO PRO B . n 
B 1 287 GLY 287 285 285 GLY GLY B . n 
B 1 288 THR 288 286 286 THR THR B . n 
B 1 289 GLY 289 287 287 GLY GLY B . n 
B 1 290 LYS 290 288 288 LYS LYS B . n 
B 1 291 SER 291 289 289 SER SER B . n 
B 1 292 HIS 292 290 290 HIS HIS B . n 
B 1 293 PHE 293 291 291 PHE PHE B . n 
B 1 294 ALA 294 292 292 ALA ALA B . n 
B 1 295 ILE 295 293 293 ILE ILE B . n 
B 1 296 GLY 296 294 294 GLY GLY B . n 
B 1 297 LEU 297 295 295 LEU LEU B . n 
B 1 298 ALA 298 296 296 ALA ALA B . n 
B 1 299 LEU 299 297 297 LEU LEU B . n 
B 1 300 TYR 300 298 298 TYR TYR B . n 
B 1 301 TYR 301 299 299 TYR TYR B . n 
B 1 302 PRO 302 300 300 PRO PRO B . n 
B 1 303 SER 303 301 301 SER SER B . n 
B 1 304 ALA 304 302 302 ALA ALA B . n 
B 1 305 ARG 305 303 303 ARG ARG B . n 
B 1 306 ILE 306 304 304 ILE ILE B . n 
B 1 307 VAL 307 305 305 VAL VAL B . n 
B 1 308 TYR 308 306 306 TYR TYR B . n 
B 1 309 THR 309 307 307 THR THR B . n 
B 1 310 ALA 310 308 308 ALA ALA B . n 
B 1 311 CYS 311 309 309 CYS CYS B . n 
B 1 312 SER 312 310 310 SER SER B . n 
B 1 313 HIS 313 311 311 HIS HIS B . n 
B 1 314 ALA 314 312 312 ALA ALA B . n 
B 1 315 ALA 315 313 313 ALA ALA B . n 
B 1 316 VAL 316 314 314 VAL VAL B . n 
B 1 317 ASP 317 315 315 ASP ASP B . n 
B 1 318 ALA 318 316 316 ALA ALA B . n 
B 1 319 LEU 319 317 317 LEU LEU B . n 
B 1 320 CYS 320 318 318 CYS CYS B . n 
B 1 321 GLU 321 319 319 GLU GLU B . n 
B 1 322 LYS 322 320 320 LYS LYS B . n 
B 1 323 ALA 323 321 321 ALA ALA B . n 
B 1 324 LEU 324 322 322 LEU LEU B . n 
B 1 325 LYS 325 323 323 LYS LYS B . n 
B 1 326 TYR 326 324 324 TYR TYR B . n 
B 1 327 LEU 327 325 325 LEU LEU B . n 
B 1 328 PRO 328 326 326 PRO PRO B . n 
B 1 329 ILE 329 327 327 ILE ILE B . n 
B 1 330 ASP 330 328 328 ASP ASP B . n 
B 1 331 LYS 331 329 329 LYS LYS B . n 
B 1 332 CYS 332 330 330 CYS CYS B . n 
B 1 333 SER 333 331 331 SER SER B . n 
B 1 334 ARG 334 332 332 ARG ARG B . n 
B 1 335 ILE 335 333 333 ILE ILE B . n 
B 1 336 ILE 336 334 334 ILE ILE B . n 
B 1 337 PRO 337 335 335 PRO PRO B . n 
B 1 338 ALA 338 336 336 ALA ALA B . n 
B 1 339 ARG 339 337 ?   ?   ?   B . n 
B 1 340 ALA 340 338 ?   ?   ?   B . n 
B 1 341 ARG 341 339 ?   ?   ?   B . n 
B 1 342 VAL 342 340 340 VAL VAL B . n 
B 1 343 GLU 343 341 341 GLU GLU B . n 
B 1 344 CYS 344 342 342 CYS CYS B . n 
B 1 345 PHE 345 343 343 PHE PHE B . n 
B 1 346 ASP 346 344 344 ASP ASP B . n 
B 1 347 LYS 347 345 345 LYS LYS B . n 
B 1 348 PHE 348 346 346 PHE PHE B . n 
B 1 349 LYS 349 347 347 LYS LYS B . n 
B 1 350 VAL 350 348 348 VAL VAL B . n 
B 1 351 ASN 351 349 349 ASN ASN B . n 
B 1 352 SER 352 350 350 SER SER B . n 
B 1 353 THR 353 351 351 THR THR B . n 
B 1 354 LEU 354 352 352 LEU LEU B . n 
B 1 355 GLU 355 353 353 GLU GLU B . n 
B 1 356 GLN 356 354 354 GLN GLN B . n 
B 1 357 TYR 357 355 355 TYR TYR B . n 
B 1 358 VAL 358 356 356 VAL VAL B . n 
B 1 359 PHE 359 357 357 PHE PHE B . n 
B 1 360 CYS 360 358 358 CYS CYS B . n 
B 1 361 THR 361 359 359 THR THR B . n 
B 1 362 VAL 362 360 360 VAL VAL B . n 
B 1 363 ASN 363 361 361 ASN ASN B . n 
B 1 364 ALA 364 362 362 ALA ALA B . n 
B 1 365 LEU 365 363 363 LEU LEU B . n 
B 1 366 PRO 366 364 364 PRO PRO B . n 
B 1 367 GLU 367 365 365 GLU GLU B . n 
B 1 368 THR 368 366 366 THR THR B . n 
B 1 369 THR 369 367 367 THR THR B . n 
B 1 370 ALA 370 368 368 ALA ALA B . n 
B 1 371 ASP 371 369 369 ASP ASP B . n 
B 1 372 ILE 372 370 370 ILE ILE B . n 
B 1 373 VAL 373 371 371 VAL VAL B . n 
B 1 374 VAL 374 372 372 VAL VAL B . n 
B 1 375 PHE 375 373 373 PHE PHE B . n 
B 1 376 ASP 376 374 374 ASP ASP B . n 
B 1 377 GLU 377 375 375 GLU GLU B . n 
B 1 378 ILE 378 376 376 ILE ILE B . n 
B 1 379 SER 379 377 377 SER SER B . n 
B 1 380 MET 380 378 378 MET MET B . n 
B 1 381 ALA 381 379 379 ALA ALA B . n 
B 1 382 THR 382 380 380 THR THR B . n 
B 1 383 ASN 383 381 381 ASN ASN B . n 
B 1 384 TYR 384 382 382 TYR TYR B . n 
B 1 385 ASP 385 383 383 ASP ASP B . n 
B 1 386 LEU 386 384 384 LEU LEU B . n 
B 1 387 SER 387 385 385 SER SER B . n 
B 1 388 VAL 388 386 386 VAL VAL B . n 
B 1 389 VAL 389 387 387 VAL VAL B . n 
B 1 390 ASN 390 388 388 ASN ASN B . n 
B 1 391 ALA 391 389 389 ALA ALA B . n 
B 1 392 ARG 392 390 390 ARG ARG B . n 
B 1 393 LEU 393 391 391 LEU LEU B . n 
B 1 394 ARG 394 392 392 ARG ARG B . n 
B 1 395 ALA 395 393 393 ALA ALA B . n 
B 1 396 LYS 396 394 394 LYS LYS B . n 
B 1 397 HIS 397 395 395 HIS HIS B . n 
B 1 398 TYR 398 396 396 TYR TYR B . n 
B 1 399 VAL 399 397 397 VAL VAL B . n 
B 1 400 TYR 400 398 398 TYR TYR B . n 
B 1 401 ILE 401 399 399 ILE ILE B . n 
B 1 402 GLY 402 400 400 GLY GLY B . n 
B 1 403 ASP 403 401 401 ASP ASP B . n 
B 1 404 PRO 404 402 402 PRO PRO B . n 
B 1 405 ALA 405 403 403 ALA ALA B . n 
B 1 406 GLN 406 404 404 GLN GLN B . n 
B 1 407 LEU 407 405 405 LEU LEU B . n 
B 1 408 PRO 408 406 406 PRO PRO B . n 
B 1 409 ALA 409 407 407 ALA ALA B . n 
B 1 410 PRO 410 408 408 PRO PRO B . n 
B 1 411 ARG 411 409 409 ARG ARG B . n 
B 1 412 THR 412 410 410 THR THR B . n 
B 1 413 LEU 413 411 411 LEU LEU B . n 
B 1 414 LEU 414 412 412 LEU LEU B . n 
B 1 415 THR 415 413 413 THR THR B . n 
B 1 416 LYS 416 414 414 LYS LYS B . n 
B 1 417 GLY 417 415 415 GLY GLY B . n 
B 1 418 THR 418 416 416 THR THR B . n 
B 1 419 LEU 419 417 417 LEU LEU B . n 
B 1 420 GLU 420 418 418 GLU GLU B . n 
B 1 421 PRO 421 419 419 PRO PRO B . n 
B 1 422 GLU 422 420 420 GLU GLU B . n 
B 1 423 TYR 423 421 421 TYR TYR B . n 
B 1 424 PHE 424 422 422 PHE PHE B . n 
B 1 425 ASN 425 423 423 ASN ASN B . n 
B 1 426 SER 426 424 424 SER SER B . n 
B 1 427 VAL 427 425 425 VAL VAL B . n 
B 1 428 CYS 428 426 426 CYS CYS B . n 
B 1 429 ARG 429 427 427 ARG ARG B . n 
B 1 430 LEU 430 428 428 LEU LEU B . n 
B 1 431 MET 431 429 429 MET MET B . n 
B 1 432 LYS 432 430 430 LYS LYS B . n 
B 1 433 THR 433 431 431 THR THR B . n 
B 1 434 ILE 434 432 432 ILE ILE B . n 
B 1 435 GLY 435 433 433 GLY GLY B . n 
B 1 436 PRO 436 434 434 PRO PRO B . n 
B 1 437 ASP 437 435 435 ASP ASP B . n 
B 1 438 MET 438 436 436 MET MET B . n 
B 1 439 PHE 439 437 437 PHE PHE B . n 
B 1 440 LEU 440 438 438 LEU LEU B . n 
B 1 441 GLY 441 439 439 GLY GLY B . n 
B 1 442 THR 442 440 440 THR THR B . n 
B 1 443 CYS 443 441 441 CYS CYS B . n 
B 1 444 ARG 444 442 442 ARG ARG B . n 
B 1 445 ARG 445 443 443 ARG ARG B . n 
B 1 446 CYS 446 444 444 CYS CYS B . n 
B 1 447 PRO 447 445 445 PRO PRO B . n 
B 1 448 ALA 448 446 446 ALA ALA B . n 
B 1 449 GLU 449 447 447 GLU GLU B . n 
B 1 450 ILE 450 448 448 ILE ILE B . n 
B 1 451 VAL 451 449 449 VAL VAL B . n 
B 1 452 ASP 452 450 450 ASP ASP B . n 
B 1 453 THR 453 451 451 THR THR B . n 
B 1 454 VAL 454 452 452 VAL VAL B . n 
B 1 455 SER 455 453 453 SER SER B . n 
B 1 456 ALA 456 454 454 ALA ALA B . n 
B 1 457 LEU 457 455 455 LEU LEU B . n 
B 1 458 VAL 458 456 456 VAL VAL B . n 
B 1 459 TYR 459 457 457 TYR TYR B . n 
B 1 460 ASP 460 458 458 ASP ASP B . n 
B 1 461 ASN 461 459 459 ASN ASN B . n 
B 1 462 LYS 462 460 460 LYS LYS B . n 
B 1 463 LEU 463 461 461 LEU LEU B . n 
B 1 464 LYS 464 462 462 LYS LYS B . n 
B 1 465 ALA 465 463 463 ALA ALA B . n 
B 1 466 HIS 466 464 464 HIS HIS B . n 
B 1 467 LYS 467 465 465 LYS LYS B . n 
B 1 468 ASP 468 466 466 ASP ASP B . n 
B 1 469 LYS 469 467 467 LYS LYS B . n 
B 1 470 SER 470 468 468 SER SER B . n 
B 1 471 ALA 471 469 469 ALA ALA B . n 
B 1 472 GLN 472 470 470 GLN GLN B . n 
B 1 473 CYS 473 471 471 CYS CYS B . n 
B 1 474 PHE 474 472 472 PHE PHE B . n 
B 1 475 LYS 475 473 473 LYS LYS B . n 
B 1 476 MET 476 474 474 MET MET B . n 
B 1 477 PHE 477 475 475 PHE PHE B . n 
B 1 478 TYR 478 476 476 TYR TYR B . n 
B 1 479 LYS 479 477 477 LYS LYS B . n 
B 1 480 GLY 480 478 478 GLY GLY B . n 
B 1 481 VAL 481 479 479 VAL VAL B . n 
B 1 482 ILE 482 480 480 ILE ILE B . n 
B 1 483 THR 483 481 481 THR THR B . n 
B 1 484 HIS 484 482 482 HIS HIS B . n 
B 1 485 ASP 485 483 483 ASP ASP B . n 
B 1 486 VAL 486 484 484 VAL VAL B . n 
B 1 487 SER 487 485 485 SER SER B . n 
B 1 488 SER 488 486 486 SER SER B . n 
B 1 489 ALA 489 487 487 ALA ALA B . n 
B 1 490 ILE 490 488 488 ILE ILE B . n 
B 1 491 ASN 491 489 489 ASN ASN B . n 
B 1 492 ARG 492 490 490 ARG ARG B . n 
B 1 493 PRO 493 491 491 PRO PRO B . n 
B 1 494 GLN 494 492 492 GLN GLN B . n 
B 1 495 ILE 495 493 493 ILE ILE B . n 
B 1 496 GLY 496 494 494 GLY GLY B . n 
B 1 497 VAL 497 495 495 VAL VAL B . n 
B 1 498 VAL 498 496 496 VAL VAL B . n 
B 1 499 ARG 499 497 497 ARG ARG B . n 
B 1 500 GLU 500 498 498 GLU GLU B . n 
B 1 501 PHE 501 499 499 PHE PHE B . n 
B 1 502 LEU 502 500 500 LEU LEU B . n 
B 1 503 THR 503 501 501 THR THR B . n 
B 1 504 ARG 504 502 502 ARG ARG B . n 
B 1 505 ASN 505 503 503 ASN ASN B . n 
B 1 506 PRO 506 504 504 PRO PRO B . n 
B 1 507 ALA 507 505 505 ALA ALA B . n 
B 1 508 TRP 508 506 506 TRP TRP B . n 
B 1 509 ARG 509 507 507 ARG ARG B . n 
B 1 510 LYS 510 508 508 LYS LYS B . n 
B 1 511 ALA 511 509 509 ALA ALA B . n 
B 1 512 VAL 512 510 510 VAL VAL B . n 
B 1 513 PHE 513 511 511 PHE PHE B . n 
B 1 514 ILE 514 512 512 ILE ILE B . n 
B 1 515 SER 515 513 513 SER SER B . n 
B 1 516 PRO 516 514 514 PRO PRO B . n 
B 1 517 TYR 517 515 515 TYR TYR B . n 
B 1 518 ASN 518 516 516 ASN ASN B . n 
B 1 519 SER 519 517 517 SER SER B . n 
B 1 520 GLN 520 518 518 GLN GLN B . n 
B 1 521 ASN 521 519 519 ASN ASN B . n 
B 1 522 ALA 522 520 520 ALA ALA B . n 
B 1 523 VAL 523 521 521 VAL VAL B . n 
B 1 524 ALA 524 522 522 ALA ALA B . n 
B 1 525 SER 525 523 523 SER SER B . n 
B 1 526 LYS 526 524 524 LYS LYS B . n 
B 1 527 ILE 527 525 525 ILE ILE B . n 
B 1 528 LEU 528 526 526 LEU LEU B . n 
B 1 529 GLY 529 527 527 GLY GLY B . n 
B 1 530 LEU 530 528 528 LEU LEU B . n 
B 1 531 PRO 531 529 529 PRO PRO B . n 
B 1 532 THR 532 530 530 THR THR B . n 
B 1 533 GLN 533 531 531 GLN GLN B . n 
B 1 534 THR 534 532 532 THR THR B . n 
B 1 535 VAL 535 533 533 VAL VAL B . n 
B 1 536 ASP 536 534 534 ASP ASP B . n 
B 1 537 SER 537 535 535 SER SER B . n 
B 1 538 SER 538 536 536 SER SER B . n 
B 1 539 GLN 539 537 537 GLN GLN B . n 
B 1 540 GLY 540 538 538 GLY GLY B . n 
B 1 541 SER 541 539 539 SER SER B . n 
B 1 542 GLU 542 540 540 GLU GLU B . n 
B 1 543 TYR 543 541 541 TYR TYR B . n 
B 1 544 ASP 544 542 542 ASP ASP B . n 
B 1 545 TYR 545 543 543 TYR TYR B . n 
B 1 546 VAL 546 544 544 VAL VAL B . n 
B 1 547 ILE 547 545 545 ILE ILE B . n 
B 1 548 PHE 548 546 546 PHE PHE B . n 
B 1 549 THR 549 547 547 THR THR B . n 
B 1 550 GLN 550 548 548 GLN GLN B . n 
B 1 551 THR 551 549 549 THR THR B . n 
B 1 552 THR 552 550 550 THR THR B . n 
B 1 553 GLU 553 551 551 GLU GLU B . n 
B 1 554 THR 554 552 552 THR THR B . n 
B 1 555 ALA 555 553 553 ALA ALA B . n 
B 1 556 HIS 556 554 554 HIS HIS B . n 
B 1 557 SER 557 555 555 SER SER B . n 
B 1 558 CYS 558 556 556 CYS CYS B . n 
B 1 559 ASN 559 557 557 ASN ASN B . n 
B 1 560 VAL 560 558 558 VAL VAL B . n 
B 1 561 ASN 561 559 559 ASN ASN B . n 
B 1 562 ARG 562 560 560 ARG ARG B . n 
B 1 563 PHE 563 561 561 PHE PHE B . n 
B 1 564 ASN 564 562 562 ASN ASN B . n 
B 1 565 VAL 565 563 563 VAL VAL B . n 
B 1 566 ALA 566 564 564 ALA ALA B . n 
B 1 567 ILE 567 565 565 ILE ILE B . n 
B 1 568 THR 568 566 566 THR THR B . n 
B 1 569 ARG 569 567 567 ARG ARG B . n 
B 1 570 ALA 570 568 568 ALA ALA B . n 
B 1 571 LYS 571 569 569 LYS LYS B . n 
B 1 572 VAL 572 570 570 VAL VAL B . n 
B 1 573 GLY 573 571 571 GLY GLY B . n 
B 1 574 ILE 574 572 572 ILE ILE B . n 
B 1 575 LEU 575 573 573 LEU LEU B . n 
B 1 576 CYS 576 574 574 CYS CYS B . n 
B 1 577 ILE 577 575 575 ILE ILE B . n 
B 1 578 MET 578 576 576 MET MET B . n 
B 1 579 SER 579 577 577 SER SER B . n 
B 1 580 ASP 580 578 578 ASP ASP B . n 
B 1 581 ARG 581 579 579 ARG ARG B . n 
B 1 582 ASP 582 580 580 ASP ASP B . n 
B 1 583 LEU 583 581 581 LEU LEU B . n 
B 1 584 TYR 584 582 582 TYR TYR B . n 
B 1 585 ASP 585 583 583 ASP ASP B . n 
B 1 586 LYS 586 584 584 LYS LYS B . n 
B 1 587 LEU 587 585 585 LEU LEU B . n 
B 1 588 GLN 588 586 586 GLN GLN B . n 
B 1 589 PHE 589 587 587 PHE PHE B . n 
B 1 590 THR 590 588 588 THR THR B . n 
B 1 591 SER 591 589 589 SER SER B . n 
B 1 592 LEU 592 590 590 LEU LEU B . n 
B 1 593 GLU 593 591 591 GLU GLU B . n 
B 1 594 ILE 594 592 592 ILE ILE B . n 
B 1 595 PRO 595 593 593 PRO PRO B . n 
B 1 596 ARG 596 594 ?   ?   ?   B . n 
B 1 597 ARG 597 595 ?   ?   ?   B . n 
B 1 598 ASN 598 596 ?   ?   ?   B . n 
B 1 599 VAL 599 597 ?   ?   ?   B . n 
B 1 600 ALA 600 598 ?   ?   ?   B . n 
B 1 601 THR 601 599 ?   ?   ?   B . n 
B 1 602 LEU 602 600 ?   ?   ?   B . n 
B 1 603 GLN 603 601 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        MYC 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   MYC 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 ZN  1   701 701 ZN  ZN  A . 
D 2 ZN  1   702 702 ZN  ZN  A . 
E 2 ZN  1   703 703 ZN  ZN  A . 
F 3 PO4 1   704 704 PO4 PO4 A . 
G 3 PO4 1   705 705 PO4 PO4 A . 
H 4 MPO 1   706 706 MPO MPO A . 
I 2 ZN  1   701 701 ZN  ZN  B . 
J 2 ZN  1   702 702 ZN  ZN  B . 
K 2 ZN  1   703 703 ZN  ZN  B . 
L 3 PO4 1   704 704 PO4 PO4 B . 
M 3 PO4 1   705 705 PO4 PO4 B . 
N 4 MPO 1   706 706 MPO MPO B . 
O 5 MYC 1   707 707 MYC MYC B . 
P 6 HOH 1   801 814 HOH HOH A . 
P 6 HOH 2   802 878 HOH HOH A . 
P 6 HOH 3   803 872 HOH HOH A . 
P 6 HOH 4   804 866 HOH HOH A . 
P 6 HOH 5   805 802 HOH HOH A . 
P 6 HOH 6   806 882 HOH HOH A . 
P 6 HOH 7   807 868 HOH HOH A . 
P 6 HOH 8   808 812 HOH HOH A . 
P 6 HOH 9   809 879 HOH HOH A . 
P 6 HOH 10  810 880 HOH HOH A . 
P 6 HOH 11  811 855 HOH HOH A . 
P 6 HOH 12  812 803 HOH HOH A . 
P 6 HOH 13  813 820 HOH HOH A . 
P 6 HOH 14  814 810 HOH HOH A . 
P 6 HOH 15  815 881 HOH HOH A . 
P 6 HOH 16  816 845 HOH HOH A . 
P 6 HOH 17  817 813 HOH HOH A . 
P 6 HOH 18  818 822 HOH HOH A . 
P 6 HOH 19  819 864 HOH HOH A . 
P 6 HOH 20  820 838 HOH HOH A . 
P 6 HOH 21  821 853 HOH HOH A . 
P 6 HOH 22  822 808 HOH HOH A . 
P 6 HOH 23  823 857 HOH HOH A . 
P 6 HOH 24  824 835 HOH HOH A . 
P 6 HOH 25  825 843 HOH HOH A . 
P 6 HOH 26  826 856 HOH HOH A . 
P 6 HOH 27  827 828 HOH HOH A . 
P 6 HOH 28  828 805 HOH HOH A . 
P 6 HOH 29  829 865 HOH HOH A . 
P 6 HOH 30  830 831 HOH HOH A . 
P 6 HOH 31  831 877 HOH HOH A . 
P 6 HOH 32  832 817 HOH HOH A . 
P 6 HOH 33  833 840 HOH HOH A . 
P 6 HOH 34  834 871 HOH HOH A . 
P 6 HOH 35  835 834 HOH HOH A . 
P 6 HOH 36  836 806 HOH HOH A . 
P 6 HOH 37  837 848 HOH HOH A . 
P 6 HOH 38  838 862 HOH HOH A . 
P 6 HOH 39  839 839 HOH HOH A . 
P 6 HOH 40  840 832 HOH HOH A . 
P 6 HOH 41  841 811 HOH HOH A . 
P 6 HOH 42  842 818 HOH HOH A . 
P 6 HOH 43  843 821 HOH HOH A . 
P 6 HOH 44  844 844 HOH HOH A . 
P 6 HOH 45  845 851 HOH HOH A . 
P 6 HOH 46  846 825 HOH HOH A . 
P 6 HOH 47  847 842 HOH HOH A . 
P 6 HOH 48  848 804 HOH HOH A . 
P 6 HOH 49  849 833 HOH HOH A . 
P 6 HOH 50  850 827 HOH HOH A . 
P 6 HOH 51  851 815 HOH HOH A . 
P 6 HOH 52  852 863 HOH HOH A . 
P 6 HOH 53  853 876 HOH HOH A . 
P 6 HOH 54  854 824 HOH HOH A . 
P 6 HOH 55  855 823 HOH HOH A . 
P 6 HOH 56  856 869 HOH HOH A . 
P 6 HOH 57  857 854 HOH HOH A . 
P 6 HOH 58  858 847 HOH HOH A . 
P 6 HOH 59  859 837 HOH HOH A . 
P 6 HOH 60  860 807 HOH HOH A . 
P 6 HOH 61  861 858 HOH HOH A . 
P 6 HOH 62  862 829 HOH HOH A . 
P 6 HOH 63  863 836 HOH HOH A . 
P 6 HOH 64  864 849 HOH HOH A . 
P 6 HOH 65  865 867 HOH HOH A . 
P 6 HOH 66  866 860 HOH HOH A . 
P 6 HOH 67  867 874 HOH HOH A . 
P 6 HOH 68  868 870 HOH HOH A . 
P 6 HOH 69  869 859 HOH HOH A . 
P 6 HOH 70  870 875 HOH HOH A . 
P 6 HOH 71  871 809 HOH HOH A . 
P 6 HOH 72  872 830 HOH HOH A . 
P 6 HOH 73  873 852 HOH HOH A . 
P 6 HOH 74  874 819 HOH HOH A . 
P 6 HOH 75  875 873 HOH HOH A . 
P 6 HOH 76  876 861 HOH HOH A . 
P 6 HOH 77  877 846 HOH HOH A . 
P 6 HOH 78  878 841 HOH HOH A . 
P 6 HOH 79  879 816 HOH HOH A . 
P 6 HOH 80  880 826 HOH HOH A . 
P 6 HOH 81  881 801 HOH HOH A . 
Q 6 HOH 1   801 941 HOH HOH B . 
Q 6 HOH 2   802 838 HOH HOH B . 
Q 6 HOH 3   803 906 HOH HOH B . 
Q 6 HOH 4   804 837 HOH HOH B . 
Q 6 HOH 5   805 919 HOH HOH B . 
Q 6 HOH 6   806 868 HOH HOH B . 
Q 6 HOH 7   807 898 HOH HOH B . 
Q 6 HOH 8   808 836 HOH HOH B . 
Q 6 HOH 9   809 940 HOH HOH B . 
Q 6 HOH 10  810 944 HOH HOH B . 
Q 6 HOH 11  811 839 HOH HOH B . 
Q 6 HOH 12  812 932 HOH HOH B . 
Q 6 HOH 13  813 908 HOH HOH B . 
Q 6 HOH 14  814 863 HOH HOH B . 
Q 6 HOH 15  815 880 HOH HOH B . 
Q 6 HOH 16  816 943 HOH HOH B . 
Q 6 HOH 17  817 865 HOH HOH B . 
Q 6 HOH 18  818 811 HOH HOH B . 
Q 6 HOH 19  819 927 HOH HOH B . 
Q 6 HOH 20  820 914 HOH HOH B . 
Q 6 HOH 21  821 832 HOH HOH B . 
Q 6 HOH 22  822 870 HOH HOH B . 
Q 6 HOH 23  823 873 HOH HOH B . 
Q 6 HOH 24  824 900 HOH HOH B . 
Q 6 HOH 25  825 840 HOH HOH B . 
Q 6 HOH 26  826 835 HOH HOH B . 
Q 6 HOH 27  827 895 HOH HOH B . 
Q 6 HOH 28  828 924 HOH HOH B . 
Q 6 HOH 29  829 826 HOH HOH B . 
Q 6 HOH 30  830 888 HOH HOH B . 
Q 6 HOH 31  831 872 HOH HOH B . 
Q 6 HOH 32  832 852 HOH HOH B . 
Q 6 HOH 33  833 813 HOH HOH B . 
Q 6 HOH 34  834 816 HOH HOH B . 
Q 6 HOH 35  835 834 HOH HOH B . 
Q 6 HOH 36  836 847 HOH HOH B . 
Q 6 HOH 37  837 861 HOH HOH B . 
Q 6 HOH 38  838 810 HOH HOH B . 
Q 6 HOH 39  839 857 HOH HOH B . 
Q 6 HOH 40  840 945 HOH HOH B . 
Q 6 HOH 41  841 833 HOH HOH B . 
Q 6 HOH 42  842 917 HOH HOH B . 
Q 6 HOH 43  843 909 HOH HOH B . 
Q 6 HOH 44  844 825 HOH HOH B . 
Q 6 HOH 45  845 851 HOH HOH B . 
Q 6 HOH 46  846 807 HOH HOH B . 
Q 6 HOH 47  847 842 HOH HOH B . 
Q 6 HOH 48  848 814 HOH HOH B . 
Q 6 HOH 49  849 818 HOH HOH B . 
Q 6 HOH 50  850 946 HOH HOH B . 
Q 6 HOH 51  851 805 HOH HOH B . 
Q 6 HOH 52  852 843 HOH HOH B . 
Q 6 HOH 53  853 920 HOH HOH B . 
Q 6 HOH 54  854 854 HOH HOH B . 
Q 6 HOH 55  855 812 HOH HOH B . 
Q 6 HOH 56  856 911 HOH HOH B . 
Q 6 HOH 57  857 803 HOH HOH B . 
Q 6 HOH 58  858 929 HOH HOH B . 
Q 6 HOH 59  859 849 HOH HOH B . 
Q 6 HOH 60  860 830 HOH HOH B . 
Q 6 HOH 61  861 821 HOH HOH B . 
Q 6 HOH 62  862 916 HOH HOH B . 
Q 6 HOH 63  863 858 HOH HOH B . 
Q 6 HOH 64  864 845 HOH HOH B . 
Q 6 HOH 65  865 819 HOH HOH B . 
Q 6 HOH 66  866 820 HOH HOH B . 
Q 6 HOH 67  867 902 HOH HOH B . 
Q 6 HOH 68  868 815 HOH HOH B . 
Q 6 HOH 69  869 871 HOH HOH B . 
Q 6 HOH 70  870 822 HOH HOH B . 
Q 6 HOH 71  871 926 HOH HOH B . 
Q 6 HOH 72  872 844 HOH HOH B . 
Q 6 HOH 73  873 846 HOH HOH B . 
Q 6 HOH 74  874 912 HOH HOH B . 
Q 6 HOH 75  875 897 HOH HOH B . 
Q 6 HOH 76  876 885 HOH HOH B . 
Q 6 HOH 77  877 893 HOH HOH B . 
Q 6 HOH 78  878 850 HOH HOH B . 
Q 6 HOH 79  879 894 HOH HOH B . 
Q 6 HOH 80  880 931 HOH HOH B . 
Q 6 HOH 81  881 841 HOH HOH B . 
Q 6 HOH 82  882 823 HOH HOH B . 
Q 6 HOH 83  883 817 HOH HOH B . 
Q 6 HOH 84  884 882 HOH HOH B . 
Q 6 HOH 85  885 886 HOH HOH B . 
Q 6 HOH 86  886 947 HOH HOH B . 
Q 6 HOH 87  887 862 HOH HOH B . 
Q 6 HOH 88  888 856 HOH HOH B . 
Q 6 HOH 89  889 896 HOH HOH B . 
Q 6 HOH 90  890 925 HOH HOH B . 
Q 6 HOH 91  891 913 HOH HOH B . 
Q 6 HOH 92  892 935 HOH HOH B . 
Q 6 HOH 93  893 808 HOH HOH B . 
Q 6 HOH 94  894 892 HOH HOH B . 
Q 6 HOH 95  895 901 HOH HOH B . 
Q 6 HOH 96  896 855 HOH HOH B . 
Q 6 HOH 97  897 918 HOH HOH B . 
Q 6 HOH 98  898 904 HOH HOH B . 
Q 6 HOH 99  899 869 HOH HOH B . 
Q 6 HOH 100 900 848 HOH HOH B . 
Q 6 HOH 101 901 948 HOH HOH B . 
Q 6 HOH 102 902 903 HOH HOH B . 
Q 6 HOH 103 903 881 HOH HOH B . 
Q 6 HOH 104 904 824 HOH HOH B . 
Q 6 HOH 105 905 883 HOH HOH B . 
Q 6 HOH 106 906 831 HOH HOH B . 
Q 6 HOH 107 907 933 HOH HOH B . 
Q 6 HOH 108 908 875 HOH HOH B . 
Q 6 HOH 109 909 874 HOH HOH B . 
Q 6 HOH 110 910 899 HOH HOH B . 
Q 6 HOH 111 911 828 HOH HOH B . 
Q 6 HOH 112 912 915 HOH HOH B . 
Q 6 HOH 113 913 922 HOH HOH B . 
Q 6 HOH 114 914 806 HOH HOH B . 
Q 6 HOH 115 915 907 HOH HOH B . 
Q 6 HOH 116 916 934 HOH HOH B . 
Q 6 HOH 117 917 876 HOH HOH B . 
Q 6 HOH 118 918 923 HOH HOH B . 
Q 6 HOH 119 919 809 HOH HOH B . 
Q 6 HOH 120 920 878 HOH HOH B . 
Q 6 HOH 121 921 939 HOH HOH B . 
Q 6 HOH 122 922 802 HOH HOH B . 
Q 6 HOH 123 923 889 HOH HOH B . 
Q 6 HOH 124 924 928 HOH HOH B . 
Q 6 HOH 125 925 938 HOH HOH B . 
Q 6 HOH 126 926 884 HOH HOH B . 
Q 6 HOH 127 927 853 HOH HOH B . 
Q 6 HOH 128 928 905 HOH HOH B . 
Q 6 HOH 129 929 879 HOH HOH B . 
Q 6 HOH 130 930 827 HOH HOH B . 
Q 6 HOH 131 931 936 HOH HOH B . 
Q 6 HOH 132 932 942 HOH HOH B . 
Q 6 HOH 133 933 921 HOH HOH B . 
Q 6 HOH 134 934 850 HOH HOH B . 
Q 6 HOH 135 935 859 HOH HOH B . 
Q 6 HOH 136 936 890 HOH HOH B . 
Q 6 HOH 137 937 867 HOH HOH B . 
Q 6 HOH 138 938 864 HOH HOH B . 
Q 6 HOH 139 939 937 HOH HOH B . 
Q 6 HOH 140 940 860 HOH HOH B . 
Q 6 HOH 141 941 804 HOH HOH B . 
Q 6 HOH 142 942 891 HOH HOH B . 
Q 6 HOH 143 943 887 HOH HOH B . 
Q 6 HOH 144 944 801 HOH HOH B . 
Q 6 HOH 145 945 866 HOH HOH B . 
Q 6 HOH 146 946 829 HOH HOH B . 
Q 6 HOH 147 947 930 HOH HOH B . 
Q 6 HOH 148 948 910 HOH HOH B . 
Q 6 HOH 149 949 877 HOH HOH 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 LYS 28  ? CG  ? A LYS 30  CG  
2   1 Y 1 A LYS 28  ? CD  ? A LYS 30  CD  
3   1 Y 1 A LYS 28  ? CE  ? A LYS 30  CE  
4   1 Y 1 A LYS 28  ? NZ  ? A LYS 30  NZ  
5   1 Y 1 A MET 68  ? CG  ? A MET 70  CG  
6   1 Y 1 A MET 68  ? SD  ? A MET 70  SD  
7   1 Y 1 A MET 68  ? CE  ? A MET 70  CE  
8   1 Y 1 A LYS 73  ? CG  ? A LYS 75  CG  
9   1 Y 1 A LYS 73  ? CD  ? A LYS 75  CD  
10  1 Y 1 A LYS 73  ? CE  ? A LYS 75  CE  
11  1 Y 1 A LYS 73  ? NZ  ? A LYS 75  NZ  
12  1 Y 1 A LYS 94  ? CG  ? A LYS 96  CG  
13  1 Y 1 A LYS 94  ? CD  ? A LYS 96  CD  
14  1 Y 1 A LYS 94  ? CE  ? A LYS 96  CE  
15  1 Y 1 A LYS 94  ? NZ  ? A LYS 96  NZ  
16  1 Y 1 A ARG 155 ? CG  ? A ARG 157 CG  
17  1 Y 1 A ARG 155 ? CD  ? A ARG 157 CD  
18  1 Y 1 A ARG 155 ? NE  ? A ARG 157 NE  
19  1 Y 1 A ARG 155 ? CZ  ? A ARG 157 CZ  
20  1 Y 1 A ARG 155 ? NH1 ? A ARG 157 NH1 
21  1 Y 1 A ARG 155 ? NH2 ? A ARG 157 NH2 
22  1 Y 1 A ARG 178 ? CG  ? A ARG 180 CG  
23  1 Y 1 A ARG 178 ? CD  ? A ARG 180 CD  
24  1 Y 1 A ARG 178 ? NE  ? A ARG 180 NE  
25  1 Y 1 A ARG 178 ? CZ  ? A ARG 180 CZ  
26  1 Y 1 A ARG 178 ? NH1 ? A ARG 180 NH1 
27  1 Y 1 A ARG 178 ? NH2 ? A ARG 180 NH2 
28  1 Y 1 A LYS 202 ? CG  ? A LYS 204 CG  
29  1 Y 1 A LYS 202 ? CD  ? A LYS 204 CD  
30  1 Y 1 A LYS 202 ? CE  ? A LYS 204 CE  
31  1 Y 1 A LYS 202 ? NZ  ? A LYS 204 NZ  
32  1 Y 1 A ARG 212 ? CG  ? A ARG 214 CG  
33  1 Y 1 A ARG 212 ? CD  ? A ARG 214 CD  
34  1 Y 1 A ARG 212 ? NE  ? A ARG 214 NE  
35  1 Y 1 A ARG 212 ? CZ  ? A ARG 214 CZ  
36  1 Y 1 A ARG 212 ? NH1 ? A ARG 214 NH1 
37  1 Y 1 A ARG 212 ? NH2 ? A ARG 214 NH2 
38  1 Y 1 A LYS 218 ? CG  ? A LYS 220 CG  
39  1 Y 1 A LYS 218 ? CD  ? A LYS 220 CD  
40  1 Y 1 A LYS 218 ? CE  ? A LYS 220 CE  
41  1 Y 1 A LYS 218 ? NZ  ? A LYS 220 NZ  
42  1 Y 1 A LEU 219 ? CG  ? A LEU 221 CG  
43  1 Y 1 A LEU 219 ? CD1 ? A LEU 221 CD1 
44  1 Y 1 A LEU 219 ? CD2 ? A LEU 221 CD2 
45  1 Y 1 A THR 228 ? OG1 ? A THR 230 OG1 
46  1 Y 1 A THR 228 ? CG2 ? A THR 230 CG2 
47  1 Y 1 A ARG 248 ? CG  ? A ARG 250 CG  
48  1 Y 1 A ARG 248 ? CD  ? A ARG 250 CD  
49  1 Y 1 A ARG 248 ? NE  ? A ARG 250 NE  
50  1 Y 1 A ARG 248 ? CZ  ? A ARG 250 CZ  
51  1 Y 1 A ARG 248 ? NH1 ? A ARG 250 NH1 
52  1 Y 1 A ARG 248 ? NH2 ? A ARG 250 NH2 
53  1 Y 1 A LYS 347 ? CG  ? A LYS 349 CG  
54  1 Y 1 A LYS 347 ? CD  ? A LYS 349 CD  
55  1 Y 1 A LYS 347 ? CE  ? A LYS 349 CE  
56  1 Y 1 A LYS 347 ? NZ  ? A LYS 349 NZ  
57  1 Y 1 B LYS 28  ? CG  ? B LYS 30  CG  
58  1 Y 1 B LYS 28  ? CD  ? B LYS 30  CD  
59  1 Y 1 B LYS 28  ? CE  ? B LYS 30  CE  
60  1 Y 1 B LYS 28  ? NZ  ? B LYS 30  NZ  
61  1 Y 1 B LYS 94  ? CG  ? B LYS 96  CG  
62  1 Y 1 B LYS 94  ? CD  ? B LYS 96  CD  
63  1 Y 1 B LYS 94  ? CE  ? B LYS 96  CE  
64  1 Y 1 B LYS 94  ? NZ  ? B LYS 96  NZ  
65  1 Y 1 B ASP 101 ? CG  ? B ASP 103 CG  
66  1 Y 1 B ASP 101 ? OD1 ? B ASP 103 OD1 
67  1 Y 1 B ASP 101 ? OD2 ? B ASP 103 OD2 
68  1 Y 1 B ASN 102 ? CG  ? B ASN 104 CG  
69  1 Y 1 B ASN 102 ? OD1 ? B ASN 104 OD1 
70  1 Y 1 B ASN 102 ? ND2 ? B ASN 104 ND2 
71  1 Y 1 B ARG 161 ? CG  ? B ARG 163 CG  
72  1 Y 1 B ARG 161 ? CD  ? B ARG 163 CD  
73  1 Y 1 B ARG 161 ? NE  ? B ARG 163 NE  
74  1 Y 1 B ARG 161 ? CZ  ? B ARG 163 CZ  
75  1 Y 1 B ARG 161 ? NH1 ? B ARG 163 NH1 
76  1 Y 1 B ARG 161 ? NH2 ? B ARG 163 NH2 
77  1 Y 1 B ARG 178 ? CG  ? B ARG 180 CG  
78  1 Y 1 B ARG 178 ? CD  ? B ARG 180 CD  
79  1 Y 1 B ARG 178 ? NE  ? B ARG 180 NE  
80  1 Y 1 B ARG 178 ? CZ  ? B ARG 180 CZ  
81  1 Y 1 B ARG 178 ? NH1 ? B ARG 180 NH1 
82  1 Y 1 B ARG 178 ? NH2 ? B ARG 180 NH2 
83  1 Y 1 B ARG 186 ? CG  ? B ARG 188 CG  
84  1 Y 1 B ARG 186 ? CD  ? B ARG 188 CD  
85  1 Y 1 B ARG 186 ? NE  ? B ARG 188 NE  
86  1 Y 1 B ARG 186 ? CZ  ? B ARG 188 CZ  
87  1 Y 1 B ARG 186 ? NH1 ? B ARG 188 NH1 
88  1 Y 1 B ARG 186 ? NH2 ? B ARG 188 NH2 
89  1 Y 1 B LYS 189 ? CG  ? B LYS 191 CG  
90  1 Y 1 B LYS 189 ? CD  ? B LYS 191 CD  
91  1 Y 1 B LYS 189 ? CE  ? B LYS 191 CE  
92  1 Y 1 B LYS 189 ? NZ  ? B LYS 191 NZ  
93  1 Y 1 B ARG 212 ? CG  ? B ARG 214 CG  
94  1 Y 1 B ARG 212 ? CD  ? B ARG 214 CD  
95  1 Y 1 B ARG 212 ? NE  ? B ARG 214 NE  
96  1 Y 1 B ARG 212 ? CZ  ? B ARG 214 CZ  
97  1 Y 1 B ARG 212 ? NH1 ? B ARG 214 NH1 
98  1 Y 1 B ARG 212 ? NH2 ? B ARG 214 NH2 
99  1 Y 1 B THR 214 ? OG1 ? B THR 216 OG1 
100 1 Y 1 B THR 214 ? CG2 ? B THR 216 CG2 
101 1 Y 1 B LYS 218 ? CG  ? B LYS 220 CG  
102 1 Y 1 B LYS 218 ? CD  ? B LYS 220 CD  
103 1 Y 1 B LYS 218 ? CE  ? B LYS 220 CE  
104 1 Y 1 B LYS 218 ? NZ  ? B LYS 220 NZ  
105 1 Y 1 B LYS 524 ? CG  ? B LYS 526 CG  
106 1 Y 1 B LYS 524 ? CD  ? B LYS 526 CD  
107 1 Y 1 B LYS 524 ? CE  ? B LYS 526 CE  
108 1 Y 1 B LYS 524 ? NZ  ? B LYS 526 NZ  
109 1 Y 1 B GLU 591 ? CG  ? B GLU 593 CG  
110 1 Y 1 B GLU 591 ? CD  ? B GLU 593 CD  
111 1 Y 1 B GLU 591 ? OE1 ? B GLU 593 OE1 
112 1 Y 1 B GLU 591 ? OE2 ? B GLU 593 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1-4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? 1.1.7       2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? 1.1.7       3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 5.8.0425    4 
# 
_cell.angle_alpha                  103.11 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   96.10 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  112.15 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9I1S 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     59.327 
_cell.length_a_esd                 ? 
_cell.length_b                     70.632 
_cell.length_b_esd                 ? 
_cell.length_c                     86.149 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         9I1S 
_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                   9I1S 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.37 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.09 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;16 % Ethylene Glycol, 8 % PEG 8000, 0.05 M Na HEPES, 0.05 M MOPS, 0.03 M Sodium nitrate, 0.03 M Sodium phosphate dibasic, 0.03 M Ammonium sulfate, 9 % MPD
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-06-12 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97625 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97625 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9I1S 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.088 
_reflns.d_resolution_low                               62.615 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     67228 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           91.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.077 
_reflns.pdbx_Rpim_I_all                                0.038 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.067 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.088 
_reflns_shell.d_res_low                                     2.124 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.4 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3108 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               2.6 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.812 
_reflns_shell.pdbx_Rpim_I_all                               0.490 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.809 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          85.2 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.642 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9I1S 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.09 
_refine.ls_d_res_low                             35.63 
_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                     67055 
_refine.ls_number_reflns_R_free                  3349 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    91.56 
_refine.ls_percent_reflns_R_free                 4.99 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2161 
_refine.ls_R_factor_R_free                       0.2412 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2148 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.97 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 30.04 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.33 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.09 
_refine_hist.d_res_low                        35.63 
_refine_hist.number_atoms_solvent             230 
_refine_hist.number_atoms_total               9217 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        8912 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         75 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.003  ? 9185  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.768  ? 12523 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.015 ? 3272  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.044  ? 1447  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.011  ? 1586  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.09 2.12 . . 145 2423 84.00 . . . . 0.3685 . . . . . . . . . . . 0.4148 
'X-RAY DIFFRACTION' 2.12 2.15 . . 111 2292 78.00 . . . . 0.3498 . . . . . . . . . . . 0.3541 
'X-RAY DIFFRACTION' 2.15 2.18 . . 119 2495 87.00 . . . . 0.3374 . . . . . . . . . . . 0.3626 
'X-RAY DIFFRACTION' 2.18 2.22 . . 139 2691 93.00 . . . . 0.3276 . . . . . . . . . . . 0.3596 
'X-RAY DIFFRACTION' 2.22 2.26 . . 150 2729 94.00 . . . . 0.3171 . . . . . . . . . . . 0.3418 
'X-RAY DIFFRACTION' 2.26 2.30 . . 123 2768 94.00 . . . . 0.2970 . . . . . . . . . . . 0.3466 
'X-RAY DIFFRACTION' 2.30 2.34 . . 126 2738 94.00 . . . . 0.2874 . . . . . . . . . . . 0.3148 
'X-RAY DIFFRACTION' 2.34 2.39 . . 138 2711 94.00 . . . . 0.2730 . . . . . . . . . . . 0.3077 
'X-RAY DIFFRACTION' 2.39 2.44 . . 156 2717 94.00 . . . . 0.2690 . . . . . . . . . . . 0.2949 
'X-RAY DIFFRACTION' 2.44 2.50 . . 122 2699 94.00 . . . . 0.2605 . . . . . . . . . . . 0.2907 
'X-RAY DIFFRACTION' 2.50 2.56 . . 132 2736 93.00 . . . . 0.2736 . . . . . . . . . . . 0.3115 
'X-RAY DIFFRACTION' 2.56 2.63 . . 155 2705 93.00 . . . . 0.2495 . . . . . . . . . . . 0.2851 
'X-RAY DIFFRACTION' 2.63 2.71 . . 130 2709 93.00 . . . . 0.2395 . . . . . . . . . . . 0.2770 
'X-RAY DIFFRACTION' 2.71 2.79 . . 145 2644 92.00 . . . . 0.2431 . . . . . . . . . . . 0.2760 
'X-RAY DIFFRACTION' 2.79 2.89 . . 148 2618 91.00 . . . . 0.2346 . . . . . . . . . . . 0.2825 
'X-RAY DIFFRACTION' 2.89 3.01 . . 149 2481 87.00 . . . . 0.2380 . . . . . . . . . . . 0.2967 
'X-RAY DIFFRACTION' 3.01 3.15 . . 123 2395 82.00 . . . . 0.2506 . . . . . . . . . . . 0.2769 
'X-RAY DIFFRACTION' 3.15 3.31 . . 158 2801 96.00 . . . . 0.2203 . . . . . . . . . . . 0.2373 
'X-RAY DIFFRACTION' 3.31 3.52 . . 141 2803 96.00 . . . . 0.2075 . . . . . . . . . . . 0.2728 
'X-RAY DIFFRACTION' 3.52 3.79 . . 139 2750 96.00 . . . . 0.1955 . . . . . . . . . . . 0.2100 
'X-RAY DIFFRACTION' 3.79 4.17 . . 152 2773 95.00 . . . . 0.1747 . . . . . . . . . . . 0.2053 
'X-RAY DIFFRACTION' 4.17 4.78 . . 144 2725 94.00 . . . . 0.1668 . . . . . . . . . . . 0.1758 
'X-RAY DIFFRACTION' 4.78 6.01 . . 169 2469 86.00 . . . . 0.1842 . . . . . . . . . . . 0.2021 
# 
_struct.entry_id                     9I1S 
_struct.title                        'Crystal structure of the SARS-CoV-2 helicase NSP13 in complex with myricetin' 
_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        9I1S 
_struct_keywords.text            'NSP13, Helicase, SARS-CoV-2, Hydrolase' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 3 ? 
H N N 4 ? 
I N N 2 ? 
J N N 2 ? 
K N N 2 ? 
L N N 3 ? 
M N N 3 ? 
N N N 4 ? 
O N N 5 ? 
P N N 6 ? 
Q N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VGACVLCNSQTSLRCGACIRRPFLCCKCCYDHVISTSHKLVLSVNPYVCNAPGCDVTDVTQLYLGGMSYYCKSHKPPISF
PLCANGQVFGLYKNTCVGSDNVTDFNAIATCDWTNAGDYILANTCTERLKLFAAETLKATEETFKLSYGIATVREVLSDR
ELHLSWEVGKPRPPLNRNYVFTGYRVTKNSKVQIGEYTFEKGDYGDAVVYRGTTTYKLNVGDYFVLTSHTVMPLSAPTLV
PQEHYVRITGLYPTLNISDEFSSNVANYQKVGMQKYSTLQGPPGTGKSHFAIGLALYYPSARIVYTACSHAAVDALCEKA
LKYLPIDKCSRIIPARARVECFDKFKVNSTLEQYVFCTVNALPETTADIVVFDEISMATNYDLSVVNARLRAKHYVYIGD
PAQLPAPRTLLTKGTLEPEYFNSVCRLMKTIGPDMFLGTCRRCPAEIVDTVSALVYDNKLKAHKDKSAQCFKMFYKGVIT
HDVSSAINRPQIGVVREFLTRNPAWRKAVFISPYNSQNAVASKILGLPTQTVDSSQGSEYDYVIFTQTTETAHSCNVNRF
NVAITRAKVGILCIMSDRDLYDKLQFTSLEIPRRNVATLQ
;
_struct_ref.pdbx_align_begin           5326 
# 
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 9I1S A 4 ? 603 ? P0DTD1 5326 ? 5925 ? 2 601 
2 1 9I1S B 4 ? 603 ? P0DTD1 5326 ? 5925 ? 2 601 
# 
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 9I1S SER A 1 ? UNP P0DTD1 ? ? 'expression tag' -1 1 
1 9I1S MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 0  2 
1 9I1S ALA A 3 ? UNP P0DTD1 ? ? 'expression tag' 1  3 
2 9I1S SER B 1 ? UNP P0DTD1 ? ? 'expression tag' -1 4 
2 9I1S MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 0  5 
2 9I1S ALA B 3 ? UNP P0DTD1 ? ? 'expression tag' 1  6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,H,P   
2 1 B,I,J,K,L,M,N,O,Q 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 CYS A 28  ? THR A 39  ? CYS A 26  THR A 37  1 ? 12 
HELX_P HELX_P2  AA2 ASP A 61  ? THR A 63  ? ASP A 59  THR A 61  5 ? 3  
HELX_P HELX_P3  AA3 THR A 106 ? CYS A 114 ? THR A 104 CYS A 112 1 ? 9  
HELX_P HELX_P4  AA4 ASN A 118 ? CYS A 128 ? ASN A 116 CYS A 126 1 ? 11 
HELX_P HELX_P5  AA5 THR A 129 ? LYS A 148 ? THR A 127 LYS A 146 1 ? 20 
HELX_P HELX_P6  AA6 SER A 261 ? SER A 266 ? SER A 259 SER A 264 5 ? 6  
HELX_P HELX_P7  AA7 ASN A 267 ? MET A 276 ? ASN A 265 MET A 274 1 ? 10 
HELX_P HELX_P8  AA8 GLY A 289 ? TYR A 301 ? GLY A 287 TYR A 299 1 ? 13 
HELX_P HELX_P9  AA9 SER A 312 ? LEU A 327 ? SER A 310 LEU A 325 1 ? 16 
HELX_P HELX_P10 AB1 ASN A 363 ? LEU A 365 ? ASN A 361 LEU A 363 5 ? 3  
HELX_P HELX_P11 AB2 GLU A 377 ? ALA A 381 ? GLU A 375 ALA A 379 5 ? 5  
HELX_P HELX_P12 AB3 THR A 382 ? ARG A 392 ? THR A 380 ARG A 390 1 ? 11 
HELX_P HELX_P13 AB4 GLU A 420 ? PHE A 424 ? GLU A 418 PHE A 422 5 ? 5  
HELX_P HELX_P14 AB5 ASN A 425 ? ILE A 434 ? ASN A 423 ILE A 432 1 ? 10 
HELX_P HELX_P15 AB6 PRO A 447 ? TYR A 459 ? PRO A 445 TYR A 457 1 ? 13 
HELX_P HELX_P16 AB7 ASN A 491 ? THR A 503 ? ASN A 489 THR A 501 1 ? 13 
HELX_P HELX_P17 AB8 ASN A 505 ? ARG A 509 ? ASN A 503 ARG A 507 5 ? 5  
HELX_P HELX_P18 AB9 TYR A 517 ? GLY A 529 ? TYR A 515 GLY A 527 1 ? 13 
HELX_P HELX_P19 AC1 VAL A 535 ? GLN A 539 ? VAL A 533 GLN A 537 1 ? 5  
HELX_P HELX_P20 AC2 THR A 554 ? ASN A 559 ? THR A 552 ASN A 557 1 ? 6  
HELX_P HELX_P21 AC3 ASN A 559 ? THR A 568 ? ASN A 557 THR A 566 1 ? 10 
HELX_P HELX_P22 AC4 ASP A 580 ? LEU A 587 ? ASP A 578 LEU A 585 1 ? 8  
HELX_P HELX_P23 AC5 CYS B 28  ? ILE B 37  ? CYS B 26  ILE B 35  1 ? 10 
HELX_P HELX_P24 AC6 ASP B 61  ? THR B 63  ? ASP B 59  THR B 61  5 ? 3  
HELX_P HELX_P25 AC7 SER B 76  ? LYS B 78  ? SER B 74  LYS B 76  5 ? 3  
HELX_P HELX_P26 AC8 VAL B 105 ? CYS B 114 ? VAL B 103 CYS B 112 1 ? 10 
HELX_P HELX_P27 AC9 ASN B 118 ? ALA B 125 ? ASN B 116 ALA B 123 1 ? 8  
HELX_P HELX_P28 AD1 THR B 129 ? SER B 150 ? THR B 127 SER B 148 1 ? 22 
HELX_P HELX_P29 AD2 PHE B 264 ? SER B 266 ? PHE B 262 SER B 264 5 ? 3  
HELX_P HELX_P30 AD3 ASN B 267 ? MET B 276 ? ASN B 265 MET B 274 1 ? 10 
HELX_P HELX_P31 AD4 GLY B 289 ? TYR B 301 ? GLY B 287 TYR B 299 1 ? 13 
HELX_P HELX_P32 AD5 SER B 312 ? LYS B 325 ? SER B 310 LYS B 323 1 ? 14 
HELX_P HELX_P33 AD6 PRO B 328 ? ASP B 330 ? PRO B 326 ASP B 328 5 ? 3  
HELX_P HELX_P34 AD7 GLU B 377 ? ALA B 381 ? GLU B 375 ALA B 379 5 ? 5  
HELX_P HELX_P35 AD8 THR B 382 ? ARG B 392 ? THR B 380 ARG B 390 1 ? 11 
HELX_P HELX_P36 AD9 GLU B 420 ? PHE B 424 ? GLU B 418 PHE B 422 5 ? 5  
HELX_P HELX_P37 AE1 ASN B 425 ? ILE B 434 ? ASN B 423 ILE B 432 1 ? 10 
HELX_P HELX_P38 AE2 PRO B 447 ? TYR B 459 ? PRO B 445 TYR B 457 1 ? 13 
HELX_P HELX_P39 AE3 ASN B 491 ? ASN B 505 ? ASN B 489 ASN B 503 1 ? 15 
HELX_P HELX_P40 AE4 PRO B 506 ? ALA B 511 ? PRO B 504 ALA B 509 5 ? 6  
HELX_P HELX_P41 AE5 TYR B 517 ? GLY B 529 ? TYR B 515 GLY B 527 1 ? 13 
HELX_P HELX_P42 AE6 VAL B 535 ? GLN B 539 ? VAL B 533 GLN B 537 1 ? 5  
HELX_P HELX_P43 AE7 THR B 554 ? ASN B 559 ? THR B 552 ASN B 557 1 ? 6  
HELX_P HELX_P44 AE8 ASN B 559 ? THR B 568 ? ASN B 557 THR B 566 1 ? 10 
HELX_P HELX_P45 AE9 ASP B 580 ? LEU B 587 ? ASP B 578 LEU B 585 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A CYS 7  SG  ? ? ? 1_555 E ZN . ZN ? ? A CYS 5  A ZN 703 1_555 ? ? ? ? ? ? ? 2.314 ? ? 
metalc2  metalc ? ? A CYS 10 SG  ? ? ? 1_555 E ZN . ZN ? ? A CYS 8  A ZN 703 1_555 ? ? ? ? ? ? ? 2.330 ? ? 
metalc3  metalc ? ? A CYS 18 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 16 A ZN 702 1_555 ? ? ? ? ? ? ? 2.297 ? ? 
metalc4  metalc ? ? A CYS 21 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 19 A ZN 702 1_555 ? ? ? ? ? ? ? 2.294 ? ? 
metalc5  metalc ? ? A CYS 28 SG  ? ? ? 1_555 E ZN . ZN ? ? A CYS 26 A ZN 703 1_555 ? ? ? ? ? ? ? 2.294 ? ? 
metalc6  metalc ? ? A CYS 31 SG  ? ? ? 1_555 E ZN . ZN ? ? A CYS 29 A ZN 703 1_555 ? ? ? ? ? ? ? 2.333 ? ? 
metalc7  metalc ? ? A HIS 35 NE2 ? ? ? 1_555 D ZN . ZN ? ? A HIS 33 A ZN 702 1_555 ? ? ? ? ? ? ? 1.996 ? ? 
metalc8  metalc ? ? A HIS 41 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 39 A ZN 702 1_555 ? ? ? ? ? ? ? 2.004 ? ? 
metalc9  metalc ? ? A CYS 52 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 50 A ZN 701 1_555 ? ? ? ? ? ? ? 2.318 ? ? 
metalc10 metalc ? ? A CYS 57 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 55 A ZN 701 1_555 ? ? ? ? ? ? ? 2.307 ? ? 
metalc11 metalc ? ? A CYS 74 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 72 A ZN 701 1_555 ? ? ? ? ? ? ? 2.317 ? ? 
metalc12 metalc ? ? A HIS 77 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 75 A ZN 701 1_555 ? ? ? ? ? ? ? 2.078 ? ? 
metalc13 metalc ? ? B CYS 7  SG  ? ? ? 1_555 J ZN . ZN ? ? B CYS 5  B ZN 702 1_555 ? ? ? ? ? ? ? 2.343 ? ? 
metalc14 metalc ? ? B CYS 10 SG  ? ? ? 1_555 J ZN . ZN ? ? B CYS 8  B ZN 702 1_555 ? ? ? ? ? ? ? 2.338 ? ? 
metalc15 metalc ? ? B CYS 18 SG  ? ? ? 1_555 I ZN . ZN ? ? B CYS 16 B ZN 701 1_555 ? ? ? ? ? ? ? 2.305 ? ? 
metalc16 metalc ? ? B CYS 21 SG  ? ? ? 1_555 I ZN . ZN ? ? B CYS 19 B ZN 701 1_555 ? ? ? ? ? ? ? 2.308 ? ? 
metalc17 metalc ? ? B CYS 28 SG  ? ? ? 1_555 J ZN . ZN ? ? B CYS 26 B ZN 702 1_555 ? ? ? ? ? ? ? 2.306 ? ? 
metalc18 metalc ? ? B CYS 31 SG  ? ? ? 1_555 J ZN . ZN ? ? B CYS 29 B ZN 702 1_555 ? ? ? ? ? ? ? 2.333 ? ? 
metalc19 metalc ? ? B HIS 35 NE2 ? ? ? 1_555 I ZN . ZN ? ? B HIS 33 B ZN 701 1_555 ? ? ? ? ? ? ? 2.062 ? ? 
metalc20 metalc ? ? B HIS 41 ND1 ? ? ? 1_555 I ZN . ZN ? ? B HIS 39 B ZN 701 1_555 ? ? ? ? ? ? ? 2.024 ? ? 
metalc21 metalc ? ? B CYS 52 SG  ? ? ? 1_555 K ZN . ZN ? ? B CYS 50 B ZN 703 1_555 ? ? ? ? ? ? ? 2.314 ? ? 
metalc22 metalc ? ? B CYS 57 SG  ? ? ? 1_555 K ZN . ZN ? ? B CYS 55 B ZN 703 1_555 ? ? ? ? ? ? ? 2.310 ? ? 
metalc23 metalc ? ? B CYS 74 SG  ? ? ? 1_555 K ZN . ZN ? ? B CYS 72 B ZN 703 1_555 ? ? ? ? ? ? ? 2.314 ? ? 
metalc24 metalc ? ? B HIS 77 ND1 ? ? ? 1_555 K ZN . ZN ? ? B HIS 75 B ZN 703 1_555 ? ? ? ? ? ? ? 2.106 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG  ? A CYS 7  ? A CYS 5  ? 1_555 ZN ? E ZN . ? A ZN 703 ? 1_555 SG  ? A CYS 10 ? A CYS 8  ? 1_555 114.7 ? 
2  SG  ? A CYS 7  ? A CYS 5  ? 1_555 ZN ? E ZN . ? A ZN 703 ? 1_555 SG  ? A CYS 28 ? A CYS 26 ? 1_555 94.7  ? 
3  SG  ? A CYS 10 ? A CYS 8  ? 1_555 ZN ? E ZN . ? A ZN 703 ? 1_555 SG  ? A CYS 28 ? A CYS 26 ? 1_555 96.8  ? 
4  SG  ? A CYS 7  ? A CYS 5  ? 1_555 ZN ? E ZN . ? A ZN 703 ? 1_555 SG  ? A CYS 31 ? A CYS 29 ? 1_555 113.6 ? 
5  SG  ? A CYS 10 ? A CYS 8  ? 1_555 ZN ? E ZN . ? A ZN 703 ? 1_555 SG  ? A CYS 31 ? A CYS 29 ? 1_555 128.7 ? 
6  SG  ? A CYS 28 ? A CYS 26 ? 1_555 ZN ? E ZN . ? A ZN 703 ? 1_555 SG  ? A CYS 31 ? A CYS 29 ? 1_555 95.6  ? 
7  SG  ? A CYS 18 ? A CYS 16 ? 1_555 ZN ? D ZN . ? A ZN 702 ? 1_555 SG  ? A CYS 21 ? A CYS 19 ? 1_555 120.7 ? 
8  SG  ? A CYS 18 ? A CYS 16 ? 1_555 ZN ? D ZN . ? A ZN 702 ? 1_555 NE2 ? A HIS 35 ? A HIS 33 ? 1_555 93.8  ? 
9  SG  ? A CYS 21 ? A CYS 19 ? 1_555 ZN ? D ZN . ? A ZN 702 ? 1_555 NE2 ? A HIS 35 ? A HIS 33 ? 1_555 98.0  ? 
10 SG  ? A CYS 18 ? A CYS 16 ? 1_555 ZN ? D ZN . ? A ZN 702 ? 1_555 ND1 ? A HIS 41 ? A HIS 39 ? 1_555 117.0 ? 
11 SG  ? A CYS 21 ? A CYS 19 ? 1_555 ZN ? D ZN . ? A ZN 702 ? 1_555 ND1 ? A HIS 41 ? A HIS 39 ? 1_555 119.5 ? 
12 NE2 ? A HIS 35 ? A HIS 33 ? 1_555 ZN ? D ZN . ? A ZN 702 ? 1_555 ND1 ? A HIS 41 ? A HIS 39 ? 1_555 94.8  ? 
13 SG  ? A CYS 52 ? A CYS 50 ? 1_555 ZN ? C ZN . ? A ZN 701 ? 1_555 SG  ? A CYS 57 ? A CYS 55 ? 1_555 112.8 ? 
14 SG  ? A CYS 52 ? A CYS 50 ? 1_555 ZN ? C ZN . ? A ZN 701 ? 1_555 SG  ? A CYS 74 ? A CYS 72 ? 1_555 113.3 ? 
15 SG  ? A CYS 57 ? A CYS 55 ? 1_555 ZN ? C ZN . ? A ZN 701 ? 1_555 SG  ? A CYS 74 ? A CYS 72 ? 1_555 111.0 ? 
16 SG  ? A CYS 52 ? A CYS 50 ? 1_555 ZN ? C ZN . ? A ZN 701 ? 1_555 ND1 ? A HIS 77 ? A HIS 75 ? 1_555 117.5 ? 
17 SG  ? A CYS 57 ? A CYS 55 ? 1_555 ZN ? C ZN . ? A ZN 701 ? 1_555 ND1 ? A HIS 77 ? A HIS 75 ? 1_555 106.0 ? 
18 SG  ? A CYS 74 ? A CYS 72 ? 1_555 ZN ? C ZN . ? A ZN 701 ? 1_555 ND1 ? A HIS 77 ? A HIS 75 ? 1_555 94.8  ? 
19 SG  ? B CYS 7  ? B CYS 5  ? 1_555 ZN ? J ZN . ? B ZN 702 ? 1_555 SG  ? B CYS 10 ? B CYS 8  ? 1_555 109.4 ? 
20 SG  ? B CYS 7  ? B CYS 5  ? 1_555 ZN ? J ZN . ? B ZN 702 ? 1_555 SG  ? B CYS 28 ? B CYS 26 ? 1_555 111.6 ? 
21 SG  ? B CYS 10 ? B CYS 8  ? 1_555 ZN ? J ZN . ? B ZN 702 ? 1_555 SG  ? B CYS 28 ? B CYS 26 ? 1_555 101.8 ? 
22 SG  ? B CYS 7  ? B CYS 5  ? 1_555 ZN ? J ZN . ? B ZN 702 ? 1_555 SG  ? B CYS 31 ? B CYS 29 ? 1_555 107.1 ? 
23 SG  ? B CYS 10 ? B CYS 8  ? 1_555 ZN ? J ZN . ? B ZN 702 ? 1_555 SG  ? B CYS 31 ? B CYS 29 ? 1_555 121.0 ? 
24 SG  ? B CYS 28 ? B CYS 26 ? 1_555 ZN ? J ZN . ? B ZN 702 ? 1_555 SG  ? B CYS 31 ? B CYS 29 ? 1_555 105.8 ? 
25 SG  ? B CYS 18 ? B CYS 16 ? 1_555 ZN ? I ZN . ? B ZN 701 ? 1_555 SG  ? B CYS 21 ? B CYS 19 ? 1_555 115.4 ? 
26 SG  ? B CYS 18 ? B CYS 16 ? 1_555 ZN ? I ZN . ? B ZN 701 ? 1_555 NE2 ? B HIS 35 ? B HIS 33 ? 1_555 111.1 ? 
27 SG  ? B CYS 21 ? B CYS 19 ? 1_555 ZN ? I ZN . ? B ZN 701 ? 1_555 NE2 ? B HIS 35 ? B HIS 33 ? 1_555 115.5 ? 
28 SG  ? B CYS 18 ? B CYS 16 ? 1_555 ZN ? I ZN . ? B ZN 701 ? 1_555 ND1 ? B HIS 41 ? B HIS 39 ? 1_555 105.3 ? 
29 SG  ? B CYS 21 ? B CYS 19 ? 1_555 ZN ? I ZN . ? B ZN 701 ? 1_555 ND1 ? B HIS 41 ? B HIS 39 ? 1_555 103.2 ? 
30 NE2 ? B HIS 35 ? B HIS 33 ? 1_555 ZN ? I ZN . ? B ZN 701 ? 1_555 ND1 ? B HIS 41 ? B HIS 39 ? 1_555 105.0 ? 
31 SG  ? B CYS 52 ? B CYS 50 ? 1_555 ZN ? K ZN . ? B ZN 703 ? 1_555 SG  ? B CYS 57 ? B CYS 55 ? 1_555 107.2 ? 
32 SG  ? B CYS 52 ? B CYS 50 ? 1_555 ZN ? K ZN . ? B ZN 703 ? 1_555 SG  ? B CYS 74 ? B CYS 72 ? 1_555 111.5 ? 
33 SG  ? B CYS 57 ? B CYS 55 ? 1_555 ZN ? K ZN . ? B ZN 703 ? 1_555 SG  ? B CYS 74 ? B CYS 72 ? 1_555 111.1 ? 
34 SG  ? B CYS 52 ? B CYS 50 ? 1_555 ZN ? K ZN . ? B ZN 703 ? 1_555 ND1 ? B HIS 77 ? B HIS 75 ? 1_555 125.7 ? 
35 SG  ? B CYS 57 ? B CYS 55 ? 1_555 ZN ? K ZN . ? B ZN 703 ? 1_555 ND1 ? B HIS 77 ? B HIS 75 ? 1_555 109.1 ? 
36 SG  ? B CYS 74 ? B CYS 72 ? 1_555 ZN ? K ZN . ? B ZN 703 ? 1_555 ND1 ? B HIS 77 ? B HIS 75 ? 1_555 91.1  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 3 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 4 ? 
AA7 ? 8 ? 
AA8 ? 2 ? 
AA9 ? 6 ? 
AB1 ? 2 ? 
AB2 ? 2 ? 
AB3 ? 2 ? 
AB4 ? 3 ? 
AB5 ? 2 ? 
AB6 ? 7 ? 
AB7 ? 8 ? 
AB8 ? 2 ? 
AB9 ? 6 ? 
AC1 ? 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 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? parallel      
AA7 5 6 ? parallel      
AA7 6 7 ? parallel      
AA7 7 8 ? parallel      
AA8 1 2 ? parallel      
AA9 1 2 ? parallel      
AA9 2 3 ? parallel      
AA9 3 4 ? parallel      
AA9 4 5 ? parallel      
AA9 5 6 ? parallel      
AB1 1 2 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB6 4 5 ? anti-parallel 
AB6 5 6 ? anti-parallel 
AB6 6 7 ? anti-parallel 
AB7 1 2 ? parallel      
AB7 2 3 ? parallel      
AB7 3 4 ? parallel      
AB7 4 5 ? parallel      
AB7 5 6 ? parallel      
AB7 6 7 ? parallel      
AB7 7 8 ? parallel      
AB8 1 2 ? parallel      
AB9 1 2 ? parallel      
AB9 2 3 ? parallel      
AB9 3 4 ? parallel      
AB9 4 5 ? parallel      
AB9 5 6 ? parallel      
AC1 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 GLY A 5   ? ALA A 6   ? GLY A 3   ALA A 4   
AA1 2 GLN A 13  ? THR A 14  ? GLN A 11  THR A 12  
AA2 1 PHE A 26  ? LEU A 27  ? PHE A 24  LEU A 25  
AA2 2 LEU A 16  ? CYS A 18  ? LEU A 14  CYS A 16  
AA2 3 VAL A 44  ? LEU A 45  ? VAL A 42  LEU A 43  
AA3 1 SER A 71  ? CYS A 74  ? SER A 69  CYS A 72  
AA3 2 LEU A 65  ? GLY A 68  ? LEU A 63  GLY A 66  
AA3 3 PHE A 83  ? PRO A 84  ? PHE A 81  PRO A 82  
AA4 1 CYS A 86  ? ALA A 87  ? CYS A 84  ALA A 85  
AA4 2 GLN A 90  ? VAL A 91  ? GLN A 88  VAL A 89  
AA5 1 ALA A 154 ? VAL A 159 ? ALA A 152 VAL A 157 
AA5 2 LEU A 165 ? TRP A 169 ? LEU A 163 TRP A 167 
AA6 1 VAL A 212 ? GLY A 215 ? VAL A 210 GLY A 213 
AA6 2 GLY A 198 ? GLU A 203 ? GLY A 196 GLU A 201 
AA6 3 PHE A 184 ? TYR A 187 ? PHE A 182 TYR A 185 
AA6 4 TYR A 226 ? TYR A 226 ? TYR A 224 TYR A 224 
AA7 1 LYS A 349 ? VAL A 350 ? LYS A 347 VAL A 348 
AA7 2 CYS A 332 ? ARG A 334 ? CYS A 330 ARG A 332 
AA7 3 TYR A 357 ? THR A 361 ? TYR A 355 THR A 359 
AA7 4 ILE A 306 ? ALA A 310 ? ILE A 304 ALA A 308 
AA7 5 THR A 368 ? PHE A 375 ? THR A 366 PHE A 373 
AA7 6 LEU A 393 ? GLY A 402 ? LEU A 391 GLY A 400 
AA7 7 TYR A 279 ? GLN A 283 ? TYR A 277 GLN A 281 
AA7 8 MET A 438 ? PHE A 439 ? MET A 436 PHE A 437 
AA8 1 THR A 442 ? CYS A 443 ? THR A 440 CYS A 441 
AA8 2 LYS A 464 ? ALA A 465 ? LYS A 462 ALA A 463 
AA9 1 THR A 532 ? THR A 534 ? THR A 530 THR A 532 
AA9 2 VAL A 512 ? SER A 515 ? VAL A 510 SER A 513 
AA9 3 TYR A 543 ? THR A 549 ? TYR A 541 THR A 547 
AA9 4 ALA A 570 ? MET A 578 ? ALA A 568 MET A 576 
AA9 5 CYS A 473 ? PHE A 477 ? CYS A 471 PHE A 475 
AA9 6 THR A 590 ? SER A 591 ? THR A 588 SER A 589 
AB1 1 THR A 483 ? ASP A 485 ? THR A 481 ASP A 483 
AB1 2 SER A 488 ? ILE A 490 ? SER A 486 ILE A 488 
AB2 1 GLY B 5   ? ALA B 6   ? GLY B 3   ALA B 4   
AB2 2 GLN B 13  ? THR B 14  ? GLN B 11  THR B 12  
AB3 1 ARG B 17  ? CYS B 18  ? ARG B 15  CYS B 16  
AB3 2 VAL B 44  ? LEU B 45  ? VAL B 42  LEU B 43  
AB4 1 SER B 71  ? CYS B 74  ? SER B 69  CYS B 72  
AB4 2 LEU B 65  ? GLY B 68  ? LEU B 63  GLY B 66  
AB4 3 PHE B 83  ? PRO B 84  ? PHE B 81  PRO B 82  
AB5 1 CYS B 86  ? ALA B 87  ? CYS B 84  ALA B 85  
AB5 2 GLN B 90  ? VAL B 91  ? GLN B 88  VAL B 89  
AB6 1 LYS B 194 ? TYR B 200 ? LYS B 192 TYR B 198 
AB6 2 PHE B 184 ? VAL B 189 ? PHE B 182 VAL B 187 
AB6 3 TYR B 226 ? LEU B 229 ? TYR B 224 LEU B 227 
AB6 4 ALA B 154 ? GLU B 158 ? ALA B 152 GLU B 156 
AB6 5 GLU B 164 ? TRP B 169 ? GLU B 162 TRP B 167 
AB6 6 VAL B 211 ? TYR B 213 ? VAL B 209 TYR B 211 
AB6 7 PHE B 202 ? GLU B 203 ? PHE B 200 GLU B 201 
AB7 1 LYS B 349 ? VAL B 350 ? LYS B 347 VAL B 348 
AB7 2 CYS B 332 ? ARG B 334 ? CYS B 330 ARG B 332 
AB7 3 TYR B 357 ? THR B 361 ? TYR B 355 THR B 359 
AB7 4 ILE B 306 ? ALA B 310 ? ILE B 304 ALA B 308 
AB7 5 THR B 368 ? PHE B 375 ? THR B 366 PHE B 373 
AB7 6 LEU B 393 ? GLY B 402 ? LEU B 391 GLY B 400 
AB7 7 TYR B 279 ? GLN B 283 ? TYR B 277 GLN B 281 
AB7 8 MET B 438 ? PHE B 439 ? MET B 436 PHE B 437 
AB8 1 THR B 442 ? CYS B 443 ? THR B 440 CYS B 441 
AB8 2 LYS B 464 ? ALA B 465 ? LYS B 462 ALA B 463 
AB9 1 THR B 532 ? THR B 534 ? THR B 530 THR B 532 
AB9 2 VAL B 512 ? SER B 515 ? VAL B 510 SER B 513 
AB9 3 TYR B 543 ? THR B 549 ? TYR B 541 THR B 547 
AB9 4 ALA B 570 ? MET B 578 ? ALA B 568 MET B 576 
AB9 5 CYS B 473 ? PHE B 477 ? CYS B 471 PHE B 475 
AB9 6 THR B 590 ? SER B 591 ? THR B 588 SER B 589 
AC1 1 THR B 483 ? HIS B 484 ? THR B 481 HIS B 482 
AC1 2 ALA B 489 ? ILE B 490 ? ALA B 487 ILE B 488 
# 
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 GLY A 5   ? N GLY A 3   O THR A 14  ? O THR A 12  
AA2 1 2 O LEU A 27  ? O LEU A 25  N LEU A 16  ? N LEU A 14  
AA2 2 3 N ARG A 17  ? N ARG A 15  O LEU A 45  ? O LEU A 43  
AA3 1 2 O TYR A 73  ? O TYR A 71  N TYR A 66  ? N TYR A 64  
AA3 2 3 N LEU A 67  ? N LEU A 65  O PHE A 83  ? O PHE A 81  
AA4 1 2 N ALA A 87  ? N ALA A 85  O GLN A 90  ? O GLN A 88  
AA5 1 2 N THR A 155 ? N THR A 153 O SER A 168 ? O SER A 166 
AA6 1 2 O VAL A 212 ? O VAL A 210 N GLU A 203 ? N GLU A 201 
AA6 2 3 O TYR A 200 ? O TYR A 198 N PHE A 184 ? N PHE A 182 
AA6 3 4 N TYR A 187 ? N TYR A 185 O TYR A 226 ? O TYR A 224 
AA7 1 2 O LYS A 349 ? O LYS A 347 N ARG A 334 ? N ARG A 332 
AA7 2 3 N SER A 333 ? N SER A 331 O PHE A 359 ? O PHE A 357 
AA7 3 4 O VAL A 358 ? O VAL A 356 N TYR A 308 ? N TYR A 306 
AA7 4 5 N THR A 309 ? N THR A 307 O VAL A 374 ? O VAL A 372 
AA7 5 6 N VAL A 373 ? N VAL A 371 O VAL A 399 ? O VAL A 397 
AA7 6 7 O TYR A 400 ? O TYR A 398 N SER A 280 ? N SER A 278 
AA7 7 8 N GLN A 283 ? N GLN A 281 O MET A 438 ? O MET A 436 
AA8 1 2 N CYS A 443 ? N CYS A 441 O LYS A 464 ? O LYS A 462 
AA9 1 2 O GLN A 533 ? O GLN A 531 N PHE A 513 ? N PHE A 511 
AA9 2 3 N ILE A 514 ? N ILE A 512 O ILE A 547 ? O ILE A 545 
AA9 3 4 N PHE A 548 ? N PHE A 546 O ILE A 577 ? O ILE A 575 
AA9 4 5 O MET A 578 ? O MET A 576 N MET A 476 ? N MET A 474 
AA9 5 6 N LYS A 475 ? N LYS A 473 O THR A 590 ? O THR A 588 
AB1 1 2 N THR A 483 ? N THR A 481 O ILE A 490 ? O ILE A 488 
AB2 1 2 N GLY B 5   ? N GLY B 3   O THR B 14  ? O THR B 12  
AB3 1 2 N ARG B 17  ? N ARG B 15  O LEU B 45  ? O LEU B 43  
AB4 1 2 O TYR B 73  ? O TYR B 71  N TYR B 66  ? N TYR B 64  
AB4 2 3 N LEU B 67  ? N LEU B 65  O PHE B 83  ? O PHE B 81  
AB5 1 2 N ALA B 87  ? N ALA B 85  O GLN B 90  ? O GLN B 88  
AB6 1 2 O TYR B 200 ? O TYR B 198 N PHE B 184 ? N PHE B 182 
AB6 2 3 N THR B 185 ? N THR B 183 O VAL B 228 ? O VAL B 226 
AB6 3 4 O PHE B 227 ? O PHE B 225 N ALA B 154 ? N ALA B 152 
AB6 4 5 N GLU B 158 ? N GLU B 156 O HIS B 166 ? O HIS B 164 
AB6 5 6 N LEU B 165 ? N LEU B 163 O VAL B 211 ? O VAL B 209 
AB6 6 7 O VAL B 212 ? O VAL B 210 N GLU B 203 ? N GLU B 201 
AB7 1 2 O LYS B 349 ? O LYS B 347 N ARG B 334 ? N ARG B 332 
AB7 2 3 N SER B 333 ? N SER B 331 O PHE B 359 ? O PHE B 357 
AB7 3 4 O VAL B 358 ? O VAL B 356 N TYR B 308 ? N TYR B 306 
AB7 4 5 N THR B 309 ? N THR B 307 O VAL B 374 ? O VAL B 372 
AB7 5 6 N VAL B 373 ? N VAL B 371 O VAL B 399 ? O VAL B 397 
AB7 6 7 O TYR B 400 ? O TYR B 398 N LEU B 282 ? N LEU B 280 
AB7 7 8 N GLN B 283 ? N GLN B 281 O MET B 438 ? O MET B 436 
AB8 1 2 N CYS B 443 ? N CYS B 441 O LYS B 464 ? O LYS B 462 
AB9 1 2 O GLN B 533 ? O GLN B 531 N PHE B 513 ? N PHE B 511 
AB9 2 3 N ILE B 514 ? N ILE B 512 O ILE B 547 ? O ILE B 545 
AB9 3 4 N PHE B 548 ? N PHE B 546 O ILE B 577 ? O ILE B 575 
AB9 4 5 O MET B 578 ? O MET B 576 N MET B 476 ? N MET B 474 
AB9 5 6 N CYS B 473 ? N CYS B 471 O THR B 590 ? O THR B 588 
AC1 1 2 N THR B 483 ? N THR B 481 O ILE B 490 ? O ILE B 488 
# 
_pdbx_entry_details.entry_id                   9I1S 
_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 THR A 12  ? ? -160.69 -168.73 
2  1 ARG A 22  ? ? 39.43   63.08   
3  1 THR A 37  ? ? -117.97 -168.65 
4  1 SER A 44  ? ? -145.90 -159.20 
5  1 SER A 159 ? ? -129.25 -163.66 
6  1 LEU A 176 ? ? -105.66 72.14   
7  1 THR A 216 ? ? -91.40  42.73   
8  1 SER A 229 ? ? -145.20 -156.35 
9  1 HIS A 230 ? ? 178.33  168.51  
10 1 SER A 236 ? ? -135.35 -40.38  
11 1 ARG A 339 ? ? -101.16 -67.07  
12 1 ASP A 344 ? ? -113.43 57.79   
13 1 LYS A 345 ? ? -143.57 -0.79   
14 1 ASN A 388 ? ? -59.49  -9.61   
15 1 ALA A 389 ? ? -96.31  -76.42  
16 1 THR A 431 ? ? -104.98 -69.56  
17 1 VAL A 484 ? ? 72.31   -90.33  
18 1 THR A 549 ? ? 73.42   -49.61  
19 1 GLU A 551 ? ? -111.63 75.75   
20 1 VAL A 570 ? ? -120.24 -57.06  
21 1 ASN B 9   ? ? 70.80   -13.99  
22 1 LYS B 94  ? ? -65.30  2.03    
23 1 ARG B 161 ? ? 76.87   -12.80  
24 1 SER B 191 ? ? -161.39 -158.75 
25 1 SER B 236 ? ? -137.85 -43.15  
26 1 TYR B 299 ? ? -118.61 69.77   
27 1 CYS B 342 ? ? -128.01 -164.55 
28 1 GLN B 404 ? ? -102.53 -168.93 
29 1 THR B 431 ? ? -97.70  -60.62  
30 1 VAL B 456 ? ? -141.48 -1.32   
31 1 ASP B 483 ? ? -107.64 -154.71 
32 1 THR B 549 ? ? 76.81   -49.61  
33 1 VAL B 570 ? ? -126.88 -60.77  
34 1 GLN B 586 ? ? -90.26  57.07   
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 0.6626   -8.2589 -43.1054 0.5099 ? 0.1027  ? 0.0447  ? 0.4218 ? 0.0301  ? 0.5838 ? 8.2981 ? 
-2.4638 ? -1.3772 ? 8.0687 ? 1.7037  ? 9.5065 ? 0.6509  ? 0.9525  ? 0.3748  ? -0.8993 ? -0.2104 ? -0.7914 ? 0.2871  ? 0.3498  ? 
-0.4273 ? 
2  'X-RAY DIFFRACTION' ? refined -10.8090 6.5823  -29.9923 0.4193 ? -0.0038 ? 0.0317  ? 0.1989 ? -0.0539 ? 0.3761 ? 7.3839 ? 
3.7960  ? 2.5651  ? 2.3106 ? 1.9954  ? 8.3536 ? 0.0188  ? 0.1395  ? -0.6152 ? 0.0930  ? -0.0455 ? -0.2331 ? 0.3500  ? -0.0320 ? 
-0.0292 ? 
3  'X-RAY DIFFRACTION' ? refined -36.8953 14.5883 -41.4641 0.9009 ? -0.0932 ? 0.0854  ? 0.4947 ? -0.0591 ? 0.5349 ? 9.9617 ? 
-1.1477 ? 1.2747  ? 9.7895 ? -0.2846 ? 5.4380 ? -0.0255 ? -0.2208 ? 0.9287  ? -0.0421 ? 0.2188  ? -0.1500 ? -1.9067 ? 0.0467  ? 
-0.1949 ? 
4  'X-RAY DIFFRACTION' ? refined -38.7821 19.8662 -44.2139 1.3460 ? -0.0400 ? 0.1276  ? 0.6100 ? 0.0844  ? 0.8075 ? 4.8565 ? 
-2.0126 ? -0.8572 ? 3.3928 ? 2.6571  ? 9.4700 ? 0.1180  ? 0.2458  ? 1.6258  ? -0.8753 ? 0.5589  ? -0.2547 ? -3.1762 ? -0.1098 ? 
-0.6176 ? 
5  'X-RAY DIFFRACTION' ? refined -0.7666  29.8429 -31.1323 0.2416 ? 0.0332  ? 0.1043  ? 0.3194 ? 0.0150  ? 0.2683 ? 1.8780 ? 
1.5394  ? 0.5312  ? 7.9480 ? 1.9156  ? 3.0866 ? -0.0782 ? 0.1706  ? 0.0111  ? -0.2794 ? 0.2199  ? -0.3258 ? -0.0747 ? 0.0108  ? 
-0.1739 ? 
6  'X-RAY DIFFRACTION' ? refined -8.8646  39.2023 -28.8749 0.2143 ? 0.0174  ? 0.0135  ? 0.2106 ? -0.0052 ? 0.3976 ? 3.0909 ? 
1.0068  ? 0.3566  ? 6.0043 ? 0.1359  ? 6.6171 ? 0.1031  ? 0.0832  ? 0.4169  ? -0.2343 ? -0.1565 ? 0.3281  ? -0.4037 ? -0.2546 ? 
0.0655  ? 
7  'X-RAY DIFFRACTION' ? refined -10.0338 27.0376 -29.4756 0.2026 ? 0.0142  ? -0.0412 ? 0.2857 ? -0.0696 ? 0.3499 ? 1.4094 ? 
0.5645  ? -0.5696 ? 4.5019 ? 0.0009  ? 3.2532 ? 0.0043  ? 0.1552  ? -0.0181 ? -0.3362 ? -0.1537 ? 0.1885  ? 0.1314  ? -0.2961 ? 
0.1214  ? 
8  'X-RAY DIFFRACTION' ? refined -32.0960 27.4344 -12.0634 0.3053 ? 0.0114  ? 0.0773  ? 0.2187 ? 0.0010  ? 0.1945 ? 8.9750 ? 
1.8933  ? 1.7370  ? 3.9079 ? 0.7304  ? 2.9049 ? -0.0364 ? -0.2626 ? 0.0485  ? 0.1893  ? 0.0521  ? 0.1193  ? -0.1312 ? -0.0650 ? 
-0.0197 ? 
9  'X-RAY DIFFRACTION' ? refined 3.4419   57.3955 -55.9446 1.2660 ? -0.0016 ? -0.4040 ? 0.6684 ? -0.1625 ? 0.8677 ? 1.0577 ? 
2.2014  ? 0.6106  ? 8.1226 ? 5.2470  ? 5.1120 ? 0.7678  ? -0.0389 ? -0.9064 ? 1.1214  ? 0.3485  ? -1.2795 ? 1.1675  ? 0.7921  ? 
-1.0653 ? 
10 'X-RAY DIFFRACTION' ? refined -6.8158  41.2250 -69.0410 1.0570 ? -0.0547 ? -0.2499 ? 0.3847 ? -0.1019 ? 0.5621 ? 3.4344 ? 
-0.8570 ? 0.7540  ? 6.5719 ? -0.1509 ? 9.6903 ? 0.2324  ? -0.4102 ? 0.3907  ? 1.7288  ? 0.2344  ? -0.8278 ? 0.0536  ? 0.1141  ? 
-0.4539 ? 
11 'X-RAY DIFFRACTION' ? refined -35.5914 35.3129 -67.6440 0.8436 ? 0.0370  ? 0.0052  ? 1.0197 ? 0.0670  ? 1.0188 ? 8.4335 ? 
8.2298  ? -1.0239 ? 8.7245 ? -2.3002 ? 2.4033 ? 0.3879  ? 0.9683  ? 1.2566  ? -0.3350 ? 0.3111  ? 1.7152  ? 0.0538  ? -0.3924 ? 
-0.6732 ? 
12 'X-RAY DIFFRACTION' ? refined -32.6691 29.2560 -63.6823 1.5468 ? -0.1198 ? -0.3927 ? 1.1845 ? -0.1656 ? 1.0799 ? 9.9599 ? 
3.1154  ? 6.5365  ? 6.1621 ? 7.5311  ? 2.0024 ? 2.3674  ? 0.1987  ? -2.3467 ? -0.3240 ? -0.9414 ? -0.4247 ? 2.0800  ? -2.2916 ? 
-1.3834 ? 
13 'X-RAY DIFFRACTION' ? refined -38.6295 29.9147 -62.7367 1.2182 ? 0.0014  ? -0.2511 ? 1.0236 ? 0.1399  ? 1.2264 ? 5.2846 ? 
-1.4348 ? 5.0730  ? 8.2704 ? -4.1653 ? 6.4127 ? 2.3024  ? 0.5642  ? -0.7566 ? 0.1475  ? -0.9753 ? 2.0565  ? 1.2532  ? -0.0001 ? 
-1.3842 ? 
14 'X-RAY DIFFRACTION' ? refined 1.0175   18.3178 -62.5848 1.1358 ? 0.0050  ? -0.4189 ? 0.8348 ? -0.0163 ? 0.6577 ? 2.7284 ? 
-2.0115 ? 0.4916  ? 5.3968 ? -0.1309 ? 2.1833 ? -0.4323 ? -0.6178 ? 0.1449  ? 1.4728  ? 0.5423  ? -0.8694 ? 0.4302  ? 0.3669  ? 
-0.1213 ? 
15 'X-RAY DIFFRACTION' ? refined -7.1473  15.8547 -67.3377 0.9564 ? 0.0207  ? -0.2049 ? 0.4546 ? -0.0594 ? 0.5166 ? 1.6305 ? 
-0.4373 ? 0.5538  ? 5.0936 ? 0.0306  ? 4.2931 ? -0.1018 ? -0.4741 ? -0.0735 ? 1.7458  ? 0.0677  ? -0.5743 ? 0.3185  ? 0.0459  ? 
0.0254  ? 
16 'X-RAY DIFFRACTION' ? refined -23.3911 18.6830 -90.0318 0.3748 ? -0.0760 ? 0.1114  ? 0.3106 ? 0.0689  ? 0.2189 ? 6.0770 ? 
-2.2426 ? 2.3225  ? 6.2385 ? 0.3258  ? 1.6326 ? 0.0527  ? -0.0515 ? -0.2538 ? 0.2632  ? 0.0655  ? 0.5073  ? 0.1148  ? -0.1073 ? 
-0.1151 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 2 through 100 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 101 through 150 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 151 through 203 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 208 through 226 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 227 through 259 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 260 through 336 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 340 through 441 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 442 through 593 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1 through 94 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 103 through 150 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 151 through 185 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 194 through 202 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 207 through 226 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 227 through 259 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 260 through 441 )
;
16 'X-RAY DIFFRACTION' 16 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 442 through 592 )
;
# 
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 SER -1  ? A SER 1   
2  1 Y 1 A MET 0   ? A MET 2   
3  1 Y 1 A ASN 95  ? A ASN 97  
4  1 Y 1 A THR 96  ? A THR 98  
5  1 Y 1 A CYS 97  ? A CYS 99  
6  1 Y 1 A VAL 98  ? A VAL 100 
7  1 Y 1 A GLY 99  ? A GLY 101 
8  1 Y 1 A SER 100 ? A SER 102 
9  1 Y 1 A ASP 101 ? A ASP 103 
10 1 Y 1 A ASN 102 ? A ASN 104 
11 1 Y 1 A ARG 186 ? A ARG 188 
12 1 Y 1 A VAL 187 ? A VAL 189 
13 1 Y 1 A THR 188 ? A THR 190 
14 1 Y 1 A LYS 189 ? A LYS 191 
15 1 Y 1 A ASN 190 ? A ASN 192 
16 1 Y 1 A SER 191 ? A SER 193 
17 1 Y 1 A LYS 192 ? A LYS 194 
18 1 Y 1 A VAL 193 ? A VAL 195 
19 1 Y 1 A GLY 203 ? A GLY 205 
20 1 Y 1 A ASP 204 ? A ASP 206 
21 1 Y 1 A TYR 205 ? A TYR 207 
22 1 Y 1 A GLY 206 ? A GLY 208 
23 1 Y 1 A PHE 225 ? A PHE 227 
24 1 Y 1 A PRO 593 ? A PRO 595 
25 1 Y 1 A ARG 594 ? A ARG 596 
26 1 Y 1 A ARG 595 ? A ARG 597 
27 1 Y 1 A ASN 596 ? A ASN 598 
28 1 Y 1 A VAL 597 ? A VAL 599 
29 1 Y 1 A ALA 598 ? A ALA 600 
30 1 Y 1 A THR 599 ? A THR 601 
31 1 Y 1 A LEU 600 ? A LEU 602 
32 1 Y 1 A GLN 601 ? A GLN 603 
33 1 Y 1 B SER -1  ? B SER 1   
34 1 Y 1 B MET 0   ? B MET 2   
35 1 Y 1 B ALA 1   ? B ALA 3   
36 1 Y 1 B ASP 204 ? B ASP 206 
37 1 Y 1 B TYR 205 ? B TYR 207 
38 1 Y 1 B GLY 206 ? B GLY 208 
39 1 Y 1 B ASP 207 ? B ASP 209 
40 1 Y 1 B ARG 337 ? B ARG 339 
41 1 Y 1 B ALA 338 ? B ALA 340 
42 1 Y 1 B ARG 339 ? B ARG 341 
43 1 Y 1 B ARG 594 ? B ARG 596 
44 1 Y 1 B ARG 595 ? B ARG 597 
45 1 Y 1 B ASN 596 ? B ASN 598 
46 1 Y 1 B VAL 597 ? B VAL 599 
47 1 Y 1 B ALA 598 ? B ALA 600 
48 1 Y 1 B THR 599 ? B THR 601 
49 1 Y 1 B LEU 600 ? B LEU 602 
50 1 Y 1 B GLN 601 ? B GLN 603 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HIS N    N  N N 137 
HIS CA   C  N S 138 
HIS C    C  N N 139 
HIS O    O  N N 140 
HIS CB   C  N N 141 
HIS CG   C  Y N 142 
HIS ND1  N  Y N 143 
HIS CD2  C  Y N 144 
HIS CE1  C  Y N 145 
HIS NE2  N  Y N 146 
HIS OXT  O  N N 147 
HIS H    H  N N 148 
HIS H2   H  N N 149 
HIS HA   H  N N 150 
HIS HB2  H  N N 151 
HIS HB3  H  N N 152 
HIS HD1  H  N N 153 
HIS HD2  H  N N 154 
HIS HE1  H  N N 155 
HIS HE2  H  N N 156 
HIS HXT  H  N N 157 
HOH O    O  N N 158 
HOH H1   H  N N 159 
HOH H2   H  N N 160 
ILE N    N  N N 161 
ILE CA   C  N S 162 
ILE C    C  N N 163 
ILE O    O  N N 164 
ILE CB   C  N S 165 
ILE CG1  C  N N 166 
ILE CG2  C  N N 167 
ILE CD1  C  N N 168 
ILE OXT  O  N N 169 
ILE H    H  N N 170 
ILE H2   H  N N 171 
ILE HA   H  N N 172 
ILE HB   H  N N 173 
ILE HG12 H  N N 174 
ILE HG13 H  N N 175 
ILE HG21 H  N N 176 
ILE HG22 H  N N 177 
ILE HG23 H  N N 178 
ILE HD11 H  N N 179 
ILE HD12 H  N N 180 
ILE HD13 H  N N 181 
ILE HXT  H  N N 182 
LEU N    N  N N 183 
LEU CA   C  N S 184 
LEU C    C  N N 185 
LEU O    O  N N 186 
LEU CB   C  N N 187 
LEU CG   C  N N 188 
LEU CD1  C  N N 189 
LEU CD2  C  N N 190 
LEU OXT  O  N N 191 
LEU H    H  N N 192 
LEU H2   H  N N 193 
LEU HA   H  N N 194 
LEU HB2  H  N N 195 
LEU HB3  H  N N 196 
LEU HG   H  N N 197 
LEU HD11 H  N N 198 
LEU HD12 H  N N 199 
LEU HD13 H  N N 200 
LEU HD21 H  N N 201 
LEU HD22 H  N N 202 
LEU HD23 H  N N 203 
LEU HXT  H  N N 204 
LYS N    N  N N 205 
LYS CA   C  N S 206 
LYS C    C  N N 207 
LYS O    O  N N 208 
LYS CB   C  N N 209 
LYS CG   C  N N 210 
LYS CD   C  N N 211 
LYS CE   C  N N 212 
LYS NZ   N  N N 213 
LYS OXT  O  N N 214 
LYS H    H  N N 215 
LYS H2   H  N N 216 
LYS HA   H  N N 217 
LYS HB2  H  N N 218 
LYS HB3  H  N N 219 
LYS HG2  H  N N 220 
LYS HG3  H  N N 221 
LYS HD2  H  N N 222 
LYS HD3  H  N N 223 
LYS HE2  H  N N 224 
LYS HE3  H  N N 225 
LYS HZ1  H  N N 226 
LYS HZ2  H  N N 227 
LYS HZ3  H  N N 228 
LYS HXT  H  N N 229 
MET N    N  N N 230 
MET CA   C  N S 231 
MET C    C  N N 232 
MET O    O  N N 233 
MET CB   C  N N 234 
MET CG   C  N N 235 
MET SD   S  N N 236 
MET CE   C  N N 237 
MET OXT  O  N N 238 
MET H    H  N N 239 
MET H2   H  N N 240 
MET HA   H  N N 241 
MET HB2  H  N N 242 
MET HB3  H  N N 243 
MET HG2  H  N N 244 
MET HG3  H  N N 245 
MET HE1  H  N N 246 
MET HE2  H  N N 247 
MET HE3  H  N N 248 
MET HXT  H  N N 249 
MPO S1   S  N N 250 
MPO O1   O  N N 251 
MPO O2   O  N N 252 
MPO O4   O  N N 253 
MPO N1   N  N N 254 
MPO C1   C  N N 255 
MPO O3   O  N N 256 
MPO C2   C  N N 257 
MPO C3   C  N N 258 
MPO C4   C  N N 259 
MPO C5   C  N N 260 
MPO C6   C  N N 261 
MPO C7   C  N N 262 
MPO H11  H  N N 263 
MPO H12  H  N N 264 
MPO HO3  H  N N 265 
MPO H21  H  N N 266 
MPO H22  H  N N 267 
MPO H31  H  N N 268 
MPO H32  H  N N 269 
MPO H41  H  N N 270 
MPO H42  H  N N 271 
MPO H51  H  N N 272 
MPO H52  H  N N 273 
MPO H61  H  N N 274 
MPO H62  H  N N 275 
MPO H71  H  N N 276 
MPO H72  H  N N 277 
MYC C1   C  Y N 278 
MYC C2   C  Y N 279 
MYC C3   C  Y N 280 
MYC C4   C  Y N 281 
MYC C5   C  Y N 282 
MYC C6   C  Y N 283 
MYC C9   C  Y N 284 
MYC C10  C  Y N 285 
MYC C11  C  Y N 286 
MYC C14  C  Y N 287 
MYC C15  C  Y N 288 
MYC C16  C  Y N 289 
MYC C17  C  Y N 290 
MYC C18  C  Y N 291 
MYC C19  C  Y N 292 
MYC O12  O  Y N 293 
MYC O13  O  N N 294 
MYC O23  O  N N 295 
MYC O24  O  N N 296 
MYC O25  O  N N 297 
MYC O27  O  N N 298 
MYC O29  O  N N 299 
MYC O30  O  N N 300 
MYC H1   H  N N 301 
MYC H5   H  N N 302 
MYC H15  H  N N 303 
MYC H19  H  N N 304 
MYC HO3  H  N N 305 
MYC HO4  H  N N 306 
MYC HO5  H  N N 307 
MYC HO7  H  N N 308 
MYC HO9  H  N N 309 
MYC HO0  H  N N 310 
PHE N    N  N N 311 
PHE CA   C  N S 312 
PHE C    C  N N 313 
PHE O    O  N N 314 
PHE CB   C  N N 315 
PHE CG   C  Y N 316 
PHE CD1  C  Y N 317 
PHE CD2  C  Y N 318 
PHE CE1  C  Y N 319 
PHE CE2  C  Y N 320 
PHE CZ   C  Y N 321 
PHE OXT  O  N N 322 
PHE H    H  N N 323 
PHE H2   H  N N 324 
PHE HA   H  N N 325 
PHE HB2  H  N N 326 
PHE HB3  H  N N 327 
PHE HD1  H  N N 328 
PHE HD2  H  N N 329 
PHE HE1  H  N N 330 
PHE HE2  H  N N 331 
PHE HZ   H  N N 332 
PHE HXT  H  N N 333 
PO4 P    P  N N 334 
PO4 O1   O  N N 335 
PO4 O2   O  N N 336 
PO4 O3   O  N N 337 
PO4 O4   O  N N 338 
PRO N    N  N N 339 
PRO CA   C  N S 340 
PRO C    C  N N 341 
PRO O    O  N N 342 
PRO CB   C  N N 343 
PRO CG   C  N N 344 
PRO CD   C  N N 345 
PRO OXT  O  N N 346 
PRO H    H  N N 347 
PRO HA   H  N N 348 
PRO HB2  H  N N 349 
PRO HB3  H  N N 350 
PRO HG2  H  N N 351 
PRO HG3  H  N N 352 
PRO HD2  H  N N 353 
PRO HD3  H  N N 354 
PRO HXT  H  N N 355 
SER N    N  N N 356 
SER CA   C  N S 357 
SER C    C  N N 358 
SER O    O  N N 359 
SER CB   C  N N 360 
SER OG   O  N N 361 
SER OXT  O  N N 362 
SER H    H  N N 363 
SER H2   H  N N 364 
SER HA   H  N N 365 
SER HB2  H  N N 366 
SER HB3  H  N N 367 
SER HG   H  N N 368 
SER HXT  H  N N 369 
THR N    N  N N 370 
THR CA   C  N S 371 
THR C    C  N N 372 
THR O    O  N N 373 
THR CB   C  N R 374 
THR OG1  O  N N 375 
THR CG2  C  N N 376 
THR OXT  O  N N 377 
THR H    H  N N 378 
THR H2   H  N N 379 
THR HA   H  N N 380 
THR HB   H  N N 381 
THR HG1  H  N N 382 
THR HG21 H  N N 383 
THR HG22 H  N N 384 
THR HG23 H  N N 385 
THR HXT  H  N N 386 
TRP N    N  N N 387 
TRP CA   C  N S 388 
TRP C    C  N N 389 
TRP O    O  N N 390 
TRP CB   C  N N 391 
TRP CG   C  Y N 392 
TRP CD1  C  Y N 393 
TRP CD2  C  Y N 394 
TRP NE1  N  Y N 395 
TRP CE2  C  Y N 396 
TRP CE3  C  Y N 397 
TRP CZ2  C  Y N 398 
TRP CZ3  C  Y N 399 
TRP CH2  C  Y N 400 
TRP OXT  O  N N 401 
TRP H    H  N N 402 
TRP H2   H  N N 403 
TRP HA   H  N N 404 
TRP HB2  H  N N 405 
TRP HB3  H  N N 406 
TRP HD1  H  N N 407 
TRP HE1  H  N N 408 
TRP HE3  H  N N 409 
TRP HZ2  H  N N 410 
TRP HZ3  H  N N 411 
TRP HH2  H  N N 412 
TRP HXT  H  N N 413 
TYR N    N  N N 414 
TYR CA   C  N S 415 
TYR C    C  N N 416 
TYR O    O  N N 417 
TYR CB   C  N N 418 
TYR CG   C  Y N 419 
TYR CD1  C  Y N 420 
TYR CD2  C  Y N 421 
TYR CE1  C  Y N 422 
TYR CE2  C  Y N 423 
TYR CZ   C  Y N 424 
TYR OH   O  N N 425 
TYR OXT  O  N N 426 
TYR H    H  N N 427 
TYR H2   H  N N 428 
TYR HA   H  N N 429 
TYR HB2  H  N N 430 
TYR HB3  H  N N 431 
TYR HD1  H  N N 432 
TYR HD2  H  N N 433 
TYR HE1  H  N N 434 
TYR HE2  H  N N 435 
TYR HH   H  N N 436 
TYR HXT  H  N N 437 
VAL N    N  N N 438 
VAL CA   C  N S 439 
VAL C    C  N N 440 
VAL O    O  N N 441 
VAL CB   C  N N 442 
VAL CG1  C  N N 443 
VAL CG2  C  N N 444 
VAL OXT  O  N N 445 
VAL H    H  N N 446 
VAL H2   H  N N 447 
VAL HA   H  N N 448 
VAL HB   H  N N 449 
VAL HG11 H  N N 450 
VAL HG12 H  N N 451 
VAL HG13 H  N N 452 
VAL HG21 H  N N 453 
VAL HG22 H  N N 454 
VAL HG23 H  N N 455 
VAL HXT  H  N N 456 
ZN  ZN   ZN N N 457 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
MPO S1  O1   doub N N 237 
MPO S1  O2   doub N N 238 
MPO S1  C1   sing N N 239 
MPO S1  O3   sing N N 240 
MPO O4  C5   sing N N 241 
MPO O4  C6   sing N N 242 
MPO N1  C3   sing N N 243 
MPO N1  C4   sing N N 244 
MPO N1  C7   sing N N 245 
MPO C1  C2   sing N N 246 
MPO C1  H11  sing N N 247 
MPO C1  H12  sing N N 248 
MPO O3  HO3  sing N N 249 
MPO C2  C3   sing N N 250 
MPO C2  H21  sing N N 251 
MPO C2  H22  sing N N 252 
MPO C3  H31  sing N N 253 
MPO C3  H32  sing N N 254 
MPO C4  C5   sing N N 255 
MPO C4  H41  sing N N 256 
MPO C4  H42  sing N N 257 
MPO C5  H51  sing N N 258 
MPO C5  H52  sing N N 259 
MPO C6  C7   sing N N 260 
MPO C6  H61  sing N N 261 
MPO C6  H62  sing N N 262 
MPO C7  H71  sing N N 263 
MPO C7  H72  sing N N 264 
MYC C1  C2   doub Y N 265 
MYC C1  C6   sing Y N 266 
MYC C1  H1   sing N N 267 
MYC C2  C3   sing Y N 268 
MYC C2  O30  sing N N 269 
MYC C3  C4   doub Y N 270 
MYC C3  C9   sing Y N 271 
MYC C4  C5   sing Y N 272 
MYC C4  O12  sing Y N 273 
MYC C5  C6   doub Y N 274 
MYC C5  H5   sing N N 275 
MYC C6  O29  sing N N 276 
MYC C9  C10  sing Y N 277 
MYC C9  O13  doub N N 278 
MYC C10 C11  doub Y N 279 
MYC C10 O27  sing N N 280 
MYC C11 C14  sing Y N 281 
MYC C11 O12  sing Y N 282 
MYC C14 C15  doub Y N 283 
MYC C14 C19  sing Y N 284 
MYC C15 C16  sing Y N 285 
MYC C15 H15  sing N N 286 
MYC C16 C17  doub Y N 287 
MYC C16 O25  sing N N 288 
MYC C17 C18  sing Y N 289 
MYC C17 O24  sing N N 290 
MYC C18 C19  doub Y N 291 
MYC C18 O23  sing N N 292 
MYC C19 H19  sing N N 293 
MYC O23 HO3  sing N N 294 
MYC O24 HO4  sing N N 295 
MYC O25 HO5  sing N N 296 
MYC O27 HO7  sing N N 297 
MYC O29 HO9  sing N N 298 
MYC O30 HO0  sing N N 299 
PHE N   CA   sing N N 300 
PHE N   H    sing N N 301 
PHE N   H2   sing N N 302 
PHE CA  C    sing N N 303 
PHE CA  CB   sing N N 304 
PHE CA  HA   sing N N 305 
PHE C   O    doub N N 306 
PHE C   OXT  sing N N 307 
PHE CB  CG   sing N N 308 
PHE CB  HB2  sing N N 309 
PHE CB  HB3  sing N N 310 
PHE CG  CD1  doub Y N 311 
PHE CG  CD2  sing Y N 312 
PHE CD1 CE1  sing Y N 313 
PHE CD1 HD1  sing N N 314 
PHE CD2 CE2  doub Y N 315 
PHE CD2 HD2  sing N N 316 
PHE CE1 CZ   doub Y N 317 
PHE CE1 HE1  sing N N 318 
PHE CE2 CZ   sing Y N 319 
PHE CE2 HE2  sing N N 320 
PHE CZ  HZ   sing N N 321 
PHE OXT HXT  sing N N 322 
PO4 P   O1   doub N N 323 
PO4 P   O2   sing N N 324 
PO4 P   O3   sing N N 325 
PO4 P   O4   sing N N 326 
PRO N   CA   sing N N 327 
PRO N   CD   sing N N 328 
PRO N   H    sing N N 329 
PRO CA  C    sing N N 330 
PRO CA  CB   sing N N 331 
PRO CA  HA   sing N N 332 
PRO C   O    doub N N 333 
PRO C   OXT  sing N N 334 
PRO CB  CG   sing N N 335 
PRO CB  HB2  sing N N 336 
PRO CB  HB3  sing N N 337 
PRO CG  CD   sing N N 338 
PRO CG  HG2  sing N N 339 
PRO CG  HG3  sing N N 340 
PRO CD  HD2  sing N N 341 
PRO CD  HD3  sing N N 342 
PRO OXT HXT  sing N N 343 
SER N   CA   sing N N 344 
SER N   H    sing N N 345 
SER N   H2   sing N N 346 
SER CA  C    sing N N 347 
SER CA  CB   sing N N 348 
SER CA  HA   sing N N 349 
SER C   O    doub N N 350 
SER C   OXT  sing N N 351 
SER CB  OG   sing N N 352 
SER CB  HB2  sing N N 353 
SER CB  HB3  sing N N 354 
SER OG  HG   sing N N 355 
SER OXT HXT  sing N N 356 
THR N   CA   sing N N 357 
THR N   H    sing N N 358 
THR N   H2   sing N N 359 
THR CA  C    sing N N 360 
THR CA  CB   sing N N 361 
THR CA  HA   sing N N 362 
THR C   O    doub N N 363 
THR C   OXT  sing N N 364 
THR CB  OG1  sing N N 365 
THR CB  CG2  sing N N 366 
THR CB  HB   sing N N 367 
THR OG1 HG1  sing N N 368 
THR CG2 HG21 sing N N 369 
THR CG2 HG22 sing N N 370 
THR CG2 HG23 sing N N 371 
THR OXT HXT  sing N N 372 
TRP N   CA   sing N N 373 
TRP N   H    sing N N 374 
TRP N   H2   sing N N 375 
TRP CA  C    sing N N 376 
TRP CA  CB   sing N N 377 
TRP CA  HA   sing N N 378 
TRP C   O    doub N N 379 
TRP C   OXT  sing N N 380 
TRP CB  CG   sing N N 381 
TRP CB  HB2  sing N N 382 
TRP CB  HB3  sing N N 383 
TRP CG  CD1  doub Y N 384 
TRP CG  CD2  sing Y N 385 
TRP CD1 NE1  sing Y N 386 
TRP CD1 HD1  sing N N 387 
TRP CD2 CE2  doub Y N 388 
TRP CD2 CE3  sing Y N 389 
TRP NE1 CE2  sing Y N 390 
TRP NE1 HE1  sing N N 391 
TRP CE2 CZ2  sing Y N 392 
TRP CE3 CZ3  doub Y N 393 
TRP CE3 HE3  sing N N 394 
TRP CZ2 CH2  doub Y N 395 
TRP CZ2 HZ2  sing N N 396 
TRP CZ3 CH2  sing Y N 397 
TRP CZ3 HZ3  sing N N 398 
TRP CH2 HH2  sing N N 399 
TRP OXT HXT  sing N N 400 
TYR N   CA   sing N N 401 
TYR N   H    sing N N 402 
TYR N   H2   sing N N 403 
TYR CA  C    sing N N 404 
TYR CA  CB   sing N N 405 
TYR CA  HA   sing N N 406 
TYR C   O    doub N N 407 
TYR C   OXT  sing N N 408 
TYR CB  CG   sing N N 409 
TYR CB  HB2  sing N N 410 
TYR CB  HB3  sing N N 411 
TYR CG  CD1  doub Y N 412 
TYR CG  CD2  sing Y N 413 
TYR CD1 CE1  sing Y N 414 
TYR CD1 HD1  sing N N 415 
TYR CD2 CE2  doub Y N 416 
TYR CD2 HD2  sing N N 417 
TYR CE1 CZ   doub Y N 418 
TYR CE1 HE1  sing N N 419 
TYR CE2 CZ   sing Y N 420 
TYR CE2 HE2  sing N N 421 
TYR CZ  OH   sing N N 422 
TYR OH  HH   sing N N 423 
TYR OXT HXT  sing N N 424 
VAL N   CA   sing N N 425 
VAL N   H    sing N N 426 
VAL N   H2   sing N N 427 
VAL CA  C    sing N N 428 
VAL CA  CB   sing N N 429 
VAL CA  HA   sing N N 430 
VAL C   O    doub N N 431 
VAL C   OXT  sing N N 432 
VAL CB  CG1  sing N N 433 
VAL CB  CG2  sing N N 434 
VAL CB  HB   sing N N 435 
VAL CG1 HG11 sing N N 436 
VAL CG1 HG12 sing N N 437 
VAL CG1 HG13 sing N N 438 
VAL CG2 HG21 sing N N 439 
VAL CG2 HG22 sing N N 440 
VAL CG2 HG23 sing N N 441 
VAL OXT HXT  sing N N 442 
# 
_pdbx_audit_support.funding_organization   'German Research Foundation (DFG)' 
_pdbx_audit_support.country                Germany 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6ZSL 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9I1S 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.016856 
_atom_sites.fract_transf_matrix[1][2]   0.006862 
_atom_sites.fract_transf_matrix[1][3]   0.003960 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.015286 
_atom_sites.fract_transf_matrix[2][3]   0.004628 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.012197 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
H  
N  
O  
P  
S  
ZN 
# 
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   . ALA A 1 3   ? 0.532   46.058  -47.653  1.00 117.95 ?  1   ALA A N   1 
ATOM   2    C  CA  . ALA A 1 3   ? 1.260   47.101  -48.366  1.00 119.16 ?  1   ALA A CA  1 
ATOM   3    C  C   . ALA A 1 3   ? 2.717   46.707  -48.592  1.00 121.33 ?  1   ALA A C   1 
ATOM   4    O  O   . ALA A 1 3   ? 3.535   47.533  -48.995  1.00 122.02 ?  1   ALA A O   1 
ATOM   5    C  CB  . ALA A 1 3   ? 1.179   48.419  -47.608  1.00 111.91 ?  1   ALA A CB  1 
ATOM   6    N  N   . VAL A 1 4   ? 3.039   45.442  -48.330  1.00 124.08 ?  2   VAL A N   1 
ATOM   7    C  CA  . VAL A 1 4   ? 4.377   44.902  -48.545  1.00 127.52 ?  2   VAL A CA  1 
ATOM   8    C  C   . VAL A 1 4   ? 4.312   43.892  -49.683  1.00 127.27 ?  2   VAL A C   1 
ATOM   9    O  O   . VAL A 1 4   ? 3.474   42.981  -49.667  1.00 129.72 ?  2   VAL A O   1 
ATOM   10   C  CB  . VAL A 1 4   ? 4.933   44.260  -47.262  1.00 135.34 ?  2   VAL A CB  1 
ATOM   11   C  CG1 . VAL A 1 4   ? 6.323   43.691  -47.506  1.00 140.63 ?  2   VAL A CG1 1 
ATOM   12   C  CG2 . VAL A 1 4   ? 4.952   45.275  -46.129  1.00 135.28 ?  2   VAL A CG2 1 
ATOM   13   N  N   . GLY A 1 5   ? 5.192   44.053  -50.665  1.00 128.70 ?  3   GLY A N   1 
ATOM   14   C  CA  . GLY A 1 5   ? 5.230   43.153  -51.804  1.00 126.12 ?  3   GLY A CA  1 
ATOM   15   C  C   . GLY A 1 5   ? 6.397   43.496  -52.703  1.00 125.71 ?  3   GLY A C   1 
ATOM   16   O  O   . GLY A 1 5   ? 7.216   44.368  -52.395  1.00 125.86 ?  3   GLY A O   1 
ATOM   17   N  N   . ALA A 1 6   ? 6.468   42.787  -53.828  1.00 125.68 ?  4   ALA A N   1 
ATOM   18   C  CA  . ALA A 1 6   ? 7.530   42.982  -54.802  1.00 127.27 ?  4   ALA A CA  1 
ATOM   19   C  C   . ALA A 1 6   ? 6.934   43.313  -56.164  1.00 125.61 ?  4   ALA A C   1 
ATOM   20   O  O   . ALA A 1 6   ? 5.760   43.045  -56.436  1.00 121.51 ?  4   ALA A O   1 
ATOM   21   C  CB  . ALA A 1 6   ? 8.424   41.739  -54.909  1.00 133.07 ?  4   ALA A CB  1 
ATOM   22   N  N   . CYS A 1 7   ? 7.761   43.904  -57.024  1.00 125.75 ?  5   CYS A N   1 
ATOM   23   C  CA  . CYS A 1 7   ? 7.285   44.347  -58.327  1.00 117.46 ?  5   CYS A CA  1 
ATOM   24   C  C   . CYS A 1 7   ? 6.760   43.165  -59.134  1.00 113.66 ?  5   CYS A C   1 
ATOM   25   O  O   . CYS A 1 7   ? 7.307   42.061  -59.074  1.00 119.09 ?  5   CYS A O   1 
ATOM   26   C  CB  . CYS A 1 7   ? 8.403   45.053  -59.090  1.00 113.27 ?  5   CYS A CB  1 
ATOM   27   S  SG  . CYS A 1 7   ? 7.815   45.929  -60.545  1.00 108.40 ?  5   CYS A SG  1 
ATOM   28   N  N   . VAL A 1 8   ? 5.693   43.400  -59.899  1.00 108.40 ?  6   VAL A N   1 
ATOM   29   C  CA  . VAL A 1 8   ? 5.100   42.339  -60.707  1.00 110.82 ?  6   VAL A CA  1 
ATOM   30   C  C   . VAL A 1 8   ? 5.736   42.315  -62.091  1.00 112.08 ?  6   VAL A C   1 
ATOM   31   O  O   . VAL A 1 8   ? 5.201   41.700  -63.020  1.00 113.28 ?  6   VAL A O   1 
ATOM   32   C  CB  . VAL A 1 8   ? 3.571   42.491  -60.812  1.00 105.11 ?  6   VAL A CB  1 
ATOM   33   C  CG1 . VAL A 1 8   ? 2.922   42.312  -59.445  1.00 106.00 ?  6   VAL A CG1 1 
ATOM   34   C  CG2 . VAL A 1 8   ? 3.201   43.830  -61.430  1.00 103.21 ?  6   VAL A CG2 1 
ATOM   35   N  N   . LEU A 1 9   ? 6.876   42.973  -62.238  1.00 113.68 ?  7   LEU A N   1 
ATOM   36   C  CA  . LEU A 1 9   ? 7.588   43.031  -63.512  1.00 112.85 ?  7   LEU A CA  1 
ATOM   37   C  C   . LEU A 1 9   ? 9.044   42.617  -63.373  1.00 118.50 ?  7   LEU A C   1 
ATOM   38   O  O   . LEU A 1 9   ? 9.583   41.969  -64.274  1.00 119.86 ?  7   LEU A O   1 
ATOM   39   C  CB  . LEU A 1 9   ? 7.494   44.442  -64.117  1.00 105.65 ?  7   LEU A CB  1 
ATOM   40   C  CG  . LEU A 1 9   ? 6.078   44.919  -64.447  1.00 99.68  ?  7   LEU A CG  1 
ATOM   41   C  CD1 . LEU A 1 9   ? 6.092   46.332  -65.010  1.00 100.90 ?  7   LEU A CD1 1 
ATOM   42   C  CD2 . LEU A 1 9   ? 5.410   43.961  -65.419  1.00 100.54 ?  7   LEU A CD2 1 
ATOM   43   N  N   . CYS A 1 10  ? 9.691   42.973  -62.264  1.00 119.65 ?  8   CYS A N   1 
ATOM   44   C  CA  . CYS A 1 10  ? 11.088  42.654  -62.026  1.00 126.47 ?  8   CYS A CA  1 
ATOM   45   C  C   . CYS A 1 10  ? 11.283  41.999  -60.668  1.00 131.37 ?  8   CYS A C   1 
ATOM   46   O  O   . CYS A 1 10  ? 12.414  41.637  -60.325  1.00 138.20 ?  8   CYS A O   1 
ATOM   47   C  CB  . CYS A 1 10  ? 11.968  43.908  -62.139  1.00 126.15 ?  8   CYS A CB  1 
ATOM   48   S  SG  . CYS A 1 10  ? 11.634  45.174  -60.912  1.00 127.23 ?  8   CYS A SG  1 
ATOM   49   N  N   . ASN A 1 11  ? 10.210  41.835  -59.893  1.00 128.86 ?  9   ASN A N   1 
ATOM   50   C  CA  . ASN A 1 11  ? 10.213  41.182  -58.589  1.00 133.53 ?  9   ASN A CA  1 
ATOM   51   C  C   . ASN A 1 11  ? 11.012  41.948  -57.539  1.00 136.13 ?  9   ASN A C   1 
ATOM   52   O  O   . ASN A 1 11  ? 11.474  41.354  -56.559  1.00 142.31 ?  9   ASN A O   1 
ATOM   53   C  CB  . ASN A 1 11  ? 10.730  39.743  -58.702  1.00 140.56 ?  9   ASN A CB  1 
ATOM   54   C  CG  . ASN A 1 11  ? 10.212  38.849  -57.593  1.00 144.26 ?  9   ASN A CG  1 
ATOM   55   O  OD1 . ASN A 1 11  ? 9.006   38.641  -57.463  1.00 140.67 ?  9   ASN A OD1 1 
ATOM   56   N  ND2 . ASN A 1 11  ? 11.122  38.311  -56.791  1.00 152.03 ?  9   ASN A ND2 1 
ATOM   57   N  N   . SER A 1 12  ? 11.187  43.257  -57.717  1.00 135.86 ?  10  SER A N   1 
ATOM   58   C  CA  . SER A 1 12  ? 11.853  44.085  -56.717  1.00 133.75 ?  10  SER A CA  1 
ATOM   59   C  C   . SER A 1 12  ? 10.856  44.505  -55.641  1.00 130.64 ?  10  SER A C   1 
ATOM   60   O  O   . SER A 1 12  ? 9.833   45.131  -55.942  1.00 131.07 ?  10  SER A O   1 
ATOM   61   C  CB  . SER A 1 12  ? 12.488  45.313  -57.369  1.00 131.06 ?  10  SER A CB  1 
ATOM   62   O  OG  . SER A 1 12  ? 13.494  44.943  -58.296  1.00 135.08 ?  10  SER A OG  1 
ATOM   63   N  N   . GLN A 1 13  ? 11.152  44.151  -54.392  1.00 135.68 ?  11  GLN A N   1 
ATOM   64   C  CA  . GLN A 1 13  ? 10.249  44.435  -53.284  1.00 133.81 ?  11  GLN A CA  1 
ATOM   65   C  C   . GLN A 1 13  ? 10.015  45.937  -53.156  1.00 131.25 ?  11  GLN A C   1 
ATOM   66   O  O   . GLN A 1 13  ? 10.920  46.744  -53.388  1.00 133.01 ?  11  GLN A O   1 
ATOM   67   C  CB  . GLN A 1 13  ? 10.826  43.871  -51.984  1.00 141.52 ?  11  GLN A CB  1 
ATOM   68   C  CG  . GLN A 1 13  ? 10.842  42.348  -51.936  1.00 147.68 ?  11  GLN A CG  1 
ATOM   69   C  CD  . GLN A 1 13  ? 9.626   41.757  -51.250  1.00 149.33 ?  11  GLN A CD  1 
ATOM   70   O  OE1 . GLN A 1 13  ? 8.810   42.477  -50.675  1.00 145.34 ?  11  GLN A OE1 1 
ATOM   71   N  NE2 . GLN A 1 13  ? 9.492   40.436  -51.321  1.00 152.13 ?  11  GLN A NE2 1 
ATOM   72   N  N   . THR A 1 14  ? 8.790   46.314  -52.804  1.00 129.13 ?  12  THR A N   1 
ATOM   73   C  CA  . THR A 1 14  ? 8.448   47.720  -52.618  1.00 121.35 ?  12  THR A CA  1 
ATOM   74   C  C   . THR A 1 14  ? 7.173   47.782  -51.774  1.00 118.01 ?  12  THR A C   1 
ATOM   75   O  O   . THR A 1 14  ? 6.739   46.777  -51.201  1.00 120.01 ?  12  THR A O   1 
ATOM   76   C  CB  . THR A 1 14  ? 8.320   48.412  -53.984  1.00 123.21 ?  12  THR A CB  1 
ATOM   77   O  OG1 . THR A 1 14  ? 9.566   48.306  -54.683  1.00 129.01 ?  12  THR A OG1 1 
ATOM   78   C  CG2 . THR A 1 14  ? 8.004   49.896  -53.839  1.00 119.48 ?  12  THR A CG2 1 
ATOM   79   N  N   . SER A 1 15  ? 6.575   48.970  -51.692  1.00 115.25 ?  13  SER A N   1 
ATOM   80   C  CA  . SER A 1 15  ? 5.316   49.191  -50.997  1.00 111.03 ?  13  SER A CA  1 
ATOM   81   C  C   . SER A 1 15  ? 4.341   49.969  -51.865  1.00 114.28 ?  13  SER A C   1 
ATOM   82   O  O   . SER A 1 15  ? 3.255   50.327  -51.395  1.00 111.11 ?  13  SER A O   1 
ATOM   83   C  CB  . SER A 1 15  ? 5.537   49.945  -49.677  1.00 110.45 ?  13  SER A CB  1 
ATOM   84   O  OG  . SER A 1 15  ? 4.303   50.215  -49.032  1.00 114.63 ?  13  SER A OG  1 
ATOM   85   N  N   . LEU A 1 16  ? 4.708   50.240  -53.112  1.00 108.31 ?  14  LEU A N   1 
ATOM   86   C  CA  . LEU A 1 16  ? 3.902   51.028  -54.027  1.00 104.46 ?  14  LEU A CA  1 
ATOM   87   C  C   . LEU A 1 16  ? 2.963   50.119  -54.807  1.00 102.68 ?  14  LEU A C   1 
ATOM   88   O  O   . LEU A 1 16  ? 3.395   49.125  -55.400  1.00 103.37 ?  14  LEU A O   1 
ATOM   89   C  CB  . LEU A 1 16  ? 4.802   51.805  -54.988  1.00 105.18 ?  14  LEU A CB  1 
ATOM   90   C  CG  . LEU A 1 16  ? 5.768   52.797  -54.341  1.00 95.97  ?  14  LEU A CG  1 
ATOM   91   C  CD1 . LEU A 1 16  ? 6.533   53.566  -55.405  1.00 95.77  ?  14  LEU A CD1 1 
ATOM   92   C  CD2 . LEU A 1 16  ? 5.022   53.746  -53.416  1.00 94.34  ?  14  LEU A CD2 1 
ATOM   93   N  N   . ARG A 1 17  ? 1.681   50.458  -54.788  1.00 101.93 ?  15  ARG A N   1 
ATOM   94   C  CA  . ARG A 1 17  ? 0.648   49.741  -55.515  1.00 93.80  ?  15  ARG A CA  1 
ATOM   95   C  C   . ARG A 1 17  ? -0.067  50.744  -56.401  1.00 90.69  ?  15  ARG A C   1 
ATOM   96   O  O   . ARG A 1 17  ? -0.260  51.898  -56.008  1.00 85.93  ?  15  ARG A O   1 
ATOM   97   C  CB  . ARG A 1 17  ? -0.365  49.099  -54.571  1.00 90.54  ?  15  ARG A CB  1 
ATOM   98   C  CG  . ARG A 1 17  ? 0.149   47.963  -53.722  1.00 101.08 ?  15  ARG A CG  1 
ATOM   99   C  CD  . ARG A 1 17  ? -0.946  47.566  -52.755  1.00 103.80 ?  15  ARG A CD  1 
ATOM   100  N  NE  . ARG A 1 17  ? -1.321  48.716  -51.941  1.00 109.51 ?  15  ARG A NE  1 
ATOM   101  C  CZ  . ARG A 1 17  ? -2.292  48.726  -51.039  1.00 104.45 ?  15  ARG A CZ  1 
ATOM   102  N  NH1 . ARG A 1 17  ? -3.204  47.769  -50.993  1.00 99.30  ?  15  ARG A NH1 1 
ATOM   103  N  NH2 . ARG A 1 17  ? -2.402  49.768  -50.219  1.00 96.64  ?  15  ARG A NH2 1 
ATOM   104  N  N   . CYS A 1 18  ? -0.463  50.316  -57.591  1.00 89.36  ?  16  CYS A N   1 
ATOM   105  C  CA  . CYS A 1 18  ? -1.227  51.203  -58.449  1.00 79.97  ?  16  CYS A CA  1 
ATOM   106  C  C   . CYS A 1 18  ? -2.685  51.187  -58.012  1.00 79.92  ?  16  CYS A C   1 
ATOM   107  O  O   . CYS A 1 18  ? -3.285  50.118  -57.861  1.00 78.39  ?  16  CYS A O   1 
ATOM   108  C  CB  . CYS A 1 18  ? -1.101  50.798  -59.913  1.00 77.34  ?  16  CYS A CB  1 
ATOM   109  S  SG  . CYS A 1 18  ? -1.980  51.931  -60.994  1.00 73.95  ?  16  CYS A SG  1 
ATOM   110  N  N   . GLY A 1 19  ? -3.256  52.373  -57.823  1.00 80.88  ?  17  GLY A N   1 
ATOM   111  C  CA  . GLY A 1 19  ? -4.630  52.483  -57.393  1.00 80.30  ?  17  GLY A CA  1 
ATOM   112  C  C   . GLY A 1 19  ? -5.623  52.608  -58.518  1.00 81.82  ?  17  GLY A C   1 
ATOM   113  O  O   . GLY A 1 19  ? -6.823  52.763  -58.270  1.00 87.25  ?  17  GLY A O   1 
ATOM   114  N  N   . ALA A 1 20  ? -5.150  52.542  -59.760  1.00 73.76  ?  18  ALA A N   1 
ATOM   115  C  CA  . ALA A 1 20  ? -6.009  52.566  -60.933  1.00 79.96  ?  18  ALA A CA  1 
ATOM   116  C  C   . ALA A 1 20  ? -6.212  51.181  -61.526  1.00 75.41  ?  18  ALA A C   1 
ATOM   117  O  O   . ALA A 1 20  ? -7.280  50.909  -62.085  1.00 78.66  ?  18  ALA A O   1 
ATOM   118  C  CB  . ALA A 1 20  ? -5.435  53.504  -61.999  1.00 75.63  ?  18  ALA A CB  1 
ATOM   119  N  N   . CYS A 1 21  ? -5.210  50.307  -61.420  1.00 73.26  ?  19  CYS A N   1 
ATOM   120  C  CA  . CYS A 1 21  ? -5.377  48.918  -61.829  1.00 77.54  ?  19  CYS A CA  1 
ATOM   121  C  C   . CYS A 1 21  ? -6.439  48.247  -60.971  1.00 75.83  ?  19  CYS A C   1 
ATOM   122  O  O   . CYS A 1 21  ? -6.471  48.416  -59.749  1.00 84.30  ?  19  CYS A O   1 
ATOM   123  C  CB  . CYS A 1 21  ? -4.061  48.146  -61.688  1.00 76.26  ?  19  CYS A CB  1 
ATOM   124  S  SG  . CYS A 1 21  ? -2.761  48.506  -62.884  1.00 75.46  ?  19  CYS A SG  1 
ATOM   125  N  N   . ILE A 1 22  ? -7.314  47.473  -61.615  1.00 80.54  ?  20  ILE A N   1 
ATOM   126  C  CA  . ILE A 1 22  ? -8.401  46.845  -60.878  1.00 81.74  ?  20  ILE A CA  1 
ATOM   127  C  C   . ILE A 1 22  ? -7.885  45.798  -59.899  1.00 86.76  ?  20  ILE A C   1 
ATOM   128  O  O   . ILE A 1 22  ? -8.587  45.451  -58.943  1.00 85.05  ?  20  ILE A O   1 
ATOM   129  C  CB  . ILE A 1 22  ? -9.426  46.231  -61.849  1.00 79.17  ?  20  ILE A CB  1 
ATOM   130  C  CG1 . ILE A 1 22  ? -10.758 45.998  -61.134  1.00 85.58  ?  20  ILE A CG1 1 
ATOM   131  C  CG2 . ILE A 1 22  ? -8.895  44.934  -62.433  1.00 81.01  ?  20  ILE A CG2 1 
ATOM   132  C  CD1 . ILE A 1 22  ? -11.381 47.264  -60.579  1.00 88.07  ?  20  ILE A CD1 1 
ATOM   133  N  N   . ARG A 1 23  ? -6.670  45.286  -60.104  1.00 83.54  ?  21  ARG A N   1 
ATOM   134  C  CA  . ARG A 1 23  ? -6.084  44.290  -59.216  1.00 87.69  ?  21  ARG A CA  1 
ATOM   135  C  C   . ARG A 1 23  ? -5.026  44.875  -58.289  1.00 91.85  ?  21  ARG A C   1 
ATOM   136  O  O   . ARG A 1 23  ? -4.397  44.124  -57.537  1.00 95.57  ?  21  ARG A O   1 
ATOM   137  C  CB  . ARG A 1 23  ? -5.482  43.140  -60.030  1.00 89.55  ?  21  ARG A CB  1 
ATOM   138  C  CG  . ARG A 1 23  ? -6.495  42.393  -60.882  1.00 89.58  ?  21  ARG A CG  1 
ATOM   139  C  CD  . ARG A 1 23  ? -7.780  42.109  -60.116  1.00 91.39  ?  21  ARG A CD  1 
ATOM   140  N  NE  . ARG A 1 23  ? -7.563  41.262  -58.949  1.00 96.06  ?  21  ARG A NE  1 
ATOM   141  C  CZ  . ARG A 1 23  ? -8.528  40.832  -58.147  1.00 98.98  ?  21  ARG A CZ  1 
ATOM   142  N  NH1 . ARG A 1 23  ? -9.760  41.305  -58.233  1.00 97.63  ?  21  ARG A NH1 1 
ATOM   143  N  NH2 . ARG A 1 23  ? -8.236  39.947  -57.199  1.00 103.90 ?  21  ARG A NH2 1 
ATOM   144  N  N   . ARG A 1 24  ? -4.831  46.193  -58.318  1.00 86.91  ?  22  ARG A N   1 
ATOM   145  C  CA  . ARG A 1 24  ? -3.907  46.927  -57.457  1.00 85.65  ?  22  ARG A CA  1 
ATOM   146  C  C   . ARG A 1 24  ? -2.595  46.160  -57.246  1.00 90.87  ?  22  ARG A C   1 
ATOM   147  O  O   . ARG A 1 24  ? -2.260  45.795  -56.115  1.00 92.41  ?  22  ARG A O   1 
ATOM   148  C  CB  . ARG A 1 24  ? -4.569  47.257  -56.124  1.00 86.49  ?  22  ARG A CB  1 
ATOM   149  C  CG  . ARG A 1 24  ? -5.788  48.149  -56.300  1.00 89.05  ?  22  ARG A CG  1 
ATOM   150  C  CD  . ARG A 1 24  ? -6.453  48.524  -54.990  1.00 90.40  ?  22  ARG A CD  1 
ATOM   151  N  NE  . ARG A 1 24  ? -7.666  49.297  -55.232  1.00 90.31  ?  22  ARG A NE  1 
ATOM   152  C  CZ  . ARG A 1 24  ? -8.468  49.764  -54.284  1.00 99.63  ?  22  ARG A CZ  1 
ATOM   153  N  NH1 . ARG A 1 24  ? -8.152  49.668  -53.002  1.00 95.05  ?  22  ARG A NH1 1 
ATOM   154  N  NH2 . ARG A 1 24  ? -9.598  50.374  -54.632  1.00 96.29  ?  22  ARG A NH2 1 
ATOM   155  N  N   . PRO A 1 25  ? -1.831  45.924  -58.309  1.00 88.38  ?  23  PRO A N   1 
ATOM   156  C  CA  . PRO A 1 25  ? -0.584  45.163  -58.179  1.00 92.37  ?  23  PRO A CA  1 
ATOM   157  C  C   . PRO A 1 25  ? 0.498   45.973  -57.484  1.00 96.95  ?  23  PRO A C   1 
ATOM   158  O  O   . PRO A 1 25  ? 0.399   47.188  -57.298  1.00 94.35  ?  23  PRO A O   1 
ATOM   159  C  CB  . PRO A 1 25  ? -0.207  44.870  -59.632  1.00 91.28  ?  23  PRO A CB  1 
ATOM   160  C  CG  . PRO A 1 25  ? -0.734  46.062  -60.366  1.00 87.36  ?  23  PRO A CG  1 
ATOM   161  C  CD  . PRO A 1 25  ? -2.049  46.379  -59.693  1.00 84.71  ?  23  PRO A CD  1 
ATOM   162  N  N   . PHE A 1 26  ? 1.555   45.266  -57.095  1.00 104.33 ?  24  PHE A N   1 
ATOM   163  C  CA  . PHE A 1 26  ? 2.712   45.884  -56.466  1.00 99.56  ?  24  PHE A CA  1 
ATOM   164  C  C   . PHE A 1 26  ? 3.726   46.221  -57.552  1.00 101.20 ?  24  PHE A C   1 
ATOM   165  O  O   . PHE A 1 26  ? 4.030   45.382  -58.405  1.00 113.30 ?  24  PHE A O   1 
ATOM   166  C  CB  . PHE A 1 26  ? 3.330   44.942  -55.431  1.00 109.12 ?  24  PHE A CB  1 
ATOM   167  C  CG  . PHE A 1 26  ? 2.751   45.086  -54.051  1.00 111.08 ?  24  PHE A CG  1 
ATOM   168  C  CD1 . PHE A 1 26  ? 3.281   45.996  -53.152  1.00 113.57 ?  24  PHE A CD1 1 
ATOM   169  C  CD2 . PHE A 1 26  ? 1.678   44.305  -53.652  1.00 110.86 ?  24  PHE A CD2 1 
ATOM   170  C  CE1 . PHE A 1 26  ? 2.750   46.127  -51.881  1.00 116.53 ?  24  PHE A CE1 1 
ATOM   171  C  CE2 . PHE A 1 26  ? 1.144   44.431  -52.383  1.00 110.59 ?  24  PHE A CE2 1 
ATOM   172  C  CZ  . PHE A 1 26  ? 1.680   45.343  -51.497  1.00 115.57 ?  24  PHE A CZ  1 
ATOM   173  N  N   . LEU A 1 27  ? 4.244   47.447  -57.523  1.00 101.70 ?  25  LEU A N   1 
ATOM   174  C  CA  . LEU A 1 27  ? 5.225   47.898  -58.500  1.00 104.18 ?  25  LEU A CA  1 
ATOM   175  C  C   . LEU A 1 27  ? 6.429   48.474  -57.770  1.00 104.74 ?  25  LEU A C   1 
ATOM   176  O  O   . LEU A 1 27  ? 6.280   49.114  -56.725  1.00 102.07 ?  25  LEU A O   1 
ATOM   177  C  CB  . LEU A 1 27  ? 4.633   48.965  -59.438  1.00 96.26  ?  25  LEU A CB  1 
ATOM   178  C  CG  . LEU A 1 27  ? 3.657   48.546  -60.543  1.00 96.99  ?  25  LEU A CG  1 
ATOM   179  C  CD1 . LEU A 1 27  ? 4.209   47.392  -61.368  1.00 99.90  ?  25  LEU A CD1 1 
ATOM   180  C  CD2 . LEU A 1 27  ? 2.286   48.206  -59.972  1.00 93.15  ?  25  LEU A CD2 1 
ATOM   181  N  N   . CYS A 1 28  ? 7.622   48.255  -58.322  1.00 109.08 ?  26  CYS A N   1 
ATOM   182  C  CA  . CYS A 1 28  ? 8.808   48.877  -57.754  1.00 109.84 ?  26  CYS A CA  1 
ATOM   183  C  C   . CYS A 1 28  ? 8.831   50.350  -58.142  1.00 110.78 ?  26  CYS A C   1 
ATOM   184  O  O   . CYS A 1 28  ? 7.910   50.872  -58.778  1.00 105.63 ?  26  CYS A O   1 
ATOM   185  C  CB  . CYS A 1 28  ? 10.092  48.220  -58.244  1.00 111.21 ?  26  CYS A CB  1 
ATOM   186  S  SG  . CYS A 1 28  ? 10.258  48.219  -60.019  1.00 123.54 ?  26  CYS A SG  1 
ATOM   187  N  N   . CYS A 1 29  ? 9.910   51.031  -57.763  1.00 105.32 ?  27  CYS A N   1 
ATOM   188  C  CA  . CYS A 1 29  ? 9.989   52.463  -58.008  1.00 103.58 ?  27  CYS A CA  1 
ATOM   189  C  C   . CYS A 1 29  ? 10.344  52.771  -59.459  1.00 101.58 ?  27  CYS A C   1 
ATOM   190  O  O   . CYS A 1 29  ? 9.954   53.824  -59.975  1.00 99.09  ?  27  CYS A O   1 
ATOM   191  C  CB  . CYS A 1 29  ? 11.017  53.093  -57.066  1.00 108.33 ?  27  CYS A CB  1 
ATOM   192  S  SG  . CYS A 1 29  ? 10.644  52.878  -55.307  1.00 113.04 ?  27  CYS A SG  1 
ATOM   193  N  N   . LYS A 1 30  ? 11.054  51.865  -60.140  1.00 103.10 ?  28  LYS A N   1 
ATOM   194  C  CA  . LYS A 1 30  ? 11.478  52.146  -61.508  1.00 103.07 ?  28  LYS A CA  1 
ATOM   195  C  C   . LYS A 1 30  ? 10.364  51.883  -62.511  1.00 110.08 ?  28  LYS A C   1 
ATOM   196  O  O   . LYS A 1 30  ? 10.267  52.586  -63.524  1.00 104.61 ?  28  LYS A O   1 
ATOM   197  C  CB  . LYS A 1 30  ? 12.709  51.310  -61.863  1.00 109.68 ?  28  LYS A CB  1 
ATOM   198  N  N   . CYS A 1 31  ? 9.511   50.896  -62.239  1.00 109.97 ?  29  CYS A N   1 
ATOM   199  C  CA  . CYS A 1 31  ? 8.456   50.503  -63.164  1.00 102.56 ?  29  CYS A CA  1 
ATOM   200  C  C   . CYS A 1 31  ? 7.197   51.328  -62.931  1.00 96.09  ?  29  CYS A C   1 
ATOM   201  O  O   . CYS A 1 31  ? 6.499   51.679  -63.889  1.00 92.97  ?  29  CYS A O   1 
ATOM   202  C  CB  . CYS A 1 31  ? 8.168   49.001  -63.042  1.00 104.24 ?  29  CYS A CB  1 
ATOM   203  S  SG  . CYS A 1 31  ? 9.605   47.912  -63.371  1.00 117.35 ?  29  CYS A SG  1 
ATOM   204  N  N   . CYS A 1 32  ? 6.889   51.628  -61.664  1.00 94.97  ?  30  CYS A N   1 
ATOM   205  C  CA  . CYS A 1 32  ? 5.762   52.499  -61.354  1.00 93.32  ?  30  CYS A CA  1 
ATOM   206  C  C   . CYS A 1 32  ? 5.833   53.784  -62.164  1.00 90.36  ?  30  CYS A C   1 
ATOM   207  O  O   . CYS A 1 32  ? 4.799   54.338  -62.555  1.00 80.96  ?  30  CYS A O   1 
ATOM   208  C  CB  . CYS A 1 32  ? 5.744   52.818  -59.857  1.00 89.47  ?  30  CYS A CB  1 
ATOM   209  S  SG  . CYS A 1 32  ? 4.139   53.309  -59.189  1.00 89.62  ?  30  CYS A SG  1 
ATOM   210  N  N   . TYR A 1 33  ? 7.050   54.263  -62.437  1.00 93.82  ?  31  TYR A N   1 
ATOM   211  C  CA  . TYR A 1 33  ? 7.220   55.498  -63.191  1.00 92.78  ?  31  TYR A CA  1 
ATOM   212  C  C   . TYR A 1 33  ? 6.718   55.340  -64.617  1.00 87.41  ?  31  TYR A C   1 
ATOM   213  O  O   . TYR A 1 33  ? 6.206   56.298  -65.206  1.00 84.67  ?  31  TYR A O   1 
ATOM   214  C  CB  . TYR A 1 33  ? 8.693   55.901  -63.174  1.00 92.95  ?  31  TYR A CB  1 
ATOM   215  C  CG  . TYR A 1 33  ? 9.024   57.153  -63.947  1.00 92.73  ?  31  TYR A CG  1 
ATOM   216  C  CD1 . TYR A 1 33  ? 8.825   58.410  -63.393  1.00 91.07  ?  31  TYR A CD1 1 
ATOM   217  C  CD2 . TYR A 1 33  ? 9.558   57.076  -65.226  1.00 95.03  ?  31  TYR A CD2 1 
ATOM   218  C  CE1 . TYR A 1 33  ? 9.136   59.557  -64.100  1.00 90.72  ?  31  TYR A CE1 1 
ATOM   219  C  CE2 . TYR A 1 33  ? 9.874   58.214  -65.938  1.00 93.85  ?  31  TYR A CE2 1 
ATOM   220  C  CZ  . TYR A 1 33  ? 9.661   59.451  -65.372  1.00 91.32  ?  31  TYR A CZ  1 
ATOM   221  O  OH  . TYR A 1 33  ? 9.977   60.586  -66.082  1.00 92.16  ?  31  TYR A OH  1 
ATOM   222  N  N   . ASP A 1 34  ? 6.832   54.140  -65.177  1.00 91.20  ?  32  ASP A N   1 
ATOM   223  C  CA  . ASP A 1 34  ? 6.429   53.917  -66.556  1.00 90.25  ?  32  ASP A CA  1 
ATOM   224  C  C   . ASP A 1 34  ? 4.942   53.619  -66.644  1.00 86.68  ?  32  ASP A C   1 
ATOM   225  O  O   . ASP A 1 34  ? 4.304   53.968  -67.643  1.00 93.26  ?  32  ASP A O   1 
ATOM   226  C  CB  . ASP A 1 34  ? 7.283   52.824  -67.198  1.00 94.81  ?  32  ASP A CB  1 
ATOM   227  C  CG  . ASP A 1 34  ? 8.693   53.310  -67.503  1.00 102.15 ?  32  ASP A CG  1 
ATOM   228  O  OD1 . ASP A 1 34  ? 8.821   54.303  -68.255  1.00 102.32 ?  32  ASP A OD1 1 
ATOM   229  O  OD2 . ASP A 1 34  ? 9.668   52.722  -66.992  1.00 102.42 -1 32  ASP A OD2 1 
ATOM   230  N  N   . HIS A 1 35  ? 4.374   52.981  -65.620  1.00 83.38  ?  33  HIS A N   1 
ATOM   231  C  CA  . HIS A 1 35  ? 2.928   52.816  -65.596  1.00 85.27  ?  33  HIS A CA  1 
ATOM   232  C  C   . HIS A 1 35  ? 2.269   54.189  -65.564  1.00 76.33  ?  33  HIS A C   1 
ATOM   233  O  O   . HIS A 1 35  ? 1.366   54.480  -66.356  1.00 73.83  ?  33  HIS A O   1 
ATOM   234  C  CB  . HIS A 1 35  ? 2.517   51.974  -64.383  1.00 80.80  ?  33  HIS A CB  1 
ATOM   235  C  CG  . HIS A 1 35  ? 1.066   51.602  -64.354  1.00 73.98  ?  33  HIS A CG  1 
ATOM   236  N  ND1 . HIS A 1 35  ? 0.317   51.421  -65.497  1.00 72.76  ?  33  HIS A ND1 1 
ATOM   237  C  CD2 . HIS A 1 35  ? 0.231   51.363  -63.316  1.00 73.55  ?  33  HIS A CD2 1 
ATOM   238  C  CE1 . HIS A 1 35  ? -0.919  51.095  -65.163  1.00 71.61  ?  33  HIS A CE1 1 
ATOM   239  N  NE2 . HIS A 1 35  ? -0.997  51.051  -63.846  1.00 72.08  ?  33  HIS A NE2 1 
ATOM   240  N  N   . VAL A 1 36  ? 2.743   55.061  -64.670  1.00 76.50  ?  34  VAL A N   1 
ATOM   241  C  CA  . VAL A 1 36  ? 2.092   56.349  -64.457  1.00 76.78  ?  34  VAL A CA  1 
ATOM   242  C  C   . VAL A 1 36  ? 2.395   57.338  -65.582  1.00 72.83  ?  34  VAL A C   1 
ATOM   243  O  O   . VAL A 1 36  ? 1.536   58.153  -65.936  1.00 69.25  ?  34  VAL A O   1 
ATOM   244  C  CB  . VAL A 1 36  ? 2.497   56.934  -63.095  1.00 74.82  ?  34  VAL A CB  1 
ATOM   245  C  CG1 . VAL A 1 36  ? 1.926   58.331  -62.937  1.00 78.56  ?  34  VAL A CG1 1 
ATOM   246  C  CG2 . VAL A 1 36  ? 2.016   56.034  -61.970  1.00 76.63  ?  34  VAL A CG2 1 
ATOM   247  N  N   . ILE A 1 37  ? 3.603   57.304  -66.159  1.00 74.99  ?  35  ILE A N   1 
ATOM   248  C  CA  . ILE A 1 37  ? 3.977   58.305  -67.158  1.00 79.72  ?  35  ILE A CA  1 
ATOM   249  C  C   . ILE A 1 37  ? 3.636   57.878  -68.579  1.00 83.69  ?  35  ILE A C   1 
ATOM   250  O  O   . ILE A 1 37  ? 3.843   58.660  -69.517  1.00 86.44  ?  35  ILE A O   1 
ATOM   251  C  CB  . ILE A 1 37  ? 5.474   58.670  -67.057  1.00 85.17  ?  35  ILE A CB  1 
ATOM   252  C  CG1 . ILE A 1 37  ? 5.666   60.162  -67.345  1.00 85.97  ?  35  ILE A CG1 1 
ATOM   253  C  CG2 . ILE A 1 37  ? 6.306   57.820  -68.003  1.00 89.66  ?  35  ILE A CG2 1 
ATOM   254  C  CD1 . ILE A 1 37  ? 7.096   60.635  -67.238  1.00 92.07  ?  35  ILE A CD1 1 
ATOM   255  N  N   . SER A 1 38  ? 3.108   56.668  -68.769  1.00 81.75  ?  36  SER A N   1 
ATOM   256  C  CA  . SER A 1 38  ? 2.752   56.167  -70.088  1.00 80.29  ?  36  SER A CA  1 
ATOM   257  C  C   . SER A 1 38  ? 1.279   55.820  -70.222  1.00 82.59  ?  36  SER A C   1 
ATOM   258  O  O   . SER A 1 38  ? 0.805   55.640  -71.349  1.00 84.24  ?  36  SER A O   1 
ATOM   259  C  CB  . SER A 1 38  ? 3.583   54.922  -70.444  1.00 77.44  ?  36  SER A CB  1 
ATOM   260  O  OG  . SER A 1 38  ? 4.949   55.103  -70.116  1.00 91.83  ?  36  SER A OG  1 
ATOM   261  N  N   . THR A 1 39  ? 0.555   55.703  -69.116  1.00 76.78  ?  37  THR A N   1 
ATOM   262  C  CA  . THR A 1 39  ? -0.860  55.369  -69.102  1.00 73.53  ?  37  THR A CA  1 
ATOM   263  C  C   . THR A 1 39  ? -1.644  56.525  -68.482  1.00 73.01  ?  37  THR A C   1 
ATOM   264  O  O   . THR A 1 39  ? -1.120  57.621  -68.265  1.00 69.01  ?  37  THR A O   1 
ATOM   265  C  CB  . THR A 1 39  ? -1.103  54.070  -68.329  1.00 72.13  ?  37  THR A CB  1 
ATOM   266  O  OG1 . THR A 1 39  ? -0.975  54.321  -66.924  1.00 75.75  ?  37  THR A OG1 1 
ATOM   267  C  CG2 . THR A 1 39  ? -0.091  53.012  -68.736  1.00 70.50  ?  37  THR A CG2 1 
ATOM   268  N  N   . SER A 1 40  ? -2.913  56.261  -68.192  1.00 73.50  ?  38  SER A N   1 
ATOM   269  C  CA  . SER A 1 40  ? -3.783  57.214  -67.523  1.00 71.90  ?  38  SER A CA  1 
ATOM   270  C  C   . SER A 1 40  ? -3.835  56.950  -66.027  1.00 69.85  ?  38  SER A C   1 
ATOM   271  O  O   . SER A 1 40  ? -4.550  57.650  -65.303  1.00 66.46  ?  38  SER A O   1 
ATOM   272  C  CB  . SER A 1 40  ? -5.194  57.155  -68.119  1.00 72.85  ?  38  SER A CB  1 
ATOM   273  O  OG  . SER A 1 40  ? -5.780  55.880  -67.913  1.00 63.89  ?  38  SER A OG  1 
ATOM   274  N  N   . HIS A 1 41  ? -3.088  55.952  -65.562  1.00 64.83  ?  39  HIS A N   1 
ATOM   275  C  CA  . HIS A 1 41  ? -3.070  55.533  -64.167  1.00 70.37  ?  39  HIS A CA  1 
ATOM   276  C  C   . HIS A 1 41  ? -2.097  56.420  -63.400  1.00 68.62  ?  39  HIS A C   1 
ATOM   277  O  O   . HIS A 1 41  ? -0.881  56.341  -63.606  1.00 66.40  ?  39  HIS A O   1 
ATOM   278  C  CB  . HIS A 1 41  ? -2.660  54.067  -64.079  1.00 69.86  ?  39  HIS A CB  1 
ATOM   279  C  CG  . HIS A 1 41  ? -3.682  53.120  -64.626  1.00 71.46  ?  39  HIS A CG  1 
ATOM   280  N  ND1 . HIS A 1 41  ? -3.820  51.828  -64.169  1.00 73.44  ?  39  HIS A ND1 1 
ATOM   281  C  CD2 . HIS A 1 41  ? -4.622  53.280  -65.588  1.00 72.10  ?  39  HIS A CD2 1 
ATOM   282  C  CE1 . HIS A 1 41  ? -4.795  51.230  -64.828  1.00 69.80  ?  39  HIS A CE1 1 
ATOM   283  N  NE2 . HIS A 1 41  ? -5.299  52.089  -65.694  1.00 74.61  ?  39  HIS A NE2 1 
ATOM   284  N  N   . LYS A 1 42  ? -2.621  57.258  -62.508  1.00 67.27  ?  40  LYS A N   1 
ATOM   285  C  CA  . LYS A 1 42  ? -1.797  58.223  -61.800  1.00 72.23  ?  40  LYS A CA  1 
ATOM   286  C  C   . LYS A 1 42  ? -1.876  58.088  -60.286  1.00 70.84  ?  40  LYS A C   1 
ATOM   287  O  O   . LYS A 1 42  ? -1.029  58.657  -59.589  1.00 66.70  ?  40  LYS A O   1 
ATOM   288  C  CB  . LYS A 1 42  ? -2.193  59.655  -62.199  1.00 68.36  ?  40  LYS A CB  1 
ATOM   289  C  CG  . LYS A 1 42  ? -2.280  59.883  -63.708  1.00 64.10  ?  40  LYS A CG  1 
ATOM   290  C  CD  . LYS A 1 42  ? -0.919  59.913  -64.387  1.00 70.88  ?  40  LYS A CD  1 
ATOM   291  C  CE  . LYS A 1 42  ? -1.074  60.102  -65.894  1.00 70.97  ?  40  LYS A CE  1 
ATOM   292  N  NZ  . LYS A 1 42  ? 0.228   60.100  -66.616  1.00 77.81  ?  40  LYS A NZ  1 
ATOM   293  N  N   . LEU A 1 43  ? -2.859  57.359  -59.762  1.00 74.08  ?  41  LEU A N   1 
ATOM   294  C  CA  . LEU A 1 43  ? -2.963  57.105  -58.329  1.00 76.90  ?  41  LEU A CA  1 
ATOM   295  C  C   . LEU A 1 43  ? -1.999  56.001  -57.907  1.00 78.17  ?  41  LEU A C   1 
ATOM   296  O  O   . LEU A 1 43  ? -2.102  54.864  -58.379  1.00 75.77  ?  41  LEU A O   1 
ATOM   297  C  CB  . LEU A 1 43  ? -4.395  56.724  -57.964  1.00 76.02  ?  41  LEU A CB  1 
ATOM   298  C  CG  . LEU A 1 43  ? -4.620  56.377  -56.492  1.00 74.81  ?  41  LEU A CG  1 
ATOM   299  C  CD1 . LEU A 1 43  ? -4.160  57.516  -55.598  1.00 74.77  ?  41  LEU A CD1 1 
ATOM   300  C  CD2 . LEU A 1 43  ? -6.081  56.045  -56.236  1.00 72.21  ?  41  LEU A CD2 1 
ATOM   301  N  N   . VAL A 1 44  ? -1.072  56.332  -57.011  1.00 76.53  ?  42  VAL A N   1 
ATOM   302  C  CA  . VAL A 1 44  ? -0.176  55.361  -56.395  1.00 78.13  ?  42  VAL A CA  1 
ATOM   303  C  C   . VAL A 1 44  ? -0.626  55.142  -54.957  1.00 84.68  ?  42  VAL A C   1 
ATOM   304  O  O   . VAL A 1 44  ? -0.975  56.097  -54.253  1.00 81.35  ?  42  VAL A O   1 
ATOM   305  C  CB  . VAL A 1 44  ? 1.292   55.826  -56.448  1.00 75.59  ?  42  VAL A CB  1 
ATOM   306  C  CG1 . VAL A 1 44  ? 2.197   54.803  -55.776  1.00 80.30  ?  42  VAL A CG1 1 
ATOM   307  C  CG2 . VAL A 1 44  ? 1.720   56.061  -57.888  1.00 77.03  ?  42  VAL A CG2 1 
ATOM   308  N  N   . LEU A 1 45  ? -0.623  53.883  -54.524  1.00 88.14  ?  43  LEU A N   1 
ATOM   309  C  CA  . LEU A 1 45  ? -1.077  53.507  -53.193  1.00 86.71  ?  43  LEU A CA  1 
ATOM   310  C  C   . LEU A 1 45  ? 0.062   52.885  -52.396  1.00 94.34  ?  43  LEU A C   1 
ATOM   311  O  O   . LEU A 1 45  ? 0.891   52.151  -52.943  1.00 92.12  ?  43  LEU A O   1 
ATOM   312  C  CB  . LEU A 1 45  ? -2.254  52.526  -53.266  1.00 90.99  ?  43  LEU A CB  1 
ATOM   313  C  CG  . LEU A 1 45  ? -3.608  53.110  -53.678  1.00 89.71  ?  43  LEU A CG  1 
ATOM   314  C  CD1 . LEU A 1 45  ? -4.720  52.086  -53.483  1.00 85.29  ?  43  LEU A CD1 1 
ATOM   315  C  CD2 . LEU A 1 45  ? -3.906  54.392  -52.914  1.00 86.11  ?  43  LEU A CD2 1 
ATOM   316  N  N   . SER A 1 46  ? 0.086   53.182  -51.103  1.00 99.55  ?  44  SER A N   1 
ATOM   317  C  CA  . SER A 1 46  ? 1.041   52.623  -50.150  1.00 101.68 ?  44  SER A CA  1 
ATOM   318  C  C   . SER A 1 46  ? 0.312   52.474  -48.820  1.00 105.43 ?  44  SER A C   1 
ATOM   319  O  O   . SER A 1 46  ? -0.922  52.421  -48.782  1.00 106.70 ?  44  SER A O   1 
ATOM   320  C  CB  . SER A 1 46  ? 2.291   53.514  -50.049  1.00 98.17  ?  44  SER A CB  1 
ATOM   321  O  OG  . SER A 1 46  ? 3.185   53.032  -49.060  1.00 100.42 ?  44  SER A OG  1 
ATOM   322  N  N   . VAL A 1 47  ? 1.068   52.393  -47.721  1.00 105.98 ?  45  VAL A N   1 
ATOM   323  C  CA  . VAL A 1 47  ? 0.407   52.369  -46.422  1.00 104.72 ?  45  VAL A CA  1 
ATOM   324  C  C   . VAL A 1 47  ? -0.476  53.597  -46.317  1.00 102.72 ?  45  VAL A C   1 
ATOM   325  O  O   . VAL A 1 47  ? -1.557  53.559  -45.717  1.00 107.61 ?  45  VAL A O   1 
ATOM   326  C  CB  . VAL A 1 47  ? 1.437   52.307  -45.277  1.00 109.76 ?  45  VAL A CB  1 
ATOM   327  C  CG1 . VAL A 1 47  ? 0.735   52.121  -43.938  1.00 114.04 ?  45  VAL A CG1 1 
ATOM   328  C  CG2 . VAL A 1 47  ? 2.439   51.191  -45.525  1.00 112.50 ?  45  VAL A CG2 1 
ATOM   329  N  N   . ASN A 1 48  ? -0.031  54.699  -46.912  1.00 99.40  ?  46  ASN A N   1 
ATOM   330  C  CA  . ASN A 1 48  ? -0.756  55.943  -46.981  1.00 97.08  ?  46  ASN A CA  1 
ATOM   331  C  C   . ASN A 1 48  ? -1.003  56.266  -48.449  1.00 96.39  ?  46  ASN A C   1 
ATOM   332  O  O   . ASN A 1 48  ? -0.085  56.133  -49.272  1.00 93.56  ?  46  ASN A O   1 
ATOM   333  C  CB  . ASN A 1 48  ? 0.026   57.076  -46.295  1.00 98.36  ?  46  ASN A CB  1 
ATOM   334  C  CG  . ASN A 1 48  ? 1.529   56.928  -46.455  1.00 99.05  ?  46  ASN A CG  1 
ATOM   335  O  OD1 . ASN A 1 48  ? 2.053   56.938  -47.568  1.00 96.90  ?  46  ASN A OD1 1 
ATOM   336  N  ND2 . ASN A 1 48  ? 2.229   56.784  -45.334  1.00 93.02  ?  46  ASN A ND2 1 
ATOM   337  N  N   . PRO A 1 49  ? -2.216  56.667  -48.821  1.00 97.46  ?  47  PRO A N   1 
ATOM   338  C  CA  . PRO A 1 49  ? -2.475  57.068  -50.210  1.00 91.23  ?  47  PRO A CA  1 
ATOM   339  C  C   . PRO A 1 49  ? -1.625  58.261  -50.619  1.00 83.34  ?  47  PRO A C   1 
ATOM   340  O  O   . PRO A 1 49  ? -1.623  59.298  -49.953  1.00 80.81  ?  47  PRO A O   1 
ATOM   341  C  CB  . PRO A 1 49  ? -3.970  57.412  -50.207  1.00 86.19  ?  47  PRO A CB  1 
ATOM   342  C  CG  . PRO A 1 49  ? -4.290  57.703  -48.773  1.00 92.19  ?  47  PRO A CG  1 
ATOM   343  C  CD  . PRO A 1 49  ? -3.413  56.790  -47.975  1.00 94.16  ?  47  PRO A CD  1 
ATOM   344  N  N   . TYR A 1 50  ? -0.885  58.108  -51.715  1.00 82.25  ?  48  TYR A N   1 
ATOM   345  C  CA  . TYR A 1 50  ? -0.097  59.228  -52.218  1.00 79.33  ?  48  TYR A CA  1 
ATOM   346  C  C   . TYR A 1 50  ? -1.097  60.255  -52.737  1.00 79.97  ?  48  TYR A C   1 
ATOM   347  O  O   . TYR A 1 50  ? -1.635  60.121  -53.838  1.00 72.21  ?  48  TYR A O   1 
ATOM   348  C  CB  . TYR A 1 50  ? 0.852   58.758  -53.316  1.00 73.47  ?  48  TYR A CB  1 
ATOM   349  C  CG  . TYR A 1 50  ? 2.181   58.204  -52.827  1.00 82.80  ?  48  TYR A CG  1 
ATOM   350  C  CD1 . TYR A 1 50  ? 2.301   57.643  -51.561  1.00 85.35  ?  48  TYR A CD1 1 
ATOM   351  C  CD2 . TYR A 1 50  ? 3.302   58.202  -53.650  1.00 85.15  ?  48  TYR A CD2 1 
ATOM   352  C  CE1 . TYR A 1 50  ? 3.508   57.124  -51.118  1.00 85.08  ?  48  TYR A CE1 1 
ATOM   353  C  CE2 . TYR A 1 50  ? 4.513   57.682  -53.215  1.00 86.30  ?  48  TYR A CE2 1 
ATOM   354  C  CZ  . TYR A 1 50  ? 4.609   57.144  -51.949  1.00 87.18  ?  48  TYR A CZ  1 
ATOM   355  O  OH  . TYR A 1 50  ? 5.808   56.626  -51.512  1.00 91.62  ?  48  TYR A OH  1 
ATOM   356  N  N   . VAL A 1 51  ? -1.346  61.293  -51.937  1.00 77.14  ?  49  VAL A N   1 
ATOM   357  C  CA  . VAL A 1 51  ? -2.284  62.356  -52.277  1.00 70.86  ?  49  VAL A CA  1 
ATOM   358  C  C   . VAL A 1 51  ? -1.855  63.606  -51.524  1.00 75.07  ?  49  VAL A C   1 
ATOM   359  O  O   . VAL A 1 51  ? -1.140  63.533  -50.523  1.00 78.18  ?  49  VAL A O   1 
ATOM   360  C  CB  . VAL A 1 51  ? -3.744  61.964  -51.931  1.00 73.64  ?  49  VAL A CB  1 
ATOM   361  C  CG1 . VAL A 1 51  ? -3.896  61.724  -50.433  1.00 78.88  ?  49  VAL A CG1 1 
ATOM   362  C  CG2 . VAL A 1 51  ? -4.728  63.018  -52.421  1.00 77.89  ?  49  VAL A CG2 1 
ATOM   363  N  N   . CYS A 1 52  ? -2.289  64.766  -52.009  1.00 72.73  ?  50  CYS A N   1 
ATOM   364  C  CA  . CYS A 1 52  ? -1.978  66.005  -51.307  1.00 70.10  ?  50  CYS A CA  1 
ATOM   365  C  C   . CYS A 1 52  ? -2.670  66.008  -49.949  1.00 60.61  ?  50  CYS A C   1 
ATOM   366  O  O   . CYS A 1 52  ? -3.895  65.866  -49.868  1.00 60.40  ?  50  CYS A O   1 
ATOM   367  C  CB  . CYS A 1 52  ? -2.412  67.212  -52.134  1.00 65.58  ?  50  CYS A CB  1 
ATOM   368  S  SG  . CYS A 1 52  ? -1.728  68.787  -51.558  1.00 60.34  ?  50  CYS A SG  1 
ATOM   369  N  N   . ASN A 1 53  ? -1.891  66.181  -48.884  1.00 63.00  ?  51  ASN A N   1 
ATOM   370  C  CA  . ASN A 1 53  ? -2.451  66.138  -47.540  1.00 66.13  ?  51  ASN A CA  1 
ATOM   371  C  C   . ASN A 1 53  ? -3.060  67.474  -47.130  1.00 66.45  ?  51  ASN A C   1 
ATOM   372  O  O   . ASN A 1 53  ? -3.578  67.588  -46.014  1.00 63.87  ?  51  ASN A O   1 
ATOM   373  C  CB  . ASN A 1 53  ? -1.383  65.694  -46.535  1.00 66.46  ?  51  ASN A CB  1 
ATOM   374  C  CG  . ASN A 1 53  ? -1.975  64.949  -45.348  1.00 73.67  ?  51  ASN A CG  1 
ATOM   375  O  OD1 . ASN A 1 53  ? -2.695  63.963  -45.518  1.00 71.09  ?  51  ASN A OD1 1 
ATOM   376  N  ND2 . ASN A 1 53  ? -1.659  65.406  -44.142  1.00 72.86  ?  51  ASN A ND2 1 
ATOM   377  N  N   . ALA A 1 54  ? -2.991  68.480  -48.001  1.00 59.58  ?  52  ALA A N   1 
ATOM   378  C  CA  . ALA A 1 54  ? -3.504  69.802  -47.679  1.00 58.44  ?  52  ALA A CA  1 
ATOM   379  C  C   . ALA A 1 54  ? -5.032  69.797  -47.722  1.00 66.03  ?  52  ALA A C   1 
ATOM   380  O  O   . ALA A 1 54  ? -5.627  69.201  -48.626  1.00 62.40  ?  52  ALA A O   1 
ATOM   381  C  CB  . ALA A 1 54  ? -2.953  70.844  -48.651  1.00 67.46  ?  52  ALA A CB  1 
ATOM   382  N  N   . PRO A 1 55  ? -5.689  70.453  -46.767  1.00 59.70  ?  53  PRO A N   1 
ATOM   383  C  CA  . PRO A 1 55  ? -7.158  70.441  -46.718  1.00 63.49  ?  53  PRO A CA  1 
ATOM   384  C  C   . PRO A 1 55  ? -7.802  70.949  -48.002  1.00 69.10  ?  53  PRO A C   1 
ATOM   385  O  O   . PRO A 1 55  ? -7.426  71.994  -48.537  1.00 69.39  ?  53  PRO A O   1 
ATOM   386  C  CB  . PRO A 1 55  ? -7.466  71.370  -45.539  1.00 74.25  ?  53  PRO A CB  1 
ATOM   387  C  CG  . PRO A 1 55  ? -6.263  71.233  -44.662  1.00 71.91  ?  53  PRO A CG  1 
ATOM   388  C  CD  . PRO A 1 55  ? -5.124  71.225  -45.649  1.00 60.18  ?  53  PRO A CD  1 
ATOM   389  N  N   . GLY A 1 56  ? -8.781  70.191  -48.495  1.00 73.27  ?  54  GLY A N   1 
ATOM   390  C  CA  . GLY A 1 56  ? -9.561  70.597  -49.644  1.00 59.91  ?  54  GLY A CA  1 
ATOM   391  C  C   . GLY A 1 56  ? -8.954  70.287  -50.991  1.00 73.02  ?  54  GLY A C   1 
ATOM   392  O  O   . GLY A 1 56  ? -9.553  70.637  -52.016  1.00 76.38  ?  54  GLY A O   1 
ATOM   393  N  N   . CYS A 1 57  ? -7.790  69.652  -51.032  1.00 72.32  ?  55  CYS A N   1 
ATOM   394  C  CA  . CYS A 1 57  ? -7.097  69.433  -52.288  1.00 69.08  ?  55  CYS A CA  1 
ATOM   395  C  C   . CYS A 1 57  ? -7.471  68.077  -52.866  1.00 70.31  ?  55  CYS A C   1 
ATOM   396  O  O   . CYS A 1 57  ? -7.515  67.072  -52.152  1.00 74.58  ?  55  CYS A O   1 
ATOM   397  C  CB  . CYS A 1 57  ? -5.586  69.524  -52.091  1.00 65.57  ?  55  CYS A CB  1 
ATOM   398  S  SG  . CYS A 1 57  ? -4.739  70.143  -53.544  1.00 63.07  ?  55  CYS A SG  1 
ATOM   399  N  N   . ASP A 1 58  ? -7.739  68.058  -54.172  1.00 75.30  ?  56  ASP A N   1 
ATOM   400  C  CA  . ASP A 1 58  ? -8.112  66.838  -54.874  1.00 69.36  ?  56  ASP A CA  1 
ATOM   401  C  C   . ASP A 1 58  ? -6.982  66.305  -55.743  1.00 68.48  ?  56  ASP A C   1 
ATOM   402  O  O   . ASP A 1 58  ? -7.223  65.466  -56.616  1.00 74.63  ?  56  ASP A O   1 
ATOM   403  C  CB  . ASP A 1 58  ? -9.351  67.080  -55.734  1.00 73.35  ?  56  ASP A CB  1 
ATOM   404  C  CG  . ASP A 1 58  ? -9.273  68.380  -56.505  1.00 74.89  ?  56  ASP A CG  1 
ATOM   405  O  OD1 . ASP A 1 58  ? -8.351  68.517  -57.339  1.00 82.42  ?  56  ASP A OD1 1 
ATOM   406  O  OD2 . ASP A 1 58  ? -10.124 69.264  -56.277  1.00 77.59  -1 56  ASP A OD2 1 
ATOM   407  N  N   . VAL A 1 59  ? -5.754  66.766  -55.527  1.00 65.87  ?  57  VAL A N   1 
ATOM   408  C  CA  . VAL A 1 59  ? -4.657  66.376  -56.402  1.00 65.79  ?  57  VAL A CA  1 
ATOM   409  C  C   . VAL A 1 59  ? -4.238  64.960  -56.033  1.00 72.59  ?  57  VAL A C   1 
ATOM   410  O  O   . VAL A 1 59  ? -3.758  64.709  -54.923  1.00 65.86  ?  57  VAL A O   1 
ATOM   411  C  CB  . VAL A 1 59  ? -3.477  67.352  -56.296  1.00 67.33  ?  57  VAL A CB  1 
ATOM   412  C  CG1 . VAL A 1 59  ? -2.289  66.827  -57.089  1.00 63.63  ?  57  VAL A CG1 1 
ATOM   413  C  CG2 . VAL A 1 59  ? -3.885  68.728  -56.797  1.00 75.23  ?  57  VAL A CG2 1 
ATOM   414  N  N   . THR A 1 60  ? -4.423  64.035  -56.972  1.00 66.88  ?  58  THR A N   1 
ATOM   415  C  CA  . THR A 1 60  ? -4.083  62.636  -56.792  1.00 66.85  ?  58  THR A CA  1 
ATOM   416  C  C   . THR A 1 60  ? -3.009  62.167  -57.756  1.00 67.78  ?  58  THR A C   1 
ATOM   417  O  O   . THR A 1 60  ? -2.431  61.096  -57.543  1.00 70.47  ?  58  THR A O   1 
ATOM   418  C  CB  . THR A 1 60  ? -5.332  61.756  -56.959  1.00 66.34  ?  58  THR A CB  1 
ATOM   419  O  OG1 . THR A 1 60  ? -6.068  62.192  -58.109  1.00 76.23  ?  58  THR A OG1 1 
ATOM   420  C  CG2 . THR A 1 60  ? -6.223  61.864  -55.732  1.00 62.53  ?  58  THR A CG2 1 
ATOM   421  N  N   . ASP A 1 61  ? -2.724  62.940  -58.799  1.00 70.75  ?  59  ASP A N   1 
ATOM   422  C  CA  . ASP A 1 61  ? -1.765  62.542  -59.816  1.00 68.54  ?  59  ASP A CA  1 
ATOM   423  C  C   . ASP A 1 61  ? -0.357  62.650  -59.247  1.00 70.74  ?  59  ASP A C   1 
ATOM   424  O  O   . ASP A 1 61  ? 0.089   63.742  -58.877  1.00 74.78  ?  59  ASP A O   1 
ATOM   425  C  CB  . ASP A 1 61  ? -1.936  63.434  -61.044  1.00 69.84  ?  59  ASP A CB  1 
ATOM   426  C  CG  . ASP A 1 61  ? -0.987  63.084  -62.168  1.00 68.76  ?  59  ASP A CG  1 
ATOM   427  O  OD1 . ASP A 1 61  ? -0.195  62.131  -62.018  1.00 69.67  ?  59  ASP A OD1 1 
ATOM   428  O  OD2 . ASP A 1 61  ? -1.037  63.771  -63.209  1.00 77.49  -1 59  ASP A OD2 1 
ATOM   429  N  N   . VAL A 1 62  ? 0.347   61.517  -59.184  1.00 69.43  ?  60  VAL A N   1 
ATOM   430  C  CA  . VAL A 1 62  ? 1.661   61.495  -58.554  1.00 72.82  ?  60  VAL A CA  1 
ATOM   431  C  C   . VAL A 1 62  ? 2.676   62.303  -59.351  1.00 74.98  ?  60  VAL A C   1 
ATOM   432  O  O   . VAL A 1 62  ? 3.703   62.717  -58.800  1.00 77.70  ?  60  VAL A O   1 
ATOM   433  C  CB  . VAL A 1 62  ? 2.127   60.040  -58.358  1.00 75.34  ?  60  VAL A CB  1 
ATOM   434  C  CG1 . VAL A 1 62  ? 2.236   59.332  -59.697  1.00 73.43  ?  60  VAL A CG1 1 
ATOM   435  C  CG2 . VAL A 1 62  ? 3.449   59.996  -57.607  1.00 74.64  ?  60  VAL A CG2 1 
ATOM   436  N  N   . THR A 1 63  ? 2.412   62.551  -60.636  1.00 73.85  ?  61  THR A N   1 
ATOM   437  C  CA  . THR A 1 63  ? 3.301   63.400  -61.416  1.00 73.95  ?  61  THR A CA  1 
ATOM   438  C  C   . THR A 1 63  ? 3.227   64.840  -60.936  1.00 76.40  ?  61  THR A C   1 
ATOM   439  O  O   . THR A 1 63  ? 4.136   65.631  -61.214  1.00 77.33  ?  61  THR A O   1 
ATOM   440  C  CB  . THR A 1 63  ? 2.954   63.328  -62.904  1.00 75.95  ?  61  THR A CB  1 
ATOM   441  O  OG1 . THR A 1 63  ? 1.668   63.919  -63.126  1.00 81.21  ?  61  THR A OG1 1 
ATOM   442  C  CG2 . THR A 1 63  ? 2.923   61.883  -63.371  1.00 73.68  ?  61  THR A CG2 1 
ATOM   443  N  N   . GLN A 1 64  ? 2.160   65.183  -60.215  1.00 75.56  ?  62  GLN A N   1 
ATOM   444  C  CA  . GLN A 1 64  ? 1.890   66.533  -59.746  1.00 72.83  ?  62  GLN A CA  1 
ATOM   445  C  C   . GLN A 1 64  ? 2.097   66.651  -58.244  1.00 74.45  ?  62  GLN A C   1 
ATOM   446  O  O   . GLN A 1 64  ? 1.723   67.668  -57.651  1.00 74.28  ?  62  GLN A O   1 
ATOM   447  C  CB  . GLN A 1 64  ? 0.454   66.929  -60.099  1.00 68.06  ?  62  GLN A CB  1 
ATOM   448  C  CG  . GLN A 1 64  ? 0.136   66.933  -61.585  1.00 69.40  ?  62  GLN A CG  1 
ATOM   449  C  CD  . GLN A 1 64  ? 0.678   68.151  -62.295  1.00 74.67  ?  62  GLN A CD  1 
ATOM   450  O  OE1 . GLN A 1 64  ? 1.509   68.040  -63.196  1.00 81.29  ?  62  GLN A OE1 1 
ATOM   451  N  NE2 . GLN A 1 64  ? 0.210   69.327  -61.892  1.00 77.02  ?  62  GLN A NE2 1 
ATOM   452  N  N   . LEU A 1 65  ? 2.692   65.639  -57.619  1.00 76.34  ?  63  LEU A N   1 
ATOM   453  C  CA  . LEU A 1 65  ? 2.825   65.551  -56.174  1.00 71.53  ?  63  LEU A CA  1 
ATOM   454  C  C   . LEU A 1 65  ? 4.288   65.678  -55.768  1.00 78.54  ?  63  LEU A C   1 
ATOM   455  O  O   . LEU A 1 65  ? 5.202   65.425  -56.558  1.00 78.42  ?  63  LEU A O   1 
ATOM   456  C  CB  . LEU A 1 65  ? 2.236   64.234  -55.657  1.00 73.72  ?  63  LEU A CB  1 
ATOM   457  C  CG  . LEU A 1 65  ? 0.709   64.215  -55.551  1.00 71.13  ?  63  LEU A CG  1 
ATOM   458  C  CD1 . LEU A 1 65  ? 0.212   62.867  -55.053  1.00 71.82  ?  63  LEU A CD1 1 
ATOM   459  C  CD2 . LEU A 1 65  ? 0.209   65.342  -54.658  1.00 71.17  ?  63  LEU A CD2 1 
ATOM   460  N  N   . TYR A 1 66  ? 4.501   66.057  -54.508  1.00 75.06  ?  64  TYR A N   1 
ATOM   461  C  CA  . TYR A 1 66  ? 5.835   66.336  -53.999  1.00 76.60  ?  64  TYR A CA  1 
ATOM   462  C  C   . TYR A 1 66  ? 5.968   65.811  -52.578  1.00 76.80  ?  64  TYR A C   1 
ATOM   463  O  O   . TYR A 1 66  ? 4.986   65.727  -51.836  1.00 76.09  ?  64  TYR A O   1 
ATOM   464  C  CB  . TYR A 1 66  ? 6.113   67.845  -53.987  1.00 78.43  ?  64  TYR A CB  1 
ATOM   465  C  CG  . TYR A 1 66  ? 6.182   68.493  -55.349  1.00 78.20  ?  64  TYR A CG  1 
ATOM   466  C  CD1 . TYR A 1 66  ? 5.035   68.991  -55.954  1.00 75.80  ?  64  TYR A CD1 1 
ATOM   467  C  CD2 . TYR A 1 66  ? 7.391   68.642  -56.015  1.00 81.83  ?  64  TYR A CD2 1 
ATOM   468  C  CE1 . TYR A 1 66  ? 5.083   69.592  -57.195  1.00 80.28  ?  64  TYR A CE1 1 
ATOM   469  C  CE2 . TYR A 1 66  ? 7.451   69.248  -57.258  1.00 84.87  ?  64  TYR A CE2 1 
ATOM   470  C  CZ  . TYR A 1 66  ? 6.292   69.721  -57.842  1.00 82.42  ?  64  TYR A CZ  1 
ATOM   471  O  OH  . TYR A 1 66  ? 6.341   70.328  -59.075  1.00 85.61  ?  64  TYR A OH  1 
ATOM   472  N  N   . LEU A 1 67  ? 7.198   65.464  -52.203  1.00 81.98  ?  65  LEU A N   1 
ATOM   473  C  CA  . LEU A 1 67  ? 7.500   64.999  -50.854  1.00 79.98  ?  65  LEU A CA  1 
ATOM   474  C  C   . LEU A 1 67  ? 7.932   66.195  -50.014  1.00 81.05  ?  65  LEU A C   1 
ATOM   475  O  O   . LEU A 1 67  ? 9.026   66.735  -50.209  1.00 83.41  ?  65  LEU A O   1 
ATOM   476  C  CB  . LEU A 1 67  ? 8.583   63.924  -50.867  1.00 81.62  ?  65  LEU A CB  1 
ATOM   477  C  CG  . LEU A 1 67  ? 9.046   63.468  -49.478  1.00 90.51  ?  65  LEU A CG  1 
ATOM   478  C  CD1 . LEU A 1 67  ? 7.881   62.919  -48.666  1.00 88.85  ?  65  LEU A CD1 1 
ATOM   479  C  CD2 . LEU A 1 67  ? 10.168  62.443  -49.576  1.00 93.36  ?  65  LEU A CD2 1 
ATOM   480  N  N   . GLY A 1 68  ? 7.080   66.606  -49.081  1.00 79.85  ?  66  GLY A N   1 
ATOM   481  C  CA  . GLY A 1 68  ? 7.390   67.729  -48.221  1.00 80.69  ?  66  GLY A CA  1 
ATOM   482  C  C   . GLY A 1 68  ? 7.366   67.299  -46.771  1.00 80.71  ?  66  GLY A C   1 
ATOM   483  O  O   . GLY A 1 68  ? 6.297   67.023  -46.218  1.00 76.54  ?  66  GLY A O   1 
ATOM   484  N  N   . GLY A 1 69  ? 8.537   67.232  -46.145  1.00 83.94  ?  67  GLY A N   1 
ATOM   485  C  CA  . GLY A 1 69  ? 8.611   66.715  -44.796  1.00 86.45  ?  67  GLY A CA  1 
ATOM   486  C  C   . GLY A 1 69  ? 8.356   65.225  -44.851  1.00 92.33  ?  67  GLY A C   1 
ATOM   487  O  O   . GLY A 1 69  ? 9.104   64.483  -45.495  1.00 96.14  ?  67  GLY A O   1 
ATOM   488  N  N   . MET A 1 70  ? 7.285   64.775  -44.197  1.00 94.00  ?  68  MET A N   1 
ATOM   489  C  CA  . MET A 1 70  ? 6.900   63.374  -44.231  1.00 87.54  ?  68  MET A CA  1 
ATOM   490  C  C   . MET A 1 70  ? 5.637   63.134  -45.041  1.00 83.56  ?  68  MET A C   1 
ATOM   491  O  O   . MET A 1 70  ? 5.361   61.986  -45.401  1.00 90.48  ?  68  MET A O   1 
ATOM   492  C  CB  . MET A 1 70  ? 6.693   62.836  -42.807  1.00 95.76  ?  68  MET A CB  1 
ATOM   493  N  N   . SER A 1 71  ? 4.881   64.186  -45.341  1.00 79.07  ?  69  SER A N   1 
ATOM   494  C  CA  . SER A 1 71  ? 3.623   64.091  -46.058  1.00 76.68  ?  69  SER A CA  1 
ATOM   495  C  C   . SER A 1 71  ? 3.848   64.449  -47.525  1.00 76.01  ?  69  SER A C   1 
ATOM   496  O  O   . SER A 1 71  ? 4.961   64.759  -47.956  1.00 76.56  ?  69  SER A O   1 
ATOM   497  C  CB  . SER A 1 71  ? 2.572   65.001  -45.420  1.00 75.00  ?  69  SER A CB  1 
ATOM   498  O  OG  . SER A 1 71  ? 2.035   64.419  -44.246  1.00 82.59  ?  69  SER A OG  1 
ATOM   499  N  N   . TYR A 1 72  ? 2.771   64.411  -48.301  1.00 72.34  ?  70  TYR A N   1 
ATOM   500  C  CA  . TYR A 1 72  ? 2.835   64.647  -49.733  1.00 70.11  ?  70  TYR A CA  1 
ATOM   501  C  C   . TYR A 1 72  ? 1.943   65.834  -50.068  1.00 68.17  ?  70  TYR A C   1 
ATOM   502  O  O   . TYR A 1 72  ? 0.880   66.009  -49.464  1.00 63.80  ?  70  TYR A O   1 
ATOM   503  C  CB  . TYR A 1 72  ? 2.407   63.391  -50.499  1.00 73.29  ?  70  TYR A CB  1 
ATOM   504  C  CG  . TYR A 1 72  ? 3.023   62.134  -49.920  1.00 75.46  ?  70  TYR A CG  1 
ATOM   505  C  CD1 . TYR A 1 72  ? 4.358   61.824  -50.143  1.00 80.43  ?  70  TYR A CD1 1 
ATOM   506  C  CD2 . TYR A 1 72  ? 2.274   61.270  -49.131  1.00 76.78  ?  70  TYR A CD2 1 
ATOM   507  C  CE1 . TYR A 1 72  ? 4.929   60.685  -49.601  1.00 83.47  ?  70  TYR A CE1 1 
ATOM   508  C  CE2 . TYR A 1 72  ? 2.835   60.127  -48.588  1.00 78.08  ?  70  TYR A CE2 1 
ATOM   509  C  CZ  . TYR A 1 72  ? 4.162   59.840  -48.826  1.00 81.87  ?  70  TYR A CZ  1 
ATOM   510  O  OH  . TYR A 1 72  ? 4.725   58.703  -48.293  1.00 93.87  ?  70  TYR A OH  1 
ATOM   511  N  N   . TYR A 1 73  ? 2.382   66.656  -51.020  1.00 64.90  ?  71  TYR A N   1 
ATOM   512  C  CA  . TYR A 1 73  ? 1.645   67.866  -51.354  1.00 61.69  ?  71  TYR A CA  1 
ATOM   513  C  C   . TYR A 1 73  ? 1.768   68.138  -52.846  1.00 62.81  ?  71  TYR A C   1 
ATOM   514  O  O   . TYR A 1 73  ? 2.642   67.598  -53.528  1.00 63.36  ?  71  TYR A O   1 
ATOM   515  C  CB  . TYR A 1 73  ? 2.159   69.070  -50.550  1.00 60.68  ?  71  TYR A CB  1 
ATOM   516  C  CG  . TYR A 1 73  ? 2.123   68.876  -49.048  1.00 61.25  ?  71  TYR A CG  1 
ATOM   517  C  CD1 . TYR A 1 73  ? 0.963   69.108  -48.320  1.00 60.43  ?  71  TYR A CD1 1 
ATOM   518  C  CD2 . TYR A 1 73  ? 3.255   68.461  -48.358  1.00 69.60  ?  71  TYR A CD2 1 
ATOM   519  C  CE1 . TYR A 1 73  ? 0.932   68.928  -46.945  1.00 62.96  ?  71  TYR A CE1 1 
ATOM   520  C  CE2 . TYR A 1 73  ? 3.234   68.281  -46.986  1.00 69.88  ?  71  TYR A CE2 1 
ATOM   521  C  CZ  . TYR A 1 73  ? 2.072   68.515  -46.285  1.00 66.93  ?  71  TYR A CZ  1 
ATOM   522  O  OH  . TYR A 1 73  ? 2.051   68.334  -44.919  1.00 67.62  ?  71  TYR A OH  1 
ATOM   523  N  N   . CYS A 1 74  ? 0.877   68.991  -53.345  1.00 60.25  ?  72  CYS A N   1 
ATOM   524  C  CA  . CYS A 1 74  ? 0.910   69.426  -54.731  1.00 65.95  ?  72  CYS A CA  1 
ATOM   525  C  C   . CYS A 1 74  ? 1.811   70.653  -54.864  1.00 67.59  ?  72  CYS A C   1 
ATOM   526  O  O   . CYS A 1 74  ? 2.418   71.121  -53.897  1.00 64.08  ?  72  CYS A O   1 
ATOM   527  C  CB  . CYS A 1 74  ? -0.498  69.731  -55.236  1.00 62.97  ?  72  CYS A CB  1 
ATOM   528  S  SG  . CYS A 1 74  ? -1.218  71.223  -54.525  1.00 62.13  ?  72  CYS A SG  1 
ATOM   529  N  N   . LYS A 1 75  ? 1.892   71.194  -56.083  1.00 65.03  ?  73  LYS A N   1 
ATOM   530  C  CA  . LYS A 1 75  ? 2.760   72.340  -56.326  1.00 70.05  ?  73  LYS A CA  1 
ATOM   531  C  C   . LYS A 1 75  ? 2.232   73.611  -55.674  1.00 72.77  ?  73  LYS A C   1 
ATOM   532  O  O   . LYS A 1 75  ? 3.004   74.555  -55.472  1.00 77.31  ?  73  LYS A O   1 
ATOM   533  C  CB  . LYS A 1 75  ? 2.934   72.560  -57.829  1.00 74.93  ?  73  LYS A CB  1 
ATOM   534  N  N   . SER A 1 76  ? 0.946   73.652  -55.326  1.00 67.64  ?  74  SER A N   1 
ATOM   535  C  CA  . SER A 1 76  ? 0.340   74.836  -54.733  1.00 69.11  ?  74  SER A CA  1 
ATOM   536  C  C   . SER A 1 76  ? 0.352   74.794  -53.213  1.00 66.66  ?  74  SER A C   1 
ATOM   537  O  O   . SER A 1 76  ? -0.025  75.783  -52.576  1.00 76.25  ?  74  SER A O   1 
ATOM   538  C  CB  . SER A 1 76  ? -1.106  74.998  -55.217  1.00 75.00  ?  74  SER A CB  1 
ATOM   539  O  OG  . SER A 1 76  ? -1.204  74.862  -56.622  1.00 81.22  ?  74  SER A OG  1 
ATOM   540  N  N   . HIS A 1 77  ? 0.779   73.675  -52.626  1.00 64.08  ?  75  HIS A N   1 
ATOM   541  C  CA  . HIS A 1 77  ? 0.741   73.475  -51.187  1.00 65.81  ?  75  HIS A CA  1 
ATOM   542  C  C   . HIS A 1 77  ? 2.067   72.978  -50.627  1.00 62.09  ?  75  HIS A C   1 
ATOM   543  O  O   . HIS A 1 77  ? 2.197   72.866  -49.403  1.00 59.47  ?  75  HIS A O   1 
ATOM   544  C  CB  . HIS A 1 77  ? -0.368  72.476  -50.810  1.00 59.42  ?  75  HIS A CB  1 
ATOM   545  C  CG  . HIS A 1 77  ? -1.757  73.001  -51.011  1.00 62.21  ?  75  HIS A CG  1 
ATOM   546  N  ND1 . HIS A 1 77  ? -2.655  72.417  -51.880  1.00 65.70  ?  75  HIS A ND1 1 
ATOM   547  C  CD2 . HIS A 1 77  ? -2.409  74.042  -50.442  1.00 65.81  ?  75  HIS A CD2 1 
ATOM   548  C  CE1 . HIS A 1 77  ? -3.795  73.083  -51.847  1.00 60.14  ?  75  HIS A CE1 1 
ATOM   549  N  NE2 . HIS A 1 77  ? -3.673  74.073  -50.981  1.00 65.93  ?  75  HIS A NE2 1 
ATOM   550  N  N   . LYS A 1 78  ? 3.053   72.693  -51.476  1.00 56.16  ?  76  LYS A N   1 
ATOM   551  C  CA  . LYS A 1 78  ? 4.286   72.087  -51.003  1.00 60.80  ?  76  LYS A CA  1 
ATOM   552  C  C   . LYS A 1 78  ? 5.154   73.111  -50.274  1.00 72.68  ?  76  LYS A C   1 
ATOM   553  O  O   . LYS A 1 78  ? 5.167   74.294  -50.626  1.00 69.14  ?  76  LYS A O   1 
ATOM   554  C  CB  . LYS A 1 78  ? 5.073   71.478  -52.162  1.00 66.31  ?  76  LYS A CB  1 
ATOM   555  C  CG  . LYS A 1 78  ? 5.681   72.484  -53.137  1.00 64.86  ?  76  LYS A CG  1 
ATOM   556  C  CD  . LYS A 1 78  ? 6.343   71.765  -54.314  1.00 71.65  ?  76  LYS A CD  1 
ATOM   557  C  CE  . LYS A 1 78  ? 7.387   72.629  -55.014  1.00 77.59  ?  76  LYS A CE  1 
ATOM   558  N  NZ  . LYS A 1 78  ? 8.668   72.727  -54.255  1.00 76.39  ?  76  LYS A NZ  1 
ATOM   559  N  N   . PRO A 1 79  ? 5.892   72.676  -49.258  1.00 69.18  ?  77  PRO A N   1 
ATOM   560  C  CA  . PRO A 1 79  ? 6.798   73.576  -48.549  1.00 70.38  ?  77  PRO A CA  1 
ATOM   561  C  C   . PRO A 1 79  ? 7.991   73.934  -49.416  1.00 73.34  ?  77  PRO A C   1 
ATOM   562  O  O   . PRO A 1 79  ? 8.234   73.288  -50.446  1.00 77.73  ?  77  PRO A O   1 
ATOM   563  C  CB  . PRO A 1 79  ? 7.215   72.740  -47.331  1.00 66.04  ?  77  PRO A CB  1 
ATOM   564  C  CG  . PRO A 1 79  ? 7.239   71.355  -47.894  1.00 69.21  ?  77  PRO A CG  1 
ATOM   565  C  CD  . PRO A 1 79  ? 5.956   71.313  -48.700  1.00 67.10  ?  77  PRO A CD  1 
ATOM   566  N  N   . PRO A 1 80  ? 8.744   74.974  -49.049  1.00 76.46  ?  78  PRO A N   1 
ATOM   567  C  CA  . PRO A 1 80  ? 9.953   75.311  -49.824  1.00 75.94  ?  78  PRO A CA  1 
ATOM   568  C  C   . PRO A 1 80  ? 10.863  74.123  -50.112  1.00 81.54  ?  78  PRO A C   1 
ATOM   569  O  O   . PRO A 1 80  ? 11.305  73.953  -51.255  1.00 88.79  ?  78  PRO A O   1 
ATOM   570  C  CB  . PRO A 1 80  ? 10.636  76.370  -48.940  1.00 73.56  ?  78  PRO A CB  1 
ATOM   571  C  CG  . PRO A 1 80  ? 9.971   76.232  -47.582  1.00 72.87  ?  78  PRO A CG  1 
ATOM   572  C  CD  . PRO A 1 80  ? 8.562   75.898  -47.921  1.00 68.90  ?  78  PRO A CD  1 
ATOM   573  N  N   . ILE A 1 81  ? 11.171  73.305  -49.107  1.00 81.04  ?  79  ILE A N   1 
ATOM   574  C  CA  . ILE A 1 81  ? 12.067  72.164  -49.277  1.00 85.87  ?  79  ILE A CA  1 
ATOM   575  C  C   . ILE A 1 81  ? 11.197  70.946  -49.575  1.00 87.19  ?  79  ILE A C   1 
ATOM   576  O  O   . ILE A 1 81  ? 10.675  70.302  -48.663  1.00 90.70  ?  79  ILE A O   1 
ATOM   577  C  CB  . ILE A 1 81  ? 12.950  71.943  -48.047  1.00 84.89  ?  79  ILE A CB  1 
ATOM   578  C  CG1 . ILE A 1 81  ? 13.858  73.152  -47.808  1.00 86.41  ?  79  ILE A CG1 1 
ATOM   579  C  CG2 . ILE A 1 81  ? 13.786  70.684  -48.211  1.00 87.90  ?  79  ILE A CG2 1 
ATOM   580  C  CD1 . ILE A 1 81  ? 13.202  74.270  -47.027  1.00 90.41  ?  79  ILE A CD1 1 
ATOM   581  N  N   . SER A 1 82  ? 11.037  70.628  -50.859  1.00 87.12  ?  80  SER A N   1 
ATOM   582  C  CA  . SER A 1 82  ? 10.189  69.520  -51.274  1.00 86.05  ?  80  SER A CA  1 
ATOM   583  C  C   . SER A 1 82  ? 10.767  68.860  -52.518  1.00 88.98  ?  80  SER A C   1 
ATOM   584  O  O   . SER A 1 82  ? 11.195  69.546  -53.450  1.00 90.89  ?  80  SER A O   1 
ATOM   585  C  CB  . SER A 1 82  ? 8.755   69.988  -51.545  1.00 81.63  ?  80  SER A CB  1 
ATOM   586  O  OG  . SER A 1 82  ? 8.741   71.304  -52.068  1.00 83.60  ?  80  SER A OG  1 
ATOM   587  N  N   . PHE A 1 83  ? 10.780  67.525  -52.524  1.00 88.88  ?  81  PHE A N   1 
ATOM   588  C  CA  . PHE A 1 83  ? 11.279  66.775  -53.669  1.00 91.34  ?  81  PHE A CA  1 
ATOM   589  C  C   . PHE A 1 83  ? 10.117  66.212  -54.478  1.00 86.63  ?  81  PHE A C   1 
ATOM   590  O  O   . PHE A 1 83  ? 9.130   65.741  -53.901  1.00 85.47  ?  81  PHE A O   1 
ATOM   591  C  CB  . PHE A 1 83  ? 12.173  65.617  -53.219  1.00 91.47  ?  81  PHE A CB  1 
ATOM   592  C  CG  . PHE A 1 83  ? 13.598  66.011  -52.957  1.00 99.40  ?  81  PHE A CG  1 
ATOM   593  C  CD1 . PHE A 1 83  ? 14.195  67.033  -53.675  1.00 104.95 ?  81  PHE A CD1 1 
ATOM   594  C  CD2 . PHE A 1 83  ? 14.342  65.353  -51.992  1.00 108.91 ?  81  PHE A CD2 1 
ATOM   595  C  CE1 . PHE A 1 83  ? 15.509  67.394  -53.432  1.00 109.59 ?  81  PHE A CE1 1 
ATOM   596  C  CE2 . PHE A 1 83  ? 15.655  65.707  -51.744  1.00 112.19 ?  81  PHE A CE2 1 
ATOM   597  C  CZ  . PHE A 1 83  ? 16.239  66.729  -52.465  1.00 111.39 ?  81  PHE A CZ  1 
ATOM   598  N  N   . PRO A 1 84  ? 10.190  66.239  -55.808  1.00 91.19  ?  82  PRO A N   1 
ATOM   599  C  CA  . PRO A 1 84  ? 9.108   65.660  -56.613  1.00 89.96  ?  82  PRO A CA  1 
ATOM   600  C  C   . PRO A 1 84  ? 9.049   64.150  -56.433  1.00 82.49  ?  82  PRO A C   1 
ATOM   601  O  O   . PRO A 1 84  ? 10.072  63.464  -56.485  1.00 86.27  ?  82  PRO A O   1 
ATOM   602  C  CB  . PRO A 1 84  ? 9.491   66.050  -58.045  1.00 86.28  ?  82  PRO A CB  1 
ATOM   603  C  CG  . PRO A 1 84  ? 10.986  66.113  -57.994  1.00 87.39  ?  82  PRO A CG  1 
ATOM   604  C  CD  . PRO A 1 84  ? 11.279  66.753  -56.657  1.00 93.58  ?  82  PRO A CD  1 
ATOM   605  N  N   . LEU A 1 85  ? 7.840   63.634  -56.206  1.00 80.01  ?  83  LEU A N   1 
ATOM   606  C  CA  . LEU A 1 85  ? 7.681   62.195  -56.024  1.00 90.40  ?  83  LEU A CA  1 
ATOM   607  C  C   . LEU A 1 85  ? 8.122   61.437  -57.270  1.00 86.93  ?  83  LEU A C   1 
ATOM   608  O  O   . LEU A 1 85  ? 8.851   60.443  -57.184  1.00 89.42  ?  83  LEU A O   1 
ATOM   609  C  CB  . LEU A 1 85  ? 6.229   61.864  -55.676  1.00 83.74  ?  83  LEU A CB  1 
ATOM   610  C  CG  . LEU A 1 85  ? 5.746   62.294  -54.290  1.00 83.40  ?  83  LEU A CG  1 
ATOM   611  C  CD1 . LEU A 1 85  ? 4.328   61.805  -54.048  1.00 80.64  ?  83  LEU A CD1 1 
ATOM   612  C  CD2 . LEU A 1 85  ? 6.686   61.779  -53.211  1.00 87.80  ?  83  LEU A CD2 1 
ATOM   613  N  N   . CYS A 1 86  ? 7.683   61.893  -58.441  1.00 87.57  ?  84  CYS A N   1 
ATOM   614  C  CA  . CYS A 1 86  ? 8.094   61.308  -59.716  1.00 90.37  ?  84  CYS A CA  1 
ATOM   615  C  C   . CYS A 1 86  ? 9.389   61.984  -60.148  1.00 90.31  ?  84  CYS A C   1 
ATOM   616  O  O   . CYS A 1 86  ? 9.384   62.972  -60.883  1.00 94.81  ?  84  CYS A O   1 
ATOM   617  C  CB  . CYS A 1 86  ? 6.994   61.469  -60.756  1.00 83.98  ?  84  CYS A CB  1 
ATOM   618  S  SG  . CYS A 1 86  ? 5.549   60.434  -60.447  1.00 77.98  ?  84  CYS A SG  1 
ATOM   619  N  N   . ALA A 1 87  ? 10.515  61.443  -59.692  1.00 90.25  ?  85  ALA A N   1 
ATOM   620  C  CA  . ALA A 1 87  ? 11.818  62.041  -59.945  1.00 97.52  ?  85  ALA A CA  1 
ATOM   621  C  C   . ALA A 1 87  ? 12.789  60.991  -60.462  1.00 103.91 ?  85  ALA A C   1 
ATOM   622  O  O   . ALA A 1 87  ? 12.778  59.843  -60.009  1.00 104.93 ?  85  ALA A O   1 
ATOM   623  C  CB  . ALA A 1 87  ? 12.383  62.694  -58.677  1.00 94.71  ?  85  ALA A CB  1 
ATOM   624  N  N   . ASN A 1 88  ? 13.631  61.401  -61.409  1.00 105.25 ?  86  ASN A N   1 
ATOM   625  C  CA  . ASN A 1 88  ? 14.683  60.559  -61.974  1.00 104.86 ?  86  ASN A CA  1 
ATOM   626  C  C   . ASN A 1 88  ? 14.144  59.172  -62.325  1.00 104.11 ?  86  ASN A C   1 
ATOM   627  O  O   . ASN A 1 88  ? 14.587  58.148  -61.801  1.00 110.31 ?  86  ASN A O   1 
ATOM   628  C  CB  . ASN A 1 88  ? 15.870  60.457  -61.012  1.00 106.55 ?  86  ASN A CB  1 
ATOM   629  C  CG  . ASN A 1 88  ? 16.243  61.795  -60.401  1.00 107.13 ?  86  ASN A CG  1 
ATOM   630  O  OD1 . ASN A 1 88  ? 16.566  62.748  -61.111  1.00 110.22 ?  86  ASN A OD1 1 
ATOM   631  N  ND2 . ASN A 1 88  ? 16.199  61.873  -59.076  1.00 105.73 ?  86  ASN A ND2 1 
ATOM   632  N  N   . GLY A 1 89  ? 13.180  59.157  -63.246  1.00 101.41 ?  87  GLY A N   1 
ATOM   633  C  CA  . GLY A 1 89  ? 12.573  57.922  -63.707  1.00 99.97  ?  87  GLY A CA  1 
ATOM   634  C  C   . GLY A 1 89  ? 12.231  56.970  -62.580  1.00 100.81 ?  87  GLY A C   1 
ATOM   635  O  O   . GLY A 1 89  ? 12.311  55.748  -62.738  1.00 99.52  ?  87  GLY A O   1 
ATOM   636  N  N   . GLN A 1 90  ? 11.833  57.526  -61.437  1.00 101.34 ?  88  GLN A N   1 
ATOM   637  C  CA  . GLN A 1 90  ? 11.494  56.736  -60.264  1.00 100.21 ?  88  GLN A CA  1 
ATOM   638  C  C   . GLN A 1 90  ? 10.374  57.427  -59.501  1.00 96.77  ?  88  GLN A C   1 
ATOM   639  O  O   . GLN A 1 90  ? 10.173  58.639  -59.618  1.00 96.55  ?  88  GLN A O   1 
ATOM   640  C  CB  . GLN A 1 90  ? 12.714  56.549  -59.353  1.00 104.53 ?  88  GLN A CB  1 
ATOM   641  C  CG  . GLN A 1 90  ? 13.545  55.309  -59.634  1.00 108.67 ?  88  GLN A CG  1 
ATOM   642  C  CD  . GLN A 1 90  ? 14.740  55.202  -58.705  1.00 115.53 ?  88  GLN A CD  1 
ATOM   643  O  OE1 . GLN A 1 90  ? 14.881  54.233  -57.960  1.00 120.78 ?  88  GLN A OE1 1 
ATOM   644  N  NE2 . GLN A 1 90  ? 15.608  56.208  -58.744  1.00 113.09 ?  88  GLN A NE2 1 
ATOM   645  N  N   . VAL A 1 91  ? 9.650   56.641  -58.710  1.00 94.48  ?  89  VAL A N   1 
ATOM   646  C  CA  . VAL A 1 91  ? 8.581   57.139  -57.851  1.00 98.08  ?  89  VAL A CA  1 
ATOM   647  C  C   . VAL A 1 91  ? 8.988   56.862  -56.411  1.00 99.12  ?  89  VAL A C   1 
ATOM   648  O  O   . VAL A 1 91  ? 9.260   55.710  -56.050  1.00 96.98  ?  89  VAL A O   1 
ATOM   649  C  CB  . VAL A 1 91  ? 7.228   56.487  -58.177  1.00 94.14  ?  89  VAL A CB  1 
ATOM   650  C  CG1 . VAL A 1 91  ? 6.160   56.966  -57.204  1.00 90.14  ?  89  VAL A CG1 1 
ATOM   651  C  CG2 . VAL A 1 91  ? 6.826   56.785  -59.615  1.00 93.37  ?  89  VAL A CG2 1 
ATOM   652  N  N   . PHE A 1 92  ? 9.034   57.915  -55.595  1.00 96.92  ?  90  PHE A N   1 
ATOM   653  C  CA  . PHE A 1 92  ? 9.486   57.798  -54.213  1.00 97.66  ?  90  PHE A CA  1 
ATOM   654  C  C   . PHE A 1 92  ? 8.808   56.636  -53.501  1.00 99.47  ?  90  PHE A C   1 
ATOM   655  O  O   . PHE A 1 92  ? 7.578   56.578  -53.403  1.00 96.10  ?  90  PHE A O   1 
ATOM   656  C  CB  . PHE A 1 92  ? 9.230   59.105  -53.459  1.00 98.73  ?  90  PHE A CB  1 
ATOM   657  C  CG  . PHE A 1 92  ? 9.252   58.958  -51.960  1.00 98.55  ?  90  PHE A CG  1 
ATOM   658  C  CD1 . PHE A 1 92  ? 10.454  58.933  -51.270  1.00 95.47  ?  90  PHE A CD1 1 
ATOM   659  C  CD2 . PHE A 1 92  ? 8.071   58.863  -51.241  1.00 96.39  ?  90  PHE A CD2 1 
ATOM   660  C  CE1 . PHE A 1 92  ? 10.478  58.801  -49.892  1.00 101.73 ?  90  PHE A CE1 1 
ATOM   661  C  CE2 . PHE A 1 92  ? 8.089   58.734  -49.863  1.00 97.66  ?  90  PHE A CE2 1 
ATOM   662  C  CZ  . PHE A 1 92  ? 9.294   58.703  -49.188  1.00 100.47 ?  90  PHE A CZ  1 
ATOM   663  N  N   . GLY A 1 93  ? 9.626   55.719  -53.001  1.00 104.45 ?  91  GLY A N   1 
ATOM   664  C  CA  . GLY A 1 93  ? 9.155   54.563  -52.263  1.00 106.51 ?  91  GLY A CA  1 
ATOM   665  C  C   . GLY A 1 93  ? 10.348  53.853  -51.667  1.00 117.15 ?  91  GLY A C   1 
ATOM   666  O  O   . GLY A 1 93  ? 11.496  54.273  -51.838  1.00 114.67 ?  91  GLY A O   1 
ATOM   667  N  N   . LEU A 1 94  ? 10.068  52.764  -50.960  1.00 118.25 ?  92  LEU A N   1 
ATOM   668  C  CA  . LEU A 1 94  ? 11.147  52.076  -50.272  1.00 121.27 ?  92  LEU A CA  1 
ATOM   669  C  C   . LEU A 1 94  ? 12.054  51.376  -51.283  1.00 124.89 ?  92  LEU A C   1 
ATOM   670  O  O   . LEU A 1 94  ? 11.720  51.217  -52.461  1.00 127.27 ?  92  LEU A O   1 
ATOM   671  C  CB  . LEU A 1 94  ? 10.587  51.068  -49.269  1.00 126.36 ?  92  LEU A CB  1 
ATOM   672  C  CG  . LEU A 1 94  ? 9.204   51.359  -48.681  1.00 124.90 ?  92  LEU A CG  1 
ATOM   673  C  CD1 . LEU A 1 94  ? 8.707   50.164  -47.881  1.00 127.41 ?  92  LEU A CD1 1 
ATOM   674  C  CD2 . LEU A 1 94  ? 9.225   52.614  -47.820  1.00 119.17 ?  92  LEU A CD2 1 
ATOM   675  N  N   . TYR A 1 95  ? 13.222  50.947  -50.800  1.00 128.81 ?  93  TYR A N   1 
ATOM   676  C  CA  . TYR A 1 95  ? 14.172  50.175  -51.605  1.00 133.65 ?  93  TYR A CA  1 
ATOM   677  C  C   . TYR A 1 95  ? 14.489  50.862  -52.932  1.00 130.03 ?  93  TYR A C   1 
ATOM   678  O  O   . TYR A 1 95  ? 14.827  50.208  -53.923  1.00 131.75 ?  93  TYR A O   1 
ATOM   679  C  CB  . TYR A 1 95  ? 13.650  48.756  -51.831  1.00 135.70 ?  93  TYR A CB  1 
ATOM   680  C  CG  . TYR A 1 95  ? 12.810  48.258  -50.675  1.00 137.56 ?  93  TYR A CG  1 
ATOM   681  C  CD1 . TYR A 1 95  ? 13.386  48.003  -49.437  1.00 143.28 ?  93  TYR A CD1 1 
ATOM   682  C  CD2 . TYR A 1 95  ? 11.442  48.068  -50.813  1.00 133.51 ?  93  TYR A CD2 1 
ATOM   683  C  CE1 . TYR A 1 95  ? 12.625  47.559  -48.373  1.00 144.76 ?  93  TYR A CE1 1 
ATOM   684  C  CE2 . TYR A 1 95  ? 10.672  47.622  -49.754  1.00 135.84 ?  93  TYR A CE2 1 
ATOM   685  C  CZ  . TYR A 1 95  ? 11.269  47.370  -48.536  1.00 139.61 ?  93  TYR A CZ  1 
ATOM   686  O  OH  . TYR A 1 95  ? 10.510  46.927  -47.477  1.00 141.65 ?  93  TYR A OH  1 
ATOM   687  N  N   . LYS A 1 96  ? 14.386  52.189  -52.957  1.00 126.99 ?  94  LYS A N   1 
ATOM   688  C  CA  . LYS A 1 96  ? 14.683  52.975  -54.151  1.00 122.97 ?  94  LYS A CA  1 
ATOM   689  C  C   . LYS A 1 96  ? 16.087  52.697  -54.679  1.00 128.73 ?  94  LYS A C   1 
ATOM   690  O  O   . LYS A 1 96  ? 16.950  53.576  -54.668  1.00 132.63 ?  94  LYS A O   1 
ATOM   691  C  CB  . LYS A 1 96  ? 14.522  54.469  -53.858  1.00 120.96 ?  94  LYS A CB  1 
ATOM   692  N  N   . VAL A 1 105 ? 7.381   46.634  -69.652  1.00 97.67  ?  103 VAL A N   1 
ATOM   693  C  CA  . VAL A 1 105 ? 6.469   47.582  -69.023  1.00 94.66  ?  103 VAL A CA  1 
ATOM   694  C  C   . VAL A 1 105 ? 5.371   47.993  -70.003  1.00 90.23  ?  103 VAL A C   1 
ATOM   695  O  O   . VAL A 1 105 ? 4.225   48.199  -69.603  1.00 89.93  ?  103 VAL A O   1 
ATOM   696  C  CB  . VAL A 1 105 ? 7.225   48.811  -68.477  1.00 101.51 ?  103 VAL A CB  1 
ATOM   697  C  CG1 . VAL A 1 105 ? 7.661   49.727  -69.609  1.00 103.52 ?  103 VAL A CG1 1 
ATOM   698  C  CG2 . VAL A 1 105 ? 6.360   49.560  -67.471  1.00 101.24 ?  103 VAL A CG2 1 
ATOM   699  N  N   . THR A 1 106 ? 5.723   48.122  -71.285  1.00 91.01  ?  104 THR A N   1 
ATOM   700  C  CA  . THR A 1 106 ? 4.713   48.410  -72.300  1.00 91.93  ?  104 THR A CA  1 
ATOM   701  C  C   . THR A 1 106 ? 3.614   47.354  -72.283  1.00 85.01  ?  104 THR A C   1 
ATOM   702  O  O   . THR A 1 106 ? 2.422   47.681  -72.262  1.00 87.10  ?  104 THR A O   1 
ATOM   703  C  CB  . THR A 1 106 ? 5.358   48.490  -73.684  1.00 91.83  ?  104 THR A CB  1 
ATOM   704  O  OG1 . THR A 1 106 ? 5.935   47.221  -74.019  1.00 97.83  ?  104 THR A OG1 1 
ATOM   705  C  CG2 . THR A 1 106 ? 6.441   49.557  -73.708  1.00 91.75  ?  104 THR A CG2 1 
ATOM   706  N  N   . ASP A 1 107 ? 4.001   46.075  -72.299  1.00 80.82  ?  105 ASP A N   1 
ATOM   707  C  CA  . ASP A 1 107 ? 3.011   45.005  -72.237  1.00 85.14  ?  105 ASP A CA  1 
ATOM   708  C  C   . ASP A 1 107 ? 2.191   45.099  -70.958  1.00 76.54  ?  105 ASP A C   1 
ATOM   709  O  O   . ASP A 1 107 ? 0.966   44.927  -70.982  1.00 75.50  ?  105 ASP A O   1 
ATOM   710  C  CB  . ASP A 1 107 ? 3.694   43.644  -72.358  1.00 86.17  ?  105 ASP A CB  1 
ATOM   711  C  CG  . ASP A 1 107 ? 4.412   43.474  -73.683  1.00 87.72  ?  105 ASP A CG  1 
ATOM   712  O  OD1 . ASP A 1 107 ? 4.346   44.401  -74.518  1.00 89.30  ?  105 ASP A OD1 1 
ATOM   713  O  OD2 . ASP A 1 107 ? 5.036   42.413  -73.892  1.00 92.67  -1 105 ASP A OD2 1 
ATOM   714  N  N   . PHE A 1 108 ? 2.848   45.360  -69.825  1.00 80.40  ?  106 PHE A N   1 
ATOM   715  C  CA  . PHE A 1 108 ? 2.102   45.543  -68.586  1.00 82.17  ?  106 PHE A CA  1 
ATOM   716  C  C   . PHE A 1 108 ? 1.105   46.680  -68.739  1.00 78.53  ?  106 PHE A C   1 
ATOM   717  O  O   . PHE A 1 108 ? -0.033  46.593  -68.264  1.00 73.17  ?  106 PHE A O   1 
ATOM   718  C  CB  . PHE A 1 108 ? 3.057   45.827  -67.426  1.00 81.47  ?  106 PHE A CB  1 
ATOM   719  C  CG  . PHE A 1 108 ? 2.360   46.220  -66.154  1.00 82.51  ?  106 PHE A CG  1 
ATOM   720  C  CD1 . PHE A 1 108 ? 1.819   45.258  -65.319  1.00 81.44  ?  106 PHE A CD1 1 
ATOM   721  C  CD2 . PHE A 1 108 ? 2.228   47.555  -65.805  1.00 85.08  ?  106 PHE A CD2 1 
ATOM   722  C  CE1 . PHE A 1 108 ? 1.175   45.618  -64.151  1.00 82.95  ?  106 PHE A CE1 1 
ATOM   723  C  CE2 . PHE A 1 108 ? 1.580   47.921  -64.640  1.00 86.58  ?  106 PHE A CE2 1 
ATOM   724  C  CZ  . PHE A 1 108 ? 1.053   46.951  -63.812  1.00 85.50  ?  106 PHE A CZ  1 
ATOM   725  N  N   . ASN A 1 109 ? 1.515   47.750  -69.425  1.00 79.42  ?  107 ASN A N   1 
ATOM   726  C  CA  . ASN A 1 109 ? 0.651   48.912  -69.581  1.00 78.53  ?  107 ASN A CA  1 
ATOM   727  C  C   . ASN A 1 109 ? -0.581  48.549  -70.397  1.00 70.36  ?  107 ASN A C   1 
ATOM   728  O  O   . ASN A 1 109 ? -1.703  48.946  -70.060  1.00 72.08  ?  107 ASN A O   1 
ATOM   729  C  CB  . ASN A 1 109 ? 1.428   50.053  -70.238  1.00 79.74  ?  107 ASN A CB  1 
ATOM   730  C  CG  . ASN A 1 109 ? 2.405   50.719  -69.284  1.00 84.98  ?  107 ASN A CG  1 
ATOM   731  O  OD1 . ASN A 1 109 ? 2.407   50.441  -68.085  1.00 86.63  ?  107 ASN A OD1 1 
ATOM   732  N  ND2 . ASN A 1 109 ? 3.249   51.596  -69.817  1.00 89.26  ?  107 ASN A ND2 1 
ATOM   733  N  N   . ALA A 1 110 ? -0.385  47.798  -71.484  1.00 75.50  ?  108 ALA A N   1 
ATOM   734  C  CA  . ALA A 1 110 ? -1.505  47.365  -72.312  1.00 69.04  ?  108 ALA A CA  1 
ATOM   735  C  C   . ALA A 1 110 ? -2.438  46.454  -71.524  1.00 68.17  ?  108 ALA A C   1 
ATOM   736  O  O   . ALA A 1 110 ? -3.664  46.610  -71.567  1.00 63.86  ?  108 ALA A O   1 
ATOM   737  C  CB  . ALA A 1 110 ? -0.988  46.658  -73.566  1.00 64.83  ?  108 ALA A CB  1 
ATOM   738  N  N   . ILE A 1 111 ? -1.868  45.491  -70.795  1.00 72.54  ?  109 ILE A N   1 
ATOM   739  C  CA  . ILE A 1 111 ? -2.682  44.559  -70.022  1.00 66.29  ?  109 ILE A CA  1 
ATOM   740  C  C   . ILE A 1 111 ? -3.467  45.297  -68.949  1.00 65.30  ?  109 ILE A C   1 
ATOM   741  O  O   . ILE A 1 111 ? -4.590  44.905  -68.607  1.00 62.11  ?  109 ILE A O   1 
ATOM   742  C  CB  . ILE A 1 111 ? -1.786  43.464  -69.407  1.00 65.31  ?  109 ILE A CB  1 
ATOM   743  C  CG1 . ILE A 1 111 ? -1.148  42.608  -70.504  1.00 62.31  ?  109 ILE A CG1 1 
ATOM   744  C  CG2 . ILE A 1 111 ? -2.568  42.616  -68.410  1.00 60.72  ?  109 ILE A CG2 1 
ATOM   745  C  CD1 . ILE A 1 111 ? -0.017  41.726  -70.009  1.00 70.91  ?  109 ILE A CD1 1 
ATOM   746  N  N   . ALA A 1 112 ? -2.906  46.380  -68.413  1.00 64.03  ?  110 ALA A N   1 
ATOM   747  C  CA  . ALA A 1 112 ? -3.572  47.102  -67.336  1.00 66.17  ?  110 ALA A CA  1 
ATOM   748  C  C   . ALA A 1 112 ? -4.653  48.042  -67.853  1.00 64.86  ?  110 ALA A C   1 
ATOM   749  O  O   . ALA A 1 112 ? -5.634  48.296  -67.146  1.00 69.01  ?  110 ALA A O   1 
ATOM   750  C  CB  . ALA A 1 112 ? -2.547  47.889  -66.517  1.00 75.30  ?  110 ALA A CB  1 
ATOM   751  N  N   . THR A 1 113 ? -4.494  48.571  -69.067  1.00 70.35  ?  111 THR A N   1 
ATOM   752  C  CA  . THR A 1 113 ? -5.407  49.574  -69.597  1.00 66.43  ?  111 THR A CA  1 
ATOM   753  C  C   . THR A 1 113 ? -6.436  49.022  -70.579  1.00 66.54  ?  111 THR A C   1 
ATOM   754  O  O   . THR A 1 113 ? -7.321  49.773  -71.002  1.00 65.02  ?  111 THR A O   1 
ATOM   755  C  CB  . THR A 1 113 ? -4.609  50.696  -70.270  1.00 65.65  ?  111 THR A CB  1 
ATOM   756  O  OG1 . THR A 1 113 ? -3.681  50.129  -71.202  1.00 68.91  ?  111 THR A OG1 1 
ATOM   757  C  CG2 . THR A 1 113 ? -3.838  51.487  -69.226  1.00 70.79  ?  111 THR A CG2 1 
ATOM   758  N  N   . CYS A 1 114 ? -6.350  47.748  -70.952  1.00 60.69  ?  112 CYS A N   1 
ATOM   759  C  CA  . CYS A 1 114 ? -7.233  47.206  -71.974  1.00 57.24  ?  112 CYS A CA  1 
ATOM   760  C  C   . CYS A 1 114 ? -8.601  46.876  -71.375  1.00 60.23  ?  112 CYS A C   1 
ATOM   761  O  O   . CYS A 1 114 ? -8.766  46.776  -70.157  1.00 61.30  ?  112 CYS A O   1 
ATOM   762  C  CB  . CYS A 1 114 ? -6.611  45.970  -72.628  1.00 51.16  ?  112 CYS A CB  1 
ATOM   763  S  SG  . CYS A 1 114 ? -6.802  44.430  -71.709  1.00 56.75  ?  112 CYS A SG  1 
ATOM   764  N  N   . ASP A 1 115 ? -9.593  46.709  -72.253  1.00 60.53  ?  113 ASP A N   1 
ATOM   765  C  CA  . ASP A 1 115 ? -10.949 46.374  -71.833  1.00 58.16  ?  113 ASP A CA  1 
ATOM   766  C  C   . ASP A 1 115 ? -11.324 44.930  -72.140  1.00 53.35  ?  113 ASP A C   1 
ATOM   767  O  O   . ASP A 1 115 ? -12.455 44.523  -71.855  1.00 59.23  ?  113 ASP A O   1 
ATOM   768  C  CB  . ASP A 1 115 ? -11.967 47.319  -72.486  1.00 59.79  ?  113 ASP A CB  1 
ATOM   769  C  CG  . ASP A 1 115 ? -11.929 47.265  -74.001  1.00 57.75  ?  113 ASP A CG  1 
ATOM   770  O  OD1 . ASP A 1 115 ? -11.077 46.540  -74.555  1.00 57.67  ?  113 ASP A OD1 1 
ATOM   771  O  OD2 . ASP A 1 115 ? -12.757 47.948  -74.640  1.00 68.24  -1 113 ASP A OD2 1 
ATOM   772  N  N   . TRP A 1 116 ? -10.413 44.156  -72.728  1.00 51.97  ?  114 TRP A N   1 
ATOM   773  C  CA  . TRP A 1 116 ? -10.592 42.732  -72.998  1.00 54.83  ?  114 TRP A CA  1 
ATOM   774  C  C   . TRP A 1 116 ? -11.669 42.451  -74.036  1.00 54.30  ?  114 TRP A C   1 
ATOM   775  O  O   . TRP A 1 116 ? -12.237 41.353  -74.062  1.00 52.66  ?  114 TRP A O   1 
ATOM   776  C  CB  . TRP A 1 116 ? -10.887 41.969  -71.704  1.00 50.00  ?  114 TRP A CB  1 
ATOM   777  C  CG  . TRP A 1 116 ? -9.822  42.180  -70.684  1.00 56.33  ?  114 TRP A CG  1 
ATOM   778  C  CD1 . TRP A 1 116 ? -9.885  42.991  -69.589  1.00 53.72  ?  114 TRP A CD1 1 
ATOM   779  C  CD2 . TRP A 1 116 ? -8.515  41.591  -70.672  1.00 59.28  ?  114 TRP A CD2 1 
ATOM   780  N  NE1 . TRP A 1 116 ? -8.704  42.936  -68.892  1.00 60.01  ?  114 TRP A NE1 1 
ATOM   781  C  CE2 . TRP A 1 116 ? -7.846  42.083  -69.535  1.00 59.55  ?  114 TRP A CE2 1 
ATOM   782  C  CE3 . TRP A 1 116 ? -7.848  40.690  -71.510  1.00 56.20  ?  114 TRP A CE3 1 
ATOM   783  C  CZ2 . TRP A 1 116 ? -6.543  41.707  -69.213  1.00 59.27  ?  114 TRP A CZ2 1 
ATOM   784  C  CZ3 . TRP A 1 116 ? -6.554  40.318  -71.189  1.00 56.21  ?  114 TRP A CZ3 1 
ATOM   785  C  CH2 . TRP A 1 116 ? -5.916  40.826  -70.050  1.00 58.64  ?  114 TRP A CH2 1 
ATOM   786  N  N   . THR A 1 117 ? -11.943 43.414  -74.911  1.00 52.94  ?  115 THR A N   1 
ATOM   787  C  CA  . THR A 1 117 ? -12.919 43.245  -75.975  1.00 56.51  ?  115 THR A CA  1 
ATOM   788  C  C   . THR A 1 117 ? -12.258 42.910  -77.302  1.00 52.43  ?  115 THR A C   1 
ATOM   789  O  O   . THR A 1 117 ? -12.955 42.548  -78.255  1.00 53.94  ?  115 THR A O   1 
ATOM   790  C  CB  . THR A 1 117 ? -13.767 44.513  -76.139  1.00 60.24  ?  115 THR A CB  1 
ATOM   791  O  OG1 . THR A 1 117 ? -12.918 45.611  -76.490  1.00 57.22  ?  115 THR A OG1 1 
ATOM   792  C  CG2 . THR A 1 117 ? -14.496 44.838  -74.847  1.00 65.34  ?  115 THR A CG2 1 
ATOM   793  N  N   . ASN A 1 118 ? -10.936 43.023  -77.377  1.00 51.96  ?  116 ASN A N   1 
ATOM   794  C  CA  . ASN A 1 118 ? -10.176 42.799  -78.594  1.00 52.72  ?  116 ASN A CA  1 
ATOM   795  C  C   . ASN A 1 118 ? -9.342  41.535  -78.451  1.00 49.46  ?  116 ASN A C   1 
ATOM   796  O  O   . ASN A 1 118 ? -8.895  41.186  -77.355  1.00 49.87  ?  116 ASN A O   1 
ATOM   797  C  CB  . ASN A 1 118 ? -9.249  43.981  -78.895  1.00 52.72  ?  116 ASN A CB  1 
ATOM   798  C  CG  . ASN A 1 118 ? -9.929  45.320  -78.703  1.00 53.71  ?  116 ASN A CG  1 
ATOM   799  O  OD1 . ASN A 1 118 ? -10.422 45.920  -79.656  1.00 50.57  ?  116 ASN A OD1 1 
ATOM   800  N  ND2 . ASN A 1 118 ? -9.953  45.799  -77.464  1.00 54.37  ?  116 ASN A ND2 1 
ATOM   801  N  N   . ALA A 1 119 ? -9.138  40.849  -79.576  1.00 45.54  ?  117 ALA A N   1 
ATOM   802  C  CA  . ALA A 1 119 ? -8.358  39.618  -79.551  1.00 50.83  ?  117 ALA A CA  1 
ATOM   803  C  C   . ALA A 1 119 ? -6.901  39.896  -79.209  1.00 49.30  ?  117 ALA A C   1 
ATOM   804  O  O   . ALA A 1 119 ? -6.248  39.067  -78.563  1.00 48.46  ?  117 ALA A O   1 
ATOM   805  C  CB  . ALA A 1 119 ? -8.467  38.894  -80.892  1.00 45.81  ?  117 ALA A CB  1 
ATOM   806  N  N   . GLY A 1 120 ? -6.378  41.050  -79.633  1.00 47.17  ?  118 GLY A N   1 
ATOM   807  C  CA  . GLY A 1 120 ? -5.009  41.405  -79.298  1.00 49.54  ?  118 GLY A CA  1 
ATOM   808  C  C   . GLY A 1 120 ? -4.749  41.450  -77.805  1.00 51.87  ?  118 GLY A C   1 
ATOM   809  O  O   . GLY A 1 120 ? -3.615  41.245  -77.363  1.00 52.53  ?  118 GLY A O   1 
ATOM   810  N  N   . ASP A 1 121 ? -5.783  41.726  -77.007  1.00 49.61  ?  119 ASP A N   1 
ATOM   811  C  CA  . ASP A 1 121 ? -5.619  41.679  -75.559  1.00 50.24  ?  119 ASP A CA  1 
ATOM   812  C  C   . ASP A 1 121 ? -5.295  40.263  -75.105  1.00 54.65  ?  119 ASP A C   1 
ATOM   813  O  O   . ASP A 1 121 ? -4.398  40.051  -74.281  1.00 58.57  ?  119 ASP A O   1 
ATOM   814  C  CB  . ASP A 1 121 ? -6.883  42.192  -74.871  1.00 50.51  ?  119 ASP A CB  1 
ATOM   815  C  CG  . ASP A 1 121 ? -7.274  43.586  -75.331  1.00 54.08  ?  119 ASP A CG  1 
ATOM   816  O  OD1 . ASP A 1 121 ? -6.479  44.222  -76.056  1.00 51.98  ?  119 ASP A OD1 1 
ATOM   817  O  OD2 . ASP A 1 121 ? -8.386  44.038  -74.985  1.00 50.52  -1 119 ASP A OD2 1 
ATOM   818  N  N   . TYR A 1 122 ? -6.011  39.277  -75.649  1.00 55.00  ?  120 TYR A N   1 
ATOM   819  C  CA  . TYR A 1 122 ? -5.796  37.892  -75.255  1.00 54.35  ?  120 TYR A CA  1 
ATOM   820  C  C   . TYR A 1 122 ? -4.491  37.365  -75.828  1.00 55.19  ?  120 TYR A C   1 
ATOM   821  O  O   . TYR A 1 122 ? -3.859  36.484  -75.235  1.00 54.13  ?  120 TYR A O   1 
ATOM   822  C  CB  . TYR A 1 122 ? -6.977  37.043  -75.716  1.00 53.33  ?  120 TYR A CB  1 
ATOM   823  C  CG  . TYR A 1 122 ? -8.283  37.486  -75.102  1.00 55.65  ?  120 TYR A CG  1 
ATOM   824  C  CD1 . TYR A 1 122 ? -9.052  38.471  -75.705  1.00 51.15  ?  120 TYR A CD1 1 
ATOM   825  C  CD2 . TYR A 1 122 ? -8.750  36.919  -73.925  1.00 51.48  ?  120 TYR A CD2 1 
ATOM   826  C  CE1 . TYR A 1 122 ? -10.240 38.892  -75.147  1.00 48.54  ?  120 TYR A CE1 1 
ATOM   827  C  CE2 . TYR A 1 122 ? -9.943  37.326  -73.363  1.00 45.91  ?  120 TYR A CE2 1 
ATOM   828  C  CZ  . TYR A 1 122 ? -10.683 38.314  -73.977  1.00 47.96  ?  120 TYR A CZ  1 
ATOM   829  O  OH  . TYR A 1 122 ? -11.876 38.720  -73.425  1.00 48.41  ?  120 TYR A OH  1 
ATOM   830  N  N   . ILE A 1 123 ? -4.075  37.896  -76.979  1.00 55.80  ?  121 ILE A N   1 
ATOM   831  C  CA  . ILE A 1 123 ? -2.808  37.490  -77.575  1.00 57.79  ?  121 ILE A CA  1 
ATOM   832  C  C   . ILE A 1 123 ? -1.657  37.905  -76.669  1.00 59.98  ?  121 ILE A C   1 
ATOM   833  O  O   . ILE A 1 123 ? -0.759  37.111  -76.366  1.00 59.64  ?  121 ILE A O   1 
ATOM   834  C  CB  . ILE A 1 123 ? -2.671  38.091  -78.986  1.00 58.45  ?  121 ILE A CB  1 
ATOM   835  C  CG1 . ILE A 1 123 ? -3.733  37.499  -79.915  1.00 58.66  ?  121 ILE A CG1 1 
ATOM   836  C  CG2 . ILE A 1 123 ? -1.273  37.856  -79.537  1.00 63.30  ?  121 ILE A CG2 1 
ATOM   837  C  CD1 . ILE A 1 123 ? -3.637  37.979  -81.343  1.00 56.74  ?  121 ILE A CD1 1 
ATOM   838  N  N   . LEU A 1 124 ? -1.675  39.164  -76.221  1.00 60.00  ?  122 LEU A N   1 
ATOM   839  C  CA  . LEU A 1 124 ? -0.655  39.649  -75.298  1.00 58.33  ?  122 LEU A CA  1 
ATOM   840  C  C   . LEU A 1 124 ? -0.669  38.865  -73.990  1.00 64.43  ?  122 LEU A C   1 
ATOM   841  O  O   . LEU A 1 124 ? 0.390   38.547  -73.438  1.00 69.13  ?  122 LEU A O   1 
ATOM   842  C  CB  . LEU A 1 124 ? -0.861  41.141  -75.034  1.00 59.27  ?  122 LEU A CB  1 
ATOM   843  C  CG  . LEU A 1 124 ? 0.333   41.922  -74.486  1.00 70.39  ?  122 LEU A CG  1 
ATOM   844  C  CD1 . LEU A 1 124 ? 1.409   42.090  -75.550  1.00 71.77  ?  122 LEU A CD1 1 
ATOM   845  C  CD2 . LEU A 1 124 ? -0.117  43.275  -73.954  1.00 70.66  ?  122 LEU A CD2 1 
ATOM   846  N  N   . ALA A 1 125 ? -1.861  38.548  -73.475  1.00 58.15  ?  123 ALA A N   1 
ATOM   847  C  CA  . ALA A 1 125 ? -1.972  37.855  -72.195  1.00 61.04  ?  123 ALA A CA  1 
ATOM   848  C  C   . ALA A 1 125 ? -1.368  36.457  -72.229  1.00 64.44  ?  123 ALA A C   1 
ATOM   849  O  O   . ALA A 1 125 ? -1.300  35.802  -71.183  1.00 58.81  ?  123 ALA A O   1 
ATOM   850  C  CB  . ALA A 1 125 ? -3.437  37.775  -71.765  1.00 55.29  ?  123 ALA A CB  1 
ATOM   851  N  N   . ASN A 1 126 ? -0.922  35.996  -73.397  1.00 66.87  ?  124 ASN A N   1 
ATOM   852  C  CA  . ASN A 1 126 ? -0.358  34.666  -73.561  1.00 68.29  ?  124 ASN A CA  1 
ATOM   853  C  C   . ASN A 1 126 ? 1.024   34.693  -74.190  1.00 68.64  ?  124 ASN A C   1 
ATOM   854  O  O   . ASN A 1 126 ? 1.679   33.647  -74.251  1.00 75.40  ?  124 ASN A O   1 
ATOM   855  C  CB  . ASN A 1 126 ? -1.281  33.791  -74.423  1.00 59.96  ?  124 ASN A CB  1 
ATOM   856  C  CG  . ASN A 1 126 ? -2.210  32.934  -73.592  1.00 64.28  ?  124 ASN A CG  1 
ATOM   857  O  OD1 . ASN A 1 126 ? -1.792  31.942  -72.996  1.00 67.01  ?  124 ASN A OD1 1 
ATOM   858  N  ND2 . ASN A 1 126 ? -3.477  33.326  -73.532  1.00 63.72  ?  124 ASN A ND2 1 
ATOM   859  N  N   . THR A 1 127 ? 1.488   35.855  -74.646  1.00 71.89  ?  125 THR A N   1 
ATOM   860  C  CA  . THR A 1 127 ? 2.823   36.032  -75.195  1.00 74.67  ?  125 THR A CA  1 
ATOM   861  C  C   . THR A 1 127 ? 3.726   36.805  -74.243  1.00 79.25  ?  125 THR A C   1 
ATOM   862  O  O   . THR A 1 127 ? 4.840   37.183  -74.622  1.00 83.19  ?  125 THR A O   1 
ATOM   863  C  CB  . THR A 1 127 ? 2.740   36.749  -76.544  1.00 78.73  ?  125 THR A CB  1 
ATOM   864  O  OG1 . THR A 1 127 ? 1.987   37.960  -76.393  1.00 71.77  ?  125 THR A OG1 1 
ATOM   865  C  CG2 . THR A 1 127 ? 2.046   35.864  -77.571  1.00 75.09  ?  125 THR A CG2 1 
ATOM   866  N  N   . CYS A 1 128 ? 3.268   37.045  -73.017  1.00 75.06  ?  126 CYS A N   1 
ATOM   867  C  CA  . CYS A 1 128 ? 3.974   37.842  -72.028  1.00 82.61  ?  126 CYS A CA  1 
ATOM   868  C  C   . CYS A 1 128 ? 4.679   36.927  -71.027  1.00 82.91  ?  126 CYS A C   1 
ATOM   869  O  O   . CYS A 1 128 ? 4.612   35.698  -71.109  1.00 89.85  ?  126 CYS A O   1 
ATOM   870  C  CB  . CYS A 1 128 ? 3.006   38.805  -71.336  1.00 82.32  ?  126 CYS A CB  1 
ATOM   871  S  SG  . CYS A 1 128 ? 1.648   38.010  -70.444  1.00 78.17  ?  126 CYS A SG  1 
ATOM   872  N  N   . THR A 1 129 ? 5.373   37.538  -70.071  1.00 83.26  ?  127 THR A N   1 
ATOM   873  C  CA  . THR A 1 129 ? 6.022   36.776  -69.015  1.00 86.81  ?  127 THR A CA  1 
ATOM   874  C  C   . THR A 1 129 ? 4.987   36.087  -68.127  1.00 83.19  ?  127 THR A C   1 
ATOM   875  O  O   . THR A 1 129 ? 3.803   36.435  -68.120  1.00 84.02  ?  127 THR A O   1 
ATOM   876  C  CB  . THR A 1 129 ? 6.910   37.688  -68.169  1.00 92.58  ?  127 THR A CB  1 
ATOM   877  O  OG1 . THR A 1 129 ? 6.110   38.358  -67.186  1.00 88.79  ?  127 THR A OG1 1 
ATOM   878  C  CG2 . THR A 1 129 ? 7.589   38.728  -69.048  1.00 91.63  ?  127 THR A CG2 1 
ATOM   879  N  N   . GLU A 1 130 ? 5.454   35.091  -67.367  1.00 87.25  ?  128 GLU A N   1 
ATOM   880  C  CA  . GLU A 1 130 ? 4.542   34.309  -66.537  1.00 86.24  ?  128 GLU A CA  1 
ATOM   881  C  C   . GLU A 1 130 ? 3.797   35.202  -65.554  1.00 85.01  ?  128 GLU A C   1 
ATOM   882  O  O   . GLU A 1 130 ? 2.565   35.148  -65.462  1.00 90.48  ?  128 GLU A O   1 
ATOM   883  C  CB  . GLU A 1 130 ? 5.302   33.206  -65.798  1.00 91.99  ?  128 GLU A CB  1 
ATOM   884  C  CG  . GLU A 1 130 ? 5.364   31.881  -66.551  1.00 92.32  ?  128 GLU A CG  1 
ATOM   885  C  CD  . GLU A 1 130 ? 4.000   31.237  -66.744  1.00 87.85  ?  128 GLU A CD  1 
ATOM   886  O  OE1 . GLU A 1 130 ? 3.268   31.055  -65.749  1.00 87.90  ?  128 GLU A OE1 1 
ATOM   887  O  OE2 . GLU A 1 130 ? 3.665   30.903  -67.899  1.00 92.02  -1 128 GLU A OE2 1 
ATOM   888  N  N   . ARG A 1 131 ? 4.528   36.023  -64.795  1.00 88.91  ?  129 ARG A N   1 
ATOM   889  C  CA  . ARG A 1 131 ? 3.861   36.890  -63.831  1.00 88.53  ?  129 ARG A CA  1 
ATOM   890  C  C   . ARG A 1 131 ? 2.847   37.779  -64.540  1.00 83.17  ?  129 ARG A C   1 
ATOM   891  O  O   . ARG A 1 131 ? 1.741   38.002  -64.035  1.00 86.85  ?  129 ARG A O   1 
ATOM   892  C  CB  . ARG A 1 131 ? 4.883   37.728  -63.061  1.00 96.64  ?  129 ARG A CB  1 
ATOM   893  C  CG  . ARG A 1 131 ? 4.386   38.170  -61.691  1.00 96.08  ?  129 ARG A CG  1 
ATOM   894  C  CD  . ARG A 1 131 ? 5.448   38.913  -60.894  1.00 111.14 ?  129 ARG A CD  1 
ATOM   895  N  NE  . ARG A 1 131 ? 6.708   38.185  -60.802  1.00 120.00 ?  129 ARG A NE  1 
ATOM   896  C  CZ  . ARG A 1 131 ? 7.878   38.666  -61.200  1.00 119.61 ?  129 ARG A CZ  1 
ATOM   897  N  NH1 . ARG A 1 131 ? 8.012   39.925  -61.584  1.00 118.77 ?  129 ARG A NH1 1 
ATOM   898  N  NH2 . ARG A 1 131 ? 8.950   37.880  -61.159  1.00 117.11 ?  129 ARG A NH2 1 
ATOM   899  N  N   . LEU A 1 132 ? 3.216   38.300  -65.713  1.00 81.13  ?  130 LEU A N   1 
ATOM   900  C  CA  . LEU A 1 132 ? 2.278   39.091  -66.504  1.00 84.82  ?  130 LEU A CA  1 
ATOM   901  C  C   . LEU A 1 132 ? 1.086   38.244  -66.933  1.00 83.52  ?  130 LEU A C   1 
ATOM   902  O  O   . LEU A 1 132 ? -0.049  38.734  -66.974  1.00 77.78  ?  130 LEU A O   1 
ATOM   903  C  CB  . LEU A 1 132 ? 2.988   39.691  -67.718  1.00 82.72  ?  130 LEU A CB  1 
ATOM   904  C  CG  . LEU A 1 132 ? 3.653   41.048  -67.475  1.00 85.84  ?  130 LEU A CG  1 
ATOM   905  C  CD1 . LEU A 1 132 ? 4.175   41.638  -68.776  1.00 83.89  ?  130 LEU A CD1 1 
ATOM   906  C  CD2 . LEU A 1 132 ? 2.678   42.003  -66.803  1.00 81.91  ?  130 LEU A CD2 1 
ATOM   907  N  N   . LYS A 1 133 ? 1.327   36.971  -67.271  1.00 82.54  ?  131 LYS A N   1 
ATOM   908  C  CA  . LYS A 1 133 ? 0.223   36.093  -67.644  1.00 76.10  ?  131 LYS A CA  1 
ATOM   909  C  C   . LYS A 1 133 ? -0.761  35.961  -66.495  1.00 74.47  ?  131 LYS A C   1 
ATOM   910  O  O   . LYS A 1 133 ? -1.974  35.863  -66.716  1.00 75.15  ?  131 LYS A O   1 
ATOM   911  C  CB  . LYS A 1 133 ? 0.736   34.702  -68.024  1.00 73.11  ?  131 LYS A CB  1 
ATOM   912  C  CG  . LYS A 1 133 ? 1.585   34.599  -69.281  1.00 78.29  ?  131 LYS A CG  1 
ATOM   913  C  CD  . LYS A 1 133 ? 1.631   33.138  -69.733  1.00 81.47  ?  131 LYS A CD  1 
ATOM   914  C  CE  . LYS A 1 133 ? 2.884   32.802  -70.533  1.00 77.44  ?  131 LYS A CE  1 
ATOM   915  N  NZ  . LYS A 1 133 ? 2.997   33.582  -71.793  1.00 84.43  ?  131 LYS A NZ  1 
ATOM   916  N  N   . LEU A 1 134 ? -0.254  35.973  -65.261  1.00 73.06  ?  132 LEU A N   1 
ATOM   917  C  CA  . LEU A 1 134 ? -1.100  35.776  -64.095  1.00 74.45  ?  132 LEU A CA  1 
ATOM   918  C  C   . LEU A 1 134 ? -1.802  37.071  -63.718  1.00 78.96  ?  132 LEU A C   1 
ATOM   919  O  O   . LEU A 1 134 ? -2.903  37.037  -63.155  1.00 83.17  ?  132 LEU A O   1 
ATOM   920  C  CB  . LEU A 1 134 ? -0.262  35.245  -62.930  1.00 79.81  ?  132 LEU A CB  1 
ATOM   921  C  CG  . LEU A 1 134 ? -0.942  34.273  -61.966  1.00 83.73  ?  132 LEU A CG  1 
ATOM   922  C  CD1 . LEU A 1 134 ? -1.160  32.932  -62.648  1.00 81.10  ?  132 LEU A CD1 1 
ATOM   923  C  CD2 . LEU A 1 134 ? -0.111  34.099  -60.706  1.00 88.01  ?  132 LEU A CD2 1 
ATOM   924  N  N   . PHE A 1 135 ? -1.178  38.214  -64.015  1.00 73.07  ?  133 PHE A N   1 
ATOM   925  C  CA  . PHE A 1 135 ? -1.837  39.496  -63.802  1.00 72.10  ?  133 PHE A CA  1 
ATOM   926  C  C   . PHE A 1 135 ? -2.993  39.654  -64.780  1.00 71.69  ?  133 PHE A C   1 
ATOM   927  O  O   . PHE A 1 135 ? -4.109  40.019  -64.392  1.00 66.47  ?  133 PHE A O   1 
ATOM   928  C  CB  . PHE A 1 135 ? -0.837  40.641  -63.975  1.00 74.60  ?  133 PHE A CB  1 
ATOM   929  C  CG  . PHE A 1 135 ? -1.448  42.009  -63.829  1.00 85.22  ?  133 PHE A CG  1 
ATOM   930  C  CD1 . PHE A 1 135 ? -2.330  42.282  -62.796  1.00 79.06  ?  133 PHE A CD1 1 
ATOM   931  C  CD2 . PHE A 1 135 ? -1.177  43.009  -64.751  1.00 83.71  ?  133 PHE A CD2 1 
ATOM   932  C  CE1 . PHE A 1 135 ? -2.900  43.536  -62.663  1.00 80.98  ?  133 PHE A CE1 1 
ATOM   933  C  CE2 . PHE A 1 135 ? -1.751  44.263  -64.627  1.00 83.11  ?  133 PHE A CE2 1 
ATOM   934  C  CZ  . PHE A 1 135 ? -2.613  44.527  -63.581  1.00 78.69  ?  133 PHE A CZ  1 
ATOM   935  N  N   . ALA A 1 136 ? -2.726  39.394  -66.064  1.00 71.77  ?  134 ALA A N   1 
ATOM   936  C  CA  . ALA A 1 136 ? -3.762  39.429  -67.090  1.00 66.02  ?  134 ALA A CA  1 
ATOM   937  C  C   . ALA A 1 136 ? -4.934  38.523  -66.731  1.00 66.22  ?  134 ALA A C   1 
ATOM   938  O  O   . ALA A 1 136 ? -6.100  38.915  -66.858  1.00 67.89  ?  134 ALA A O   1 
ATOM   939  C  CB  . ALA A 1 136 ? -3.168  39.030  -68.441  1.00 63.60  ?  134 ALA A CB  1 
ATOM   940  N  N   . ALA A 1 137 ? -4.642  37.293  -66.302  1.00 61.41  ?  135 ALA A N   1 
ATOM   941  C  CA  . ALA A 1 137 ? -5.710  36.348  -65.992  1.00 69.65  ?  135 ALA A CA  1 
ATOM   942  C  C   . ALA A 1 137 ? -6.631  36.912  -64.920  1.00 62.92  ?  135 ALA A C   1 
ATOM   943  O  O   . ALA A 1 137 ? -7.859  36.898  -65.063  1.00 67.24  ?  135 ALA A O   1 
ATOM   944  C  CB  . ALA A 1 137 ? -5.119  35.010  -65.550  1.00 64.29  ?  135 ALA A CB  1 
ATOM   945  N  N   . GLU A 1 138 ? -6.048  37.412  -63.832  1.00 66.10  ?  136 GLU A N   1 
ATOM   946  C  CA  . GLU A 1 138 ? -6.851  37.879  -62.710  1.00 74.89  ?  136 GLU A CA  1 
ATOM   947  C  C   . GLU A 1 138 ? -7.583  39.165  -63.078  1.00 73.24  ?  136 GLU A C   1 
ATOM   948  O  O   . GLU A 1 138 ? -8.749  39.354  -62.711  1.00 75.66  ?  136 GLU A O   1 
ATOM   949  C  CB  . GLU A 1 138 ? -5.942  38.066  -61.495  1.00 72.89  ?  136 GLU A CB  1 
ATOM   950  C  CG  . GLU A 1 138 ? -6.614  38.433  -60.194  1.00 81.19  ?  136 GLU A CG  1 
ATOM   951  C  CD  . GLU A 1 138 ? -5.597  38.847  -59.146  1.00 93.65  ?  136 GLU A CD  1 
ATOM   952  O  OE1 . GLU A 1 138 ? -4.384  38.719  -59.423  1.00 93.33  ?  136 GLU A OE1 1 
ATOM   953  O  OE2 . GLU A 1 138 ? -6.001  39.301  -58.055  1.00 92.01  -1 136 GLU A OE2 1 
ATOM   954  N  N   . THR A 1 139 ? -6.912  40.056  -63.811  1.00 70.78  ?  137 THR A N   1 
ATOM   955  C  CA  . THR A 1 139 ? -7.564  41.261  -64.312  1.00 72.22  ?  137 THR A CA  1 
ATOM   956  C  C   . THR A 1 139 ? -8.743  40.902  -65.208  1.00 67.77  ?  137 THR A C   1 
ATOM   957  O  O   . THR A 1 139 ? -9.844  41.446  -65.060  1.00 64.57  ?  137 THR A O   1 
ATOM   958  C  CB  . THR A 1 139 ? -6.552  42.126  -65.064  1.00 73.21  ?  137 THR A CB  1 
ATOM   959  O  OG1 . THR A 1 139 ? -5.319  42.158  -64.335  1.00 75.88  ?  137 THR A OG1 1 
ATOM   960  C  CG2 . THR A 1 139 ? -7.072  43.546  -65.222  1.00 67.55  ?  137 THR A CG2 1 
ATOM   961  N  N   . LEU A 1 140 ? -8.524  39.981  -66.151  1.00 64.13  ?  138 LEU A N   1 
ATOM   962  C  CA  . LEU A 1 140 ? -9.589  39.570  -67.060  1.00 62.29  ?  138 LEU A CA  1 
ATOM   963  C  C   . LEU A 1 140 ? -10.784 39.037  -66.281  1.00 64.57  ?  138 LEU A C   1 
ATOM   964  O  O   . LEU A 1 140 ? -11.929 39.434  -66.526  1.00 62.25  ?  138 LEU A O   1 
ATOM   965  C  CB  . LEU A 1 140 ? -9.061  38.517  -68.037  1.00 60.92  ?  138 LEU A CB  1 
ATOM   966  C  CG  . LEU A 1 140 ? -10.063 37.825  -68.963  1.00 57.72  ?  138 LEU A CG  1 
ATOM   967  C  CD1 . LEU A 1 140 ? -10.790 38.841  -69.826  1.00 50.93  ?  138 LEU A CD1 1 
ATOM   968  C  CD2 . LEU A 1 140 ? -9.363  36.784  -69.824  1.00 55.03  ?  138 LEU A CD2 1 
ATOM   969  N  N   . LYS A 1 141 ? -10.533 38.131  -65.333  1.00 66.00  ?  139 LYS A N   1 
ATOM   970  C  CA  . LYS A 1 141 ? -11.628 37.563  -64.556  1.00 67.60  ?  139 LYS A CA  1 
ATOM   971  C  C   . LYS A 1 141 ? -12.363 38.668  -63.809  1.00 72.22  ?  139 LYS A C   1 
ATOM   972  O  O   . LYS A 1 141 ? -13.599 38.679  -63.753  1.00 71.45  ?  139 LYS A O   1 
ATOM   973  C  CB  . LYS A 1 141 ? -11.087 36.513  -63.584  1.00 68.83  ?  139 LYS A CB  1 
ATOM   974  C  CG  . LYS A 1 141 ? -12.140 35.688  -62.858  1.00 74.02  ?  139 LYS A CG  1 
ATOM   975  C  CD  . LYS A 1 141 ? -12.259 34.292  -63.455  1.00 78.38  ?  139 LYS A CD  1 
ATOM   976  C  CE  . LYS A 1 141 ? -13.397 33.505  -62.820  1.00 78.72  ?  139 LYS A CE  1 
ATOM   977  N  NZ  . LYS A 1 141 ? -13.491 32.118  -63.359  1.00 84.34  ?  139 LYS A NZ  1 
ATOM   978  N  N   . ALA A 1 142 ? -11.612 39.612  -63.235  1.00 67.74  ?  140 ALA A N   1 
ATOM   979  C  CA  . ALA A 1 142 ? -12.228 40.730  -62.531  1.00 71.60  ?  140 ALA A CA  1 
ATOM   980  C  C   . ALA A 1 142 ? -13.087 41.545  -63.487  1.00 72.44  ?  140 ALA A C   1 
ATOM   981  O  O   . ALA A 1 142 ? -14.252 41.843  -63.198  1.00 77.44  ?  140 ALA A O   1 
ATOM   982  C  CB  . ALA A 1 142 ? -11.153 41.604  -61.885  1.00 70.10  ?  140 ALA A CB  1 
ATOM   983  N  N   . THR A 1 143 ? -12.518 41.921  -64.636  1.00 69.21  ?  141 THR A N   1 
ATOM   984  C  CA  . THR A 1 143 ? -13.267 42.715  -65.602  1.00 63.98  ?  141 THR A CA  1 
ATOM   985  C  C   . THR A 1 143 ? -14.513 41.965  -66.047  1.00 71.01  ?  141 THR A C   1 
ATOM   986  O  O   . THR A 1 143 ? -15.574 42.565  -66.253  1.00 75.33  ?  141 THR A O   1 
ATOM   987  C  CB  . THR A 1 143 ? -12.387 43.048  -66.807  1.00 63.43  ?  141 THR A CB  1 
ATOM   988  O  OG1 . THR A 1 143 ? -11.132 43.575  -66.359  1.00 58.60  ?  141 THR A OG1 1 
ATOM   989  C  CG2 . THR A 1 143 ? -13.071 44.071  -67.698  1.00 64.01  ?  141 THR A CG2 1 
ATOM   990  N  N   . GLU A 1 144 ? -14.399 40.642  -66.189  1.00 67.55  ?  142 GLU A N   1 
ATOM   991  C  CA  . GLU A 1 144 ? -15.547 39.827  -66.564  1.00 70.35  ?  142 GLU A CA  1 
ATOM   992  C  C   . GLU A 1 144 ? -16.630 39.903  -65.495  1.00 74.66  ?  142 GLU A C   1 
ATOM   993  O  O   . GLU A 1 144 ? -17.825 39.946  -65.810  1.00 72.38  ?  142 GLU A O   1 
ATOM   994  C  CB  . GLU A 1 144 ? -15.106 38.378  -66.778  1.00 66.96  ?  142 GLU A CB  1 
ATOM   995  C  CG  . GLU A 1 144 ? -14.567 38.061  -68.168  1.00 62.46  ?  142 GLU A CG  1 
ATOM   996  C  CD  . GLU A 1 144 ? -14.023 36.643  -68.264  1.00 67.01  ?  142 GLU A CD  1 
ATOM   997  O  OE1 . GLU A 1 144 ? -13.984 35.951  -67.224  1.00 60.14  ?  142 GLU A OE1 1 
ATOM   998  O  OE2 . GLU A 1 144 ? -13.635 36.219  -69.374  1.00 56.29  -1 142 GLU A OE2 1 
ATOM   999  N  N   . GLU A 1 145 ? -16.227 39.916  -64.222  1.00 74.56  ?  143 GLU A N   1 
ATOM   1000 C  CA  . GLU A 1 145 ? -17.184 39.897  -63.121  1.00 81.60  ?  143 GLU A CA  1 
ATOM   1001 C  C   . GLU A 1 145 ? -17.766 41.284  -62.871  1.00 80.10  ?  143 GLU A C   1 
ATOM   1002 O  O   . GLU A 1 145 ? -18.988 41.443  -62.770  1.00 81.13  ?  143 GLU A O   1 
ATOM   1003 C  CB  . GLU A 1 145 ? -16.514 39.363  -61.852  1.00 82.66  ?  143 GLU A CB  1 
ATOM   1004 C  CG  . GLU A 1 145 ? -16.288 37.859  -61.839  1.00 87.17  ?  143 GLU A CG  1 
ATOM   1005 C  CD  . GLU A 1 145 ? -17.583 37.070  -61.870  1.00 99.26  ?  143 GLU A CD  1 
ATOM   1006 O  OE1 . GLU A 1 145 ? -18.484 37.375  -61.061  1.00 103.65 ?  143 GLU A OE1 1 
ATOM   1007 O  OE2 . GLU A 1 145 ? -17.697 36.142  -62.700  1.00 99.98  -1 143 GLU A OE2 1 
ATOM   1008 N  N   . THR A 1 146 ? -16.904 42.302  -62.775  1.00 80.59  ?  144 THR A N   1 
ATOM   1009 C  CA  . THR A 1 146 ? -17.362 43.666  -62.526  1.00 83.30  ?  144 THR A CA  1 
ATOM   1010 C  C   . THR A 1 146 ? -18.364 44.141  -63.568  1.00 89.90  ?  144 THR A C   1 
ATOM   1011 O  O   . THR A 1 146 ? -18.991 45.188  -63.374  1.00 94.79  ?  144 THR A O   1 
ATOM   1012 C  CB  . THR A 1 146 ? -16.177 44.632  -62.490  1.00 80.45  ?  144 THR A CB  1 
ATOM   1013 O  OG1 . THR A 1 146 ? -15.575 44.701  -63.789  1.00 86.27  ?  144 THR A OG1 1 
ATOM   1014 C  CG2 . THR A 1 146 ? -15.137 44.163  -61.485  1.00 76.29  ?  144 THR A CG2 1 
ATOM   1015 N  N   . PHE A 1 147 ? -18.525 43.398  -64.660  1.00 84.89  ?  145 PHE A N   1 
ATOM   1016 C  CA  . PHE A 1 147 ? -19.405 43.763  -65.758  1.00 86.03  ?  145 PHE A CA  1 
ATOM   1017 C  C   . PHE A 1 147 ? -20.647 42.891  -65.804  1.00 91.07  ?  145 PHE A C   1 
ATOM   1018 O  O   . PHE A 1 147 ? -21.684 43.333  -66.301  1.00 97.11  ?  145 PHE A O   1 
ATOM   1019 C  CB  . PHE A 1 147 ? -18.651 43.667  -67.091  1.00 83.38  ?  145 PHE A CB  1 
ATOM   1020 C  CG  . PHE A 1 147 ? -19.521 43.824  -68.307  1.00 89.97  ?  145 PHE A CG  1 
ATOM   1021 C  CD1 . PHE A 1 147 ? -19.787 45.082  -68.823  1.00 91.50  ?  145 PHE A CD1 1 
ATOM   1022 C  CD2 . PHE A 1 147 ? -20.049 42.717  -68.950  1.00 89.91  ?  145 PHE A CD2 1 
ATOM   1023 C  CE1 . PHE A 1 147 ? -20.577 45.235  -69.946  1.00 85.52  ?  145 PHE A CE1 1 
ATOM   1024 C  CE2 . PHE A 1 147 ? -20.840 42.864  -70.075  1.00 90.90  ?  145 PHE A CE2 1 
ATOM   1025 C  CZ  . PHE A 1 147 ? -21.104 44.125  -70.573  1.00 88.92  ?  145 PHE A CZ  1 
ATOM   1026 N  N   . LYS A 1 148 ? -20.559 41.666  -65.276  1.00 92.59  ?  146 LYS A N   1 
ATOM   1027 C  CA  . LYS A 1 148 ? -21.702 40.766  -65.195  1.00 93.99  ?  146 LYS A CA  1 
ATOM   1028 C  C   . LYS A 1 148 ? -22.826 41.344  -64.347  1.00 99.13  ?  146 LYS A C   1 
ATOM   1029 O  O   . LYS A 1 148 ? -23.904 40.744  -64.278  1.00 102.87 ?  146 LYS A O   1 
ATOM   1030 C  CB  . LYS A 1 148 ? -21.259 39.412  -64.627  1.00 91.75  ?  146 LYS A CB  1 
ATOM   1031 C  CG  . LYS A 1 148 ? -20.518 38.528  -65.625  1.00 91.15  ?  146 LYS A CG  1 
ATOM   1032 C  CD  . LYS A 1 148 ? -19.930 37.279  -64.969  1.00 87.26  ?  146 LYS A CD  1 
ATOM   1033 C  CE  . LYS A 1 148 ? -20.981 36.193  -64.768  1.00 94.51  ?  146 LYS A CE  1 
ATOM   1034 N  NZ  . LYS A 1 148 ? -20.432 34.999  -64.060  1.00 90.03  ?  146 LYS A NZ  1 
ATOM   1035 N  N   . LEU A 1 149 ? -22.592 42.482  -63.692  1.00 96.47  ?  147 LEU A N   1 
ATOM   1036 C  CA  . LEU A 1 149 ? -23.584 43.178  -62.887  1.00 95.23  ?  147 LEU A CA  1 
ATOM   1037 C  C   . LEU A 1 149 ? -24.265 44.305  -63.654  1.00 96.38  ?  147 LEU A C   1 
ATOM   1038 O  O   . LEU A 1 149 ? -24.913 45.160  -63.042  1.00 102.95 ?  147 LEU A O   1 
ATOM   1039 C  CB  . LEU A 1 149 ? -22.941 43.728  -61.611  1.00 101.76 ?  147 LEU A CB  1 
ATOM   1040 C  CG  . LEU A 1 149 ? -21.593 44.439  -61.762  1.00 98.21  ?  147 LEU A CG  1 
ATOM   1041 C  CD1 . LEU A 1 149 ? -21.782 45.917  -62.074  1.00 103.31 ?  147 LEU A CD1 1 
ATOM   1042 C  CD2 . LEU A 1 149 ? -20.765 44.262  -60.498  1.00 91.51  ?  147 LEU A CD2 1 
ATOM   1043 N  N   . SER A 1 150 ? -24.136 44.326  -64.982  1.00 101.64 ?  148 SER A N   1 
ATOM   1044 C  CA  . SER A 1 150 ? -24.650 45.430  -65.784  1.00 107.37 ?  148 SER A CA  1 
ATOM   1045 C  C   . SER A 1 150 ? -25.709 44.989  -66.789  1.00 111.86 ?  148 SER A C   1 
ATOM   1046 O  O   . SER A 1 150 ? -25.977 45.711  -67.755  1.00 111.02 ?  148 SER A O   1 
ATOM   1047 C  CB  . SER A 1 150 ? -23.498 46.129  -66.509  1.00 106.07 ?  148 SER A CB  1 
ATOM   1048 O  OG  . SER A 1 150 ? -22.415 46.371  -65.627  1.00 97.77  ?  148 SER A OG  1 
ATOM   1049 N  N   . TYR A 1 151 ? -26.319 43.826  -66.591  1.00 108.20 ?  149 TYR A N   1 
ATOM   1050 C  CA  . TYR A 1 151 ? -27.438 43.395  -67.414  1.00 111.24 ?  149 TYR A CA  1 
ATOM   1051 C  C   . TYR A 1 151 ? -28.730 43.508  -66.612  1.00 108.98 ?  149 TYR A C   1 
ATOM   1052 O  O   . TYR A 1 151 ? -28.718 43.647  -65.386  1.00 109.69 ?  149 TYR A O   1 
ATOM   1053 C  CB  . TYR A 1 151 ? -27.215 41.970  -67.933  1.00 105.09 ?  149 TYR A CB  1 
ATOM   1054 C  CG  . TYR A 1 151 ? -26.317 41.933  -69.153  1.00 110.29 ?  149 TYR A CG  1 
ATOM   1055 C  CD1 . TYR A 1 151 ? -24.936 41.855  -69.018  1.00 107.70 ?  149 TYR A CD1 1 
ATOM   1056 C  CD2 . TYR A 1 151 ? -26.845 42.003  -70.436  1.00 114.85 ?  149 TYR A CD2 1 
ATOM   1057 C  CE1 . TYR A 1 151 ? -24.107 41.831  -70.125  1.00 100.54 ?  149 TYR A CE1 1 
ATOM   1058 C  CE2 . TYR A 1 151 ? -26.022 41.981  -71.551  1.00 108.27 ?  149 TYR A CE2 1 
ATOM   1059 C  CZ  . TYR A 1 151 ? -24.655 41.894  -71.388  1.00 102.23 ?  149 TYR A CZ  1 
ATOM   1060 O  OH  . TYR A 1 151 ? -23.831 41.874  -72.491  1.00 104.77 ?  149 TYR A OH  1 
ATOM   1061 N  N   . GLY A 1 152 ? -29.855 43.443  -67.317  1.00 116.14 ?  150 GLY A N   1 
ATOM   1062 C  CA  . GLY A 1 152 ? -31.142 43.613  -66.673  1.00 117.24 ?  150 GLY A CA  1 
ATOM   1063 C  C   . GLY A 1 152 ? -31.572 42.404  -65.864  1.00 119.34 ?  150 GLY A C   1 
ATOM   1064 O  O   . GLY A 1 152 ? -31.030 41.303  -65.971  1.00 121.25 ?  150 GLY A O   1 
ATOM   1065 N  N   . ILE A 1 153 ? -32.585 42.625  -65.033  1.00 114.18 ?  151 ILE A N   1 
ATOM   1066 C  CA  . ILE A 1 153 ? -33.109 41.594  -64.157  1.00 117.09 ?  151 ILE A CA  1 
ATOM   1067 C  C   . ILE A 1 153 ? -34.369 41.025  -64.797  1.00 121.12 ?  151 ILE A C   1 
ATOM   1068 O  O   . ILE A 1 153 ? -35.032 41.671  -65.613  1.00 121.62 ?  151 ILE A O   1 
ATOM   1069 C  CB  . ILE A 1 153 ? -33.379 42.148  -62.738  1.00 113.78 ?  151 ILE A CB  1 
ATOM   1070 C  CG1 . ILE A 1 153 ? -32.070 42.640  -62.115  1.00 108.73 ?  151 ILE A CG1 1 
ATOM   1071 C  CG2 . ILE A 1 153 ? -34.004 41.087  -61.848  1.00 111.67 ?  151 ILE A CG2 1 
ATOM   1072 C  CD1 . ILE A 1 153 ? -32.160 42.947  -60.638  1.00 102.97 ?  151 ILE A CD1 1 
ATOM   1073 N  N   . ALA A 1 154 ? -34.707 39.792  -64.428  1.00 123.14 ?  152 ALA A N   1 
ATOM   1074 C  CA  . ALA A 1 154 ? -35.830 39.073  -65.016  1.00 123.20 ?  152 ALA A CA  1 
ATOM   1075 C  C   . ALA A 1 154 ? -36.970 38.945  -64.016  1.00 123.82 ?  152 ALA A C   1 
ATOM   1076 O  O   . ALA A 1 154 ? -36.745 38.605  -62.850  1.00 124.01 ?  152 ALA A O   1 
ATOM   1077 C  CB  . ALA A 1 154 ? -35.397 37.686  -65.497  1.00 124.22 ?  152 ALA A CB  1 
ATOM   1078 N  N   . THR A 1 155 ? -38.189 39.221  -64.477  1.00 124.84 ?  153 THR A N   1 
ATOM   1079 C  CA  . THR A 1 155 ? -39.397 39.053  -63.681  1.00 127.05 ?  153 THR A CA  1 
ATOM   1080 C  C   . THR A 1 155 ? -40.380 38.190  -64.461  1.00 127.45 ?  153 THR A C   1 
ATOM   1081 O  O   . THR A 1 155 ? -40.563 38.379  -65.666  1.00 129.95 ?  153 THR A O   1 
ATOM   1082 C  CB  . THR A 1 155 ? -40.030 40.406  -63.327  1.00 127.32 ?  153 THR A CB  1 
ATOM   1083 O  OG1 . THR A 1 155 ? -39.697 41.371  -64.333  1.00 127.88 ?  153 THR A OG1 1 
ATOM   1084 C  CG2 . THR A 1 155 ? -39.517 40.896  -61.980  1.00 121.46 ?  153 THR A CG2 1 
ATOM   1085 N  N   . VAL A 1 156 ? -41.005 37.241  -63.769  1.00 126.51 ?  154 VAL A N   1 
ATOM   1086 C  CA  . VAL A 1 156 ? -41.883 36.264  -64.411  1.00 132.82 ?  154 VAL A CA  1 
ATOM   1087 C  C   . VAL A 1 156 ? -43.247 36.890  -64.679  1.00 135.40 ?  154 VAL A C   1 
ATOM   1088 O  O   . VAL A 1 156 ? -43.936 37.326  -63.750  1.00 133.40 ?  154 VAL A O   1 
ATOM   1089 C  CB  . VAL A 1 156 ? -42.020 34.997  -63.555  1.00 136.94 ?  154 VAL A CB  1 
ATOM   1090 C  CG1 . VAL A 1 156 ? -43.142 34.119  -64.090  1.00 138.81 ?  154 VAL A CG1 1 
ATOM   1091 C  CG2 . VAL A 1 156 ? -40.708 34.231  -63.531  1.00 131.68 ?  154 VAL A CG2 1 
ATOM   1092 N  N   . ARG A 1 157 ? -43.640 36.933  -65.954  1.00 135.42 ?  155 ARG A N   1 
ATOM   1093 C  CA  . ARG A 1 157 ? -44.970 37.421  -66.306  1.00 134.84 ?  155 ARG A CA  1 
ATOM   1094 C  C   . ARG A 1 157 ? -46.043 36.414  -65.901  1.00 138.62 ?  155 ARG A C   1 
ATOM   1095 O  O   . ARG A 1 157 ? -46.885 36.696  -65.041  1.00 139.27 ?  155 ARG A O   1 
ATOM   1096 C  CB  . ARG A 1 157 ? -45.041 37.718  -67.805  1.00 132.73 ?  155 ARG A CB  1 
ATOM   1097 N  N   . GLU A 1 158 ? -46.027 35.231  -66.513  1.00 136.94 ?  156 GLU A N   1 
ATOM   1098 C  CA  . GLU A 1 158 ? -46.917 34.147  -66.123  1.00 137.52 ?  156 GLU A CA  1 
ATOM   1099 C  C   . GLU A 1 158 ? -46.188 32.817  -66.259  1.00 139.26 ?  156 GLU A C   1 
ATOM   1100 O  O   . GLU A 1 158 ? -45.287 32.665  -67.088  1.00 138.42 ?  156 GLU A O   1 
ATOM   1101 C  CB  . GLU A 1 158 ? -48.205 34.137  -66.961  1.00 135.72 ?  156 GLU A CB  1 
ATOM   1102 C  CG  . GLU A 1 158 ? -47.978 34.123  -68.464  1.00 137.96 ?  156 GLU A CG  1 
ATOM   1103 C  CD  . GLU A 1 158 ? -49.238 34.451  -69.245  1.00 134.78 ?  156 GLU A CD  1 
ATOM   1104 O  OE1 . GLU A 1 158 ? -49.799 35.548  -69.039  1.00 129.80 ?  156 GLU A OE1 1 
ATOM   1105 O  OE2 . GLU A 1 158 ? -49.668 33.611  -70.065  1.00 138.50 -1 156 GLU A OE2 1 
ATOM   1106 N  N   . VAL A 1 159 ? -46.591 31.856  -65.433  1.00 140.69 ?  157 VAL A N   1 
ATOM   1107 C  CA  . VAL A 1 159 ? -46.033 30.508  -65.442  1.00 139.44 ?  157 VAL A CA  1 
ATOM   1108 C  C   . VAL A 1 159 ? -47.006 29.594  -66.174  1.00 138.99 ?  157 VAL A C   1 
ATOM   1109 O  O   . VAL A 1 159 ? -48.131 29.374  -65.709  1.00 136.20 ?  157 VAL A O   1 
ATOM   1110 C  CB  . VAL A 1 159 ? -45.766 30.005  -64.014  1.00 141.12 ?  157 VAL A CB  1 
ATOM   1111 C  CG1 . VAL A 1 159 ? -45.040 28.668  -64.046  1.00 140.25 ?  157 VAL A CG1 1 
ATOM   1112 C  CG2 . VAL A 1 159 ? -44.972 31.039  -63.229  1.00 144.45 ?  157 VAL A CG2 1 
ATOM   1113 N  N   . LEU A 1 160 ? -46.578 29.057  -67.316  1.00 136.21 ?  158 LEU A N   1 
ATOM   1114 C  CA  . LEU A 1 160 ? -47.462 28.240  -68.139  1.00 133.56 ?  158 LEU A CA  1 
ATOM   1115 C  C   . LEU A 1 160 ? -47.378 26.759  -67.784  1.00 128.88 ?  158 LEU A C   1 
ATOM   1116 O  O   . LEU A 1 160 ? -48.401 26.124  -67.510  1.00 124.59 ?  158 LEU A O   1 
ATOM   1117 C  CB  . LEU A 1 160 ? -47.125 28.444  -69.619  1.00 133.39 ?  158 LEU A CB  1 
ATOM   1118 C  CG  . LEU A 1 160 ? -46.576 29.825  -69.977  1.00 134.10 ?  158 LEU A CG  1 
ATOM   1119 C  CD1 . LEU A 1 160 ? -46.003 29.831  -71.385  1.00 133.41 ?  158 LEU A CD1 1 
ATOM   1120 C  CD2 . LEU A 1 160 ? -47.660 30.880  -69.830  1.00 134.88 ?  158 LEU A CD2 1 
ATOM   1121 N  N   . SER A 1 161 ? -46.174 26.200  -67.782  1.00 130.07 ?  159 SER A N   1 
ATOM   1122 C  CA  . SER A 1 161 ? -45.973 24.786  -67.492  1.00 123.74 ?  159 SER A CA  1 
ATOM   1123 C  C   . SER A 1 161 ? -44.893 24.677  -66.419  1.00 129.73 ?  159 SER A C   1 
ATOM   1124 O  O   . SER A 1 161 ? -44.553 25.646  -65.728  1.00 133.79 ?  159 SER A O   1 
ATOM   1125 C  CB  . SER A 1 161 ? -45.614 24.017  -68.771  1.00 120.58 ?  159 SER A CB  1 
ATOM   1126 O  OG  . SER A 1 161 ? -44.393 24.481  -69.320  1.00 124.33 ?  159 SER A OG  1 
ATOM   1127 N  N   . ASP A 1 162 ? -44.339 23.478  -66.267  1.00 128.27 ?  160 ASP A N   1 
ATOM   1128 C  CA  . ASP A 1 162 ? -43.224 23.261  -65.359  1.00 126.18 ?  160 ASP A CA  1 
ATOM   1129 C  C   . ASP A 1 162 ? -41.886 23.501  -66.039  1.00 128.22 ?  160 ASP A C   1 
ATOM   1130 O  O   . ASP A 1 162 ? -40.849 23.484  -65.367  1.00 131.62 ?  160 ASP A O   1 
ATOM   1131 C  CB  . ASP A 1 162 ? -43.259 21.836  -64.791  1.00 121.56 ?  160 ASP A CB  1 
ATOM   1132 C  CG  . ASP A 1 162 ? -43.425 20.778  -65.869  1.00 116.16 ?  160 ASP A CG  1 
ATOM   1133 O  OD1 . ASP A 1 162 ? -43.468 21.138  -67.064  1.00 118.17 ?  160 ASP A OD1 1 
ATOM   1134 O  OD2 . ASP A 1 162 ? -43.508 19.581  -65.519  1.00 110.88 -1 160 ASP A OD2 1 
ATOM   1135 N  N   . ARG A 1 163 ? -41.894 23.725  -67.357  1.00 127.56 ?  161 ARG A N   1 
ATOM   1136 C  CA  . ARG A 1 163 ? -40.680 23.866  -68.151  1.00 128.95 ?  161 ARG A CA  1 
ATOM   1137 C  C   . ARG A 1 163 ? -40.730 25.087  -69.063  1.00 130.96 ?  161 ARG A C   1 
ATOM   1138 O  O   . ARG A 1 163 ? -39.917 25.194  -69.987  1.00 128.01 ?  161 ARG A O   1 
ATOM   1139 C  CB  . ARG A 1 163 ? -40.486 22.606  -68.991  1.00 123.38 ?  161 ARG A CB  1 
ATOM   1140 C  CG  . ARG A 1 163 ? -41.723 22.307  -69.827  1.00 121.97 ?  161 ARG A CG  1 
ATOM   1141 C  CD  . ARG A 1 163 ? -41.767 20.886  -70.334  1.00 118.63 ?  161 ARG A CD  1 
ATOM   1142 N  NE  . ARG A 1 163 ? -41.776 19.939  -69.227  1.00 115.69 ?  161 ARG A NE  1 
ATOM   1143 C  CZ  . ARG A 1 163 ? -41.753 18.621  -69.366  1.00 116.48 ?  161 ARG A CZ  1 
ATOM   1144 N  NH1 . ARG A 1 163 ? -41.454 18.054  -70.523  1.00 116.69 ?  161 ARG A NH1 1 
ATOM   1145 N  NH2 . ARG A 1 163 ? -41.959 17.854  -68.300  1.00 116.47 ?  161 ARG A NH2 1 
ATOM   1146 N  N   . GLU A 1 164 ? -41.657 26.013  -68.824  1.00 134.56 ?  162 GLU A N   1 
ATOM   1147 C  CA  . GLU A 1 164 ? -41.813 27.183  -69.677  1.00 131.88 ?  162 GLU A CA  1 
ATOM   1148 C  C   . GLU A 1 164 ? -42.435 28.315  -68.874  1.00 134.55 ?  162 GLU A C   1 
ATOM   1149 O  O   . GLU A 1 164 ? -43.346 28.088  -68.073  1.00 134.75 ?  162 GLU A O   1 
ATOM   1150 C  CB  . GLU A 1 164 ? -42.689 26.882  -70.902  1.00 130.35 ?  162 GLU A CB  1 
ATOM   1151 C  CG  . GLU A 1 164 ? -42.070 25.939  -71.923  1.00 127.29 ?  162 GLU A CG  1 
ATOM   1152 C  CD  . GLU A 1 164 ? -43.095 25.010  -72.550  1.00 124.82 ?  162 GLU A CD  1 
ATOM   1153 O  OE1 . GLU A 1 164 ? -43.763 24.265  -71.802  1.00 123.73 ?  162 GLU A OE1 1 
ATOM   1154 O  OE2 . GLU A 1 164 ? -43.236 25.027  -73.792  1.00 126.00 -1 162 GLU A OE2 1 
ATOM   1155 N  N   . LEU A 1 165 ? -41.942 29.532  -69.094  1.00 134.47 ?  163 LEU A N   1 
ATOM   1156 C  CA  . LEU A 1 165 ? -42.438 30.704  -68.388  1.00 136.17 ?  163 LEU A CA  1 
ATOM   1157 C  C   . LEU A 1 165 ? -42.539 31.875  -69.355  1.00 135.63 ?  163 LEU A C   1 
ATOM   1158 O  O   . LEU A 1 165 ? -42.027 31.834  -70.477  1.00 134.53 ?  163 LEU A O   1 
ATOM   1159 C  CB  . LEU A 1 165 ? -41.548 31.065  -67.187  1.00 136.60 ?  163 LEU A CB  1 
ATOM   1160 C  CG  . LEU A 1 165 ? -40.021 31.125  -67.326  1.00 137.27 ?  163 LEU A CG  1 
ATOM   1161 C  CD1 . LEU A 1 165 ? -39.564 32.182  -68.325  1.00 134.08 ?  163 LEU A CD1 1 
ATOM   1162 C  CD2 . LEU A 1 165 ? -39.389 31.366  -65.962  1.00 138.55 ?  163 LEU A CD2 1 
ATOM   1163 N  N   . HIS A 1 166 ? -43.221 32.924  -68.906  1.00 136.03 ?  164 HIS A N   1 
ATOM   1164 C  CA  . HIS A 1 166 ? -43.258 34.205  -69.597  1.00 136.16 ?  164 HIS A CA  1 
ATOM   1165 C  C   . HIS A 1 166 ? -42.424 35.181  -68.780  1.00 134.62 ?  164 HIS A C   1 
ATOM   1166 O  O   . HIS A 1 166 ? -42.571 35.250  -67.555  1.00 134.87 ?  164 HIS A O   1 
ATOM   1167 C  CB  . HIS A 1 166 ? -44.696 34.702  -69.763  1.00 136.02 ?  164 HIS A CB  1 
ATOM   1168 C  CG  . HIS A 1 166 ? -45.277 34.419  -71.114  1.00 134.54 ?  164 HIS A CG  1 
ATOM   1169 N  ND1 . HIS A 1 166 ? -46.634 34.356  -71.344  1.00 137.80 ?  164 HIS A ND1 1 
ATOM   1170 C  CD2 . HIS A 1 166 ? -44.682 34.170  -72.305  1.00 131.36 ?  164 HIS A CD2 1 
ATOM   1171 C  CE1 . HIS A 1 166 ? -46.851 34.086  -72.620  1.00 135.50 ?  164 HIS A CE1 1 
ATOM   1172 N  NE2 . HIS A 1 166 ? -45.683 33.969  -73.225  1.00 134.84 ?  164 HIS A NE2 1 
ATOM   1173 N  N   . LEU A 1 167 ? -41.548 35.925  -69.449  1.00 132.58 ?  165 LEU A N   1 
ATOM   1174 C  CA  . LEU A 1 167 ? -40.584 36.770  -68.763  1.00 132.65 ?  165 LEU A CA  1 
ATOM   1175 C  C   . LEU A 1 167 ? -40.789 38.244  -69.096  1.00 130.27 ?  165 LEU A C   1 
ATOM   1176 O  O   . LEU A 1 167 ? -41.204 38.599  -70.203  1.00 128.55 ?  165 LEU A O   1 
ATOM   1177 C  CB  . LEU A 1 167 ? -39.159 36.336  -69.134  1.00 132.43 ?  165 LEU A CB  1 
ATOM   1178 C  CG  . LEU A 1 167 ? -38.069 36.391  -68.066  1.00 131.41 ?  165 LEU A CG  1 
ATOM   1179 C  CD1 . LEU A 1 167 ? -38.553 35.727  -66.791  1.00 133.33 ?  165 LEU A CD1 1 
ATOM   1180 C  CD2 . LEU A 1 167 ? -36.820 35.697  -68.581  1.00 129.66 ?  165 LEU A CD2 1 
ATOM   1181 N  N   . SER A 1 168 ? -40.491 39.096  -68.113  1.00 131.51 ?  166 SER A N   1 
ATOM   1182 C  CA  . SER A 1 168 ? -40.514 40.548  -68.257  1.00 133.01 ?  166 SER A CA  1 
ATOM   1183 C  C   . SER A 1 168 ? -39.159 41.092  -67.826  1.00 130.79 ?  166 SER A C   1 
ATOM   1184 O  O   . SER A 1 168 ? -38.656 40.728  -66.758  1.00 130.14 ?  166 SER A O   1 
ATOM   1185 C  CB  . SER A 1 168 ? -41.639 41.181  -67.428  1.00 131.85 ?  166 SER A CB  1 
ATOM   1186 O  OG  . SER A 1 168 ? -41.654 40.678  -66.103  1.00 132.18 ?  166 SER A OG  1 
ATOM   1187 N  N   . TRP A 1 169 ? -38.570 41.958  -68.647  1.00 129.83 ?  167 TRP A N   1 
ATOM   1188 C  CA  . TRP A 1 169 ? -37.218 42.447  -68.418  1.00 129.94 ?  167 TRP A CA  1 
ATOM   1189 C  C   . TRP A 1 169 ? -37.197 43.906  -67.975  1.00 128.94 ?  167 TRP A C   1 
ATOM   1190 O  O   . TRP A 1 169 ? -38.049 44.712  -68.360  1.00 126.59 ?  167 TRP A O   1 
ATOM   1191 C  CB  . TRP A 1 169 ? -36.358 42.274  -69.673  1.00 131.96 ?  167 TRP A CB  1 
ATOM   1192 C  CG  . TRP A 1 169 ? -36.041 40.841  -69.962  1.00 129.85 ?  167 TRP A CG  1 
ATOM   1193 C  CD1 . TRP A 1 169 ? -36.722 40.000  -70.793  1.00 128.73 ?  167 TRP A CD1 1 
ATOM   1194 C  CD2 . TRP A 1 169 ? -34.969 40.073  -69.403  1.00 130.15 ?  167 TRP A CD2 1 
ATOM   1195 N  NE1 . TRP A 1 169 ? -36.134 38.758  -70.794  1.00 130.66 ?  167 TRP A NE1 1 
ATOM   1196 C  CE2 . TRP A 1 169 ? -35.056 38.777  -69.948  1.00 132.30 ?  167 TRP A CE2 1 
ATOM   1197 C  CE3 . TRP A 1 169 ? -33.941 40.357  -68.499  1.00 128.67 ?  167 TRP A CE3 1 
ATOM   1198 C  CZ2 . TRP A 1 169 ? -34.155 37.766  -69.618  1.00 130.10 ?  167 TRP A CZ2 1 
ATOM   1199 C  CZ3 . TRP A 1 169 ? -33.048 39.353  -68.172  1.00 126.71 ?  167 TRP A CZ3 1 
ATOM   1200 C  CH2 . TRP A 1 169 ? -33.160 38.074  -68.730  1.00 127.80 ?  167 TRP A CH2 1 
ATOM   1201 N  N   . GLU A 1 170 ? -36.197 44.222  -67.154  1.00 127.46 ?  168 GLU A N   1 
ATOM   1202 C  CA  . GLU A 1 170 ? -36.010 45.554  -66.596  1.00 126.81 ?  168 GLU A CA  1 
ATOM   1203 C  C   . GLU A 1 170 ? -35.652 46.570  -67.678  1.00 127.84 ?  168 GLU A C   1 
ATOM   1204 O  O   . GLU A 1 170 ? -34.993 46.251  -68.672  1.00 125.72 ?  168 GLU A O   1 
ATOM   1205 C  CB  . GLU A 1 170 ? -34.917 45.508  -65.524  1.00 124.38 ?  168 GLU A CB  1 
ATOM   1206 C  CG  . GLU A 1 170 ? -34.203 46.821  -65.245  1.00 127.18 ?  168 GLU A CG  1 
ATOM   1207 C  CD  . GLU A 1 170 ? -33.340 46.750  -63.994  1.00 124.35 ?  168 GLU A CD  1 
ATOM   1208 O  OE1 . GLU A 1 170 ? -33.442 45.747  -63.255  1.00 116.75 ?  168 GLU A OE1 1 
ATOM   1209 O  OE2 . GLU A 1 170 ? -32.555 47.693  -63.753  1.00 121.72 -1 168 GLU A OE2 1 
ATOM   1210 N  N   . VAL A 1 171 ? -36.096 47.812  -67.471  1.00 130.42 ?  169 VAL A N   1 
ATOM   1211 C  CA  . VAL A 1 171 ? -35.822 48.919  -68.382  1.00 129.61 ?  169 VAL A CA  1 
ATOM   1212 C  C   . VAL A 1 171 ? -34.531 49.603  -67.957  1.00 131.34 ?  169 VAL A C   1 
ATOM   1213 O  O   . VAL A 1 171 ? -34.247 49.734  -66.760  1.00 131.62 ?  169 VAL A O   1 
ATOM   1214 C  CB  . VAL A 1 171 ? -36.996 49.917  -68.403  1.00 125.02 ?  169 VAL A CB  1 
ATOM   1215 C  CG1 . VAL A 1 171 ? -36.715 51.053  -69.377  1.00 126.42 ?  169 VAL A CG1 1 
ATOM   1216 C  CG2 . VAL A 1 171 ? -38.296 49.210  -68.755  1.00 122.93 ?  169 VAL A CG2 1 
ATOM   1217 N  N   . GLY A 1 172 ? -33.739 50.045  -68.939  1.00 132.12 ?  170 GLY A N   1 
ATOM   1218 C  CA  . GLY A 1 172 ? -32.509 50.773  -68.700  1.00 128.17 ?  170 GLY A CA  1 
ATOM   1219 C  C   . GLY A 1 172 ? -31.249 49.967  -68.958  1.00 130.51 ?  170 GLY A C   1 
ATOM   1220 O  O   . GLY A 1 172 ? -30.229 50.544  -69.358  1.00 128.02 ?  170 GLY A O   1 
ATOM   1221 N  N   . LYS A 1 173 ? -31.294 48.652  -68.735  1.00 131.28 ?  171 LYS A N   1 
ATOM   1222 C  CA  . LYS A 1 173 ? -30.115 47.812  -68.880  1.00 128.56 ?  171 LYS A CA  1 
ATOM   1223 C  C   . LYS A 1 173 ? -30.289 46.847  -70.051  1.00 128.54 ?  171 LYS A C   1 
ATOM   1224 O  O   . LYS A 1 173 ? -31.415 46.470  -70.391  1.00 129.07 ?  171 LYS A O   1 
ATOM   1225 C  CB  . LYS A 1 173 ? -29.867 47.003  -67.599  1.00 121.34 ?  171 LYS A CB  1 
ATOM   1226 C  CG  . LYS A 1 173 ? -29.494 47.824  -66.362  1.00 116.92 ?  171 LYS A CG  1 
ATOM   1227 C  CD  . LYS A 1 173 ? -27.990 47.960  -66.137  1.00 114.66 ?  171 LYS A CD  1 
ATOM   1228 C  CE  . LYS A 1 173 ? -27.291 48.749  -67.228  1.00 114.55 ?  171 LYS A CE  1 
ATOM   1229 N  NZ  . LYS A 1 173 ? -25.811 48.711  -67.040  1.00 111.70 ?  171 LYS A NZ  1 
ATOM   1230 N  N   . PRO A 1 174 ? -29.198 46.430  -70.690  1.00 125.67 ?  172 PRO A N   1 
ATOM   1231 C  CA  . PRO A 1 174 ? -29.301 45.414  -71.742  1.00 126.47 ?  172 PRO A CA  1 
ATOM   1232 C  C   . PRO A 1 174 ? -29.754 44.074  -71.182  1.00 124.70 ?  172 PRO A C   1 
ATOM   1233 O  O   . PRO A 1 174 ? -29.651 43.797  -69.985  1.00 120.88 ?  172 PRO A O   1 
ATOM   1234 C  CB  . PRO A 1 174 ? -27.876 45.338  -72.301  1.00 124.20 ?  172 PRO A CB  1 
ATOM   1235 C  CG  . PRO A 1 174 ? -27.016 45.781  -71.163  1.00 123.05 ?  172 PRO A CG  1 
ATOM   1236 C  CD  . PRO A 1 174 ? -27.807 46.873  -70.493  1.00 122.49 ?  172 PRO A CD  1 
ATOM   1237 N  N   . ARG A 1 175 ? -30.264 43.224  -72.085  1.00 125.89 ?  173 ARG A N   1 
ATOM   1238 C  CA  . ARG A 1 175 ? -30.759 41.917  -71.671  1.00 123.29 ?  173 ARG A CA  1 
ATOM   1239 C  C   . ARG A 1 175 ? -29.723 40.847  -71.979  1.00 122.60 ?  173 ARG A C   1 
ATOM   1240 O  O   . ARG A 1 175 ? -29.186 40.819  -73.097  1.00 123.72 ?  173 ARG A O   1 
ATOM   1241 C  CB  . ARG A 1 175 ? -32.063 41.594  -72.396  1.00 123.57 ?  173 ARG A CB  1 
ATOM   1242 C  CG  . ARG A 1 175 ? -33.160 42.637  -72.217  1.00 129.29 ?  173 ARG A CG  1 
ATOM   1243 C  CD  . ARG A 1 175 ? -34.419 42.239  -72.977  1.00 132.05 ?  173 ARG A CD  1 
ATOM   1244 N  NE  . ARG A 1 175 ? -35.540 43.135  -72.719  1.00 131.98 ?  173 ARG A NE  1 
ATOM   1245 C  CZ  . ARG A 1 175 ? -36.765 42.960  -73.195  1.00 132.44 ?  173 ARG A CZ  1 
ATOM   1246 N  NH1 . ARG A 1 175 ? -37.012 42.090  -74.161  1.00 133.76 ?  173 ARG A NH1 1 
ATOM   1247 N  NH2 . ARG A 1 175 ? -37.751 43.734  -72.751  1.00 129.61 ?  173 ARG A NH2 1 
ATOM   1248 N  N   . PRO A 1 176 ? -29.417 39.960  -71.037  1.00 118.79 ?  174 PRO A N   1 
ATOM   1249 C  CA  . PRO A 1 176 ? -28.480 38.860  -71.314  1.00 117.19 ?  174 PRO A CA  1 
ATOM   1250 C  C   . PRO A 1 176 ? -29.108 37.806  -72.207  1.00 121.04 ?  174 PRO A C   1 
ATOM   1251 O  O   . PRO A 1 176 ? -30.290 37.465  -72.046  1.00 122.32 ?  174 PRO A O   1 
ATOM   1252 C  CB  . PRO A 1 176 ? -28.168 38.300  -69.919  1.00 120.52 ?  174 PRO A CB  1 
ATOM   1253 C  CG  . PRO A 1 176 ? -29.343 38.677  -69.087  1.00 125.70 ?  174 PRO A CG  1 
ATOM   1254 C  CD  . PRO A 1 176 ? -29.879 39.967  -69.638  1.00 122.09 ?  174 PRO A CD  1 
ATOM   1255 N  N   . PRO A 1 177 ? -28.345 37.262  -73.166  1.00 122.49 ?  175 PRO A N   1 
ATOM   1256 C  CA  . PRO A 1 177 ? -28.855 36.164  -74.004  1.00 123.15 ?  175 PRO A CA  1 
ATOM   1257 C  C   . PRO A 1 177 ? -29.386 34.982  -73.204  1.00 123.73 ?  175 PRO A C   1 
ATOM   1258 O  O   . PRO A 1 177 ? -29.043 34.811  -72.030  1.00 125.32 ?  175 PRO A O   1 
ATOM   1259 C  CB  . PRO A 1 177 ? -27.632 35.761  -74.843  1.00 119.68 ?  175 PRO A CB  1 
ATOM   1260 C  CG  . PRO A 1 177 ? -26.450 36.410  -74.176  1.00 118.21 ?  175 PRO A CG  1 
ATOM   1261 C  CD  . PRO A 1 177 ? -26.976 37.650  -73.537  1.00 119.46 ?  175 PRO A CD  1 
ATOM   1262 N  N   . LEU A 1 178 ? -30.222 34.162  -73.835  1.00 125.31 ?  176 LEU A N   1 
ATOM   1263 C  CA  . LEU A 1 178 ? -30.857 33.017  -73.184  1.00 128.63 ?  176 LEU A CA  1 
ATOM   1264 C  C   . LEU A 1 178 ? -30.204 31.717  -73.649  1.00 125.60 ?  176 LEU A C   1 
ATOM   1265 O  O   . LEU A 1 178 ? -30.782 30.933  -74.405  1.00 125.98 ?  176 LEU A O   1 
ATOM   1266 C  CB  . LEU A 1 178 ? -32.363 33.015  -73.465  1.00 130.71 ?  176 LEU A CB  1 
ATOM   1267 C  CG  . LEU A 1 178 ? -33.146 34.243  -73.001  1.00 131.18 ?  176 LEU A CG  1 
ATOM   1268 C  CD1 . LEU A 1 178 ? -34.641 34.014  -73.157  1.00 131.90 ?  176 LEU A CD1 1 
ATOM   1269 C  CD2 . LEU A 1 178 ? -32.799 34.583  -71.559  1.00 131.23 ?  176 LEU A CD2 1 
ATOM   1270 N  N   . ASN A 1 179 ? -28.979 31.488  -73.184  1.00 123.22 ?  177 ASN A N   1 
ATOM   1271 C  CA  . ASN A 1 179 ? -28.283 30.232  -73.411  1.00 122.06 ?  177 ASN A CA  1 
ATOM   1272 C  C   . ASN A 1 179 ? -27.819 29.682  -72.069  1.00 124.78 ?  177 ASN A C   1 
ATOM   1273 O  O   . ASN A 1 179 ? -27.798 30.393  -71.060  1.00 124.34 ?  177 ASN A O   1 
ATOM   1274 C  CB  . ASN A 1 179 ? -27.091 30.402  -74.368  1.00 117.34 ?  177 ASN A CB  1 
ATOM   1275 C  CG  . ASN A 1 179 ? -26.225 31.600  -74.022  1.00 119.78 ?  177 ASN A CG  1 
ATOM   1276 O  OD1 . ASN A 1 179 ? -26.502 32.327  -73.068  1.00 120.60 ?  177 ASN A OD1 1 
ATOM   1277 N  ND2 . ASN A 1 179 ? -25.172 31.814  -74.804  1.00 115.48 ?  177 ASN A ND2 1 
ATOM   1278 N  N   . ARG A 1 180 ? -27.448 28.398  -72.057  1.00 124.86 ?  178 ARG A N   1 
ATOM   1279 C  CA  . ARG A 1 180 ? -26.969 27.808  -70.814  1.00 122.87 ?  178 ARG A CA  1 
ATOM   1280 C  C   . ARG A 1 180 ? -25.643 28.420  -70.394  1.00 124.13 ?  178 ARG A C   1 
ATOM   1281 O  O   . ARG A 1 180 ? -25.295 28.379  -69.209  1.00 125.36 ?  178 ARG A O   1 
ATOM   1282 C  CB  . ARG A 1 180 ? -26.831 26.292  -70.958  1.00 122.09 ?  178 ARG A CB  1 
ATOM   1283 N  N   . ASN A 1 181 ? -24.902 28.985  -71.349  1.00 123.18 ?  179 ASN A N   1 
ATOM   1284 C  CA  . ASN A 1 181 ? -23.675 29.699  -71.025  1.00 121.76 ?  179 ASN A CA  1 
ATOM   1285 C  C   . ASN A 1 181 ? -23.957 30.841  -70.060  1.00 120.63 ?  179 ASN A C   1 
ATOM   1286 O  O   . ASN A 1 181 ? -23.097 31.204  -69.249  1.00 122.50 ?  179 ASN A O   1 
ATOM   1287 C  CB  . ASN A 1 181 ? -23.033 30.226  -72.308  1.00 121.59 ?  179 ASN A CB  1 
ATOM   1288 C  CG  . ASN A 1 181 ? -22.879 29.147  -73.366  1.00 123.97 ?  179 ASN A CG  1 
ATOM   1289 O  OD1 . ASN A 1 181 ? -23.861 28.542  -73.799  1.00 122.65 ?  179 ASN A OD1 1 
ATOM   1290 N  ND2 . ASN A 1 181 ? -21.645 28.907  -73.794  1.00 117.50 ?  179 ASN A ND2 1 
ATOM   1291 N  N   . TYR A 1 182 ? -25.155 31.419  -70.143  1.00 119.07 ?  180 TYR A N   1 
ATOM   1292 C  CA  . TYR A 1 182 ? -25.588 32.531  -69.300  1.00 120.75 ?  180 TYR A CA  1 
ATOM   1293 C  C   . TYR A 1 182 ? -26.494 31.956  -68.213  1.00 120.04 ?  180 TYR A C   1 
ATOM   1294 O  O   . TYR A 1 182 ? -27.717 31.916  -68.355  1.00 121.23 ?  180 TYR A O   1 
ATOM   1295 C  CB  . TYR A 1 182 ? -26.305 33.578  -70.145  1.00 115.99 ?  180 TYR A CB  1 
ATOM   1296 C  CG  . TYR A 1 182 ? -25.408 34.669  -70.689  1.00 114.46 ?  180 TYR A CG  1 
ATOM   1297 C  CD1 . TYR A 1 182 ? -24.574 34.426  -71.774  1.00 113.71 ?  180 TYR A CD1 1 
ATOM   1298 C  CD2 . TYR A 1 182 ? -25.419 35.947  -70.147  1.00 111.91 ?  180 TYR A CD2 1 
ATOM   1299 C  CE1 . TYR A 1 182 ? -23.756 35.415  -72.285  1.00 110.16 ?  180 TYR A CE1 1 
ATOM   1300 C  CE2 . TYR A 1 182 ? -24.607 36.947  -70.655  1.00 110.23 ?  180 TYR A CE2 1 
ATOM   1301 C  CZ  . TYR A 1 182 ? -23.778 36.674  -71.724  1.00 109.82 ?  180 TYR A CZ  1 
ATOM   1302 O  OH  . TYR A 1 182 ? -22.968 37.661  -72.237  1.00 103.64 ?  180 TYR A OH  1 
ATOM   1303 N  N   . VAL A 1 183 ? -25.884 31.502  -67.117  1.00 117.29 ?  181 VAL A N   1 
ATOM   1304 C  CA  . VAL A 1 183 ? -26.630 30.915  -66.009  1.00 122.22 ?  181 VAL A CA  1 
ATOM   1305 C  C   . VAL A 1 183 ? -27.133 32.022  -65.092  1.00 121.58 ?  181 VAL A C   1 
ATOM   1306 O  O   . VAL A 1 183 ? -26.525 33.093  -64.982  1.00 119.32 ?  181 VAL A O   1 
ATOM   1307 C  CB  . VAL A 1 183 ? -25.763 29.897  -65.241  1.00 122.18 ?  181 VAL A CB  1 
ATOM   1308 C  CG1 . VAL A 1 183 ? -26.570 29.238  -64.130  1.00 120.76 ?  181 VAL A CG1 1 
ATOM   1309 C  CG2 . VAL A 1 183 ? -25.206 28.850  -66.192  1.00 119.29 ?  181 VAL A CG2 1 
ATOM   1310 N  N   . PHE A 1 184 ? -28.251 31.760  -64.417  1.00 122.91 ?  182 PHE A N   1 
ATOM   1311 C  CA  . PHE A 1 184 ? -28.884 32.743  -63.552  1.00 121.34 ?  182 PHE A CA  1 
ATOM   1312 C  C   . PHE A 1 184 ? -29.124 32.155  -62.171  1.00 120.36 ?  182 PHE A C   1 
ATOM   1313 O  O   . PHE A 1 184 ? -29.374 30.956  -62.022  1.00 122.03 ?  182 PHE A O   1 
ATOM   1314 C  CB  . PHE A 1 184 ? -30.239 33.199  -64.114  1.00 122.25 ?  182 PHE A CB  1 
ATOM   1315 C  CG  . PHE A 1 184 ? -30.139 34.223  -65.200  1.00 121.63 ?  182 PHE A CG  1 
ATOM   1316 C  CD1 . PHE A 1 184 ? -30.040 35.570  -64.900  1.00 120.34 ?  182 PHE A CD1 1 
ATOM   1317 C  CD2 . PHE A 1 184 ? -30.172 33.836  -66.528  1.00 122.94 ?  182 PHE A CD2 1 
ATOM   1318 C  CE1 . PHE A 1 184 ? -29.956 36.511  -65.907  1.00 120.79 ?  182 PHE A CE1 1 
ATOM   1319 C  CE2 . PHE A 1 184 ? -30.091 34.770  -67.538  1.00 123.60 ?  182 PHE A CE2 1 
ATOM   1320 C  CZ  . PHE A 1 184 ? -29.983 36.109  -67.228  1.00 122.33 ?  182 PHE A CZ  1 
ATOM   1321 N  N   . THR A 1 185 ? -29.049 33.016  -61.162  1.00 117.76 ?  183 THR A N   1 
ATOM   1322 C  CA  . THR A 1 185 ? -29.379 32.649  -59.793  1.00 114.18 ?  183 THR A CA  1 
ATOM   1323 C  C   . THR A 1 185 ? -30.780 33.159  -59.485  1.00 112.49 ?  183 THR A C   1 
ATOM   1324 O  O   . THR A 1 185 ? -31.070 34.345  -59.677  1.00 110.97 ?  183 THR A O   1 
ATOM   1325 C  CB  . THR A 1 185 ? -28.366 33.220  -58.800  1.00 109.16 ?  183 THR A CB  1 
ATOM   1326 O  OG1 . THR A 1 185 ? -27.037 32.932  -59.254  1.00 106.18 ?  183 THR A OG1 1 
ATOM   1327 C  CG2 . THR A 1 185 ? -28.567 32.606  -57.423  1.00 105.94 ?  183 THR A CG2 1 
ATOM   1328 N  N   . GLY A 1 186 ? -31.641 32.269  -59.006  1.00 116.28 ?  184 GLY A N   1 
ATOM   1329 C  CA  . GLY A 1 186 ? -33.031 32.597  -58.736  1.00 113.81 ?  184 GLY A CA  1 
ATOM   1330 C  C   . GLY A 1 186 ? -33.274 32.890  -57.266  1.00 112.32 ?  184 GLY A C   1 
ATOM   1331 O  O   . GLY A 1 186 ? -32.672 32.270  -56.389  1.00 112.67 ?  184 GLY A O   1 
ATOM   1332 N  N   . TYR A 1 187 ? -34.164 33.844  -57.012  1.00 111.16 ?  185 TYR A N   1 
ATOM   1333 C  CA  . TYR A 1 187 ? -34.544 34.208  -55.653  1.00 106.71 ?  185 TYR A CA  1 
ATOM   1334 C  C   . TYR A 1 187 ? -36.054 34.393  -55.554  1.00 103.89 ?  185 TYR A C   1 
ATOM   1335 O  O   . TYR A 1 187 ? -36.654 35.115  -56.350  1.00 106.49 ?  185 TYR A O   1 
ATOM   1336 C  CB  . TYR A 1 187 ? -33.832 35.487  -55.203  1.00 99.80  ?  185 TYR A CB  1 
ATOM   1337 C  CG  . TYR A 1 187 ? -32.321 35.450  -55.295  1.00 106.04 ?  185 TYR A CG  1 
ATOM   1338 C  CD1 . TYR A 1 187 ? -31.556 34.970  -54.240  1.00 104.00 ?  185 TYR A CD1 1 
ATOM   1339 C  CD2 . TYR A 1 187 ? -31.659 35.922  -56.422  1.00 105.13 ?  185 TYR A CD2 1 
ATOM   1340 C  CE1 . TYR A 1 187 ? -30.175 34.942  -54.310  1.00 98.25  ?  185 TYR A CE1 1 
ATOM   1341 C  CE2 . TYR A 1 187 ? -30.276 35.900  -56.501  1.00 103.49 ?  185 TYR A CE2 1 
ATOM   1342 C  CZ  . TYR A 1 187 ? -29.540 35.408  -55.441  1.00 97.97  ?  185 TYR A CZ  1 
ATOM   1343 O  OH  . TYR A 1 187 ? -28.165 35.383  -55.507  1.00 86.49  ?  185 TYR A OH  1 
ATOM   1344 N  N   . GLN A 1 196 ? -33.622 32.404  -52.438  1.00 102.68 ?  194 GLN A N   1 
ATOM   1345 C  CA  . GLN A 1 196 ? -32.632 31.589  -53.133  1.00 108.67 ?  194 GLN A CA  1 
ATOM   1346 C  C   . GLN A 1 196 ? -33.271 30.321  -53.688  1.00 117.58 ?  194 GLN A C   1 
ATOM   1347 O  O   . GLN A 1 196 ? -33.082 29.236  -53.139  1.00 120.04 ?  194 GLN A O   1 
ATOM   1348 C  CB  . GLN A 1 196 ? -31.484 31.222  -52.191  1.00 104.87 ?  194 GLN A CB  1 
ATOM   1349 C  CG  . GLN A 1 196 ? -31.091 32.330  -51.230  1.00 107.16 ?  194 GLN A CG  1 
ATOM   1350 C  CD  . GLN A 1 196 ? -29.965 31.925  -50.299  1.00 104.32 ?  194 GLN A CD  1 
ATOM   1351 O  OE1 . GLN A 1 196 ? -29.418 30.827  -50.407  1.00 108.42 ?  194 GLN A OE1 1 
ATOM   1352 N  NE2 . GLN A 1 196 ? -29.621 32.807  -49.369  1.00 97.79  ?  194 GLN A NE2 1 
ATOM   1353 N  N   . ILE A 1 197 ? -34.029 30.457  -54.782  1.00 113.36 ?  195 ILE A N   1 
ATOM   1354 C  CA  . ILE A 1 197 ? -34.757 29.315  -55.334  1.00 116.37 ?  195 ILE A CA  1 
ATOM   1355 C  C   . ILE A 1 197 ? -33.878 28.417  -56.186  1.00 121.50 ?  195 ILE A C   1 
ATOM   1356 O  O   . ILE A 1 197 ? -34.381 27.443  -56.762  1.00 123.23 ?  195 ILE A O   1 
ATOM   1357 C  CB  . ILE A 1 197 ? -35.981 29.777  -56.153  1.00 125.96 ?  195 ILE A CB  1 
ATOM   1358 C  CG1 . ILE A 1 197 ? -35.549 30.406  -57.479  1.00 121.95 ?  195 ILE A CG1 1 
ATOM   1359 C  CG2 . ILE A 1 197 ? -36.826 30.752  -55.344  1.00 123.30 ?  195 ILE A CG2 1 
ATOM   1360 C  CD1 . ILE A 1 197 ? -36.691 31.042  -58.249  1.00 121.89 ?  195 ILE A CD1 1 
ATOM   1361 N  N   . GLY A 1 198 ? -32.591 28.713  -56.291  1.00 117.27 ?  196 GLY A N   1 
ATOM   1362 C  CA  . GLY A 1 198 ? -31.648 27.876  -57.003  1.00 120.71 ?  196 GLY A CA  1 
ATOM   1363 C  C   . GLY A 1 198 ? -31.247 28.475  -58.341  1.00 120.53 ?  196 GLY A C   1 
ATOM   1364 O  O   . GLY A 1 198 ? -31.868 29.402  -58.862  1.00 120.04 ?  196 GLY A O   1 
ATOM   1365 N  N   . GLU A 1 199 ? -30.176 27.914  -58.895  1.00 123.53 ?  197 GLU A N   1 
ATOM   1366 C  CA  . GLU A 1 199 ? -29.679 28.378  -60.180  1.00 122.81 ?  197 GLU A CA  1 
ATOM   1367 C  C   . GLU A 1 199 ? -30.680 28.038  -61.279  1.00 129.66 ?  197 GLU A C   1 
ATOM   1368 O  O   . GLU A 1 199 ? -31.452 27.081  -61.174  1.00 131.25 ?  197 GLU A O   1 
ATOM   1369 C  CB  . GLU A 1 199 ? -28.316 27.758  -60.487  1.00 116.81 ?  197 GLU A CB  1 
ATOM   1370 C  CG  . GLU A 1 199 ? -27.166 28.407  -59.733  1.00 111.59 ?  197 GLU A CG  1 
ATOM   1371 C  CD  . GLU A 1 199 ? -25.809 27.991  -60.264  1.00 107.49 ?  197 GLU A CD  1 
ATOM   1372 O  OE1 . GLU A 1 199 ? -25.764 27.197  -61.227  1.00 103.06 ?  197 GLU A OE1 1 
ATOM   1373 O  OE2 . GLU A 1 199 ? -24.787 28.461  -59.721  1.00 110.27 -1 197 GLU A OE2 1 
ATOM   1374 N  N   . TYR A 1 200 ? -30.655 28.830  -62.348  1.00 128.89 ?  198 TYR A N   1 
ATOM   1375 C  CA  . TYR A 1 200 ? -31.622 28.671  -63.422  1.00 133.02 ?  198 TYR A CA  1 
ATOM   1376 C  C   . TYR A 1 200 ? -30.973 29.022  -64.752  1.00 131.82 ?  198 TYR A C   1 
ATOM   1377 O  O   . TYR A 1 200 ? -30.081 29.871  -64.821  1.00 128.36 ?  198 TYR A O   1 
ATOM   1378 C  CB  . TYR A 1 200 ? -32.846 29.573  -63.203  1.00 134.06 ?  198 TYR A CB  1 
ATOM   1379 C  CG  . TYR A 1 200 ? -34.006 28.948  -62.456  1.00 133.38 ?  198 TYR A CG  1 
ATOM   1380 C  CD1 . TYR A 1 200 ? -34.043 28.946  -61.068  1.00 130.32 ?  198 TYR A CD1 1 
ATOM   1381 C  CD2 . TYR A 1 200 ? -35.084 28.400  -63.140  1.00 137.17 ?  198 TYR A CD2 1 
ATOM   1382 C  CE1 . TYR A 1 200 ? -35.108 28.390  -60.381  1.00 130.60 ?  198 TYR A CE1 1 
ATOM   1383 C  CE2 . TYR A 1 200 ? -36.155 27.844  -62.461  1.00 137.90 ?  198 TYR A CE2 1 
ATOM   1384 C  CZ  . TYR A 1 200 ? -36.161 27.842  -61.082  1.00 136.30 ?  198 TYR A CZ  1 
ATOM   1385 O  OH  . TYR A 1 200 ? -37.224 27.292  -60.403  1.00 139.16 ?  198 TYR A OH  1 
ATOM   1386 N  N   . THR A 1 201 ? -31.432 28.353  -65.807  1.00 135.20 ?  199 THR A N   1 
ATOM   1387 C  CA  . THR A 1 201 ? -31.024 28.646  -67.171  1.00 136.12 ?  199 THR A CA  1 
ATOM   1388 C  C   . THR A 1 201 ? -32.278 28.826  -68.015  1.00 137.20 ?  199 THR A C   1 
ATOM   1389 O  O   . THR A 1 201 ? -33.330 28.257  -67.712  1.00 136.84 ?  199 THR A O   1 
ATOM   1390 C  CB  . THR A 1 201 ? -30.136 27.535  -67.755  1.00 133.00 ?  199 THR A CB  1 
ATOM   1391 O  OG1 . THR A 1 201 ? -30.787 26.268  -67.602  1.00 131.65 ?  199 THR A OG1 1 
ATOM   1392 C  CG2 . THR A 1 201 ? -28.793 27.497  -67.040  1.00 128.68 ?  199 THR A CG2 1 
ATOM   1393 N  N   . PHE A 1 202 ? -32.164 29.619  -69.079  1.00 137.83 ?  200 PHE A N   1 
ATOM   1394 C  CA  . PHE A 1 202 ? -33.316 29.966  -69.898  1.00 138.25 ?  200 PHE A CA  1 
ATOM   1395 C  C   . PHE A 1 202 ? -33.000 29.746  -71.372  1.00 134.71 ?  200 PHE A C   1 
ATOM   1396 O  O   . PHE A 1 202 ? -31.871 29.960  -71.820  1.00 135.17 ?  200 PHE A O   1 
ATOM   1397 C  CB  . PHE A 1 202 ? -33.743 31.419  -69.648  1.00 137.98 ?  200 PHE A CB  1 
ATOM   1398 C  CG  . PHE A 1 202 ? -34.167 31.686  -68.229  1.00 135.23 ?  200 PHE A CG  1 
ATOM   1399 C  CD1 . PHE A 1 202 ? -35.467 31.439  -67.818  1.00 135.53 ?  200 PHE A CD1 1 
ATOM   1400 C  CD2 . PHE A 1 202 ? -33.259 32.171  -67.301  1.00 135.61 ?  200 PHE A CD2 1 
ATOM   1401 C  CE1 . PHE A 1 202 ? -35.855 31.679  -66.512  1.00 137.63 ?  200 PHE A CE1 1 
ATOM   1402 C  CE2 . PHE A 1 202 ? -33.640 32.413  -65.994  1.00 134.59 ?  200 PHE A CE2 1 
ATOM   1403 C  CZ  . PHE A 1 202 ? -34.940 32.167  -65.599  1.00 137.06 ?  200 PHE A CZ  1 
ATOM   1404 N  N   . GLU A 1 203 ? -34.015 29.317  -72.123  1.00 135.46 ?  201 GLU A N   1 
ATOM   1405 C  CA  . GLU A 1 203 ? -33.901 29.103  -73.561  1.00 135.67 ?  201 GLU A CA  1 
ATOM   1406 C  C   . GLU A 1 203 ? -35.003 29.857  -74.291  1.00 132.25 ?  201 GLU A C   1 
ATOM   1407 O  O   . GLU A 1 203 ? -36.188 29.680  -73.987  1.00 128.98 ?  201 GLU A O   1 
ATOM   1408 C  CB  . GLU A 1 203 ? -33.963 27.610  -73.904  1.00 136.62 ?  201 GLU A CB  1 
ATOM   1409 C  CG  . GLU A 1 203 ? -32.672 26.856  -73.612  1.00 139.24 ?  201 GLU A CG  1 
ATOM   1410 C  CD  . GLU A 1 203 ? -32.668 25.450  -74.185  1.00 143.15 ?  201 GLU A CD  1 
ATOM   1411 O  OE1 . GLU A 1 203 ? -33.522 24.635  -73.775  1.00 144.24 ?  201 GLU A OE1 1 
ATOM   1412 O  OE2 . GLU A 1 203 ? -31.809 25.159  -75.045  1.00 136.31 -1 201 GLU A OE2 1 
ATOM   1413 N  N   . LYS A 1 204 ? -34.612 30.689  -75.253  1.00 134.29 ?  202 LYS A N   1 
ATOM   1414 C  CA  . LYS A 1 204 ? -35.565 31.453  -76.054  1.00 132.12 ?  202 LYS A CA  1 
ATOM   1415 C  C   . LYS A 1 204 ? -36.474 30.534  -76.866  1.00 129.60 ?  202 LYS A C   1 
ATOM   1416 O  O   . LYS A 1 204 ? -36.003 29.711  -77.652  1.00 132.82 ?  202 LYS A O   1 
ATOM   1417 C  CB  . LYS A 1 204 ? -34.827 32.416  -76.987  1.00 124.10 ?  202 LYS A CB  1 
ATOM   1418 N  N   . ASP A 1 209 ? -41.722 33.935  -78.128  1.00 123.10 ?  207 ASP A N   1 
ATOM   1419 C  CA  . ASP A 1 209 ? -42.442 34.523  -77.005  1.00 121.80 ?  207 ASP A CA  1 
ATOM   1420 C  C   . ASP A 1 209 ? -42.079 33.792  -75.713  1.00 123.71 ?  207 ASP A C   1 
ATOM   1421 O  O   . ASP A 1 209 ? -41.331 34.313  -74.885  1.00 126.07 ?  207 ASP A O   1 
ATOM   1422 C  CB  . ASP A 1 209 ? -43.953 34.475  -77.253  1.00 121.46 ?  207 ASP A CB  1 
ATOM   1423 C  CG  . ASP A 1 209 ? -44.747 35.207  -76.186  1.00 126.55 ?  207 ASP A CG  1 
ATOM   1424 O  OD1 . ASP A 1 209 ? -44.128 35.824  -75.294  1.00 128.92 ?  207 ASP A OD1 1 
ATOM   1425 O  OD2 . ASP A 1 209 ? -45.995 35.173  -76.247  1.00 127.24 -1 207 ASP A OD2 1 
ATOM   1426 N  N   . ALA A 1 210 ? -42.608 32.582  -75.550  1.00 125.39 ?  208 ALA A N   1 
ATOM   1427 C  CA  . ALA A 1 210 ? -42.387 31.821  -74.328  1.00 123.42 ?  208 ALA A CA  1 
ATOM   1428 C  C   . ALA A 1 210 ? -40.920 31.429  -74.194  1.00 123.46 ?  208 ALA A C   1 
ATOM   1429 O  O   . ALA A 1 210 ? -40.247 31.129  -75.184  1.00 123.39 ?  208 ALA A O   1 
ATOM   1430 C  CB  . ALA A 1 210 ? -43.269 30.573  -74.311  1.00 124.91 ?  208 ALA A CB  1 
ATOM   1431 N  N   . VAL A 1 211 ? -40.426 31.431  -72.958  1.00 126.11 ?  209 VAL A N   1 
ATOM   1432 C  CA  . VAL A 1 211 ? -39.057 31.036  -72.645  1.00 124.46 ?  209 VAL A CA  1 
ATOM   1433 C  C   . VAL A 1 211 ? -39.094 29.768  -71.801  1.00 124.70 ?  209 VAL A C   1 
ATOM   1434 O  O   . VAL A 1 211 ? -39.877 29.670  -70.848  1.00 126.95 ?  209 VAL A O   1 
ATOM   1435 C  CB  . VAL A 1 211 ? -38.304 32.161  -71.914  1.00 125.11 ?  209 VAL A CB  1 
ATOM   1436 C  CG1 . VAL A 1 211 ? -36.935 31.680  -71.459  1.00 126.30 ?  209 VAL A CG1 1 
ATOM   1437 C  CG2 . VAL A 1 211 ? -38.179 33.385  -72.810  1.00 120.05 ?  209 VAL A CG2 1 
ATOM   1438 N  N   . VAL A 1 212 ? -38.252 28.801  -72.156  1.00 127.72 ?  210 VAL A N   1 
ATOM   1439 C  CA  . VAL A 1 212 ? -38.146 27.549  -71.414  1.00 126.74 ?  210 VAL A CA  1 
ATOM   1440 C  C   . VAL A 1 212 ? -37.207 27.746  -70.230  1.00 129.00 ?  210 VAL A C   1 
ATOM   1441 O  O   . VAL A 1 212 ? -36.089 28.252  -70.391  1.00 130.09 ?  210 VAL A O   1 
ATOM   1442 C  CB  . VAL A 1 212 ? -37.651 26.419  -72.331  1.00 123.62 ?  210 VAL A CB  1 
ATOM   1443 C  CG1 . VAL A 1 212 ? -37.316 25.175  -71.520  1.00 126.73 ?  210 VAL A CG1 1 
ATOM   1444 C  CG2 . VAL A 1 212 ? -38.683 26.110  -73.406  1.00 119.02 ?  210 VAL A CG2 1 
ATOM   1445 N  N   . TYR A 1 213 ? -37.647 27.343  -69.039  1.00 131.82 ?  211 TYR A N   1 
ATOM   1446 C  CA  . TYR A 1 213 ? -36.853 27.531  -67.833  1.00 133.91 ?  211 TYR A CA  1 
ATOM   1447 C  C   . TYR A 1 213 ? -36.393 26.181  -67.298  1.00 131.78 ?  211 TYR A C   1 
ATOM   1448 O  O   . TYR A 1 213 ? -37.060 25.158  -67.481  1.00 133.68 ?  211 TYR A O   1 
ATOM   1449 C  CB  . TYR A 1 213 ? -37.623 28.327  -66.764  1.00 142.34 ?  211 TYR A CB  1 
ATOM   1450 C  CG  . TYR A 1 213 ? -38.748 27.621  -66.027  1.00 147.92 ?  211 TYR A CG  1 
ATOM   1451 C  CD1 . TYR A 1 213 ? -40.057 27.679  -66.493  1.00 154.13 ?  211 TYR A CD1 1 
ATOM   1452 C  CD2 . TYR A 1 213 ? -38.512 26.955  -64.830  1.00 149.86 ?  211 TYR A CD2 1 
ATOM   1453 C  CE1 . TYR A 1 213 ? -41.091 27.061  -65.808  1.00 159.50 ?  211 TYR A CE1 1 
ATOM   1454 C  CE2 . TYR A 1 213 ? -39.541 26.334  -64.139  1.00 154.45 ?  211 TYR A CE2 1 
ATOM   1455 C  CZ  . TYR A 1 213 ? -40.827 26.391  -64.632  1.00 159.94 ?  211 TYR A CZ  1 
ATOM   1456 O  OH  . TYR A 1 213 ? -41.852 25.774  -63.949  1.00 165.51 ?  211 TYR A OH  1 
ATOM   1457 N  N   . ARG A 1 214 ? -35.237 26.187  -66.633  1.00 128.43 ?  212 ARG A N   1 
ATOM   1458 C  CA  . ARG A 1 214 ? -34.608 24.966  -66.129  1.00 132.01 ?  212 ARG A CA  1 
ATOM   1459 C  C   . ARG A 1 214 ? -34.135 25.184  -64.695  1.00 131.37 ?  212 ARG A C   1 
ATOM   1460 O  O   . ARG A 1 214 ? -33.080 25.781  -64.462  1.00 130.13 ?  212 ARG A O   1 
ATOM   1461 C  CB  . ARG A 1 214 ? -33.448 24.544  -67.028  1.00 126.13 ?  212 ARG A CB  1 
ATOM   1462 N  N   . GLY A 1 215 ? -34.920 24.693  -63.742  1.00 133.14 ?  213 GLY A N   1 
ATOM   1463 C  CA  . GLY A 1 215 ? -34.621 24.852  -62.335  1.00 134.39 ?  213 GLY A CA  1 
ATOM   1464 C  C   . GLY A 1 215 ? -33.755 23.729  -61.802  1.00 134.23 ?  213 GLY A C   1 
ATOM   1465 O  O   . GLY A 1 215 ? -34.139 22.558  -61.875  1.00 133.09 ?  213 GLY A O   1 
ATOM   1466 N  N   . THR A 1 216 ? -32.579 24.068  -61.271  1.00 132.22 ?  214 THR A N   1 
ATOM   1467 C  CA  . THR A 1 216 ? -31.701 23.080  -60.650  1.00 131.28 ?  214 THR A CA  1 
ATOM   1468 C  C   . THR A 1 216 ? -32.440 22.305  -59.564  1.00 135.16 ?  214 THR A C   1 
ATOM   1469 O  O   . THR A 1 216 ? -31.952 21.281  -59.074  1.00 127.45 ?  214 THR A O   1 
ATOM   1470 C  CB  . THR A 1 216 ? -30.464 23.760  -60.061  1.00 125.23 ?  214 THR A CB  1 
ATOM   1471 O  OG1 . THR A 1 216 ? -30.866 24.909  -59.306  1.00 128.80 ?  214 THR A OG1 1 
ATOM   1472 C  CG2 . THR A 1 216 ? -29.524 24.200  -61.171  1.00 116.67 ?  214 THR A CG2 1 
ATOM   1473 N  N   . THR A 1 217 ? -33.617 22.796  -59.187  1.00 137.35 ?  215 THR A N   1 
ATOM   1474 C  CA  . THR A 1 217 ? -34.492 22.160  -58.217  1.00 139.14 ?  215 THR A CA  1 
ATOM   1475 C  C   . THR A 1 217 ? -35.886 22.073  -58.819  1.00 141.41 ?  215 THR A C   1 
ATOM   1476 O  O   . THR A 1 217 ? -36.193 22.730  -59.817  1.00 142.98 ?  215 THR A O   1 
ATOM   1477 C  CB  . THR A 1 217 ? -34.542 22.931  -56.889  1.00 137.57 ?  215 THR A CB  1 
ATOM   1478 O  OG1 . THR A 1 217 ? -35.621 23.875  -56.924  1.00 141.08 ?  215 THR A OG1 1 
ATOM   1479 C  CG2 . THR A 1 217 ? -33.237 23.673  -56.651  1.00 135.07 ?  215 THR A CG2 1 
ATOM   1480 N  N   . THR A 1 218 ? -36.733 21.251  -58.208  1.00 140.57 ?  216 THR A N   1 
ATOM   1481 C  CA  . THR A 1 218 ? -38.115 21.113  -58.667  1.00 144.54 ?  216 THR A CA  1 
ATOM   1482 C  C   . THR A 1 218 ? -39.040 22.085  -57.951  1.00 146.53 ?  216 THR A C   1 
ATOM   1483 O  O   . THR A 1 218 ? -40.153 21.729  -57.550  1.00 145.57 ?  216 THR A O   1 
ATOM   1484 C  CB  . THR A 1 218 ? -38.585 19.675  -58.484  1.00 143.38 ?  216 THR A CB  1 
ATOM   1485 O  OG1 . THR A 1 218 ? -37.479 18.782  -58.667  1.00 137.36 ?  216 THR A OG1 1 
ATOM   1486 C  CG2 . THR A 1 218 ? -39.668 19.338  -59.501  1.00 138.29 ?  216 THR A CG2 1 
ATOM   1487 N  N   . TYR A 1 219 ? -38.589 23.327  -57.787  1.00 149.75 ?  217 TYR A N   1 
ATOM   1488 C  CA  . TYR A 1 219 ? -39.406 24.373  -57.192  1.00 151.77 ?  217 TYR A CA  1 
ATOM   1489 C  C   . TYR A 1 219 ? -40.325 24.955  -58.258  1.00 157.51 ?  217 TYR A C   1 
ATOM   1490 O  O   . TYR A 1 219 ? -39.867 25.353  -59.335  1.00 158.51 ?  217 TYR A O   1 
ATOM   1491 C  CB  . TYR A 1 219 ? -38.490 25.444  -56.590  1.00 146.69 ?  217 TYR A CB  1 
ATOM   1492 C  CG  . TYR A 1 219 ? -39.098 26.807  -56.330  1.00 148.16 ?  217 TYR A CG  1 
ATOM   1493 C  CD1 . TYR A 1 219 ? -39.074 27.798  -57.305  1.00 149.56 ?  217 TYR A CD1 1 
ATOM   1494 C  CD2 . TYR A 1 219 ? -39.655 27.118  -55.097  1.00 144.12 ?  217 TYR A CD2 1 
ATOM   1495 C  CE1 . TYR A 1 219 ? -39.611 29.051  -57.067  1.00 149.31 ?  217 TYR A CE1 1 
ATOM   1496 C  CE2 . TYR A 1 219 ? -40.195 28.368  -54.850  1.00 146.49 ?  217 TYR A CE2 1 
ATOM   1497 C  CZ  . TYR A 1 219 ? -40.170 29.330  -55.838  1.00 146.32 ?  217 TYR A CZ  1 
ATOM   1498 O  OH  . TYR A 1 219 ? -40.704 30.576  -55.595  1.00 140.05 ?  217 TYR A OH  1 
ATOM   1499 N  N   . LYS A 1 220 ? -41.625 24.998  -57.957  1.00 158.59 ?  218 LYS A N   1 
ATOM   1500 C  CA  . LYS A 1 220 ? -42.588 25.477  -58.935  1.00 161.23 ?  218 LYS A CA  1 
ATOM   1501 C  C   . LYS A 1 220 ? -42.474 26.979  -59.137  1.00 163.77 ?  218 LYS A C   1 
ATOM   1502 O  O   . LYS A 1 220 ? -43.091 27.755  -58.400  1.00 161.72 ?  218 LYS A O   1 
ATOM   1503 C  CB  . LYS A 1 220 ? -44.011 25.112  -58.493  1.00 160.39 ?  218 LYS A CB  1 
ATOM   1504 N  N   . LEU A 1 221 ? -41.633 27.397  -60.077  1.00 164.63 ?  219 LEU A N   1 
ATOM   1505 C  CA  . LEU A 1 221 ? -41.394 28.821  -60.268  1.00 166.13 ?  219 LEU A CA  1 
ATOM   1506 C  C   . LEU A 1 221 ? -42.736 29.556  -60.336  1.00 165.24 ?  219 LEU A C   1 
ATOM   1507 O  O   . LEU A 1 221 ? -43.549 29.277  -61.220  1.00 169.03 ?  219 LEU A O   1 
ATOM   1508 C  CB  . LEU A 1 221 ? -40.584 29.033  -61.554  1.00 172.70 ?  219 LEU A CB  1 
ATOM   1509 N  N   . ASN A 1 222 ? -42.980 30.480  -59.417  1.00 160.77 ?  220 ASN A N   1 
ATOM   1510 C  CA  . ASN A 1 222 ? -44.217 31.258  -59.384  1.00 157.38 ?  220 ASN A CA  1 
ATOM   1511 C  C   . ASN A 1 222 ? -43.969 32.661  -59.967  1.00 151.83 ?  220 ASN A C   1 
ATOM   1512 O  O   . ASN A 1 222 ? -42.846 32.990  -60.369  1.00 151.65 ?  220 ASN A O   1 
ATOM   1513 C  CB  . ASN A 1 222 ? -44.769 31.321  -57.954  1.00 153.40 ?  220 ASN A CB  1 
ATOM   1514 C  CG  . ASN A 1 222 ? -43.687 31.317  -56.907  1.00 152.68 ?  220 ASN A CG  1 
ATOM   1515 O  OD1 . ASN A 1 222 ? -42.903 30.375  -56.831  1.00 153.22 ?  220 ASN A OD1 1 
ATOM   1516 N  ND2 . ASN A 1 222 ? -43.635 32.364  -56.092  1.00 147.66 ?  220 ASN A ND2 1 
ATOM   1517 N  N   . VAL A 1 223 ? -45.038 33.478  -60.055  1.00 149.60 ?  221 VAL A N   1 
ATOM   1518 C  CA  . VAL A 1 223 ? -44.915 34.843  -60.584  1.00 146.10 ?  221 VAL A CA  1 
ATOM   1519 C  C   . VAL A 1 223 ? -44.479 35.734  -59.424  1.00 142.44 ?  221 VAL A C   1 
ATOM   1520 O  O   . VAL A 1 223 ? -44.590 35.360  -58.256  1.00 142.40 ?  221 VAL A O   1 
ATOM   1521 C  CB  . VAL A 1 223 ? -46.244 35.321  -61.223  1.00 146.08 ?  221 VAL A CB  1 
ATOM   1522 C  CG1 . VAL A 1 223 ? -46.171 36.781  -61.690  1.00 140.09 ?  221 VAL A CG1 1 
ATOM   1523 C  CG2 . VAL A 1 223 ? -46.673 34.404  -62.356  1.00 152.76 ?  221 VAL A CG2 1 
ATOM   1524 N  N   . GLY A 1 224 ? -43.963 36.915  -59.728  1.00 137.30 ?  222 GLY A N   1 
ATOM   1525 C  CA  . GLY A 1 224 ? -43.430 37.770  -58.686  1.00 130.55 ?  222 GLY A CA  1 
ATOM   1526 C  C   . GLY A 1 224 ? -42.026 37.350  -58.318  1.00 129.89 ?  222 GLY A C   1 
ATOM   1527 O  O   . GLY A 1 224 ? -41.359 38.033  -57.525  1.00 124.73 ?  222 GLY A O   1 
ATOM   1528 N  N   . ASP A 1 225 ? -41.574 36.225  -58.862  1.00 135.30 ?  223 ASP A N   1 
ATOM   1529 C  CA  . ASP A 1 225 ? -40.226 35.744  -58.646  1.00 132.74 ?  223 ASP A CA  1 
ATOM   1530 C  C   . ASP A 1 225 ? -39.291 36.566  -59.538  1.00 127.56 ?  223 ASP A C   1 
ATOM   1531 O  O   . ASP A 1 225 ? -39.735 37.381  -60.354  1.00 124.95 ?  223 ASP A O   1 
ATOM   1532 C  CB  . ASP A 1 225 ? -40.146 34.235  -58.923  1.00 136.13 ?  223 ASP A CB  1 
ATOM   1533 C  CG  . ASP A 1 225 ? -41.056 33.414  -58.002  1.00 144.15 ?  223 ASP A CG  1 
ATOM   1534 O  OD1 . ASP A 1 225 ? -41.816 34.019  -57.204  1.00 141.40 ?  223 ASP A OD1 1 
ATOM   1535 O  OD2 . ASP A 1 225 ? -40.998 32.169  -58.062  1.00 150.86 -1 223 ASP A OD2 1 
ATOM   1536 N  N   . TYR A 1 226 ? -37.998 36.388  -59.350  1.00 125.72 ?  224 TYR A N   1 
ATOM   1537 C  CA  . TYR A 1 226 ? -37.019 37.183  -60.092  1.00 125.03 ?  224 TYR A CA  1 
ATOM   1538 C  C   . TYR A 1 226 ? -35.701 36.434  -60.370  1.00 126.02 ?  224 TYR A C   1 
ATOM   1539 O  O   . TYR A 1 226 ? -35.041 35.934  -59.460  1.00 123.62 ?  224 TYR A O   1 
ATOM   1540 C  CB  . TYR A 1 226 ? -36.817 38.526  -59.344  1.00 119.15 ?  224 TYR A CB  1 
ATOM   1541 C  CG  . TYR A 1 226 ? -35.693 38.661  -58.337  1.00 113.38 ?  224 TYR A CG  1 
ATOM   1542 C  CD1 . TYR A 1 226 ? -34.415 39.015  -58.737  1.00 109.88 ?  224 TYR A CD1 1 
ATOM   1543 C  CD2 . TYR A 1 226 ? -35.918 38.440  -56.979  1.00 111.40 ?  224 TYR A CD2 1 
ATOM   1544 C  CE1 . TYR A 1 226 ? -33.389 39.152  -57.820  1.00 105.41 ?  224 TYR A CE1 1 
ATOM   1545 C  CE2 . TYR A 1 226 ? -34.892 38.569  -56.054  1.00 109.06 ?  224 TYR A CE2 1 
ATOM   1546 C  CZ  . TYR A 1 226 ? -33.630 38.925  -56.484  1.00 102.09 ?  224 TYR A CZ  1 
ATOM   1547 O  OH  . TYR A 1 226 ? -32.601 39.064  -55.576  1.00 96.66  ?  224 TYR A OH  1 
ATOM   1548 N  N   . VAL A 1 228 ? -30.992 36.552  -60.752  1.00 119.25 ?  226 VAL A N   1 
ATOM   1549 C  CA  . VAL A 1 228 ? -30.037 37.496  -61.294  1.00 117.23 ?  226 VAL A CA  1 
ATOM   1550 C  C   . VAL A 1 228 ? -28.845 36.721  -61.879  1.00 121.54 ?  226 VAL A C   1 
ATOM   1551 O  O   . VAL A 1 228 ? -28.551 35.623  -61.414  1.00 122.42 ?  226 VAL A O   1 
ATOM   1552 C  CB  . VAL A 1 228 ? -29.589 38.501  -60.189  1.00 112.89 ?  226 VAL A CB  1 
ATOM   1553 C  CG1 . VAL A 1 228 ? -28.064 38.601  -60.106  1.00 107.48 ?  226 VAL A CG1 1 
ATOM   1554 C  CG2 . VAL A 1 228 ? -30.242 39.860  -60.389  1.00 104.05 ?  226 VAL A CG2 1 
ATOM   1555 N  N   . LEU A 1 229 ? -28.181 37.282  -62.892  1.00 117.79 ?  227 LEU A N   1 
ATOM   1556 C  CA  . LEU A 1 229 ? -27.032 36.619  -63.507  1.00 119.99 ?  227 LEU A CA  1 
ATOM   1557 C  C   . LEU A 1 229 ? -26.057 36.150  -62.433  1.00 121.59 ?  227 LEU A C   1 
ATOM   1558 O  O   . LEU A 1 229 ? -25.693 36.919  -61.537  1.00 119.68 ?  227 LEU A O   1 
ATOM   1559 C  CB  . LEU A 1 229 ? -26.335 37.586  -64.479  1.00 119.02 ?  227 LEU A CB  1 
ATOM   1560 C  CG  . LEU A 1 229 ? -26.585 37.374  -65.976  1.00 120.13 ?  227 LEU A CG  1 
ATOM   1561 C  CD1 . LEU A 1 229 ? -25.698 38.284  -66.809  1.00 116.49 ?  227 LEU A CD1 1 
ATOM   1562 C  CD2 . LEU A 1 229 ? -26.373 35.921  -66.360  1.00 119.73 ?  227 LEU A CD2 1 
ATOM   1563 N  N   . THR A 1 230 ? -25.595 34.908  -62.550  1.00 121.11 ?  228 THR A N   1 
ATOM   1564 C  CA  . THR A 1 230 ? -24.636 34.361  -61.594  1.00 116.98 ?  228 THR A CA  1 
ATOM   1565 C  C   . THR A 1 230 ? -23.384 35.239  -61.602  1.00 115.54 ?  228 THR A C   1 
ATOM   1566 O  O   . THR A 1 230 ? -23.056 35.870  -62.605  1.00 111.94 ?  228 THR A O   1 
ATOM   1567 C  CB  . THR A 1 230 ? -24.271 32.913  -61.955  1.00 110.22 ?  228 THR A CB  1 
ATOM   1568 N  N   . SER A 1 231 ? -22.664 35.280  -60.483  1.00 112.29 ?  229 SER A N   1 
ATOM   1569 C  CA  . SER A 1 231 ? -21.385 36.023  -60.456  1.00 109.27 ?  229 SER A CA  1 
ATOM   1570 C  C   . SER A 1 231 ? -20.395 35.294  -59.541  1.00 108.50 ?  229 SER A C   1 
ATOM   1571 O  O   . SER A 1 231 ? -20.524 34.091  -59.297  1.00 108.57 ?  229 SER A O   1 
ATOM   1572 C  CB  . SER A 1 231 ? -21.622 37.486  -60.033  1.00 112.23 ?  229 SER A CB  1 
ATOM   1573 O  OG  . SER A 1 231 ? -22.679 38.057  -60.776  1.00 113.88 ?  229 SER A OG  1 
ATOM   1574 N  N   . HIS A 1 232 ? -19.405 36.026  -59.013  1.00 107.50 ?  230 HIS A N   1 
ATOM   1575 C  CA  . HIS A 1 232 ? -18.349 35.438  -58.179  1.00 107.44 ?  230 HIS A CA  1 
ATOM   1576 C  C   . HIS A 1 232 ? -17.353 36.514  -57.766  1.00 107.39 ?  230 HIS A C   1 
ATOM   1577 O  O   . HIS A 1 232 ? -17.343 37.622  -58.308  1.00 107.63 ?  230 HIS A O   1 
ATOM   1578 C  CB  . HIS A 1 232 ? -17.546 34.406  -58.959  1.00 106.44 ?  230 HIS A CB  1 
ATOM   1579 C  CG  . HIS A 1 232 ? -16.979 33.292  -58.133  1.00 110.22 ?  230 HIS A CG  1 
ATOM   1580 N  ND1 . HIS A 1 232 ? -16.650 33.405  -56.796  1.00 112.04 ?  230 HIS A ND1 1 
ATOM   1581 C  CD2 . HIS A 1 232 ? -16.642 32.033  -58.494  1.00 109.05 ?  230 HIS A CD2 1 
ATOM   1582 C  CE1 . HIS A 1 232 ? -16.180 32.246  -56.364  1.00 108.32 ?  230 HIS A CE1 1 
ATOM   1583 N  NE2 . HIS A 1 232 ? -16.159 31.400  -57.378  1.00 110.59 ?  230 HIS A NE2 1 
ATOM   1584 N  N   . THR A 1 233 ? -16.482 36.163  -56.816  1.00 107.85 ?  231 THR A N   1 
ATOM   1585 C  CA  . THR A 1 233 ? -15.444 37.070  -56.347  1.00 105.76 ?  231 THR A CA  1 
ATOM   1586 C  C   . THR A 1 233 ? -14.105 36.533  -56.842  1.00 104.02 ?  231 THR A C   1 
ATOM   1587 O  O   . THR A 1 233 ? -13.773 35.363  -56.605  1.00 105.75 ?  231 THR A O   1 
ATOM   1588 C  CB  . THR A 1 233 ? -15.440 37.196  -54.821  1.00 107.01 ?  231 THR A CB  1 
ATOM   1589 O  OG1 . THR A 1 233 ? -16.707 37.697  -54.382  1.00 104.57 ?  231 THR A OG1 1 
ATOM   1590 C  CG2 . THR A 1 233 ? -14.341 38.148  -54.371  1.00 107.95 ?  231 THR A CG2 1 
ATOM   1591 N  N   . VAL A 1 234 ? -13.338 37.385  -57.520  1.00 102.71 ?  232 VAL A N   1 
ATOM   1592 C  CA  . VAL A 1 234 ? -12.074 36.981  -58.137  1.00 96.28  ?  232 VAL A CA  1 
ATOM   1593 C  C   . VAL A 1 234 ? -11.021 36.839  -57.041  1.00 95.49  ?  232 VAL A C   1 
ATOM   1594 O  O   . VAL A 1 234 ? -10.409 37.827  -56.631  1.00 89.07  ?  232 VAL A O   1 
ATOM   1595 C  CB  . VAL A 1 234 ? -11.630 37.959  -59.226  1.00 90.12  ?  232 VAL A CB  1 
ATOM   1596 C  CG1 . VAL A 1 234 ? -10.346 37.469  -59.879  1.00 84.50  ?  232 VAL A CG1 1 
ATOM   1597 C  CG2 . VAL A 1 234 ? -12.731 38.128  -60.262  1.00 92.92  ?  232 VAL A CG2 1 
ATOM   1598 N  N   . MET A 1 235 ? -10.803 35.619  -56.564  1.00 92.70  ?  233 MET A N   1 
ATOM   1599 C  CA  . MET A 1 235 ? -9.716  35.386  -55.632  1.00 89.10  ?  233 MET A CA  1 
ATOM   1600 C  C   . MET A 1 235 ? -8.383  35.581  -56.355  1.00 87.26  ?  233 MET A C   1 
ATOM   1601 O  O   . MET A 1 235 ? -8.282  35.330  -57.558  1.00 82.96  ?  233 MET A O   1 
ATOM   1602 C  CB  . MET A 1 235 ? -9.793  33.979  -55.046  1.00 88.87  ?  233 MET A CB  1 
ATOM   1603 C  CG  . MET A 1 235 ? -11.114 33.643  -54.364  1.00 90.58  ?  233 MET A CG  1 
ATOM   1604 S  SD  . MET A 1 235 ? -11.495 34.693  -52.946  1.00 102.97 ?  233 MET A SD  1 
ATOM   1605 C  CE  . MET A 1 235 ? -10.016 34.489  -51.955  1.00 95.14  ?  233 MET A CE  1 
ATOM   1606 N  N   . PRO A 1 236 ? -7.349  36.032  -55.653  1.00 90.78  ?  234 PRO A N   1 
ATOM   1607 C  CA  . PRO A 1 236 ? -6.055  36.249  -56.309  1.00 91.46  ?  234 PRO A CA  1 
ATOM   1608 C  C   . PRO A 1 236 ? -5.401  34.926  -56.684  1.00 91.06  ?  234 PRO A C   1 
ATOM   1609 O  O   . PRO A 1 236 ? -5.833  33.843  -56.285  1.00 87.56  ?  234 PRO A O   1 
ATOM   1610 C  CB  . PRO A 1 236 ? -5.255  37.001  -55.244  1.00 88.87  ?  234 PRO A CB  1 
ATOM   1611 C  CG  . PRO A 1 236 ? -5.808  36.462  -53.965  1.00 90.65  ?  234 PRO A CG  1 
ATOM   1612 C  CD  . PRO A 1 236 ? -7.295  36.401  -54.228  1.00 92.30  ?  234 PRO A CD  1 
ATOM   1613 N  N   . LEU A 1 237 ? -4.327  35.031  -57.463  1.00 88.21  ?  235 LEU A N   1 
ATOM   1614 C  CA  . LEU A 1 237 ? -3.603  33.871  -57.960  1.00 81.88  ?  235 LEU A CA  1 
ATOM   1615 C  C   . LEU A 1 237 ? -2.153  33.944  -57.505  1.00 82.13  ?  235 LEU A C   1 
ATOM   1616 O  O   . LEU A 1 237 ? -1.612  35.029  -57.275  1.00 84.84  ?  235 LEU A O   1 
ATOM   1617 C  CB  . LEU A 1 237 ? -3.660  33.789  -59.493  1.00 83.68  ?  235 LEU A CB  1 
ATOM   1618 C  CG  . LEU A 1 237 ? -5.018  33.555  -60.163  1.00 83.44  ?  235 LEU A CG  1 
ATOM   1619 C  CD1 . LEU A 1 237 ? -4.863  33.498  -61.676  1.00 74.79  ?  235 LEU A CD1 1 
ATOM   1620 C  CD2 . LEU A 1 237 ? -5.682  32.290  -59.643  1.00 76.28  ?  235 LEU A CD2 1 
ATOM   1621 N  N   . SER A 1 238 ? -1.524  32.775  -57.382  1.00 81.95  ?  236 SER A N   1 
ATOM   1622 C  CA  . SER A 1 238 ? -0.153  32.701  -56.891  1.00 86.91  ?  236 SER A CA  1 
ATOM   1623 C  C   . SER A 1 238 ? 0.695   31.754  -57.731  1.00 84.27  ?  236 SER A C   1 
ATOM   1624 O  O   . SER A 1 238 ? 1.862   32.041  -58.013  1.00 88.08  ?  236 SER A O   1 
ATOM   1625 C  CB  . SER A 1 238 ? -0.138  32.261  -55.425  1.00 88.79  ?  236 SER A CB  1 
ATOM   1626 O  OG  . SER A 1 238 ? -0.820  31.031  -55.256  1.00 87.44  ?  236 SER A OG  1 
ATOM   1627 N  N   . ALA A 1 239 ? 0.121   30.624  -58.128  1.00 80.59  ?  237 ALA A N   1 
ATOM   1628 C  CA  . ALA A 1 239 ? 0.901   29.615  -58.823  1.00 81.70  ?  237 ALA A CA  1 
ATOM   1629 C  C   . ALA A 1 239 ? 0.976   29.934  -60.314  1.00 79.00  ?  237 ALA A C   1 
ATOM   1630 O  O   . ALA A 1 239 ? 0.062   30.546  -60.872  1.00 79.83  ?  237 ALA A O   1 
ATOM   1631 C  CB  . ALA A 1 239 ? 0.290   28.232  -58.620  1.00 78.16  ?  237 ALA A CB  1 
ATOM   1632 N  N   . PRO A 1 240 ? 2.055   29.536  -60.980  1.00 81.02  ?  238 PRO A N   1 
ATOM   1633 C  CA  . PRO A 1 240 ? 2.148   29.749  -62.427  1.00 76.16  ?  238 PRO A CA  1 
ATOM   1634 C  C   . PRO A 1 240 ? 1.182   28.848  -63.182  1.00 76.18  ?  238 PRO A C   1 
ATOM   1635 O  O   . PRO A 1 240 ? 0.607   27.901  -62.641  1.00 70.87  ?  238 PRO A O   1 
ATOM   1636 C  CB  . PRO A 1 240 ? 3.606   29.393  -62.725  1.00 76.47  ?  238 PRO A CB  1 
ATOM   1637 C  CG  . PRO A 1 240 ? 3.900   28.315  -61.725  1.00 77.00  ?  238 PRO A CG  1 
ATOM   1638 C  CD  . PRO A 1 240 ? 3.229   28.809  -60.461  1.00 78.70  ?  238 PRO A CD  1 
ATOM   1639 N  N   . THR A 1 241 ? 0.996   29.167  -64.466  1.00 70.06  ?  239 THR A N   1 
ATOM   1640 C  CA  . THR A 1 241 ? 0.141   28.337  -65.308  1.00 74.90  ?  239 THR A CA  1 
ATOM   1641 C  C   . THR A 1 241 ? 0.766   26.963  -65.490  1.00 75.39  ?  239 THR A C   1 
ATOM   1642 O  O   . THR A 1 241 ? 0.096   25.933  -65.344  1.00 69.65  ?  239 THR A O   1 
ATOM   1643 C  CB  . THR A 1 241 ? -0.084  29.002  -66.668  1.00 71.07  ?  239 THR A CB  1 
ATOM   1644 O  OG1 . THR A 1 241 ? 1.182   29.257  -67.292  1.00 72.59  ?  239 THR A OG1 1 
ATOM   1645 C  CG2 . THR A 1 241 ? -0.839  30.314  -66.509  1.00 70.82  ?  239 THR A CG2 1 
ATOM   1646 N  N   . LEU A 1 242 ? 2.052   26.940  -65.827  1.00 77.89  ?  240 LEU A N   1 
ATOM   1647 C  CA  . LEU A 1 242 ? 2.839   25.727  -65.981  1.00 75.05  ?  240 LEU A CA  1 
ATOM   1648 C  C   . LEU A 1 242 ? 4.011   25.799  -65.016  1.00 79.18  ?  240 LEU A C   1 
ATOM   1649 O  O   . LEU A 1 242 ? 4.729   26.804  -64.986  1.00 82.09  ?  240 LEU A O   1 
ATOM   1650 C  CB  . LEU A 1 242 ? 3.352   25.582  -67.415  1.00 72.93  ?  240 LEU A CB  1 
ATOM   1651 C  CG  . LEU A 1 242 ? 2.375   25.085  -68.476  1.00 73.94  ?  240 LEU A CG  1 
ATOM   1652 C  CD1 . LEU A 1 242 ? 3.067   25.033  -69.827  1.00 69.04  ?  240 LEU A CD1 1 
ATOM   1653 C  CD2 . LEU A 1 242 ? 1.831   23.720  -68.096  1.00 73.94  ?  240 LEU A CD2 1 
ATOM   1654 N  N   . VAL A 1 243 ? 4.202   24.749  -64.224  1.00 80.92  ?  241 VAL A N   1 
ATOM   1655 C  CA  . VAL A 1 243 ? 5.379   24.678  -63.364  1.00 80.34  ?  241 VAL A CA  1 
ATOM   1656 C  C   . VAL A 1 243 ? 6.599   24.595  -64.273  1.00 78.39  ?  241 VAL A C   1 
ATOM   1657 O  O   . VAL A 1 243 ? 6.495   24.075  -65.393  1.00 82.79  ?  241 VAL A O   1 
ATOM   1658 C  CB  . VAL A 1 243 ? 5.309   23.486  -62.397  1.00 79.74  ?  241 VAL A CB  1 
ATOM   1659 C  CG1 . VAL A 1 243 ? 4.245   23.723  -61.336  1.00 80.30  ?  241 VAL A CG1 1 
ATOM   1660 C  CG2 . VAL A 1 243 ? 5.030   22.201  -63.160  1.00 79.26  ?  241 VAL A CG2 1 
ATOM   1661 N  N   . PRO A 1 244 ? 7.756   25.111  -63.859  1.00 84.00  ?  242 PRO A N   1 
ATOM   1662 C  CA  . PRO A 1 244 ? 8.958   24.971  -64.687  1.00 85.02  ?  242 PRO A CA  1 
ATOM   1663 C  C   . PRO A 1 244 ? 9.172   23.516  -65.077  1.00 88.01  ?  242 PRO A C   1 
ATOM   1664 O  O   . PRO A 1 244 ? 8.886   22.599  -64.305  1.00 88.40  ?  242 PRO A O   1 
ATOM   1665 C  CB  . PRO A 1 244 ? 10.073  25.477  -63.766  1.00 87.41  ?  242 PRO A CB  1 
ATOM   1666 C  CG  . PRO A 1 244 ? 9.375   26.488  -62.913  1.00 92.02  ?  242 PRO A CG  1 
ATOM   1667 C  CD  . PRO A 1 244 ? 8.048   25.830  -62.607  1.00 86.37  ?  242 PRO A CD  1 
ATOM   1668 N  N   . GLN A 1 245 ? 9.690   23.304  -66.283  1.00 91.43  ?  243 GLN A N   1 
ATOM   1669 C  CA  . GLN A 1 245 ? 9.823   21.944  -66.780  1.00 91.28  ?  243 GLN A CA  1 
ATOM   1670 C  C   . GLN A 1 245 ? 11.025  21.273  -66.135  1.00 96.05  ?  243 GLN A C   1 
ATOM   1671 O  O   . GLN A 1 245 ? 12.049  21.905  -65.861  1.00 102.68 ?  243 GLN A O   1 
ATOM   1672 C  CB  . GLN A 1 245 ? 9.965   21.925  -68.303  1.00 86.21  ?  243 GLN A CB  1 
ATOM   1673 C  CG  . GLN A 1 245 ? 10.068  20.526  -68.919  1.00 85.71  ?  243 GLN A CG  1 
ATOM   1674 C  CD  . GLN A 1 245 ? 8.829   19.672  -68.695  1.00 84.27  ?  243 GLN A CD  1 
ATOM   1675 O  OE1 . GLN A 1 245 ? 8.601   19.160  -67.599  1.00 82.34  ?  243 GLN A OE1 1 
ATOM   1676 N  NE2 . GLN A 1 245 ? 8.026   19.510  -69.742  1.00 85.38  ?  243 GLN A NE2 1 
ATOM   1677 N  N   . GLU A 1 246 ? 10.888  19.974  -65.891  1.00 92.38  ?  244 GLU A N   1 
ATOM   1678 C  CA  . GLU A 1 246 ? 11.969  19.157  -65.366  1.00 97.36  ?  244 GLU A CA  1 
ATOM   1679 C  C   . GLU A 1 246 ? 12.057  17.892  -66.201  1.00 100.62 ?  244 GLU A C   1 
ATOM   1680 O  O   . GLU A 1 246 ? 11.055  17.192  -66.378  1.00 91.76  ?  244 GLU A O   1 
ATOM   1681 C  CB  . GLU A 1 246 ? 11.731  18.822  -63.891  1.00 92.09  ?  244 GLU A CB  1 
ATOM   1682 C  CG  . GLU A 1 246 ? 11.599  20.053  -63.007  1.00 94.66  ?  244 GLU A CG  1 
ATOM   1683 C  CD  . GLU A 1 246 ? 11.786  19.745  -61.537  1.00 96.20  ?  244 GLU A CD  1 
ATOM   1684 O  OE1 . GLU A 1 246 ? 11.039  18.895  -61.008  1.00 97.06  ?  244 GLU A OE1 1 
ATOM   1685 O  OE2 . GLU A 1 246 ? 12.672  20.361  -60.908  1.00 103.20 -1 244 GLU A OE2 1 
ATOM   1686 N  N   . HIS A 1 247 ? 13.246  17.606  -66.720  1.00 102.74 ?  245 HIS A N   1 
ATOM   1687 C  CA  . HIS A 1 247 ? 13.497  16.385  -67.473  1.00 100.93 ?  245 HIS A CA  1 
ATOM   1688 C  C   . HIS A 1 247 ? 14.398  15.474  -66.652  1.00 104.03 ?  245 HIS A C   1 
ATOM   1689 O  O   . HIS A 1 247 ? 15.520  15.853  -66.298  1.00 99.24  ?  245 HIS A O   1 
ATOM   1690 C  CB  . HIS A 1 247 ? 14.122  16.696  -68.831  1.00 102.41 ?  245 HIS A CB  1 
ATOM   1691 C  CG  . HIS A 1 247 ? 13.176  17.348  -69.788  1.00 102.16 ?  245 HIS A CG  1 
ATOM   1692 N  ND1 . HIS A 1 247 ? 12.350  16.628  -70.625  1.00 99.75  ?  245 HIS A ND1 1 
ATOM   1693 C  CD2 . HIS A 1 247 ? 12.916  18.653  -70.036  1.00 102.92 ?  245 HIS A CD2 1 
ATOM   1694 C  CE1 . HIS A 1 247 ? 11.625  17.461  -71.349  1.00 98.85  ?  245 HIS A CE1 1 
ATOM   1695 N  NE2 . HIS A 1 247 ? 11.950  18.696  -71.011  1.00 98.85  ?  245 HIS A NE2 1 
ATOM   1696 N  N   . TYR A 1 248 ? 13.900  14.283  -66.352  1.00 102.32 ?  246 TYR A N   1 
ATOM   1697 C  CA  . TYR A 1 248 ? 14.597  13.313  -65.526  1.00 100.74 ?  246 TYR A CA  1 
ATOM   1698 C  C   . TYR A 1 248 ? 15.306  12.296  -66.412  1.00 106.39 ?  246 TYR A C   1 
ATOM   1699 O  O   . TYR A 1 248 ? 15.062  12.203  -67.617  1.00 105.43 ?  246 TYR A O   1 
ATOM   1700 C  CB  . TYR A 1 248 ? 13.602  12.623  -64.590  1.00 97.74  ?  246 TYR A CB  1 
ATOM   1701 C  CG  . TYR A 1 248 ? 12.661  13.603  -63.930  1.00 101.03 ?  246 TYR A CG  1 
ATOM   1702 C  CD1 . TYR A 1 248 ? 13.135  14.788  -63.384  1.00 102.66 ?  246 TYR A CD1 1 
ATOM   1703 C  CD2 . TYR A 1 248 ? 11.292  13.371  -63.905  1.00 96.06  ?  246 TYR A CD2 1 
ATOM   1704 C  CE1 . TYR A 1 248 ? 12.277  15.697  -62.796  1.00 102.26 ?  246 TYR A CE1 1 
ATOM   1705 C  CE2 . TYR A 1 248 ? 10.425  14.276  -63.322  1.00 91.82  ?  246 TYR A CE2 1 
ATOM   1706 C  CZ  . TYR A 1 248 ? 10.923  15.437  -62.770  1.00 94.30  ?  246 TYR A CZ  1 
ATOM   1707 O  OH  . TYR A 1 248 ? 10.066  16.342  -62.187  1.00 98.43  ?  246 TYR A OH  1 
ATOM   1708 N  N   . VAL A 1 249 ? 16.196  11.519  -65.796  1.00 113.87 ?  247 VAL A N   1 
ATOM   1709 C  CA  . VAL A 1 249 ? 16.925  10.499  -66.539  1.00 114.07 ?  247 VAL A CA  1 
ATOM   1710 C  C   . VAL A 1 249 ? 16.157  9.185   -66.584  1.00 112.52 ?  247 VAL A C   1 
ATOM   1711 O  O   . VAL A 1 249 ? 16.389  8.370   -67.489  1.00 109.97 ?  247 VAL A O   1 
ATOM   1712 C  CB  . VAL A 1 249 ? 18.322  10.272  -65.934  1.00 112.38 ?  247 VAL A CB  1 
ATOM   1713 C  CG1 . VAL A 1 249 ? 19.181  11.515  -66.105  1.00 110.36 ?  247 VAL A CG1 1 
ATOM   1714 C  CG2 . VAL A 1 249 ? 18.207  9.891   -64.466  1.00 113.70 ?  247 VAL A CG2 1 
ATOM   1715 N  N   . ARG A 1 250 ? 15.245  8.966   -65.642  1.00 113.10 ?  248 ARG A N   1 
ATOM   1716 C  CA  . ARG A 1 250 ? 14.487  7.731   -65.537  1.00 109.24 ?  248 ARG A CA  1 
ATOM   1717 C  C   . ARG A 1 250 ? 13.158  8.057   -64.872  1.00 104.77 ?  248 ARG A C   1 
ATOM   1718 O  O   . ARG A 1 250 ? 12.956  9.159   -64.353  1.00 99.70  ?  248 ARG A O   1 
ATOM   1719 C  CB  . ARG A 1 250 ? 15.255  6.662   -64.752  1.00 107.71 ?  248 ARG A CB  1 
ATOM   1720 N  N   . ILE A 1 251 ? 12.241  7.091   -64.907  1.00 101.39 ?  249 ILE A N   1 
ATOM   1721 C  CA  . ILE A 1 251 ? 10.947  7.281   -64.263  1.00 99.60  ?  249 ILE A CA  1 
ATOM   1722 C  C   . ILE A 1 251 ? 11.176  7.647   -62.805  1.00 102.59 ?  249 ILE A C   1 
ATOM   1723 O  O   . ILE A 1 251 ? 11.779  6.880   -62.044  1.00 95.57  ?  249 ILE A O   1 
ATOM   1724 C  CB  . ILE A 1 251 ? 10.085  6.022   -64.398  1.00 102.20 ?  249 ILE A CB  1 
ATOM   1725 C  CG1 . ILE A 1 251 ? 9.864   5.683   -65.873  1.00 98.97  ?  249 ILE A CG1 1 
ATOM   1726 C  CG2 . ILE A 1 251 ? 8.759   6.204   -63.672  1.00 100.97 ?  249 ILE A CG2 1 
ATOM   1727 C  CD1 . ILE A 1 251 ? 8.903   4.538   -66.098  1.00 98.88  ?  249 ILE A CD1 1 
ATOM   1728 N  N   . THR A 1 252 ? 10.702  8.824   -62.410  1.00 100.84 ?  250 THR A N   1 
ATOM   1729 C  CA  . THR A 1 252 ? 10.942  9.360   -61.077  1.00 99.20  ?  250 THR A CA  1 
ATOM   1730 C  C   . THR A 1 252 ? 9.625   9.434   -60.319  1.00 94.85  ?  250 THR A C   1 
ATOM   1731 O  O   . THR A 1 252 ? 8.643   9.990   -60.825  1.00 90.99  ?  250 THR A O   1 
ATOM   1732 C  CB  . THR A 1 252 ? 11.585  10.747  -61.154  1.00 101.21 ?  250 THR A CB  1 
ATOM   1733 O  OG1 . THR A 1 252 ? 12.746  10.690  -61.993  1.00 105.71 ?  250 THR A OG1 1 
ATOM   1734 C  CG2 . THR A 1 252 ? 11.995  11.221  -59.768  1.00 102.03 ?  250 THR A CG2 1 
ATOM   1735 N  N   . GLY A 1 253 ? 9.605   8.874   -59.111  1.00 93.93  ?  251 GLY A N   1 
ATOM   1736 C  CA  . GLY A 1 253 ? 8.457   8.977   -58.240  1.00 95.65  ?  251 GLY A CA  1 
ATOM   1737 C  C   . GLY A 1 253 ? 7.385   7.934   -58.467  1.00 96.38  ?  251 GLY A C   1 
ATOM   1738 O  O   . GLY A 1 253 ? 6.446   7.850   -57.665  1.00 99.46  ?  251 GLY A O   1 
ATOM   1739 N  N   . LEU A 1 254 ? 7.491   7.137   -59.526  1.00 96.71  ?  252 LEU A N   1 
ATOM   1740 C  CA  . LEU A 1 254 ? 6.445   6.201   -59.902  1.00 95.11  ?  252 LEU A CA  1 
ATOM   1741 C  C   . LEU A 1 254 ? 7.037   4.810   -60.057  1.00 96.39  ?  252 LEU A C   1 
ATOM   1742 O  O   . LEU A 1 254 ? 8.236   4.642   -60.296  1.00 98.01  ?  252 LEU A O   1 
ATOM   1743 C  CB  . LEU A 1 254 ? 5.746   6.632   -61.197  1.00 93.65  ?  252 LEU A CB  1 
ATOM   1744 C  CG  . LEU A 1 254 ? 4.501   7.484   -60.954  1.00 90.97  ?  252 LEU A CG  1 
ATOM   1745 C  CD1 . LEU A 1 254 ? 3.719   6.916   -59.784  1.00 98.29  ?  252 LEU A CD1 1 
ATOM   1746 C  CD2 . LEU A 1 254 ? 4.886   8.930   -60.689  1.00 92.66  ?  252 LEU A CD2 1 
ATOM   1747 N  N   . TYR A 1 255 ? 6.175   3.808   -59.914  1.00 97.78  ?  253 TYR A N   1 
ATOM   1748 C  CA  . TYR A 1 255 ? 6.595   2.408   -59.932  1.00 95.85  ?  253 TYR A CA  1 
ATOM   1749 C  C   . TYR A 1 255 ? 5.870   1.660   -61.040  1.00 96.04  ?  253 TYR A C   1 
ATOM   1750 O  O   . TYR A 1 255 ? 4.706   1.254   -60.870  1.00 93.70  ?  253 TYR A O   1 
ATOM   1751 C  CB  . TYR A 1 255 ? 6.339   1.786   -58.562  1.00 100.89 ?  253 TYR A CB  1 
ATOM   1752 C  CG  . TYR A 1 255 ? 6.933   2.647   -57.466  1.00 102.89 ?  253 TYR A CG  1 
ATOM   1753 C  CD1 . TYR A 1 255 ? 8.268   2.522   -57.106  1.00 103.39 ?  253 TYR A CD1 1 
ATOM   1754 C  CD2 . TYR A 1 255 ? 6.175   3.628   -56.836  1.00 105.18 ?  253 TYR A CD2 1 
ATOM   1755 C  CE1 . TYR A 1 255 ? 8.824   3.320   -56.123  1.00 105.29 ?  253 TYR A CE1 1 
ATOM   1756 C  CE2 . TYR A 1 255 ? 6.723   4.434   -55.852  1.00 103.59 ?  253 TYR A CE2 1 
ATOM   1757 C  CZ  . TYR A 1 255 ? 8.048   4.275   -55.500  1.00 107.94 ?  253 TYR A CZ  1 
ATOM   1758 O  OH  . TYR A 1 255 ? 8.599   5.072   -54.522  1.00 115.19 ?  253 TYR A OH  1 
ATOM   1759 N  N   . PRO A 1 256 ? 6.515   1.463   -62.187  1.00 96.31  ?  254 PRO A N   1 
ATOM   1760 C  CA  . PRO A 1 256 ? 5.840   0.843   -63.332  1.00 95.60  ?  254 PRO A CA  1 
ATOM   1761 C  C   . PRO A 1 256 ? 5.483   -0.612  -63.090  1.00 100.34 ?  254 PRO A C   1 
ATOM   1762 O  O   . PRO A 1 256 ? 6.155   -1.332  -62.347  1.00 102.30 ?  254 PRO A O   1 
ATOM   1763 C  CB  . PRO A 1 256 ? 6.876   0.968   -64.457  1.00 96.24  ?  254 PRO A CB  1 
ATOM   1764 C  CG  . PRO A 1 256 ? 8.187   1.064   -63.736  1.00 98.45  ?  254 PRO A CG  1 
ATOM   1765 C  CD  . PRO A 1 256 ? 7.883   1.887   -62.525  1.00 98.37  ?  254 PRO A CD  1 
ATOM   1766 N  N   . THR A 1 257 ? 4.407   -1.041  -63.736  1.00 97.26  ?  255 THR A N   1 
ATOM   1767 C  CA  . THR A 1 257 ? 4.064   -2.450  -63.758  1.00 103.47 ?  255 THR A CA  1 
ATOM   1768 C  C   . THR A 1 257 ? 4.831   -3.131  -64.887  1.00 104.39 ?  255 THR A C   1 
ATOM   1769 O  O   . THR A 1 257 ? 5.448   -2.484  -65.736  1.00 103.37 ?  255 THR A O   1 
ATOM   1770 C  CB  . THR A 1 257 ? 2.559   -2.649  -63.943  1.00 99.69  ?  255 THR A CB  1 
ATOM   1771 O  OG1 . THR A 1 257 ? 2.254   -4.049  -63.919  1.00 101.53 ?  255 THR A OG1 1 
ATOM   1772 C  CG2 . THR A 1 257 ? 2.107   -2.071  -65.276  1.00 95.43  ?  255 THR A CG2 1 
ATOM   1773 N  N   . LEU A 1 258 ? 4.786   -4.458  -64.892  1.00 110.61 ?  256 LEU A N   1 
ATOM   1774 C  CA  . LEU A 1 258 ? 5.413   -5.244  -65.941  1.00 110.45 ?  256 LEU A CA  1 
ATOM   1775 C  C   . LEU A 1 258 ? 4.410   -6.162  -66.617  1.00 108.53 ?  256 LEU A C   1 
ATOM   1776 O  O   . LEU A 1 258 ? 4.770   -6.867  -67.567  1.00 111.95 ?  256 LEU A O   1 
ATOM   1777 C  CB  . LEU A 1 258 ? 6.582   -6.070  -65.382  1.00 111.71 ?  256 LEU A CB  1 
ATOM   1778 C  CG  . LEU A 1 258 ? 7.768   -5.322  -64.762  1.00 113.86 ?  256 LEU A CG  1 
ATOM   1779 C  CD1 . LEU A 1 258 ? 8.186   -4.136  -65.625  1.00 112.08 ?  256 LEU A CD1 1 
ATOM   1780 C  CD2 . LEU A 1 258 ? 7.471   -4.885  -63.332  1.00 112.65 ?  256 LEU A CD2 1 
ATOM   1781 N  N   . ASN A 1 259 ? 3.162   -6.166  -66.147  1.00 107.86 ?  257 ASN A N   1 
ATOM   1782 C  CA  . ASN A 1 259 ? 2.056   -6.905  -66.751  1.00 108.72 ?  257 ASN A CA  1 
ATOM   1783 C  C   . ASN A 1 259 ? 0.920   -5.921  -67.014  1.00 108.08 ?  257 ASN A C   1 
ATOM   1784 O  O   . ASN A 1 259 ? -0.061  -5.880  -66.269  1.00 110.16 ?  257 ASN A O   1 
ATOM   1785 C  CB  . ASN A 1 259 ? 1.611   -8.048  -65.851  1.00 111.02 ?  257 ASN A CB  1 
ATOM   1786 C  CG  . ASN A 1 259 ? 0.586   -8.941  -66.513  1.00 113.46 ?  257 ASN A CG  1 
ATOM   1787 O  OD1 . ASN A 1 259 ? 0.264   -8.768  -67.689  1.00 113.99 ?  257 ASN A OD1 1 
ATOM   1788 N  ND2 . ASN A 1 259 ? 0.054   -9.894  -65.757  1.00 115.10 ?  257 ASN A ND2 1 
ATOM   1789 N  N   . ILE A 1 260 ? 1.052   -5.122  -68.069  1.00 107.23 ?  258 ILE A N   1 
ATOM   1790 C  CA  . ILE A 1 260 ? -0.004  -4.204  -68.476  1.00 103.98 ?  258 ILE A CA  1 
ATOM   1791 C  C   . ILE A 1 260 ? -0.819  -4.880  -69.569  1.00 98.30  ?  258 ILE A C   1 
ATOM   1792 O  O   . ILE A 1 260 ? -0.257  -5.454  -70.511  1.00 98.35  ?  258 ILE A O   1 
ATOM   1793 C  CB  . ILE A 1 260 ? 0.563   -2.854  -68.949  1.00 98.82  ?  258 ILE A CB  1 
ATOM   1794 C  CG1 . ILE A 1 260 ? -0.562  -1.817  -69.032  1.00 93.73  ?  258 ILE A CG1 1 
ATOM   1795 C  CG2 . ILE A 1 260 ? 1.281   -3.001  -70.283  1.00 100.05 ?  258 ILE A CG2 1 
ATOM   1796 C  CD1 . ILE A 1 260 ? -0.114  -0.448  -69.494  1.00 93.72  ?  258 ILE A CD1 1 
ATOM   1797 N  N   . SER A 1 261 ? -2.141  -4.834  -69.426  1.00 100.68 ?  259 SER A N   1 
ATOM   1798 C  CA  . SER A 1 261 ? -3.044  -5.376  -70.432  1.00 97.81  ?  259 SER A CA  1 
ATOM   1799 C  C   . SER A 1 261 ? -2.633  -4.947  -71.835  1.00 95.71  ?  259 SER A C   1 
ATOM   1800 O  O   . SER A 1 261 ? -2.151  -3.830  -72.044  1.00 95.65  ?  259 SER A O   1 
ATOM   1801 C  CB  . SER A 1 261 ? -4.475  -4.919  -70.139  1.00 93.47  ?  259 SER A CB  1 
ATOM   1802 O  OG  . SER A 1 261 ? -5.338  -5.186  -71.230  1.00 93.53  ?  259 SER A OG  1 
ATOM   1803 N  N   . ASP A 1 262 ? -2.826  -5.848  -72.803  1.00 89.75  ?  260 ASP A N   1 
ATOM   1804 C  CA  . ASP A 1 262 ? -2.490  -5.518  -74.183  1.00 83.46  ?  260 ASP A CA  1 
ATOM   1805 C  C   . ASP A 1 262 ? -3.331  -4.358  -74.687  1.00 82.31  ?  260 ASP A C   1 
ATOM   1806 O  O   . ASP A 1 262 ? -2.924  -3.665  -75.625  1.00 81.68  ?  260 ASP A O   1 
ATOM   1807 C  CB  . ASP A 1 262 ? -2.681  -6.733  -75.092  1.00 83.55  ?  260 ASP A CB  1 
ATOM   1808 C  CG  . ASP A 1 262 ? -1.458  -7.627  -75.136  1.00 90.08  ?  260 ASP A CG  1 
ATOM   1809 O  OD1 . ASP A 1 262 ? -0.367  -7.124  -75.479  1.00 95.83  ?  260 ASP A OD1 1 
ATOM   1810 O  OD2 . ASP A 1 262 ? -1.589  -8.832  -74.835  1.00 90.75  -1 260 ASP A OD2 1 
ATOM   1811 N  N   . GLU A 1 263 ? -4.496  -4.137  -74.076  1.00 82.50  ?  261 GLU A N   1 
ATOM   1812 C  CA  . GLU A 1 263 ? -5.388  -3.070  -74.499  1.00 75.86  ?  261 GLU A CA  1 
ATOM   1813 C  C   . GLU A 1 263 ? -4.736  -1.710  -74.313  1.00 74.56  ?  261 GLU A C   1 
ATOM   1814 O  O   . GLU A 1 263 ? -5.168  -0.729  -74.930  1.00 74.98  ?  261 GLU A O   1 
ATOM   1815 C  CB  . GLU A 1 263 ? -6.692  -3.161  -73.708  1.00 75.03  ?  261 GLU A CB  1 
ATOM   1816 C  CG  . GLU A 1 263 ? -7.854  -2.383  -74.285  1.00 79.90  ?  261 GLU A CG  1 
ATOM   1817 C  CD  . GLU A 1 263 ? -9.128  -2.611  -73.496  1.00 81.78  ?  261 GLU A CD  1 
ATOM   1818 O  OE1 . GLU A 1 263 ? -9.092  -3.406  -72.531  1.00 75.36  ?  261 GLU A OE1 1 
ATOM   1819 O  OE2 . GLU A 1 263 ? -10.162 -2.000  -73.836  1.00 87.80  -1 261 GLU A OE2 1 
ATOM   1820 N  N   . PHE A 1 264 ? -3.705  -1.639  -73.472  1.00 80.05  ?  262 PHE A N   1 
ATOM   1821 C  CA  . PHE A 1 264 ? -3.025  -0.399  -73.129  1.00 78.78  ?  262 PHE A CA  1 
ATOM   1822 C  C   . PHE A 1 264 ? -1.548  -0.462  -73.495  1.00 78.12  ?  262 PHE A C   1 
ATOM   1823 O  O   . PHE A 1 264 ? -0.796  0.468   -73.177  1.00 75.91  ?  262 PHE A O   1 
ATOM   1824 C  CB  . PHE A 1 264 ? -3.186  -0.114  -71.632  1.00 74.76  ?  262 PHE A CB  1 
ATOM   1825 C  CG  . PHE A 1 264 ? -4.605  0.156   -71.215  1.00 75.03  ?  262 PHE A CG  1 
ATOM   1826 C  CD1 . PHE A 1 264 ? -5.153  1.423   -71.334  1.00 65.82  ?  262 PHE A CD1 1 
ATOM   1827 C  CD2 . PHE A 1 264 ? -5.396  -0.867  -70.713  1.00 75.25  ?  262 PHE A CD2 1 
ATOM   1828 C  CE1 . PHE A 1 264 ? -6.461  1.667   -70.950  1.00 65.54  ?  262 PHE A CE1 1 
ATOM   1829 C  CE2 . PHE A 1 264 ? -6.704  -0.631  -70.330  1.00 74.55  ?  262 PHE A CE2 1 
ATOM   1830 C  CZ  . PHE A 1 264 ? -7.237  0.638   -70.448  1.00 68.04  ?  262 PHE A CZ  1 
ATOM   1831 N  N   . SER A 1 265 ? -1.118  -1.535  -74.168  1.00 72.15  ?  263 SER A N   1 
ATOM   1832 C  CA  . SER A 1 265 ? 0.296   -1.729  -74.470  1.00 72.28  ?  263 SER A CA  1 
ATOM   1833 C  C   . SER A 1 265 ? 0.818   -0.683  -75.447  1.00 70.02  ?  263 SER A C   1 
ATOM   1834 O  O   . SER A 1 265 ? 2.018   -0.384  -75.449  1.00 75.97  ?  263 SER A O   1 
ATOM   1835 C  CB  . SER A 1 265 ? 0.531   -3.139  -75.017  1.00 79.34  ?  263 SER A CB  1 
ATOM   1836 O  OG  . SER A 1 265 ? -0.278  -3.400  -76.151  1.00 85.17  ?  263 SER A OG  1 
ATOM   1837 N  N   . SER A 1 266 ? -0.052  -0.128  -76.292  1.00 67.36  ?  264 SER A N   1 
ATOM   1838 C  CA  . SER A 1 266 ? 0.407   0.821   -77.297  1.00 72.94  ?  264 SER A CA  1 
ATOM   1839 C  C   . SER A 1 266 ? 0.870   2.132   -76.675  1.00 76.58  ?  264 SER A C   1 
ATOM   1840 O  O   . SER A 1 266 ? 1.601   2.888   -77.323  1.00 78.08  ?  264 SER A O   1 
ATOM   1841 C  CB  . SER A 1 266 ? -0.699  1.087   -78.321  1.00 70.29  ?  264 SER A CB  1 
ATOM   1842 O  OG  . SER A 1 266 ? -1.918  1.427   -77.684  1.00 78.12  ?  264 SER A OG  1 
ATOM   1843 N  N   . ASN A 1 267 ? 0.458   2.419   -75.441  1.00 73.53  ?  265 ASN A N   1 
ATOM   1844 C  CA  . ASN A 1 267 ? 0.761   3.683   -74.785  1.00 70.48  ?  265 ASN A CA  1 
ATOM   1845 C  C   . ASN A 1 267 ? 1.936   3.583   -73.819  1.00 69.61  ?  265 ASN A C   1 
ATOM   1846 O  O   . ASN A 1 267 ? 2.208   4.547   -73.097  1.00 76.79  ?  265 ASN A O   1 
ATOM   1847 C  CB  . ASN A 1 267 ? -0.471  4.206   -74.042  1.00 69.64  ?  265 ASN A CB  1 
ATOM   1848 C  CG  . ASN A 1 267 ? -1.595  4.608   -74.976  1.00 71.88  ?  265 ASN A CG  1 
ATOM   1849 O  OD1 . ASN A 1 267 ? -1.392  5.372   -75.921  1.00 68.02  ?  265 ASN A OD1 1 
ATOM   1850 N  ND2 . ASN A 1 267 ? -2.795  4.104   -74.709  1.00 70.89  ?  265 ASN A ND2 1 
ATOM   1851 N  N   . VAL A 1 268 ? 2.639   2.447   -73.782  1.00 70.42  ?  266 VAL A N   1 
ATOM   1852 C  CA  . VAL A 1 268 ? 3.685   2.275   -72.776  1.00 75.75  ?  266 VAL A CA  1 
ATOM   1853 C  C   . VAL A 1 268 ? 4.822   3.259   -73.017  1.00 77.54  ?  266 VAL A C   1 
ATOM   1854 O  O   . VAL A 1 268 ? 5.343   3.866   -72.073  1.00 77.23  ?  266 VAL A O   1 
ATOM   1855 C  CB  . VAL A 1 268 ? 4.185   0.818   -72.739  1.00 78.96  ?  266 VAL A CB  1 
ATOM   1856 C  CG1 . VAL A 1 268 ? 3.066   -0.114  -72.296  1.00 84.36  ?  266 VAL A CG1 1 
ATOM   1857 C  CG2 . VAL A 1 268 ? 4.745   0.400   -74.089  1.00 83.94  ?  266 VAL A CG2 1 
ATOM   1858 N  N   . ALA A 1 269 ? 5.242   3.424   -74.275  1.00 76.99  ?  267 ALA A N   1 
ATOM   1859 C  CA  . ALA A 1 269 ? 6.339   4.344   -74.548  1.00 77.04  ?  267 ALA A CA  1 
ATOM   1860 C  C   . ALA A 1 269 ? 5.954   5.766   -74.167  1.00 80.26  ?  267 ALA A C   1 
ATOM   1861 O  O   . ALA A 1 269 ? 6.806   6.550   -73.732  1.00 85.40  ?  267 ALA A O   1 
ATOM   1862 C  CB  . ALA A 1 269 ? 6.745   4.269   -76.019  1.00 72.78  ?  267 ALA A CB  1 
ATOM   1863 N  N   . ASN A 1 270 ? 4.671   6.109   -74.307  1.00 76.19  ?  268 ASN A N   1 
ATOM   1864 C  CA  . ASN A 1 270 ? 4.186   7.409   -73.858  1.00 77.61  ?  268 ASN A CA  1 
ATOM   1865 C  C   . ASN A 1 270 ? 4.037   7.427   -72.342  1.00 77.52  ?  268 ASN A C   1 
ATOM   1866 O  O   . ASN A 1 270 ? 4.301   8.449   -71.699  1.00 75.57  ?  268 ASN A O   1 
ATOM   1867 C  CB  . ASN A 1 270 ? 2.858   7.742   -74.538  1.00 74.36  ?  268 ASN A CB  1 
ATOM   1868 C  CG  . ASN A 1 270 ? 3.028   8.125   -75.997  1.00 71.76  ?  268 ASN A CG  1 
ATOM   1869 O  OD1 . ASN A 1 270 ? 4.145   8.334   -76.471  1.00 76.21  ?  268 ASN A OD1 1 
ATOM   1870 N  ND2 . ASN A 1 270 ? 1.917   8.204   -76.720  1.00 67.69  ?  268 ASN A ND2 1 
ATOM   1871 N  N   . TYR A 1 271 ? 3.607   6.303   -71.759  1.00 74.91  ?  269 TYR A N   1 
ATOM   1872 C  CA  . TYR A 1 271 ? 3.438   6.234   -70.314  1.00 74.85  ?  269 TYR A CA  1 
ATOM   1873 C  C   . TYR A 1 271 ? 4.772   6.393   -69.603  1.00 85.14  ?  269 TYR A C   1 
ATOM   1874 O  O   . TYR A 1 271 ? 4.801   6.743   -68.417  1.00 91.10  ?  269 TYR A O   1 
ATOM   1875 C  CB  . TYR A 1 271 ? 2.794   4.906   -69.913  1.00 73.41  ?  269 TYR A CB  1 
ATOM   1876 C  CG  . TYR A 1 271 ? 1.314   4.813   -70.204  1.00 72.67  ?  269 TYR A CG  1 
ATOM   1877 C  CD1 . TYR A 1 271 ? 0.527   5.954   -70.276  1.00 70.55  ?  269 TYR A CD1 1 
ATOM   1878 C  CD2 . TYR A 1 271 ? 0.703   3.582   -70.402  1.00 70.70  ?  269 TYR A CD2 1 
ATOM   1879 C  CE1 . TYR A 1 271 ? -0.828  5.871   -70.538  1.00 70.47  ?  269 TYR A CE1 1 
ATOM   1880 C  CE2 . TYR A 1 271 ? -0.650  3.489   -70.667  1.00 69.41  ?  269 TYR A CE2 1 
ATOM   1881 C  CZ  . TYR A 1 271 ? -1.411  4.636   -70.732  1.00 70.33  ?  269 TYR A CZ  1 
ATOM   1882 O  OH  . TYR A 1 271 ? -2.758  4.550   -71.000  1.00 73.56  ?  269 TYR A OH  1 
ATOM   1883 N  N   . GLN A 1 272 ? 5.876   6.146   -70.312  1.00 83.92  ?  270 GLN A N   1 
ATOM   1884 C  CA  . GLN A 1 272 ? 7.206   6.278   -69.735  1.00 83.91  ?  270 GLN A CA  1 
ATOM   1885 C  C   . GLN A 1 272 ? 7.659   7.729   -69.786  1.00 83.37  ?  270 GLN A C   1 
ATOM   1886 O  O   . GLN A 1 272 ? 8.271   8.229   -68.836  1.00 85.70  ?  270 GLN A O   1 
ATOM   1887 C  CB  . GLN A 1 272 ? 8.186   5.373   -70.482  1.00 86.27  ?  270 GLN A CB  1 
ATOM   1888 C  CG  . GLN A 1 272 ? 8.010   3.893   -70.182  1.00 82.67  ?  270 GLN A CG  1 
ATOM   1889 C  CD  . GLN A 1 272 ? 8.840   3.011   -71.094  1.00 88.05  ?  270 GLN A CD  1 
ATOM   1890 O  OE1 . GLN A 1 272 ? 9.532   3.499   -71.988  1.00 91.90  ?  270 GLN A OE1 1 
ATOM   1891 N  NE2 . GLN A 1 272 ? 8.774   1.703   -70.874  1.00 85.85  ?  270 GLN A NE2 1 
ATOM   1892 N  N   . LYS A 1 273 ? 7.374   8.409   -70.899  1.00 79.54  ?  271 LYS A N   1 
ATOM   1893 C  CA  . LYS A 1 273 ? 7.751   9.811   -71.034  1.00 80.13  ?  271 LYS A CA  1 
ATOM   1894 C  C   . LYS A 1 273 ? 7.105   10.639  -69.932  1.00 81.00  ?  271 LYS A C   1 
ATOM   1895 O  O   . LYS A 1 273 ? 7.713   11.581  -69.409  1.00 85.17  ?  271 LYS A O   1 
ATOM   1896 C  CB  . LYS A 1 273 ? 7.333   10.327  -72.410  1.00 74.72  ?  271 LYS A CB  1 
ATOM   1897 C  CG  . LYS A 1 273 ? 8.059   11.573  -72.883  1.00 84.40  ?  271 LYS A CG  1 
ATOM   1898 C  CD  . LYS A 1 273 ? 7.676   11.889  -74.322  1.00 77.56  ?  271 LYS A CD  1 
ATOM   1899 C  CE  . LYS A 1 273 ? 8.705   12.772  -75.006  1.00 84.16  ?  271 LYS A CE  1 
ATOM   1900 N  NZ  . LYS A 1 273 ? 8.453   12.859  -76.473  1.00 77.87  ?  271 LYS A NZ  1 
ATOM   1901 N  N   . VAL A 1 274 ? 5.866   10.295  -69.572  1.00 78.55  ?  272 VAL A N   1 
ATOM   1902 C  CA  . VAL A 1 274 ? 5.162   10.983  -68.494  1.00 76.46  ?  272 VAL A CA  1 
ATOM   1903 C  C   . VAL A 1 274 ? 5.979   10.934  -67.209  1.00 83.19  ?  272 VAL A C   1 
ATOM   1904 O  O   . VAL A 1 274 ? 6.004   11.897  -66.432  1.00 76.31  ?  272 VAL A O   1 
ATOM   1905 C  CB  . VAL A 1 274 ? 3.764   10.368  -68.300  1.00 70.92  ?  272 VAL A CB  1 
ATOM   1906 C  CG1 . VAL A 1 274 ? 3.172   10.790  -66.963  1.00 72.28  ?  272 VAL A CG1 1 
ATOM   1907 C  CG2 . VAL A 1 274 ? 2.848   10.752  -69.450  1.00 72.56  ?  272 VAL A CG2 1 
ATOM   1908 N  N   . GLY A 1 275 ? 6.665   9.813   -66.967  1.00 81.67  ?  273 GLY A N   1 
ATOM   1909 C  CA  . GLY A 1 275 ? 7.424   9.651   -65.740  1.00 81.64  ?  273 GLY A CA  1 
ATOM   1910 C  C   . GLY A 1 275 ? 8.805   10.262  -65.782  1.00 84.93  ?  273 GLY A C   1 
ATOM   1911 O  O   . GLY A 1 275 ? 9.413   10.468  -64.727  1.00 92.12  ?  273 GLY A O   1 
ATOM   1912 N  N   . MET A 1 276 ? 9.309   10.565  -66.977  1.00 83.81  ?  274 MET A N   1 
ATOM   1913 C  CA  . MET A 1 276 ? 10.641  11.123  -67.156  1.00 91.02  ?  274 MET A CA  1 
ATOM   1914 C  C   . MET A 1 276 ? 10.595  12.630  -67.382  1.00 95.37  ?  274 MET A C   1 
ATOM   1915 O  O   . MET A 1 276 ? 11.563  13.210  -67.885  1.00 96.72  ?  274 MET A O   1 
ATOM   1916 C  CB  . MET A 1 276 ? 11.343  10.433  -68.326  1.00 90.37  ?  274 MET A CB  1 
ATOM   1917 C  CG  . MET A 1 276 ? 11.485  8.926   -68.171  1.00 94.79  ?  274 MET A CG  1 
ATOM   1918 S  SD  . MET A 1 276 ? 12.962  8.278   -68.975  1.00 105.55 ?  274 MET A SD  1 
ATOM   1919 C  CE  . MET A 1 276 ? 12.856  9.079   -70.574  1.00 94.92  ?  274 MET A CE  1 
ATOM   1920 N  N   . GLN A 1 277 ? 9.489   13.271  -67.004  1.00 90.21  ?  275 GLN A N   1 
ATOM   1921 C  CA  . GLN A 1 277 ? 9.279   14.697  -67.208  1.00 88.96  ?  275 GLN A CA  1 
ATOM   1922 C  C   . GLN A 1 277 ? 8.354   15.221  -66.119  1.00 89.84  ?  275 GLN A C   1 
ATOM   1923 O  O   . GLN A 1 277 ? 7.556   14.471  -65.551  1.00 89.89  ?  275 GLN A O   1 
ATOM   1924 C  CB  . GLN A 1 277 ? 8.673   14.984  -68.587  1.00 88.70  ?  275 GLN A CB  1 
ATOM   1925 C  CG  . GLN A 1 277 ? 9.622   14.786  -69.754  1.00 89.94  ?  275 GLN A CG  1 
ATOM   1926 C  CD  . GLN A 1 277 ? 9.010   15.221  -71.071  1.00 88.43  ?  275 GLN A CD  1 
ATOM   1927 O  OE1 . GLN A 1 277 ? 7.896   15.744  -71.108  1.00 90.71  ?  275 GLN A OE1 1 
ATOM   1928 N  NE2 . GLN A 1 277 ? 9.735   15.004  -72.162  1.00 91.38  ?  275 GLN A NE2 1 
ATOM   1929 N  N   . LYS A 1 278 ? 8.464   16.522  -65.836  1.00 88.59  ?  276 LYS A N   1 
ATOM   1930 C  CA  . LYS A 1 278 ? 7.607   17.128  -64.821  1.00 84.47  ?  276 LYS A CA  1 
ATOM   1931 C  C   . LYS A 1 278 ? 6.175   17.255  -65.331  1.00 80.00  ?  276 LYS A C   1 
ATOM   1932 O  O   . LYS A 1 278 ? 5.231   16.800  -64.675  1.00 82.43  ?  276 LYS A O   1 
ATOM   1933 C  CB  . LYS A 1 278 ? 8.169   18.494  -64.421  1.00 89.11  ?  276 LYS A CB  1 
ATOM   1934 C  CG  . LYS A 1 278 ? 7.416   19.234  -63.315  1.00 88.59  ?  276 LYS A CG  1 
ATOM   1935 C  CD  . LYS A 1 278 ? 7.417   18.487  -61.986  1.00 87.37  ?  276 LYS A CD  1 
ATOM   1936 C  CE  . LYS A 1 278 ? 6.996   19.418  -60.850  1.00 92.24  ?  276 LYS A CE  1 
ATOM   1937 N  NZ  . LYS A 1 278 ? 6.740   18.706  -59.566  1.00 96.98  ?  276 LYS A NZ  1 
ATOM   1938 N  N   . TYR A 1 279 ? 5.991   17.870  -66.501  1.00 73.28  ?  277 TYR A N   1 
ATOM   1939 C  CA  . TYR A 1 279 ? 4.685   17.948  -67.141  1.00 71.30  ?  277 TYR A CA  1 
ATOM   1940 C  C   . TYR A 1 279 ? 4.805   17.441  -68.573  1.00 72.38  ?  277 TYR A C   1 
ATOM   1941 O  O   . TYR A 1 279 ? 5.890   17.446  -69.161  1.00 78.98  ?  277 TYR A O   1 
ATOM   1942 C  CB  . TYR A 1 279 ? 4.106   19.376  -67.130  1.00 66.68  ?  277 TYR A CB  1 
ATOM   1943 C  CG  . TYR A 1 279 ? 4.867   20.402  -67.948  1.00 70.86  ?  277 TYR A CG  1 
ATOM   1944 C  CD1 . TYR A 1 279 ? 4.662   20.513  -69.318  1.00 71.64  ?  277 TYR A CD1 1 
ATOM   1945 C  CD2 . TYR A 1 279 ? 5.758   21.285  -67.347  1.00 80.61  ?  277 TYR A CD2 1 
ATOM   1946 C  CE1 . TYR A 1 279 ? 5.342   21.452  -70.072  1.00 76.85  ?  277 TYR A CE1 1 
ATOM   1947 C  CE2 . TYR A 1 279 ? 6.441   22.232  -68.096  1.00 79.66  ?  277 TYR A CE2 1 
ATOM   1948 C  CZ  . TYR A 1 279 ? 6.228   22.309  -69.458  1.00 82.02  ?  277 TYR A CZ  1 
ATOM   1949 O  OH  . TYR A 1 279 ? 6.900   23.247  -70.210  1.00 84.41  ?  277 TYR A OH  1 
ATOM   1950 N  N   . SER A 1 280 ? 3.685   16.966  -69.122  1.00 69.30  ?  278 SER A N   1 
ATOM   1951 C  CA  . SER A 1 280 ? 3.660   16.404  -70.468  1.00 70.08  ?  278 SER A CA  1 
ATOM   1952 C  C   . SER A 1 280 ? 2.408   16.858  -71.217  1.00 62.22  ?  278 SER A C   1 
ATOM   1953 O  O   . SER A 1 280 ? 1.344   17.031  -70.618  1.00 63.62  ?  278 SER A O   1 
ATOM   1954 C  CB  . SER A 1 280 ? 3.744   14.874  -70.394  1.00 68.82  ?  278 SER A CB  1 
ATOM   1955 O  OG  . SER A 1 280 ? 2.853   14.373  -69.411  1.00 73.09  ?  278 SER A OG  1 
ATOM   1956 N  N   . THR A 1 281 ? 2.540   17.047  -72.535  1.00 60.84  ?  279 THR A N   1 
ATOM   1957 C  CA  . THR A 1 281 ? 1.448   17.513  -73.392  1.00 65.03  ?  279 THR A CA  1 
ATOM   1958 C  C   . THR A 1 281 ? 1.020   16.428  -74.380  1.00 63.07  ?  279 THR A C   1 
ATOM   1959 O  O   . THR A 1 281 ? 1.856   15.901  -75.121  1.00 61.52  ?  279 THR A O   1 
ATOM   1960 C  CB  . THR A 1 281 ? 1.874   18.763  -74.165  1.00 58.12  ?  279 THR A CB  1 
ATOM   1961 O  OG1 . THR A 1 281 ? 3.039   18.462  -74.943  1.00 72.40  ?  279 THR A OG1 1 
ATOM   1962 C  CG2 . THR A 1 281 ? 2.197   19.904  -73.207  1.00 63.48  ?  279 THR A CG2 1 
ATOM   1963 N  N   . LEU A 1 282 ? -0.280  16.113  -74.416  1.00 54.79  ?  280 LEU A N   1 
ATOM   1964 C  CA  . LEU A 1 282 ? -0.828  15.135  -75.362  1.00 57.52  ?  280 LEU A CA  1 
ATOM   1965 C  C   . LEU A 1 282 ? -1.893  15.744  -76.277  1.00 54.94  ?  280 LEU A C   1 
ATOM   1966 O  O   . LEU A 1 282 ? -2.964  16.135  -75.800  1.00 50.18  ?  280 LEU A O   1 
ATOM   1967 C  CB  . LEU A 1 282 ? -1.407  13.939  -74.606  1.00 56.12  ?  280 LEU A CB  1 
ATOM   1968 C  CG  . LEU A 1 282 ? -2.207  12.914  -75.416  1.00 59.62  ?  280 LEU A CG  1 
ATOM   1969 C  CD1 . LEU A 1 282 ? -1.315  12.260  -76.457  1.00 63.75  ?  280 LEU A CD1 1 
ATOM   1970 C  CD2 . LEU A 1 282 ? -2.836  11.866  -74.509  1.00 60.49  ?  280 LEU A CD2 1 
ATOM   1971 N  N   . GLN A 1 283 ? -1.622  15.833  -77.583  1.00 53.48  ?  281 GLN A N   1 
ATOM   1972 C  CA  . GLN A 1 283 ? -2.648  16.271  -78.528  1.00 52.52  ?  281 GLN A CA  1 
ATOM   1973 C  C   . GLN A 1 283 ? -3.449  15.043  -78.941  1.00 48.36  ?  281 GLN A C   1 
ATOM   1974 O  O   . GLN A 1 283 ? -2.900  14.119  -79.550  1.00 51.03  ?  281 GLN A O   1 
ATOM   1975 C  CB  . GLN A 1 283 ? -2.093  16.948  -79.782  1.00 51.09  ?  281 GLN A CB  1 
ATOM   1976 C  CG  . GLN A 1 283 ? -3.229  17.487  -80.681  1.00 46.13  ?  281 GLN A CG  1 
ATOM   1977 C  CD  . GLN A 1 283 ? -2.748  18.406  -81.787  1.00 51.37  ?  281 GLN A CD  1 
ATOM   1978 O  OE1 . GLN A 1 283 ? -1.556  18.682  -81.901  1.00 47.17  ?  281 GLN A OE1 1 
ATOM   1979 N  NE2 . GLN A 1 283 ? -3.681  18.892  -82.606  1.00 47.85  ?  281 GLN A NE2 1 
ATOM   1980 N  N   . GLY A 1 284 ? -4.734  15.031  -78.605  1.00 50.42  ?  282 GLY A N   1 
ATOM   1981 C  CA  . GLY A 1 284 ? -5.600  13.915  -78.904  1.00 44.79  ?  282 GLY A CA  1 
ATOM   1982 C  C   . GLY A 1 284 ? -6.784  14.313  -79.763  1.00 43.35  ?  282 GLY A C   1 
ATOM   1983 O  O   . GLY A 1 284 ? -7.836  14.704  -79.249  1.00 43.11  ?  282 GLY A O   1 
ATOM   1984 N  N   . PRO A 1 285 ? -6.639  14.233  -81.084  1.00 41.43  ?  283 PRO A N   1 
ATOM   1985 C  CA  . PRO A 1 285 ? -7.782  14.471  -81.980  1.00 42.04  ?  283 PRO A CA  1 
ATOM   1986 C  C   . PRO A 1 285 ? -8.972  13.602  -81.613  1.00 39.73  ?  283 PRO A C   1 
ATOM   1987 O  O   . PRO A 1 285 ? -8.830  12.612  -80.879  1.00 40.75  ?  283 PRO A O   1 
ATOM   1988 C  CB  . PRO A 1 285 ? -7.219  14.098  -83.359  1.00 39.44  ?  283 PRO A CB  1 
ATOM   1989 C  CG  . PRO A 1 285 ? -5.769  14.449  -83.234  1.00 42.85  ?  283 PRO A CG  1 
ATOM   1990 C  CD  . PRO A 1 285 ? -5.412  13.950  -81.849  1.00 45.25  ?  283 PRO A CD  1 
ATOM   1991 N  N   . PRO A 1 286 ? -10.164 13.941  -82.110  1.00 38.13  ?  284 PRO A N   1 
ATOM   1992 C  CA  . PRO A 1 286 ? -11.370 13.186  -81.743  1.00 40.68  ?  284 PRO A CA  1 
ATOM   1993 C  C   . PRO A 1 286 ? -11.259 11.696  -82.039  1.00 41.29  ?  284 PRO A C   1 
ATOM   1994 O  O   . PRO A 1 286 ? -10.767 11.282  -83.091  1.00 39.06  ?  284 PRO A O   1 
ATOM   1995 C  CB  . PRO A 1 286 ? -12.460 13.846  -82.596  1.00 38.01  ?  284 PRO A CB  1 
ATOM   1996 C  CG  . PRO A 1 286 ? -11.952 15.248  -82.774  1.00 36.79  ?  284 PRO A CG  1 
ATOM   1997 C  CD  . PRO A 1 286 ? -10.489 15.030  -83.046  1.00 37.18  ?  284 PRO A CD  1 
ATOM   1998 N  N   . GLY A 1 287 ? -11.706 10.891  -81.076  1.00 43.28  ?  285 GLY A N   1 
ATOM   1999 C  CA  . GLY A 1 287 ? -11.774 9.453   -81.241  1.00 42.41  ?  285 GLY A CA  1 
ATOM   2000 C  C   . GLY A 1 287 ? -10.445 8.740   -81.259  1.00 43.74  ?  285 GLY A C   1 
ATOM   2001 O  O   . GLY A 1 287 ? -10.380 7.588   -81.694  1.00 43.36  ?  285 GLY A O   1 
ATOM   2002 N  N   . THR A 1 288 ? -9.380  9.390   -80.795  1.00 42.64  ?  286 THR A N   1 
ATOM   2003 C  CA  . THR A 1 288 ? -8.041  8.819   -80.831  1.00 43.83  ?  286 THR A CA  1 
ATOM   2004 C  C   . THR A 1 288 ? -7.669  8.098   -79.544  1.00 46.44  ?  286 THR A C   1 
ATOM   2005 O  O   . THR A 1 288 ? -6.590  7.500   -79.477  1.00 49.84  ?  286 THR A O   1 
ATOM   2006 C  CB  . THR A 1 288 ? -7.005  9.907   -81.125  1.00 44.28  ?  286 THR A CB  1 
ATOM   2007 O  OG1 . THR A 1 288 ? -7.161  10.979  -80.188  1.00 43.44  ?  286 THR A OG1 1 
ATOM   2008 C  CG2 . THR A 1 288 ? -7.178  10.438  -82.541  1.00 41.79  ?  286 THR A CG2 1 
ATOM   2009 N  N   . GLY A 1 289 ? -8.523  8.153   -78.524  1.00 49.55  ?  287 GLY A N   1 
ATOM   2010 C  CA  . GLY A 1 289 ? -8.301  7.428   -77.289  1.00 49.00  ?  287 GLY A CA  1 
ATOM   2011 C  C   . GLY A 1 289 ? -7.649  8.225   -76.177  1.00 51.71  ?  287 GLY A C   1 
ATOM   2012 O  O   . GLY A 1 289 ? -6.678  7.765   -75.568  1.00 56.52  ?  287 GLY A O   1 
ATOM   2013 N  N   . LYS A 1 290 ? -8.180  9.417   -75.892  1.00 49.12  ?  288 LYS A N   1 
ATOM   2014 C  CA  . LYS A 1 290 ? -7.625  10.229  -74.812  1.00 53.28  ?  288 LYS A CA  1 
ATOM   2015 C  C   . LYS A 1 290 ? -7.993  9.641   -73.456  1.00 54.66  ?  288 LYS A C   1 
ATOM   2016 O  O   . LYS A 1 290 ? -7.121  9.401   -72.613  1.00 55.01  ?  288 LYS A O   1 
ATOM   2017 C  CB  . LYS A 1 290 ? -8.114  11.674  -74.922  1.00 48.88  ?  288 LYS A CB  1 
ATOM   2018 C  CG  . LYS A 1 290 ? -7.559  12.448  -76.106  1.00 47.91  ?  288 LYS A CG  1 
ATOM   2019 C  CD  . LYS A 1 290 ? -8.103  13.872  -76.138  1.00 45.45  ?  288 LYS A CD  1 
ATOM   2020 C  CE  . LYS A 1 290 ? -9.570  13.907  -76.532  1.00 44.80  ?  288 LYS A CE  1 
ATOM   2021 N  NZ  . LYS A 1 290 ? -9.771  13.491  -77.947  1.00 43.24  ?  288 LYS A NZ  1 
ATOM   2022 N  N   . SER A 1 291 ? -9.289  9.411   -73.226  1.00 56.45  ?  289 SER A N   1 
ATOM   2023 C  CA  . SER A 1 291 ? -9.721  8.810   -71.969  1.00 56.15  ?  289 SER A CA  1 
ATOM   2024 C  C   . SER A 1 291 ? -9.034  7.470   -71.757  1.00 63.41  ?  289 SER A C   1 
ATOM   2025 O  O   . SER A 1 291 ? -8.665  7.118   -70.631  1.00 61.54  ?  289 SER A O   1 
ATOM   2026 C  CB  . SER A 1 291 ? -11.240 8.648   -71.960  1.00 64.92  ?  289 SER A CB  1 
ATOM   2027 O  OG  . SER A 1 291 ? -11.883 9.893   -72.171  1.00 75.96  ?  289 SER A OG  1 
ATOM   2028 N  N   . HIS A 1 292 ? -8.844  6.715   -72.841  1.00 59.40  ?  290 HIS A N   1 
ATOM   2029 C  CA  . HIS A 1 292 ? -8.167  5.428   -72.747  1.00 55.28  ?  290 HIS A CA  1 
ATOM   2030 C  C   . HIS A 1 292 ? -6.734  5.619   -72.275  1.00 59.40  ?  290 HIS A C   1 
ATOM   2031 O  O   . HIS A 1 292 ? -6.241  4.862   -71.431  1.00 66.86  ?  290 HIS A O   1 
ATOM   2032 C  CB  . HIS A 1 292 ? -8.204  4.731   -74.107  1.00 60.81  ?  290 HIS A CB  1 
ATOM   2033 C  CG  . HIS A 1 292 ? -7.951  3.258   -74.046  1.00 62.08  ?  290 HIS A CG  1 
ATOM   2034 N  ND1 . HIS A 1 292 ? -8.947  2.342   -73.789  1.00 65.47  ?  290 HIS A ND1 1 
ATOM   2035 C  CD2 . HIS A 1 292 ? -6.817  2.541   -74.227  1.00 62.83  ?  290 HIS A CD2 1 
ATOM   2036 C  CE1 . HIS A 1 292 ? -8.437  1.124   -73.806  1.00 71.16  ?  290 HIS A CE1 1 
ATOM   2037 N  NE2 . HIS A 1 292 ? -7.146  1.217   -74.069  1.00 71.83  ?  290 HIS A NE2 1 
ATOM   2038 N  N   . PHE A 1 293 ? -6.052  6.634   -72.809  1.00 58.69  ?  291 PHE A N   1 
ATOM   2039 C  CA  . PHE A 1 293 ? -4.702  6.941   -72.353  1.00 67.60  ?  291 PHE A CA  1 
ATOM   2040 C  C   . PHE A 1 293 ? -4.708  7.345   -70.884  1.00 60.40  ?  291 PHE A C   1 
ATOM   2041 O  O   . PHE A 1 293 ? -3.785  7.009   -70.134  1.00 59.86  ?  291 PHE A O   1 
ATOM   2042 C  CB  . PHE A 1 293 ? -4.111  8.055   -73.220  1.00 60.53  ?  291 PHE A CB  1 
ATOM   2043 C  CG  . PHE A 1 293 ? -2.744  8.509   -72.794  1.00 61.68  ?  291 PHE A CG  1 
ATOM   2044 C  CD1 . PHE A 1 293 ? -2.586  9.422   -71.763  1.00 60.82  ?  291 PHE A CD1 1 
ATOM   2045 C  CD2 . PHE A 1 293 ? -1.617  8.050   -73.451  1.00 64.74  ?  291 PHE A CD2 1 
ATOM   2046 C  CE1 . PHE A 1 293 ? -1.327  9.846   -71.380  1.00 66.60  ?  291 PHE A CE1 1 
ATOM   2047 C  CE2 . PHE A 1 293 ? -0.356  8.474   -73.075  1.00 70.66  ?  291 PHE A CE2 1 
ATOM   2048 C  CZ  . PHE A 1 293 ? -0.211  9.372   -72.038  1.00 65.86  ?  291 PHE A CZ  1 
ATOM   2049 N  N   . ALA A 1 294 ? -5.748  8.064   -70.455  1.00 59.04  ?  292 ALA A N   1 
ATOM   2050 C  CA  . ALA A 1 294 ? -5.776  8.589   -69.094  1.00 63.28  ?  292 ALA A CA  1 
ATOM   2051 C  C   . ALA A 1 294 ? -5.929  7.464   -68.079  1.00 63.50  ?  292 ALA A C   1 
ATOM   2052 O  O   . ALA A 1 294 ? -5.122  7.335   -67.151  1.00 64.06  ?  292 ALA A O   1 
ATOM   2053 C  CB  . ALA A 1 294 ? -6.905  9.609   -68.947  1.00 62.32  ?  292 ALA A CB  1 
ATOM   2054 N  N   . ILE A 1 295 ? -6.967  6.639   -68.239  1.00 62.60  ?  293 ILE A N   1 
ATOM   2055 C  CA  . ILE A 1 295 ? -7.196  5.550   -67.298  1.00 73.15  ?  293 ILE A CA  1 
ATOM   2056 C  C   . ILE A 1 295 ? -6.079  4.521   -67.396  1.00 67.86  ?  293 ILE A C   1 
ATOM   2057 O  O   . ILE A 1 295 ? -5.753  3.851   -66.409  1.00 68.49  ?  293 ILE A O   1 
ATOM   2058 C  CB  . ILE A 1 295 ? -8.581  4.923   -67.543  1.00 72.65  ?  293 ILE A CB  1 
ATOM   2059 C  CG1 . ILE A 1 295 ? -9.668  5.992   -67.406  1.00 71.12  ?  293 ILE A CG1 1 
ATOM   2060 C  CG2 . ILE A 1 295 ? -8.827  3.765   -66.589  1.00 71.62  ?  293 ILE A CG2 1 
ATOM   2061 C  CD1 . ILE A 1 295 ? -9.488  6.897   -66.202  1.00 73.71  ?  293 ILE A CD1 1 
ATOM   2062 N  N   . GLY A 1 296 ? -5.462  4.388   -68.572  1.00 66.25  ?  294 GLY A N   1 
ATOM   2063 C  CA  . GLY A 1 296 ? -4.395  3.417   -68.731  1.00 65.92  ?  294 GLY A CA  1 
ATOM   2064 C  C   . GLY A 1 296 ? -3.146  3.825   -67.982  1.00 65.69  ?  294 GLY A C   1 
ATOM   2065 O  O   . GLY A 1 296 ? -2.330  2.975   -67.615  1.00 72.48  ?  294 GLY A O   1 
ATOM   2066 N  N   . LEU A 1 297 ? -2.976  5.129   -67.751  1.00 70.08  ?  295 LEU A N   1 
ATOM   2067 C  CA  . LEU A 1 297 ? -1.819  5.609   -67.010  1.00 66.22  ?  295 LEU A CA  1 
ATOM   2068 C  C   . LEU A 1 297 ? -1.834  5.060   -65.590  1.00 72.16  ?  295 LEU A C   1 
ATOM   2069 O  O   . LEU A 1 297 ? -0.773  4.813   -65.003  1.00 71.63  ?  295 LEU A O   1 
ATOM   2070 C  CB  . LEU A 1 297 ? -1.819  7.139   -67.016  1.00 67.27  ?  295 LEU A CB  1 
ATOM   2071 C  CG  . LEU A 1 297 ? -0.615  7.956   -66.551  1.00 76.98  ?  295 LEU A CG  1 
ATOM   2072 C  CD1 . LEU A 1 297 ? 0.601   7.674   -67.418  1.00 69.26  ?  295 LEU A CD1 1 
ATOM   2073 C  CD2 . LEU A 1 297 ? -0.969  9.436   -66.586  1.00 74.31  ?  295 LEU A CD2 1 
ATOM   2074 N  N   . ALA A 1 298 ? -3.031  4.851   -65.032  1.00 75.88  ?  296 ALA A N   1 
ATOM   2075 C  CA  . ALA A 1 298 ? -3.157  4.299   -63.688  1.00 74.47  ?  296 ALA A CA  1 
ATOM   2076 C  C   . ALA A 1 298 ? -2.849  2.809   -63.679  1.00 81.06  ?  296 ALA A C   1 
ATOM   2077 O  O   . ALA A 1 298 ? -2.307  2.290   -62.696  1.00 78.88  ?  296 ALA A O   1 
ATOM   2078 C  CB  . ALA A 1 298 ? -4.559  4.557   -63.137  1.00 72.53  ?  296 ALA A CB  1 
ATOM   2079 N  N   . LEU A 1 299 ? -3.198  2.105   -64.759  1.00 77.73  ?  297 LEU A N   1 
ATOM   2080 C  CA  . LEU A 1 299 ? -2.933  0.675   -64.824  1.00 77.78  ?  297 LEU A CA  1 
ATOM   2081 C  C   . LEU A 1 299 ? -1.444  0.411   -64.981  1.00 81.12  ?  297 LEU A C   1 
ATOM   2082 O  O   . LEU A 1 299 ? -0.956  -0.656  -64.592  1.00 87.09  ?  297 LEU A O   1 
ATOM   2083 C  CB  . LEU A 1 299 ? -3.717  0.051   -65.977  1.00 79.00  ?  297 LEU A CB  1 
ATOM   2084 C  CG  . LEU A 1 299 ? -5.236  0.038   -65.797  1.00 82.97  ?  297 LEU A CG  1 
ATOM   2085 C  CD1 . LEU A 1 299 ? -5.914  -0.702  -66.936  1.00 75.26  ?  297 LEU A CD1 1 
ATOM   2086 C  CD2 . LEU A 1 299 ? -5.602  -0.585  -64.459  1.00 76.67  ?  297 LEU A CD2 1 
ATOM   2087 N  N   . TYR A 1 300 ? -0.710  1.377   -65.535  1.00 81.76  ?  298 TYR A N   1 
ATOM   2088 C  CA  . TYR A 1 300 ? 0.736   1.253   -65.652  1.00 84.42  ?  298 TYR A CA  1 
ATOM   2089 C  C   . TYR A 1 300 ? 1.425   1.641   -64.350  1.00 86.99  ?  298 TYR A C   1 
ATOM   2090 O  O   . TYR A 1 300 ? 2.525   1.154   -64.063  1.00 89.33  ?  298 TYR A O   1 
ATOM   2091 C  CB  . TYR A 1 300 ? 1.236   2.113   -66.815  1.00 74.95  ?  298 TYR A CB  1 
ATOM   2092 C  CG  . TYR A 1 300 ? 2.637   1.788   -67.278  1.00 80.13  ?  298 TYR A CG  1 
ATOM   2093 C  CD1 . TYR A 1 300 ? 2.869   0.757   -68.179  1.00 82.86  ?  298 TYR A CD1 1 
ATOM   2094 C  CD2 . TYR A 1 300 ? 3.726   2.525   -66.831  1.00 84.74  ?  298 TYR A CD2 1 
ATOM   2095 C  CE1 . TYR A 1 300 ? 4.148   0.457   -68.609  1.00 83.32  ?  298 TYR A CE1 1 
ATOM   2096 C  CE2 . TYR A 1 300 ? 5.009   2.233   -67.258  1.00 89.04  ?  298 TYR A CE2 1 
ATOM   2097 C  CZ  . TYR A 1 300 ? 5.213   1.199   -68.146  1.00 87.78  ?  298 TYR A CZ  1 
ATOM   2098 O  OH  . TYR A 1 300 ? 6.487   0.907   -68.575  1.00 88.15  ?  298 TYR A OH  1 
ATOM   2099 N  N   . TYR A 1 301 ? 0.788   2.504   -63.553  1.00 80.77  ?  299 TYR A N   1 
ATOM   2100 C  CA  . TYR A 1 301 ? 1.282   2.932   -62.245  1.00 87.64  ?  299 TYR A CA  1 
ATOM   2101 C  C   . TYR A 1 301 ? 0.189   2.604   -61.233  1.00 87.08  ?  299 TYR A C   1 
ATOM   2102 O  O   . TYR A 1 301 ? -0.527  3.500   -60.760  1.00 85.28  ?  299 TYR A O   1 
ATOM   2103 C  CB  . TYR A 1 301 ? 1.631   4.418   -62.242  1.00 82.69  ?  299 TYR A CB  1 
ATOM   2104 C  CG  . TYR A 1 301 ? 2.707   4.782   -63.240  1.00 84.27  ?  299 TYR A CG  1 
ATOM   2105 C  CD1 . TYR A 1 301 ? 3.962   4.190   -63.186  1.00 85.12  ?  299 TYR A CD1 1 
ATOM   2106 C  CD2 . TYR A 1 301 ? 2.458   5.698   -64.254  1.00 86.13  ?  299 TYR A CD2 1 
ATOM   2107 C  CE1 . TYR A 1 301 ? 4.946   4.517   -64.100  1.00 84.70  ?  299 TYR A CE1 1 
ATOM   2108 C  CE2 . TYR A 1 301 ? 3.434   6.028   -65.175  1.00 80.99  ?  299 TYR A CE2 1 
ATOM   2109 C  CZ  . TYR A 1 301 ? 4.676   5.435   -65.093  1.00 85.76  ?  299 TYR A CZ  1 
ATOM   2110 O  OH  . TYR A 1 301 ? 5.648   5.762   -66.011  1.00 87.21  ?  299 TYR A OH  1 
ATOM   2111 N  N   . PRO A 1 302 ? 0.045   1.327   -60.862  1.00 88.35  ?  300 PRO A N   1 
ATOM   2112 C  CA  . PRO A 1 302 ? -1.125  0.909   -60.073  1.00 91.20  ?  300 PRO A CA  1 
ATOM   2113 C  C   . PRO A 1 302 ? -1.093  1.353   -58.621  1.00 93.00  ?  300 PRO A C   1 
ATOM   2114 O  O   . PRO A 1 302 ? -2.102  1.184   -57.924  1.00 94.13  ?  300 PRO A O   1 
ATOM   2115 C  CB  . PRO A 1 302 ? -1.087  -0.626  -60.181  1.00 96.29  ?  300 PRO A CB  1 
ATOM   2116 C  CG  . PRO A 1 302 ? -0.006  -0.931  -61.223  1.00 91.37  ?  300 PRO A CG  1 
ATOM   2117 C  CD  . PRO A 1 302 ? 0.954   0.199   -61.103  1.00 91.09  ?  300 PRO A CD  1 
ATOM   2118 N  N   . SER A 1 303 ? 0.018   1.906   -58.141  1.00 95.03  ?  301 SER A N   1 
ATOM   2119 C  CA  . SER A 1 303 ? 0.124   2.353   -56.760  1.00 98.68  ?  301 SER A CA  1 
ATOM   2120 C  C   . SER A 1 303 ? 0.025   3.866   -56.624  1.00 96.65  ?  301 SER A C   1 
ATOM   2121 O  O   . SER A 1 303 ? -0.049  4.370   -55.498  1.00 99.42  ?  301 SER A O   1 
ATOM   2122 C  CB  . SER A 1 303 ? 1.443   1.868   -56.144  1.00 103.47 ?  301 SER A CB  1 
ATOM   2123 O  OG  . SER A 1 303 ? 2.559   2.414   -56.826  1.00 102.42 ?  301 SER A OG  1 
ATOM   2124 N  N   . ALA A 1 304 ? 0.024   4.591   -57.736  1.00 92.20  ?  302 ALA A N   1 
ATOM   2125 C  CA  . ALA A 1 304 ? 0.053   6.043   -57.712  1.00 93.88  ?  302 ALA A CA  1 
ATOM   2126 C  C   . ALA A 1 304 ? -1.321  6.629   -57.413  1.00 89.54  ?  302 ALA A C   1 
ATOM   2127 O  O   . ALA A 1 304 ? -2.359  6.069   -57.778  1.00 86.99  ?  302 ALA A O   1 
ATOM   2128 C  CB  . ALA A 1 304 ? 0.558   6.588   -59.048  1.00 86.59  ?  302 ALA A CB  1 
ATOM   2129 N  N   . ARG A 1 305 ? -1.312  7.777   -56.744  1.00 89.44  ?  303 ARG A N   1 
ATOM   2130 C  CA  . ARG A 1 305 ? -2.524  8.535   -56.481  1.00 88.01  ?  303 ARG A CA  1 
ATOM   2131 C  C   . ARG A 1 305 ? -2.712  9.448   -57.681  1.00 84.87  ?  303 ARG A C   1 
ATOM   2132 O  O   . ARG A 1 305 ? -1.782  10.157  -58.076  1.00 86.86  ?  303 ARG A O   1 
ATOM   2133 C  CB  . ARG A 1 305 ? -2.393  9.346   -55.189  1.00 92.50  ?  303 ARG A CB  1 
ATOM   2134 C  CG  . ARG A 1 305 ? -3.679  9.975   -54.638  1.00 92.69  ?  303 ARG A CG  1 
ATOM   2135 C  CD  . ARG A 1 305 ? -3.319  11.142  -53.712  1.00 94.01  ?  303 ARG A CD  1 
ATOM   2136 N  NE  . ARG A 1 305 ? -4.419  11.638  -52.889  1.00 95.53  ?  303 ARG A NE  1 
ATOM   2137 C  CZ  . ARG A 1 305 ? -5.529  12.202  -53.347  1.00 92.67  ?  303 ARG A CZ  1 
ATOM   2138 N  NH1 . ARG A 1 305 ? -5.852  12.156  -54.628  1.00 99.08  ?  303 ARG A NH1 1 
ATOM   2139 N  NH2 . ARG A 1 305 ? -6.365  12.776  -52.486  1.00 94.86  ?  303 ARG A NH2 1 
ATOM   2140 N  N   . ILE A 1 306 ? -3.901  9.423   -58.270  1.00 84.17  ?  304 ILE A N   1 
ATOM   2141 C  CA  . ILE A 1 306 ? -4.157  10.175  -59.489  1.00 81.82  ?  304 ILE A CA  1 
ATOM   2142 C  C   . ILE A 1 306 ? -5.379  11.046  -59.278  1.00 79.60  ?  304 ILE A C   1 
ATOM   2143 O  O   . ILE A 1 306 ? -6.437  10.556  -58.867  1.00 78.09  ?  304 ILE A O   1 
ATOM   2144 C  CB  . ILE A 1 306 ? -4.371  9.255   -60.707  1.00 76.40  ?  304 ILE A CB  1 
ATOM   2145 C  CG1 . ILE A 1 306 ? -3.378  8.092   -60.695  1.00 84.61  ?  304 ILE A CG1 1 
ATOM   2146 C  CG2 . ILE A 1 306 ? -4.235  10.051  -61.996  1.00 75.17  ?  304 ILE A CG2 1 
ATOM   2147 C  CD1 . ILE A 1 306 ? -1.977  8.486   -61.096  1.00 86.53  ?  304 ILE A CD1 1 
ATOM   2148 N  N   . VAL A 1 307 ? -5.227  12.334  -59.547  1.00 72.96  ?  305 VAL A N   1 
ATOM   2149 C  CA  . VAL A 1 307 ? -6.334  13.273  -59.524  1.00 76.37  ?  305 VAL A CA  1 
ATOM   2150 C  C   . VAL A 1 307 ? -6.695  13.542  -60.976  1.00 70.03  ?  305 VAL A C   1 
ATOM   2151 O  O   . VAL A 1 307 ? -5.857  14.008  -61.757  1.00 68.47  ?  305 VAL A O   1 
ATOM   2152 C  CB  . VAL A 1 307 ? -5.967  14.566  -58.780  1.00 77.28  ?  305 VAL A CB  1 
ATOM   2153 C  CG1 . VAL A 1 307 ? -7.084  15.590  -58.908  1.00 71.89  ?  305 VAL A CG1 1 
ATOM   2154 C  CG2 . VAL A 1 307 ? -5.673  14.267  -57.316  1.00 79.60  ?  305 VAL A CG2 1 
ATOM   2155 N  N   . TYR A 1 308 ? -7.932  13.231  -61.341  1.00 69.47  ?  306 TYR A N   1 
ATOM   2156 C  CA  . TYR A 1 308 ? -8.444  13.488  -62.677  1.00 70.64  ?  306 TYR A CA  1 
ATOM   2157 C  C   . TYR A 1 308 ? -9.303  14.741  -62.596  1.00 62.68  ?  306 TYR A C   1 
ATOM   2158 O  O   . TYR A 1 308 ? -10.308 14.760  -61.876  1.00 63.49  ?  306 TYR A O   1 
ATOM   2159 C  CB  . TYR A 1 308 ? -9.251  12.291  -63.182  1.00 70.28  ?  306 TYR A CB  1 
ATOM   2160 C  CG  . TYR A 1 308 ? -8.407  11.066  -63.473  1.00 74.15  ?  306 TYR A CG  1 
ATOM   2161 C  CD1 . TYR A 1 308 ? -7.673  10.959  -64.648  1.00 71.44  ?  306 TYR A CD1 1 
ATOM   2162 C  CD2 . TYR A 1 308 ? -8.342  10.017  -62.564  1.00 69.98  ?  306 TYR A CD2 1 
ATOM   2163 C  CE1 . TYR A 1 308 ? -6.902  9.838   -64.910  1.00 66.58  ?  306 TYR A CE1 1 
ATOM   2164 C  CE2 . TYR A 1 308 ? -7.575  8.895   -62.817  1.00 73.94  ?  306 TYR A CE2 1 
ATOM   2165 C  CZ  . TYR A 1 308 ? -6.858  8.810   -63.992  1.00 73.73  ?  306 TYR A CZ  1 
ATOM   2166 O  OH  . TYR A 1 308 ? -6.093  7.694   -64.245  1.00 68.65  ?  306 TYR A OH  1 
ATOM   2167 N  N   . THR A 1 309 ? -8.909  15.786  -63.319  1.00 61.10  ?  307 THR A N   1 
ATOM   2168 C  CA  . THR A 1 309 ? -9.614  17.056  -63.252  1.00 68.60  ?  307 THR A CA  1 
ATOM   2169 C  C   . THR A 1 309 ? -9.843  17.634  -64.641  1.00 65.49  ?  307 THR A C   1 
ATOM   2170 O  O   . THR A 1 309 ? -9.096  17.362  -65.586  1.00 61.10  ?  307 THR A O   1 
ATOM   2171 C  CB  . THR A 1 309 ? -8.837  18.068  -62.391  1.00 68.51  ?  307 THR A CB  1 
ATOM   2172 O  OG1 . THR A 1 309 ? -9.667  19.201  -62.106  1.00 75.80  ?  307 THR A OG1 1 
ATOM   2173 C  CG2 . THR A 1 309 ? -7.579  18.530  -63.113  1.00 69.29  ?  307 THR A CG2 1 
ATOM   2174 N  N   . ALA A 1 310 ? -10.900 18.435  -64.744  1.00 66.15  ?  308 ALA A N   1 
ATOM   2175 C  CA  . ALA A 1 310 ? -11.257 19.158  -65.957  1.00 64.11  ?  308 ALA A CA  1 
ATOM   2176 C  C   . ALA A 1 310 ? -12.145 20.324  -65.546  1.00 67.18  ?  308 ALA A C   1 
ATOM   2177 O  O   . ALA A 1 310 ? -12.637 20.383  -64.416  1.00 62.45  ?  308 ALA A O   1 
ATOM   2178 C  CB  . ALA A 1 310 ? -11.957 18.251  -66.974  1.00 55.64  ?  308 ALA A CB  1 
ATOM   2179 N  N   . CYS A 1 311 ? -12.350 21.257  -66.476  1.00 52.79  ?  309 CYS A N   1 
ATOM   2180 C  CA  . CYS A 1 311 ? -13.120 22.447  -66.130  1.00 62.32  ?  309 CYS A CA  1 
ATOM   2181 C  C   . CYS A 1 311 ? -14.615 22.166  -66.072  1.00 62.27  ?  309 CYS A C   1 
ATOM   2182 O  O   . CYS A 1 311 ? -15.324 22.774  -65.263  1.00 64.37  ?  309 CYS A O   1 
ATOM   2183 C  CB  . CYS A 1 311 ? -12.845 23.571  -67.131  1.00 62.04  ?  309 CYS A CB  1 
ATOM   2184 S  SG  . CYS A 1 311 ? -11.126 24.118  -67.196  1.00 69.32  ?  309 CYS A SG  1 
ATOM   2185 N  N   . SER A 1 312 ? -15.105 21.244  -66.891  1.00 56.38  ?  310 SER A N   1 
ATOM   2186 C  CA  . SER A 1 312 ? -16.527 20.955  -66.981  1.00 63.52  ?  310 SER A CA  1 
ATOM   2187 C  C   . SER A 1 312 ? -16.883 19.689  -66.210  1.00 63.52  ?  310 SER A C   1 
ATOM   2188 O  O   . SER A 1 312 ? -16.041 18.822  -65.959  1.00 60.81  ?  310 SER A O   1 
ATOM   2189 C  CB  . SER A 1 312 ? -16.951 20.809  -68.446  1.00 58.81  ?  310 SER A CB  1 
ATOM   2190 O  OG  . SER A 1 312 ? -16.186 19.808  -69.096  1.00 68.41  ?  310 SER A OG  1 
ATOM   2191 N  N   . HIS A 1 313 ? -18.163 19.592  -65.841  1.00 69.91  ?  311 HIS A N   1 
ATOM   2192 C  CA  . HIS A 1 313 ? -18.634 18.407  -65.133  1.00 68.40  ?  311 HIS A CA  1 
ATOM   2193 C  C   . HIS A 1 313 ? -18.769 17.228  -66.083  1.00 69.51  ?  311 HIS A C   1 
ATOM   2194 O  O   . HIS A 1 313 ? -18.613 16.073  -65.668  1.00 68.22  ?  311 HIS A O   1 
ATOM   2195 C  CB  . HIS A 1 313 ? -19.972 18.687  -64.450  1.00 65.98  ?  311 HIS A CB  1 
ATOM   2196 C  CG  . HIS A 1 313 ? -19.849 19.400  -63.141  1.00 72.18  ?  311 HIS A CG  1 
ATOM   2197 N  ND1 . HIS A 1 313 ? -19.418 18.775  -61.991  1.00 69.33  ?  311 HIS A ND1 1 
ATOM   2198 C  CD2 . HIS A 1 313 ? -20.114 20.682  -62.795  1.00 75.49  ?  311 HIS A CD2 1 
ATOM   2199 C  CE1 . HIS A 1 313 ? -19.415 19.643  -60.995  1.00 78.00  ?  311 HIS A CE1 1 
ATOM   2200 N  NE2 . HIS A 1 313 ? -19.833 20.808  -61.456  1.00 78.42  ?  311 HIS A NE2 1 
ATOM   2201 N  N   . ALA A 1 314 ? -19.060 17.498  -67.358  1.00 65.51  ?  312 ALA A N   1 
ATOM   2202 C  CA  . ALA A 1 314 ? -19.247 16.419  -68.318  1.00 69.90  ?  312 ALA A CA  1 
ATOM   2203 C  C   . ALA A 1 314 ? -17.930 15.719  -68.620  1.00 67.54  ?  312 ALA A C   1 
ATOM   2204 O  O   . ALA A 1 314 ? -17.914 14.505  -68.859  1.00 68.04  ?  312 ALA A O   1 
ATOM   2205 C  CB  . ALA A 1 314 ? -19.877 16.959  -69.601  1.00 68.01  ?  312 ALA A CB  1 
ATOM   2206 N  N   . ALA A 1 315 ? -16.821 16.461  -68.615  1.00 66.46  ?  313 ALA A N   1 
ATOM   2207 C  CA  . ALA A 1 315 ? -15.522 15.848  -68.864  1.00 64.66  ?  313 ALA A CA  1 
ATOM   2208 C  C   . ALA A 1 315 ? -15.152 14.900  -67.732  1.00 64.21  ?  313 ALA A C   1 
ATOM   2209 O  O   . ALA A 1 315 ? -14.727 13.764  -67.974  1.00 65.25  ?  313 ALA A O   1 
ATOM   2210 C  CB  . ALA A 1 315 ? -14.455 16.928  -69.040  1.00 58.58  ?  313 ALA A CB  1 
ATOM   2211 N  N   . VAL A 1 316 ? -15.290 15.359  -66.486  1.00 65.40  ?  314 VAL A N   1 
ATOM   2212 C  CA  . VAL A 1 316 ? -14.978 14.507  -65.342  1.00 68.93  ?  314 VAL A CA  1 
ATOM   2213 C  C   . VAL A 1 316 ? -15.855 13.262  -65.364  1.00 69.67  ?  314 VAL A C   1 
ATOM   2214 O  O   . VAL A 1 316 ? -15.387 12.148  -65.098  1.00 71.99  ?  314 VAL A O   1 
ATOM   2215 C  CB  . VAL A 1 316 ? -15.140 15.291  -64.026  1.00 66.60  ?  314 VAL A CB  1 
ATOM   2216 C  CG1 . VAL A 1 316 ? -14.902 14.377  -62.834  1.00 67.60  ?  314 VAL A CG1 1 
ATOM   2217 C  CG2 . VAL A 1 316 ? -14.187 16.477  -63.991  1.00 63.06  ?  314 VAL A CG2 1 
ATOM   2218 N  N   . ASP A 1 317 ? -17.144 13.435  -65.672  1.00 72.69  ?  315 ASP A N   1 
ATOM   2219 C  CA  . ASP A 1 317 ? -18.050 12.294  -65.753  1.00 74.48  ?  315 ASP A CA  1 
ATOM   2220 C  C   . ASP A 1 317 ? -17.614 11.330  -66.848  1.00 73.50  ?  315 ASP A C   1 
ATOM   2221 O  O   . ASP A 1 317 ? -17.738 10.108  -66.697  1.00 73.76  ?  315 ASP A O   1 
ATOM   2222 C  CB  . ASP A 1 317 ? -19.481 12.776  -65.988  1.00 73.23  ?  315 ASP A CB  1 
ATOM   2223 C  CG  . ASP A 1 317 ? -20.075 13.450  -64.764  1.00 78.81  ?  315 ASP A CG  1 
ATOM   2224 O  OD1 . ASP A 1 317 ? -19.384 13.516  -63.726  1.00 75.07  ?  315 ASP A OD1 1 
ATOM   2225 O  OD2 . ASP A 1 317 ? -21.231 13.916  -64.841  1.00 85.37  -1 315 ASP A OD2 1 
ATOM   2226 N  N   . ALA A 1 318 ? -17.102 11.861  -67.961  1.00 71.49  ?  316 ALA A N   1 
ATOM   2227 C  CA  . ALA A 1 318 ? -16.605 10.995  -69.024  1.00 74.27  ?  316 ALA A CA  1 
ATOM   2228 C  C   . ALA A 1 318 ? -15.425 10.179  -68.523  1.00 73.15  ?  316 ALA A C   1 
ATOM   2229 O  O   . ALA A 1 318 ? -15.297 8.990   -68.839  1.00 71.30  ?  316 ALA A O   1 
ATOM   2230 C  CB  . ALA A 1 318 ? -16.213 11.824  -70.247  1.00 68.62  ?  316 ALA A CB  1 
ATOM   2231 N  N   . LEU A 1 319 ? -14.544 10.812  -67.747  1.00 70.71  ?  317 LEU A N   1 
ATOM   2232 C  CA  . LEU A 1 319 ? -13.382 10.110  -67.223  1.00 70.82  ?  317 LEU A CA  1 
ATOM   2233 C  C   . LEU A 1 319 ? -13.807 9.110   -66.155  1.00 76.60  ?  317 LEU A C   1 
ATOM   2234 O  O   . LEU A 1 319 ? -13.190 8.047   -66.017  1.00 74.29  ?  317 LEU A O   1 
ATOM   2235 C  CB  . LEU A 1 319 ? -12.376 11.121  -66.672  1.00 69.36  ?  317 LEU A CB  1 
ATOM   2236 C  CG  . LEU A 1 319 ? -10.933 11.027  -67.168  1.00 69.99  ?  317 LEU A CG  1 
ATOM   2237 C  CD1 . LEU A 1 319 ? -10.899 10.992  -68.684  1.00 70.12  ?  317 LEU A CD1 1 
ATOM   2238 C  CD2 . LEU A 1 319 ? -10.129 12.210  -66.656  1.00 71.80  ?  317 LEU A CD2 1 
ATOM   2239 N  N   . CYS A 1 320 ? -14.859 9.434   -65.396  1.00 72.09  ?  318 CYS A N   1 
ATOM   2240 C  CA  . CYS A 1 320 ? -15.381 8.502   -64.402  1.00 75.64  ?  318 CYS A CA  1 
ATOM   2241 C  C   . CYS A 1 320 ? -15.934 7.256   -65.079  1.00 76.25  ?  318 CYS A C   1 
ATOM   2242 O  O   . CYS A 1 320 ? -15.617 6.126   -64.687  1.00 72.14  ?  318 CYS A O   1 
ATOM   2243 C  CB  . CYS A 1 320 ? -16.468 9.174   -63.563  1.00 77.03  ?  318 CYS A CB  1 
ATOM   2244 S  SG  . CYS A 1 320 ? -15.891 10.462  -62.439  1.00 71.78  ?  318 CYS A SG  1 
ATOM   2245 N  N   . GLU A 1 321 ? -16.774 7.447   -66.102  1.00 77.01  ?  319 GLU A N   1 
ATOM   2246 C  CA  . GLU A 1 321 ? -17.376 6.307   -66.783  1.00 80.22  ?  319 GLU A CA  1 
ATOM   2247 C  C   . GLU A 1 321 ? -16.303 5.392   -67.351  1.00 78.21  ?  319 GLU A C   1 
ATOM   2248 O  O   . GLU A 1 321 ? -16.479 4.168   -67.382  1.00 77.61  ?  319 GLU A O   1 
ATOM   2249 C  CB  . GLU A 1 321 ? -18.316 6.793   -67.886  1.00 76.22  ?  319 GLU A CB  1 
ATOM   2250 C  CG  . GLU A 1 321 ? -19.794 6.682   -67.535  1.00 77.36  ?  319 GLU A CG  1 
ATOM   2251 C  CD  . GLU A 1 321 ? -20.246 5.250   -67.344  1.00 84.81  ?  319 GLU A CD  1 
ATOM   2252 O  OE1 . GLU A 1 321 ? -19.981 4.418   -68.237  1.00 91.08  ?  319 GLU A OE1 1 
ATOM   2253 O  OE2 . GLU A 1 321 ? -20.869 4.955   -66.302  1.00 89.06  -1 319 GLU A OE2 1 
ATOM   2254 N  N   . LYS A 1 322 ? -15.177 5.966   -67.786  1.00 72.20  ?  320 LYS A N   1 
ATOM   2255 C  CA  . LYS A 1 322 ? -14.089 5.159   -68.325  1.00 76.87  ?  320 LYS A CA  1 
ATOM   2256 C  C   . LYS A 1 322 ? -13.377 4.407   -67.209  1.00 74.66  ?  320 LYS A C   1 
ATOM   2257 O  O   . LYS A 1 322 ? -12.925 3.276   -67.412  1.00 80.75  ?  320 LYS A O   1 
ATOM   2258 C  CB  . LYS A 1 322 ? -13.109 6.049   -69.092  1.00 72.31  ?  320 LYS A CB  1 
ATOM   2259 C  CG  . LYS A 1 322 ? -11.899 5.328   -69.685  1.00 77.07  ?  320 LYS A CG  1 
ATOM   2260 C  CD  . LYS A 1 322 ? -12.270 4.194   -70.637  1.00 69.83  ?  320 LYS A CD  1 
ATOM   2261 C  CE  . LYS A 1 322 ? -12.576 4.710   -72.037  1.00 66.08  ?  320 LYS A CE  1 
ATOM   2262 N  NZ  . LYS A 1 322 ? -12.695 3.600   -73.026  1.00 76.63  ?  320 LYS A NZ  1 
ATOM   2263 N  N   . ALA A 1 323 ? -13.271 5.022   -66.029  1.00 73.11  ?  321 ALA A N   1 
ATOM   2264 C  CA  . ALA A 1 323 ? -12.605 4.378   -64.902  1.00 79.56  ?  321 ALA A CA  1 
ATOM   2265 C  C   . ALA A 1 323 ? -13.449 3.236   -64.353  1.00 74.13  ?  321 ALA A C   1 
ATOM   2266 O  O   . ALA A 1 323 ? -12.906 2.233   -63.875  1.00 72.12  ?  321 ALA A O   1 
ATOM   2267 C  CB  . ALA A 1 323 ? -12.309 5.401   -63.805  1.00 73.29  ?  321 ALA A CB  1 
ATOM   2268 N  N   . LEU A 1 324 ? -14.773 3.382   -64.404  1.00 71.22  ?  322 LEU A N   1 
ATOM   2269 C  CA  . LEU A 1 324 ? -15.723 2.411   -63.877  1.00 73.60  ?  322 LEU A CA  1 
ATOM   2270 C  C   . LEU A 1 324 ? -15.595 1.058   -64.567  1.00 77.90  ?  322 LEU A C   1 
ATOM   2271 O  O   . LEU A 1 324 ? -16.260 0.091   -64.181  1.00 89.60  ?  322 LEU A O   1 
ATOM   2272 C  CB  . LEU A 1 324 ? -17.147 2.951   -64.041  1.00 75.90  ?  322 LEU A CB  1 
ATOM   2273 C  CG  . LEU A 1 324 ? -18.337 2.126   -63.548  1.00 86.27  ?  322 LEU A CG  1 
ATOM   2274 C  CD1 . LEU A 1 324 ? -18.382 2.069   -62.029  1.00 83.39  ?  322 LEU A CD1 1 
ATOM   2275 C  CD2 . LEU A 1 324 ? -19.631 2.697   -64.111  1.00 86.35  ?  322 LEU A CD2 1 
ATOM   2276 N  N   . LYS A 1 325 ? -14.728 0.973   -65.574  1.00 75.76  ?  323 LYS A N   1 
ATOM   2277 C  CA  . LYS A 1 325 ? -14.560 -0.239  -66.362  1.00 76.10  ?  323 LYS A CA  1 
ATOM   2278 C  C   . LYS A 1 325 ? -13.200 -0.889  -66.169  1.00 74.49  ?  323 LYS A C   1 
ATOM   2279 O  O   . LYS A 1 325 ? -13.080 -2.103  -66.342  1.00 74.68  ?  323 LYS A O   1 
ATOM   2280 C  CB  . LYS A 1 325 ? -14.771 0.066   -67.852  1.00 74.06  ?  323 LYS A CB  1 
ATOM   2281 C  CG  . LYS A 1 325 ? -14.443 -1.074  -68.808  1.00 78.75  ?  323 LYS A CG  1 
ATOM   2282 C  CD  . LYS A 1 325 ? -15.347 -2.279  -68.577  1.00 77.59  ?  323 LYS A CD  1 
ATOM   2283 C  CE  . LYS A 1 325 ? -14.970 -3.434  -69.492  1.00 79.26  ?  323 LYS A CE  1 
ATOM   2284 N  NZ  . LYS A 1 325 ? -14.853 -2.982  -70.909  1.00 82.07  ?  323 LYS A NZ  1 
ATOM   2285 N  N   . TYR A 1 326 ? -12.177 -0.110  -65.808  1.00 73.68  ?  324 TYR A N   1 
ATOM   2286 C  CA  . TYR A 1 326 ? -10.819 -0.618  -65.710  1.00 75.65  ?  324 TYR A CA  1 
ATOM   2287 C  C   . TYR A 1 326 ? -10.168 -0.363  -64.357  1.00 78.00  ?  324 TYR A C   1 
ATOM   2288 O  O   . TYR A 1 326 ? -9.023  -0.783  -64.157  1.00 76.40  ?  324 TYR A O   1 
ATOM   2289 C  CB  . TYR A 1 326 ? -9.931  0.001   -66.804  1.00 68.85  ?  324 TYR A CB  1 
ATOM   2290 C  CG  . TYR A 1 326 ? -10.382 -0.270  -68.223  1.00 70.67  ?  324 TYR A CG  1 
ATOM   2291 C  CD1 . TYR A 1 326 ? -9.963  -1.408  -68.900  1.00 72.41  ?  324 TYR A CD1 1 
ATOM   2292 C  CD2 . TYR A 1 326 ? -11.204 0.627   -68.896  1.00 73.46  ?  324 TYR A CD2 1 
ATOM   2293 C  CE1 . TYR A 1 326 ? -10.365 -1.655  -70.203  1.00 73.40  ?  324 TYR A CE1 1 
ATOM   2294 C  CE2 . TYR A 1 326 ? -11.611 0.388   -70.199  1.00 69.63  ?  324 TYR A CE2 1 
ATOM   2295 C  CZ  . TYR A 1 326 ? -11.187 -0.754  -70.846  1.00 68.19  ?  324 TYR A CZ  1 
ATOM   2296 O  OH  . TYR A 1 326 ? -11.589 -0.999  -72.138  1.00 72.43  ?  324 TYR A OH  1 
ATOM   2297 N  N   . LEU A 1 327 ? -10.856 0.288   -63.422  1.00 76.14  ?  325 LEU A N   1 
ATOM   2298 C  CA  . LEU A 1 327 ? -10.253 0.647   -62.148  1.00 81.32  ?  325 LEU A CA  1 
ATOM   2299 C  C   . LEU A 1 327 ? -11.086 0.139   -60.981  1.00 82.89  ?  325 LEU A C   1 
ATOM   2300 O  O   . LEU A 1 327 ? -12.310 0.007   -61.090  1.00 83.18  ?  325 LEU A O   1 
ATOM   2301 C  CB  . LEU A 1 327 ? -10.084 2.169   -62.033  1.00 79.04  ?  325 LEU A CB  1 
ATOM   2302 C  CG  . LEU A 1 327 ? -9.022  2.774   -62.956  1.00 76.73  ?  325 LEU A CG  1 
ATOM   2303 C  CD1 . LEU A 1 327 ? -8.890  4.271   -62.726  1.00 74.88  ?  325 LEU A CD1 1 
ATOM   2304 C  CD2 . LEU A 1 327 ? -7.680  2.075   -62.779  1.00 78.37  ?  325 LEU A CD2 1 
ATOM   2305 N  N   . PRO A 1 328 ? -10.445 -0.155  -59.849  1.00 86.55  ?  326 PRO A N   1 
ATOM   2306 C  CA  . PRO A 1 328 ? -11.190 -0.562  -58.646  1.00 92.67  ?  326 PRO A CA  1 
ATOM   2307 C  C   . PRO A 1 328 ? -12.203 0.493   -58.229  1.00 91.46  ?  326 PRO A C   1 
ATOM   2308 O  O   . PRO A 1 328 ? -11.851 1.634   -57.920  1.00 92.66  ?  326 PRO A O   1 
ATOM   2309 C  CB  . PRO A 1 328 ? -10.082 -0.735  -57.600  1.00 94.40  ?  326 PRO A CB  1 
ATOM   2310 C  CG  . PRO A 1 328 ? -8.878  -1.088  -58.423  1.00 92.59  ?  326 PRO A CG  1 
ATOM   2311 C  CD  . PRO A 1 328 ? -8.992  -0.172  -59.609  1.00 87.28  ?  326 PRO A CD  1 
ATOM   2312 N  N   . ILE A 1 329 ? -13.475 0.097   -58.212  1.00 91.99  ?  327 ILE A N   1 
ATOM   2313 C  CA  . ILE A 1 329 ? -14.577 1.010   -57.926  1.00 91.90  ?  327 ILE A CA  1 
ATOM   2314 C  C   . ILE A 1 329 ? -14.552 1.461   -56.469  1.00 100.92 ?  327 ILE A C   1 
ATOM   2315 O  O   . ILE A 1 329 ? -15.386 2.271   -56.047  1.00 96.39  ?  327 ILE A O   1 
ATOM   2316 C  CB  . ILE A 1 329 ? -15.927 0.358   -58.273  1.00 93.16  ?  327 ILE A CB  1 
ATOM   2317 C  CG1 . ILE A 1 329 ? -17.001 1.425   -58.482  1.00 91.63  ?  327 ILE A CG1 1 
ATOM   2318 C  CG2 . ILE A 1 329 ? -16.348 -0.609  -57.175  1.00 98.93  ?  327 ILE A CG2 1 
ATOM   2319 C  CD1 . ILE A 1 329 ? -18.368 0.855   -58.780  1.00 93.40  ?  327 ILE A CD1 1 
ATOM   2320 N  N   . ASP A 1 330 ? -13.595 0.952   -55.690  1.00 98.60  ?  328 ASP A N   1 
ATOM   2321 C  CA  . ASP A 1 330 ? -13.511 1.275   -54.273  1.00 104.99 ?  328 ASP A CA  1 
ATOM   2322 C  C   . ASP A 1 330 ? -12.362 2.222   -53.959  1.00 101.69 ?  328 ASP A C   1 
ATOM   2323 O  O   . ASP A 1 330 ? -12.287 2.729   -52.834  1.00 104.85 ?  328 ASP A O   1 
ATOM   2324 C  CB  . ASP A 1 330 ? -13.398 -0.002  -53.419  1.00 108.17 ?  328 ASP A CB  1 
ATOM   2325 C  CG  . ASP A 1 330 ? -12.132 -0.788  -53.689  1.00 110.09 ?  328 ASP A CG  1 
ATOM   2326 O  OD1 . ASP A 1 330 ? -11.936 -1.235  -54.839  1.00 104.88 ?  328 ASP A OD1 1 
ATOM   2327 O  OD2 . ASP A 1 330 ? -11.344 -0.982  -52.737  1.00 113.63 -1 328 ASP A OD2 1 
ATOM   2328 N  N   . LYS A 1 331 ? -11.470 2.469   -54.920  1.00 97.61  ?  329 LYS A N   1 
ATOM   2329 C  CA  . LYS A 1 331 ? -10.401 3.448   -54.785  1.00 96.27  ?  329 LYS A CA  1 
ATOM   2330 C  C   . LYS A 1 331 ? -10.710 4.733   -55.552  1.00 92.24  ?  329 LYS A C   1 
ATOM   2331 O  O   . LYS A 1 331 ? -9.797  5.518   -55.831  1.00 89.67  ?  329 LYS A O   1 
ATOM   2332 C  CB  . LYS A 1 331 ? -9.068  2.869   -55.270  1.00 95.52  ?  329 LYS A CB  1 
ATOM   2333 C  CG  . LYS A 1 331 ? -8.371  1.882   -54.334  1.00 100.44 ?  329 LYS A CG  1 
ATOM   2334 C  CD  . LYS A 1 331 ? -9.057  0.522   -54.309  1.00 103.37 ?  329 LYS A CD  1 
ATOM   2335 C  CE  . LYS A 1 331 ? -8.297  -0.464  -53.428  1.00 109.84 ?  329 LYS A CE  1 
ATOM   2336 N  NZ  . LYS A 1 331 ? -8.905  -1.827  -53.441  1.00 115.57 ?  329 LYS A NZ  1 
ATOM   2337 N  N   . CYS A 1 332 ? -11.978 4.959   -55.896  1.00 92.94  ?  330 CYS A N   1 
ATOM   2338 C  CA  . CYS A 1 332 ? -12.403 6.085   -56.720  1.00 91.22  ?  330 CYS A CA  1 
ATOM   2339 C  C   . CYS A 1 332 ? -13.436 6.920   -55.975  1.00 88.34  ?  330 CYS A C   1 
ATOM   2340 O  O   . CYS A 1 332 ? -14.314 6.377   -55.297  1.00 91.86  ?  330 CYS A O   1 
ATOM   2341 C  CB  . CYS A 1 332 ? -13.004 5.606   -58.050  1.00 86.99  ?  330 CYS A CB  1 
ATOM   2342 S  SG  . CYS A 1 332 ? -11.893 4.644   -59.102  1.00 80.95  ?  330 CYS A SG  1 
ATOM   2343 N  N   . SER A 1 333 ? -13.325 8.244   -56.095  1.00 86.31  ?  331 SER A N   1 
ATOM   2344 C  CA  . SER A 1 333 ? -14.313 9.154   -55.530  1.00 87.78  ?  331 SER A CA  1 
ATOM   2345 C  C   . SER A 1 333 ? -14.585 10.314  -56.479  1.00 88.12  ?  331 SER A C   1 
ATOM   2346 O  O   . SER A 1 333 ? -13.655 10.897  -57.045  1.00 80.71  ?  331 SER A O   1 
ATOM   2347 C  CB  . SER A 1 333 ? -13.857 9.700   -54.172  1.00 91.62  ?  331 SER A CB  1 
ATOM   2348 O  OG  . SER A 1 333 ? -14.840 10.558  -53.621  1.00 93.42  ?  331 SER A OG  1 
ATOM   2349 N  N   . ARG A 1 334 ? -15.870 10.633  -56.654  1.00 91.97  ?  332 ARG A N   1 
ATOM   2350 C  CA  . ARG A 1 334 ? -16.314 11.797  -57.419  1.00 84.87  ?  332 ARG A CA  1 
ATOM   2351 C  C   . ARG A 1 334 ? -16.597 12.944  -56.451  1.00 87.25  ?  332 ARG A C   1 
ATOM   2352 O  O   . ARG A 1 334 ? -17.548 12.877  -55.664  1.00 88.72  ?  332 ARG A O   1 
ATOM   2353 C  CB  . ARG A 1 334 ? -17.557 11.464  -58.243  1.00 79.64  ?  332 ARG A CB  1 
ATOM   2354 C  CG  . ARG A 1 334 ? -18.081 12.616  -59.101  1.00 76.68  ?  332 ARG A CG  1 
ATOM   2355 C  CD  . ARG A 1 334 ? -17.057 13.036  -60.148  1.00 77.71  ?  332 ARG A CD  1 
ATOM   2356 N  NE  . ARG A 1 334 ? -17.630 13.843  -61.221  1.00 73.53  ?  332 ARG A NE  1 
ATOM   2357 C  CZ  . ARG A 1 334 ? -18.086 15.080  -61.080  1.00 72.53  ?  332 ARG A CZ  1 
ATOM   2358 N  NH1 . ARG A 1 334 ? -17.866 15.777  -59.977  1.00 76.03  ?  332 ARG A NH1 1 
ATOM   2359 N  NH2 . ARG A 1 334 ? -18.714 15.660  -62.100  1.00 75.05  ?  332 ARG A NH2 1 
ATOM   2360 N  N   . ILE A 1 335 ? -15.776 13.989  -56.502  1.00 81.64  ?  333 ILE A N   1 
ATOM   2361 C  CA  . ILE A 1 335 ? -15.971 15.153  -55.642  1.00 84.03  ?  333 ILE A CA  1 
ATOM   2362 C  C   . ILE A 1 335 ? -16.968 16.094  -56.304  1.00 82.32  ?  333 ILE A C   1 
ATOM   2363 O  O   . ILE A 1 335 ? -16.835 16.426  -57.488  1.00 88.66  ?  333 ILE A O   1 
ATOM   2364 C  CB  . ILE A 1 335 ? -14.639 15.869  -55.360  1.00 83.64  ?  333 ILE A CB  1 
ATOM   2365 C  CG1 . ILE A 1 335 ? -13.738 15.030  -54.449  1.00 86.61  ?  333 ILE A CG1 1 
ATOM   2366 C  CG2 . ILE A 1 335 ? -14.897 17.221  -54.713  1.00 85.56  ?  333 ILE A CG2 1 
ATOM   2367 C  CD1 . ILE A 1 335 ? -13.161 13.794  -55.097  1.00 87.17  ?  333 ILE A CD1 1 
ATOM   2368 N  N   . ILE A 1 336 ? -17.976 16.519  -55.547  1.00 87.22  ?  334 ILE A N   1 
ATOM   2369 C  CA  . ILE A 1 336 ? -19.004 17.415  -56.071  1.00 84.98  ?  334 ILE A CA  1 
ATOM   2370 C  C   . ILE A 1 336 ? -19.005 18.710  -55.267  1.00 91.56  ?  334 ILE A C   1 
ATOM   2371 O  O   . ILE A 1 336 ? -18.767 18.688  -54.050  1.00 91.37  ?  334 ILE A O   1 
ATOM   2372 C  CB  . ILE A 1 336 ? -20.390 16.749  -56.050  1.00 87.23  ?  334 ILE A CB  1 
ATOM   2373 C  CG1 . ILE A 1 336 ? -20.870 16.537  -54.611  1.00 94.25  ?  334 ILE A CG1 1 
ATOM   2374 C  CG2 . ILE A 1 336 ? -20.360 15.427  -56.801  1.00 87.64  ?  334 ILE A CG2 1 
ATOM   2375 C  CD1 . ILE A 1 336 ? -21.907 17.543  -54.147  1.00 96.07  ?  334 ILE A CD1 1 
ATOM   2376 N  N   . PRO A 1 337 ? -19.258 19.854  -55.899  1.00 95.11  ?  335 PRO A N   1 
ATOM   2377 C  CA  . PRO A 1 337 ? -19.369 21.104  -55.140  1.00 91.16  ?  335 PRO A CA  1 
ATOM   2378 C  C   . PRO A 1 337 ? -20.659 21.138  -54.340  1.00 94.70  ?  335 PRO A C   1 
ATOM   2379 O  O   . PRO A 1 337 ? -21.716 20.717  -54.818  1.00 95.90  ?  335 PRO A O   1 
ATOM   2380 C  CB  . PRO A 1 337 ? -19.358 22.180  -56.231  1.00 90.90  ?  335 PRO A CB  1 
ATOM   2381 C  CG  . PRO A 1 337 ? -19.957 21.491  -57.413  1.00 88.30  ?  335 PRO A CG  1 
ATOM   2382 C  CD  . PRO A 1 337 ? -19.450 20.070  -57.343  1.00 87.63  ?  335 PRO A CD  1 
ATOM   2383 N  N   . ALA A 1 338 ? -20.565 21.628  -53.101  1.00 97.21  ?  336 ALA A N   1 
ATOM   2384 C  CA  . ALA A 1 338 ? -21.759 21.714  -52.268  1.00 106.41 ?  336 ALA A CA  1 
ATOM   2385 C  C   . ALA A 1 338 ? -22.862 22.491  -52.975  1.00 105.64 ?  336 ALA A C   1 
ATOM   2386 O  O   . ALA A 1 338 ? -24.050 22.269  -52.712  1.00 107.72 ?  336 ALA A O   1 
ATOM   2387 C  CB  . ALA A 1 338 ? -21.421 22.360  -50.923  1.00 106.98 ?  336 ALA A CB  1 
ATOM   2388 N  N   . ARG A 1 339 ? -22.488 23.405  -53.870  1.00 106.43 ?  337 ARG A N   1 
ATOM   2389 C  CA  . ARG A 1 339 ? -23.429 24.118  -54.732  1.00 102.28 ?  337 ARG A CA  1 
ATOM   2390 C  C   . ARG A 1 339 ? -23.590 23.281  -55.996  1.00 99.23  ?  337 ARG A C   1 
ATOM   2391 O  O   . ARG A 1 339 ? -22.795 23.393  -56.933  1.00 102.78 ?  337 ARG A O   1 
ATOM   2392 C  CB  . ARG A 1 339 ? -22.919 25.520  -55.044  1.00 98.74  ?  337 ARG A CB  1 
ATOM   2393 C  CG  . ARG A 1 339 ? -22.204 26.193  -53.880  1.00 104.65 ?  337 ARG A CG  1 
ATOM   2394 C  CD  . ARG A 1 339 ? -22.014 27.681  -54.129  1.00 104.65 ?  337 ARG A CD  1 
ATOM   2395 N  NE  . ARG A 1 339 ? -23.269 28.353  -54.442  1.00 108.21 ?  337 ARG A NE  1 
ATOM   2396 C  CZ  . ARG A 1 339 ? -24.309 28.420  -53.621  1.00 104.71 ?  337 ARG A CZ  1 
ATOM   2397 N  NH1 . ARG A 1 339 ? -24.211 28.059  -52.352  1.00 108.99 ?  337 ARG A NH1 1 
ATOM   2398 N  NH2 . ARG A 1 339 ? -25.455 28.926  -54.066  1.00 106.35 ?  337 ARG A NH2 1 
ATOM   2399 N  N   . ALA A 1 340 ? -24.624 22.444  -56.033  1.00 103.80 ?  338 ALA A N   1 
ATOM   2400 C  CA  . ALA A 1 340 ? -24.749 21.381  -57.027  1.00 102.14 ?  338 ALA A CA  1 
ATOM   2401 C  C   . ALA A 1 340 ? -25.803 21.742  -58.070  1.00 97.30  ?  338 ALA A C   1 
ATOM   2402 O  O   . ALA A 1 340 ? -26.996 21.816  -57.755  1.00 100.01 ?  338 ALA A O   1 
ATOM   2403 C  CB  . ALA A 1 340 ? -25.090 20.055  -56.349  1.00 95.43  ?  338 ALA A CB  1 
ATOM   2404 N  N   . ARG A 1 341 ? -25.359 21.964  -59.311  1.00 91.27  ?  339 ARG A N   1 
ATOM   2405 C  CA  . ARG A 1 341 ? -26.243 22.421  -60.379  1.00 95.72  ?  339 ARG A CA  1 
ATOM   2406 C  C   . ARG A 1 341 ? -26.627 21.251  -61.278  1.00 95.48  ?  339 ARG A C   1 
ATOM   2407 O  O   . ARG A 1 341 ? -27.793 20.844  -61.309  1.00 99.57  ?  339 ARG A O   1 
ATOM   2408 C  CB  . ARG A 1 341 ? -25.584 23.530  -61.210  1.00 93.29  ?  339 ARG A CB  1 
ATOM   2409 C  CG  . ARG A 1 341 ? -26.334 23.880  -62.506  1.00 88.57  ?  339 ARG A CG  1 
ATOM   2410 C  CD  . ARG A 1 341 ? -25.672 25.038  -63.263  1.00 91.36  ?  339 ARG A CD  1 
ATOM   2411 N  NE  . ARG A 1 341 ? -24.832 24.624  -64.383  1.00 89.38  ?  339 ARG A NE  1 
ATOM   2412 C  CZ  . ARG A 1 341 ? -25.287 24.132  -65.529  1.00 89.33  ?  339 ARG A CZ  1 
ATOM   2413 N  NH1 . ARG A 1 341 ? -26.584 24.012  -65.764  1.00 96.06  ?  339 ARG A NH1 1 
ATOM   2414 N  NH2 . ARG A 1 341 ? -24.420 23.778  -66.474  1.00 83.27  ?  339 ARG A NH2 1 
ATOM   2415 N  N   . VAL A 1 342 ? -25.657 20.702  -62.008  1.00 84.29  ?  340 VAL A N   1 
ATOM   2416 C  CA  . VAL A 1 342 ? -25.907 19.557  -62.872  1.00 86.07  ?  340 VAL A CA  1 
ATOM   2417 C  C   . VAL A 1 342 ? -25.736 18.271  -62.070  1.00 89.82  ?  340 VAL A C   1 
ATOM   2418 O  O   . VAL A 1 342 ? -25.042 18.227  -61.051  1.00 94.20  ?  340 VAL A O   1 
ATOM   2419 C  CB  . VAL A 1 342 ? -24.991 19.558  -64.116  1.00 91.69  ?  340 VAL A CB  1 
ATOM   2420 C  CG1 . VAL A 1 342 ? -25.481 20.572  -65.143  1.00 82.40  ?  340 VAL A CG1 1 
ATOM   2421 C  CG2 . VAL A 1 342 ? -23.545 19.830  -63.722  1.00 86.11  ?  340 VAL A CG2 1 
ATOM   2422 N  N   . GLU A 1 343 ? -26.395 17.212  -62.534  1.00 92.59  ?  341 GLU A N   1 
ATOM   2423 C  CA  . GLU A 1 343 ? -26.175 15.879  -61.987  1.00 86.62  ?  341 GLU A CA  1 
ATOM   2424 C  C   . GLU A 1 343 ? -24.787 15.375  -62.365  1.00 89.07  ?  341 GLU A C   1 
ATOM   2425 O  O   . GLU A 1 343 ? -24.408 15.395  -63.540  1.00 83.64  ?  341 GLU A O   1 
ATOM   2426 C  CB  . GLU A 1 343 ? -27.239 14.910  -62.500  1.00 82.17  ?  341 GLU A CB  1 
ATOM   2427 C  CG  . GLU A 1 343 ? -28.665 15.285  -62.138  1.00 97.00  ?  341 GLU A CG  1 
ATOM   2428 C  CD  . GLU A 1 343 ? -29.670 14.268  -62.643  1.00 104.92 ?  341 GLU A CD  1 
ATOM   2429 O  OE1 . GLU A 1 343 ? -29.730 14.054  -63.873  1.00 97.66  ?  341 GLU A OE1 1 
ATOM   2430 O  OE2 . GLU A 1 343 ? -30.397 13.682  -61.813  1.00 93.59  -1 341 GLU A OE2 1 
ATOM   2431 N  N   . CYS A 1 344 ? -24.027 14.926  -61.373  1.00 83.44  ?  342 CYS A N   1 
ATOM   2432 C  CA  . CYS A 1 344 ? -22.712 14.364  -61.628  1.00 84.74  ?  342 CYS A CA  1 
ATOM   2433 C  C   . CYS A 1 344 ? -22.790 12.835  -61.658  1.00 87.32  ?  342 CYS A C   1 
ATOM   2434 O  O   . CYS A 1 344 ? -23.873 12.252  -61.786  1.00 84.83  ?  342 CYS A O   1 
ATOM   2435 C  CB  . CYS A 1 344 ? -21.722 14.879  -60.578  1.00 80.65  ?  342 CYS A CB  1 
ATOM   2436 S  SG  . CYS A 1 344 ? -21.660 16.676  -60.436  1.00 90.73  ?  342 CYS A SG  1 
ATOM   2437 N  N   . PHE A 1 345 ? -21.640 12.181  -61.526  1.00 87.41  ?  343 PHE A N   1 
ATOM   2438 C  CA  . PHE A 1 345 ? -21.546 10.731  -61.626  1.00 86.86  ?  343 PHE A CA  1 
ATOM   2439 C  C   . PHE A 1 345 ? -21.979 10.115  -60.298  1.00 84.61  ?  343 PHE A C   1 
ATOM   2440 O  O   . PHE A 1 345 ? -21.420 10.445  -59.246  1.00 95.42  ?  343 PHE A O   1 
ATOM   2441 C  CB  . PHE A 1 345 ? -20.106 10.366  -61.991  1.00 81.74  ?  343 PHE A CB  1 
ATOM   2442 C  CG  . PHE A 1 345 ? -19.883 8.918   -62.311  1.00 80.53  ?  343 PHE A CG  1 
ATOM   2443 C  CD1 . PHE A 1 345 ? -20.223 8.410   -63.554  1.00 79.18  ?  343 PHE A CD1 1 
ATOM   2444 C  CD2 . PHE A 1 345 ? -19.265 8.081   -61.398  1.00 82.56  ?  343 PHE A CD2 1 
ATOM   2445 C  CE1 . PHE A 1 345 ? -19.995 7.084   -63.864  1.00 78.45  ?  343 PHE A CE1 1 
ATOM   2446 C  CE2 . PHE A 1 345 ? -19.032 6.753   -61.701  1.00 86.44  ?  343 PHE A CE2 1 
ATOM   2447 C  CZ  . PHE A 1 345 ? -19.398 6.254   -62.936  1.00 88.49  ?  343 PHE A CZ  1 
ATOM   2448 N  N   . ASP A 1 346 ? -22.968 9.219   -60.343  1.00 87.88  ?  344 ASP A N   1 
ATOM   2449 C  CA  . ASP A 1 346 ? -23.487 8.600   -59.125  1.00 89.06  ?  344 ASP A CA  1 
ATOM   2450 C  C   . ASP A 1 346 ? -23.190 7.108   -59.062  1.00 90.51  ?  344 ASP A C   1 
ATOM   2451 O  O   . ASP A 1 346 ? -24.109 6.289   -58.949  1.00 100.70 ?  344 ASP A O   1 
ATOM   2452 C  CB  . ASP A 1 346 ? -24.997 8.827   -58.993  1.00 92.42  ?  344 ASP A CB  1 
ATOM   2453 C  CG  . ASP A 1 346 ? -25.342 9.895   -57.967  1.00 101.17 ?  344 ASP A CG  1 
ATOM   2454 O  OD1 . ASP A 1 346 ? -24.414 10.435  -57.329  1.00 106.73 ?  344 ASP A OD1 1 
ATOM   2455 O  OD2 . ASP A 1 346 ? -26.546 10.177  -57.782  1.00 105.95 -1 344 ASP A OD2 1 
ATOM   2456 N  N   . LYS A 1 347 ? -21.912 6.749   -59.129  1.00 88.37  ?  345 LYS A N   1 
ATOM   2457 C  CA  . LYS A 1 347 ? -21.496 5.356   -59.049  1.00 91.41  ?  345 LYS A CA  1 
ATOM   2458 C  C   . LYS A 1 347 ? -20.187 5.193   -58.292  1.00 91.54  ?  345 LYS A C   1 
ATOM   2459 O  O   . LYS A 1 347 ? -19.729 4.059   -58.118  1.00 91.84  ?  345 LYS A O   1 
ATOM   2460 C  CB  . LYS A 1 347 ? -21.371 4.738   -60.453  1.00 86.34  ?  345 LYS A CB  1 
ATOM   2461 C  CG  . LYS A 1 347 ? -22.700 4.599   -61.188  1.00 90.83  ?  345 LYS A CG  1 
ATOM   2462 C  CD  . LYS A 1 347 ? -22.497 4.112   -62.616  1.00 94.86  ?  345 LYS A CD  1 
ATOM   2463 C  CE  . LYS A 1 347 ? -23.820 3.965   -63.353  1.00 92.95  ?  345 LYS A CE  1 
ATOM   2464 N  NZ  . LYS A 1 347 ? -24.599 5.235   -63.363  1.00 93.48  ?  345 LYS A NZ  1 
ATOM   2465 N  N   . PHE A 1 348 ? -19.588 6.283   -57.825  1.00 89.30  ?  346 PHE A N   1 
ATOM   2466 C  CA  . PHE A 1 348 ? -18.380 6.291   -57.018  1.00 90.23  ?  346 PHE A CA  1 
ATOM   2467 C  C   . PHE A 1 348 ? -18.711 6.915   -55.670  1.00 96.95  ?  346 PHE A C   1 
ATOM   2468 O  O   . PHE A 1 348 ? -19.778 7.506   -55.479  1.00 95.74  ?  346 PHE A O   1 
ATOM   2469 C  CB  . PHE A 1 348 ? -17.259 7.113   -57.675  1.00 88.62  ?  346 PHE A CB  1 
ATOM   2470 C  CG  . PHE A 1 348 ? -16.648 6.485   -58.899  1.00 88.81  ?  346 PHE A CG  1 
ATOM   2471 C  CD1 . PHE A 1 348 ? -16.686 5.117   -59.106  1.00 85.06  ?  346 PHE A CD1 1 
ATOM   2472 C  CD2 . PHE A 1 348 ? -16.009 7.283   -59.837  1.00 80.70  ?  346 PHE A CD2 1 
ATOM   2473 C  CE1 . PHE A 1 348 ? -16.108 4.560   -60.237  1.00 89.74  ?  346 PHE A CE1 1 
ATOM   2474 C  CE2 . PHE A 1 348 ? -15.431 6.734   -60.964  1.00 74.63  ?  346 PHE A CE2 1 
ATOM   2475 C  CZ  . PHE A 1 348 ? -15.480 5.372   -61.167  1.00 77.93  ?  346 PHE A CZ  1 
ATOM   2476 N  N   . LYS A 1 349 ? -17.792 6.774   -54.720  1.00 96.62  ?  347 LYS A N   1 
ATOM   2477 C  CA  . LYS A 1 349 ? -17.963 7.448   -53.442  1.00 100.53 ?  347 LYS A CA  1 
ATOM   2478 C  C   . LYS A 1 349 ? -17.933 8.953   -53.678  1.00 97.88  ?  347 LYS A C   1 
ATOM   2479 O  O   . LYS A 1 349 ? -17.077 9.460   -54.409  1.00 93.74  ?  347 LYS A O   1 
ATOM   2480 C  CB  . LYS A 1 349 ? -16.867 7.030   -52.464  1.00 103.39 ?  347 LYS A CB  1 
ATOM   2481 N  N   . VAL A 1 350 ? -18.868 9.672   -53.065  1.00 102.99 ?  348 VAL A N   1 
ATOM   2482 C  CA  . VAL A 1 350 ? -18.999 11.111  -53.267  1.00 100.11 ?  348 VAL A CA  1 
ATOM   2483 C  C   . VAL A 1 350 ? -18.259 11.843  -52.156  1.00 101.13 ?  348 VAL A C   1 
ATOM   2484 O  O   . VAL A 1 350 ? -18.456 11.553  -50.969  1.00 106.19 ?  348 VAL A O   1 
ATOM   2485 C  CB  . VAL A 1 350 ? -20.477 11.534  -53.322  1.00 100.22 ?  348 VAL A CB  1 
ATOM   2486 C  CG1 . VAL A 1 350 ? -20.591 13.019  -53.618  1.00 98.13  ?  348 VAL A CG1 1 
ATOM   2487 C  CG2 . VAL A 1 350 ? -21.220 10.723  -54.376  1.00 98.37  ?  348 VAL A CG2 1 
ATOM   2488 N  N   . ASN A 1 351 ? -17.401 12.789  -52.546  1.00 103.61 ?  349 ASN A N   1 
ATOM   2489 C  CA  . ASN A 1 351 ? -16.679 13.657  -51.611  1.00 101.52 ?  349 ASN A CA  1 
ATOM   2490 C  C   . ASN A 1 351 ? -15.798 12.855  -50.652  1.00 103.80 ?  349 ASN A C   1 
ATOM   2491 O  O   . ASN A 1 351 ? -15.874 13.004  -49.430  1.00 108.30 ?  349 ASN A O   1 
ATOM   2492 C  CB  . ASN A 1 351 ? -17.643 14.562  -50.840  1.00 103.55 ?  349 ASN A CB  1 
ATOM   2493 C  CG  . ASN A 1 351 ? -18.485 15.433  -51.752  1.00 100.59 ?  349 ASN A CG  1 
ATOM   2494 O  OD1 . ASN A 1 351 ? -17.959 16.132  -52.619  1.00 103.83 ?  349 ASN A OD1 1 
ATOM   2495 N  ND2 . ASN A 1 351 ? -19.796 15.409  -51.550  1.00 103.19 ?  349 ASN A ND2 1 
ATOM   2496 N  N   . SER A 1 352 ? -14.940 12.006  -51.215  1.00 103.96 ?  350 SER A N   1 
ATOM   2497 C  CA  . SER A 1 352 ? -13.965 11.238  -50.439  1.00 104.16 ?  350 SER A CA  1 
ATOM   2498 C  C   . SER A 1 352 ? -12.575 11.528  -51.002  1.00 100.99 ?  350 SER A C   1 
ATOM   2499 O  O   . SER A 1 352 ? -12.052 10.782  -51.832  1.00 99.30  ?  350 SER A O   1 
ATOM   2500 C  CB  . SER A 1 352 ? -14.293 9.738   -50.471  1.00 105.65 ?  350 SER A CB  1 
ATOM   2501 O  OG  . SER A 1 352 ? -13.318 8.987   -49.768  1.00 108.59 ?  350 SER A OG  1 
ATOM   2502 N  N   . THR A 1 353 ? -11.976 12.625  -50.533  1.00 101.75 ?  351 THR A N   1 
ATOM   2503 C  CA  . THR A 1 353 ? -10.671 13.049  -51.029  1.00 99.25  ?  351 THR A CA  1 
ATOM   2504 C  C   . THR A 1 353 ? -9.577  12.031  -50.734  1.00 101.04 ?  351 THR A C   1 
ATOM   2505 O  O   . THR A 1 353 ? -8.499  12.101  -51.336  1.00 98.81  ?  351 THR A O   1 
ATOM   2506 C  CB  . THR A 1 353 ? -10.302 14.401  -50.411  1.00 100.79 ?  351 THR A CB  1 
ATOM   2507 O  OG1 . THR A 1 353 ? -11.379 15.325  -50.610  1.00 99.72  ?  351 THR A OG1 1 
ATOM   2508 C  CG2 . THR A 1 353 ? -9.038  14.959  -51.045  1.00 103.44 ?  351 THR A CG2 1 
ATOM   2509 N  N   . LEU A 1 354 ? -9.832  11.085  -49.832  1.00 105.31 ?  352 LEU A N   1 
ATOM   2510 C  CA  . LEU A 1 354 ? -8.821  10.133  -49.394  1.00 108.14 ?  352 LEU A CA  1 
ATOM   2511 C  C   . LEU A 1 354 ? -8.580  9.006   -50.389  1.00 105.16 ?  352 LEU A C   1 
ATOM   2512 O  O   . LEU A 1 354 ? -7.616  8.252   -50.222  1.00 111.77 ?  352 LEU A O   1 
ATOM   2513 C  CB  . LEU A 1 354 ? -9.229  9.543   -48.042  1.00 113.97 ?  352 LEU A CB  1 
ATOM   2514 C  CG  . LEU A 1 354 ? -9.444  10.573  -46.930  1.00 117.67 ?  352 LEU A CG  1 
ATOM   2515 C  CD1 . LEU A 1 354 ? -9.818  9.897   -45.616  1.00 124.01 ?  352 LEU A CD1 1 
ATOM   2516 C  CD2 . LEU A 1 354 ? -8.219  11.460  -46.762  1.00 117.77 ?  352 LEU A CD2 1 
ATOM   2517 N  N   . GLU A 1 355 ? -9.415  8.876   -51.415  1.00 101.28 ?  353 GLU A N   1 
ATOM   2518 C  CA  . GLU A 1 355 ? -9.288  7.761   -52.339  1.00 100.25 ?  353 GLU A CA  1 
ATOM   2519 C  C   . GLU A 1 355 ? -8.082  7.947   -53.258  1.00 95.71  ?  353 GLU A C   1 
ATOM   2520 O  O   . GLU A 1 355 ? -7.603  9.061   -53.493  1.00 93.82  ?  353 GLU A O   1 
ATOM   2521 C  CB  . GLU A 1 355 ? -10.565 7.605   -53.167  1.00 96.28  ?  353 GLU A CB  1 
ATOM   2522 C  CG  . GLU A 1 355 ? -11.824 7.358   -52.339  1.00 100.32 ?  353 GLU A CG  1 
ATOM   2523 C  CD  . GLU A 1 355 ? -11.825 6.011   -51.634  1.00 107.59 ?  353 GLU A CD  1 
ATOM   2524 O  OE1 . GLU A 1 355 ? -10.844 5.251   -51.782  1.00 104.45 ?  353 GLU A OE1 1 
ATOM   2525 O  OE2 . GLU A 1 355 ? -12.812 5.713   -50.927  1.00 111.70 -1 353 GLU A OE2 1 
ATOM   2526 N  N   . GLN A 1 356 ? -7.594  6.821   -53.785  1.00 95.30  ?  354 GLN A N   1 
ATOM   2527 C  CA  . GLN A 1 356 ? -6.449  6.851   -54.688  1.00 93.20  ?  354 GLN A CA  1 
ATOM   2528 C  C   . GLN A 1 356 ? -6.797  7.511   -56.014  1.00 87.25  ?  354 GLN A C   1 
ATOM   2529 O  O   . GLN A 1 356 ? -5.916  8.062   -56.684  1.00 84.94  ?  354 GLN A O   1 
ATOM   2530 C  CB  . GLN A 1 356 ? -5.948  5.427   -54.927  1.00 93.90  ?  354 GLN A CB  1 
ATOM   2531 C  CG  . GLN A 1 356 ? -4.706  5.319   -55.792  1.00 92.00  ?  354 GLN A CG  1 
ATOM   2532 C  CD  . GLN A 1 356 ? -4.356  3.879   -56.116  1.00 93.26  ?  354 GLN A CD  1 
ATOM   2533 O  OE1 . GLN A 1 356 ? -5.044  2.949   -55.692  1.00 95.55  ?  354 GLN A OE1 1 
ATOM   2534 N  NE2 . GLN A 1 356 ? -3.284  3.686   -56.876  1.00 92.08  ?  354 GLN A NE2 1 
ATOM   2535 N  N   . TYR A 1 357 ? -8.070  7.481   -56.395  1.00 85.66  ?  355 TYR A N   1 
ATOM   2536 C  CA  . TYR A 1 357 ? -8.548  8.023   -57.662  1.00 81.53  ?  355 TYR A CA  1 
ATOM   2537 C  C   . TYR A 1 357 ? -9.602  9.072   -57.343  1.00 80.55  ?  355 TYR A C   1 
ATOM   2538 O  O   . TYR A 1 357 ? -10.696 8.738   -56.877  1.00 90.63  ?  355 TYR A O   1 
ATOM   2539 C  CB  . TYR A 1 357 ? -9.099  6.905   -58.545  1.00 80.22  ?  355 TYR A CB  1 
ATOM   2540 C  CG  . TYR A 1 357 ? -8.030  5.910   -58.931  1.00 83.00  ?  355 TYR A CG  1 
ATOM   2541 C  CD1 . TYR A 1 357 ? -6.737  6.335   -59.202  1.00 85.47  ?  355 TYR A CD1 1 
ATOM   2542 C  CD2 . TYR A 1 357 ? -8.293  4.547   -58.969  1.00 91.54  ?  355 TYR A CD2 1 
ATOM   2543 C  CE1 . TYR A 1 357 ? -5.744  5.439   -59.537  1.00 87.06  ?  355 TYR A CE1 1 
ATOM   2544 C  CE2 . TYR A 1 357 ? -7.302  3.639   -59.303  1.00 88.79  ?  355 TYR A CE2 1 
ATOM   2545 C  CZ  . TYR A 1 357 ? -6.029  4.094   -59.585  1.00 85.33  ?  355 TYR A CZ  1 
ATOM   2546 O  OH  . TYR A 1 357 ? -5.034  3.207   -59.921  1.00 84.37  ?  355 TYR A OH  1 
ATOM   2547 N  N   . VAL A 1 358 ? -9.273  10.336  -57.593  1.00 78.58  ?  356 VAL A N   1 
ATOM   2548 C  CA  . VAL A 1 358 ? -10.163 11.456  -57.320  1.00 78.43  ?  356 VAL A CA  1 
ATOM   2549 C  C   . VAL A 1 358 ? -10.531 12.118  -58.639  1.00 77.60  ?  356 VAL A C   1 
ATOM   2550 O  O   . VAL A 1 358 ? -9.651  12.508  -59.416  1.00 71.30  ?  356 VAL A O   1 
ATOM   2551 C  CB  . VAL A 1 358 ? -9.515  12.467  -56.357  1.00 80.77  ?  356 VAL A CB  1 
ATOM   2552 C  CG1 . VAL A 1 358 ? -10.039 13.869  -56.622  1.00 82.58  ?  356 VAL A CG1 1 
ATOM   2553 C  CG2 . VAL A 1 358 ? -9.764  12.057  -54.913  1.00 89.68  ?  356 VAL A CG2 1 
ATOM   2554 N  N   . PHE A 1 359 ? -11.831 12.232  -58.889  1.00 73.21  ?  357 PHE A N   1 
ATOM   2555 C  CA  . PHE A 1 359 ? -12.375 12.871  -60.081  1.00 74.89  ?  357 PHE A CA  1 
ATOM   2556 C  C   . PHE A 1 359 ? -13.044 14.162  -59.623  1.00 78.52  ?  357 PHE A C   1 
ATOM   2557 O  O   . PHE A 1 359 ? -14.055 14.122  -58.913  1.00 72.77  ?  357 PHE A O   1 
ATOM   2558 C  CB  . PHE A 1 359 ? -13.354 11.928  -60.775  1.00 71.92  ?  357 PHE A CB  1 
ATOM   2559 C  CG  . PHE A 1 359 ? -12.726 10.633  -61.220  1.00 74.23  ?  357 PHE A CG  1 
ATOM   2560 C  CD1 . PHE A 1 359 ? -12.554 9.590   -60.320  1.00 77.14  ?  357 PHE A CD1 1 
ATOM   2561 C  CD2 . PHE A 1 359 ? -12.312 10.454  -62.528  1.00 69.68  ?  357 PHE A CD2 1 
ATOM   2562 C  CE1 . PHE A 1 359 ? -11.976 8.398   -60.715  1.00 76.62  ?  357 PHE A CE1 1 
ATOM   2563 C  CE2 . PHE A 1 359 ? -11.735 9.261   -62.930  1.00 73.32  ?  357 PHE A CE2 1 
ATOM   2564 C  CZ  . PHE A 1 359 ? -11.567 8.233   -62.023  1.00 76.15  ?  357 PHE A CZ  1 
ATOM   2565 N  N   . CYS A 1 360 ? -12.475 15.305  -60.005  1.00 69.05  ?  358 CYS A N   1 
ATOM   2566 C  CA  . CYS A 1 360 ? -12.986 16.581  -59.525  1.00 70.25  ?  358 CYS A CA  1 
ATOM   2567 C  C   . CYS A 1 360 ? -12.799 17.687  -60.554  1.00 70.46  ?  358 CYS A C   1 
ATOM   2568 O  O   . CYS A 1 360 ? -11.751 17.775  -61.200  1.00 63.92  ?  358 CYS A O   1 
ATOM   2569 C  CB  . CYS A 1 360 ? -12.291 16.979  -58.219  1.00 74.65  ?  358 CYS A CB  1 
ATOM   2570 S  SG  . CYS A 1 360 ? -13.032 18.389  -57.382  1.00 81.13  ?  358 CYS A SG  1 
ATOM   2571 N  N   . THR A 1 361 ? -13.823 18.526  -60.699  1.00 74.04  ?  359 THR A N   1 
ATOM   2572 C  CA  . THR A 1 361 ? -13.704 19.720  -61.521  1.00 67.17  ?  359 THR A CA  1 
ATOM   2573 C  C   . THR A 1 361 ? -12.713 20.693  -60.878  1.00 68.04  ?  359 THR A C   1 
ATOM   2574 O  O   . THR A 1 361 ? -12.474 20.666  -59.667  1.00 68.18  ?  359 THR A O   1 
ATOM   2575 C  CB  . THR A 1 361 ? -15.069 20.387  -61.707  1.00 64.48  ?  359 THR A CB  1 
ATOM   2576 O  OG1 . THR A 1 361 ? -15.601 20.763  -60.429  1.00 69.77  ?  359 THR A OG1 1 
ATOM   2577 C  CG2 . THR A 1 361 ? -16.039 19.436  -62.393  1.00 62.52  ?  359 THR A CG2 1 
ATOM   2578 N  N   . VAL A 1 362 ? -12.135 21.568  -61.707  1.00 65.59  ?  360 VAL A N   1 
ATOM   2579 C  CA  . VAL A 1 362 ? -11.083 22.461  -61.223  1.00 72.01  ?  360 VAL A CA  1 
ATOM   2580 C  C   . VAL A 1 362 ? -11.581 23.339  -60.081  1.00 67.32  ?  360 VAL A C   1 
ATOM   2581 O  O   . VAL A 1 362 ? -10.880 23.529  -59.079  1.00 70.25  ?  360 VAL A O   1 
ATOM   2582 C  CB  . VAL A 1 362 ? -10.525 23.314  -62.376  1.00 68.69  ?  360 VAL A CB  1 
ATOM   2583 C  CG1 . VAL A 1 362 ? -9.538  24.338  -61.833  1.00 70.27  ?  360 VAL A CG1 1 
ATOM   2584 C  CG2 . VAL A 1 362 ? -9.857  22.432  -63.413  1.00 63.17  ?  360 VAL A CG2 1 
ATOM   2585 N  N   . ASN A 1 363 ? -12.794 23.885  -60.204  1.00 67.39  ?  361 ASN A N   1 
ATOM   2586 C  CA  . ASN A 1 363 ? -13.277 24.830  -59.202  1.00 74.47  ?  361 ASN A CA  1 
ATOM   2587 C  C   . ASN A 1 363 ? -13.505 24.173  -57.849  1.00 79.66  ?  361 ASN A C   1 
ATOM   2588 O  O   . ASN A 1 363 ? -13.471 24.864  -56.825  1.00 78.29  ?  361 ASN A O   1 
ATOM   2589 C  CB  . ASN A 1 363 ? -14.566 25.504  -59.676  1.00 81.29  ?  361 ASN A CB  1 
ATOM   2590 C  CG  . ASN A 1 363 ? -14.314 26.569  -60.726  1.00 76.53  ?  361 ASN A CG  1 
ATOM   2591 O  OD1 . ASN A 1 363 ? -13.500 27.471  -60.529  1.00 85.53  ?  361 ASN A OD1 1 
ATOM   2592 N  ND2 . ASN A 1 363 ? -15.021 26.474  -61.846  1.00 79.24  ?  361 ASN A ND2 1 
ATOM   2593 N  N   . ALA A 1 364 ? -13.733 22.864  -57.824  1.00 79.81  ?  362 ALA A N   1 
ATOM   2594 C  CA  . ALA A 1 364 ? -13.986 22.135  -56.592  1.00 78.43  ?  362 ALA A CA  1 
ATOM   2595 C  C   . ALA A 1 364 ? -12.755 21.384  -56.110  1.00 79.37  ?  362 ALA A C   1 
ATOM   2596 O  O   . ALA A 1 364 ? -12.863 20.544  -55.212  1.00 82.35  ?  362 ALA A O   1 
ATOM   2597 C  CB  . ALA A 1 364 ? -15.152 21.163  -56.786  1.00 78.37  ?  362 ALA A CB  1 
ATOM   2598 N  N   . LEU A 1 365 ? -11.592 21.671  -56.683  1.00 77.26  ?  363 LEU A N   1 
ATOM   2599 C  CA  . LEU A 1 365 ? -10.392 20.938  -56.320  1.00 78.26  ?  363 LEU A CA  1 
ATOM   2600 C  C   . LEU A 1 365 ? -10.068 21.164  -54.848  1.00 87.31  ?  363 LEU A C   1 
ATOM   2601 O  O   . LEU A 1 365 ? -10.160 22.294  -54.354  1.00 85.09  ?  363 LEU A O   1 
ATOM   2602 C  CB  . LEU A 1 365 ? -9.205  21.376  -57.179  1.00 75.70  ?  363 LEU A CB  1 
ATOM   2603 C  CG  . LEU A 1 365 ? -9.019  20.702  -58.540  1.00 79.26  ?  363 LEU A CG  1 
ATOM   2604 C  CD1 . LEU A 1 365 ? -7.746  21.204  -59.207  1.00 74.46  ?  363 LEU A CD1 1 
ATOM   2605 C  CD2 . LEU A 1 365 ? -8.999  19.186  -58.403  1.00 71.88  ?  363 LEU A CD2 1 
ATOM   2606 N  N   . PRO A 1 366 ? -9.687  20.123  -54.121  1.00 89.20  ?  364 PRO A N   1 
ATOM   2607 C  CA  . PRO A 1 366 ? -9.217  20.303  -52.751  1.00 90.60  ?  364 PRO A CA  1 
ATOM   2608 C  C   . PRO A 1 366 ? -7.729  20.628  -52.775  1.00 90.95  ?  364 PRO A C   1 
ATOM   2609 O  O   . PRO A 1 366 ? -7.046  20.477  -53.790  1.00 91.34  ?  364 PRO A O   1 
ATOM   2610 C  CB  . PRO A 1 366 ? -9.478  18.929  -52.129  1.00 93.39  ?  364 PRO A CB  1 
ATOM   2611 C  CG  . PRO A 1 366 ? -9.158  18.001  -53.261  1.00 88.98  ?  364 PRO A CG  1 
ATOM   2612 C  CD  . PRO A 1 366 ? -9.720  18.697  -54.497  1.00 88.09  ?  364 PRO A CD  1 
ATOM   2613 N  N   . GLU A 1 367 ? -7.239  21.094  -51.634  1.00 95.39  ?  365 GLU A N   1 
ATOM   2614 C  CA  . GLU A 1 367 ? -5.816  21.372  -51.482  1.00 101.61 ?  365 GLU A CA  1 
ATOM   2615 C  C   . GLU A 1 367 ? -5.180  20.060  -51.048  1.00 98.74  ?  365 GLU A C   1 
ATOM   2616 O  O   . GLU A 1 367 ? -5.276  19.664  -49.884  1.00 103.12 ?  365 GLU A O   1 
ATOM   2617 C  CB  . GLU A 1 367 ? -5.603  22.496  -50.477  1.00 100.99 ?  365 GLU A CB  1 
ATOM   2618 C  CG  . GLU A 1 367 ? -6.666  23.576  -50.608  1.00 100.17 ?  365 GLU A CG  1 
ATOM   2619 C  CD  . GLU A 1 367 ? -6.197  24.939  -50.154  1.00 103.39 ?  365 GLU A CD  1 
ATOM   2620 O  OE1 . GLU A 1 367 ? -5.018  25.067  -49.765  1.00 105.21 ?  365 GLU A OE1 1 
ATOM   2621 O  OE2 . GLU A 1 367 ? -7.012  25.886  -50.194  1.00 105.75 -1 365 GLU A OE2 1 
ATOM   2622 N  N   . THR A 1 368 ? -4.533  19.376  -51.987  1.00 95.75  ?  366 THR A N   1 
ATOM   2623 C  CA  . THR A 1 368 ? -4.026  18.041  -51.712  1.00 98.01  ?  366 THR A CA  1 
ATOM   2624 C  C   . THR A 1 368 ? -2.732  17.814  -52.483  1.00 98.31  ?  366 THR A C   1 
ATOM   2625 O  O   . THR A 1 368 ? -2.138  18.743  -53.038  1.00 94.46  ?  366 THR A O   1 
ATOM   2626 C  CB  . THR A 1 368 ? -5.083  16.988  -52.071  1.00 102.37 ?  366 THR A CB  1 
ATOM   2627 O  OG1 . THR A 1 368 ? -4.587  15.680  -51.758  1.00 101.69 ?  366 THR A OG1 1 
ATOM   2628 C  CG2 . THR A 1 368 ? -5.422  17.057  -53.556  1.00 92.34  ?  366 THR A CG2 1 
ATOM   2629 N  N   . THR A 1 369 ? -2.309  16.553  -52.511  1.00 98.46  ?  367 THR A N   1 
ATOM   2630 C  CA  . THR A 1 369 ? -1.087  16.105  -53.154  1.00 95.88  ?  367 THR A CA  1 
ATOM   2631 C  C   . THR A 1 369 ? -1.402  14.867  -53.981  1.00 94.46  ?  367 THR A C   1 
ATOM   2632 O  O   . THR A 1 369 ? -2.395  14.174  -53.740  1.00 92.96  ?  367 THR A O   1 
ATOM   2633 C  CB  . THR A 1 369 ? 0.006   15.795  -52.123  1.00 101.22 ?  367 THR A CB  1 
ATOM   2634 O  OG1 . THR A 1 369 ? 1.086   15.101  -52.758  1.00 105.56 ?  367 THR A OG1 1 
ATOM   2635 C  CG2 . THR A 1 369 ? -0.556  14.940  -50.994  1.00 104.87 ?  367 THR A CG2 1 
ATOM   2636 N  N   . ALA A 1 370 ? -0.557  14.593  -54.970  1.00 90.98  ?  368 ALA A N   1 
ATOM   2637 C  CA  . ALA A 1 370 ? -0.733  13.392  -55.774  1.00 88.86  ?  368 ALA A CA  1 
ATOM   2638 C  C   . ALA A 1 370 ? 0.552   13.095  -56.532  1.00 88.40  ?  368 ALA A C   1 
ATOM   2639 O  O   . ALA A 1 370 ? 1.468   13.918  -56.597  1.00 89.30  ?  368 ALA A O   1 
ATOM   2640 C  CB  . ALA A 1 370 ? -1.912  13.538  -56.742  1.00 85.72  ?  368 ALA A CB  1 
ATOM   2641 N  N   . ASP A 1 371 ? 0.601   11.896  -57.109  1.00 87.44  ?  369 ASP A N   1 
ATOM   2642 C  CA  . ASP A 1 371 ? 1.745   11.448  -57.892  1.00 87.33  ?  369 ASP A CA  1 
ATOM   2643 C  C   . ASP A 1 371 ? 1.630   11.908  -59.339  1.00 89.78  ?  369 ASP A C   1 
ATOM   2644 O  O   . ASP A 1 371 ? 2.613   12.373  -59.926  1.00 86.30  ?  369 ASP A O   1 
ATOM   2645 C  CB  . ASP A 1 371 ? 1.863   9.921   -57.836  1.00 88.92  ?  369 ASP A CB  1 
ATOM   2646 C  CG  . ASP A 1 371 ? 1.840   9.382   -56.415  1.00 96.32  ?  369 ASP A CG  1 
ATOM   2647 O  OD1 . ASP A 1 371 ? 2.761   9.704   -55.635  1.00 97.88  ?  369 ASP A OD1 1 
ATOM   2648 O  OD2 . ASP A 1 371 ? 0.900   8.629   -56.079  1.00 97.03  -1 369 ASP A OD2 1 
ATOM   2649 N  N   . ILE A 1 372 ? 0.436   11.789  -59.916  1.00 79.60  ?  370 ILE A N   1 
ATOM   2650 C  CA  . ILE A 1 372 ? 0.146   12.229  -61.274  1.00 79.77  ?  370 ILE A CA  1 
ATOM   2651 C  C   . ILE A 1 372 ? -1.173  12.985  -61.254  1.00 77.95  ?  370 ILE A C   1 
ATOM   2652 O  O   . ILE A 1 372 ? -2.159  12.506  -60.682  1.00 79.97  ?  370 ILE A O   1 
ATOM   2653 C  CB  . ILE A 1 372 ? 0.062   11.054  -62.269  1.00 81.47  ?  370 ILE A CB  1 
ATOM   2654 C  CG1 . ILE A 1 372 ? 1.274   10.133  -62.144  1.00 79.85  ?  370 ILE A CG1 1 
ATOM   2655 C  CG2 . ILE A 1 372 ? -0.083  11.574  -63.694  1.00 79.02  ?  370 ILE A CG2 1 
ATOM   2656 C  CD1 . ILE A 1 372 ? 1.172   8.895   -63.010  1.00 74.61  ?  370 ILE A CD1 1 
ATOM   2657 N  N   . VAL A 1 373 ? -1.186  14.169  -61.856  1.00 74.92  ?  371 VAL A N   1 
ATOM   2658 C  CA  . VAL A 1 373 ? -2.407  14.934  -62.073  1.00 69.45  ?  371 VAL A CA  1 
ATOM   2659 C  C   . VAL A 1 373 ? -2.698  14.915  -63.565  1.00 63.42  ?  371 VAL A C   1 
ATOM   2660 O  O   . VAL A 1 373 ? -1.813  15.206  -64.379  1.00 62.51  ?  371 VAL A O   1 
ATOM   2661 C  CB  . VAL A 1 373 ? -2.282  16.376  -61.551  1.00 68.54  ?  371 VAL A CB  1 
ATOM   2662 C  CG1 . VAL A 1 373 ? -3.297  17.274  -62.242  1.00 69.29  ?  371 VAL A CG1 1 
ATOM   2663 C  CG2 . VAL A 1 373 ? -2.476  16.413  -60.043  1.00 72.31  ?  371 VAL A CG2 1 
ATOM   2664 N  N   . VAL A 1 374 ? -3.926  14.551  -63.923  1.00 67.65  ?  372 VAL A N   1 
ATOM   2665 C  CA  . VAL A 1 374 ? -4.376  14.518  -65.310  1.00 63.96  ?  372 VAL A CA  1 
ATOM   2666 C  C   . VAL A 1 374 ? -5.418  15.613  -65.498  1.00 61.79  ?  372 VAL A C   1 
ATOM   2667 O  O   . VAL A 1 374 ? -6.491  15.570  -64.882  1.00 64.48  ?  372 VAL A O   1 
ATOM   2668 C  CB  . VAL A 1 374 ? -4.939  13.140  -65.691  1.00 67.09  ?  372 VAL A CB  1 
ATOM   2669 C  CG1 . VAL A 1 374 ? -5.494  13.166  -67.108  1.00 60.34  ?  372 VAL A CG1 1 
ATOM   2670 C  CG2 . VAL A 1 374 ? -3.866  12.070  -65.549  1.00 63.36  ?  372 VAL A CG2 1 
ATOM   2671 N  N   . PHE A 1 375 ? -5.101  16.600  -66.334  1.00 56.72  ?  373 PHE A N   1 
ATOM   2672 C  CA  . PHE A 1 375 ? -6.021  17.678  -66.686  1.00 59.94  ?  373 PHE A CA  1 
ATOM   2673 C  C   . PHE A 1 375 ? -6.439  17.443  -68.134  1.00 59.63  ?  373 PHE A C   1 
ATOM   2674 O  O   . PHE A 1 375 ? -5.614  17.554  -69.047  1.00 52.23  ?  373 PHE A O   1 
ATOM   2675 C  CB  . PHE A 1 375 ? -5.335  19.036  -66.513  1.00 56.87  ?  373 PHE A CB  1 
ATOM   2676 C  CG  . PHE A 1 375 ? -6.278  20.213  -66.420  1.00 55.94  ?  373 PHE A CG  1 
ATOM   2677 C  CD1 . PHE A 1 375 ? -7.582  20.135  -66.878  1.00 58.14  ?  373 PHE A CD1 1 
ATOM   2678 C  CD2 . PHE A 1 375 ? -5.829  21.419  -65.902  1.00 63.88  ?  373 PHE A CD2 1 
ATOM   2679 C  CE1 . PHE A 1 375 ? -8.428  21.232  -66.793  1.00 57.84  ?  373 PHE A CE1 1 
ATOM   2680 C  CE2 . PHE A 1 375 ? -6.666  22.516  -65.820  1.00 65.36  ?  373 PHE A CE2 1 
ATOM   2681 C  CZ  . PHE A 1 375 ? -7.966  22.423  -66.267  1.00 59.19  ?  373 PHE A CZ  1 
ATOM   2682 N  N   . ASP A 1 376 ? -7.717  17.134  -68.344  1.00 62.41  ?  374 ASP A N   1 
ATOM   2683 C  CA  . ASP A 1 376 ? -8.245  16.831  -69.667  1.00 61.04  ?  374 ASP A CA  1 
ATOM   2684 C  C   . ASP A 1 376 ? -9.022  18.029  -70.214  1.00 52.85  ?  374 ASP A C   1 
ATOM   2685 O  O   . ASP A 1 376 ? -9.299  18.997  -69.502  1.00 51.36  ?  374 ASP A O   1 
ATOM   2686 C  CB  . ASP A 1 376 ? -9.128  15.577  -69.599  1.00 61.80  ?  374 ASP A CB  1 
ATOM   2687 C  CG  . ASP A 1 376 ? -9.362  14.940  -70.958  1.00 69.23  ?  374 ASP A CG  1 
ATOM   2688 O  OD1 . ASP A 1 376 ? -8.774  15.410  -71.957  1.00 68.76  ?  374 ASP A OD1 1 
ATOM   2689 O  OD2 . ASP A 1 376 ? -10.128 13.953  -71.021  1.00 74.60  -1 374 ASP A OD2 1 
ATOM   2690 N  N   . GLU A 1 377 ? -9.373  17.955  -71.502  1.00 50.00  ?  375 GLU A N   1 
ATOM   2691 C  CA  . GLU A 1 377 ? -10.127 19.023  -72.170  1.00 50.18  ?  375 GLU A CA  1 
ATOM   2692 C  C   . GLU A 1 377 ? -9.398  20.357  -72.020  1.00 47.17  ?  375 GLU A C   1 
ATOM   2693 O  O   . GLU A 1 377 ? -10.002 21.392  -71.731  1.00 46.51  ?  375 GLU A O   1 
ATOM   2694 C  CB  . GLU A 1 377 ? -11.569 19.114  -71.656  1.00 50.69  ?  375 GLU A CB  1 
ATOM   2695 C  CG  . GLU A 1 377 ? -12.563 19.651  -72.697  1.00 57.03  ?  375 GLU A CG  1 
ATOM   2696 C  CD  . GLU A 1 377 ? -14.002 19.719  -72.194  1.00 68.88  ?  375 GLU A CD  1 
ATOM   2697 O  OE1 . GLU A 1 377 ? -14.257 20.405  -71.181  1.00 70.70  ?  375 GLU A OE1 1 
ATOM   2698 O  OE2 . GLU A 1 377 ? -14.885 19.102  -72.831  1.00 64.45  -1 375 GLU A OE2 1 
ATOM   2699 N  N   . ILE A 1 378 ? -8.080  20.328  -72.236  1.00 47.37  ?  376 ILE A N   1 
ATOM   2700 C  CA  . ILE A 1 378 ? -7.238  21.495  -72.001  1.00 51.62  ?  376 ILE A CA  1 
ATOM   2701 C  C   . ILE A 1 378 ? -7.542  22.652  -72.944  1.00 46.12  ?  376 ILE A C   1 
ATOM   2702 O  O   . ILE A 1 378 ? -7.210  23.800  -72.624  1.00 50.23  ?  376 ILE A O   1 
ATOM   2703 C  CB  . ILE A 1 378 ? -5.755  21.087  -72.087  1.00 54.74  ?  376 ILE A CB  1 
ATOM   2704 C  CG1 . ILE A 1 378 ? -4.931  21.870  -71.064  1.00 56.66  ?  376 ILE A CG1 1 
ATOM   2705 C  CG2 . ILE A 1 378 ? -5.222  21.287  -73.497  1.00 55.76  ?  376 ILE A CG2 1 
ATOM   2706 C  CD1 . ILE A 1 378 ? -5.458  21.763  -69.648  1.00 61.18  ?  376 ILE A CD1 1 
ATOM   2707 N  N   . SER A 1 379 ? -8.162  22.399  -74.099  1.00 40.98  ?  377 SER A N   1 
ATOM   2708 C  CA  . SER A 1 379 ? -8.525  23.512  -74.971  1.00 45.81  ?  377 SER A CA  1 
ATOM   2709 C  C   . SER A 1 379 ? -9.536  24.421  -74.285  1.00 49.61  ?  377 SER A C   1 
ATOM   2710 O  O   . SER A 1 379 ? -9.563  25.631  -74.541  1.00 41.83  ?  377 SER A O   1 
ATOM   2711 C  CB  . SER A 1 379 ? -9.067  23.003  -76.309  1.00 42.71  ?  377 SER A CB  1 
ATOM   2712 O  OG  . SER A 1 379 ? -10.331 22.380  -76.166  1.00 42.92  ?  377 SER A OG  1 
ATOM   2713 N  N   . MET A 1 380 ? -10.362 23.857  -73.404  1.00 48.77  ?  378 MET A N   1 
ATOM   2714 C  CA  . MET A 1 380 ? -11.416 24.579  -72.709  1.00 52.25  ?  378 MET A CA  1 
ATOM   2715 C  C   . MET A 1 380 ? -10.917 25.261  -71.445  1.00 51.30  ?  378 MET A C   1 
ATOM   2716 O  O   . MET A 1 380 ? -11.723 25.821  -70.695  1.00 60.07  ?  378 MET A O   1 
ATOM   2717 C  CB  . MET A 1 380 ? -12.549 23.618  -72.342  1.00 54.68  ?  378 MET A CB  1 
ATOM   2718 C  CG  . MET A 1 380 ? -13.313 23.064  -73.521  1.00 54.92  ?  378 MET A CG  1 
ATOM   2719 S  SD  . MET A 1 380 ? -14.314 24.350  -74.277  1.00 59.85  ?  378 MET A SD  1 
ATOM   2720 C  CE  . MET A 1 380 ? -15.504 24.628  -72.969  1.00 47.88  ?  378 MET A CE  1 
ATOM   2721 N  N   . ALA A 1 381 ? -9.615  25.246  -71.204  1.00 51.64  ?  379 ALA A N   1 
ATOM   2722 C  CA  . ALA A 1 381 ? -9.050  25.782  -69.979  1.00 51.92  ?  379 ALA A CA  1 
ATOM   2723 C  C   . ALA A 1 381 ? -8.568  27.206  -70.203  1.00 54.71  ?  379 ALA A C   1 
ATOM   2724 O  O   . ALA A 1 381 ? -8.107  27.564  -71.290  1.00 55.02  ?  379 ALA A O   1 
ATOM   2725 C  CB  . ALA A 1 381 ? -7.889  24.916  -69.483  1.00 51.52  ?  379 ALA A CB  1 
ATOM   2726 N  N   . THR A 1 382 ? -8.695  28.017  -69.162  1.00 58.12  ?  380 THR A N   1 
ATOM   2727 C  CA  . THR A 1 382 ? -8.148  29.362  -69.146  1.00 61.06  ?  380 THR A CA  1 
ATOM   2728 C  C   . THR A 1 382 ? -6.884  29.357  -68.299  1.00 62.18  ?  380 THR A C   1 
ATOM   2729 O  O   . THR A 1 382 ? -6.653  28.449  -67.496  1.00 59.13  ?  380 THR A O   1 
ATOM   2730 C  CB  . THR A 1 382 ? -9.158  30.373  -68.591  1.00 63.61  ?  380 THR A CB  1 
ATOM   2731 O  OG1 . THR A 1 382 ? -9.538  30.000  -67.260  1.00 64.98  ?  380 THR A OG1 1 
ATOM   2732 C  CG2 . THR A 1 382 ? -10.400 30.433  -69.472  1.00 56.94  ?  380 THR A CG2 1 
ATOM   2733 N  N   . ASN A 1 383 ? -6.051  30.378  -68.496  1.00 61.11  ?  381 ASN A N   1 
ATOM   2734 C  CA  . ASN A 1 383 ? -4.848  30.478  -67.682  1.00 59.17  ?  381 ASN A CA  1 
ATOM   2735 C  C   . ASN A 1 383 ? -5.191  30.595  -66.205  1.00 66.42  ?  381 ASN A C   1 
ATOM   2736 O  O   . ASN A 1 383 ? -4.369  30.235  -65.355  1.00 65.18  ?  381 ASN A O   1 
ATOM   2737 C  CB  . ASN A 1 383 ? -3.986  31.643  -68.158  1.00 58.18  ?  381 ASN A CB  1 
ATOM   2738 C  CG  . ASN A 1 383 ? -3.026  31.228  -69.258  1.00 64.05  ?  381 ASN A CG  1 
ATOM   2739 O  OD1 . ASN A 1 383 ? -2.893  30.041  -69.560  1.00 61.61  ?  381 ASN A OD1 1 
ATOM   2740 N  ND2 . ASN A 1 383 ? -2.362  32.201  -69.870  1.00 61.67  ?  381 ASN A ND2 1 
ATOM   2741 N  N   . TYR A 1 384 ? -6.391  31.082  -65.884  1.00 63.79  ?  382 TYR A N   1 
ATOM   2742 C  CA  . TYR A 1 384 ? -6.831  31.105  -64.496  1.00 65.98  ?  382 TYR A CA  1 
ATOM   2743 C  C   . TYR A 1 384 ? -6.975  29.681  -63.973  1.00 67.94  ?  382 TYR A C   1 
ATOM   2744 O  O   . TYR A 1 384 ? -6.465  29.341  -62.898  1.00 67.43  ?  382 TYR A O   1 
ATOM   2745 C  CB  . TYR A 1 384 ? -8.156  31.861  -64.383  1.00 63.02  ?  382 TYR A CB  1 
ATOM   2746 C  CG  . TYR A 1 384 ? -8.532  32.259  -62.973  1.00 72.68  ?  382 TYR A CG  1 
ATOM   2747 C  CD1 . TYR A 1 384 ? -9.277  31.411  -62.163  1.00 69.39  ?  382 TYR A CD1 1 
ATOM   2748 C  CD2 . TYR A 1 384 ? -8.154  33.492  -62.458  1.00 72.29  ?  382 TYR A CD2 1 
ATOM   2749 C  CE1 . TYR A 1 384 ? -9.627  31.777  -60.875  1.00 71.33  ?  382 TYR A CE1 1 
ATOM   2750 C  CE2 . TYR A 1 384 ? -8.497  33.866  -61.172  1.00 73.49  ?  382 TYR A CE2 1 
ATOM   2751 C  CZ  . TYR A 1 384 ? -9.234  33.007  -60.386  1.00 76.89  ?  382 TYR A CZ  1 
ATOM   2752 O  OH  . TYR A 1 384 ? -9.573  33.376  -59.102  1.00 78.32  ?  382 TYR A OH  1 
ATOM   2753 N  N   . ASP A 1 385 ? -7.686  28.837  -64.727  1.00 61.27  ?  383 ASP A N   1 
ATOM   2754 C  CA  . ASP A 1 385 ? -7.843  27.434  -64.356  1.00 70.44  ?  383 ASP A CA  1 
ATOM   2755 C  C   . ASP A 1 385 ? -6.492  26.748  -64.181  1.00 71.73  ?  383 ASP A C   1 
ATOM   2756 O  O   . ASP A 1 385 ? -6.294  25.984  -63.229  1.00 67.02  ?  383 ASP A O   1 
ATOM   2757 C  CB  . ASP A 1 385 ? -8.674  26.707  -65.412  1.00 59.90  ?  383 ASP A CB  1 
ATOM   2758 C  CG  . ASP A 1 385 ? -10.087 27.249  -65.518  1.00 70.09  ?  383 ASP A CG  1 
ATOM   2759 O  OD1 . ASP A 1 385 ? -10.813 27.235  -64.501  1.00 70.32  ?  383 ASP A OD1 1 
ATOM   2760 O  OD2 . ASP A 1 385 ? -10.472 27.683  -66.626  1.00 68.88  -1 383 ASP A OD2 1 
ATOM   2761 N  N   . LEU A 1 386 ? -5.550  27.007  -65.092  1.00 67.24  ?  384 LEU A N   1 
ATOM   2762 C  CA  . LEU A 1 386 ? -4.250  26.347  -65.020  1.00 67.17  ?  384 LEU A CA  1 
ATOM   2763 C  C   . LEU A 1 386 ? -3.526  26.715  -63.734  1.00 68.18  ?  384 LEU A C   1 
ATOM   2764 O  O   . LEU A 1 386 ? -2.850  25.876  -63.127  1.00 71.50  ?  384 LEU A O   1 
ATOM   2765 C  CB  . LEU A 1 386 ? -3.403  26.715  -66.238  1.00 59.88  ?  384 LEU A CB  1 
ATOM   2766 C  CG  . LEU A 1 386 ? -3.867  26.165  -67.588  1.00 66.01  ?  384 LEU A CG  1 
ATOM   2767 C  CD1 . LEU A 1 386 ? -2.866  26.522  -68.672  1.00 73.43  ?  384 LEU A CD1 1 
ATOM   2768 C  CD2 . LEU A 1 386 ? -4.070  24.658  -67.521  1.00 65.58  ?  384 LEU A CD2 1 
ATOM   2769 N  N   . SER A 1 387 ? -3.643  27.974  -63.313  1.00 71.19  ?  385 SER A N   1 
ATOM   2770 C  CA  . SER A 1 387 ? -2.982  28.414  -62.092  1.00 69.70  ?  385 SER A CA  1 
ATOM   2771 C  C   . SER A 1 387 ? -3.628  27.762  -60.875  1.00 76.50  ?  385 SER A C   1 
ATOM   2772 O  O   . SER A 1 387 ? -2.934  27.262  -59.982  1.00 75.62  ?  385 SER A O   1 
ATOM   2773 C  CB  . SER A 1 387 ? -3.035  29.938  -61.990  1.00 71.32  ?  385 SER A CB  1 
ATOM   2774 O  OG  . SER A 1 387 ? -2.587  30.379  -60.722  1.00 75.69  ?  385 SER A OG  1 
ATOM   2775 N  N   . VAL A 1 388 ? -4.963  27.786  -60.816  1.00 73.30  ?  386 VAL A N   1 
ATOM   2776 C  CA  . VAL A 1 388 ? -5.688  27.179  -59.701  1.00 77.41  ?  386 VAL A CA  1 
ATOM   2777 C  C   . VAL A 1 388 ? -5.220  25.747  -59.476  1.00 78.39  ?  386 VAL A C   1 
ATOM   2778 O  O   . VAL A 1 388 ? -5.081  25.292  -58.333  1.00 80.14  ?  386 VAL A O   1 
ATOM   2779 C  CB  . VAL A 1 388 ? -7.206  27.245  -59.955  1.00 70.71  ?  386 VAL A CB  1 
ATOM   2780 C  CG1 . VAL A 1 388 ? -7.956  26.393  -58.941  1.00 74.92  ?  386 VAL A CG1 1 
ATOM   2781 C  CG2 . VAL A 1 388 ? -7.688  28.688  -59.913  1.00 74.59  ?  386 VAL A CG2 1 
ATOM   2782 N  N   . VAL A 1 389 ? -4.965  25.016  -60.563  1.00 70.54  ?  387 VAL A N   1 
ATOM   2783 C  CA  . VAL A 1 389 ? -4.570  23.616  -60.446  1.00 77.09  ?  387 VAL A CA  1 
ATOM   2784 C  C   . VAL A 1 389 ? -3.157  23.512  -59.887  1.00 80.99  ?  387 VAL A C   1 
ATOM   2785 O  O   . VAL A 1 389 ? -2.903  22.776  -58.926  1.00 81.21  ?  387 VAL A O   1 
ATOM   2786 C  CB  . VAL A 1 389 ? -4.691  22.906  -61.806  1.00 70.59  ?  387 VAL A CB  1 
ATOM   2787 C  CG1 . VAL A 1 389 ? -4.016  21.544  -61.752  1.00 73.04  ?  387 VAL A CG1 1 
ATOM   2788 C  CG2 . VAL A 1 389 ? -6.153  22.769  -62.207  1.00 67.52  ?  387 VAL A CG2 1 
ATOM   2789 N  N   . ASN A 1 390 ? -2.213  24.241  -60.486  1.00 80.86  ?  388 ASN A N   1 
ATOM   2790 C  CA  . ASN A 1 390 ? -0.833  24.215  -60.018  1.00 75.39  ?  388 ASN A CA  1 
ATOM   2791 C  C   . ASN A 1 390 ? -0.708  24.665  -58.569  1.00 84.32  ?  388 ASN A C   1 
ATOM   2792 O  O   . ASN A 1 390 ? 0.366   24.512  -57.975  1.00 85.15  ?  388 ASN A O   1 
ATOM   2793 C  CB  . ASN A 1 390 ? 0.029   25.083  -60.932  1.00 77.71  ?  388 ASN A CB  1 
ATOM   2794 C  CG  . ASN A 1 390 ? 0.671   24.283  -62.046  1.00 87.14  ?  388 ASN A CG  1 
ATOM   2795 O  OD1 . ASN A 1 390 ? 0.590   23.054  -62.065  1.00 85.84  ?  388 ASN A OD1 1 
ATOM   2796 N  ND2 . ASN A 1 390 ? 1.280   24.975  -63.001  1.00 88.91  ?  388 ASN A ND2 1 
ATOM   2797 N  N   . ALA A 1 391 ? -1.782  25.197  -57.989  1.00 80.38  ?  389 ALA A N   1 
ATOM   2798 C  CA  . ALA A 1 391 ? -1.804  25.628  -56.600  1.00 88.16  ?  389 ALA A CA  1 
ATOM   2799 C  C   . ALA A 1 391 ? -2.395  24.508  -55.755  1.00 90.40  ?  389 ALA A C   1 
ATOM   2800 O  O   . ALA A 1 391 ? -1.665  23.792  -55.061  1.00 103.81 ?  389 ALA A O   1 
ATOM   2801 C  CB  . ALA A 1 391 ? -2.607  26.921  -56.439  1.00 85.18  ?  389 ALA A CB  1 
ATOM   2802 N  N   . ARG A 1 392 ? -3.721  24.354  -55.807  1.00 85.94  ?  390 ARG A N   1 
ATOM   2803 C  CA  . ARG A 1 392 ? -4.414  23.394  -54.955  1.00 95.15  ?  390 ARG A CA  1 
ATOM   2804 C  C   . ARG A 1 392 ? -3.841  21.982  -55.033  1.00 93.15  ?  390 ARG A C   1 
ATOM   2805 O  O   . ARG A 1 392 ? -4.060  21.187  -54.111  1.00 88.76  ?  390 ARG A O   1 
ATOM   2806 C  CB  . ARG A 1 392 ? -5.902  23.359  -55.328  1.00 83.69  ?  390 ARG A CB  1 
ATOM   2807 C  CG  . ARG A 1 392 ? -6.611  24.698  -55.197  1.00 84.22  ?  390 ARG A CG  1 
ATOM   2808 C  CD  . ARG A 1 392 ? -8.092  24.584  -55.531  1.00 85.67  ?  390 ARG A CD  1 
ATOM   2809 N  NE  . ARG A 1 392 ? -8.753  25.884  -55.514  1.00 89.63  ?  390 ARG A NE  1 
ATOM   2810 C  CZ  . ARG A 1 392 ? -10.036 26.080  -55.788  1.00 88.73  ?  390 ARG A CZ  1 
ATOM   2811 N  NH1 . ARG A 1 392 ? -10.811 25.095  -56.215  1.00 83.89  ?  390 ARG A NH1 1 
ATOM   2812 N  NH2 . ARG A 1 392 ? -10.550 27.300  -55.657  1.00 82.96  ?  390 ARG A NH2 1 
ATOM   2813 N  N   . LEU A 1 393 ? -3.097  21.649  -56.088  1.00 88.30  ?  391 LEU A N   1 
ATOM   2814 C  CA  . LEU A 1 393 ? -2.618  20.285  -56.304  1.00 90.87  ?  391 LEU A CA  1 
ATOM   2815 C  C   . LEU A 1 393 ? -1.109  20.280  -56.509  1.00 90.11  ?  391 LEU A C   1 
ATOM   2816 O  O   . LEU A 1 393 ? -0.624  20.659  -57.580  1.00 85.69  ?  391 LEU A O   1 
ATOM   2817 C  CB  . LEU A 1 393 ? -3.313  19.654  -57.513  1.00 80.14  ?  391 LEU A CB  1 
ATOM   2818 C  CG  . LEU A 1 393 ? -4.636  18.906  -57.345  1.00 83.00  ?  391 LEU A CG  1 
ATOM   2819 C  CD1 . LEU A 1 393 ? -5.644  19.729  -56.564  1.00 90.31  ?  391 LEU A CD1 1 
ATOM   2820 C  CD2 . LEU A 1 393 ? -5.188  18.557  -58.718  1.00 77.29  ?  391 LEU A CD2 1 
ATOM   2821 N  N   . ARG A 1 394 ? -0.370  19.845  -55.493  1.00 88.54  ?  392 ARG A N   1 
ATOM   2822 C  CA  . ARG A 1 394 ? 1.075   19.694  -55.601  1.00 94.06  ?  392 ARG A CA  1 
ATOM   2823 C  C   . ARG A 1 394 ? 1.350   18.241  -55.977  1.00 94.52  ?  392 ARG A C   1 
ATOM   2824 O  O   . ARG A 1 394 ? 0.889   17.324  -55.288  1.00 91.36  ?  392 ARG A O   1 
ATOM   2825 C  CB  . ARG A 1 394 ? 1.747   20.076  -54.281  1.00 96.10  ?  392 ARG A CB  1 
ATOM   2826 C  CG  . ARG A 1 394 ? 3.239   20.344  -54.366  1.00 101.48 ?  392 ARG A CG  1 
ATOM   2827 C  CD  . ARG A 1 394 ? 3.565   21.360  -55.458  1.00 103.54 ?  392 ARG A CD  1 
ATOM   2828 N  NE  . ARG A 1 394 ? 2.768   22.582  -55.391  1.00 103.26 ?  392 ARG A NE  1 
ATOM   2829 C  CZ  . ARG A 1 394 ? 2.755   23.431  -54.371  1.00 105.08 ?  392 ARG A CZ  1 
ATOM   2830 N  NH1 . ARG A 1 394 ? 3.605   23.316  -53.364  1.00 103.72 ?  392 ARG A NH1 1 
ATOM   2831 N  NH2 . ARG A 1 394 ? 1.911   24.460  -54.395  1.00 100.37 ?  392 ARG A NH2 1 
ATOM   2832 N  N   . ALA A 1 395 ? 2.101   18.025  -57.056  1.00 93.01  ?  393 ALA A N   1 
ATOM   2833 C  CA  . ALA A 1 395 ? 2.266   16.666  -57.558  1.00 86.84  ?  393 ALA A CA  1 
ATOM   2834 C  C   . ALA A 1 395 ? 3.611   16.484  -58.246  1.00 87.54  ?  393 ALA A C   1 
ATOM   2835 O  O   . ALA A 1 395 ? 4.316   17.446  -58.563  1.00 92.18  ?  393 ALA A O   1 
ATOM   2836 C  CB  . ALA A 1 395 ? 1.134   16.296  -58.521  1.00 86.43  ?  393 ALA A CB  1 
ATOM   2837 N  N   . LYS A 1 396 ? 3.947   15.212  -58.485  1.00 87.93  ?  394 LYS A N   1 
ATOM   2838 C  CA  . LYS A 1 396 ? 5.216   14.850  -59.102  1.00 89.16  ?  394 LYS A CA  1 
ATOM   2839 C  C   . LYS A 1 396 ? 5.158   14.990  -60.616  1.00 87.28  ?  394 LYS A C   1 
ATOM   2840 O  O   . LYS A 1 396 ? 6.163   15.344  -61.244  1.00 86.74  ?  394 LYS A O   1 
ATOM   2841 C  CB  . LYS A 1 396 ? 5.579   13.401  -58.766  1.00 91.61  ?  394 LYS A CB  1 
ATOM   2842 C  CG  . LYS A 1 396 ? 5.371   12.971  -57.323  1.00 95.57  ?  394 LYS A CG  1 
ATOM   2843 C  CD  . LYS A 1 396 ? 5.642   11.473  -57.187  1.00 97.55  ?  394 LYS A CD  1 
ATOM   2844 C  CE  . LYS A 1 396 ? 5.634   11.004  -55.740  1.00 102.35 ?  394 LYS A CE  1 
ATOM   2845 N  NZ  . LYS A 1 396 ? 6.691   11.655  -54.924  1.00 107.10 ?  394 LYS A NZ  1 
ATOM   2846 N  N   . HIS A 1 397 ? 3.998   14.713  -61.209  1.00 84.38  ?  395 HIS A N   1 
ATOM   2847 C  CA  . HIS A 1 397 ? 3.814   14.721  -62.653  1.00 76.69  ?  395 HIS A CA  1 
ATOM   2848 C  C   . HIS A 1 397 ? 2.424   15.238  -62.985  1.00 81.95  ?  395 HIS A C   1 
ATOM   2849 O  O   . HIS A 1 397 ? 1.431   14.752  -62.435  1.00 83.06  ?  395 HIS A O   1 
ATOM   2850 C  CB  . HIS A 1 397 ? 4.009   13.320  -63.244  1.00 76.73  ?  395 HIS A CB  1 
ATOM   2851 C  CG  . HIS A 1 397 ? 5.369   12.745  -63.002  1.00 80.34  ?  395 HIS A CG  1 
ATOM   2852 N  ND1 . HIS A 1 397 ? 6.448   13.022  -63.812  1.00 80.96  ?  395 HIS A ND1 1 
ATOM   2853 C  CD2 . HIS A 1 397 ? 5.828   11.915  -62.035  1.00 84.32  ?  395 HIS A CD2 1 
ATOM   2854 C  CE1 . HIS A 1 397 ? 7.513   12.384  -63.360  1.00 85.18  ?  395 HIS A CE1 1 
ATOM   2855 N  NE2 . HIS A 1 397 ? 7.163   11.705  -62.282  1.00 87.25  ?  395 HIS A NE2 1 
ATOM   2856 N  N   . TYR A 1 398 ? 2.359   16.219  -63.879  1.00 77.26  ?  396 TYR A N   1 
ATOM   2857 C  CA  . TYR A 1 398 ? 1.104   16.774  -64.368  1.00 73.11  ?  396 TYR A CA  1 
ATOM   2858 C  C   . TYR A 1 398 ? 0.970   16.402  -65.839  1.00 69.05  ?  396 TYR A C   1 
ATOM   2859 O  O   . TYR A 1 398 ? 1.905   16.613  -66.620  1.00 71.54  ?  396 TYR A O   1 
ATOM   2860 C  CB  . TYR A 1 398 ? 1.067   18.298  -64.207  1.00 71.74  ?  396 TYR A CB  1 
ATOM   2861 C  CG  . TYR A 1 398 ? 1.185   18.820  -62.788  1.00 75.90  ?  396 TYR A CG  1 
ATOM   2862 C  CD1 . TYR A 1 398 ? 0.060   18.986  -61.987  1.00 82.30  ?  396 TYR A CD1 1 
ATOM   2863 C  CD2 . TYR A 1 398 ? 2.420   19.179  -62.260  1.00 82.55  ?  396 TYR A CD2 1 
ATOM   2864 C  CE1 . TYR A 1 398 ? 0.167   19.477  -60.692  1.00 82.90  ?  396 TYR A CE1 1 
ATOM   2865 C  CE2 . TYR A 1 398 ? 2.536   19.672  -60.968  1.00 80.06  ?  396 TYR A CE2 1 
ATOM   2866 C  CZ  . TYR A 1 398 ? 1.406   19.818  -60.190  1.00 80.25  ?  396 TYR A CZ  1 
ATOM   2867 O  OH  . TYR A 1 398 ? 1.516   20.306  -58.907  1.00 83.06  ?  396 TYR A OH  1 
ATOM   2868 N  N   . VAL A 1 399 ? -0.177  15.844  -66.218  1.00 64.83  ?  397 VAL A N   1 
ATOM   2869 C  CA  . VAL A 1 399 ? -0.435  15.449  -67.600  1.00 61.16  ?  397 VAL A CA  1 
ATOM   2870 C  C   . VAL A 1 399 ? -1.586  16.286  -68.145  1.00 62.60  ?  397 VAL A C   1 
ATOM   2871 O  O   . VAL A 1 399 ? -2.686  16.284  -67.578  1.00 60.89  ?  397 VAL A O   1 
ATOM   2872 C  CB  . VAL A 1 399 ? -0.743  13.947  -67.714  1.00 65.38  ?  397 VAL A CB  1 
ATOM   2873 C  CG1 . VAL A 1 399 ? -1.088  13.581  -69.148  1.00 58.55  ?  397 VAL A CG1 1 
ATOM   2874 C  CG2 . VAL A 1 399 ? 0.444   13.129  -67.227  1.00 65.88  ?  397 VAL A CG2 1 
ATOM   2875 N  N   . TYR A 1 400 ? -1.329  16.995  -69.247  1.00 58.80  ?  398 TYR A N   1 
ATOM   2876 C  CA  . TYR A 1 400 ? -2.303  17.866  -69.902  1.00 56.11  ?  398 TYR A CA  1 
ATOM   2877 C  C   . TYR A 1 400 ? -2.745  17.207  -71.203  1.00 56.84  ?  398 TYR A C   1 
ATOM   2878 O  O   . TYR A 1 400 ? -1.944  17.055  -72.132  1.00 57.28  ?  398 TYR A O   1 
ATOM   2879 C  CB  . TYR A 1 400 ? -1.710  19.249  -70.163  1.00 56.42  ?  398 TYR A CB  1 
ATOM   2880 C  CG  . TYR A 1 400 ? -1.299  19.988  -68.912  1.00 62.91  ?  398 TYR A CG  1 
ATOM   2881 C  CD1 . TYR A 1 400 ? -2.228  20.702  -68.167  1.00 61.70  ?  398 TYR A CD1 1 
ATOM   2882 C  CD2 . TYR A 1 400 ? 0.017   19.963  -68.469  1.00 60.16  ?  398 TYR A CD2 1 
ATOM   2883 C  CE1 . TYR A 1 400 ? -1.857  21.376  -67.018  1.00 63.60  ?  398 TYR A CE1 1 
ATOM   2884 C  CE2 . TYR A 1 400 ? 0.398   20.634  -67.324  1.00 66.46  ?  398 TYR A CE2 1 
ATOM   2885 C  CZ  . TYR A 1 400 ? -0.542  21.338  -66.601  1.00 65.99  ?  398 TYR A CZ  1 
ATOM   2886 O  OH  . TYR A 1 400 ? -0.163  22.008  -65.460  1.00 71.62  ?  398 TYR A OH  1 
ATOM   2887 N  N   . ILE A 1 401 ? -4.017  16.824  -71.274  1.00 54.75  ?  399 ILE A N   1 
ATOM   2888 C  CA  . ILE A 1 401 ? -4.579  16.133  -72.428  1.00 55.39  ?  399 ILE A CA  1 
ATOM   2889 C  C   . ILE A 1 401 ? -5.612  17.040  -73.081  1.00 58.86  ?  399 ILE A C   1 
ATOM   2890 O  O   . ILE A 1 401 ? -6.488  17.585  -72.398  1.00 56.56  ?  399 ILE A O   1 
ATOM   2891 C  CB  . ILE A 1 401 ? -5.204  14.789  -72.023  1.00 58.32  ?  399 ILE A CB  1 
ATOM   2892 C  CG1 . ILE A 1 401 ? -4.175  13.933  -71.281  1.00 57.39  ?  399 ILE A CG1 1 
ATOM   2893 C  CG2 . ILE A 1 401 ? -5.735  14.058  -73.247  1.00 53.51  ?  399 ILE A CG2 1 
ATOM   2894 C  CD1 . ILE A 1 401 ? -4.701  12.588  -70.843  1.00 57.17  ?  399 ILE A CD1 1 
ATOM   2895 N  N   . GLY A 1 402 ? -5.515  17.200  -74.394  1.00 51.67  ?  400 GLY A N   1 
ATOM   2896 C  CA  . GLY A 1 402 ? -6.534  17.937  -75.112  1.00 54.27  ?  400 GLY A CA  1 
ATOM   2897 C  C   . GLY A 1 402 ? -6.250  17.998  -76.594  1.00 51.89  ?  400 GLY A C   1 
ATOM   2898 O  O   . GLY A 1 402 ? -5.546  17.151  -77.147  1.00 50.99  ?  400 GLY A O   1 
ATOM   2899 N  N   . ASP A 1 403 ? -6.815  19.020  -77.231  1.00 49.80  ?  401 ASP A N   1 
ATOM   2900 C  CA  . ASP A 1 403 ? -6.646  19.237  -78.661  1.00 44.04  ?  401 ASP A CA  1 
ATOM   2901 C  C   . ASP A 1 403 ? -6.867  20.707  -78.984  1.00 42.16  ?  401 ASP A C   1 
ATOM   2902 O  O   . ASP A 1 403 ? -7.992  21.209  -78.859  1.00 37.53  ?  401 ASP A O   1 
ATOM   2903 C  CB  . ASP A 1 403 ? -7.621  18.364  -79.452  1.00 42.25  ?  401 ASP A CB  1 
ATOM   2904 C  CG  . ASP A 1 403 ? -7.339  18.369  -80.944  1.00 40.00  ?  401 ASP A CG  1 
ATOM   2905 O  OD1 . ASP A 1 403 ? -6.337  18.984  -81.363  1.00 38.94  ?  401 ASP A OD1 1 
ATOM   2906 O  OD2 . ASP A 1 403 ? -8.125  17.757  -81.697  1.00 41.93  -1 401 ASP A OD2 1 
ATOM   2907 N  N   . PRO A 1 404 ? -5.831  21.426  -79.424  1.00 44.50  ?  402 PRO A N   1 
ATOM   2908 C  CA  . PRO A 1 404 ? -6.017  22.838  -79.782  1.00 43.94  ?  402 PRO A CA  1 
ATOM   2909 C  C   . PRO A 1 404 ? -6.843  23.037  -81.039  1.00 41.15  ?  402 PRO A C   1 
ATOM   2910 O  O   . PRO A 1 404 ? -7.166  24.185  -81.370  1.00 38.71  ?  402 PRO A O   1 
ATOM   2911 C  CB  . PRO A 1 404 ? -4.578  23.329  -79.959  1.00 52.13  ?  402 PRO A CB  1 
ATOM   2912 C  CG  . PRO A 1 404 ? -3.902  22.120  -80.528  1.00 47.99  ?  402 PRO A CG  1 
ATOM   2913 C  CD  . PRO A 1 404 ? -4.437  21.003  -79.650  1.00 43.34  ?  402 PRO A CD  1 
ATOM   2914 N  N   . ALA A 1 405 ? -7.198  21.964  -81.741  1.00 39.44  ?  403 ALA A N   1 
ATOM   2915 C  CA  . ALA A 1 405 ? -8.021  22.052  -82.937  1.00 41.08  ?  403 ALA A CA  1 
ATOM   2916 C  C   . ALA A 1 405 ? -9.501  21.961  -82.605  1.00 39.92  ?  403 ALA A C   1 
ATOM   2917 O  O   . ALA A 1 405 ? -10.336 21.951  -83.516  1.00 42.13  ?  403 ALA A O   1 
ATOM   2918 C  CB  . ALA A 1 405 ? -7.642  20.951  -83.931  1.00 36.39  ?  403 ALA A CB  1 
ATOM   2919 N  N   . GLN A 1 406 ? -9.834  21.880  -81.324  1.00 39.42  ?  404 GLN A N   1 
ATOM   2920 C  CA  . GLN A 1 406 ? -11.195 21.842  -80.831  1.00 35.77  ?  404 GLN A CA  1 
ATOM   2921 C  C   . GLN A 1 406 ? -11.537 23.199  -80.203  1.00 38.33  ?  404 GLN A C   1 
ATOM   2922 O  O   . GLN A 1 406 ? -10.778 24.169  -80.320  1.00 37.02  ?  404 GLN A O   1 
ATOM   2923 C  CB  . GLN A 1 406 ? -11.332 20.645  -79.892  1.00 40.25  ?  404 GLN A CB  1 
ATOM   2924 C  CG  . GLN A 1 406 ? -11.035 19.352  -80.654  1.00 40.01  ?  404 GLN A CG  1 
ATOM   2925 C  CD  . GLN A 1 406 ? -11.624 18.114  -80.025  1.00 40.49  ?  404 GLN A CD  1 
ATOM   2926 O  OE1 . GLN A 1 406 ? -12.797 18.088  -79.660  1.00 40.15  ?  404 GLN A OE1 1 
ATOM   2927 N  NE2 . GLN A 1 406 ? -10.818 17.061  -79.930  1.00 42.47  ?  404 GLN A NE2 1 
ATOM   2928 N  N   . LEU A 1 407 ? -12.679 23.269  -79.527  1.00 38.29  ?  405 LEU A N   1 
ATOM   2929 C  CA  . LEU A 1 407 ? -13.194 24.565  -79.104  1.00 38.24  ?  405 LEU A CA  1 
ATOM   2930 C  C   . LEU A 1 407 ? -12.564 25.076  -77.806  1.00 44.36  ?  405 LEU A C   1 
ATOM   2931 O  O   . LEU A 1 407 ? -12.211 24.292  -76.920  1.00 41.22  ?  405 LEU A O   1 
ATOM   2932 C  CB  . LEU A 1 407 ? -14.708 24.499  -78.947  1.00 41.25  ?  405 LEU A CB  1 
ATOM   2933 C  CG  . LEU A 1 407 ? -15.422 24.385  -80.295  1.00 39.58  ?  405 LEU A CG  1 
ATOM   2934 C  CD1 . LEU A 1 407 ? -16.879 24.005  -80.116  1.00 42.30  ?  405 LEU A CD1 1 
ATOM   2935 C  CD2 . LEU A 1 407 ? -15.292 25.686  -81.076  1.00 41.44  ?  405 LEU A CD2 1 
ATOM   2936 N  N   . PRO A 1 408 ? -12.395 26.391  -77.693  1.00 43.64  ?  406 PRO A N   1 
ATOM   2937 C  CA  . PRO A 1 408 ? -11.885 27.000  -76.465  1.00 45.40  ?  406 PRO A CA  1 
ATOM   2938 C  C   . PRO A 1 408 ? -13.028 27.402  -75.538  1.00 40.87  ?  406 PRO A C   1 
ATOM   2939 O  O   . PRO A 1 408 ? -14.207 27.344  -75.896  1.00 43.07  ?  406 PRO A O   1 
ATOM   2940 C  CB  . PRO A 1 408 ? -11.151 28.236  -76.992  1.00 37.87  ?  406 PRO A CB  1 
ATOM   2941 C  CG  . PRO A 1 408 ? -12.045 28.682  -78.112  1.00 37.68  ?  406 PRO A CG  1 
ATOM   2942 C  CD  . PRO A 1 408 ? -12.559 27.398  -78.759  1.00 37.65  ?  406 PRO A CD  1 
ATOM   2943 N  N   . ALA A 1 409 ? -12.652 27.836  -74.339  1.00 50.02  ?  407 ALA A N   1 
ATOM   2944 C  CA  . ALA A 1 409 ? -13.642 28.358  -73.409  1.00 48.33  ?  407 ALA A CA  1 
ATOM   2945 C  C   . ALA A 1 409 ? -14.164 29.706  -73.901  1.00 51.49  ?  407 ALA A C   1 
ATOM   2946 O  O   . ALA A 1 409 ? -13.385 30.542  -74.368  1.00 59.20  ?  407 ALA A O   1 
ATOM   2947 C  CB  . ALA A 1 409 ? -13.044 28.510  -72.010  1.00 53.85  ?  407 ALA A CB  1 
ATOM   2948 N  N   . PRO A 1 410 ? -15.470 29.944  -73.814  1.00 50.58  ?  408 PRO A N   1 
ATOM   2949 C  CA  . PRO A 1 410 ? -16.025 31.218  -74.287  1.00 51.39  ?  408 PRO A CA  1 
ATOM   2950 C  C   . PRO A 1 410 ? -15.432 32.400  -73.535  1.00 52.66  ?  408 PRO A C   1 
ATOM   2951 O  O   . PRO A 1 410 ? -15.339 32.393  -72.306  1.00 56.30  ?  408 PRO A O   1 
ATOM   2952 C  CB  . PRO A 1 410 ? -17.525 31.066  -74.010  1.00 55.29  ?  408 PRO A CB  1 
ATOM   2953 C  CG  . PRO A 1 410 ? -17.736 29.575  -74.026  1.00 56.86  ?  408 PRO A CG  1 
ATOM   2954 C  CD  . PRO A 1 410 ? -16.530 29.062  -73.299  1.00 51.44  ?  408 PRO A CD  1 
ATOM   2955 N  N   . ARG A 1 411 ? -15.019 33.415  -74.288  1.00 52.26  ?  409 ARG A N   1 
ATOM   2956 C  CA  . ARG A 1 411 ? -14.529 34.673  -73.729  1.00 53.24  ?  409 ARG A CA  1 
ATOM   2957 C  C   . ARG A 1 411 ? -15.633 35.695  -73.992  1.00 52.47  ?  409 ARG A C   1 
ATOM   2958 O  O   . ARG A 1 411 ? -15.669 36.341  -75.040  1.00 53.54  ?  409 ARG A O   1 
ATOM   2959 C  CB  . ARG A 1 411 ? -13.196 35.077  -74.358  1.00 53.10  ?  409 ARG A CB  1 
ATOM   2960 C  CG  . ARG A 1 411 ? -12.173 33.943  -74.429  1.00 55.70  ?  409 ARG A CG  1 
ATOM   2961 C  CD  . ARG A 1 411 ? -11.659 33.564  -73.050  1.00 59.15  ?  409 ARG A CD  1 
ATOM   2962 N  NE  . ARG A 1 411 ? -10.311 33.004  -73.079  1.00 64.30  ?  409 ARG A NE  1 
ATOM   2963 C  CZ  . ARG A 1 411 ? -9.990  31.828  -73.603  1.00 61.34  ?  409 ARG A CZ  1 
ATOM   2964 N  NH1 . ARG A 1 411 ? -10.913 30.991  -74.047  1.00 57.88  ?  409 ARG A NH1 1 
ATOM   2965 N  NH2 . ARG A 1 411 ? -8.712  31.459  -73.632  1.00 61.80  ?  409 ARG A NH2 1 
ATOM   2966 N  N   . THR A 1 412 ? -16.540 35.833  -73.022  1.00 53.89  ?  410 THR A N   1 
ATOM   2967 C  CA  . THR A 1 412 ? -17.740 36.645  -73.199  1.00 57.20  ?  410 THR A CA  1 
ATOM   2968 C  C   . THR A 1 412 ? -17.469 38.132  -73.391  1.00 59.59  ?  410 THR A C   1 
ATOM   2969 O  O   . THR A 1 412 ? -18.380 38.848  -73.820  1.00 63.03  ?  410 THR A O   1 
ATOM   2970 C  CB  . THR A 1 412 ? -18.678 36.453  -72.005  1.00 65.94  ?  410 THR A CB  1 
ATOM   2971 O  OG1 . THR A 1 412 ? -17.970 36.727  -70.789  1.00 72.57  ?  410 THR A OG1 1 
ATOM   2972 C  CG2 . THR A 1 412 ? -19.212 35.029  -71.974  1.00 71.55  ?  410 THR A CG2 1 
ATOM   2973 N  N   . LEU A 1 413 ? -16.265 38.623  -73.102  1.00 56.39  ?  411 LEU A N   1 
ATOM   2974 C  CA  . LEU A 1 413 ? -15.976 40.024  -73.383  1.00 58.35  ?  411 LEU A CA  1 
ATOM   2975 C  C   . LEU A 1 413 ? -15.396 40.240  -74.773  1.00 56.56  ?  411 LEU A C   1 
ATOM   2976 O  O   . LEU A 1 413 ? -15.459 41.361  -75.289  1.00 60.27  ?  411 LEU A O   1 
ATOM   2977 C  CB  . LEU A 1 413 ? -15.018 40.606  -72.336  1.00 60.59  ?  411 LEU A CB  1 
ATOM   2978 C  CG  . LEU A 1 413 ? -15.485 40.610  -70.877  1.00 64.05  ?  411 LEU A CG  1 
ATOM   2979 C  CD1 . LEU A 1 413 ? -14.525 41.413  -70.006  1.00 65.92  ?  411 LEU A CD1 1 
ATOM   2980 C  CD2 . LEU A 1 413 ? -16.904 41.152  -70.756  1.00 65.29  ?  411 LEU A CD2 1 
ATOM   2981 N  N   . LEU A 1 414 ? -14.854 39.196  -75.391  1.00 53.63  ?  412 LEU A N   1 
ATOM   2982 C  CA  . LEU A 1 414 ? -14.210 39.312  -76.694  1.00 52.14  ?  412 LEU A CA  1 
ATOM   2983 C  C   . LEU A 1 414 ? -15.260 39.446  -77.791  1.00 51.60  ?  412 LEU A C   1 
ATOM   2984 O  O   . LEU A 1 414 ? -16.019 38.508  -78.053  1.00 50.02  ?  412 LEU A O   1 
ATOM   2985 C  CB  . LEU A 1 414 ? -13.318 38.101  -76.939  1.00 50.33  ?  412 LEU A CB  1 
ATOM   2986 C  CG  . LEU A 1 414 ? -12.661 38.049  -78.312  1.00 49.41  ?  412 LEU A CG  1 
ATOM   2987 C  CD1 . LEU A 1 414 ? -11.870 39.320  -78.547  1.00 51.22  ?  412 LEU A CD1 1 
ATOM   2988 C  CD2 . LEU A 1 414 ? -11.768 36.827  -78.402  1.00 48.90  ?  412 LEU A CD2 1 
ATOM   2989 N  N   . THR A 1 415 ? -15.293 40.611  -78.444  1.00 57.29  ?  413 THR A N   1 
ATOM   2990 C  CA  . THR A 1 415 ? -16.239 40.889  -79.516  1.00 56.24  ?  413 THR A CA  1 
ATOM   2991 C  C   . THR A 1 415 ? -15.574 41.264  -80.831  1.00 61.47  ?  413 THR A C   1 
ATOM   2992 O  O   . THR A 1 415 ? -16.210 41.131  -81.882  1.00 63.22  ?  413 THR A O   1 
ATOM   2993 C  CB  . THR A 1 415 ? -17.206 42.018  -79.122  1.00 57.33  ?  413 THR A CB  1 
ATOM   2994 O  OG1 . THR A 1 415 ? -16.464 43.197  -78.783  1.00 62.58  ?  413 THR A OG1 1 
ATOM   2995 C  CG2 . THR A 1 415 ? -18.067 41.600  -77.942  1.00 57.27  ?  413 THR A CG2 1 
ATOM   2996 N  N   . LYS A 1 416 ? -14.325 41.726  -80.806  1.00 54.74  ?  414 LYS A N   1 
ATOM   2997 C  CA  . LYS A 1 416 ? -13.617 42.185  -81.996  1.00 54.88  ?  414 LYS A CA  1 
ATOM   2998 C  C   . LYS A 1 416 ? -12.408 41.280  -82.195  1.00 59.66  ?  414 LYS A C   1 
ATOM   2999 O  O   . LYS A 1 416 ? -11.493 41.264  -81.364  1.00 61.73  ?  414 LYS A O   1 
ATOM   3000 C  CB  . LYS A 1 416 ? -13.200 43.647  -81.855  1.00 56.71  ?  414 LYS A CB  1 
ATOM   3001 C  CG  . LYS A 1 416 ? -14.371 44.612  -81.787  1.00 59.07  ?  414 LYS A CG  1 
ATOM   3002 C  CD  . LYS A 1 416 ? -13.971 45.918  -81.128  1.00 62.50  ?  414 LYS A CD  1 
ATOM   3003 C  CE  . LYS A 1 416 ? -13.666 45.705  -79.655  1.00 62.94  ?  414 LYS A CE  1 
ATOM   3004 N  NZ  . LYS A 1 416 ? -13.012 46.891  -79.044  1.00 66.35  ?  414 LYS A NZ  1 
ATOM   3005 N  N   . GLY A 1 417 ? -12.411 40.523  -83.285  1.00 52.06  ?  415 GLY A N   1 
ATOM   3006 C  CA  . GLY A 1 417 ? -11.314 39.641  -83.617  1.00 52.04  ?  415 GLY A CA  1 
ATOM   3007 C  C   . GLY A 1 417 ? -11.614 38.201  -83.240  1.00 58.91  ?  415 GLY A C   1 
ATOM   3008 O  O   . GLY A 1 417 ? -12.596 37.885  -82.563  1.00 66.44  ?  415 GLY A O   1 
ATOM   3009 N  N   . THR A 1 418 ? -10.730 37.314  -83.685  1.00 56.81  ?  416 THR A N   1 
ATOM   3010 C  CA  . THR A 1 418 ? -10.858 35.884  -83.443  1.00 55.60  ?  416 THR A CA  1 
ATOM   3011 C  C   . THR A 1 418 ? -9.637  35.386  -82.684  1.00 51.53  ?  416 THR A C   1 
ATOM   3012 O  O   . THR A 1 418 ? -8.502  35.715  -83.044  1.00 55.80  ?  416 THR A O   1 
ATOM   3013 C  CB  . THR A 1 418 ? -11.017 35.119  -84.761  1.00 66.71  ?  416 THR A CB  1 
ATOM   3014 O  OG1 . THR A 1 418 ? -10.107 35.647  -85.735  1.00 65.89  ?  416 THR A OG1 1 
ATOM   3015 C  CG2 . THR A 1 418 ? -12.443 35.253  -85.283  1.00 62.38  ?  416 THR A CG2 1 
ATOM   3016 N  N   . LEU A 1 419 ? -9.874  34.619  -81.622  1.00 52.86  ?  417 LEU A N   1 
ATOM   3017 C  CA  . LEU A 1 419 ? -8.793  34.029  -80.842  1.00 54.11  ?  417 LEU A CA  1 
ATOM   3018 C  C   . LEU A 1 419 ? -8.308  32.752  -81.520  1.00 48.17  ?  417 LEU A C   1 
ATOM   3019 O  O   . LEU A 1 419 ? -9.068  31.787  -81.653  1.00 49.20  ?  417 LEU A O   1 
ATOM   3020 C  CB  . LEU A 1 419 ? -9.262  33.739  -79.419  1.00 51.67  ?  417 LEU A CB  1 
ATOM   3021 C  CG  . LEU A 1 419 ? -8.133  33.548  -78.410  1.00 55.81  ?  417 LEU A CG  1 
ATOM   3022 C  CD1 . LEU A 1 419 ? -7.169  34.720  -78.500  1.00 60.08  ?  417 LEU A CD1 1 
ATOM   3023 C  CD2 . LEU A 1 419 ? -8.683  33.403  -77.001  1.00 58.51  ?  417 LEU A CD2 1 
ATOM   3024 N  N   . GLU A 1 420 ? -7.046  32.733  -81.926  1.00 48.27  ?  418 GLU A N   1 
ATOM   3025 C  CA  . GLU A 1 420 ? -6.494  31.545  -82.553  1.00 54.27  ?  418 GLU A CA  1 
ATOM   3026 C  C   . GLU A 1 420 ? -6.059  30.522  -81.506  1.00 50.33  ?  418 GLU A C   1 
ATOM   3027 O  O   . GLU A 1 420 ? -5.809  30.865  -80.348  1.00 45.99  ?  418 GLU A O   1 
ATOM   3028 C  CB  . GLU A 1 420 ? -5.331  31.929  -83.459  1.00 50.10  ?  418 GLU A CB  1 
ATOM   3029 C  CG  . GLU A 1 420 ? -5.775  32.771  -84.648  1.00 57.25  ?  418 GLU A CG  1 
ATOM   3030 C  CD  . GLU A 1 420 ? -6.935  32.142  -85.405  1.00 70.00  ?  418 GLU A CD  1 
ATOM   3031 O  OE1 . GLU A 1 420 ? -6.748  31.059  -85.999  1.00 64.46  ?  418 GLU A OE1 1 
ATOM   3032 O  OE2 . GLU A 1 420 ? -8.041  32.726  -85.395  1.00 77.04  -1 418 GLU A OE2 1 
ATOM   3033 N  N   . PRO A 1 421 ? -5.972  29.246  -81.895  1.00 50.49  ?  419 PRO A N   1 
ATOM   3034 C  CA  . PRO A 1 421 ? -5.633  28.191  -80.923  1.00 49.79  ?  419 PRO A CA  1 
ATOM   3035 C  C   . PRO A 1 421 ? -4.351  28.422  -80.142  1.00 49.69  ?  419 PRO A C   1 
ATOM   3036 O  O   . PRO A 1 421 ? -4.280  28.036  -78.968  1.00 48.68  ?  419 PRO A O   1 
ATOM   3037 C  CB  . PRO A 1 421 ? -5.532  26.946  -81.814  1.00 45.88  ?  419 PRO A CB  1 
ATOM   3038 C  CG  . PRO A 1 421 ? -6.508  27.242  -82.913  1.00 46.51  ?  419 PRO A CG  1 
ATOM   3039 C  CD  . PRO A 1 421 ? -6.203  28.680  -83.234  1.00 45.37  ?  419 PRO A CD  1 
ATOM   3040 N  N   . GLU A 1 422 ? -3.334  29.043  -80.741  1.00 47.79  ?  420 GLU A N   1 
ATOM   3041 C  CA  . GLU A 1 422 ? -2.084  29.235  -80.018  1.00 52.42  ?  420 GLU A CA  1 
ATOM   3042 C  C   . GLU A 1 422 ? -2.227  30.208  -78.857  1.00 55.50  ?  420 GLU A C   1 
ATOM   3043 O  O   . GLU A 1 422 ? -1.278  30.369  -78.082  1.00 60.49  ?  420 GLU A O   1 
ATOM   3044 C  CB  . GLU A 1 422 ? -0.987  29.705  -80.973  1.00 59.85  ?  420 GLU A CB  1 
ATOM   3045 C  CG  . GLU A 1 422 ? -1.166  31.111  -81.496  1.00 62.42  ?  420 GLU A CG  1 
ATOM   3046 C  CD  . GLU A 1 422 ? 0.002   31.555  -82.352  1.00 72.74  ?  420 GLU A CD  1 
ATOM   3047 O  OE1 . GLU A 1 422 ? 1.145   31.565  -81.845  1.00 71.31  ?  420 GLU A OE1 1 
ATOM   3048 O  OE2 . GLU A 1 422 ? -0.222  31.887  -83.535  1.00 83.42  -1 420 GLU A OE2 1 
ATOM   3049 N  N   . TYR A 1 423 ? -3.385  30.847  -78.713  1.00 52.57  ?  421 TYR A N   1 
ATOM   3050 C  CA  . TYR A 1 423 ? -3.608  31.854  -77.686  1.00 54.87  ?  421 TYR A CA  1 
ATOM   3051 C  C   . TYR A 1 423 ? -4.679  31.403  -76.704  1.00 53.81  ?  421 TYR A C   1 
ATOM   3052 O  O   . TYR A 1 423 ? -5.087  32.184  -75.836  1.00 56.71  ?  421 TYR A O   1 
ATOM   3053 C  CB  . TYR A 1 423 ? -3.981  33.198  -78.320  1.00 54.90  ?  421 TYR A CB  1 
ATOM   3054 C  CG  . TYR A 1 423 ? -2.999  33.665  -79.376  1.00 55.33  ?  421 TYR A CG  1 
ATOM   3055 C  CD1 . TYR A 1 423 ? -1.684  33.966  -79.044  1.00 64.00  ?  421 TYR A CD1 1 
ATOM   3056 C  CD2 . TYR A 1 423 ? -3.385  33.800  -80.703  1.00 54.38  ?  421 TYR A CD2 1 
ATOM   3057 C  CE1 . TYR A 1 423 ? -0.782  34.393  -80.004  1.00 66.90  ?  421 TYR A CE1 1 
ATOM   3058 C  CE2 . TYR A 1 423 ? -2.490  34.225  -81.670  1.00 53.19  ?  421 TYR A CE2 1 
ATOM   3059 C  CZ  . TYR A 1 423 ? -1.191  34.520  -81.316  1.00 62.75  ?  421 TYR A CZ  1 
ATOM   3060 O  OH  . TYR A 1 423 ? -0.298  34.940  -82.275  1.00 65.65  ?  421 TYR A OH  1 
ATOM   3061 N  N   . PHE A 1 424 ? -5.127  30.149  -76.811  1.00 52.36  ?  422 PHE A N   1 
ATOM   3062 C  CA  . PHE A 1 424 ? -6.170  29.642  -75.927  1.00 52.37  ?  422 PHE A CA  1 
ATOM   3063 C  C   . PHE A 1 424 ? -5.685  29.627  -74.484  1.00 52.27  ?  422 PHE A C   1 
ATOM   3064 O  O   . PHE A 1 424 ? -6.381  30.091  -73.573  1.00 52.39  ?  422 PHE A O   1 
ATOM   3065 C  CB  . PHE A 1 424 ? -6.569  28.232  -76.367  1.00 44.11  ?  422 PHE A CB  1 
ATOM   3066 C  CG  . PHE A 1 424 ? -7.453  28.189  -77.583  1.00 48.52  ?  422 PHE A CG  1 
ATOM   3067 C  CD1 . PHE A 1 424 ? -7.780  29.344  -78.272  1.00 48.39  ?  422 PHE A CD1 1 
ATOM   3068 C  CD2 . PHE A 1 424 ? -7.923  26.976  -78.061  1.00 48.60  ?  422 PHE A CD2 1 
ATOM   3069 C  CE1 . PHE A 1 424 ? -8.583  29.292  -79.398  1.00 41.18  ?  422 PHE A CE1 1 
ATOM   3070 C  CE2 . PHE A 1 424 ? -8.723  26.918  -79.187  1.00 42.66  ?  422 PHE A CE2 1 
ATOM   3071 C  CZ  . PHE A 1 424 ? -9.054  28.077  -79.856  1.00 43.60  ?  422 PHE A CZ  1 
ATOM   3072 N  N   . ASN A 1 425 ? -4.487  29.096  -74.261  1.00 55.07  ?  423 ASN A N   1 
ATOM   3073 C  CA  . ASN A 1 425 ? -3.859  29.025  -72.945  1.00 55.16  ?  423 ASN A CA  1 
ATOM   3074 C  C   . ASN A 1 425 ? -2.389  28.678  -73.160  1.00 57.36  ?  423 ASN A C   1 
ATOM   3075 O  O   . ASN A 1 425 ? -1.919  28.563  -74.296  1.00 57.19  ?  423 ASN A O   1 
ATOM   3076 C  CB  . ASN A 1 425 ? -4.560  28.022  -72.025  1.00 54.98  ?  423 ASN A CB  1 
ATOM   3077 C  CG  . ASN A 1 425 ? -4.599  26.624  -72.601  1.00 50.83  ?  423 ASN A CG  1 
ATOM   3078 O  OD1 . ASN A 1 425 ? -3.561  26.015  -72.857  1.00 53.83  ?  423 ASN A OD1 1 
ATOM   3079 N  ND2 . ASN A 1 425 ? -5.803  26.099  -72.794  1.00 48.11  ?  423 ASN A ND2 1 
ATOM   3080 N  N   . SER A 1 426 ? -1.666  28.495  -72.052  1.00 59.95  ?  424 SER A N   1 
ATOM   3081 C  CA  . SER A 1 426 ? -0.229  28.248  -72.139  1.00 60.69  ?  424 SER A CA  1 
ATOM   3082 C  C   . SER A 1 426 ? 0.070   26.877  -72.735  1.00 58.49  ?  424 SER A C   1 
ATOM   3083 O  O   . SER A 1 426 ? 1.061   26.713  -73.457  1.00 53.87  ?  424 SER A O   1 
ATOM   3084 C  CB  . SER A 1 426 ? 0.410   28.380  -70.757  1.00 62.02  ?  424 SER A CB  1 
ATOM   3085 O  OG  . SER A 1 426 ? -0.021  29.563  -70.107  1.00 68.97  ?  424 SER A OG  1 
ATOM   3086 N  N   . VAL A 1 427 ? -0.760  25.877  -72.428  1.00 55.97  ?  425 VAL A N   1 
ATOM   3087 C  CA  . VAL A 1 427 ? -0.543  24.537  -72.967  1.00 59.54  ?  425 VAL A CA  1 
ATOM   3088 C  C   . VAL A 1 427 ? -0.799  24.519  -74.469  1.00 60.52  ?  425 VAL A C   1 
ATOM   3089 O  O   . VAL A 1 427 ? -0.019  23.949  -75.242  1.00 58.59  ?  425 VAL A O   1 
ATOM   3090 C  CB  . VAL A 1 427 ? -1.425  23.512  -72.232  1.00 56.53  ?  425 VAL A CB  1 
ATOM   3091 C  CG1 . VAL A 1 427 ? -1.247  22.131  -72.841  1.00 55.69  ?  425 VAL A CG1 1 
ATOM   3092 C  CG2 . VAL A 1 427 ? -1.084  23.492  -70.750  1.00 56.75  ?  425 VAL A CG2 1 
ATOM   3093 N  N   . CYS A 1 428 ? -1.897  25.144  -74.907  1.00 58.62  ?  426 CYS A N   1 
ATOM   3094 C  CA  . CYS A 1 428 ? -2.209  25.169  -76.333  1.00 53.84  ?  426 CYS A CA  1 
ATOM   3095 C  C   . CYS A 1 428 ? -1.167  25.961  -77.107  1.00 53.75  ?  426 CYS A C   1 
ATOM   3096 O  O   . CYS A 1 428 ? -0.878  25.639  -78.265  1.00 58.15  ?  426 CYS A O   1 
ATOM   3097 C  CB  . CYS A 1 428 ? -3.605  25.744  -76.567  1.00 46.86  ?  426 CYS A CB  1 
ATOM   3098 S  SG  . CYS A 1 428 ? -4.953  24.701  -75.961  1.00 65.82  ?  426 CYS A SG  1 
ATOM   3099 N  N   . ARG A 1 429 ? -0.607  27.007  -76.496  1.00 51.49  ?  427 ARG A N   1 
ATOM   3100 C  CA  . ARG A 1 429 ? 0.476   27.737  -77.142  1.00 57.20  ?  427 ARG A CA  1 
ATOM   3101 C  C   . ARG A 1 429 ? 1.673   26.821  -77.367  1.00 62.92  ?  427 ARG A C   1 
ATOM   3102 O  O   . ARG A 1 429 ? 2.280   26.822  -78.444  1.00 64.37  ?  427 ARG A O   1 
ATOM   3103 C  CB  . ARG A 1 429 ? 0.869   28.952  -76.302  1.00 51.05  ?  427 ARG A CB  1 
ATOM   3104 C  CG  . ARG A 1 429 ? 1.953   29.808  -76.931  1.00 55.95  ?  427 ARG A CG  1 
ATOM   3105 C  CD  . ARG A 1 429 ? 1.912   31.234  -76.408  1.00 67.44  ?  427 ARG A CD  1 
ATOM   3106 N  NE  . ARG A 1 429 ? 2.933   32.070  -77.026  1.00 75.46  ?  427 ARG A NE  1 
ATOM   3107 C  CZ  . ARG A 1 429 ? 2.999   32.346  -78.322  1.00 71.35  ?  427 ARG A CZ  1 
ATOM   3108 N  NH1 . ARG A 1 429 ? 1.974   32.126  -79.128  1.00 70.84  ?  427 ARG A NH1 1 
ATOM   3109 N  NH2 . ARG A 1 429 ? 4.088   32.938  -78.804  1.00 78.27  ?  427 ARG A NH2 1 
ATOM   3110 N  N   . LEU A 1 430 ? 2.037   26.042  -76.345  1.00 61.93  ?  428 LEU A N   1 
ATOM   3111 C  CA  . LEU A 1 430 ? 3.124   25.078  -76.496  1.00 67.23  ?  428 LEU A CA  1 
ATOM   3112 C  C   . LEU A 1 430 ? 2.817   24.085  -77.612  1.00 63.26  ?  428 LEU A C   1 
ATOM   3113 O  O   . LEU A 1 430 ? 3.654   23.840  -78.489  1.00 60.82  ?  428 LEU A O   1 
ATOM   3114 C  CB  . LEU A 1 430 ? 3.375   24.349  -75.175  1.00 63.58  ?  428 LEU A CB  1 
ATOM   3115 C  CG  . LEU A 1 430 ? 4.108   25.130  -74.081  1.00 65.92  ?  428 LEU A CG  1 
ATOM   3116 C  CD1 . LEU A 1 430 ? 4.508   24.207  -72.938  1.00 68.94  ?  428 LEU A CD1 1 
ATOM   3117 C  CD2 . LEU A 1 430 ? 5.327   25.849  -74.644  1.00 65.95  ?  428 LEU A CD2 1 
ATOM   3118 N  N   . MET A 1 431 ? 1.616   23.498  -77.592  1.00 55.49  ?  429 MET A N   1 
ATOM   3119 C  CA  . MET A 1 431 ? 1.258   22.496  -78.590  1.00 58.34  ?  429 MET A CA  1 
ATOM   3120 C  C   . MET A 1 431 ? 1.304   23.054  -80.004  1.00 59.25  ?  429 MET A C   1 
ATOM   3121 O  O   . MET A 1 431 ? 1.497   22.290  -80.956  1.00 56.11  ?  429 MET A O   1 
ATOM   3122 C  CB  . MET A 1 431 ? -0.142  21.937  -78.318  1.00 58.42  ?  429 MET A CB  1 
ATOM   3123 C  CG  . MET A 1 431 ? -0.268  21.041  -77.095  1.00 61.11  ?  429 MET A CG  1 
ATOM   3124 S  SD  . MET A 1 431 ? -1.935  20.348  -76.982  1.00 63.64  ?  429 MET A SD  1 
ATOM   3125 C  CE  . MET A 1 431 ? -1.815  19.342  -75.506  1.00 57.03  ?  429 MET A CE  1 
ATOM   3126 N  N   . LYS A 1 432 ? 1.144   24.367  -80.163  1.00 61.48  ?  430 LYS A N   1 
ATOM   3127 C  CA  . LYS A 1 432 ? 1.080   24.990  -81.475  1.00 59.47  ?  430 LYS A CA  1 
ATOM   3128 C  C   . LYS A 1 432 ? 2.410   25.605  -81.887  1.00 62.39  ?  430 LYS A C   1 
ATOM   3129 O  O   . LYS A 1 432 ? 2.586   25.935  -83.064  1.00 63.73  ?  430 LYS A O   1 
ATOM   3130 C  CB  . LYS A 1 432 ? -0.006  26.074  -81.487  1.00 58.52  ?  430 LYS A CB  1 
ATOM   3131 C  CG  . LYS A 1 432 ? -1.431  25.547  -81.350  1.00 54.84  ?  430 LYS A CG  1 
ATOM   3132 C  CD  . LYS A 1 432 ? -1.866  24.664  -82.507  1.00 52.18  ?  430 LYS A CD  1 
ATOM   3133 C  CE  . LYS A 1 432 ? -1.928  25.431  -83.813  1.00 53.23  ?  430 LYS A CE  1 
ATOM   3134 N  NZ  . LYS A 1 432 ? -2.435  24.563  -84.911  1.00 50.60  ?  430 LYS A NZ  1 
ATOM   3135 N  N   . THR A 1 433 ? 3.343   25.760  -80.947  1.00 69.97  ?  431 THR A N   1 
ATOM   3136 C  CA  . THR A 1 433 ? 4.640   26.370  -81.212  1.00 64.68  ?  431 THR A CA  1 
ATOM   3137 C  C   . THR A 1 433 ? 5.722   25.298  -81.265  1.00 71.36  ?  431 THR A C   1 
ATOM   3138 O  O   . THR A 1 433 ? 6.269   25.016  -82.336  1.00 77.75  ?  431 THR A O   1 
ATOM   3139 C  CB  . THR A 1 433 ? 4.966   27.429  -80.154  1.00 70.32  ?  431 THR A CB  1 
ATOM   3140 O  OG1 . THR A 1 433 ? 4.906   26.843  -78.848  1.00 72.73  ?  431 THR A OG1 1 
ATOM   3141 C  CG2 . THR A 1 433 ? 3.979   28.586  -80.237  1.00 69.70  ?  431 THR A CG2 1 
ATOM   3142 N  N   . ILE A 1 434 ? 6.041   24.692  -80.121  1.00 72.86  ?  432 ILE A N   1 
ATOM   3143 C  CA  . ILE A 1 434 ? 7.121   23.713  -80.080  1.00 64.80  ?  432 ILE A CA  1 
ATOM   3144 C  C   . ILE A 1 434 ? 6.613   22.326  -80.447  1.00 73.28  ?  432 ILE A C   1 
ATOM   3145 O  O   . ILE A 1 434 ? 7.407   21.474  -80.873  1.00 78.19  ?  432 ILE A O   1 
ATOM   3146 C  CB  . ILE A 1 434 ? 7.796   23.675  -78.696  1.00 62.30  ?  432 ILE A CB  1 
ATOM   3147 C  CG1 . ILE A 1 434 ? 6.842   23.110  -77.643  1.00 67.46  ?  432 ILE A CG1 1 
ATOM   3148 C  CG2 . ILE A 1 434 ? 8.242   25.067  -78.289  1.00 69.85  ?  432 ILE A CG2 1 
ATOM   3149 C  CD1 . ILE A 1 434 ? 7.463   22.983  -76.266  1.00 71.04  ?  432 ILE A CD1 1 
ATOM   3150 N  N   . GLY A 1 435 ? 5.317   22.076  -80.287  1.00 63.99  ?  433 GLY A N   1 
ATOM   3151 C  CA  . GLY A 1 435 ? 4.725   20.793  -80.565  1.00 61.52  ?  433 GLY A CA  1 
ATOM   3152 C  C   . GLY A 1 435 ? 4.284   20.120  -79.285  1.00 59.23  ?  433 GLY A C   1 
ATOM   3153 O  O   . GLY A 1 435 ? 4.756   20.447  -78.191  1.00 59.53  ?  433 GLY A O   1 
ATOM   3154 N  N   . PRO A 1 436 ? 3.367   19.168  -79.393  1.00 55.23  ?  434 PRO A N   1 
ATOM   3155 C  CA  . PRO A 1 436 ? 2.992   18.374  -78.224  1.00 60.06  ?  434 PRO A CA  1 
ATOM   3156 C  C   . PRO A 1 436 ? 4.028   17.294  -77.946  1.00 64.33  ?  434 PRO A C   1 
ATOM   3157 O  O   . PRO A 1 436 ? 4.830   16.923  -78.805  1.00 66.22  ?  434 PRO A O   1 
ATOM   3158 C  CB  . PRO A 1 436 ? 1.646   17.772  -78.637  1.00 61.31  ?  434 PRO A CB  1 
ATOM   3159 C  CG  . PRO A 1 436 ? 1.800   17.576  -80.111  1.00 57.72  ?  434 PRO A CG  1 
ATOM   3160 C  CD  . PRO A 1 436 ? 2.598   18.777  -80.590  1.00 59.13  ?  434 PRO A CD  1 
ATOM   3161 N  N   . ASP A 1 437 ? 4.002   16.793  -76.710  1.00 66.44  ?  435 ASP A N   1 
ATOM   3162 C  CA  . ASP A 1 437 ? 4.927   15.726  -76.342  1.00 65.76  ?  435 ASP A CA  1 
ATOM   3163 C  C   . ASP A 1 437 ? 4.485   14.398  -76.941  1.00 69.33  ?  435 ASP A C   1 
ATOM   3164 O  O   . ASP A 1 437 ? 5.322   13.576  -77.331  1.00 67.88  ?  435 ASP A O   1 
ATOM   3165 C  CB  . ASP A 1 437 ? 5.031   15.610  -74.819  1.00 63.91  ?  435 ASP A CB  1 
ATOM   3166 C  CG  . ASP A 1 437 ? 5.627   16.848  -74.174  1.00 76.94  ?  435 ASP A CG  1 
ATOM   3167 O  OD1 . ASP A 1 437 ? 6.747   17.246  -74.561  1.00 74.85  ?  435 ASP A OD1 1 
ATOM   3168 O  OD2 . ASP A 1 437 ? 4.975   17.420  -73.275  1.00 71.71  -1 435 ASP A OD2 1 
ATOM   3169 N  N   . MET A 1 438 ? 3.175   14.182  -77.025  1.00 63.05  ?  436 MET A N   1 
ATOM   3170 C  CA  . MET A 1 438 ? 2.602   12.960  -77.561  1.00 58.74  ?  436 MET A CA  1 
ATOM   3171 C  C   . MET A 1 438 ? 1.433   13.335  -78.461  1.00 59.87  ?  436 MET A C   1 
ATOM   3172 O  O   . MET A 1 438 ? 0.731   14.318  -78.208  1.00 59.72  ?  436 MET A O   1 
ATOM   3173 C  CB  . MET A 1 438 ? 2.167   12.023  -76.424  1.00 60.20  ?  436 MET A CB  1 
ATOM   3174 C  CG  . MET A 1 438 ? 3.257   11.808  -75.372  1.00 61.86  ?  436 MET A CG  1 
ATOM   3175 S  SD  . MET A 1 438 ? 2.667   11.325  -73.732  1.00 78.53  ?  436 MET A SD  1 
ATOM   3176 C  CE  . MET A 1 438 ? 2.058   12.884  -73.097  1.00 67.32  ?  436 MET A CE  1 
ATOM   3177 N  N   . PHE A 1 439 ? 1.229   12.547  -79.518  1.00 58.82  ?  437 PHE A N   1 
ATOM   3178 C  CA  . PHE A 1 439 ? 0.162   12.796  -80.488  1.00 56.37  ?  437 PHE A CA  1 
ATOM   3179 C  C   . PHE A 1 439 ? -0.502  11.478  -80.860  1.00 53.80  ?  437 PHE A C   1 
ATOM   3180 O  O   . PHE A 1 439 ? 0.134   10.614  -81.472  1.00 54.13  ?  437 PHE A O   1 
ATOM   3181 C  CB  . PHE A 1 439 ? 0.716   13.490  -81.735  1.00 52.93  ?  437 PHE A CB  1 
ATOM   3182 C  CG  . PHE A 1 439 ? -0.299  13.685  -82.831  1.00 52.32  ?  437 PHE A CG  1 
ATOM   3183 C  CD1 . PHE A 1 439 ? -1.274  14.664  -82.731  1.00 53.32  ?  437 PHE A CD1 1 
ATOM   3184 C  CD2 . PHE A 1 439 ? -0.271  12.890  -83.966  1.00 48.72  ?  437 PHE A CD2 1 
ATOM   3185 C  CE1 . PHE A 1 439 ? -2.204  14.844  -83.741  1.00 49.96  ?  437 PHE A CE1 1 
ATOM   3186 C  CE2 . PHE A 1 439 ? -1.198  13.065  -84.978  1.00 49.58  ?  437 PHE A CE2 1 
ATOM   3187 C  CZ  . PHE A 1 439 ? -2.164  14.043  -84.865  1.00 48.85  ?  437 PHE A CZ  1 
ATOM   3188 N  N   . LEU A 1 440 ? -1.773  11.320  -80.488  1.00 49.72  ?  438 LEU A N   1 
ATOM   3189 C  CA  . LEU A 1 440 ? -2.563  10.161  -80.897  1.00 52.74  ?  438 LEU A CA  1 
ATOM   3190 C  C   . LEU A 1 440 ? -3.030  10.372  -82.334  1.00 46.72  ?  438 LEU A C   1 
ATOM   3191 O  O   . LEU A 1 440 ? -3.866  11.243  -82.599  1.00 46.86  ?  438 LEU A O   1 
ATOM   3192 C  CB  . LEU A 1 440 ? -3.739  9.958   -79.947  1.00 47.79  ?  438 LEU A CB  1 
ATOM   3193 C  CG  . LEU A 1 440 ? -3.361  9.911   -78.464  1.00 49.83  ?  438 LEU A CG  1 
ATOM   3194 C  CD1 . LEU A 1 440 ? -4.590  9.679   -77.599  1.00 50.92  ?  438 LEU A CD1 1 
ATOM   3195 C  CD2 . LEU A 1 440 ? -2.305  8.841   -78.211  1.00 52.62  ?  438 LEU A CD2 1 
ATOM   3196 N  N   . GLY A 1 441 ? -2.506  9.577   -83.262  1.00 46.60  ?  439 GLY A N   1 
ATOM   3197 C  CA  . GLY A 1 441 ? -2.743  9.789   -84.675  1.00 50.80  ?  439 GLY A CA  1 
ATOM   3198 C  C   . GLY A 1 441 ? -3.754  8.912   -85.388  1.00 50.76  ?  439 GLY A C   1 
ATOM   3199 O  O   . GLY A 1 441 ? -3.878  9.029   -86.613  1.00 48.89  ?  439 GLY A O   1 
ATOM   3200 N  N   . THR A 1 442 ? -4.492  8.053   -84.688  1.00 44.16  ?  440 THR A N   1 
ATOM   3201 C  CA  . THR A 1 442 ? -5.424  7.144   -85.351  1.00 43.32  ?  440 THR A CA  1 
ATOM   3202 C  C   . THR A 1 442 ? -6.822  7.347   -84.784  1.00 42.31  ?  440 THR A C   1 
ATOM   3203 O  O   . THR A 1 442 ? -7.081  7.017   -83.621  1.00 44.05  ?  440 THR A O   1 
ATOM   3204 C  CB  . THR A 1 442 ? -4.990  5.686   -85.197  1.00 47.40  ?  440 THR A CB  1 
ATOM   3205 O  OG1 . THR A 1 442 ? -3.737  5.487   -85.861  1.00 56.11  ?  440 THR A OG1 1 
ATOM   3206 C  CG2 . THR A 1 442 ? -6.030  4.757   -85.815  1.00 46.59  ?  440 THR A CG2 1 
ATOM   3207 N  N   . CYS A 1 443 ? -7.720  7.878   -85.609  1.00 42.83  ?  441 CYS A N   1 
ATOM   3208 C  CA  . CYS A 1 443 ? -9.111  8.035   -85.215  1.00 42.66  ?  441 CYS A CA  1 
ATOM   3209 C  C   . CYS A 1 443 ? -9.830  6.706   -85.400  1.00 40.54  ?  441 CYS A C   1 
ATOM   3210 O  O   . CYS A 1 443 ? -9.807  6.126   -86.490  1.00 41.79  ?  441 CYS A O   1 
ATOM   3211 C  CB  . CYS A 1 443 ? -9.777  9.131   -86.048  1.00 38.92  ?  441 CYS A CB  1 
ATOM   3212 S  SG  . CYS A 1 443 ? -11.502 9.485   -85.634  1.00 39.37  ?  441 CYS A SG  1 
ATOM   3213 N  N   . ARG A 1 444 ? -10.474 6.227   -84.341  1.00 38.54  ?  442 ARG A N   1 
ATOM   3214 C  CA  . ARG A 1 444 ? -11.164 4.948   -84.377  1.00 39.42  ?  442 ARG A CA  1 
ATOM   3215 C  C   . ARG A 1 444 ? -12.678 5.095   -84.357  1.00 38.73  ?  442 ARG A C   1 
ATOM   3216 O  O   . ARG A 1 444 ? -13.388 4.097   -84.502  1.00 40.29  ?  442 ARG A O   1 
ATOM   3217 C  CB  . ARG A 1 444 ? -10.685 4.067   -83.215  1.00 44.85  ?  442 ARG A CB  1 
ATOM   3218 C  CG  . ARG A 1 444 ? -9.201  3.702   -83.318  1.00 46.98  ?  442 ARG A CG  1 
ATOM   3219 C  CD  . ARG A 1 444 ? -8.809  2.579   -82.369  1.00 63.54  ?  442 ARG A CD  1 
ATOM   3220 N  NE  . ARG A 1 444 ? -7.389  2.249   -82.451  1.00 71.33  ?  442 ARG A NE  1 
ATOM   3221 C  CZ  . ARG A 1 444 ? -6.397  3.064   -82.113  1.00 71.81  ?  442 ARG A CZ  1 
ATOM   3222 N  NH1 . ARG A 1 444 ? -6.614  4.166   -81.412  1.00 64.44  ?  442 ARG A NH1 1 
ATOM   3223 N  NH2 . ARG A 1 444 ? -5.146  2.720   -82.410  1.00 66.67  ?  442 ARG A NH2 1 
ATOM   3224 N  N   . ARG A 1 445 ? -13.188 6.317   -84.236  1.00 37.62  ?  443 ARG A N   1 
ATOM   3225 C  CA  . ARG A 1 445 ? -14.617 6.584   -84.141  1.00 40.67  ?  443 ARG A CA  1 
ATOM   3226 C  C   . ARG A 1 445 ? -15.279 6.943   -85.465  1.00 39.04  ?  443 ARG A C   1 
ATOM   3227 O  O   . ARG A 1 445 ? -16.375 6.454   -85.756  1.00 43.69  ?  443 ARG A O   1 
ATOM   3228 C  CB  . ARG A 1 445 ? -14.846 7.750   -83.174  1.00 36.15  ?  443 ARG A CB  1 
ATOM   3229 C  CG  . ARG A 1 445 ? -16.230 8.365   -83.265  1.00 43.74  ?  443 ARG A CG  1 
ATOM   3230 C  CD  . ARG A 1 445 ? -16.206 9.797   -82.755  1.00 44.72  ?  443 ARG A CD  1 
ATOM   3231 N  NE  . ARG A 1 445 ? -15.741 9.893   -81.378  1.00 48.19  ?  443 ARG A NE  1 
ATOM   3232 C  CZ  . ARG A 1 445 ? -15.485 11.036  -80.757  1.00 43.23  ?  443 ARG A CZ  1 
ATOM   3233 N  NH1 . ARG A 1 445 ? -15.513 12.191  -81.399  1.00 33.84  ?  443 ARG A NH1 1 
ATOM   3234 N  NH2 . ARG A 1 445 ? -15.156 11.015  -79.469  1.00 38.64  ?  443 ARG A NH2 1 
ATOM   3235 N  N   . CYS A 1 446 ? -14.636 7.755   -86.277  1.00 34.52  ?  444 CYS A N   1 
ATOM   3236 C  CA  . CYS A 1 446 ? -15.333 8.348   -87.408  1.00 39.25  ?  444 CYS A CA  1 
ATOM   3237 C  C   . CYS A 1 446 ? -15.072 7.614   -88.717  1.00 43.75  ?  444 CYS A C   1 
ATOM   3238 O  O   . CYS A 1 446 ? -13.979 7.084   -88.943  1.00 43.84  ?  444 CYS A O   1 
ATOM   3239 C  CB  . CYS A 1 446 ? -14.931 9.815   -87.569  1.00 33.33  ?  444 CYS A CB  1 
ATOM   3240 S  SG  . CYS A 1 446 ? -15.200 10.797  -86.078  1.00 37.78  ?  444 CYS A SG  1 
ATOM   3241 N  N   . PRO A 1 447 ? -16.090 7.573   -89.577  1.00 43.80  ?  445 PRO A N   1 
ATOM   3242 C  CA  . PRO A 1 447 ? -15.897 7.033   -90.924  1.00 38.14  ?  445 PRO A CA  1 
ATOM   3243 C  C   . PRO A 1 447 ? -14.794 7.796   -91.642  1.00 41.96  ?  445 PRO A C   1 
ATOM   3244 O  O   . PRO A 1 447 ? -14.563 8.981   -91.388  1.00 36.93  ?  445 PRO A O   1 
ATOM   3245 C  CB  . PRO A 1 447 ? -17.263 7.261   -91.583  1.00 38.43  ?  445 PRO A CB  1 
ATOM   3246 C  CG  . PRO A 1 447 ? -18.211 7.171   -90.414  1.00 46.36  ?  445 PRO A CG  1 
ATOM   3247 C  CD  . PRO A 1 447 ? -17.490 7.976   -89.362  1.00 43.74  ?  445 PRO A CD  1 
ATOM   3248 N  N   . ALA A 1 448 ? -14.114 7.101   -92.556  1.00 37.21  ?  446 ALA A N   1 
ATOM   3249 C  CA  . ALA A 1 448 ? -12.934 7.672   -93.202  1.00 37.39  ?  446 ALA A CA  1 
ATOM   3250 C  C   . ALA A 1 448 ? -13.228 9.009   -93.878  1.00 36.22  ?  446 ALA A C   1 
ATOM   3251 O  O   . ALA A 1 448 ? -12.380 9.909   -93.870  1.00 37.57  ?  446 ALA A O   1 
ATOM   3252 C  CB  . ALA A 1 448 ? -12.358 6.677   -94.210  1.00 36.50  ?  446 ALA A CB  1 
ATOM   3253 N  N   . GLU A 1 449 ? -14.413 9.159   -94.482  1.00 35.74  ?  447 GLU A N   1 
ATOM   3254 C  CA  . GLU A 1 449 ? -14.763 10.436  -95.106  1.00 33.92  ?  447 GLU A CA  1 
ATOM   3255 C  C   . GLU A 1 449 ? -14.597 11.605  -94.143  1.00 31.34  ?  447 GLU A C   1 
ATOM   3256 O  O   . GLU A 1 449 ? -14.066 12.657  -94.515  1.00 31.74  ?  447 GLU A O   1 
ATOM   3257 C  CB  . GLU A 1 449 ? -16.190 10.397  -95.661  1.00 35.13  ?  447 GLU A CB  1 
ATOM   3258 C  CG  . GLU A 1 449 ? -16.492 9.177   -96.521  1.00 42.15  ?  447 GLU A CG  1 
ATOM   3259 C  CD  . GLU A 1 449 ? -17.290 8.117   -95.790  1.00 46.57  ?  447 GLU A CD  1 
ATOM   3260 O  OE1 . GLU A 1 449 ? -16.863 7.696   -94.694  1.00 41.10  ?  447 GLU A OE1 1 
ATOM   3261 O  OE2 . GLU A 1 449 ? -18.337 7.691   -96.324  1.00 49.27  -1 447 GLU A OE2 1 
ATOM   3262 N  N   . ILE A 1 450 ? -15.049 11.443  -92.900  1.00 33.44  ?  448 ILE A N   1 
ATOM   3263 C  CA  . ILE A 1 450 ? -14.880 12.500  -91.910  1.00 28.78  ?  448 ILE A CA  1 
ATOM   3264 C  C   . ILE A 1 450 ? -13.407 12.667  -91.557  1.00 35.92  ?  448 ILE A C   1 
ATOM   3265 O  O   . ILE A 1 450 ? -12.872 13.783  -91.569  1.00 33.08  ?  448 ILE A O   1 
ATOM   3266 C  CB  . ILE A 1 450 ? -15.734 12.204  -90.665  1.00 31.14  ?  448 ILE A CB  1 
ATOM   3267 C  CG1 . ILE A 1 450 ? -17.217 12.160  -91.054  1.00 32.08  ?  448 ILE A CG1 1 
ATOM   3268 C  CG2 . ILE A 1 450 ? -15.464 13.236  -89.585  1.00 29.92  ?  448 ILE A CG2 1 
ATOM   3269 C  CD1 . ILE A 1 450 ? -18.134 11.679  -89.962  1.00 31.69  ?  448 ILE A CD1 1 
ATOM   3270 N  N   . VAL A 1 451 ? -12.726 11.559  -91.255  1.00 34.15  ?  449 VAL A N   1 
ATOM   3271 C  CA  . VAL A 1 451 ? -11.326 11.633  -90.845  1.00 36.18  ?  449 VAL A CA  1 
ATOM   3272 C  C   . VAL A 1 451 ? -10.503 12.334  -91.916  1.00 37.00  ?  449 VAL A C   1 
ATOM   3273 O  O   . VAL A 1 451 ? -9.744  13.268  -91.633  1.00 38.24  ?  449 VAL A O   1 
ATOM   3274 C  CB  . VAL A 1 451 ? -10.776 10.228  -90.546  1.00 37.53  ?  449 VAL A CB  1 
ATOM   3275 C  CG1 . VAL A 1 451 ? -9.284  10.294  -90.252  1.00 38.66  ?  449 VAL A CG1 1 
ATOM   3276 C  CG2 . VAL A 1 451 ? -11.524 9.604   -89.380  1.00 38.80  ?  449 VAL A CG2 1 
ATOM   3277 N  N   . ASP A 1 452 ? -10.655 11.902  -93.167  1.00 36.30  ?  450 ASP A N   1 
ATOM   3278 C  CA  . ASP A 1 452 ? -9.906  12.521  -94.251  1.00 35.84  ?  450 ASP A CA  1 
ATOM   3279 C  C   . ASP A 1 452 ? -10.137 14.029  -94.288  1.00 35.34  ?  450 ASP A C   1 
ATOM   3280 O  O   . ASP A 1 452 ? -9.188  14.800  -94.469  1.00 36.04  ?  450 ASP A O   1 
ATOM   3281 C  CB  . ASP A 1 452 ? -10.271 11.859  -95.583  1.00 34.58  ?  450 ASP A CB  1 
ATOM   3282 C  CG  . ASP A 1 452 ? -9.742  10.427  -95.689  1.00 46.38  ?  450 ASP A CG  1 
ATOM   3283 O  OD1 . ASP A 1 452 ? -8.974  10.002  -94.798  1.00 52.67  ?  450 ASP A OD1 1 
ATOM   3284 O  OD2 . ASP A 1 452 ? -10.100 9.720   -96.656  1.00 47.89  -1 450 ASP A OD2 1 
ATOM   3285 N  N   . THR A 1 453 ? -11.387 14.475  -94.105  1.00 29.01  ?  451 THR A N   1 
ATOM   3286 C  CA  . THR A 1 453 ? -11.666 15.907  -94.200  1.00 32.62  ?  451 THR A CA  1 
ATOM   3287 C  C   . THR A 1 453 ? -10.971 16.697  -93.094  1.00 34.59  ?  451 THR A C   1 
ATOM   3288 O  O   . THR A 1 453 ? -10.301 17.700  -93.368  1.00 35.82  ?  451 THR A O   1 
ATOM   3289 C  CB  . THR A 1 453 ? -13.173 16.171  -94.153  1.00 34.48  ?  451 THR A CB  1 
ATOM   3290 O  OG1 . THR A 1 453 ? -13.831 15.454  -95.203  1.00 40.35  ?  451 THR A OG1 1 
ATOM   3291 C  CG2 . THR A 1 453 ? -13.446 17.662  -94.305  1.00 32.31  ?  451 THR A CG2 1 
ATOM   3292 N  N   . VAL A 1 454 ? -11.110 16.259  -91.837  1.00 30.09  ?  452 VAL A N   1 
ATOM   3293 C  CA  . VAL A 1 454 ? -10.514 17.002  -90.726  1.00 31.39  ?  452 VAL A CA  1 
ATOM   3294 C  C   . VAL A 1 454 ? -8.995  16.906  -90.763  1.00 38.44  ?  452 VAL A C   1 
ATOM   3295 O  O   . VAL A 1 454 ? -8.294  17.870  -90.432  1.00 40.49  ?  452 VAL A O   1 
ATOM   3296 C  CB  . VAL A 1 454 ? -11.076 16.528  -89.372  1.00 34.51  ?  452 VAL A CB  1 
ATOM   3297 C  CG1 . VAL A 1 454 ? -12.589 16.734  -89.309  1.00 26.94  ?  452 VAL A CG1 1 
ATOM   3298 C  CG2 . VAL A 1 454 ? -10.695 15.084  -89.101  1.00 34.70  ?  452 VAL A CG2 1 
ATOM   3299 N  N   . SER A 1 455 ? -8.458  15.744  -91.151  1.00 41.45  ?  453 SER A N   1 
ATOM   3300 C  CA  . SER A 1 455 ? -7.008  15.578  -91.144  1.00 46.57  ?  453 SER A CA  1 
ATOM   3301 C  C   . SER A 1 455 ? -6.347  16.651  -91.994  1.00 43.99  ?  453 SER A C   1 
ATOM   3302 O  O   . SER A 1 455 ? -5.322  17.221  -91.604  1.00 45.89  ?  453 SER A O   1 
ATOM   3303 C  CB  . SER A 1 455 ? -6.631  14.185  -91.649  1.00 46.95  ?  453 SER A CB  1 
ATOM   3304 O  OG  . SER A 1 455 ? -5.295  13.863  -91.303  1.00 49.96  ?  453 SER A OG  1 
ATOM   3305 N  N   . ALA A 1 456 ? -6.935  16.957  -93.148  1.00 39.16  ?  454 ALA A N   1 
ATOM   3306 C  CA  . ALA A 1 456 ? -6.384  17.995  -94.004  1.00 46.01  ?  454 ALA A CA  1 
ATOM   3307 C  C   . ALA A 1 456 ? -6.722  19.379  -93.469  1.00 40.58  ?  454 ALA A C   1 
ATOM   3308 O  O   . ALA A 1 456 ? -5.913  20.303  -93.594  1.00 44.43  ?  454 ALA A O   1 
ATOM   3309 C  CB  . ALA A 1 456 ? -6.904  17.840  -95.435  1.00 36.09  ?  454 ALA A CB  1 
ATOM   3310 N  N   . LEU A 1 457 ? -7.898  19.531  -92.857  1.00 37.61  ?  455 LEU A N   1 
ATOM   3311 C  CA  . LEU A 1 457 ? -8.358  20.858  -92.470  1.00 41.76  ?  455 LEU A CA  1 
ATOM   3312 C  C   . LEU A 1 457 ? -7.555  21.425  -91.304  1.00 42.30  ?  455 LEU A C   1 
ATOM   3313 O  O   . LEU A 1 457 ? -7.160  22.595  -91.337  1.00 36.91  ?  455 LEU A O   1 
ATOM   3314 C  CB  . LEU A 1 457 ? -9.845  20.811  -92.120  1.00 35.83  ?  455 LEU A CB  1 
ATOM   3315 C  CG  . LEU A 1 457 ? -10.524 22.136  -91.762  1.00 40.52  ?  455 LEU A CG  1 
ATOM   3316 C  CD1 . LEU A 1 457 ? -11.044 22.821  -93.009  1.00 42.81  ?  455 LEU A CD1 1 
ATOM   3317 C  CD2 . LEU A 1 457 ? -11.655 21.915  -90.760  1.00 36.35  ?  455 LEU A CD2 1 
ATOM   3318 N  N   . VAL A 1 458 ? -7.275  20.620  -90.278  1.00 39.70  ?  456 VAL A N   1 
ATOM   3319 C  CA  . VAL A 1 458 ? -6.661  21.188  -89.080  1.00 42.43  ?  456 VAL A CA  1 
ATOM   3320 C  C   . VAL A 1 458 ? -5.467  20.385  -88.580  1.00 44.03  ?  456 VAL A C   1 
ATOM   3321 O  O   . VAL A 1 458 ? -4.723  20.855  -87.713  1.00 43.76  ?  456 VAL A O   1 
ATOM   3322 C  CB  . VAL A 1 458 ? -7.701  21.327  -87.953  1.00 41.13  ?  456 VAL A CB  1 
ATOM   3323 C  CG1 . VAL A 1 458 ? -8.645  22.489  -88.239  1.00 40.32  ?  456 VAL A CG1 1 
ATOM   3324 C  CG2 . VAL A 1 458 ? -8.464  20.025  -87.766  1.00 40.46  ?  456 VAL A CG2 1 
ATOM   3325 N  N   . TYR A 1 459 ? -5.268  19.178  -89.103  1.00 45.67  ?  457 TYR A N   1 
ATOM   3326 C  CA  . TYR A 1 459 ? -4.239  18.287  -88.580  1.00 46.74  ?  457 TYR A CA  1 
ATOM   3327 C  C   . TYR A 1 459 ? -3.093  18.059  -89.559  1.00 48.64  ?  457 TYR A C   1 
ATOM   3328 O  O   . TYR A 1 459 ? -2.288  17.145  -89.353  1.00 49.83  ?  457 TYR A O   1 
ATOM   3329 C  CB  . TYR A 1 459 ? -4.867  16.954  -88.171  1.00 45.93  ?  457 TYR A CB  1 
ATOM   3330 C  CG  . TYR A 1 459 ? -5.907  17.085  -87.077  1.00 42.08  ?  457 TYR A CG  1 
ATOM   3331 C  CD1 . TYR A 1 459 ? -5.564  17.559  -85.815  1.00 39.83  ?  457 TYR A CD1 1 
ATOM   3332 C  CD2 . TYR A 1 459 ? -7.234  16.752  -87.314  1.00 41.17  ?  457 TYR A CD2 1 
ATOM   3333 C  CE1 . TYR A 1 459 ? -6.516  17.681  -84.814  1.00 42.27  ?  457 TYR A CE1 1 
ATOM   3334 C  CE2 . TYR A 1 459 ? -8.192  16.874  -86.322  1.00 37.98  ?  457 TYR A CE2 1 
ATOM   3335 C  CZ  . TYR A 1 459 ? -7.829  17.338  -85.075  1.00 40.50  ?  457 TYR A CZ  1 
ATOM   3336 O  OH  . TYR A 1 459 ? -8.785  17.457  -84.089  1.00 36.67  ?  457 TYR A OH  1 
ATOM   3337 N  N   . ASP A 1 460 ? -3.001  18.868  -90.615  1.00 47.12  ?  458 ASP A N   1 
ATOM   3338 C  CA  . ASP A 1 460 ? -1.904  18.794  -91.580  1.00 54.01  ?  458 ASP A CA  1 
ATOM   3339 C  C   . ASP A 1 460 ? -1.679  17.361  -92.060  1.00 58.04  ?  458 ASP A C   1 
ATOM   3340 O  O   . ASP A 1 460 ? -0.546  16.915  -92.254  1.00 52.49  ?  458 ASP A O   1 
ATOM   3341 C  CB  . ASP A 1 460 ? -0.624  19.391  -90.987  1.00 56.87  ?  458 ASP A CB  1 
ATOM   3342 C  CG  . ASP A 1 460 ? 0.410   19.737  -92.048  1.00 66.92  ?  458 ASP A CG  1 
ATOM   3343 O  OD1 . ASP A 1 460 ? 0.081   20.517  -92.968  1.00 66.81  ?  458 ASP A OD1 1 
ATOM   3344 O  OD2 . ASP A 1 460 ? 1.558   19.252  -91.949  1.00 70.76  -1 458 ASP A OD2 1 
ATOM   3345 N  N   . ASN A 1 461 ? -2.778  16.632  -92.260  1.00 49.51  ?  459 ASN A N   1 
ATOM   3346 C  CA  . ASN A 1 461 ? -2.773  15.293  -92.843  1.00 49.90  ?  459 ASN A CA  1 
ATOM   3347 C  C   . ASN A 1 461 ? -2.067  14.266  -91.969  1.00 51.02  ?  459 ASN A C   1 
ATOM   3348 O  O   . ASN A 1 461 ? -1.623  13.227  -92.469  1.00 53.92  ?  459 ASN A O   1 
ATOM   3349 C  CB  . ASN A 1 461 ? -2.155  15.297  -94.246  1.00 51.62  ?  459 ASN A CB  1 
ATOM   3350 C  CG  . ASN A 1 461 ? -2.981  16.089  -95.238  1.00 59.72  ?  459 ASN A CG  1 
ATOM   3351 O  OD1 . ASN A 1 461 ? -4.061  15.659  -95.647  1.00 55.63  ?  459 ASN A OD1 1 
ATOM   3352 N  ND2 . ASN A 1 461 ? -2.479  17.255  -95.630  1.00 56.86  ?  459 ASN A ND2 1 
ATOM   3353 N  N   . LYS A 1 462 ? -1.973  14.520  -90.667  1.00 53.98  ?  460 LYS A N   1 
ATOM   3354 C  CA  . LYS A 1 462 ? -1.301  13.619  -89.743  1.00 52.67  ?  460 LYS A CA  1 
ATOM   3355 C  C   . LYS A 1 462 ? -2.276  12.718  -88.998  1.00 53.24  ?  460 LYS A C   1 
ATOM   3356 O  O   . LYS A 1 462 ? -1.840  11.840  -88.246  1.00 54.49  ?  460 LYS A O   1 
ATOM   3357 C  CB  . LYS A 1 462 ? -0.466  14.421  -88.738  1.00 51.22  ?  460 LYS A CB  1 
ATOM   3358 C  CG  . LYS A 1 462 ? 0.988   14.638  -89.148  1.00 67.57  ?  460 LYS A CG  1 
ATOM   3359 C  CD  . LYS A 1 462 ? 1.115   14.938  -90.636  1.00 68.45  ?  460 LYS A CD  1 
ATOM   3360 C  CE  . LYS A 1 462 ? 2.566   15.171  -91.039  1.00 75.15  ?  460 LYS A CE  1 
ATOM   3361 N  NZ  . LYS A 1 462 ? 2.697   15.429  -92.502  1.00 73.40  ?  460 LYS A NZ  1 
ATOM   3362 N  N   . LEU A 1 463 ? -3.579  12.901  -89.201  1.00 47.41  ?  461 LEU A N   1 
ATOM   3363 C  CA  . LEU A 1 463 ? -4.590  12.061  -88.577  1.00 44.69  ?  461 LEU A CA  1 
ATOM   3364 C  C   . LEU A 1 463 ? -4.965  10.933  -89.527  1.00 46.73  ?  461 LEU A C   1 
ATOM   3365 O  O   . LEU A 1 463 ? -5.292  11.178  -90.693  1.00 45.59  ?  461 LEU A O   1 
ATOM   3366 C  CB  . LEU A 1 463 ? -5.831  12.881  -88.220  1.00 43.81  ?  461 LEU A CB  1 
ATOM   3367 C  CG  . LEU A 1 463 ? -6.936  12.151  -87.451  1.00 45.42  ?  461 LEU A CG  1 
ATOM   3368 C  CD1 . LEU A 1 463 ? -6.408  11.621  -86.127  1.00 41.93  ?  461 LEU A CD1 1 
ATOM   3369 C  CD2 . LEU A 1 463 ? -8.152  13.048  -87.237  1.00 37.51  ?  461 LEU A CD2 1 
ATOM   3370 N  N   . LYS A 1 464 ? -4.930  9.703   -89.027  1.00 41.06  ?  462 LYS A N   1 
ATOM   3371 C  CA  . LYS A 1 464 ? -5.196  8.538   -89.853  1.00 45.35  ?  462 LYS A CA  1 
ATOM   3372 C  C   . LYS A 1 464 ? -6.542  7.943   -89.469  1.00 45.23  ?  462 LYS A C   1 
ATOM   3373 O  O   . LYS A 1 464 ? -7.011  8.097   -88.338  1.00 44.62  ?  462 LYS A O   1 
ATOM   3374 C  CB  . LYS A 1 464 ? -4.091  7.486   -89.701  1.00 47.45  ?  462 LYS A CB  1 
ATOM   3375 C  CG  . LYS A 1 464 ? -2.711  7.982   -90.105  1.00 58.37  ?  462 LYS A CG  1 
ATOM   3376 C  CD  . LYS A 1 464 ? -2.746  8.677   -91.460  1.00 64.72  ?  462 LYS A CD  1 
ATOM   3377 C  CE  . LYS A 1 464 ? -1.414  9.342   -91.775  1.00 68.56  ?  462 LYS A CE  1 
ATOM   3378 N  NZ  . LYS A 1 464 ? -1.415  9.973   -93.124  1.00 77.28  ?  462 LYS A NZ  1 
ATOM   3379 N  N   . ALA A 1 465 ? -7.151  7.246   -90.420  1.00 40.18  ?  463 ALA A N   1 
ATOM   3380 C  CA  . ALA A 1 465 ? -8.451  6.628   -90.222  1.00 46.73  ?  463 ALA A CA  1 
ATOM   3381 C  C   . ALA A 1 465 ? -8.292  5.130   -90.014  1.00 47.87  ?  463 ALA A C   1 
ATOM   3382 O  O   . ALA A 1 465 ? -7.573  4.466   -90.767  1.00 52.85  ?  463 ALA A O   1 
ATOM   3383 C  CB  . ALA A 1 465 ? -9.367  6.896   -91.417  1.00 40.85  ?  463 ALA A CB  1 
ATOM   3384 N  N   . HIS A 1 466 ? -8.964  4.606   -88.993  1.00 47.94  ?  464 HIS A N   1 
ATOM   3385 C  CA  . HIS A 1 466 ? -8.995  3.168   -88.773  1.00 49.33  ?  464 HIS A CA  1 
ATOM   3386 C  C   . HIS A 1 466 ? -10.186 2.544   -89.476  1.00 49.74  ?  464 HIS A C   1 
ATOM   3387 O  O   . HIS A 1 466 ? -10.088 1.433   -90.009  1.00 51.10  ?  464 HIS A O   1 
ATOM   3388 C  CB  . HIS A 1 466 ? -9.059  2.839   -87.282  1.00 50.35  ?  464 HIS A CB  1 
ATOM   3389 C  CG  . HIS A 1 466 ? -9.188  1.375   -87.007  1.00 49.74  ?  464 HIS A CG  1 
ATOM   3390 N  ND1 . HIS A 1 466 ? -8.141  0.493   -87.169  1.00 56.70  ?  464 HIS A ND1 1 
ATOM   3391 C  CD2 . HIS A 1 466 ? -10.252 0.630   -86.625  1.00 56.31  ?  464 HIS A CD2 1 
ATOM   3392 C  CE1 . HIS A 1 466 ? -8.548  -0.728  -86.873  1.00 63.51  ?  464 HIS A CE1 1 
ATOM   3393 N  NE2 . HIS A 1 466 ? -9.826  -0.672  -86.541  1.00 64.97  ?  464 HIS A NE2 1 
ATOM   3394 N  N   . LYS A 1 467 ? -11.310 3.249   -89.486  1.00 47.30  ?  465 LYS A N   1 
ATOM   3395 C  CA  . LYS A 1 467 ? -12.512 2.758   -90.124  1.00 47.86  ?  465 LYS A CA  1 
ATOM   3396 C  C   . LYS A 1 467 ? -12.443 2.998   -91.625  1.00 43.44  ?  465 LYS A C   1 
ATOM   3397 O  O   . LYS A 1 467 ? -11.674 3.826   -92.120  1.00 42.14  ?  465 LYS A O   1 
ATOM   3398 C  CB  . LYS A 1 467 ? -13.756 3.451   -89.567  1.00 47.16  ?  465 LYS A CB  1 
ATOM   3399 C  CG  . LYS A 1 467 ? -14.155 3.051   -88.163  1.00 51.47  ?  465 LYS A CG  1 
ATOM   3400 C  CD  . LYS A 1 467 ? -15.503 3.667   -87.822  1.00 46.71  ?  465 LYS A CD  1 
ATOM   3401 C  CE  . LYS A 1 467 ? -16.043 3.150   -86.502  1.00 49.23  ?  465 LYS A CE  1 
ATOM   3402 N  NZ  . LYS A 1 467 ? -17.365 3.761   -86.191  1.00 48.69  ?  465 LYS A NZ  1 
ATOM   3403 N  N   . ASP A 1 468 ? -13.270 2.255   -92.345  1.00 46.19  ?  466 ASP A N   1 
ATOM   3404 C  CA  . ASP A 1 468 ? -13.424 2.428   -93.775  1.00 49.48  ?  466 ASP A CA  1 
ATOM   3405 C  C   . ASP A 1 468 ? -14.396 3.573   -94.033  1.00 44.48  ?  466 ASP A C   1 
ATOM   3406 O  O   . ASP A 1 468 ? -15.022 4.107   -93.113  1.00 40.92  ?  466 ASP A O   1 
ATOM   3407 C  CB  . ASP A 1 468 ? -13.939 1.133   -94.406  1.00 48.37  ?  466 ASP A CB  1 
ATOM   3408 C  CG  . ASP A 1 468 ? -13.813 1.118   -95.915  1.00 55.88  ?  466 ASP A CG  1 
ATOM   3409 O  OD1 . ASP A 1 468 ? -13.209 2.053   -96.482  1.00 66.28  ?  466 ASP A OD1 1 
ATOM   3410 O  OD2 . ASP A 1 468 ? -14.333 0.168   -96.537  1.00 68.17  -1 466 ASP A OD2 1 
ATOM   3411 N  N   . LYS A 1 469 ? -14.509 3.973   -95.296  1.00 44.64  ?  467 LYS A N   1 
ATOM   3412 C  CA  . LYS A 1 469 ? -15.536 4.937   -95.656  1.00 44.19  ?  467 LYS A CA  1 
ATOM   3413 C  C   . LYS A 1 469 ? -16.899 4.306   -95.411  1.00 46.02  ?  467 LYS A C   1 
ATOM   3414 O  O   . LYS A 1 469 ? -17.132 3.149   -95.772  1.00 46.77  ?  467 LYS A O   1 
ATOM   3415 C  CB  . LYS A 1 469 ? -15.393 5.353   -97.120  1.00 48.52  ?  467 LYS A CB  1 
ATOM   3416 C  CG  . LYS A 1 469 ? -14.080 6.038   -97.454  1.00 52.56  ?  467 LYS A CG  1 
ATOM   3417 C  CD  . LYS A 1 469 ? -14.048 6.489   -98.905  1.00 53.55  ?  467 LYS A CD  1 
ATOM   3418 C  CE  . LYS A 1 469 ? -12.757 7.225   -99.222  1.00 60.96  ?  467 LYS A CE  1 
ATOM   3419 N  NZ  . LYS A 1 469 ? -12.832 7.960   -100.515 1.00 73.94  ?  467 LYS A NZ  1 
ATOM   3420 N  N   . SER A 1 470 ? -17.798 5.060   -94.776  1.00 41.83  ?  468 SER A N   1 
ATOM   3421 C  CA  . SER A 1 470 ? -19.104 4.507   -94.438  1.00 44.58  ?  468 SER A CA  1 
ATOM   3422 C  C   . SER A 1 470 ? -20.057 4.515   -95.622  1.00 45.03  ?  468 SER A C   1 
ATOM   3423 O  O   . SER A 1 470 ? -20.968 3.679   -95.687  1.00 42.08  ?  468 SER A O   1 
ATOM   3424 C  CB  . SER A 1 470 ? -19.735 5.290   -93.285  1.00 40.83  ?  468 SER A CB  1 
ATOM   3425 O  OG  . SER A 1 470 ? -20.061 6.612   -93.688  1.00 39.38  ?  468 SER A OG  1 
ATOM   3426 N  N   . ALA A 1 471 ? -19.880 5.452   -96.550  1.00 40.56  ?  469 ALA A N   1 
ATOM   3427 C  CA  . ALA A 1 471 ? -20.818 5.668   -97.642  1.00 40.17  ?  469 ALA A CA  1 
ATOM   3428 C  C   . ALA A 1 471 ? -22.154 6.171   -97.120  1.00 39.40  ?  469 ALA A C   1 
ATOM   3429 O  O   . ALA A 1 471 ? -23.176 6.062   -97.804  1.00 42.66  ?  469 ALA A O   1 
ATOM   3430 C  CB  . ALA A 1 471 ? -21.014 4.400   -98.482  1.00 49.28  ?  469 ALA A CB  1 
ATOM   3431 N  N   . GLN A 1 472 ? -22.155 6.696   -95.892  1.00 39.94  ?  470 GLN A N   1 
ATOM   3432 C  CA  . GLN A 1 472 ? -23.323 7.291   -95.257  1.00 43.58  ?  470 GLN A CA  1 
ATOM   3433 C  C   . GLN A 1 472 ? -23.016 8.714   -94.797  1.00 41.43  ?  470 GLN A C   1 
ATOM   3434 O  O   . GLN A 1 472 ? -23.592 9.196   -93.818  1.00 39.61  ?  470 GLN A O   1 
ATOM   3435 C  CB  . GLN A 1 472 ? -23.798 6.432   -94.084  1.00 40.67  ?  470 GLN A CB  1 
ATOM   3436 C  CG  . GLN A 1 472 ? -24.107 4.988   -94.465  1.00 46.17  ?  470 GLN A CG  1 
ATOM   3437 C  CD  . GLN A 1 472 ? -24.837 4.228   -93.372  1.00 46.61  ?  470 GLN A CD  1 
ATOM   3438 O  OE1 . GLN A 1 472 ? -25.946 4.591   -92.981  1.00 51.56  ?  470 GLN A OE1 1 
ATOM   3439 N  NE2 . GLN A 1 472 ? -24.214 3.165   -92.873  1.00 48.35  ?  470 GLN A NE2 1 
ATOM   3440 N  N   . CYS A 1 473 ? -22.083 9.382   -95.478  1.00 41.21  ?  471 CYS A N   1 
ATOM   3441 C  CA  . CYS A 1 473 ? -21.679 10.755  -95.184  1.00 40.26  ?  471 CYS A CA  1 
ATOM   3442 C  C   . CYS A 1 473 ? -22.067 11.620  -96.375  1.00 39.36  ?  471 CYS A C   1 
ATOM   3443 O  O   . CYS A 1 473 ? -21.442 11.531  -97.438  1.00 37.71  ?  471 CYS A O   1 
ATOM   3444 C  CB  . CYS A 1 473 ? -20.179 10.846  -94.907  1.00 37.82  ?  471 CYS A CB  1 
ATOM   3445 S  SG  . CYS A 1 473 ? -19.620 10.003  -93.406  1.00 38.68  ?  471 CYS A SG  1 
ATOM   3446 N  N   . PHE A 1 474 ? -23.088 12.455  -96.208  1.00 40.20  ?  472 PHE A N   1 
ATOM   3447 C  CA  . PHE A 1 474 ? -23.631 13.225  -97.316  1.00 39.61  ?  472 PHE A CA  1 
ATOM   3448 C  C   . PHE A 1 474 ? -23.522 14.718  -97.035  1.00 38.14  ?  472 PHE A C   1 
ATOM   3449 O  O   . PHE A 1 474 ? -23.478 15.157  -95.882  1.00 32.39  ?  472 PHE A O   1 
ATOM   3450 C  CB  . PHE A 1 474 ? -25.093 12.844  -97.576  1.00 43.46  ?  472 PHE A CB  1 
ATOM   3451 C  CG  . PHE A 1 474 ? -25.312 11.366  -97.736  1.00 43.54  ?  472 PHE A CG  1 
ATOM   3452 C  CD1 . PHE A 1 474 ? -25.078 10.745  -98.950  1.00 42.27  ?  472 PHE A CD1 1 
ATOM   3453 C  CD2 . PHE A 1 474 ? -25.752 10.597  -96.670  1.00 43.13  ?  472 PHE A CD2 1 
ATOM   3454 C  CE1 . PHE A 1 474 ? -25.280 9.383   -99.100  1.00 42.10  ?  472 PHE A CE1 1 
ATOM   3455 C  CE2 . PHE A 1 474 ? -25.955 9.237   -96.812  1.00 43.12  ?  472 PHE A CE2 1 
ATOM   3456 C  CZ  . PHE A 1 474 ? -25.718 8.628   -98.028  1.00 43.76  ?  472 PHE A CZ  1 
ATOM   3457 N  N   . LYS A 1 475 ? -23.496 15.503  -98.112  1.00 32.64  ?  473 LYS A N   1 
ATOM   3458 C  CA  . LYS A 1 475 ? -23.417 16.951  -98.005  1.00 28.48  ?  473 LYS A CA  1 
ATOM   3459 C  C   . LYS A 1 475 ? -24.369 17.590  -99.005  1.00 32.69  ?  473 LYS A C   1 
ATOM   3460 O  O   . LYS A 1 475 ? -24.675 17.014  -100.053 1.00 34.92  ?  473 LYS A O   1 
ATOM   3461 C  CB  . LYS A 1 475 ? -21.981 17.457  -98.233  1.00 29.14  ?  473 LYS A CB  1 
ATOM   3462 C  CG  . LYS A 1 475 ? -21.438 17.242  -99.655  1.00 30.44  ?  473 LYS A CG  1 
ATOM   3463 C  CD  . LYS A 1 475 ? -20.031 17.814  -99.786  1.00 30.60  ?  473 LYS A CD  1 
ATOM   3464 C  CE  . LYS A 1 475 ? -19.548 17.823  -101.236 1.00 39.29  ?  473 LYS A CE  1 
ATOM   3465 N  NZ  . LYS A 1 475 ? -18.186 18.415  -101.353 1.00 34.18  ?  473 LYS A NZ  1 
ATOM   3466 N  N   . MET A 1 476 ? -24.828 18.794  -98.671  1.00 34.67  ?  474 MET A N   1 
ATOM   3467 C  CA  . MET A 1 476 ? -25.715 19.552  -99.544  1.00 31.52  ?  474 MET A CA  1 
ATOM   3468 C  C   . MET A 1 476 ? -25.501 21.037  -99.304  1.00 30.28  ?  474 MET A C   1 
ATOM   3469 O  O   . MET A 1 476 ? -25.466 21.484  -98.154  1.00 32.63  ?  474 MET A O   1 
ATOM   3470 C  CB  . MET A 1 476 ? -27.184 19.192  -99.308  1.00 38.73  ?  474 MET A CB  1 
ATOM   3471 C  CG  . MET A 1 476 ? -28.091 19.577  -100.465 1.00 46.44  ?  474 MET A CG  1 
ATOM   3472 S  SD  . MET A 1 476 ? -29.839 19.551  -100.020 1.00 53.86  ?  474 MET A SD  1 
ATOM   3473 C  CE  . MET A 1 476 ? -29.963 17.916  -99.297  1.00 51.65  ?  474 MET A CE  1 
ATOM   3474 N  N   . PHE A 1 477 ? -25.346 21.789  -100.387 1.00 32.28  ?  475 PHE A N   1 
ATOM   3475 C  CA  . PHE A 1 477 ? -25.185 23.237  -100.329 1.00 33.06  ?  475 PHE A CA  1 
ATOM   3476 C  C   . PHE A 1 477 ? -26.553 23.879  -100.559 1.00 33.97  ?  475 PHE A C   1 
ATOM   3477 O  O   . PHE A 1 477 ? -27.109 23.799  -101.659 1.00 34.66  ?  475 PHE A O   1 
ATOM   3478 C  CB  . PHE A 1 477 ? -24.143 23.675  -101.358 1.00 35.15  ?  475 PHE A CB  1 
ATOM   3479 C  CG  . PHE A 1 477 ? -23.814 25.137  -101.321 1.00 44.19  ?  475 PHE A CG  1 
ATOM   3480 C  CD1 . PHE A 1 477 ? -22.857 25.621  -100.444 1.00 35.97  ?  475 PHE A CD1 1 
ATOM   3481 C  CD2 . PHE A 1 477 ? -24.396 26.013  -102.220 1.00 45.14  ?  475 PHE A CD2 1 
ATOM   3482 C  CE1 . PHE A 1 477 ? -22.536 26.962  -100.420 1.00 44.06  ?  475 PHE A CE1 1 
ATOM   3483 C  CE2 . PHE A 1 477 ? -24.072 27.356  -102.207 1.00 43.86  ?  475 PHE A CE2 1 
ATOM   3484 C  CZ  . PHE A 1 477 ? -23.139 27.831  -101.307 1.00 47.89  ?  475 PHE A CZ  1 
ATOM   3485 N  N   . TYR A 1 478 ? -27.084 24.527  -99.519  1.00 31.28  ?  476 TYR A N   1 
ATOM   3486 C  CA  . TYR A 1 478 ? -28.407 25.152  -99.578  1.00 34.58  ?  476 TYR A CA  1 
ATOM   3487 C  C   . TYR A 1 478 ? -28.402 26.339  -98.616  1.00 34.09  ?  476 TYR A C   1 
ATOM   3488 O  O   . TYR A 1 478 ? -28.530 26.153  -97.401  1.00 31.26  ?  476 TYR A O   1 
ATOM   3489 C  CB  . TYR A 1 478 ? -29.477 24.127  -99.211  1.00 39.97  ?  476 TYR A CB  1 
ATOM   3490 C  CG  . TYR A 1 478 ? -30.917 24.544  -99.422  1.00 45.80  ?  476 TYR A CG  1 
ATOM   3491 C  CD1 . TYR A 1 478 ? -31.632 25.179  -98.416  1.00 45.86  ?  476 TYR A CD1 1 
ATOM   3492 C  CD2 . TYR A 1 478 ? -31.571 24.268  -100.615 1.00 49.93  ?  476 TYR A CD2 1 
ATOM   3493 C  CE1 . TYR A 1 478 ? -32.953 25.546  -98.599  1.00 49.36  ?  476 TYR A CE1 1 
ATOM   3494 C  CE2 . TYR A 1 478 ? -32.891 24.633  -100.809 1.00 52.95  ?  476 TYR A CE2 1 
ATOM   3495 C  CZ  . TYR A 1 478 ? -33.577 25.272  -99.797  1.00 52.72  ?  476 TYR A CZ  1 
ATOM   3496 O  OH  . TYR A 1 478 ? -34.891 25.637  -99.987  1.00 59.05  ?  476 TYR A OH  1 
ATOM   3497 N  N   . LYS A 1 479 ? -28.275 27.553  -99.160  1.00 32.71  ?  477 LYS A N   1 
ATOM   3498 C  CA  . LYS A 1 479 ? -28.164 28.732  -98.301  1.00 37.89  ?  477 LYS A CA  1 
ATOM   3499 C  C   . LYS A 1 479 ? -29.444 28.976  -97.505  1.00 37.65  ?  477 LYS A C   1 
ATOM   3500 O  O   . LYS A 1 479 ? -29.387 29.378  -96.337  1.00 34.12  ?  477 LYS A O   1 
ATOM   3501 C  CB  . LYS A 1 479 ? -27.797 29.963  -99.132  1.00 42.58  ?  477 LYS A CB  1 
ATOM   3502 C  CG  . LYS A 1 479 ? -26.331 30.016  -99.571  1.00 40.27  ?  477 LYS A CG  1 
ATOM   3503 C  CD  . LYS A 1 479 ? -26.136 31.005  -100.715 1.00 51.77  ?  477 LYS A CD  1 
ATOM   3504 C  CE  . LYS A 1 479 ? -24.679 31.092  -101.153 1.00 49.55  ?  477 LYS A CE  1 
ATOM   3505 N  NZ  . LYS A 1 479 ? -23.861 31.961  -100.262 1.00 58.99  ?  477 LYS A NZ  1 
ATOM   3506 N  N   . GLY A 1 480 ? -30.603 28.743  -98.116  1.00 40.77  ?  478 GLY A N   1 
ATOM   3507 C  CA  . GLY A 1 480 ? -31.862 28.903  -97.403  1.00 42.71  ?  478 GLY A CA  1 
ATOM   3508 C  C   . GLY A 1 480 ? -32.191 30.356  -97.110  1.00 43.17  ?  478 GLY A C   1 
ATOM   3509 O  O   . GLY A 1 480 ? -31.919 31.258  -97.909  1.00 42.88  ?  478 GLY A O   1 
ATOM   3510 N  N   . VAL A 1 481 ? -32.798 30.585  -95.946  1.00 43.72  ?  479 VAL A N   1 
ATOM   3511 C  CA  . VAL A 1 481 ? -33.203 31.915  -95.499  1.00 44.82  ?  479 VAL A CA  1 
ATOM   3512 C  C   . VAL A 1 481 ? -32.843 32.053  -94.028  1.00 44.53  ?  479 VAL A C   1 
ATOM   3513 O  O   . VAL A 1 481 ? -33.176 31.177  -93.222  1.00 45.01  ?  479 VAL A O   1 
ATOM   3514 C  CB  . VAL A 1 481 ? -34.712 32.156  -95.710  1.00 47.57  ?  479 VAL A CB  1 
ATOM   3515 C  CG1 . VAL A 1 481 ? -35.138 33.474  -95.075  1.00 48.39  ?  479 VAL A CG1 1 
ATOM   3516 C  CG2 . VAL A 1 481 ? -35.055 32.125  -97.190  1.00 48.61  ?  479 VAL A CG2 1 
ATOM   3517 N  N   . ILE A 1 482 ? -32.163 33.137  -93.669  1.00 44.11  ?  480 ILE A N   1 
ATOM   3518 C  CA  . ILE A 1 482 ? -31.677 33.319  -92.307  1.00 45.06  ?  480 ILE A CA  1 
ATOM   3519 C  C   . ILE A 1 482 ? -32.541 34.347  -91.595  1.00 51.32  ?  480 ILE A C   1 
ATOM   3520 O  O   . ILE A 1 482 ? -32.631 35.507  -92.018  1.00 48.59  ?  480 ILE A O   1 
ATOM   3521 C  CB  . ILE A 1 482 ? -30.197 33.734  -92.262  1.00 42.58  ?  480 ILE A CB  1 
ATOM   3522 C  CG1 . ILE A 1 482 ? -29.320 32.722  -93.003  1.00 40.97  ?  480 ILE A CG1 1 
ATOM   3523 C  CG2 . ILE A 1 482 ? -29.742 33.910  -90.819  1.00 44.74  ?  480 ILE A CG2 1 
ATOM   3524 C  CD1 . ILE A 1 482 ? -29.085 33.054  -94.452  1.00 38.59  ?  480 ILE A CD1 1 
ATOM   3525 N  N   . THR A 1 483 ? -33.163 33.914  -90.507  1.00 50.72  ?  481 THR A N   1 
ATOM   3526 C  CA  . THR A 1 483 ? -33.955 34.749  -89.625  1.00 51.94  ?  481 THR A CA  1 
ATOM   3527 C  C   . THR A 1 483 ? -33.212 34.788  -88.296  1.00 51.83  ?  481 THR A C   1 
ATOM   3528 O  O   . THR A 1 483 ? -32.350 33.948  -88.028  1.00 51.39  ?  481 THR A O   1 
ATOM   3529 C  CB  . THR A 1 483 ? -35.382 34.200  -89.462  1.00 52.56  ?  481 THR A CB  1 
ATOM   3530 O  OG1 . THR A 1 483 ? -36.057 34.239  -90.726  1.00 52.80  ?  481 THR A OG1 1 
ATOM   3531 C  CG2 . THR A 1 483 ? -36.175 35.041  -88.479  1.00 57.35  ?  481 THR A CG2 1 
ATOM   3532 N  N   . HIS A 1 484 ? -33.534 35.766  -87.459  1.00 51.92  ?  482 HIS A N   1 
ATOM   3533 C  CA  . HIS A 1 484 ? -32.798 35.922  -86.212  1.00 52.18  ?  482 HIS A CA  1 
ATOM   3534 C  C   . HIS A 1 484 ? -33.739 36.184  -85.050  1.00 57.05  ?  482 HIS A C   1 
ATOM   3535 O  O   . HIS A 1 484 ? -34.621 37.044  -85.139  1.00 58.56  ?  482 HIS A O   1 
ATOM   3536 C  CB  . HIS A 1 484 ? -31.765 37.054  -86.301  1.00 51.05  ?  482 HIS A CB  1 
ATOM   3537 C  CG  . HIS A 1 484 ? -30.794 36.907  -87.432  1.00 50.14  ?  482 HIS A CG  1 
ATOM   3538 N  ND1 . HIS A 1 484 ? -29.578 36.275  -87.290  1.00 49.59  ?  482 HIS A ND1 1 
ATOM   3539 C  CD2 . HIS A 1 484 ? -30.851 37.326  -88.718  1.00 48.94  ?  482 HIS A CD2 1 
ATOM   3540 C  CE1 . HIS A 1 484 ? -28.931 36.302  -88.441  1.00 47.79  ?  482 HIS A CE1 1 
ATOM   3541 N  NE2 . HIS A 1 484 ? -29.682 36.935  -89.325  1.00 47.96  ?  482 HIS A NE2 1 
ATOM   3542 N  N   . ASP A 1 485 ? -33.562 35.414  -83.979  1.00 62.36  ?  483 ASP A N   1 
ATOM   3543 C  CA  . ASP A 1 485 ? -34.262 35.638  -82.718  1.00 66.32  ?  483 ASP A CA  1 
ATOM   3544 C  C   . ASP A 1 485 ? -33.271 36.453  -81.893  1.00 66.60  ?  483 ASP A C   1 
ATOM   3545 O  O   . ASP A 1 485 ? -32.381 35.910  -81.236  1.00 70.39  ?  483 ASP A O   1 
ATOM   3546 C  CB  . ASP A 1 485 ? -34.649 34.322  -82.051  1.00 64.46  ?  483 ASP A CB  1 
ATOM   3547 C  CG  . ASP A 1 485 ? -35.646 34.510  -80.922  1.00 85.68  ?  483 ASP A CG  1 
ATOM   3548 O  OD1 . ASP A 1 485 ? -35.395 35.360  -80.040  1.00 84.12  ?  483 ASP A OD1 1 
ATOM   3549 O  OD2 . ASP A 1 485 ? -36.682 33.811  -80.918  1.00 92.97  -1 483 ASP A OD2 1 
ATOM   3550 N  N   . VAL A 1 486 ? -33.416 37.776  -81.964  1.00 70.49  ?  484 VAL A N   1 
ATOM   3551 C  CA  . VAL A 1 486 ? -32.474 38.714  -81.362  1.00 72.45  ?  484 VAL A CA  1 
ATOM   3552 C  C   . VAL A 1 486 ? -31.216 38.667  -82.218  1.00 70.83  ?  484 VAL A C   1 
ATOM   3553 O  O   . VAL A 1 486 ? -31.089 39.405  -83.202  1.00 77.96  ?  484 VAL A O   1 
ATOM   3554 C  CB  . VAL A 1 486 ? -32.172 38.391  -79.888  1.00 71.89  ?  484 VAL A CB  1 
ATOM   3555 C  CG1 . VAL A 1 486 ? -31.238 39.441  -79.306  1.00 68.15  ?  484 VAL A CG1 1 
ATOM   3556 C  CG2 . VAL A 1 486 ? -33.461 38.336  -79.086  1.00 71.71  ?  484 VAL A CG2 1 
ATOM   3557 N  N   . SER A 1 487 ? -30.292 37.778  -81.860  1.00 71.65  ?  485 SER A N   1 
ATOM   3558 C  CA  . SER A 1 487 ? -29.075 37.554  -82.629  1.00 66.84  ?  485 SER A CA  1 
ATOM   3559 C  C   . SER A 1 487 ? -28.821 36.087  -82.930  1.00 66.88  ?  485 SER A C   1 
ATOM   3560 O  O   . SER A 1 487 ? -28.022 35.792  -83.828  1.00 68.46  ?  485 SER A O   1 
ATOM   3561 C  CB  . SER A 1 487 ? -27.854 38.133  -81.899  1.00 61.67  ?  485 SER A CB  1 
ATOM   3562 O  OG  . SER A 1 487 ? -28.092 39.473  -81.503  1.00 75.52  ?  485 SER A OG  1 
ATOM   3563 N  N   . SER A 1 488 ? -29.458 35.163  -82.213  1.00 64.74  ?  486 SER A N   1 
ATOM   3564 C  CA  . SER A 1 488 ? -29.332 33.745  -82.516  1.00 59.58  ?  486 SER A CA  1 
ATOM   3565 C  C   . SER A 1 488 ? -29.972 33.473  -83.872  1.00 53.84  ?  486 SER A C   1 
ATOM   3566 O  O   . SER A 1 488 ? -31.105 33.892  -84.126  1.00 55.14  ?  486 SER A O   1 
ATOM   3567 C  CB  . SER A 1 488 ? -29.994 32.909  -81.422  1.00 62.06  ?  486 SER A CB  1 
ATOM   3568 O  OG  . SER A 1 488 ? -29.513 31.576  -81.433  1.00 57.85  ?  486 SER A OG  1 
ATOM   3569 N  N   . ALA A 1 489 ? -29.258 32.765  -84.740  1.00 48.20  ?  487 ALA A N   1 
ATOM   3570 C  CA  . ALA A 1 489 ? -29.721 32.567  -86.105  1.00 49.83  ?  487 ALA A CA  1 
ATOM   3571 C  C   . ALA A 1 489 ? -30.610 31.337  -86.250  1.00 45.69  ?  487 ALA A C   1 
ATOM   3572 O  O   . ALA A 1 489 ? -30.511 30.371  -85.489  1.00 41.70  ?  487 ALA A O   1 
ATOM   3573 C  CB  . ALA A 1 489 ? -28.530 32.450  -87.057  1.00 48.52  ?  487 ALA A CB  1 
ATOM   3574 N  N   . ILE A 1 490 ? -31.474 31.389  -87.261  1.00 47.27  ?  488 ILE A N   1 
ATOM   3575 C  CA  . ILE A 1 490 ? -32.392 30.311  -87.613  1.00 44.62  ?  488 ILE A CA  1 
ATOM   3576 C  C   . ILE A 1 490 ? -32.439 30.218  -89.132  1.00 45.62  ?  488 ILE A C   1 
ATOM   3577 O  O   . ILE A 1 490 ? -32.435 31.242  -89.823  1.00 49.24  ?  488 ILE A O   1 
ATOM   3578 C  CB  . ILE A 1 490 ? -33.808 30.548  -87.044  1.00 45.27  ?  488 ILE A CB  1 
ATOM   3579 C  CG1 . ILE A 1 490 ? -33.780 30.605  -85.515  1.00 44.75  ?  488 ILE A CG1 1 
ATOM   3580 C  CG2 . ILE A 1 490 ? -34.769 29.478  -87.535  1.00 43.25  ?  488 ILE A CG2 1 
ATOM   3581 C  CD1 . ILE A 1 490 ? -35.084 31.084  -84.904  1.00 45.45  ?  488 ILE A CD1 1 
ATOM   3582 N  N   . ASN A 1 491 ? -32.474 28.993  -89.655  1.00 40.95  ?  489 ASN A N   1 
ATOM   3583 C  CA  . ASN A 1 491 ? -32.646 28.762  -91.091  1.00 40.34  ?  489 ASN A CA  1 
ATOM   3584 C  C   . ASN A 1 491 ? -33.731 27.702  -91.273  1.00 40.94  ?  489 ASN A C   1 
ATOM   3585 O  O   . ASN A 1 491 ? -33.438 26.506  -91.356  1.00 35.94  ?  489 ASN A O   1 
ATOM   3586 C  CB  . ASN A 1 491 ? -31.329 28.347  -91.749  1.00 36.19  ?  489 ASN A CB  1 
ATOM   3587 C  CG  . ASN A 1 491 ? -31.372 28.460  -93.260  1.00 36.94  ?  489 ASN A CG  1 
ATOM   3588 O  OD1 . ASN A 1 491 ? -32.324 28.017  -93.902  1.00 38.93  ?  489 ASN A OD1 1 
ATOM   3589 N  ND2 . ASN A 1 491 ? -30.329 29.048  -93.838  1.00 35.48  ?  489 ASN A ND2 1 
ATOM   3590 N  N   . ARG A 1 492 ? -34.987 28.147  -91.310  1.00 42.73  ?  490 ARG A N   1 
ATOM   3591 C  CA  . ARG A 1 492 ? -36.103 27.221  -91.491  1.00 42.03  ?  490 ARG A CA  1 
ATOM   3592 C  C   . ARG A 1 492 ? -35.964 26.400  -92.767  1.00 41.45  ?  490 ARG A C   1 
ATOM   3593 O  O   . ARG A 1 492 ? -36.157 25.173  -92.710  1.00 39.49  ?  490 ARG A O   1 
ATOM   3594 C  CB  . ARG A 1 492 ? -37.423 27.998  -91.443  1.00 45.03  ?  490 ARG A CB  1 
ATOM   3595 C  CG  . ARG A 1 492 ? -37.577 28.853  -90.186  1.00 50.39  ?  490 ARG A CG  1 
ATOM   3596 C  CD  . ARG A 1 492 ? -39.011 29.324  -89.954  1.00 54.39  ?  490 ARG A CD  1 
ATOM   3597 N  NE  . ARG A 1 492 ? -39.326 29.503  -88.540  1.00 53.02  ?  490 ARG A NE  1 
ATOM   3598 C  CZ  . ARG A 1 492 ? -39.781 28.553  -87.734  1.00 65.55  ?  490 ARG A CZ  1 
ATOM   3599 N  NH1 . ARG A 1 492 ? -40.179 27.381  -88.200  1.00 55.88  ?  490 ARG A NH1 1 
ATOM   3600 N  NH2 . ARG A 1 492 ? -39.902 28.810  -86.434  1.00 65.97  ?  490 ARG A NH2 1 
ATOM   3601 N  N   . PRO A 1 493 ? -35.683 26.987  -93.934  1.00 43.40  ?  491 PRO A N   1 
ATOM   3602 C  CA  . PRO A 1 493 ? -35.514 26.164  -95.145  1.00 43.88  ?  491 PRO A CA  1 
ATOM   3603 C  C   . PRO A 1 493 ? -34.506 25.034  -94.988  1.00 41.24  ?  491 PRO A C   1 
ATOM   3604 O  O   . PRO A 1 493 ? -34.690 23.970  -95.596  1.00 42.04  ?  491 PRO A O   1 
ATOM   3605 C  CB  . PRO A 1 493 ? -35.069 27.195  -96.190  1.00 46.21  ?  491 PRO A CB  1 
ATOM   3606 C  CG  . PRO A 1 493 ? -35.738 28.453  -95.728  1.00 47.31  ?  491 PRO A CG  1 
ATOM   3607 C  CD  . PRO A 1 493 ? -35.541 28.420  -94.237  1.00 45.60  ?  491 PRO A CD  1 
ATOM   3608 N  N   . GLN A 1 494 ? -33.442 25.221  -94.200  1.00 38.10  ?  492 GLN A N   1 
ATOM   3609 C  CA  . GLN A 1 494 ? -32.490 24.130  -94.011  1.00 34.84  ?  492 GLN A CA  1 
ATOM   3610 C  C   . GLN A 1 494 ? -33.111 23.013  -93.182  1.00 34.89  ?  492 GLN A C   1 
ATOM   3611 O  O   . GLN A 1 494 ? -32.817 21.833  -93.411  1.00 32.92  ?  492 GLN A O   1 
ATOM   3612 C  CB  . GLN A 1 494 ? -31.196 24.637  -93.363  1.00 30.82  ?  492 GLN A CB  1 
ATOM   3613 C  CG  . GLN A 1 494 ? -30.225 25.312  -94.335  1.00 37.51  ?  492 GLN A CG  1 
ATOM   3614 C  CD  . GLN A 1 494 ? -28.903 25.693  -93.685  1.00 42.72  ?  492 GLN A CD  1 
ATOM   3615 O  OE1 . GLN A 1 494 ? -28.729 25.558  -92.472  1.00 27.37  ?  492 GLN A OE1 1 
ATOM   3616 N  NE2 . GLN A 1 494 ? -27.964 26.176  -94.493  1.00 27.49  ?  492 GLN A NE2 1 
ATOM   3617 N  N   . ILE A 1 495 ? -33.967 23.363  -92.215  1.00 33.85  ?  493 ILE A N   1 
ATOM   3618 C  CA  . ILE A 1 495 ? -34.706 22.341  -91.478  1.00 40.51  ?  493 ILE A CA  1 
ATOM   3619 C  C   . ILE A 1 495 ? -35.651 21.606  -92.417  1.00 39.73  ?  493 ILE A C   1 
ATOM   3620 O  O   . ILE A 1 495 ? -35.821 20.384  -92.323  1.00 41.59  ?  493 ILE A O   1 
ATOM   3621 C  CB  . ILE A 1 495 ? -35.473 22.968  -90.298  1.00 37.47  ?  493 ILE A CB  1 
ATOM   3622 C  CG1 . ILE A 1 495 ? -34.548 23.827  -89.434  1.00 39.74  ?  493 ILE A CG1 1 
ATOM   3623 C  CG2 . ILE A 1 495 ? -36.160 21.886  -89.471  1.00 39.83  ?  493 ILE A CG2 1 
ATOM   3624 C  CD1 . ILE A 1 495 ? -33.598 23.025  -88.584  1.00 46.96  ?  493 ILE A CD1 1 
ATOM   3625 N  N   . GLY A 1 496 ? -36.275 22.338  -93.341  1.00 38.91  ?  494 GLY A N   1 
ATOM   3626 C  CA  . GLY A 1 496 ? -37.205 21.705  -94.258  1.00 40.11  ?  494 GLY A CA  1 
ATOM   3627 C  C   . GLY A 1 496 ? -36.516 20.662  -95.113  1.00 39.71  ?  494 GLY A C   1 
ATOM   3628 O  O   . GLY A 1 496 ? -37.051 19.574  -95.338  1.00 44.16  ?  494 GLY A O   1 
ATOM   3629 N  N   . VAL A 1 497 ? -35.316 20.985  -95.600  1.00 40.56  ?  495 VAL A N   1 
ATOM   3630 C  CA  . VAL A 1 497 ? -34.539 20.029  -96.381  1.00 42.08  ?  495 VAL A CA  1 
ATOM   3631 C  C   . VAL A 1 497 ? -34.254 18.779  -95.559  1.00 40.35  ?  495 VAL A C   1 
ATOM   3632 O  O   . VAL A 1 497 ? -34.293 17.656  -96.076  1.00 40.33  ?  495 VAL A O   1 
ATOM   3633 C  CB  . VAL A 1 497 ? -33.238 20.688  -96.871  1.00 43.67  ?  495 VAL A CB  1 
ATOM   3634 C  CG1 . VAL A 1 497 ? -32.263 19.634  -97.365  1.00 45.20  ?  495 VAL A CG1 1 
ATOM   3635 C  CG2 . VAL A 1 497 ? -33.535 21.722  -97.947  1.00 47.63  ?  495 VAL A CG2 1 
ATOM   3636 N  N   . VAL A 1 498 ? -33.975 18.951  -94.265  1.00 35.54  ?  496 VAL A N   1 
ATOM   3637 C  CA  . VAL A 1 498 ? -33.715 17.795  -93.413  1.00 39.12  ?  496 VAL A CA  1 
ATOM   3638 C  C   . VAL A 1 498 ? -34.974 16.951  -93.296  1.00 43.13  ?  496 VAL A C   1 
ATOM   3639 O  O   . VAL A 1 498 ? -34.922 15.717  -93.354  1.00 42.30  ?  496 VAL A O   1 
ATOM   3640 C  CB  . VAL A 1 498 ? -33.194 18.242  -92.036  1.00 36.55  ?  496 VAL A CB  1 
ATOM   3641 C  CG1 . VAL A 1 498 ? -33.038 17.043  -91.112  1.00 35.81  ?  496 VAL A CG1 1 
ATOM   3642 C  CG2 . VAL A 1 498 ? -31.871 18.972  -92.184  1.00 36.04  ?  496 VAL A CG2 1 
ATOM   3643 N  N   . ARG A 1 499 ? -36.124 17.606  -93.131  1.00 43.87  ?  497 ARG A N   1 
ATOM   3644 C  CA  . ARG A 1 499 ? -37.390 16.887  -93.069  1.00 47.20  ?  497 ARG A CA  1 
ATOM   3645 C  C   . ARG A 1 499 ? -37.580 16.030  -94.316  1.00 51.75  ?  497 ARG A C   1 
ATOM   3646 O  O   . ARG A 1 499 ? -37.939 14.850  -94.226  1.00 58.32  ?  497 ARG A O   1 
ATOM   3647 C  CB  . ARG A 1 499 ? -38.533 17.887  -92.910  1.00 45.91  ?  497 ARG A CB  1 
ATOM   3648 C  CG  . ARG A 1 499 ? -39.913 17.285  -92.704  1.00 54.35  ?  497 ARG A CG  1 
ATOM   3649 C  CD  . ARG A 1 499 ? -40.915 18.413  -92.569  1.00 58.72  ?  497 ARG A CD  1 
ATOM   3650 N  NE  . ARG A 1 499 ? -40.667 19.412  -93.602  1.00 74.03  ?  497 ARG A NE  1 
ATOM   3651 C  CZ  . ARG A 1 499 ? -41.241 20.606  -93.660  1.00 79.99  ?  497 ARG A CZ  1 
ATOM   3652 N  NH1 . ARG A 1 499 ? -41.986 21.065  -92.667  1.00 77.76  ?  497 ARG A NH1 1 
ATOM   3653 N  NH2 . ARG A 1 499 ? -41.009 21.385  -94.713  1.00 68.79  ?  497 ARG A NH2 1 
ATOM   3654 N  N   . GLU A 1 500 ? -37.342 16.613  -95.497  1.00 50.15  ?  498 GLU A N   1 
ATOM   3655 C  CA  . GLU A 1 500 ? -37.486 15.851  -96.734  1.00 59.91  ?  498 GLU A CA  1 
ATOM   3656 C  C   . GLU A 1 500 ? -36.517 14.674  -96.772  1.00 52.96  ?  498 GLU A C   1 
ATOM   3657 O  O   . GLU A 1 500 ? -36.806 13.651  -97.403  1.00 59.83  ?  498 GLU A O   1 
ATOM   3658 C  CB  . GLU A 1 500 ? -37.278 16.757  -97.950  1.00 55.95  ?  498 GLU A CB  1 
ATOM   3659 C  CG  . GLU A 1 500 ? -38.182 17.988  -98.001  1.00 60.15  ?  498 GLU A CG  1 
ATOM   3660 C  CD  . GLU A 1 500 ? -39.642 17.684  -97.699  1.00 76.13  ?  498 GLU A CD  1 
ATOM   3661 O  OE1 . GLU A 1 500 ? -40.239 16.834  -98.395  1.00 78.20  ?  498 GLU A OE1 1 
ATOM   3662 O  OE2 . GLU A 1 500 ? -40.197 18.315  -96.772  1.00 82.41  -1 498 GLU A OE2 1 
ATOM   3663 N  N   . PHE A 1 501 ? -35.369 14.802  -96.101  1.00 43.74  ?  499 PHE A N   1 
ATOM   3664 C  CA  . PHE A 1 501 ? -34.360 13.747  -96.088  1.00 46.09  ?  499 PHE A CA  1 
ATOM   3665 C  C   . PHE A 1 501 ? -34.778 12.619  -95.154  1.00 49.90  ?  499 PHE A C   1 
ATOM   3666 O  O   . PHE A 1 501 ? -34.610 11.439  -95.484  1.00 48.01  ?  499 PHE A O   1 
ATOM   3667 C  CB  . PHE A 1 501 ? -33.004 14.331  -95.671  1.00 39.93  ?  499 PHE A CB  1 
ATOM   3668 C  CG  . PHE A 1 501 ? -31.921 13.297  -95.439  1.00 40.40  ?  499 PHE A CG  1 
ATOM   3669 C  CD1 . PHE A 1 501 ? -31.133 12.845  -96.487  1.00 42.58  ?  499 PHE A CD1 1 
ATOM   3670 C  CD2 . PHE A 1 501 ? -31.675 12.802  -94.168  1.00 39.74  ?  499 PHE A CD2 1 
ATOM   3671 C  CE1 . PHE A 1 501 ? -30.133 11.908  -96.275  1.00 41.60  ?  499 PHE A CE1 1 
ATOM   3672 C  CE2 . PHE A 1 501 ? -30.678 11.862  -93.949  1.00 41.48  ?  499 PHE A CE2 1 
ATOM   3673 C  CZ  . PHE A 1 501 ? -29.907 11.415  -95.004  1.00 42.72  ?  499 PHE A CZ  1 
ATOM   3674 N  N   . LEU A 1 502 ? -35.310 12.968  -93.981  1.00 48.85  ?  500 LEU A N   1 
ATOM   3675 C  CA  . LEU A 1 502 ? -35.707 11.956  -93.009  1.00 56.71  ?  500 LEU A CA  1 
ATOM   3676 C  C   . LEU A 1 502 ? -36.816 11.066  -93.556  1.00 51.50  ?  500 LEU A C   1 
ATOM   3677 O  O   . LEU A 1 502 ? -36.837 9.856   -93.298  1.00 55.52  ?  500 LEU A O   1 
ATOM   3678 C  CB  . LEU A 1 502 ? -36.155 12.634  -91.716  1.00 49.13  ?  500 LEU A CB  1 
ATOM   3679 C  CG  . LEU A 1 502 ? -35.013 13.227  -90.893  1.00 55.53  ?  500 LEU A CG  1 
ATOM   3680 C  CD1 . LEU A 1 502 ? -35.545 13.909  -89.642  1.00 49.00  ?  500 LEU A CD1 1 
ATOM   3681 C  CD2 . LEU A 1 502 ? -34.006 12.144  -90.542  1.00 51.04  ?  500 LEU A CD2 1 
ATOM   3682 N  N   . THR A 1 503 ? -37.733 11.642  -94.340  1.00 52.92  ?  501 THR A N   1 
ATOM   3683 C  CA  . THR A 1 503 ? -38.831 10.864  -94.903  1.00 56.26  ?  501 THR A CA  1 
ATOM   3684 C  C   . THR A 1 503 ? -38.328 9.768   -95.826  1.00 57.45  ?  501 THR A C   1 
ATOM   3685 O  O   . THR A 1 503 ? -39.020 8.763   -96.021  1.00 65.46  ?  501 THR A O   1 
ATOM   3686 C  CB  . THR A 1 503 ? -39.803 11.772  -95.663  1.00 63.26  ?  501 THR A CB  1 
ATOM   3687 O  OG1 . THR A 1 503 ? -39.105 12.456  -96.712  1.00 74.24  ?  501 THR A OG1 1 
ATOM   3688 C  CG2 . THR A 1 503 ? -40.426 12.795  -94.725  1.00 63.00  ?  501 THR A CG2 1 
ATOM   3689 N  N   . ARG A 1 504 ? -37.139 9.941   -96.394  1.00 54.10  ?  502 ARG A N   1 
ATOM   3690 C  CA  . ARG A 1 504 ? -36.594 9.012   -97.365  1.00 56.99  ?  502 ARG A CA  1 
ATOM   3691 C  C   . ARG A 1 504 ? -35.410 8.229   -96.821  1.00 58.41  ?  502 ARG A C   1 
ATOM   3692 O  O   . ARG A 1 504 ? -34.931 7.312   -97.497  1.00 65.42  ?  502 ARG A O   1 
ATOM   3693 C  CB  . ARG A 1 504 ? -36.190 9.783   -98.631  1.00 57.75  ?  502 ARG A CB  1 
ATOM   3694 C  CG  . ARG A 1 504 ? -37.301 10.723  -99.094  1.00 57.30  ?  502 ARG A CG  1 
ATOM   3695 C  CD  . ARG A 1 504 ? -36.927 11.583  -100.291 1.00 57.86  ?  502 ARG A CD  1 
ATOM   3696 N  NE  . ARG A 1 504 ? -37.959 12.584  -100.541 1.00 79.18  ?  502 ARG A NE  1 
ATOM   3697 C  CZ  . ARG A 1 504 ? -37.932 13.474  -101.524 1.00 86.75  ?  502 ARG A CZ  1 
ATOM   3698 N  NH1 . ARG A 1 504 ? -37.043 13.400  -102.501 1.00 83.00  ?  502 ARG A NH1 1 
ATOM   3699 N  NH2 . ARG A 1 504 ? -38.860 14.427  -101.561 1.00 87.21  ?  502 ARG A NH2 1 
ATOM   3700 N  N   . ASN A 1 505 ? -34.935 8.558   -95.620  1.00 51.46  ?  503 ASN A N   1 
ATOM   3701 C  CA  . ASN A 1 505 ? -33.829 7.853   -94.973  1.00 55.04  ?  503 ASN A CA  1 
ATOM   3702 C  C   . ASN A 1 505 ? -34.263 7.473   -93.561  1.00 57.24  ?  503 ASN A C   1 
ATOM   3703 O  O   . ASN A 1 505 ? -33.873 8.122   -92.581  1.00 58.76  ?  503 ASN A O   1 
ATOM   3704 C  CB  . ASN A 1 505 ? -32.567 8.712   -94.968  1.00 48.82  ?  503 ASN A CB  1 
ATOM   3705 C  CG  . ASN A 1 505 ? -32.100 9.058   -96.369  1.00 50.33  ?  503 ASN A CG  1 
ATOM   3706 O  OD1 . ASN A 1 505 ? -32.784 9.773   -97.104  1.00 48.31  ?  503 ASN A OD1 1 
ATOM   3707 N  ND2 . ASN A 1 505 ? -30.945 8.533   -96.755  1.00 47.93  ?  503 ASN A ND2 1 
ATOM   3708 N  N   . PRO A 1 506 ? -35.053 6.404   -93.420  1.00 61.87  ?  504 PRO A N   1 
ATOM   3709 C  CA  . PRO A 1 506 ? -35.606 6.070   -92.095  1.00 60.16  ?  504 PRO A CA  1 
ATOM   3710 C  C   . PRO A 1 506 ? -34.547 5.796   -91.044  1.00 64.36  ?  504 PRO A C   1 
ATOM   3711 O  O   . PRO A 1 506 ? -34.763 6.113   -89.867  1.00 66.64  ?  504 PRO A O   1 
ATOM   3712 C  CB  . PRO A 1 506 ? -36.464 4.828   -92.378  1.00 63.59  ?  504 PRO A CB  1 
ATOM   3713 C  CG  . PRO A 1 506 ? -35.884 4.249   -93.631  1.00 66.04  ?  504 PRO A CG  1 
ATOM   3714 C  CD  . PRO A 1 506 ? -35.468 5.437   -94.448  1.00 65.74  ?  504 PRO A CD  1 
ATOM   3715 N  N   . ALA A 1 507 ? -33.408 5.212   -91.426  1.00 64.26  ?  505 ALA A N   1 
ATOM   3716 C  CA  . ALA A 1 507 ? -32.389 4.855   -90.447  1.00 56.39  ?  505 ALA A CA  1 
ATOM   3717 C  C   . ALA A 1 507 ? -31.833 6.073   -89.726  1.00 61.49  ?  505 ALA A C   1 
ATOM   3718 O  O   . ALA A 1 507 ? -31.031 5.917   -88.798  1.00 58.43  ?  505 ALA A O   1 
ATOM   3719 C  CB  . ALA A 1 507 ? -31.252 4.086   -91.122  1.00 62.89  ?  505 ALA A CB  1 
ATOM   3720 N  N   . TRP A 1 508 ? -32.241 7.274   -90.129  1.00 62.83  ?  506 TRP A N   1 
ATOM   3721 C  CA  . TRP A 1 508 ? -31.729 8.519   -89.583  1.00 52.87  ?  506 TRP A CA  1 
ATOM   3722 C  C   . TRP A 1 508 ? -32.686 9.132   -88.574  1.00 47.77  ?  506 TRP A C   1 
ATOM   3723 O  O   . TRP A 1 508 ? -32.391 10.195  -88.020  1.00 57.47  ?  506 TRP A O   1 
ATOM   3724 C  CB  . TRP A 1 508 ? -31.468 9.511   -90.720  1.00 49.40  ?  506 TRP A CB  1 
ATOM   3725 C  CG  . TRP A 1 508 ? -30.323 9.129   -91.612  1.00 54.32  ?  506 TRP A CG  1 
ATOM   3726 C  CD1 . TRP A 1 508 ? -30.309 8.135   -92.549  1.00 52.32  ?  506 TRP A CD1 1 
ATOM   3727 C  CD2 . TRP A 1 508 ? -29.047 9.777   -91.698  1.00 42.57  ?  506 TRP A CD2 1 
ATOM   3728 N  NE1 . TRP A 1 508 ? -29.091 8.101   -93.186  1.00 44.33  ?  506 TRP A NE1 1 
ATOM   3729 C  CE2 . TRP A 1 508 ? -28.300 9.100   -92.684  1.00 42.96  ?  506 TRP A CE2 1 
ATOM   3730 C  CE3 . TRP A 1 508 ? -28.458 10.852  -91.026  1.00 42.46  ?  506 TRP A CE3 1 
ATOM   3731 C  CZ2 . TRP A 1 508 ? -26.997 9.466   -93.016  1.00 42.29  ?  506 TRP A CZ2 1 
ATOM   3732 C  CZ3 . TRP A 1 508 ? -27.165 11.212  -91.358  1.00 40.44  ?  506 TRP A CZ3 1 
ATOM   3733 C  CH2 . TRP A 1 508 ? -26.449 10.521  -92.343  1.00 35.74  ?  506 TRP A CH2 1 
ATOM   3734 N  N   . ARG A 1 509 ? -33.820 8.477   -88.311  1.00 59.15  ?  507 ARG A N   1 
ATOM   3735 C  CA  . ARG A 1 509 ? -34.787 9.021   -87.369  1.00 67.31  ?  507 ARG A CA  1 
ATOM   3736 C  C   . ARG A 1 509 ? -34.185 9.114   -85.976  1.00 57.34  ?  507 ARG A C   1 
ATOM   3737 O  O   . ARG A 1 509 ? -34.701 9.847   -85.126  1.00 67.38  ?  507 ARG A O   1 
ATOM   3738 C  CB  . ARG A 1 509 ? -36.060 8.169   -87.374  1.00 59.13  ?  507 ARG A CB  1 
ATOM   3739 C  CG  . ARG A 1 509 ? -37.322 8.989   -87.604  1.00 70.05  ?  507 ARG A CG  1 
ATOM   3740 C  CD  . ARG A 1 509 ? -38.599 8.215   -87.312  1.00 72.54  ?  507 ARG A CD  1 
ATOM   3741 N  NE  . ARG A 1 509 ? -39.770 9.076   -87.442  1.00 75.59  ?  507 ARG A NE  1 
ATOM   3742 C  CZ  . ARG A 1 509 ? -41.022 8.683   -87.251  1.00 79.60  ?  507 ARG A CZ  1 
ATOM   3743 N  NH1 . ARG A 1 509 ? -41.315 7.430   -86.942  1.00 83.17  ?  507 ARG A NH1 1 
ATOM   3744 N  NH2 . ARG A 1 509 ? -42.007 9.568   -87.383  1.00 87.58  ?  507 ARG A NH2 1 
ATOM   3745 N  N   . LYS A 1 510 ? -33.091 8.392   -85.746  1.00 53.67  ?  508 LYS A N   1 
ATOM   3746 C  CA  . LYS A 1 510 ? -32.345 8.353   -84.498  1.00 54.10  ?  508 LYS A CA  1 
ATOM   3747 C  C   . LYS A 1 510 ? -31.192 9.347   -84.476  1.00 60.52  ?  508 LYS A C   1 
ATOM   3748 O  O   . LYS A 1 510 ? -30.418 9.360   -83.513  1.00 62.10  ?  508 LYS A O   1 
ATOM   3749 C  CB  . LYS A 1 510 ? -31.790 6.942   -84.292  1.00 67.98  ?  508 LYS A CB  1 
ATOM   3750 C  CG  . LYS A 1 510 ? -30.971 6.488   -85.500  1.00 62.38  ?  508 LYS A CG  1 
ATOM   3751 C  CD  . LYS A 1 510 ? -30.253 5.164   -85.298  1.00 73.73  ?  508 LYS A CD  1 
ATOM   3752 C  CE  . LYS A 1 510 ? -29.221 5.238   -84.189  1.00 72.80  ?  508 LYS A CE  1 
ATOM   3753 N  NZ  . LYS A 1 510 ? -28.360 4.021   -84.181  1.00 72.66  ?  508 LYS A NZ  1 
ATOM   3754 N  N   . ALA A 1 511 ? -31.059 10.171  -85.511  1.00 46.37  ?  509 ALA A N   1 
ATOM   3755 C  CA  . ALA A 1 511 ? -29.940 11.094  -85.613  1.00 54.71  ?  509 ALA A CA  1 
ATOM   3756 C  C   . ALA A 1 511 ? -30.052 12.208  -84.580  1.00 58.10  ?  509 ALA A C   1 
ATOM   3757 O  O   . ALA A 1 511 ? -31.144 12.562  -84.125  1.00 45.11  ?  509 ALA A O   1 
ATOM   3758 C  CB  . ALA A 1 511 ? -29.869 11.695  -87.016  1.00 39.72  ?  509 ALA A CB  1 
ATOM   3759 N  N   . VAL A 1 512 ? -28.901 12.741  -84.188  1.00 42.56  ?  510 VAL A N   1 
ATOM   3760 C  CA  . VAL A 1 512 ? -28.847 13.914  -83.328  1.00 40.62  ?  510 VAL A CA  1 
ATOM   3761 C  C   . VAL A 1 512 ? -28.713 15.138  -84.220  1.00 44.00  ?  510 VAL A C   1 
ATOM   3762 O  O   . VAL A 1 512 ? -27.844 15.180  -85.101  1.00 34.80  ?  510 VAL A O   1 
ATOM   3763 C  CB  . VAL A 1 512 ? -27.676 13.821  -82.334  1.00 48.26  ?  510 VAL A CB  1 
ATOM   3764 C  CG1 . VAL A 1 512 ? -27.545 15.115  -81.539  1.00 46.97  ?  510 VAL A CG1 1 
ATOM   3765 C  CG2 . VAL A 1 512 ? -27.858 12.636  -81.405  1.00 44.41  ?  510 VAL A CG2 1 
ATOM   3766 N  N   . PHE A 1 513 ? -29.587 16.122  -84.017  1.00 38.34  ?  511 PHE A N   1 
ATOM   3767 C  CA  . PHE A 1 513 ? -29.485 17.380  -84.744  1.00 46.59  ?  511 PHE A CA  1 
ATOM   3768 C  C   . PHE A 1 513 ? -28.457 18.273  -84.059  1.00 42.23  ?  511 PHE A C   1 
ATOM   3769 O  O   . PHE A 1 513 ? -28.533 18.499  -82.846  1.00 37.03  ?  511 PHE A O   1 
ATOM   3770 C  CB  . PHE A 1 513 ? -30.844 18.080  -84.810  1.00 37.57  ?  511 PHE A CB  1 
ATOM   3771 C  CG  . PHE A 1 513 ? -30.833 19.340  -85.633  1.00 39.96  ?  511 PHE A CG  1 
ATOM   3772 C  CD1 . PHE A 1 513 ? -30.484 20.556  -85.068  1.00 35.21  ?  511 PHE A CD1 1 
ATOM   3773 C  CD2 . PHE A 1 513 ? -31.169 19.302  -86.977  1.00 34.33  ?  511 PHE A CD2 1 
ATOM   3774 C  CE1 . PHE A 1 513 ? -30.473 21.710  -85.825  1.00 44.01  ?  511 PHE A CE1 1 
ATOM   3775 C  CE2 . PHE A 1 513 ? -31.158 20.455  -87.740  1.00 40.01  ?  511 PHE A CE2 1 
ATOM   3776 C  CZ  . PHE A 1 513 ? -30.808 21.660  -87.163  1.00 43.58  ?  511 PHE A CZ  1 
ATOM   3777 N  N   . ILE A 1 514 ? -27.494 18.778  -84.827  1.00 32.10  ?  512 ILE A N   1 
ATOM   3778 C  CA  . ILE A 1 514 ? -26.453 19.648  -84.293  1.00 31.28  ?  512 ILE A CA  1 
ATOM   3779 C  C   . ILE A 1 514 ? -26.329 20.888  -85.168  1.00 45.22  ?  512 ILE A C   1 
ATOM   3780 O  O   . ILE A 1 514 ? -26.336 20.788  -86.400  1.00 31.16  ?  512 ILE A O   1 
ATOM   3781 C  CB  . ILE A 1 514 ? -25.100 18.919  -84.198  1.00 30.27  ?  512 ILE A CB  1 
ATOM   3782 C  CG1 . ILE A 1 514 ? -25.249 17.618  -83.406  1.00 54.95  ?  512 ILE A CG1 1 
ATOM   3783 C  CG2 . ILE A 1 514 ? -24.060 19.822  -83.552  1.00 30.01  ?  512 ILE A CG2 1 
ATOM   3784 C  CD1 . ILE A 1 514 ? -23.932 16.956  -83.057  1.00 49.85  ?  512 ILE A CD1 1 
ATOM   3785 N  N   . SER A 1 515 ? -26.243 22.052  -84.531  1.00 45.36  ?  513 SER A N   1 
ATOM   3786 C  CA  . SER A 1 515 ? -26.119 23.328  -85.219  1.00 45.47  ?  513 SER A CA  1 
ATOM   3787 C  C   . SER A 1 515 ? -25.274 24.260  -84.368  1.00 42.21  ?  513 SER A C   1 
ATOM   3788 O  O   . SER A 1 515 ? -25.108 24.029  -83.165  1.00 43.71  ?  513 SER A O   1 
ATOM   3789 C  CB  . SER A 1 515 ? -27.490 23.964  -85.480  1.00 47.76  ?  513 SER A CB  1 
ATOM   3790 O  OG  . SER A 1 515 ? -27.841 24.842  -84.422  1.00 40.28  ?  513 SER A OG  1 
ATOM   3791 N  N   . PRO A 1 516 ? -24.745 25.337  -84.953  1.00 28.93  ?  514 PRO A N   1 
ATOM   3792 C  CA  . PRO A 1 516 ? -23.988 26.311  -84.161  1.00 30.01  ?  514 PRO A CA  1 
ATOM   3793 C  C   . PRO A 1 516 ? -24.874 27.276  -83.388  1.00 40.89  ?  514 PRO A C   1 
ATOM   3794 O  O   . PRO A 1 516 ? -24.341 28.143  -82.686  1.00 41.27  ?  514 PRO A O   1 
ATOM   3795 C  CB  . PRO A 1 516 ? -23.159 27.058  -85.231  1.00 29.23  ?  514 PRO A CB  1 
ATOM   3796 C  CG  . PRO A 1 516 ? -23.382 26.278  -86.528  1.00 26.87  ?  514 PRO A CG  1 
ATOM   3797 C  CD  . PRO A 1 516 ? -24.747 25.710  -86.376  1.00 35.73  ?  514 PRO A CD  1 
ATOM   3798 N  N   . TYR A 1 517 ? -26.201 27.172  -83.510  1.00 37.55  ?  515 TYR A N   1 
ATOM   3799 C  CA  . TYR A 1 517 ? -27.112 28.138  -82.905  1.00 42.90  ?  515 TYR A CA  1 
ATOM   3800 C  C   . TYR A 1 517 ? -28.211 27.478  -82.070  1.00 45.08  ?  515 TYR A C   1 
ATOM   3801 O  O   . TYR A 1 517 ? -28.909 26.576  -82.547  1.00 43.11  ?  515 TYR A O   1 
ATOM   3802 C  CB  . TYR A 1 517 ? -27.706 29.026  -84.003  1.00 34.89  ?  515 TYR A CB  1 
ATOM   3803 C  CG  . TYR A 1 517 ? -26.654 29.901  -84.672  1.00 42.66  ?  515 TYR A CG  1 
ATOM   3804 C  CD1 . TYR A 1 517 ? -26.281 31.117  -84.111  1.00 42.79  ?  515 TYR A CD1 1 
ATOM   3805 C  CD2 . TYR A 1 517 ? -26.027 29.508  -85.851  1.00 36.98  ?  515 TYR A CD2 1 
ATOM   3806 C  CE1 . TYR A 1 517 ? -25.320 31.921  -84.701  1.00 47.58  ?  515 TYR A CE1 1 
ATOM   3807 C  CE2 . TYR A 1 517 ? -25.059 30.313  -86.455  1.00 41.72  ?  515 TYR A CE2 1 
ATOM   3808 C  CZ  . TYR A 1 517 ? -24.713 31.516  -85.873  1.00 45.02  ?  515 TYR A CZ  1 
ATOM   3809 O  OH  . TYR A 1 517 ? -23.761 32.319  -86.458  1.00 49.89  ?  515 TYR A OH  1 
ATOM   3810 N  N   . ASN A 1 518 ? -28.375 27.957  -80.830  1.00 46.84  ?  516 ASN A N   1 
ATOM   3811 C  CA  . ASN A 1 518 ? -29.417 27.445  -79.936  1.00 47.38  ?  516 ASN A CA  1 
ATOM   3812 C  C   . ASN A 1 518 ? -30.809 27.604  -80.541  1.00 47.10  ?  516 ASN A C   1 
ATOM   3813 O  O   . ASN A 1 518 ? -31.634 26.685  -80.470  1.00 59.04  ?  516 ASN A O   1 
ATOM   3814 C  CB  . ASN A 1 518 ? -29.349 28.141  -78.573  1.00 60.46  ?  516 ASN A CB  1 
ATOM   3815 C  CG  . ASN A 1 518 ? -28.445 27.417  -77.586  1.00 69.68  ?  516 ASN A CG  1 
ATOM   3816 O  OD1 . ASN A 1 518 ? -28.706 26.271  -77.219  1.00 69.81  ?  516 ASN A OD1 1 
ATOM   3817 N  ND2 . ASN A 1 518 ? -27.386 28.087  -77.145  1.00 75.21  ?  516 ASN A ND2 1 
ATOM   3818 N  N   . SER A 1 519 ? -31.092 28.767  -81.131  1.00 44.45  ?  517 SER A N   1 
ATOM   3819 C  CA  . SER A 1 519 ? -32.416 29.023  -81.692  1.00 45.67  ?  517 SER A CA  1 
ATOM   3820 C  C   . SER A 1 519 ? -32.734 28.039  -82.812  1.00 49.94  ?  517 SER A C   1 
ATOM   3821 O  O   . SER A 1 519 ? -33.851 27.510  -82.881  1.00 49.91  ?  517 SER A O   1 
ATOM   3822 C  CB  . SER A 1 519 ? -32.509 30.465  -82.184  1.00 49.32  ?  517 SER A CB  1 
ATOM   3823 O  OG  . SER A 1 519 ? -31.488 30.731  -83.128  1.00 62.01  ?  517 SER A OG  1 
ATOM   3824 N  N   . GLN A 1 520 ? -31.778 27.796  -83.715  1.00 39.71  ?  518 GLN A N   1 
ATOM   3825 C  CA  . GLN A 1 520 ? -32.020 26.810  -84.762  1.00 44.01  ?  518 GLN A CA  1 
ATOM   3826 C  C   . GLN A 1 520 ? -32.352 25.473  -84.120  1.00 45.67  ?  518 GLN A C   1 
ATOM   3827 O  O   . GLN A 1 520 ? -33.259 24.765  -84.571  1.00 45.27  ?  518 GLN A O   1 
ATOM   3828 C  CB  . GLN A 1 520 ? -30.813 26.683  -85.695  1.00 47.06  ?  518 GLN A CB  1 
ATOM   3829 C  CG  . GLN A 1 520 ? -30.962 25.604  -86.780  1.00 47.08  ?  518 GLN A CG  1 
ATOM   3830 C  CD  . GLN A 1 520 ? -31.638 26.113  -88.043  1.00 32.94  ?  518 GLN A CD  1 
ATOM   3831 O  OE1 . GLN A 1 520 ? -32.628 26.843  -87.980  1.00 41.22  ?  518 GLN A OE1 1 
ATOM   3832 N  NE2 . GLN A 1 520 ? -31.110 25.722  -89.196  1.00 37.89  ?  518 GLN A NE2 1 
ATOM   3833 N  N   . ASN A 1 521 ? -31.609 25.097  -83.076  1.00 44.97  ?  519 ASN A N   1 
ATOM   3834 C  CA  . ASN A 1 521 ? -31.849 23.802  -82.457  1.00 49.36  ?  519 ASN A CA  1 
ATOM   3835 C  C   . ASN A 1 521 ? -33.266 23.751  -81.897  1.00 45.26  ?  519 ASN A C   1 
ATOM   3836 O  O   . ASN A 1 521 ? -33.943 22.722  -81.992  1.00 46.59  ?  519 ASN A O   1 
ATOM   3837 C  CB  . ASN A 1 521 ? -30.821 23.541  -81.354  1.00 49.99  ?  519 ASN A CB  1 
ATOM   3838 C  CG  . ASN A 1 521 ? -29.424 23.298  -81.901  1.00 50.63  ?  519 ASN A CG  1 
ATOM   3839 O  OD1 . ASN A 1 521 ? -29.253 22.981  -83.077  1.00 51.88  ?  519 ASN A OD1 1 
ATOM   3840 N  ND2 . ASN A 1 521 ? -28.418 23.438  -81.045  1.00 53.18  ?  519 ASN A ND2 1 
ATOM   3841 N  N   . ALA A 1 522 ? -33.746 24.870  -81.343  1.00 47.41  ?  520 ALA A N   1 
ATOM   3842 C  CA  . ALA A 1 522 ? -35.098 24.897  -80.794  1.00 51.55  ?  520 ALA A CA  1 
ATOM   3843 C  C   . ALA A 1 522 ? -36.128 24.683  -81.895  1.00 51.17  ?  520 ALA A C   1 
ATOM   3844 O  O   . ALA A 1 522 ? -37.098 23.936  -81.716  1.00 53.98  ?  520 ALA A O   1 
ATOM   3845 C  CB  . ALA A 1 522 ? -35.352 26.217  -80.068  1.00 54.03  ?  520 ALA A CB  1 
ATOM   3846 N  N   . VAL A 1 523 ? -35.941 25.345  -83.040  1.00 48.18  ?  521 VAL A N   1 
ATOM   3847 C  CA  . VAL A 1 523 ? -36.868 25.172  -84.150  1.00 48.00  ?  521 VAL A CA  1 
ATOM   3848 C  C   . VAL A 1 523 ? -36.787 23.753  -84.697  1.00 53.87  ?  521 VAL A C   1 
ATOM   3849 O  O   . VAL A 1 523 ? -37.798 23.190  -85.137  1.00 58.07  ?  521 VAL A O   1 
ATOM   3850 C  CB  . VAL A 1 523 ? -36.580 26.219  -85.242  1.00 47.51  ?  521 VAL A CB  1 
ATOM   3851 C  CG1 . VAL A 1 523 ? -37.362 25.903  -86.505  1.00 45.10  ?  521 VAL A CG1 1 
ATOM   3852 C  CG2 . VAL A 1 523 ? -36.915 27.612  -84.734  1.00 50.16  ?  521 VAL A CG2 1 
ATOM   3853 N  N   . ALA A 1 524 ? -35.600 23.142  -84.659  1.00 47.01  ?  522 ALA A N   1 
ATOM   3854 C  CA  . ALA A 1 524 ? -35.443 21.795  -85.200  1.00 51.90  ?  522 ALA A CA  1 
ATOM   3855 C  C   . ALA A 1 524 ? -36.091 20.762  -84.290  1.00 50.43  ?  522 ALA A C   1 
ATOM   3856 O  O   . ALA A 1 524 ? -36.676 19.783  -84.767  1.00 65.24  ?  522 ALA A O   1 
ATOM   3857 C  CB  . ALA A 1 524 ? -33.962 21.478  -85.406  1.00 43.63  ?  522 ALA A CB  1 
ATOM   3858 N  N   . SER A 1 525 ? -35.984 20.958  -82.976  1.00 49.62  ?  523 SER A N   1 
ATOM   3859 C  CA  . SER A 1 525 ? -36.656 20.073  -82.032  1.00 53.90  ?  523 SER A CA  1 
ATOM   3860 C  C   . SER A 1 525 ? -38.146 19.986  -82.336  1.00 57.09  ?  523 SER A C   1 
ATOM   3861 O  O   . SER A 1 525 ? -38.723 18.894  -82.390  1.00 59.44  ?  523 SER A O   1 
ATOM   3862 C  CB  . SER A 1 525 ? -36.423 20.570  -80.603  1.00 56.56  ?  523 SER A CB  1 
ATOM   3863 O  OG  . SER A 1 525 ? -37.101 19.764  -79.656  1.00 63.11  ?  523 SER A OG  1 
ATOM   3864 N  N   . LYS A 1 526 ? -38.780 21.138  -82.561  1.00 61.48  ?  524 LYS A N   1 
ATOM   3865 C  CA  . LYS A 1 526 ? -40.222 21.173  -82.778  1.00 60.96  ?  524 LYS A CA  1 
ATOM   3866 C  C   . LYS A 1 526 ? -40.615 20.573  -84.125  1.00 59.54  ?  524 LYS A C   1 
ATOM   3867 O  O   . LYS A 1 526 ? -41.583 19.809  -84.206  1.00 62.86  ?  524 LYS A O   1 
ATOM   3868 C  CB  . LYS A 1 526 ? -40.720 22.612  -82.649  1.00 61.84  ?  524 LYS A CB  1 
ATOM   3869 C  CG  . LYS A 1 526 ? -40.292 23.267  -81.340  1.00 63.56  ?  524 LYS A CG  1 
ATOM   3870 C  CD  . LYS A 1 526 ? -40.485 24.775  -81.345  1.00 79.05  ?  524 LYS A CD  1 
ATOM   3871 C  CE  . LYS A 1 526 ? -39.813 25.405  -80.130  1.00 80.00  ?  524 LYS A CE  1 
ATOM   3872 N  NZ  . LYS A 1 526 ? -39.873 26.894  -80.141  1.00 86.77  ?  524 LYS A NZ  1 
ATOM   3873 N  N   . ILE A 1 527 ? -39.879 20.888  -85.194  1.00 55.13  ?  525 ILE A N   1 
ATOM   3874 C  CA  . ILE A 1 527 ? -40.305 20.436  -86.517  1.00 54.35  ?  525 ILE A CA  1 
ATOM   3875 C  C   . ILE A 1 527 ? -39.919 18.983  -86.757  1.00 61.38  ?  525 ILE A C   1 
ATOM   3876 O  O   . ILE A 1 527 ? -40.716 18.198  -87.284  1.00 56.32  ?  525 ILE A O   1 
ATOM   3877 C  CB  . ILE A 1 527 ? -39.717 21.349  -87.609  1.00 58.99  ?  525 ILE A CB  1 
ATOM   3878 C  CG1 . ILE A 1 527 ? -40.165 22.800  -87.412  1.00 62.90  ?  525 ILE A CG1 1 
ATOM   3879 C  CG2 . ILE A 1 527 ? -40.070 20.819  -88.995  1.00 56.24  ?  525 ILE A CG2 1 
ATOM   3880 C  CD1 . ILE A 1 527 ? -39.554 23.764  -88.413  1.00 57.58  ?  525 ILE A CD1 1 
ATOM   3881 N  N   . LEU A 1 528 ? -38.718 18.586  -86.341  1.00 51.88  ?  526 LEU A N   1 
ATOM   3882 C  CA  . LEU A 1 528 ? -38.194 17.261  -86.651  1.00 55.63  ?  526 LEU A CA  1 
ATOM   3883 C  C   . LEU A 1 528 ? -38.379 16.269  -85.515  1.00 56.87  ?  526 LEU A C   1 
ATOM   3884 O  O   . LEU A 1 528 ? -38.625 15.086  -85.765  1.00 56.56  ?  526 LEU A O   1 
ATOM   3885 C  CB  . LEU A 1 528 ? -36.705 17.344  -87.010  1.00 48.60  ?  526 LEU A CB  1 
ATOM   3886 C  CG  . LEU A 1 528 ? -36.295 18.357  -88.080  1.00 47.67  ?  526 LEU A CG  1 
ATOM   3887 C  CD1 . LEU A 1 528 ? -34.771 18.466  -88.190  1.00 44.50  ?  526 LEU A CD1 1 
ATOM   3888 C  CD2 . LEU A 1 528 ? -36.903 17.976  -89.419  1.00 44.09  ?  526 LEU A CD2 1 
ATOM   3889 N  N   . GLY A 1 529 ? -38.252 16.719  -84.272  1.00 63.29  ?  527 GLY A N   1 
ATOM   3890 C  CA  . GLY A 1 529 ? -38.435 15.854  -83.133  1.00 60.22  ?  527 GLY A CA  1 
ATOM   3891 C  C   . GLY A 1 529 ? -37.170 15.166  -82.684  1.00 58.62  ?  527 GLY A C   1 
ATOM   3892 O  O   . GLY A 1 529 ? -37.218 14.359  -81.748  1.00 63.17  ?  527 GLY A O   1 
ATOM   3893 N  N   . LEU A 1 530 ? -36.047 15.456  -83.319  1.00 60.03  ?  528 LEU A N   1 
ATOM   3894 C  CA  . LEU A 1 530 ? -34.808 14.779  -82.999  1.00 56.70  ?  528 LEU A CA  1 
ATOM   3895 C  C   . LEU A 1 530 ? -34.163 15.419  -81.777  1.00 55.68  ?  528 LEU A C   1 
ATOM   3896 O  O   . LEU A 1 530 ? -34.380 16.601  -81.497  1.00 52.66  ?  528 LEU A O   1 
ATOM   3897 C  CB  . LEU A 1 530 ? -33.840 14.859  -84.172  1.00 47.71  ?  528 LEU A CB  1 
ATOM   3898 C  CG  . LEU A 1 530 ? -34.372 14.437  -85.536  1.00 55.92  ?  528 LEU A CG  1 
ATOM   3899 C  CD1 . LEU A 1 530 ? -33.402 14.866  -86.626  1.00 42.81  ?  528 LEU A CD1 1 
ATOM   3900 C  CD2 . LEU A 1 530 ? -34.595 12.935  -85.560  1.00 49.62  ?  528 LEU A CD2 1 
ATOM   3901 N  N   . PRO A 1 531 ? -33.362 14.662  -81.034  1.00 53.63  ?  529 PRO A N   1 
ATOM   3902 C  CA  . PRO A 1 531 ? -32.566 15.285  -79.979  1.00 55.70  ?  529 PRO A CA  1 
ATOM   3903 C  C   . PRO A 1 531 ? -31.640 16.309  -80.615  1.00 49.10  ?  529 PRO A C   1 
ATOM   3904 O  O   . PRO A 1 531 ? -31.182 16.141  -81.748  1.00 45.69  ?  529 PRO A O   1 
ATOM   3905 C  CB  . PRO A 1 531 ? -31.792 14.108  -79.373  1.00 55.11  ?  529 PRO A CB  1 
ATOM   3906 C  CG  . PRO A 1 531 ? -31.777 13.076  -80.472  1.00 53.56  ?  529 PRO A CG  1 
ATOM   3907 C  CD  . PRO A 1 531 ? -33.118 13.213  -81.122  1.00 54.77  ?  529 PRO A CD  1 
ATOM   3908 N  N   . THR A 1 532 ? -31.368 17.382  -79.880  1.00 49.43  ?  530 THR A N   1 
ATOM   3909 C  CA  . THR A 1 532 ? -30.608 18.495  -80.427  1.00 45.75  ?  530 THR A CA  1 
ATOM   3910 C  C   . THR A 1 532 ? -29.430 18.810  -79.523  1.00 45.74  ?  530 THR A C   1 
ATOM   3911 O  O   . THR A 1 532 ? -29.439 18.532  -78.320  1.00 49.18  ?  530 THR A O   1 
ATOM   3912 C  CB  . THR A 1 532 ? -31.466 19.759  -80.604  1.00 46.15  ?  530 THR A CB  1 
ATOM   3913 O  OG1 . THR A 1 532 ? -31.861 20.255  -79.318  1.00 63.82  ?  530 THR A OG1 1 
ATOM   3914 C  CG2 . THR A 1 532 ? -32.698 19.463  -81.448  1.00 46.73  ?  530 THR A CG2 1 
ATOM   3915 N  N   . GLN A 1 533 ? -28.414 19.411  -80.133  1.00 42.23  ?  531 GLN A N   1 
ATOM   3916 C  CA  . GLN A 1 533 ? -27.203 19.785  -79.428  1.00 42.03  ?  531 GLN A CA  1 
ATOM   3917 C  C   . GLN A 1 533 ? -26.489 20.887  -80.191  1.00 49.14  ?  531 GLN A C   1 
ATOM   3918 O  O   . GLN A 1 533 ? -26.397 20.831  -81.420  1.00 36.07  ?  531 GLN A O   1 
ATOM   3919 C  CB  . GLN A 1 533 ? -26.277 18.573  -79.310  1.00 41.61  ?  531 GLN A CB  1 
ATOM   3920 C  CG  . GLN A 1 533 ? -25.101 18.780  -78.403  1.00 45.28  ?  531 GLN A CG  1 
ATOM   3921 C  CD  . GLN A 1 533 ? -25.217 17.941  -77.158  1.00 46.38  ?  531 GLN A CD  1 
ATOM   3922 O  OE1 . GLN A 1 533 ? -25.281 16.713  -77.230  1.00 52.47  ?  531 GLN A OE1 1 
ATOM   3923 N  NE2 . GLN A 1 533 ? -25.266 18.596  -76.008  1.00 49.57  ?  531 GLN A NE2 1 
ATOM   3924 N  N   . THR A 1 534 ? -25.953 21.863  -79.461  1.00 39.84  ?  532 THR A N   1 
ATOM   3925 C  CA  . THR A 1 534 ? -25.064 22.818  -80.099  1.00 48.57  ?  532 THR A CA  1 
ATOM   3926 C  C   . THR A 1 534 ? -23.716 22.145  -80.281  1.00 49.07  ?  532 THR A C   1 
ATOM   3927 O  O   . THR A 1 534 ? -23.355 21.229  -79.535  1.00 41.19  ?  532 THR A O   1 
ATOM   3928 C  CB  . THR A 1 534 ? -24.889 24.097  -79.275  1.00 50.73  ?  532 THR A CB  1 
ATOM   3929 O  OG1 . THR A 1 534 ? -24.475 23.763  -77.944  1.00 57.64  ?  532 THR A OG1 1 
ATOM   3930 C  CG2 . THR A 1 534 ? -26.177 24.910  -79.233  1.00 51.51  ?  532 THR A CG2 1 
ATOM   3931 N  N   . VAL A 1 535 ? -22.965 22.608  -81.279  1.00 42.40  ?  533 VAL A N   1 
ATOM   3932 C  CA  . VAL A 1 535 ? -21.634 22.054  -81.505  1.00 45.32  ?  533 VAL A CA  1 
ATOM   3933 C  C   . VAL A 1 535 ? -20.807 22.149  -80.232  1.00 45.48  ?  533 VAL A C   1 
ATOM   3934 O  O   . VAL A 1 535 ? -20.250 21.155  -79.748  1.00 34.55  ?  533 VAL A O   1 
ATOM   3935 C  CB  . VAL A 1 535 ? -20.945 22.781  -82.673  1.00 45.87  ?  533 VAL A CB  1 
ATOM   3936 C  CG1 . VAL A 1 535 ? -19.558 22.203  -82.916  1.00 50.80  ?  533 VAL A CG1 1 
ATOM   3937 C  CG2 . VAL A 1 535 ? -21.802 22.711  -83.927  1.00 44.53  ?  533 VAL A CG2 1 
ATOM   3938 N  N   . ASP A 1 536 ? -20.745 23.348  -79.651  1.00 35.87  ?  534 ASP A N   1 
ATOM   3939 C  CA  . ASP A 1 536 ? -19.924 23.556  -78.466  1.00 40.81  ?  534 ASP A CA  1 
ATOM   3940 C  C   . ASP A 1 536 ? -20.320 22.622  -77.327  1.00 43.06  ?  534 ASP A C   1 
ATOM   3941 O  O   . ASP A 1 536 ? -19.450 22.158  -76.582  1.00 45.17  ?  534 ASP A O   1 
ATOM   3942 C  CB  . ASP A 1 536 ? -20.007 25.021  -78.034  1.00 52.90  ?  534 ASP A CB  1 
ATOM   3943 C  CG  . ASP A 1 536 ? -19.696 25.986  -79.175  1.00 64.55  ?  534 ASP A CG  1 
ATOM   3944 O  OD1 . ASP A 1 536 ? -20.396 25.948  -80.213  1.00 51.36  ?  534 ASP A OD1 1 
ATOM   3945 O  OD2 . ASP A 1 536 ? -18.751 26.791  -79.031  1.00 69.46  -1 534 ASP A OD2 1 
ATOM   3946 N  N   . SER A 1 537 ? -21.608 22.291  -77.205  1.00 41.66  ?  535 SER A N   1 
ATOM   3947 C  CA  . SER A 1 537 ? -22.030 21.361  -76.162  1.00 46.53  ?  535 SER A CA  1 
ATOM   3948 C  C   . SER A 1 537 ? -21.878 19.906  -76.584  1.00 47.44  ?  535 SER A C   1 
ATOM   3949 O  O   . SER A 1 537 ? -21.931 19.016  -75.728  1.00 46.55  ?  535 SER A O   1 
ATOM   3950 C  CB  . SER A 1 537 ? -23.480 21.633  -75.752  1.00 47.47  ?  535 SER A CB  1 
ATOM   3951 O  OG  . SER A 1 537 ? -24.380 21.358  -76.811  1.00 51.56  ?  535 SER A OG  1 
ATOM   3952 N  N   . SER A 1 538 ? -21.666 19.644  -77.873  1.00 40.07  ?  536 SER A N   1 
ATOM   3953 C  CA  . SER A 1 538 ? -21.504 18.278  -78.343  1.00 39.15  ?  536 SER A CA  1 
ATOM   3954 C  C   . SER A 1 538 ? -20.091 17.778  -78.107  1.00 38.95  ?  536 SER A C   1 
ATOM   3955 O  O   . SER A 1 538 ? -19.830 16.584  -78.284  1.00 38.90  ?  536 SER A O   1 
ATOM   3956 C  CB  . SER A 1 538 ? -21.841 18.180  -79.834  1.00 35.89  ?  536 SER A CB  1 
ATOM   3957 O  OG  . SER A 1 538 ? -20.827 18.792  -80.603  1.00 33.34  ?  536 SER A OG  1 
ATOM   3958 N  N   . GLN A 1 539 ? -19.180 18.671  -77.723  1.00 39.13  ?  537 GLN A N   1 
ATOM   3959 C  CA  . GLN A 1 539 ? -17.770 18.325  -77.626  1.00 44.98  ?  537 GLN A CA  1 
ATOM   3960 C  C   . GLN A 1 539 ? -17.570 17.241  -76.581  1.00 45.77  ?  537 GLN A C   1 
ATOM   3961 O  O   . GLN A 1 539 ? -18.056 17.350  -75.453  1.00 45.29  ?  537 GLN A O   1 
ATOM   3962 C  CB  . GLN A 1 539 ? -16.943 19.564  -77.280  1.00 49.03  ?  537 GLN A CB  1 
ATOM   3963 C  CG  . GLN A 1 539 ? -15.438 19.341  -77.351  1.00 50.30  ?  537 GLN A CG  1 
ATOM   3964 C  CD  . GLN A 1 539 ? -14.661 20.637  -77.472  1.00 51.09  ?  537 GLN A CD  1 
ATOM   3965 O  OE1 . GLN A 1 539 ? -14.743 21.331  -78.485  1.00 43.76  ?  537 GLN A OE1 1 
ATOM   3966 N  NE2 . GLN A 1 539 ? -13.915 20.979  -76.428  1.00 55.37  ?  537 GLN A NE2 1 
ATOM   3967 N  N   . GLY A 1 540 ? -16.867 16.185  -76.973  1.00 49.88  ?  538 GLY A N   1 
ATOM   3968 C  CA  . GLY A 1 540 ? -16.615 15.053  -76.114  1.00 50.00  ?  538 GLY A CA  1 
ATOM   3969 C  C   . GLY A 1 540 ? -17.682 13.987  -76.175  1.00 52.76  ?  538 GLY A C   1 
ATOM   3970 O  O   . GLY A 1 540 ? -17.544 12.954  -75.506  1.00 47.72  ?  538 GLY A O   1 
ATOM   3971 N  N   . SER A 1 541 ? -18.750 14.215  -76.933  1.00 43.31  ?  539 SER A N   1 
ATOM   3972 C  CA  . SER A 1 541 ? -19.847 13.276  -77.086  1.00 44.48  ?  539 SER A CA  1 
ATOM   3973 C  C   . SER A 1 541 ? -19.786 12.652  -78.474  1.00 46.34  ?  539 SER A C   1 
ATOM   3974 O  O   . SER A 1 541 ? -19.267 13.253  -79.419  1.00 38.26  ?  539 SER A O   1 
ATOM   3975 C  CB  . SER A 1 541 ? -21.198 13.964  -76.869  1.00 45.63  ?  539 SER A CB  1 
ATOM   3976 O  OG  . SER A 1 541 ? -21.560 13.944  -75.495  1.00 50.10  ?  539 SER A OG  1 
ATOM   3977 N  N   . GLU A 1 542 ? -20.317 11.439  -78.594  1.00 42.90  ?  540 GLU A N   1 
ATOM   3978 C  CA  . GLU A 1 542 ? -20.279 10.713  -79.854  1.00 53.14  ?  540 GLU A CA  1 
ATOM   3979 C  C   . GLU A 1 542 ? -21.655 10.139  -80.159  1.00 47.92  ?  540 GLU A C   1 
ATOM   3980 O  O   . GLU A 1 542 ? -22.411 9.782   -79.253  1.00 45.60  ?  540 GLU A O   1 
ATOM   3981 C  CB  . GLU A 1 542 ? -19.207 9.608   -79.828  1.00 46.52  ?  540 GLU A CB  1 
ATOM   3982 C  CG  . GLU A 1 542 ? -19.546 8.387   -79.006  1.00 55.48  ?  540 GLU A CG  1 
ATOM   3983 C  CD  . GLU A 1 542 ? -18.488 7.307   -79.132  1.00 61.15  ?  540 GLU A CD  1 
ATOM   3984 O  OE1 . GLU A 1 542 ? -17.502 7.528   -79.869  1.00 51.52  ?  540 GLU A OE1 1 
ATOM   3985 O  OE2 . GLU A 1 542 ? -18.635 6.244   -78.492  1.00 58.67  -1 540 GLU A OE2 1 
ATOM   3986 N  N   . TYR A 1 543 ? -21.974 10.055  -81.449  1.00 39.90  ?  541 TYR A N   1 
ATOM   3987 C  CA  . TYR A 1 543 ? -23.293 9.611   -81.870  1.00 41.16  ?  541 TYR A CA  1 
ATOM   3988 C  C   . TYR A 1 543 ? -23.179 8.871   -83.190  1.00 44.65  ?  541 TYR A C   1 
ATOM   3989 O  O   . TYR A 1 543 ? -22.298 9.153   -84.008  1.00 40.28  ?  541 TYR A O   1 
ATOM   3990 C  CB  . TYR A 1 543 ? -24.283 10.771  -82.054  1.00 40.34  ?  541 TYR A CB  1 
ATOM   3991 C  CG  . TYR A 1 543 ? -24.273 11.809  -80.962  1.00 41.18  ?  541 TYR A CG  1 
ATOM   3992 C  CD1 . TYR A 1 543 ? -24.981 11.614  -79.783  1.00 45.06  ?  541 TYR A CD1 1 
ATOM   3993 C  CD2 . TYR A 1 543 ? -23.582 13.001  -81.122  1.00 38.61  ?  541 TYR A CD2 1 
ATOM   3994 C  CE1 . TYR A 1 543 ? -24.978 12.569  -78.787  1.00 46.34  ?  541 TYR A CE1 1 
ATOM   3995 C  CE2 . TYR A 1 543 ? -23.578 13.963  -80.137  1.00 42.51  ?  541 TYR A CE2 1 
ATOM   3996 C  CZ  . TYR A 1 543 ? -24.276 13.741  -78.967  1.00 43.63  ?  541 TYR A CZ  1 
ATOM   3997 O  OH  . TYR A 1 543 ? -24.275 14.703  -77.984  1.00 48.64  ?  541 TYR A OH  1 
ATOM   3998 N  N   . ASP A 1 544 ? -24.104 7.935   -83.396  1.00 42.18  ?  542 ASP A N   1 
ATOM   3999 C  CA  . ASP A 1 544 ? -24.089 7.131   -84.611  1.00 44.59  ?  542 ASP A CA  1 
ATOM   4000 C  C   . ASP A 1 544 ? -24.362 7.996   -85.830  1.00 42.28  ?  542 ASP A C   1 
ATOM   4001 O  O   . ASP A 1 544 ? -23.569 8.030   -86.778  1.00 37.89  ?  542 ASP A O   1 
ATOM   4002 C  CB  . ASP A 1 544 ? -25.122 6.012   -84.501  1.00 45.31  ?  542 ASP A CB  1 
ATOM   4003 C  CG  . ASP A 1 544 ? -24.585 4.808   -83.779  1.00 55.32  ?  542 ASP A CG  1 
ATOM   4004 O  OD1 . ASP A 1 544 ? -23.357 4.764   -83.557  1.00 59.53  ?  542 ASP A OD1 1 
ATOM   4005 O  OD2 . ASP A 1 544 ? -25.384 3.918   -83.419  1.00 59.06  -1 542 ASP A OD2 1 
ATOM   4006 N  N   . TYR A 1 545 ? -25.480 8.714   -85.814  1.00 39.04  ?  543 TYR A N   1 
ATOM   4007 C  CA  . TYR A 1 545 ? -25.901 9.557   -86.921  1.00 41.93  ?  543 TYR A CA  1 
ATOM   4008 C  C   . TYR A 1 545 ? -26.019 10.992  -86.430  1.00 36.50  ?  543 TYR A C   1 
ATOM   4009 O  O   . TYR A 1 545 ? -26.555 11.239  -85.345  1.00 38.47  ?  543 TYR A O   1 
ATOM   4010 C  CB  . TYR A 1 545 ? -27.229 9.073   -87.508  1.00 46.07  ?  543 TYR A CB  1 
ATOM   4011 C  CG  . TYR A 1 545 ? -27.120 7.785   -88.300  1.00 46.85  ?  543 TYR A CG  1 
ATOM   4012 C  CD1 . TYR A 1 545 ? -26.722 7.795   -89.631  1.00 38.90  ?  543 TYR A CD1 1 
ATOM   4013 C  CD2 . TYR A 1 545 ? -27.439 6.562   -87.722  1.00 44.41  ?  543 TYR A CD2 1 
ATOM   4014 C  CE1 . TYR A 1 545 ? -26.629 6.620   -90.361  1.00 40.63  ?  543 TYR A CE1 1 
ATOM   4015 C  CE2 . TYR A 1 545 ? -27.351 5.383   -88.445  1.00 54.53  ?  543 TYR A CE2 1 
ATOM   4016 C  CZ  . TYR A 1 545 ? -26.946 5.418   -89.763  1.00 51.32  ?  543 TYR A CZ  1 
ATOM   4017 O  OH  . TYR A 1 545 ? -26.857 4.249   -90.483  1.00 56.46  ?  543 TYR A OH  1 
ATOM   4018 N  N   . VAL A 1 546 ? -25.492 11.924  -87.218  1.00 36.96  ?  544 VAL A N   1 
ATOM   4019 C  CA  . VAL A 1 546 ? -25.498 13.346  -86.901  1.00 42.70  ?  544 VAL A CA  1 
ATOM   4020 C  C   . VAL A 1 546 ? -26.054 14.098  -88.100  1.00 36.50  ?  544 VAL A C   1 
ATOM   4021 O  O   . VAL A 1 546 ? -25.717 13.785  -89.248  1.00 42.07  ?  544 VAL A O   1 
ATOM   4022 C  CB  . VAL A 1 546 ? -24.083 13.864  -86.557  1.00 44.49  ?  544 VAL A CB  1 
ATOM   4023 C  CG1 . VAL A 1 546 ? -24.034 15.386  -86.628  1.00 40.69  ?  544 VAL A CG1 1 
ATOM   4024 C  CG2 . VAL A 1 546 ? -23.651 13.377  -85.191  1.00 31.43  ?  544 VAL A CG2 1 
ATOM   4025 N  N   . ILE A 1 547 ? -26.916 15.078  -87.840  1.00 31.10  ?  545 ILE A N   1 
ATOM   4026 C  CA  . ILE A 1 547 ? -27.441 15.962  -88.877  1.00 37.90  ?  545 ILE A CA  1 
ATOM   4027 C  C   . ILE A 1 547 ? -27.018 17.378  -88.518  1.00 39.91  ?  545 ILE A C   1 
ATOM   4028 O  O   . ILE A 1 547 ? -27.314 17.858  -87.418  1.00 29.25  ?  545 ILE A O   1 
ATOM   4029 C  CB  . ILE A 1 547 ? -28.968 15.856  -89.015  1.00 40.03  ?  545 ILE A CB  1 
ATOM   4030 C  CG1 . ILE A 1 547 ? -29.356 14.475  -89.547  1.00 33.12  ?  545 ILE A CG1 1 
ATOM   4031 C  CG2 . ILE A 1 547 ? -29.497 16.957  -89.926  1.00 37.75  ?  545 ILE A CG2 1 
ATOM   4032 C  CD1 . ILE A 1 547 ? -30.848 14.261  -89.682  1.00 44.81  ?  545 ILE A CD1 1 
ATOM   4033 N  N   . PHE A 1 548 ? -26.327 18.045  -89.438  1.00 26.58  ?  546 PHE A N   1 
ATOM   4034 C  CA  . PHE A 1 548 ? -25.760 19.355  -89.154  1.00 25.64  ?  546 PHE A CA  1 
ATOM   4035 C  C   . PHE A 1 548 ? -26.220 20.370  -90.187  1.00 38.66  ?  546 PHE A C   1 
ATOM   4036 O  O   . PHE A 1 548 ? -26.129 20.121  -91.394  1.00 26.57  ?  546 PHE A O   1 
ATOM   4037 C  CB  . PHE A 1 548 ? -24.226 19.266  -89.111  1.00 24.50  ?  546 PHE A CB  1 
ATOM   4038 C  CG  . PHE A 1 548 ? -23.535 20.592  -89.006  1.00 32.55  ?  546 PHE A CG  1 
ATOM   4039 C  CD1 . PHE A 1 548 ? -23.316 21.168  -87.772  1.00 24.43  ?  546 PHE A CD1 1 
ATOM   4040 C  CD2 . PHE A 1 548 ? -23.054 21.240  -90.140  1.00 24.20  ?  546 PHE A CD2 1 
ATOM   4041 C  CE1 . PHE A 1 548 ? -22.666 22.383  -87.657  1.00 33.68  ?  546 PHE A CE1 1 
ATOM   4042 C  CE2 . PHE A 1 548 ? -22.400 22.453  -90.029  1.00 25.18  ?  546 PHE A CE2 1 
ATOM   4043 C  CZ  . PHE A 1 548 ? -22.202 23.025  -88.790  1.00 30.63  ?  546 PHE A CZ  1 
ATOM   4044 N  N   . THR A 1 549 ? -26.719 21.506  -89.706  1.00 40.30  ?  547 THR A N   1 
ATOM   4045 C  CA  . THR A 1 549 ? -27.098 22.634  -90.547  1.00 27.48  ?  547 THR A CA  1 
ATOM   4046 C  C   . THR A 1 549 ? -26.232 23.816  -90.144  1.00 30.92  ?  547 THR A C   1 
ATOM   4047 O  O   . THR A 1 549 ? -26.276 24.251  -88.988  1.00 25.90  ?  547 THR A O   1 
ATOM   4048 C  CB  . THR A 1 549 ? -28.586 22.978  -90.400  1.00 33.81  ?  547 THR A CB  1 
ATOM   4049 O  OG1 . THR A 1 549 ? -28.899 23.188  -89.016  1.00 31.85  ?  547 THR A OG1 1 
ATOM   4050 C  CG2 . THR A 1 549 ? -29.455 21.852  -90.948  1.00 32.69  ?  547 THR A CG2 1 
ATOM   4051 N  N   . GLN A 1 550 ? -25.436 24.328  -91.088  1.00 24.62  ?  548 GLN A N   1 
ATOM   4052 C  CA  . GLN A 1 550 ? -24.540 25.427  -90.753  1.00 24.62  ?  548 GLN A CA  1 
ATOM   4053 C  C   . GLN A 1 550 ? -25.320 26.674  -90.364  1.00 25.71  ?  548 GLN A C   1 
ATOM   4054 O  O   . GLN A 1 550 ? -24.811 27.519  -89.622  1.00 33.40  ?  548 GLN A O   1 
ATOM   4055 C  CB  . GLN A 1 550 ? -23.597 25.719  -91.928  1.00 24.41  ?  548 GLN A CB  1 
ATOM   4056 C  CG  . GLN A 1 550 ? -22.293 26.360  -91.505  1.00 24.51  ?  548 GLN A CG  1 
ATOM   4057 C  CD  . GLN A 1 550 ? -21.353 26.577  -92.669  1.00 35.88  ?  548 GLN A CD  1 
ATOM   4058 O  OE1 . GLN A 1 550 ? -21.707 26.319  -93.817  1.00 25.22  ?  548 GLN A OE1 1 
ATOM   4059 N  NE2 . GLN A 1 550 ? -20.143 27.042  -92.377  1.00 25.35  ?  548 GLN A NE2 1 
ATOM   4060 N  N   . THR A 1 551 ? -26.552 26.800  -90.855  1.00 26.38  ?  549 THR A N   1 
ATOM   4061 C  CA  . THR A 1 551 ? -27.482 27.868  -90.498  1.00 27.76  ?  549 THR A CA  1 
ATOM   4062 C  C   . THR A 1 551 ? -27.101 29.209  -91.117  1.00 30.72  ?  549 THR A C   1 
ATOM   4063 O  O   . THR A 1 551 ? -27.950 29.866  -91.727  1.00 35.64  ?  549 THR A O   1 
ATOM   4064 C  CB  . THR A 1 551 ? -27.593 28.001  -88.977  1.00 34.09  ?  549 THR A CB  1 
ATOM   4065 O  OG1 . THR A 1 551 ? -27.735 26.697  -88.403  1.00 28.37  ?  549 THR A OG1 1 
ATOM   4066 C  CG2 . THR A 1 551 ? -28.819 28.837  -88.609  1.00 34.22  ?  549 THR A CG2 1 
ATOM   4067 N  N   . THR A 1 552 ? -25.841 29.629  -90.982  1.00 30.62  ?  550 THR A N   1 
ATOM   4068 C  CA  . THR A 1 552 ? -25.411 30.923  -91.499  1.00 36.94  ?  550 THR A CA  1 
ATOM   4069 C  C   . THR A 1 552 ? -23.998 30.809  -92.049  1.00 34.44  ?  550 THR A C   1 
ATOM   4070 O  O   . THR A 1 552 ? -23.321 29.791  -91.886  1.00 33.95  ?  550 THR A O   1 
ATOM   4071 C  CB  . THR A 1 552 ? -25.447 32.027  -90.430  1.00 43.14  ?  550 THR A CB  1 
ATOM   4072 O  OG1 . THR A 1 552 ? -24.656 31.634  -89.303  1.00 43.57  ?  550 THR A OG1 1 
ATOM   4073 C  CG2 . THR A 1 552 ? -26.870 32.289  -89.971  1.00 41.95  ?  550 THR A CG2 1 
ATOM   4074 N  N   . GLU A 1 553 ? -23.565 31.878  -92.714  1.00 42.77  ?  551 GLU A N   1 
ATOM   4075 C  CA  . GLU A 1 553 ? -22.195 32.043  -93.196  1.00 50.12  ?  551 GLU A CA  1 
ATOM   4076 C  C   . GLU A 1 553 ? -21.548 33.164  -92.384  1.00 45.40  ?  551 GLU A C   1 
ATOM   4077 O  O   . GLU A 1 553 ? -21.407 34.294  -92.852  1.00 56.44  ?  551 GLU A O   1 
ATOM   4078 C  CB  . GLU A 1 553 ? -22.144 32.355  -94.711  1.00 47.70  ?  551 GLU A CB  1 
ATOM   4079 C  CG  . GLU A 1 553 ? -23.354 31.914  -95.509  1.00 50.41  ?  551 GLU A CG  1 
ATOM   4080 C  CD  . GLU A 1 553 ? -23.227 32.263  -96.982  1.00 62.86  ?  551 GLU A CD  1 
ATOM   4081 O  OE1 . GLU A 1 553 ? -22.099 32.567  -97.428  1.00 61.02  ?  551 GLU A OE1 1 
ATOM   4082 O  OE2 . GLU A 1 553 ? -24.256 32.238  -97.691  1.00 66.77  -1 551 GLU A OE2 1 
ATOM   4083 N  N   . THR A 1 554 ? -21.183 32.853  -91.145  1.00 43.14  ?  552 THR A N   1 
ATOM   4084 C  CA  . THR A 1 554 ? -20.560 33.809  -90.239  1.00 42.75  ?  552 THR A CA  1 
ATOM   4085 C  C   . THR A 1 554 ? -19.223 33.260  -89.762  1.00 41.90  ?  552 THR A C   1 
ATOM   4086 O  O   . THR A 1 554 ? -18.891 32.090  -89.974  1.00 39.05  ?  552 THR A O   1 
ATOM   4087 C  CB  . THR A 1 554 ? -21.447 34.101  -89.020  1.00 40.93  ?  552 THR A CB  1 
ATOM   4088 O  OG1 . THR A 1 554 ? -21.621 32.899  -88.257  1.00 38.64  ?  552 THR A OG1 1 
ATOM   4089 C  CG2 . THR A 1 554 ? -22.807 34.642  -89.443  1.00 41.75  ?  552 THR A CG2 1 
ATOM   4090 N  N   . ALA A 1 555 ? -18.464 34.113  -89.072  1.00 38.08  ?  553 ALA A N   1 
ATOM   4091 C  CA  . ALA A 1 555 ? -17.199 33.658  -88.506  1.00 42.38  ?  553 ALA A CA  1 
ATOM   4092 C  C   . ALA A 1 555 ? -17.440 32.560  -87.480  1.00 37.80  ?  553 ALA A C   1 
ATOM   4093 O  O   . ALA A 1 555 ? -16.647 31.617  -87.365  1.00 36.28  ?  553 ALA A O   1 
ATOM   4094 C  CB  . ALA A 1 555 ? -16.446 34.832  -87.883  1.00 45.88  ?  553 ALA A CB  1 
ATOM   4095 N  N   . HIS A 1 556 ? -18.535 32.668  -86.725  1.00 39.20  ?  554 HIS A N   1 
ATOM   4096 C  CA  . HIS A 1 556 ? -18.902 31.618  -85.781  1.00 42.95  ?  554 HIS A CA  1 
ATOM   4097 C  C   . HIS A 1 556 ? -19.250 30.319  -86.506  1.00 38.51  ?  554 HIS A C   1 
ATOM   4098 O  O   . HIS A 1 556 ? -18.795 29.242  -86.108  1.00 38.52  ?  554 HIS A O   1 
ATOM   4099 C  CB  . HIS A 1 556 ? -20.068 32.110  -84.917  1.00 43.20  ?  554 HIS A CB  1 
ATOM   4100 C  CG  . HIS A 1 556 ? -20.641 31.077  -83.997  1.00 42.45  ?  554 HIS A CG  1 
ATOM   4101 N  ND1 . HIS A 1 556 ? -20.159 30.865  -82.723  1.00 41.52  ?  554 HIS A ND1 1 
ATOM   4102 C  CD2 . HIS A 1 556 ? -21.683 30.226  -84.151  1.00 47.19  ?  554 HIS A CD2 1 
ATOM   4103 C  CE1 . HIS A 1 556 ? -20.867 29.915  -82.139  1.00 42.42  ?  554 HIS A CE1 1 
ATOM   4104 N  NE2 . HIS A 1 556 ? -21.798 29.511  -82.984  1.00 41.86  ?  554 HIS A NE2 1 
ATOM   4105 N  N   . SER A 1 557 ? -20.031 30.401  -87.589  1.00 35.26  ?  555 SER A N   1 
ATOM   4106 C  CA  . SER A 1 557 ? -20.471 29.201  -88.297  1.00 40.43  ?  555 SER A CA  1 
ATOM   4107 C  C   . SER A 1 557 ? -19.370 28.573  -89.143  1.00 33.08  ?  555 SER A C   1 
ATOM   4108 O  O   . SER A 1 557 ? -19.470 27.386  -89.477  1.00 28.42  ?  555 SER A O   1 
ATOM   4109 C  CB  . SER A 1 557 ? -21.688 29.498  -89.182  1.00 30.79  ?  555 SER A CB  1 
ATOM   4110 O  OG  . SER A 1 557 ? -21.336 30.252  -90.325  1.00 48.43  ?  555 SER A OG  1 
ATOM   4111 N  N   . CYS A 1 558 ? -18.352 29.343  -89.534  1.00 39.91  ?  556 CYS A N   1 
ATOM   4112 C  CA  . CYS A 1 558 ? -17.285 28.848  -90.395  1.00 41.29  ?  556 CYS A CA  1 
ATOM   4113 C  C   . CYS A 1 558 ? -15.976 28.598  -89.653  1.00 38.92  ?  556 CYS A C   1 
ATOM   4114 O  O   . CYS A 1 558 ? -14.997 28.192  -90.285  1.00 29.53  ?  556 CYS A O   1 
ATOM   4115 C  CB  . CYS A 1 558 ? -17.020 29.825  -91.554  1.00 38.24  ?  556 CYS A CB  1 
ATOM   4116 S  SG  . CYS A 1 558 ? -18.386 30.123  -92.717  1.00 40.31  ?  556 CYS A SG  1 
ATOM   4117 N  N   . ASN A 1 559 ? -15.930 28.819  -88.337  1.00 32.40  ?  557 ASN A N   1 
ATOM   4118 C  CA  . ASN A 1 559 ? -14.727 28.526  -87.563  1.00 33.51  ?  557 ASN A CA  1 
ATOM   4119 C  C   . ASN A 1 559 ? -14.288 27.080  -87.784  1.00 31.17  ?  557 ASN A C   1 
ATOM   4120 O  O   . ASN A 1 559 ? -15.099 26.155  -87.691  1.00 33.40  ?  557 ASN A O   1 
ATOM   4121 C  CB  . ASN A 1 559 ? -14.998 28.785  -86.079  1.00 37.71  ?  557 ASN A CB  1 
ATOM   4122 C  CG  . ASN A 1 559 ? -13.753 28.662  -85.226  1.00 41.36  ?  557 ASN A CG  1 
ATOM   4123 O  OD1 . ASN A 1 559 ? -13.514 27.628  -84.607  1.00 38.50  ?  557 ASN A OD1 1 
ATOM   4124 N  ND2 . ASN A 1 559 ? -12.963 29.732  -85.169  1.00 37.99  ?  557 ASN A ND2 1 
ATOM   4125 N  N   . VAL A 1 560 ? -12.997 26.879  -88.073  1.00 32.19  ?  558 VAL A N   1 
ATOM   4126 C  CA  . VAL A 1 560 ? -12.560 25.531  -88.442  1.00 30.36  ?  558 VAL A CA  1 
ATOM   4127 C  C   . VAL A 1 560 ? -12.567 24.600  -87.237  1.00 32.64  ?  558 VAL A C   1 
ATOM   4128 O  O   . VAL A 1 560 ? -12.821 23.399  -87.379  1.00 29.89  ?  558 VAL A O   1 
ATOM   4129 C  CB  . VAL A 1 560 ? -11.168 25.551  -89.103  1.00 31.63  ?  558 VAL A CB  1 
ATOM   4130 C  CG1 . VAL A 1 560 ? -11.225 26.234  -90.469  1.00 30.65  ?  558 VAL A CG1 1 
ATOM   4131 C  CG2 . VAL A 1 560 ? -10.134 26.192  -88.183  1.00 35.04  ?  558 VAL A CG2 1 
ATOM   4132 N  N   . ASN A 1 561 ? -12.278 25.115  -86.041  1.00 36.24  ?  559 ASN A N   1 
ATOM   4133 C  CA  . ASN A 1 561 ? -12.337 24.264  -84.857  1.00 36.78  ?  559 ASN A CA  1 
ATOM   4134 C  C   . ASN A 1 561 ? -13.763 23.795  -84.608  1.00 34.20  ?  559 ASN A C   1 
ATOM   4135 O  O   . ASN A 1 561 ? -14.008 22.608  -84.369  1.00 35.69  ?  559 ASN A O   1 
ATOM   4136 C  CB  . ASN A 1 561 ? -11.782 25.006  -83.638  1.00 37.13  ?  559 ASN A CB  1 
ATOM   4137 C  CG  . ASN A 1 561 ? -10.293 25.277  -83.748  1.00 41.24  ?  559 ASN A CG  1 
ATOM   4138 O  OD1 . ASN A 1 561 ? -9.798  25.683  -84.799  1.00 48.86  ?  559 ASN A OD1 1 
ATOM   4139 N  ND2 . ASN A 1 561 ? -9.569  25.056  -82.656  1.00 38.50  ?  559 ASN A ND2 1 
ATOM   4140 N  N   . ARG A 1 562 ? -14.722 24.718  -84.693  1.00 34.05  ?  560 ARG A N   1 
ATOM   4141 C  CA  . ARG A 1 562 ? -16.127 24.368  -84.514  1.00 27.90  ?  560 ARG A CA  1 
ATOM   4142 C  C   . ARG A 1 562 ? -16.599 23.375  -85.572  1.00 30.13  ?  560 ARG A C   1 
ATOM   4143 O  O   . ARG A 1 562 ? -17.289 22.400  -85.258  1.00 25.57  ?  560 ARG A O   1 
ATOM   4144 C  CB  . ARG A 1 562 ? -16.975 25.640  -84.528  1.00 30.58  ?  560 ARG A CB  1 
ATOM   4145 C  CG  . ARG A 1 562 ? -18.469 25.422  -84.404  1.00 37.68  ?  560 ARG A CG  1 
ATOM   4146 C  CD  . ARG A 1 562 ? -19.167 26.721  -84.028  1.00 44.12  ?  560 ARG A CD  1 
ATOM   4147 N  NE  . ARG A 1 562 ? -18.795 27.156  -82.686  1.00 44.16  ?  560 ARG A NE  1 
ATOM   4148 C  CZ  . ARG A 1 562 ? -18.067 28.230  -82.413  1.00 37.08  ?  560 ARG A CZ  1 
ATOM   4149 N  NH1 . ARG A 1 562 ? -17.491 28.938  -83.371  1.00 39.08  ?  560 ARG A NH1 1 
ATOM   4150 N  NH2 . ARG A 1 562 ? -17.882 28.582  -81.143  1.00 41.25  ?  560 ARG A NH2 1 
ATOM   4151 N  N   . PHE A 1 563 ? -16.261 23.613  -86.842  1.00 25.08  ?  561 PHE A N   1 
ATOM   4152 C  CA  . PHE A 1 563 ? -16.631 22.649  -87.872  1.00 23.96  ?  561 PHE A CA  1 
ATOM   4153 C  C   . PHE A 1 563 ? -15.991 21.289  -87.621  1.00 23.88  ?  561 PHE A C   1 
ATOM   4154 O  O   . PHE A 1 563 ? -16.598 20.246  -87.898  1.00 23.39  ?  561 PHE A O   1 
ATOM   4155 C  CB  . PHE A 1 563 ? -16.252 23.171  -89.259  1.00 23.92  ?  561 PHE A CB  1 
ATOM   4156 C  CG  . PHE A 1 563 ? -16.937 22.445  -90.372  1.00 28.12  ?  561 PHE A CG  1 
ATOM   4157 C  CD1 . PHE A 1 563 ? -18.314 22.308  -90.383  1.00 37.45  ?  561 PHE A CD1 1 
ATOM   4158 C  CD2 . PHE A 1 563 ? -16.204 21.906  -91.419  1.00 37.86  ?  561 PHE A CD2 1 
ATOM   4159 C  CE1 . PHE A 1 563 ? -18.949 21.636  -91.412  1.00 50.97  ?  561 PHE A CE1 1 
ATOM   4160 C  CE2 . PHE A 1 563 ? -16.831 21.231  -92.444  1.00 23.45  ?  561 PHE A CE2 1 
ATOM   4161 C  CZ  . PHE A 1 563 ? -18.205 21.100  -92.448  1.00 22.94  ?  561 PHE A CZ  1 
ATOM   4162 N  N   . ASN A 1 564 ? -14.749 21.282  -87.136  1.00 24.67  ?  562 ASN A N   1 
ATOM   4163 C  CA  . ASN A 1 564 ? -14.055 20.030  -86.850  1.00 24.93  ?  562 ASN A CA  1 
ATOM   4164 C  C   . ASN A 1 564 ? -14.804 19.229  -85.787  1.00 27.84  ?  562 ASN A C   1 
ATOM   4165 O  O   . ASN A 1 564 ? -15.103 18.043  -85.974  1.00 25.07  ?  562 ASN A O   1 
ATOM   4166 C  CB  . ASN A 1 564 ? -12.617 20.346  -86.419  1.00 27.93  ?  562 ASN A CB  1 
ATOM   4167 C  CG  . ASN A 1 564 ? -11.880 19.143  -85.863  1.00 32.66  ?  562 ASN A CG  1 
ATOM   4168 O  OD1 . ASN A 1 564 ? -11.891 18.059  -86.449  1.00 32.21  ?  562 ASN A OD1 1 
ATOM   4169 N  ND2 . ASN A 1 564 ? -11.194 19.345  -84.743  1.00 33.27  ?  562 ASN A ND2 1 
ATOM   4170 N  N   . VAL A 1 565 ? -15.092 19.860  -84.652  1.00 26.22  ?  563 VAL A N   1 
ATOM   4171 C  CA  . VAL A 1 565 ? -15.829 19.186  -83.584  1.00 27.63  ?  563 VAL A CA  1 
ATOM   4172 C  C   . VAL A 1 565 ? -17.159 18.643  -84.103  1.00 28.60  ?  563 VAL A C   1 
ATOM   4173 O  O   . VAL A 1 565 ? -17.454 17.450  -83.977  1.00 27.24  ?  563 VAL A O   1 
ATOM   4174 C  CB  . VAL A 1 565 ? -16.044 20.149  -82.403  1.00 31.62  ?  563 VAL A CB  1 
ATOM   4175 C  CG1 . VAL A 1 565 ? -17.035 19.564  -81.403  1.00 30.47  ?  563 VAL A CG1 1 
ATOM   4176 C  CG2 . VAL A 1 565 ? -14.714 20.473  -81.737  1.00 33.13  ?  563 VAL A CG2 1 
ATOM   4177 N  N   . ALA A 1 566 ? -17.947 19.504  -84.755  1.00 41.33  ?  564 ALA A N   1 
ATOM   4178 C  CA  . ALA A 1 566 ? -19.270 19.136  -85.259  1.00 43.82  ?  564 ALA A CA  1 
ATOM   4179 C  C   . ALA A 1 566 ? -19.277 17.828  -86.049  1.00 43.65  ?  564 ALA A C   1 
ATOM   4180 O  O   . ALA A 1 566 ? -20.035 16.905  -85.732  1.00 25.77  ?  564 ALA A O   1 
ATOM   4181 C  CB  . ALA A 1 566 ? -19.816 20.278  -86.124  1.00 31.09  ?  564 ALA A CB  1 
ATOM   4182 N  N   . ILE A 1 567 ? -18.441 17.730  -87.084  1.00 23.94  ?  565 ILE A N   1 
ATOM   4183 C  CA  . ILE A 1 567 ? -18.481 16.568  -87.970  1.00 30.30  ?  565 ILE A CA  1 
ATOM   4184 C  C   . ILE A 1 567 ? -17.798 15.354  -87.361  1.00 25.59  ?  565 ILE A C   1 
ATOM   4185 O  O   . ILE A 1 567 ? -18.094 14.222  -87.766  1.00 28.45  ?  565 ILE A O   1 
ATOM   4186 C  CB  . ILE A 1 567 ? -17.896 16.905  -89.352  1.00 23.16  ?  565 ILE A CB  1 
ATOM   4187 C  CG1 . ILE A 1 567 ? -16.396 17.179  -89.267  1.00 26.03  ?  565 ILE A CG1 1 
ATOM   4188 C  CG2 . ILE A 1 567 ? -18.650 18.073  -89.973  1.00 29.33  ?  565 ILE A CG2 1 
ATOM   4189 C  CD1 . ILE A 1 567 ? -15.784 17.543  -90.638  1.00 23.34  ?  565 ILE A CD1 1 
ATOM   4190 N  N   . THR A 1 568 ? -16.880 15.553  -86.415  1.00 31.27  ?  566 THR A N   1 
ATOM   4191 C  CA  . THR A 1 568 ? -16.165 14.450  -85.787  1.00 29.33  ?  566 THR A CA  1 
ATOM   4192 C  C   . THR A 1 568 ? -16.974 13.824  -84.663  1.00 34.49  ?  566 THR A C   1 
ATOM   4193 O  O   . THR A 1 568 ? -16.420 13.085  -83.838  1.00 29.51  ?  566 THR A O   1 
ATOM   4194 C  CB  . THR A 1 568 ? -14.819 14.918  -85.230  1.00 26.81  ?  566 THR A CB  1 
ATOM   4195 O  OG1 . THR A 1 568 ? -15.030 16.048  -84.370  1.00 27.34  ?  566 THR A OG1 1 
ATOM   4196 C  CG2 . THR A 1 568 ? -13.869 15.299  -86.366  1.00 32.96  ?  566 THR A CG2 1 
ATOM   4197 N  N   . ARG A 1 569 ? -18.274 14.112  -84.619  1.00 36.23  ?  567 ARG A N   1 
ATOM   4198 C  CA  . ARG A 1 569 ? -19.151 13.536  -83.611  1.00 30.99  ?  567 ARG A CA  1 
ATOM   4199 C  C   . ARG A 1 569 ? -19.789 12.243  -84.096  1.00 31.09  ?  567 ARG A C   1 
ATOM   4200 O  O   . ARG A 1 569 ? -20.273 11.452  -83.276  1.00 33.45  ?  567 ARG A O   1 
ATOM   4201 C  CB  . ARG A 1 569 ? -20.279 14.516  -83.256  1.00 40.95  ?  567 ARG A CB  1 
ATOM   4202 C  CG  . ARG A 1 569 ? -19.884 15.866  -82.651  1.00 42.84  ?  567 ARG A CG  1 
ATOM   4203 C  CD  . ARG A 1 569 ? -18.951 15.753  -81.457  1.00 38.81  ?  567 ARG A CD  1 
ATOM   4204 N  NE  . ARG A 1 569 ? -17.557 15.796  -81.880  1.00 32.87  ?  567 ARG A NE  1 
ATOM   4205 C  CZ  . ARG A 1 569 ? -16.527 15.519  -81.095  1.00 40.12  ?  567 ARG A CZ  1 
ATOM   4206 N  NH1 . ARG A 1 569 ? -16.698 15.002  -79.886  1.00 34.81  ?  567 ARG A NH1 1 
ATOM   4207 N  NH2 . ARG A 1 569 ? -15.295 15.719  -81.550  1.00 31.18  ?  567 ARG A NH2 1 
ATOM   4208 N  N   . ALA A 1 570 ? -19.787 12.014  -85.405  1.00 29.72  ?  568 ALA A N   1 
ATOM   4209 C  CA  . ALA A 1 570 ? -20.510 10.910  -86.013  1.00 31.66  ?  568 ALA A CA  1 
ATOM   4210 C  C   . ALA A 1 570 ? -19.650 9.654   -86.055  1.00 33.44  ?  568 ALA A C   1 
ATOM   4211 O  O   . ALA A 1 570 ? -18.466 9.703   -86.401  1.00 35.84  ?  568 ALA A O   1 
ATOM   4212 C  CB  . ALA A 1 570 ? -20.958 11.278  -87.429  1.00 33.38  ?  568 ALA A CB  1 
ATOM   4213 N  N   . LYS A 1 571 ? -20.274 8.522   -85.745  1.00 34.30  ?  569 LYS A N   1 
ATOM   4214 C  CA  . LYS A 1 571 ? -19.616 7.224   -85.774  1.00 40.26  ?  569 LYS A CA  1 
ATOM   4215 C  C   . LYS A 1 571 ? -19.973 6.428   -87.015  1.00 36.11  ?  569 LYS A C   1 
ATOM   4216 O  O   . LYS A 1 571 ? -19.173 5.600   -87.459  1.00 40.60  ?  569 LYS A O   1 
ATOM   4217 C  CB  . LYS A 1 571 ? -19.985 6.392   -84.537  1.00 38.83  ?  569 LYS A CB  1 
ATOM   4218 C  CG  . LYS A 1 571 ? -19.498 6.957   -83.215  1.00 43.67  ?  569 LYS A CG  1 
ATOM   4219 C  CD  . LYS A 1 571 ? -19.725 5.966   -82.078  1.00 50.73  ?  569 LYS A CD  1 
ATOM   4220 C  CE  . LYS A 1 571 ? -21.195 5.832   -81.722  1.00 51.35  ?  569 LYS A CE  1 
ATOM   4221 N  NZ  . LYS A 1 571 ? -21.460 4.567   -80.973  1.00 53.76  ?  569 LYS A NZ  1 
ATOM   4222 N  N   . VAL A 1 572 ? -21.158 6.665   -87.577  1.00 38.57  ?  570 VAL A N   1 
ATOM   4223 C  CA  . VAL A 1 572 ? -21.639 5.912   -88.728  1.00 39.35  ?  570 VAL A CA  1 
ATOM   4224 C  C   . VAL A 1 572 ? -21.901 6.837   -89.910  1.00 40.16  ?  570 VAL A C   1 
ATOM   4225 O  O   . VAL A 1 572 ? -21.339 6.643   -90.992  1.00 40.57  ?  570 VAL A O   1 
ATOM   4226 C  CB  . VAL A 1 572 ? -22.911 5.125   -88.371  1.00 40.10  ?  570 VAL A CB  1 
ATOM   4227 C  CG1 . VAL A 1 572 ? -23.443 4.395   -89.595  1.00 43.95  ?  570 VAL A CG1 1 
ATOM   4228 C  CG2 . VAL A 1 572 ? -22.631 4.149   -87.236  1.00 42.70  ?  570 VAL A CG2 1 
ATOM   4229 N  N   . GLY A 1 573 ? -22.756 7.841   -89.726  1.00 37.13  ?  571 GLY A N   1 
ATOM   4230 C  CA  . GLY A 1 573 ? -23.131 8.702   -90.826  1.00 33.42  ?  571 GLY A CA  1 
ATOM   4231 C  C   . GLY A 1 573 ? -23.347 10.136  -90.388  1.00 31.24  ?  571 GLY A C   1 
ATOM   4232 O  O   . GLY A 1 573 ? -23.617 10.425  -89.220  1.00 39.08  ?  571 GLY A O   1 
ATOM   4233 N  N   . ILE A 1 574 ? -23.244 11.035  -91.364  1.00 34.29  ?  572 ILE A N   1 
ATOM   4234 C  CA  . ILE A 1 574 ? -23.481 12.452  -91.134  1.00 34.99  ?  572 ILE A CA  1 
ATOM   4235 C  C   . ILE A 1 574 ? -24.088 13.054  -92.392  1.00 35.34  ?  572 ILE A C   1 
ATOM   4236 O  O   . ILE A 1 574 ? -23.785 12.641  -93.515  1.00 38.38  ?  572 ILE A O   1 
ATOM   4237 C  CB  . ILE A 1 574 ? -22.190 13.200  -90.722  1.00 39.55  ?  572 ILE A CB  1 
ATOM   4238 C  CG1 . ILE A 1 574 ? -22.523 14.647  -90.350  1.00 42.22  ?  572 ILE A CG1 1 
ATOM   4239 C  CG2 . ILE A 1 574 ? -21.144 13.136  -91.837  1.00 33.72  ?  572 ILE A CG2 1 
ATOM   4240 C  CD1 . ILE A 1 574 ? -21.462 15.333  -89.519  1.00 38.91  ?  572 ILE A CD1 1 
ATOM   4241 N  N   . LEU A 1 575 ? -24.980 14.018  -92.186  1.00 31.80  ?  573 LEU A N   1 
ATOM   4242 C  CA  . LEU A 1 575 ? -25.569 14.828  -93.244  1.00 31.08  ?  573 LEU A CA  1 
ATOM   4243 C  C   . LEU A 1 575 ? -25.262 16.283  -92.934  1.00 37.88  ?  573 LEU A C   1 
ATOM   4244 O  O   . LEU A 1 575 ? -25.602 16.770  -91.853  1.00 26.01  ?  573 LEU A O   1 
ATOM   4245 C  CB  . LEU A 1 575 ? -27.079 14.607  -93.348  1.00 30.31  ?  573 LEU A CB  1 
ATOM   4246 C  CG  . LEU A 1 575 ? -27.827 15.624  -94.214  1.00 37.61  ?  573 LEU A CG  1 
ATOM   4247 C  CD1 . LEU A 1 575 ? -27.394 15.525  -95.672  1.00 38.89  ?  573 LEU A CD1 1 
ATOM   4248 C  CD2 . LEU A 1 575 ? -29.331 15.453  -94.082  1.00 33.72  ?  573 LEU A CD2 1 
ATOM   4249 N  N   . CYS A 1 576 ? -24.569 16.962  -93.840  1.00 26.91  ?  574 CYS A N   1 
ATOM   4250 C  CA  . CYS A 1 576 ? -24.188 18.350  -93.612  1.00 26.14  ?  574 CYS A CA  1 
ATOM   4251 C  C   . CYS A 1 576 ? -24.904 19.251  -94.608  1.00 35.57  ?  574 CYS A C   1 
ATOM   4252 O  O   . CYS A 1 576 ? -24.638 19.189  -95.816  1.00 25.80  ?  574 CYS A O   1 
ATOM   4253 C  CB  . CYS A 1 576 ? -22.672 18.527  -93.700  1.00 32.82  ?  574 CYS A CB  1 
ATOM   4254 S  SG  . CYS A 1 576 ? -21.770 17.825  -92.305  1.00 37.54  ?  574 CYS A SG  1 
ATOM   4255 N  N   . ILE A 1 577 ? -25.825 20.069  -94.104  1.00 29.51  ?  575 ILE A N   1 
ATOM   4256 C  CA  . ILE A 1 577 ? -26.484 21.086  -94.915  1.00 35.71  ?  575 ILE A CA  1 
ATOM   4257 C  C   . ILE A 1 577 ? -25.607 22.325  -94.791  1.00 35.65  ?  575 ILE A C   1 
ATOM   4258 O  O   . ILE A 1 577 ? -25.547 22.952  -93.729  1.00 35.82  ?  575 ILE A O   1 
ATOM   4259 C  CB  . ILE A 1 577 ? -27.920 21.356  -94.452  1.00 31.36  ?  575 ILE A CB  1 
ATOM   4260 C  CG1 . ILE A 1 577 ? -28.695 20.042  -94.299  1.00 33.85  ?  575 ILE A CG1 1 
ATOM   4261 C  CG2 . ILE A 1 577 ? -28.616 22.332  -95.406  1.00 28.25  ?  575 ILE A CG2 1 
ATOM   4262 C  CD1 . ILE A 1 577 ? -28.848 19.262  -95.587  1.00 34.89  ?  575 ILE A CD1 1 
ATOM   4263 N  N   . MET A 1 578 ? -24.921 22.667  -95.870  1.00 32.48  ?  576 MET A N   1 
ATOM   4264 C  CA  . MET A 1 578 ? -23.895 23.698  -95.856  1.00 37.68  ?  576 MET A CA  1 
ATOM   4265 C  C   . MET A 1 578 ? -24.375 25.049  -96.359  1.00 32.15  ?  576 MET A C   1 
ATOM   4266 O  O   . MET A 1 578 ? -25.209 25.150  -97.263  1.00 36.36  ?  576 MET A O   1 
ATOM   4267 C  CB  . MET A 1 578 ? -22.682 23.246  -96.665  1.00 29.22  ?  576 MET A CB  1 
ATOM   4268 C  CG  . MET A 1 578 ? -21.969 22.083  -96.000  1.00 35.60  ?  576 MET A CG  1 
ATOM   4269 S  SD  . MET A 1 578 ? -21.226 22.631  -94.450  1.00 33.23  ?  576 MET A SD  1 
ATOM   4270 C  CE  . MET A 1 578 ? -22.277 21.858  -93.223  1.00 35.41  ?  576 MET A CE  1 
ATOM   4271 N  N   . SER A 1 579 ? -23.827 26.094  -95.746  1.00 28.10  ?  577 SER A N   1 
ATOM   4272 C  CA  . SER A 1 579 ? -24.076 27.459  -96.167  1.00 46.50  ?  577 SER A CA  1 
ATOM   4273 C  C   . SER A 1 579 ? -22.829 28.145  -96.718  1.00 31.39  ?  577 SER A C   1 
ATOM   4274 O  O   . SER A 1 579 ? -22.956 29.194  -97.360  1.00 51.82  ?  577 SER A O   1 
ATOM   4275 C  CB  . SER A 1 579 ? -24.625 28.272  -94.984  1.00 28.38  ?  577 SER A CB  1 
ATOM   4276 O  OG  . SER A 1 579 ? -26.035 28.180  -94.918  1.00 36.47  ?  577 SER A OG  1 
ATOM   4277 N  N   . ASP A 1 580 ? -21.643 27.565  -96.517  1.00 40.34  ?  578 ASP A N   1 
ATOM   4278 C  CA  . ASP A 1 580 ? -20.365 28.145  -96.928  1.00 36.92  ?  578 ASP A CA  1 
ATOM   4279 C  C   . ASP A 1 580 ? -19.725 27.316  -98.041  1.00 30.87  ?  578 ASP A C   1 
ATOM   4280 O  O   . ASP A 1 580 ? -19.481 26.118  -97.865  1.00 29.74  ?  578 ASP A O   1 
ATOM   4281 C  CB  . ASP A 1 580 ? -19.432 28.218  -95.713  1.00 46.35  ?  578 ASP A CB  1 
ATOM   4282 C  CG  . ASP A 1 580 ? -18.085 28.837  -96.031  1.00 35.42  ?  578 ASP A CG  1 
ATOM   4283 O  OD1 . ASP A 1 580 ? -18.025 30.073  -96.190  1.00 37.30  ?  578 ASP A OD1 1 
ATOM   4284 O  OD2 . ASP A 1 580 ? -17.085 28.088  -96.099  1.00 32.49  -1 578 ASP A OD2 1 
ATOM   4285 N  N   . ARG A 1 581 ? -19.400 27.960  -99.169  1.00 33.97  ?  579 ARG A N   1 
ATOM   4286 C  CA  . ARG A 1 581 ? -18.884 27.215  -100.317 1.00 35.19  ?  579 ARG A CA  1 
ATOM   4287 C  C   . ARG A 1 581 ? -17.558 26.525  -100.005 1.00 34.96  ?  579 ARG A C   1 
ATOM   4288 O  O   . ARG A 1 581 ? -17.335 25.382  -100.421 1.00 35.02  ?  579 ARG A O   1 
ATOM   4289 C  CB  . ARG A 1 581 ? -18.743 28.135  -101.536 1.00 38.74  ?  579 ARG A CB  1 
ATOM   4290 C  CG  . ARG A 1 581 ? -18.152 27.446  -102.768 1.00 50.83  ?  579 ARG A CG  1 
ATOM   4291 C  CD  . ARG A 1 581 ? -18.941 26.219  -103.231 1.00 62.03  ?  579 ARG A CD  1 
ATOM   4292 N  NE  . ARG A 1 581 ? -20.121 26.535  -104.029 1.00 66.90  ?  579 ARG A NE  1 
ATOM   4293 C  CZ  . ARG A 1 581 ? -20.896 25.623  -104.603 1.00 62.93  ?  579 ARG A CZ  1 
ATOM   4294 N  NH1 . ARG A 1 581 ? -20.576 24.339  -104.592 1.00 59.40  ?  579 ARG A NH1 1 
ATOM   4295 N  NH2 . ARG A 1 581 ? -21.995 26.014  -105.242 1.00 62.91  ?  579 ARG A NH2 1 
ATOM   4296 N  N   . ASP A 1 582 ? -16.658 27.206  -99.292  1.00 40.46  ?  580 ASP A N   1 
ATOM   4297 C  CA  . ASP A 1 582 ? -15.346 26.631  -98.997  1.00 35.26  ?  580 ASP A CA  1 
ATOM   4298 C  C   . ASP A 1 582 ? -15.471 25.365  -98.159  1.00 44.27  ?  580 ASP A C   1 
ATOM   4299 O  O   . ASP A 1 582 ? -14.975 24.297  -98.537  1.00 36.19  ?  580 ASP A O   1 
ATOM   4300 C  CB  . ASP A 1 582 ? -14.476 27.663  -98.278  1.00 44.72  ?  580 ASP A CB  1 
ATOM   4301 C  CG  . ASP A 1 582 ? -13.068 27.156  -98.004  1.00 60.52  ?  580 ASP A CG  1 
ATOM   4302 O  OD1 . ASP A 1 582 ? -12.639 26.176  -98.652  1.00 71.98  ?  580 ASP A OD1 1 
ATOM   4303 O  OD2 . ASP A 1 582 ? -12.387 27.742  -97.136  1.00 66.56  -1 580 ASP A OD2 1 
ATOM   4304 N  N   . LEU A 1 583 ? -16.107 25.469  -96.993  1.00 33.84  ?  581 LEU A N   1 
ATOM   4305 C  CA  . LEU A 1 583 ? -16.216 24.289  -96.145  1.00 29.51  ?  581 LEU A CA  1 
ATOM   4306 C  C   . LEU A 1 583 ? -17.000 23.184  -96.840  1.00 27.92  ?  581 LEU A C   1 
ATOM   4307 O  O   . LEU A 1 583 ? -16.655 22.005  -96.710  1.00 27.48  ?  581 LEU A O   1 
ATOM   4308 C  CB  . LEU A 1 583 ? -16.842 24.661  -94.800  1.00 28.86  ?  581 LEU A CB  1 
ATOM   4309 C  CG  . LEU A 1 583 ? -15.889 25.454  -93.899  1.00 27.34  ?  581 LEU A CG  1 
ATOM   4310 C  CD1 . LEU A 1 583 ? -16.603 25.961  -92.653  1.00 40.53  ?  581 LEU A CD1 1 
ATOM   4311 C  CD2 . LEU A 1 583 ? -14.660 24.626  -93.536  1.00 27.16  ?  581 LEU A CD2 1 
ATOM   4312 N  N   . TYR A 1 584 ? -17.994 23.548  -97.657  1.00 45.35  ?  582 TYR A N   1 
ATOM   4313 C  CA  . TYR A 1 584 ? -18.740 22.544  -98.412  1.00 41.84  ?  582 TYR A CA  1 
ATOM   4314 C  C   . TYR A 1 584 ? -17.832 21.785  -99.375  1.00 31.88  ?  582 TYR A C   1 
ATOM   4315 O  O   . TYR A 1 584 ? -17.874 20.552  -99.441  1.00 30.83  ?  582 TYR A O   1 
ATOM   4316 C  CB  . TYR A 1 584 ? -19.903 23.195  -99.165  1.00 29.89  ?  582 TYR A CB  1 
ATOM   4317 C  CG  . TYR A 1 584 ? -20.613 22.236  -100.099 1.00 40.09  ?  582 TYR A CG  1 
ATOM   4318 C  CD1 . TYR A 1 584 ? -21.639 21.409  -99.646  1.00 29.82  ?  582 TYR A CD1 1 
ATOM   4319 C  CD2 . TYR A 1 584 ? -20.249 22.152  -101.437 1.00 33.70  ?  582 TYR A CD2 1 
ATOM   4320 C  CE1 . TYR A 1 584 ? -22.279 20.527  -100.503 1.00 31.24  ?  582 TYR A CE1 1 
ATOM   4321 C  CE2 . TYR A 1 584 ? -20.878 21.277  -102.294 1.00 35.17  ?  582 TYR A CE2 1 
ATOM   4322 C  CZ  . TYR A 1 584 ? -21.891 20.469  -101.830 1.00 33.89  ?  582 TYR A CZ  1 
ATOM   4323 O  OH  . TYR A 1 584 ? -22.509 19.602  -102.703 1.00 35.79  ?  582 TYR A OH  1 
ATOM   4324 N  N   . ASP A 1 585 ? -17.005 22.502  -100.142 1.00 48.94  ?  583 ASP A N   1 
ATOM   4325 C  CA  . ASP A 1 585 ? -16.157 21.816  -101.112 1.00 37.11  ?  583 ASP A CA  1 
ATOM   4326 C  C   . ASP A 1 585 ? -15.162 20.903  -100.414 1.00 49.30  ?  583 ASP A C   1 
ATOM   4327 O  O   . ASP A 1 585 ? -14.813 19.840  -100.940 1.00 53.55  ?  583 ASP A O   1 
ATOM   4328 C  CB  . ASP A 1 585 ? -15.408 22.820  -101.987 1.00 47.16  ?  583 ASP A CB  1 
ATOM   4329 C  CG  . ASP A 1 585 ? -16.295 23.464  -103.029 1.00 52.25  ?  583 ASP A CG  1 
ATOM   4330 O  OD1 . ASP A 1 585 ? -17.110 22.744  -103.645 1.00 52.03  ?  583 ASP A OD1 1 
ATOM   4331 O  OD2 . ASP A 1 585 ? -16.168 24.688  -103.239 1.00 55.58  -1 583 ASP A OD2 1 
ATOM   4332 N  N   . LYS A 1 586 ? -14.695 21.301  -99.231  1.00 41.04  ?  584 LYS A N   1 
ATOM   4333 C  CA  . LYS A 1 586 ? -13.702 20.515  -98.516  1.00 46.44  ?  584 LYS A CA  1 
ATOM   4334 C  C   . LYS A 1 586 ? -14.289 19.226  -97.956  1.00 41.03  ?  584 LYS A C   1 
ATOM   4335 O  O   . LYS A 1 586 ? -13.531 18.301  -97.643  1.00 49.87  ?  584 LYS A O   1 
ATOM   4336 C  CB  . LYS A 1 586 ? -13.082 21.364  -97.404  1.00 44.20  ?  584 LYS A CB  1 
ATOM   4337 C  CG  . LYS A 1 586 ? -11.989 22.320  -97.904  1.00 33.98  ?  584 LYS A CG  1 
ATOM   4338 C  CD  . LYS A 1 586 ? -11.594 23.333  -96.834  1.00 36.67  ?  584 LYS A CD  1 
ATOM   4339 C  CE  . LYS A 1 586 ? -10.287 24.039  -97.153  1.00 54.09  ?  584 LYS A CE  1 
ATOM   4340 N  NZ  . LYS A 1 586 ? -10.271 24.611  -98.532  1.00 50.23  ?  584 LYS A NZ  1 
ATOM   4341 N  N   . LEU A 1 587 ? -15.613 19.133  -97.834  1.00 29.88  ?  585 LEU A N   1 
ATOM   4342 C  CA  . LEU A 1 587 ? -16.235 17.925  -97.297  1.00 43.55  ?  585 LEU A CA  1 
ATOM   4343 C  C   . LEU A 1 587 ? -16.131 16.808  -98.328  1.00 36.50  ?  585 LEU A C   1 
ATOM   4344 O  O   . LEU A 1 587 ? -16.761 16.865  -99.389  1.00 33.90  ?  585 LEU A O   1 
ATOM   4345 C  CB  . LEU A 1 587 ? -17.694 18.182  -96.923  1.00 26.85  ?  585 LEU A CB  1 
ATOM   4346 C  CG  . LEU A 1 587 ? -17.997 18.954  -95.639  1.00 38.97  ?  585 LEU A CG  1 
ATOM   4347 C  CD1 . LEU A 1 587 ? -19.495 19.200  -95.510  1.00 31.62  ?  585 LEU A CD1 1 
ATOM   4348 C  CD2 . LEU A 1 587 ? -17.480 18.192  -94.425  1.00 42.24  ?  585 LEU A CD2 1 
ATOM   4349 N  N   . GLN A 1 588 ? -15.339 15.787  -98.010  1.00 36.28  ?  586 GLN A N   1 
ATOM   4350 C  CA  . GLN A 1 588 ? -15.157 14.630  -98.882  1.00 32.32  ?  586 GLN A CA  1 
ATOM   4351 C  C   . GLN A 1 588 ? -16.336 13.667  -98.714  1.00 39.04  ?  586 GLN A C   1 
ATOM   4352 O  O   . GLN A 1 588 ? -16.190 12.495  -98.364  1.00 33.99  ?  586 GLN A O   1 
ATOM   4353 C  CB  . GLN A 1 588 ? -13.820 13.965  -98.582  1.00 33.11  ?  586 GLN A CB  1 
ATOM   4354 C  CG  . GLN A 1 588 ? -12.659 14.960  -98.590  1.00 37.74  ?  586 GLN A CG  1 
ATOM   4355 C  CD  . GLN A 1 588 ? -11.293 14.308  -98.490  1.00 43.85  ?  586 GLN A CD  1 
ATOM   4356 O  OE1 . GLN A 1 588 ? -11.163 13.084  -98.540  1.00 45.85  ?  586 GLN A OE1 1 
ATOM   4357 N  NE2 . GLN A 1 588 ? -10.261 15.132  -98.335  1.00 36.23  ?  586 GLN A NE2 1 
ATOM   4358 N  N   . PHE A 1 589 ? -17.531 14.198  -98.975  1.00 32.35  ?  587 PHE A N   1 
ATOM   4359 C  CA  . PHE A 1 589 ? -18.770 13.454  -98.829  1.00 31.50  ?  587 PHE A CA  1 
ATOM   4360 C  C   . PHE A 1 589 ? -19.470 13.376  -100.172 1.00 41.54  ?  587 PHE A C   1 
ATOM   4361 O  O   . PHE A 1 589 ? -19.145 14.106  -101.111 1.00 38.46  ?  587 PHE A O   1 
ATOM   4362 C  CB  . PHE A 1 589 ? -19.756 14.109  -97.846  1.00 35.89  ?  587 PHE A CB  1 
ATOM   4363 C  CG  . PHE A 1 589 ? -19.239 14.272  -96.448  1.00 35.48  ?  587 PHE A CG  1 
ATOM   4364 C  CD1 . PHE A 1 589 ? -18.107 13.607  -96.014  1.00 35.83  ?  587 PHE A CD1 1 
ATOM   4365 C  CD2 . PHE A 1 589 ? -19.929 15.071  -95.549  1.00 34.77  ?  587 PHE A CD2 1 
ATOM   4366 C  CE1 . PHE A 1 589 ? -17.653 13.772  -94.714  1.00 34.79  ?  587 PHE A CE1 1 
ATOM   4367 C  CE2 . PHE A 1 589 ? -19.486 15.231  -94.255  1.00 36.20  ?  587 PHE A CE2 1 
ATOM   4368 C  CZ  . PHE A 1 589 ? -18.348 14.582  -93.834  1.00 44.16  ?  587 PHE A CZ  1 
ATOM   4369 N  N   . THR A 1 590 ? -20.441 12.473  -100.252 1.00 42.46  ?  588 THR A N   1 
ATOM   4370 C  CA  . THR A 1 590 ? -21.266 12.375  -101.443 1.00 39.19  ?  588 THR A CA  1 
ATOM   4371 C  C   . THR A 1 590 ? -22.278 13.517  -101.419 1.00 37.48  ?  588 THR A C   1 
ATOM   4372 O  O   . THR A 1 590 ? -22.929 13.755  -100.398 1.00 34.78  ?  588 THR A O   1 
ATOM   4373 C  CB  . THR A 1 590 ? -21.968 11.018  -101.478 1.00 39.85  ?  588 THR A CB  1 
ATOM   4374 O  OG1 . THR A 1 590 ? -21.005 9.990   -101.744 1.00 52.85  ?  588 THR A OG1 1 
ATOM   4375 C  CG2 . THR A 1 590 ? -23.048 10.992  -102.545 1.00 41.60  ?  588 THR A CG2 1 
ATOM   4376 N  N   . SER A 1 591 ? -22.396 14.233  -102.535 1.00 37.86  ?  589 SER A N   1 
ATOM   4377 C  CA  . SER A 1 591 ? -23.339 15.340  -102.640 1.00 37.44  ?  589 SER A CA  1 
ATOM   4378 C  C   . SER A 1 591 ? -24.759 14.848  -102.896 1.00 42.23  ?  589 SER A C   1 
ATOM   4379 O  O   . SER A 1 591 ? -24.982 13.974  -103.739 1.00 45.84  ?  589 SER A O   1 
ATOM   4380 C  CB  . SER A 1 591 ? -22.913 16.308  -103.744 1.00 44.56  ?  589 SER A CB  1 
ATOM   4381 O  OG  . SER A 1 591 ? -22.828 15.662  -104.999 1.00 59.37  ?  589 SER A OG  1 
ATOM   4382 N  N   . LEU A 1 592 ? -25.716 15.404  -102.164 1.00 40.15  ?  590 LEU A N   1 
ATOM   4383 C  CA  . LEU A 1 592 ? -27.120 15.093  -102.373 1.00 43.35  ?  590 LEU A CA  1 
ATOM   4384 C  C   . LEU A 1 592 ? -27.769 16.263  -103.104 1.00 57.61  ?  590 LEU A C   1 
ATOM   4385 O  O   . LEU A 1 592 ? -27.290 17.398  -103.050 1.00 59.32  ?  590 LEU A O   1 
ATOM   4386 C  CB  . LEU A 1 592 ? -27.832 14.829  -101.043 1.00 47.05  ?  590 LEU A CB  1 
ATOM   4387 C  CG  . LEU A 1 592 ? -27.423 13.563  -100.285 1.00 46.97  ?  590 LEU A CG  1 
ATOM   4388 C  CD1 . LEU A 1 592 ? -28.288 13.376  -99.050  1.00 51.53  ?  590 LEU A CD1 1 
ATOM   4389 C  CD2 . LEU A 1 592 ? -27.513 12.341  -101.189 1.00 46.30  ?  590 LEU A CD2 1 
ATOM   4390 N  N   . GLU A 1 593 ? -28.866 15.979  -103.799 1.00 58.50  ?  591 GLU A N   1 
ATOM   4391 C  CA  . GLU A 1 593 ? -29.549 16.999  -104.581 1.00 60.74  ?  591 GLU A CA  1 
ATOM   4392 C  C   . GLU A 1 593 ? -31.017 17.052  -104.186 1.00 73.40  ?  591 GLU A C   1 
ATOM   4393 O  O   . GLU A 1 593 ? -31.645 16.015  -103.950 1.00 73.29  ?  591 GLU A O   1 
ATOM   4394 C  CB  . GLU A 1 593 ? -29.405 16.734  -106.090 1.00 60.21  ?  591 GLU A CB  1 
ATOM   4395 C  CG  . GLU A 1 593 ? -29.678 17.949  -106.973 1.00 81.49  ?  591 GLU A CG  1 
ATOM   4396 C  CD  . GLU A 1 593 ? -28.584 19.008  -106.885 1.00 76.03  ?  591 GLU A CD  1 
ATOM   4397 O  OE1 . GLU A 1 593 ? -27.573 18.771  -106.189 1.00 78.45  ?  591 GLU A OE1 1 
ATOM   4398 O  OE2 . GLU A 1 593 ? -28.736 20.077  -107.514 1.00 74.95  -1 591 GLU A OE2 1 
ATOM   4399 N  N   . ILE A 1 594 ? -31.555 18.266  -104.116 1.00 73.76  ?  592 ILE A N   1 
ATOM   4400 C  CA  . ILE A 1 594 ? -32.963 18.480  -103.805 1.00 76.74  ?  592 ILE A CA  1 
ATOM   4401 C  C   . ILE A 1 594 ? -33.255 19.974  -103.817 1.00 76.40  ?  592 ILE A C   1 
ATOM   4402 O  O   . ILE A 1 594 ? -32.346 20.787  -103.986 1.00 79.29  ?  592 ILE A O   1 
ATOM   4403 C  CB  . ILE A 1 594 ? -33.351 17.854  -102.450 1.00 72.22  ?  592 ILE A CB  1 
ATOM   4404 C  CG1 . ILE A 1 594 ? -34.814 17.403  -102.464 1.00 75.75  ?  592 ILE A CG1 1 
ATOM   4405 C  CG2 . ILE A 1 594 ? -33.108 18.840  -101.317 1.00 70.63  ?  592 ILE A CG2 1 
ATOM   4406 C  CD1 . ILE A 1 594 ? -35.152 16.421  -103.567 1.00 70.66  ?  592 ILE A CD1 1 
ATOM   4407 N  N   . VAL B 1 4   ? 2.576   3.132   -48.811  1.00 86.83  ?  2   VAL B N   1 
ATOM   4408 C  CA  . VAL B 1 4   ? 3.756   3.247   -47.964  1.00 87.45  ?  2   VAL B CA  1 
ATOM   4409 C  C   . VAL B 1 4   ? 3.637   4.493   -47.087  1.00 86.88  ?  2   VAL B C   1 
ATOM   4410 O  O   . VAL B 1 4   ? 3.076   5.504   -47.513  1.00 85.66  ?  2   VAL B O   1 
ATOM   4411 C  CB  . VAL B 1 4   ? 5.042   3.282   -48.817  1.00 85.37  ?  2   VAL B CB  1 
ATOM   4412 C  CG1 . VAL B 1 4   ? 6.272   3.453   -47.937  1.00 85.55  ?  2   VAL B CG1 1 
ATOM   4413 C  CG2 . VAL B 1 4   ? 5.152   2.021   -49.666  1.00 86.72  ?  2   VAL B CG2 1 
ATOM   4414 N  N   . GLY B 1 5   ? 4.179   4.427   -45.878  1.00 79.61  ?  3   GLY B N   1 
ATOM   4415 C  CA  . GLY B 1 5   ? 4.084   5.550   -44.965  1.00 79.50  ?  3   GLY B CA  1 
ATOM   4416 C  C   . GLY B 1 5   ? 4.853   5.289   -43.690  1.00 77.49  ?  3   GLY B C   1 
ATOM   4417 O  O   . GLY B 1 5   ? 5.789   4.489   -43.670  1.00 79.83  ?  3   GLY B O   1 
ATOM   4418 N  N   . ALA B 1 6   ? 4.443   5.964   -42.616  1.00 77.06  ?  4   ALA B N   1 
ATOM   4419 C  CA  . ALA B 1 6   ? 5.143   5.899   -41.340  1.00 76.57  ?  4   ALA B CA  1 
ATOM   4420 C  C   . ALA B 1 6   ? 4.265   5.271   -40.266  1.00 76.56  ?  4   ALA B C   1 
ATOM   4421 O  O   . ALA B 1 6   ? 3.057   5.523   -40.211  1.00 78.71  ?  4   ALA B O   1 
ATOM   4422 C  CB  . ALA B 1 6   ? 5.587   7.295   -40.888  1.00 83.45  ?  4   ALA B CB  1 
ATOM   4423 N  N   . CYS B 1 7   ? 4.887   4.470   -39.402  1.00 73.57  ?  5   CYS B N   1 
ATOM   4424 C  CA  . CYS B 1 7   ? 4.151   3.772   -38.357  1.00 74.37  ?  5   CYS B CA  1 
ATOM   4425 C  C   . CYS B 1 7   ? 3.711   4.771   -37.292  1.00 65.43  ?  5   CYS B C   1 
ATOM   4426 O  O   . CYS B 1 7   ? 4.485   5.635   -36.871  1.00 70.28  ?  5   CYS B O   1 
ATOM   4427 C  CB  . CYS B 1 7   ? 5.028   2.668   -37.754  1.00 74.99  ?  5   CYS B CB  1 
ATOM   4428 S  SG  . CYS B 1 7   ? 4.416   1.846   -36.258  1.00 64.89  ?  5   CYS B SG  1 
ATOM   4429 N  N   . VAL B 1 8   ? 2.456   4.645   -36.845  1.00 70.98  ?  6   VAL B N   1 
ATOM   4430 C  CA  . VAL B 1 8   ? 1.912   5.583   -35.863  1.00 72.63  ?  6   VAL B CA  1 
ATOM   4431 C  C   . VAL B 1 8   ? 2.416   5.348   -34.449  1.00 76.30  ?  6   VAL B C   1 
ATOM   4432 O  O   . VAL B 1 8   ? 2.044   6.104   -33.542  1.00 72.66  ?  6   VAL B O   1 
ATOM   4433 C  CB  . VAL B 1 8   ? 0.371   5.540   -35.858  1.00 67.23  ?  6   VAL B CB  1 
ATOM   4434 C  CG1 . VAL B 1 8   ? -0.170  5.797   -37.257  1.00 69.25  ?  6   VAL B CG1 1 
ATOM   4435 C  CG2 . VAL B 1 8   ? -0.116  4.200   -35.333  1.00 63.79  ?  6   VAL B CG2 1 
ATOM   4436 N  N   . LEU B 1 9   ? 3.269   4.349   -34.230  1.00 73.83  ?  7   LEU B N   1 
ATOM   4437 C  CA  . LEU B 1 9   ? 3.737   4.030   -32.887  1.00 71.01  ?  7   LEU B CA  1 
ATOM   4438 C  C   . LEU B 1 9   ? 5.221   4.285   -32.696  1.00 76.84  ?  7   LEU B C   1 
ATOM   4439 O  O   . LEU B 1 9   ? 5.651   4.560   -31.574  1.00 80.59  ?  7   LEU B O   1 
ATOM   4440 C  CB  . LEU B 1 9   ? 3.434   2.565   -32.553  1.00 65.81  ?  7   LEU B CB  1 
ATOM   4441 C  CG  . LEU B 1 9   ? 2.000   2.284   -32.097  1.00 65.42  ?  7   LEU B CG  1 
ATOM   4442 C  CD1 . LEU B 1 9   ? 1.811   0.808   -31.781  1.00 59.13  ?  7   LEU B CD1 1 
ATOM   4443 C  CD2 . LEU B 1 9   ? 1.645   3.144   -30.895  1.00 61.69  ?  7   LEU B CD2 1 
ATOM   4444 N  N   . CYS B 1 10  ? 6.004   4.208   -33.768  1.00 74.61  ?  8   CYS B N   1 
ATOM   4445 C  CA  . CYS B 1 10  ? 7.446   4.380   -33.701  1.00 74.46  ?  8   CYS B CA  1 
ATOM   4446 C  C   . CYS B 1 10  ? 7.960   5.208   -34.869  1.00 79.08  ?  8   CYS B C   1 
ATOM   4447 O  O   . CYS B 1 10  ? 9.163   5.479   -34.934  1.00 85.75  ?  8   CYS B O   1 
ATOM   4448 C  CB  . CYS B 1 10  ? 8.159   3.017   -33.645  1.00 72.36  ?  8   CYS B CB  1 
ATOM   4449 S  SG  . CYS B 1 10  ? 8.065   2.035   -35.146  1.00 84.15  ?  8   CYS B SG  1 
ATOM   4450 N  N   . ASN B 1 11  ? 7.083   5.605   -35.792  1.00 81.16  ?  9   ASN B N   1 
ATOM   4451 C  CA  . ASN B 1 11  ? 7.394   6.426   -36.957  1.00 82.36  ?  9   ASN B CA  1 
ATOM   4452 C  C   . ASN B 1 11  ? 8.210   5.678   -38.004  1.00 86.05  ?  9   ASN B C   1 
ATOM   4453 O  O   . ASN B 1 11  ? 8.360   6.162   -39.131  1.00 87.04  ?  9   ASN B O   1 
ATOM   4454 C  CB  . ASN B 1 11  ? 8.118   7.709   -36.557  1.00 90.63  ?  9   ASN B CB  1 
ATOM   4455 C  CG  . ASN B 1 11  ? 7.860   8.832   -37.539  1.00 95.54  ?  9   ASN B CG  1 
ATOM   4456 O  OD1 . ASN B 1 11  ? 6.715   9.096   -37.906  1.00 99.45  ?  9   ASN B OD1 1 
ATOM   4457 N  ND2 . ASN B 1 11  ? 8.916   9.468   -38.002  1.00 103.40 ?  9   ASN B ND2 1 
ATOM   4458 N  N   . SER B 1 12  ? 8.774   4.527   -37.640  1.00 84.36  ?  10  SER B N   1 
ATOM   4459 C  CA  . SER B 1 12  ? 9.511   3.725   -38.606  1.00 85.49  ?  10  SER B CA  1 
ATOM   4460 C  C   . SER B 1 12  ? 8.675   3.516   -39.863  1.00 78.71  ?  10  SER B C   1 
ATOM   4461 O  O   . SER B 1 12  ? 7.459   3.317   -39.796  1.00 81.49  ?  10  SER B O   1 
ATOM   4462 C  CB  . SER B 1 12  ? 9.900   2.376   -37.997  1.00 80.52  ?  10  SER B CB  1 
ATOM   4463 O  OG  . SER B 1 12  ? 10.500  2.545   -36.724  1.00 83.92  ?  10  SER B OG  1 
ATOM   4464 N  N   . GLN B 1 13  ? 9.339   3.563   -41.013  1.00 81.29  ?  11  GLN B N   1 
ATOM   4465 C  CA  . GLN B 1 13  ? 8.647   3.478   -42.291  1.00 80.14  ?  11  GLN B CA  1 
ATOM   4466 C  C   . GLN B 1 13  ? 8.051   2.086   -42.477  1.00 80.54  ?  11  GLN B C   1 
ATOM   4467 O  O   . GLN B 1 13  ? 8.539   1.098   -41.923  1.00 81.46  ?  11  GLN B O   1 
ATOM   4468 C  CB  . GLN B 1 13  ? 9.619   3.817   -43.423  1.00 87.24  ?  11  GLN B CB  1 
ATOM   4469 C  CG  . GLN B 1 13  ? 8.975   4.165   -44.750  1.00 89.22  ?  11  GLN B CG  1 
ATOM   4470 C  CD  . GLN B 1 13  ? 9.909   4.958   -45.648  1.00 99.78  ?  11  GLN B CD  1 
ATOM   4471 O  OE1 . GLN B 1 13  ? 11.054  5.237   -45.284  1.00 103.25 ?  11  GLN B OE1 1 
ATOM   4472 N  NE2 . GLN B 1 13  ? 9.423   5.331   -46.826  1.00 104.18 ?  11  GLN B NE2 1 
ATOM   4473 N  N   . THR B 1 14  ? 6.973   2.012   -43.257  1.00 83.16  ?  12  THR B N   1 
ATOM   4474 C  CA  . THR B 1 14  ? 6.270   0.747   -43.418  1.00 67.57  ?  12  THR B CA  1 
ATOM   4475 C  C   . THR B 1 14  ? 5.454   0.759   -44.701  1.00 71.29  ?  12  THR B C   1 
ATOM   4476 O  O   . THR B 1 14  ? 5.138   1.816   -45.254  1.00 77.49  ?  12  THR B O   1 
ATOM   4477 C  CB  . THR B 1 14  ? 5.351   0.462   -42.224  1.00 67.60  ?  12  THR B CB  1 
ATOM   4478 O  OG1 . THR B 1 14  ? 4.593   -0.728  -42.472  1.00 57.24  ?  12  THR B OG1 1 
ATOM   4479 C  CG2 . THR B 1 14  ? 4.390   1.622   -42.011  1.00 68.23  ?  12  THR B CG2 1 
ATOM   4480 N  N   . SER B 1 15  ? 5.120   -0.446  -45.164  1.00 64.97  ?  13  SER B N   1 
ATOM   4481 C  CA  . SER B 1 15  ? 4.233   -0.650  -46.303  1.00 69.45  ?  13  SER B CA  1 
ATOM   4482 C  C   . SER B 1 15  ? 2.957   -1.369  -45.885  1.00 63.89  ?  13  SER B C   1 
ATOM   4483 O  O   . SER B 1 15  ? 2.266   -1.947  -46.729  1.00 67.29  ?  13  SER B O   1 
ATOM   4484 C  CB  . SER B 1 15  ? 4.939   -1.435  -47.410  1.00 69.66  ?  13  SER B CB  1 
ATOM   4485 O  OG  . SER B 1 15  ? 5.163   -2.777  -47.012  1.00 71.55  ?  13  SER B OG  1 
ATOM   4486 N  N   . LEU B 1 16  ? 2.643   -1.357  -44.592  1.00 64.13  ?  14  LEU B N   1 
ATOM   4487 C  CA  . LEU B 1 16  ? 1.532   -2.113  -44.037  1.00 61.32  ?  14  LEU B CA  1 
ATOM   4488 C  C   . LEU B 1 16  ? 0.573   -1.191  -43.298  1.00 61.36  ?  14  LEU B C   1 
ATOM   4489 O  O   . LEU B 1 16  ? 0.992   -0.217  -42.664  1.00 60.85  ?  14  LEU B O   1 
ATOM   4490 C  CB  . LEU B 1 16  ? 2.033   -3.202  -43.083  1.00 58.88  ?  14  LEU B CB  1 
ATOM   4491 C  CG  . LEU B 1 16  ? 3.032   -4.205  -43.661  1.00 65.22  ?  14  LEU B CG  1 
ATOM   4492 C  CD1 . LEU B 1 16  ? 3.530   -5.145  -42.575  1.00 59.52  ?  14  LEU B CD1 1 
ATOM   4493 C  CD2 . LEU B 1 16  ? 2.415   -4.983  -44.812  1.00 67.13  ?  14  LEU B CD2 1 
ATOM   4494 N  N   . ARG B 1 17  ? -0.716  -1.502  -43.400  1.00 57.83  ?  15  ARG B N   1 
ATOM   4495 C  CA  . ARG B 1 17  ? -1.763  -0.819  -42.656  1.00 59.24  ?  15  ARG B CA  1 
ATOM   4496 C  C   . ARG B 1 17  ? -2.727  -1.868  -42.130  1.00 53.12  ?  15  ARG B C   1 
ATOM   4497 O  O   . ARG B 1 17  ? -2.876  -2.942  -42.718  1.00 50.93  ?  15  ARG B O   1 
ATOM   4498 C  CB  . ARG B 1 17  ? -2.539  0.192   -43.507  1.00 59.00  ?  15  ARG B CB  1 
ATOM   4499 C  CG  . ARG B 1 17  ? -1.733  1.354   -44.047  1.00 63.40  ?  15  ARG B CG  1 
ATOM   4500 C  CD  . ARG B 1 17  ? -2.480  1.955   -45.220  1.00 66.38  ?  15  ARG B CD  1 
ATOM   4501 N  NE  . ARG B 1 17  ? -2.763  0.933   -46.219  1.00 71.13  ?  15  ARG B NE  1 
ATOM   4502 C  CZ  . ARG B 1 17  ? -3.534  1.108   -47.283  1.00 68.97  ?  15  ARG B CZ  1 
ATOM   4503 N  NH1 . ARG B 1 17  ? -4.296  2.181   -47.416  1.00 71.87  ?  15  ARG B NH1 1 
ATOM   4504 N  NH2 . ARG B 1 17  ? -3.597  0.148   -48.202  1.00 78.70  ?  15  ARG B NH2 1 
ATOM   4505 N  N   . CYS B 1 18  ? -3.379  -1.554  -41.015  1.00 57.68  ?  16  CYS B N   1 
ATOM   4506 C  CA  . CYS B 1 18  ? -4.378  -2.450  -40.445  1.00 48.90  ?  16  CYS B CA  1 
ATOM   4507 C  C   . CYS B 1 18  ? -5.687  -2.255  -41.198  1.00 52.14  ?  16  CYS B C   1 
ATOM   4508 O  O   . CYS B 1 18  ? -6.297  -1.183  -41.129  1.00 56.26  ?  16  CYS B O   1 
ATOM   4509 C  CB  . CYS B 1 18  ? -4.558  -2.183  -38.954  1.00 52.56  ?  16  CYS B CB  1 
ATOM   4510 S  SG  . CYS B 1 18  ? -5.676  -3.342  -38.123  1.00 51.65  ?  16  CYS B SG  1 
ATOM   4511 N  N   . GLY B 1 19  ? -6.115  -3.284  -41.929  1.00 53.32  ?  17  GLY B N   1 
ATOM   4512 C  CA  . GLY B 1 19  ? -7.382  -3.208  -42.632  1.00 56.18  ?  17  GLY B CA  1 
ATOM   4513 C  C   . GLY B 1 19  ? -8.597  -3.280  -41.734  1.00 55.36  ?  17  GLY B C   1 
ATOM   4514 O  O   . GLY B 1 19  ? -9.716  -3.071  -42.216  1.00 65.81  ?  17  GLY B O   1 
ATOM   4515 N  N   . ALA B 1 20  ? -8.401  -3.550  -40.444  1.00 50.14  ?  18  ALA B N   1 
ATOM   4516 C  CA  . ALA B 1 20  ? -9.495  -3.698  -39.494  1.00 58.05  ?  18  ALA B CA  1 
ATOM   4517 C  C   . ALA B 1 20  ? -9.726  -2.441  -38.672  1.00 57.65  ?  18  ALA B C   1 
ATOM   4518 O  O   . ALA B 1 20  ? -10.843 -2.221  -38.193  1.00 57.49  ?  18  ALA B O   1 
ATOM   4519 C  CB  . ALA B 1 20  ? -9.232  -4.880  -38.555  1.00 52.70  ?  18  ALA B CB  1 
ATOM   4520 N  N   . CYS B 1 21  ? -8.693  -1.620  -38.500  1.00 59.07  ?  19  CYS B N   1 
ATOM   4521 C  CA  . CYS B 1 21  ? -8.854  -0.330  -37.846  1.00 51.44  ?  19  CYS B CA  1 
ATOM   4522 C  C   . CYS B 1 21  ? -9.577  0.615   -38.794  1.00 55.18  ?  19  CYS B C   1 
ATOM   4523 O  O   . CYS B 1 21  ? -9.344  0.598   -40.006  1.00 57.60  ?  19  CYS B O   1 
ATOM   4524 C  CB  . CYS B 1 21  ? -7.488  0.251   -37.472  1.00 53.92  ?  19  CYS B CB  1 
ATOM   4525 S  SG  . CYS B 1 21  ? -6.780  -0.328  -35.910  1.00 52.32  ?  19  CYS B SG  1 
ATOM   4526 N  N   . ILE B 1 22  ? -10.463 1.449   -38.245  1.00 52.72  ?  20  ILE B N   1 
ATOM   4527 C  CA  . ILE B 1 22  ? -11.269 2.288   -39.125  1.00 52.30  ?  20  ILE B CA  1 
ATOM   4528 C  C   . ILE B 1 22  ? -10.408 3.344   -39.803  1.00 54.59  ?  20  ILE B C   1 
ATOM   4529 O  O   . ILE B 1 22  ? -10.748 3.825   -40.892  1.00 58.23  ?  20  ILE B O   1 
ATOM   4530 C  CB  . ILE B 1 22  ? -12.437 2.929   -38.354  1.00 64.47  ?  20  ILE B CB  1 
ATOM   4531 C  CG1 . ILE B 1 22  ? -11.916 3.843   -37.246  1.00 55.83  ?  20  ILE B CG1 1 
ATOM   4532 C  CG2 . ILE B 1 22  ? -13.344 1.853   -37.772  1.00 65.50  ?  20  ILE B CG2 1 
ATOM   4533 C  CD1 . ILE B 1 22  ? -13.017 4.561   -36.497  1.00 61.40  ?  20  ILE B CD1 1 
ATOM   4534 N  N   . ARG B 1 23  ? -9.293  3.730   -39.187  1.00 53.39  ?  21  ARG B N   1 
ATOM   4535 C  CA  . ARG B 1 23  ? -8.434  4.768   -39.737  1.00 59.72  ?  21  ARG B CA  1 
ATOM   4536 C  C   . ARG B 1 23  ? -7.273  4.207   -40.550  1.00 54.91  ?  21  ARG B C   1 
ATOM   4537 O  O   . ARG B 1 23  ? -6.434  4.981   -41.021  1.00 57.86  ?  21  ARG B O   1 
ATOM   4538 C  CB  . ARG B 1 23  ? -7.904  5.661   -38.609  1.00 57.76  ?  21  ARG B CB  1 
ATOM   4539 C  CG  . ARG B 1 23  ? -8.998  6.410   -37.864  1.00 60.68  ?  21  ARG B CG  1 
ATOM   4540 C  CD  . ARG B 1 23  ? -9.909  7.145   -38.830  1.00 65.56  ?  21  ARG B CD  1 
ATOM   4541 N  NE  . ARG B 1 23  ? -9.182  8.134   -39.615  1.00 69.86  ?  21  ARG B NE  1 
ATOM   4542 C  CZ  . ARG B 1 23  ? -9.697  8.812   -40.629  1.00 75.01  ?  21  ARG B CZ  1 
ATOM   4543 N  NH1 . ARG B 1 23  ? -10.836 8.449   -41.194  1.00 75.94  ?  21  ARG B NH1 1 
ATOM   4544 N  NH2 . ARG B 1 23  ? -9.013  9.832   -41.141  1.00 79.97  ?  21  ARG B NH2 1 
ATOM   4545 N  N   . ARG B 1 24  ? -7.220  2.890   -40.742  1.00 55.75  ?  22  ARG B N   1 
ATOM   4546 C  CA  . ARG B 1 24  ? -6.167  2.193   -41.480  1.00 62.01  ?  22  ARG B CA  1 
ATOM   4547 C  C   . ARG B 1 24  ? -4.774  2.747   -41.148  1.00 58.67  ?  22  ARG B C   1 
ATOM   4548 O  O   . ARG B 1 24  ? -4.044  3.178   -42.047  1.00 53.44  ?  22  ARG B O   1 
ATOM   4549 C  CB  . ARG B 1 24  ? -6.434  2.244   -42.980  1.00 61.65  ?  22  ARG B CB  1 
ATOM   4550 C  CG  . ARG B 1 24  ? -7.671  1.465   -43.407  1.00 60.52  ?  22  ARG B CG  1 
ATOM   4551 C  CD  . ARG B 1 24  ? -7.902  1.568   -44.906  1.00 74.12  ?  22  ARG B CD  1 
ATOM   4552 N  NE  . ARG B 1 24  ? -9.097  0.848   -45.329  1.00 80.89  ?  22  ARG B NE  1 
ATOM   4553 C  CZ  . ARG B 1 24  ? -9.503  0.747   -46.588  1.00 84.85  ?  22  ARG B CZ  1 
ATOM   4554 N  NH1 . ARG B 1 24  ? -8.782  1.229   -47.587  1.00 83.77  ?  22  ARG B NH1 1 
ATOM   4555 N  NH2 . ARG B 1 24  ? -10.649 0.124   -46.852  1.00 85.92  ?  22  ARG B NH2 1 
ATOM   4556 N  N   . PRO B 1 25  ? -4.388  2.757   -39.874  1.00 52.98  ?  23  PRO B N   1 
ATOM   4557 C  CA  . PRO B 1 25  ? -3.076  3.297   -39.495  1.00 52.11  ?  23  PRO B CA  1 
ATOM   4558 C  C   . PRO B 1 25  ? -1.923  2.490   -40.077  1.00 58.25  ?  23  PRO B C   1 
ATOM   4559 O  O   . PRO B 1 25  ? -1.962  1.258   -40.117  1.00 59.24  ?  23  PRO B O   1 
ATOM   4560 C  CB  . PRO B 1 25  ? -3.090  3.210   -37.964  1.00 54.25  ?  23  PRO B CB  1 
ATOM   4561 C  CG  . PRO B 1 25  ? -4.043  2.087   -37.677  1.00 44.79  ?  23  PRO B CG  1 
ATOM   4562 C  CD  . PRO B 1 25  ? -5.128  2.260   -38.702  1.00 53.77  ?  23  PRO B CD  1 
ATOM   4563 N  N   . PHE B 1 26  ? -0.884  3.195   -40.525  1.00 60.44  ?  24  PHE B N   1 
ATOM   4564 C  CA  . PHE B 1 26  ? 0.323   2.507   -40.964  1.00 61.99  ?  24  PHE B CA  1 
ATOM   4565 C  C   . PHE B 1 26  ? 0.999   1.873   -39.754  1.00 61.24  ?  24  PHE B C   1 
ATOM   4566 O  O   . PHE B 1 26  ? 1.062   2.470   -38.676  1.00 65.90  ?  24  PHE B O   1 
ATOM   4567 C  CB  . PHE B 1 26  ? 1.309   3.472   -41.631  1.00 58.84  ?  24  PHE B CB  1 
ATOM   4568 C  CG  . PHE B 1 26  ? 0.946   3.877   -43.036  1.00 64.13  ?  24  PHE B CG  1 
ATOM   4569 C  CD1 . PHE B 1 26  ? 1.292   3.076   -44.113  1.00 72.16  ?  24  PHE B CD1 1 
ATOM   4570 C  CD2 . PHE B 1 26  ? 0.332   5.093   -43.287  1.00 72.19  ?  24  PHE B CD2 1 
ATOM   4571 C  CE1 . PHE B 1 26  ? 0.985   3.455   -45.409  1.00 74.95  ?  24  PHE B CE1 1 
ATOM   4572 C  CE2 . PHE B 1 26  ? 0.027   5.481   -44.583  1.00 72.90  ?  24  PHE B CE2 1 
ATOM   4573 C  CZ  . PHE B 1 26  ? 0.354   4.660   -45.644  1.00 70.36  ?  24  PHE B CZ  1 
ATOM   4574 N  N   . LEU B 1 27  ? 1.504   0.654   -39.932  1.00 48.51  ?  25  LEU B N   1 
ATOM   4575 C  CA  . LEU B 1 27  ? 2.177   -0.071  -38.861  1.00 60.08  ?  25  LEU B CA  1 
ATOM   4576 C  C   . LEU B 1 27  ? 3.353   -0.833  -39.454  1.00 53.98  ?  25  LEU B C   1 
ATOM   4577 O  O   . LEU B 1 27  ? 3.191   -1.524  -40.464  1.00 54.14  ?  25  LEU B O   1 
ATOM   4578 C  CB  . LEU B 1 27  ? 1.214   -1.040  -38.159  1.00 49.72  ?  25  LEU B CB  1 
ATOM   4579 C  CG  . LEU B 1 27  ? 0.136   -0.484  -37.222  1.00 53.54  ?  25  LEU B CG  1 
ATOM   4580 C  CD1 . LEU B 1 27  ? -0.827  -1.591  -36.820  1.00 48.39  ?  25  LEU B CD1 1 
ATOM   4581 C  CD2 . LEU B 1 27  ? 0.739   0.167   -35.987  1.00 54.61  ?  25  LEU B CD2 1 
ATOM   4582 N  N   . CYS B 1 28  ? 4.530   -0.705  -38.843  1.00 54.35  ?  26  CYS B N   1 
ATOM   4583 C  CA  . CYS B 1 28  ? 5.680   -1.453  -39.329  1.00 61.67  ?  26  CYS B CA  1 
ATOM   4584 C  C   . CYS B 1 28  ? 5.545   -2.929  -38.968  1.00 61.17  ?  26  CYS B C   1 
ATOM   4585 O  O   . CYS B 1 28  ? 4.650   -3.344  -38.224  1.00 55.75  ?  26  CYS B O   1 
ATOM   4586 C  CB  . CYS B 1 28  ? 6.989   -0.934  -38.741  1.00 66.76  ?  26  CYS B CB  1 
ATOM   4587 S  SG  . CYS B 1 28  ? 7.015   -0.899  -36.958  1.00 66.00  ?  26  CYS B SG  1 
ATOM   4588 N  N   . CYS B 1 29  ? 6.449   -3.730  -39.533  1.00 61.07  ?  27  CYS B N   1 
ATOM   4589 C  CA  . CYS B 1 29  ? 6.404   -5.173  -39.329  1.00 61.06  ?  27  CYS B CA  1 
ATOM   4590 C  C   . CYS B 1 29  ? 6.313   -5.525  -37.848  1.00 58.46  ?  27  CYS B C   1 
ATOM   4591 O  O   . CYS B 1 29  ? 5.573   -6.437  -37.462  1.00 59.04  ?  27  CYS B O   1 
ATOM   4592 C  CB  . CYS B 1 29  ? 7.642   -5.818  -39.953  1.00 69.31  ?  27  CYS B CB  1 
ATOM   4593 S  SG  . CYS B 1 29  ? 7.991   -5.275  -41.646  1.00 73.09  ?  27  CYS B SG  1 
ATOM   4594 N  N   . LYS B 1 30  ? 7.050   -4.802  -36.999  1.00 58.14  ?  28  LYS B N   1 
ATOM   4595 C  CA  . LYS B 1 30  ? 7.090   -5.143  -35.579  1.00 61.71  ?  28  LYS B CA  1 
ATOM   4596 C  C   . LYS B 1 30  ? 5.793   -4.758  -34.879  1.00 62.41  ?  28  LYS B C   1 
ATOM   4597 O  O   . LYS B 1 30  ? 5.190   -5.575  -34.173  1.00 58.06  ?  28  LYS B O   1 
ATOM   4598 C  CB  . LYS B 1 30  ? 8.285   -4.463  -34.910  1.00 60.77  ?  28  LYS B CB  1 
ATOM   4599 N  N   . CYS B 1 31  ? 5.331   -3.521  -35.079  1.00 56.87  ?  29  CYS B N   1 
ATOM   4600 C  CA  . CYS B 1 31  ? 4.131   -3.081  -34.378  1.00 52.83  ?  29  CYS B CA  1 
ATOM   4601 C  C   . CYS B 1 31  ? 2.889   -3.718  -34.984  1.00 52.80  ?  29  CYS B C   1 
ATOM   4602 O  O   . CYS B 1 31  ? 1.930   -4.020  -34.263  1.00 50.76  ?  29  CYS B O   1 
ATOM   4603 C  CB  . CYS B 1 31  ? 4.027   -1.552  -34.403  1.00 53.82  ?  29  CYS B CB  1 
ATOM   4604 S  SG  . CYS B 1 31  ? 5.418   -0.652  -33.630  1.00 61.81  ?  29  CYS B SG  1 
ATOM   4605 N  N   . CYS B 1 32  ? 2.898   -3.958  -36.296  1.00 51.02  ?  30  CYS B N   1 
ATOM   4606 C  CA  . CYS B 1 32  ? 1.763   -4.618  -36.927  1.00 51.25  ?  30  CYS B CA  1 
ATOM   4607 C  C   . CYS B 1 32  ? 1.593   -6.031  -36.382  1.00 51.19  ?  30  CYS B C   1 
ATOM   4608 O  O   . CYS B 1 32  ? 0.467   -6.483  -36.143  1.00 42.46  ?  30  CYS B O   1 
ATOM   4609 C  CB  . CYS B 1 32  ? 1.951   -4.630  -38.444  1.00 52.31  ?  30  CYS B CB  1 
ATOM   4610 S  SG  . CYS B 1 32  ? 0.584   -5.340  -39.375  1.00 53.90  ?  30  CYS B SG  1 
ATOM   4611 N  N   . TYR B 1 33  ? 2.706   -6.739  -36.163  1.00 52.15  ?  31  TYR B N   1 
ATOM   4612 C  CA  . TYR B 1 33  ? 2.639   -8.071  -35.571  1.00 58.67  ?  31  TYR B CA  1 
ATOM   4613 C  C   . TYR B 1 33  ? 2.070   -8.009  -34.159  1.00 55.73  ?  31  TYR B C   1 
ATOM   4614 O  O   . TYR B 1 33  ? 1.159   -8.769  -33.809  1.00 54.96  ?  31  TYR B O   1 
ATOM   4615 C  CB  . TYR B 1 33  ? 4.027   -8.718  -35.564  1.00 57.03  ?  31  TYR B CB  1 
ATOM   4616 C  CG  . TYR B 1 33  ? 4.090   -10.040 -34.826  1.00 56.03  ?  31  TYR B CG  1 
ATOM   4617 C  CD1 . TYR B 1 33  ? 4.313   -10.085 -33.454  1.00 59.93  ?  31  TYR B CD1 1 
ATOM   4618 C  CD2 . TYR B 1 33  ? 3.931   -11.242 -35.501  1.00 62.53  ?  31  TYR B CD2 1 
ATOM   4619 C  CE1 . TYR B 1 33  ? 4.368   -11.289 -32.776  1.00 59.93  ?  31  TYR B CE1 1 
ATOM   4620 C  CE2 . TYR B 1 33  ? 3.989   -12.452 -34.832  1.00 60.55  ?  31  TYR B CE2 1 
ATOM   4621 C  CZ  . TYR B 1 33  ? 4.207   -12.470 -33.471  1.00 60.04  ?  31  TYR B CZ  1 
ATOM   4622 O  OH  . TYR B 1 33  ? 4.267   -13.672 -32.804  1.00 62.71  ?  31  TYR B OH  1 
ATOM   4623 N  N   . ASP B 1 34  ? 2.602   -7.109  -33.327  1.00 52.55  ?  32  ASP B N   1 
ATOM   4624 C  CA  . ASP B 1 34  ? 2.143   -7.028  -31.945  1.00 56.95  ?  32  ASP B CA  1 
ATOM   4625 C  C   . ASP B 1 34  ? 0.670   -6.645  -31.872  1.00 53.99  ?  32  ASP B C   1 
ATOM   4626 O  O   . ASP B 1 34  ? -0.014  -6.994  -30.904  1.00 56.45  ?  32  ASP B O   1 
ATOM   4627 C  CB  . ASP B 1 34  ? 2.994   -6.029  -31.160  1.00 58.95  ?  32  ASP B CB  1 
ATOM   4628 C  CG  . ASP B 1 34  ? 4.434   -6.481  -31.008  1.00 69.04  ?  32  ASP B CG  1 
ATOM   4629 O  OD1 . ASP B 1 34  ? 4.657   -7.609  -30.518  1.00 72.19  ?  32  ASP B OD1 1 
ATOM   4630 O  OD2 . ASP B 1 34  ? 5.345   -5.706  -31.369  1.00 75.41  -1 32  ASP B OD2 1 
ATOM   4631 N  N   . HIS B 1 35  ? 0.169   -5.926  -32.880  1.00 46.75  ?  33  HIS B N   1 
ATOM   4632 C  CA  . HIS B 1 35  ? -1.244  -5.563  -32.912  1.00 53.61  ?  33  HIS B CA  1 
ATOM   4633 C  C   . HIS B 1 35  ? -2.116  -6.763  -33.273  1.00 51.76  ?  33  HIS B C   1 
ATOM   4634 O  O   . HIS B 1 35  ? -3.088  -7.069  -32.571  1.00 49.39  ?  33  HIS B O   1 
ATOM   4635 C  CB  . HIS B 1 35  ? -1.457  -4.415  -33.905  1.00 52.65  ?  33  HIS B CB  1 
ATOM   4636 C  CG  . HIS B 1 35  ? -2.877  -3.943  -34.008  1.00 51.93  ?  33  HIS B CG  1 
ATOM   4637 N  ND1 . HIS B 1 35  ? -3.710  -3.828  -32.915  1.00 50.69  ?  33  HIS B ND1 1 
ATOM   4638 C  CD2 . HIS B 1 35  ? -3.607  -3.548  -35.078  1.00 52.75  ?  33  HIS B CD2 1 
ATOM   4639 C  CE1 . HIS B 1 35  ? -4.892  -3.386  -33.309  1.00 48.48  ?  33  HIS B CE1 1 
ATOM   4640 N  NE2 . HIS B 1 35  ? -4.857  -3.209  -34.617  1.00 47.09  ?  33  HIS B NE2 1 
ATOM   4641 N  N   . VAL B 1 36  ? -1.781  -7.461  -34.363  1.00 52.43  ?  34  VAL B N   1 
ATOM   4642 C  CA  . VAL B 1 36  ? -2.622  -8.559  -34.838  1.00 50.95  ?  34  VAL B CA  1 
ATOM   4643 C  C   . VAL B 1 36  ? -2.631  -9.740  -33.870  1.00 49.51  ?  34  VAL B C   1 
ATOM   4644 O  O   . VAL B 1 36  ? -3.644  -10.440 -33.760  1.00 48.52  ?  34  VAL B O   1 
ATOM   4645 C  CB  . VAL B 1 36  ? -2.194  -9.006  -36.250  1.00 51.04  ?  34  VAL B CB  1 
ATOM   4646 C  CG1 . VAL B 1 36  ? -2.322  -7.852  -37.237  1.00 46.49  ?  34  VAL B CG1 1 
ATOM   4647 C  CG2 . VAL B 1 36  ? -0.782  -9.570  -36.238  1.00 55.24  ?  34  VAL B CG2 1 
ATOM   4648 N  N   . ILE B 1 37  ? -1.527  -9.991  -33.155  1.00 55.05  ?  35  ILE B N   1 
ATOM   4649 C  CA  . ILE B 1 37  ? -1.444  -11.185 -32.315  1.00 55.50  ?  35  ILE B CA  1 
ATOM   4650 C  C   . ILE B 1 37  ? -2.036  -10.972 -30.930  1.00 55.78  ?  35  ILE B C   1 
ATOM   4651 O  O   . ILE B 1 37  ? -2.074  -11.918 -30.131  1.00 55.66  ?  35  ILE B O   1 
ATOM   4652 C  CB  . ILE B 1 37  ? 0.010   -11.689 -32.171  1.00 64.89  ?  35  ILE B CB  1 
ATOM   4653 C  CG1 . ILE B 1 37  ? 0.852   -10.713 -31.343  1.00 64.56  ?  35  ILE B CG1 1 
ATOM   4654 C  CG2 . ILE B 1 37  ? 0.634   -11.931 -33.539  1.00 59.05  ?  35  ILE B CG2 1 
ATOM   4655 C  CD1 . ILE B 1 37  ? 0.968   -11.090 -29.878  1.00 60.90  ?  35  ILE B CD1 1 
ATOM   4656 N  N   . SER B 1 38  ? -2.494  -9.763  -30.615  1.00 57.01  ?  36  SER B N   1 
ATOM   4657 C  CA  . SER B 1 38  ? -3.019  -9.450  -29.296  1.00 58.17  ?  36  SER B CA  1 
ATOM   4658 C  C   . SER B 1 38  ? -4.448  -8.931  -29.348  1.00 58.97  ?  36  SER B C   1 
ATOM   4659 O  O   . SER B 1 38  ? -5.021  -8.628  -28.295  1.00 65.45  ?  36  SER B O   1 
ATOM   4660 C  CB  . SER B 1 38  ? -2.122  -8.425  -28.592  1.00 62.77  ?  36  SER B CB  1 
ATOM   4661 O  OG  . SER B 1 38  ? -1.977  -7.259  -29.381  1.00 63.80  ?  36  SER B OG  1 
ATOM   4662 N  N   . THR B 1 39  ? -5.035  -8.819  -30.538  1.00 53.75  ?  37  THR B N   1 
ATOM   4663 C  CA  . THR B 1 39  ? -6.383  -8.296  -30.723  1.00 57.63  ?  37  THR B CA  1 
ATOM   4664 C  C   . THR B 1 39  ? -7.085  -9.162  -31.762  1.00 54.04  ?  37  THR B C   1 
ATOM   4665 O  O   . THR B 1 39  ? -6.546  -10.171 -32.228  1.00 48.91  ?  37  THR B O   1 
ATOM   4666 C  CB  . THR B 1 39  ? -6.378  -6.827  -31.170  1.00 54.13  ?  37  THR B CB  1 
ATOM   4667 O  OG1 . THR B 1 39  ? -5.885  -6.738  -32.513  1.00 54.10  ?  37  THR B OG1 1 
ATOM   4668 C  CG2 . THR B 1 39  ? -5.511  -5.980  -30.259  1.00 56.73  ?  37  THR B CG2 1 
ATOM   4669 N  N   . SER B 1 40  ? -8.290  -8.743  -32.140  1.00 53.79  ?  38  SER B N   1 
ATOM   4670 C  CA  . SER B 1 40  ? -9.072  -9.409  -33.170  1.00 51.84  ?  38  SER B CA  1 
ATOM   4671 C  C   . SER B 1 40  ? -8.753  -8.893  -34.567  1.00 50.31  ?  38  SER B C   1 
ATOM   4672 O  O   . SER B 1 40  ? -9.259  -9.447  -35.548  1.00 51.20  ?  38  SER B O   1 
ATOM   4673 C  CB  . SER B 1 40  ? -10.569 -9.238  -32.893  1.00 55.36  ?  38  SER B CB  1 
ATOM   4674 O  OG  . SER B 1 40  ? -10.915 -7.867  -32.799  1.00 57.50  ?  38  SER B OG  1 
ATOM   4675 N  N   . HIS B 1 41  ? -7.943  -7.844  -34.677  1.00 50.31  ?  39  HIS B N   1 
ATOM   4676 C  CA  . HIS B 1 41  ? -7.604  -7.250  -35.965  1.00 51.45  ?  39  HIS B CA  1 
ATOM   4677 C  C   . HIS B 1 41  ? -6.588  -8.142  -36.666  1.00 52.27  ?  39  HIS B C   1 
ATOM   4678 O  O   . HIS B 1 41  ? -5.454  -8.290  -36.199  1.00 50.01  ?  39  HIS B O   1 
ATOM   4679 C  CB  . HIS B 1 41  ? -7.051  -5.841  -35.773  1.00 52.64  ?  39  HIS B CB  1 
ATOM   4680 C  CG  . HIS B 1 41  ? -8.068  -4.849  -35.304  1.00 51.26  ?  39  HIS B CG  1 
ATOM   4681 N  ND1 . HIS B 1 41  ? -7.950  -3.497  -35.541  1.00 50.76  ?  39  HIS B ND1 1 
ATOM   4682 C  CD2 . HIS B 1 41  ? -9.220  -5.009  -34.611  1.00 56.12  ?  39  HIS B CD2 1 
ATOM   4683 C  CE1 . HIS B 1 41  ? -8.986  -2.867  -35.016  1.00 54.45  ?  39  HIS B CE1 1 
ATOM   4684 N  NE2 . HIS B 1 41  ? -9.772  -3.762  -34.445  1.00 55.52  ?  39  HIS B NE2 1 
ATOM   4685 N  N   . LYS B 1 42  ? -6.990  -8.742  -37.787  1.00 49.53  ?  40  LYS B N   1 
ATOM   4686 C  CA  . LYS B 1 42  ? -6.117  -9.645  -38.519  1.00 55.06  ?  40  LYS B CA  1 
ATOM   4687 C  C   . LYS B 1 42  ? -5.966  -9.279  -39.986  1.00 52.96  ?  40  LYS B C   1 
ATOM   4688 O  O   . LYS B 1 42  ? -5.135  -9.889  -40.669  1.00 56.32  ?  40  LYS B O   1 
ATOM   4689 C  CB  . LYS B 1 42  ? -6.639  -11.088 -38.437  1.00 56.61  ?  40  LYS B CB  1 
ATOM   4690 C  CG  . LYS B 1 42  ? -6.994  -11.558 -37.039  1.00 52.22  ?  40  LYS B CG  1 
ATOM   4691 C  CD  . LYS B 1 42  ? -5.793  -11.640 -36.123  1.00 51.84  ?  40  LYS B CD  1 
ATOM   4692 C  CE  . LYS B 1 42  ? -6.217  -12.160 -34.760  1.00 51.06  ?  40  LYS B CE  1 
ATOM   4693 N  NZ  . LYS B 1 42  ? -5.087  -12.211 -33.798  1.00 54.81  ?  40  LYS B NZ  1 
ATOM   4694 N  N   . LEU B 1 43  ? -6.730  -8.315  -40.490  1.00 54.08  ?  41  LEU B N   1 
ATOM   4695 C  CA  . LEU B 1 43  ? -6.629  -7.897  -41.882  1.00 55.96  ?  41  LEU B CA  1 
ATOM   4696 C  C   . LEU B 1 43  ? -5.507  -6.876  -42.031  1.00 53.47  ?  41  LEU B C   1 
ATOM   4697 O  O   . LEU B 1 43  ? -5.584  -5.776  -41.473  1.00 57.14  ?  41  LEU B O   1 
ATOM   4698 C  CB  . LEU B 1 43  ? -7.953  -7.315  -42.367  1.00 58.52  ?  41  LEU B CB  1 
ATOM   4699 C  CG  . LEU B 1 43  ? -7.933  -6.798  -43.806  1.00 62.67  ?  41  LEU B CG  1 
ATOM   4700 C  CD1 . LEU B 1 43  ? -7.563  -7.916  -44.770  1.00 63.14  ?  41  LEU B CD1 1 
ATOM   4701 C  CD2 . LEU B 1 43  ? -9.270  -6.180  -44.178  1.00 65.35  ?  41  LEU B CD2 1 
ATOM   4702 N  N   . VAL B 1 44  ? -4.474  -7.231  -42.787  1.00 53.49  ?  42  VAL B N   1 
ATOM   4703 C  CA  . VAL B 1 44  ? -3.324  -6.364  -43.012  1.00 61.20  ?  42  VAL B CA  1 
ATOM   4704 C  C   . VAL B 1 44  ? -3.332  -5.940  -44.473  1.00 59.70  ?  42  VAL B C   1 
ATOM   4705 O  O   . VAL B 1 44  ? -3.523  -6.773  -45.367  1.00 65.34  ?  42  VAL B O   1 
ATOM   4706 C  CB  . VAL B 1 44  ? -2.008  -7.070  -42.642  1.00 58.88  ?  42  VAL B CB  1 
ATOM   4707 C  CG1 . VAL B 1 44  ? -0.815  -6.184  -42.967  1.00 57.24  ?  42  VAL B CG1 1 
ATOM   4708 C  CG2 . VAL B 1 44  ? -2.014  -7.458  -41.169  1.00 53.45  ?  42  VAL B CG2 1 
ATOM   4709 N  N   . LEU B 1 45  ? -3.126  -4.648  -44.715  1.00 56.05  ?  43  LEU B N   1 
ATOM   4710 C  CA  . LEU B 1 45  ? -3.199  -4.081  -46.053  1.00 58.24  ?  43  LEU B CA  1 
ATOM   4711 C  C   . LEU B 1 45  ? -1.828  -3.586  -46.490  1.00 65.15  ?  43  LEU B C   1 
ATOM   4712 O  O   . LEU B 1 45  ? -1.111  -2.942  -45.718  1.00 59.77  ?  43  LEU B O   1 
ATOM   4713 C  CB  . LEU B 1 45  ? -4.206  -2.927  -46.119  1.00 60.74  ?  43  LEU B CB  1 
ATOM   4714 C  CG  . LEU B 1 45  ? -5.683  -3.254  -45.884  1.00 64.63  ?  43  LEU B CG  1 
ATOM   4715 C  CD1 . LEU B 1 45  ? -6.557  -2.039  -46.179  1.00 71.22  ?  43  LEU B CD1 1 
ATOM   4716 C  CD2 . LEU B 1 45  ? -6.120  -4.452  -46.714  1.00 65.62  ?  43  LEU B CD2 1 
ATOM   4717 N  N   . SER B 1 46  ? -1.481  -3.890  -47.735  1.00 71.91  ?  44  SER B N   1 
ATOM   4718 C  CA  . SER B 1 46  ? -0.251  -3.414  -48.355  1.00 74.51  ?  44  SER B CA  1 
ATOM   4719 C  C   . SER B 1 46  ? -0.640  -2.863  -49.724  1.00 81.57  ?  44  SER B C   1 
ATOM   4720 O  O   . SER B 1 46  ? -1.804  -2.521  -49.976  1.00 82.25  ?  44  SER B O   1 
ATOM   4721 C  CB  . SER B 1 46  ? 0.790   -4.539  -48.424  1.00 73.56  ?  44  SER B CB  1 
ATOM   4722 O  OG  . SER B 1 46  ? 2.089   -4.026  -48.657  1.00 76.73  ?  44  SER B OG  1 
ATOM   4723 N  N   . VAL B 1 47  ? 0.344   -2.739  -50.618  1.00 78.99  ?  45  VAL B N   1 
ATOM   4724 C  CA  . VAL B 1 47  ? 0.099   -2.349  -52.004  1.00 81.10  ?  45  VAL B CA  1 
ATOM   4725 C  C   . VAL B 1 47  ? -1.131  -3.099  -52.496  1.00 81.08  ?  45  VAL B C   1 
ATOM   4726 O  O   . VAL B 1 47  ? -1.958  -2.557  -53.238  1.00 86.03  ?  45  VAL B O   1 
ATOM   4727 C  CB  . VAL B 1 47  ? 1.319   -2.636  -52.896  1.00 83.41  ?  45  VAL B CB  1 
ATOM   4728 C  CG1 . VAL B 1 47  ? 1.001   -2.321  -54.350  1.00 83.31  ?  45  VAL B CG1 1 
ATOM   4729 C  CG2 . VAL B 1 47  ? 2.523   -1.842  -52.418  1.00 81.76  ?  45  VAL B CG2 1 
ATOM   4730 N  N   . ASN B 1 48  ? -1.250  -4.351  -52.073  1.00 84.70  ?  46  ASN B N   1 
ATOM   4731 C  CA  . ASN B 1 48  ? -2.416  -5.192  -52.261  1.00 86.91  ?  46  ASN B CA  1 
ATOM   4732 C  C   . ASN B 1 48  ? -2.832  -5.714  -50.896  1.00 82.54  ?  46  ASN B C   1 
ATOM   4733 O  O   . ASN B 1 48  ? -1.992  -5.846  -50.000  1.00 78.74  ?  46  ASN B O   1 
ATOM   4734 C  CB  . ASN B 1 48  ? -2.115  -6.371  -53.198  1.00 84.98  ?  46  ASN B CB  1 
ATOM   4735 C  CG  . ASN B 1 48  ? -1.566  -5.924  -54.540  1.00 93.38  ?  46  ASN B CG  1 
ATOM   4736 O  OD1 . ASN B 1 48  ? -2.201  -5.155  -55.261  1.00 93.98  ?  46  ASN B OD1 1 
ATOM   4737 N  ND2 . ASN B 1 48  ? -0.375  -6.406  -54.881  1.00 94.10  ?  46  ASN B ND2 1 
ATOM   4738 N  N   . PRO B 1 49  ? -4.114  -6.011  -50.700  1.00 82.87  ?  47  PRO B N   1 
ATOM   4739 C  CA  . PRO B 1 49  ? -4.524  -6.621  -49.432  1.00 77.81  ?  47  PRO B CA  1 
ATOM   4740 C  C   . PRO B 1 49  ? -3.942  -8.017  -49.296  1.00 80.35  ?  47  PRO B C   1 
ATOM   4741 O  O   . PRO B 1 49  ? -3.856  -8.772  -50.267  1.00 78.40  ?  47  PRO B O   1 
ATOM   4742 C  CB  . PRO B 1 49  ? -6.053  -6.652  -49.535  1.00 72.73  ?  47  PRO B CB  1 
ATOM   4743 C  CG  . PRO B 1 49  ? -6.304  -6.725  -51.009  1.00 81.72  ?  47  PRO B CG  1 
ATOM   4744 C  CD  . PRO B 1 49  ? -5.259  -5.819  -51.606  1.00 85.00  ?  47  PRO B CD  1 
ATOM   4745 N  N   . TYR B 1 50  ? -3.535  -8.357  -48.075  1.00 73.95  ?  48  TYR B N   1 
ATOM   4746 C  CA  . TYR B 1 50  ? -3.061  -9.709  -47.796  1.00 74.26  ?  48  TYR B CA  1 
ATOM   4747 C  C   . TYR B 1 50  ? -4.283  -10.610 -47.725  1.00 74.59  ?  48  TYR B C   1 
ATOM   4748 O  O   . TYR B 1 50  ? -4.928  -10.753 -46.686  1.00 72.26  ?  48  TYR B O   1 
ATOM   4749 C  CB  . TYR B 1 50  ? -2.248  -9.749  -46.509  1.00 69.89  ?  48  TYR B CB  1 
ATOM   4750 C  CG  . TYR B 1 50  ? -0.886  -9.103  -46.622  1.00 71.32  ?  48  TYR B CG  1 
ATOM   4751 C  CD1 . TYR B 1 50  ? -0.338  -8.803  -47.863  1.00 75.27  ?  48  TYR B CD1 1 
ATOM   4752 C  CD2 . TYR B 1 50  ? -0.139  -8.810  -45.490  1.00 66.57  ?  48  TYR B CD2 1 
ATOM   4753 C  CE1 . TYR B 1 50  ? 0.907   -8.211  -47.970  1.00 74.14  ?  48  TYR B CE1 1 
ATOM   4754 C  CE2 . TYR B 1 50  ? 1.109   -8.225  -45.588  1.00 66.24  ?  48  TYR B CE2 1 
ATOM   4755 C  CZ  . TYR B 1 50  ? 1.627   -7.927  -46.830  1.00 71.21  ?  48  TYR B CZ  1 
ATOM   4756 O  OH  . TYR B 1 50  ? 2.872   -7.351  -46.930  1.00 70.43  ?  48  TYR B OH  1 
ATOM   4757 N  N   . VAL B 1 51  ? -4.599  -11.229 -48.859  1.00 77.51  ?  49  VAL B N   1 
ATOM   4758 C  CA  . VAL B 1 51  ? -5.722  -12.147 -48.980  1.00 78.90  ?  49  VAL B CA  1 
ATOM   4759 C  C   . VAL B 1 51  ? -5.281  -13.293 -49.876  1.00 78.71  ?  49  VAL B C   1 
ATOM   4760 O  O   . VAL B 1 51  ? -4.484  -13.109 -50.801  1.00 83.85  ?  49  VAL B O   1 
ATOM   4761 C  CB  . VAL B 1 51  ? -6.980  -11.442 -49.541  1.00 83.67  ?  49  VAL B CB  1 
ATOM   4762 C  CG1 . VAL B 1 51  ? -6.638  -10.661 -50.805  1.00 78.42  ?  49  VAL B CG1 1 
ATOM   4763 C  CG2 . VAL B 1 51  ? -8.094  -12.445 -49.799  1.00 84.23  ?  49  VAL B CG2 1 
ATOM   4764 N  N   . CYS B 1 52  ? -5.788  -14.490 -49.590  1.00 78.48  ?  50  CYS B N   1 
ATOM   4765 C  CA  . CYS B 1 52  ? -5.481  -15.628 -50.447  1.00 84.52  ?  50  CYS B CA  1 
ATOM   4766 C  C   . CYS B 1 52  ? -6.015  -15.382 -51.853  1.00 88.91  ?  50  CYS B C   1 
ATOM   4767 O  O   . CYS B 1 52  ? -7.231  -15.380 -52.071  1.00 85.39  ?  50  CYS B O   1 
ATOM   4768 C  CB  . CYS B 1 52  ? -6.059  -16.922 -49.875  1.00 78.32  ?  50  CYS B CB  1 
ATOM   4769 S  SG  . CYS B 1 52  ? -5.612  -18.387 -50.836  1.00 89.54  ?  50  CYS B SG  1 
ATOM   4770 N  N   . ASN B 1 53  ? -5.114  -15.169 -52.810  1.00 89.92  ?  51  ASN B N   1 
ATOM   4771 C  CA  . ASN B 1 53  ? -5.517  -14.891 -54.182  1.00 89.86  ?  51  ASN B CA  1 
ATOM   4772 C  C   . ASN B 1 53  ? -5.812  -16.182 -54.936  1.00 96.56  ?  51  ASN B C   1 
ATOM   4773 O  O   . ASN B 1 53  ? -5.310  -16.389 -56.045  1.00 104.92 ?  51  ASN B O   1 
ATOM   4774 C  CB  . ASN B 1 53  ? -4.433  -14.087 -54.905  1.00 88.97  ?  51  ASN B CB  1 
ATOM   4775 C  CG  . ASN B 1 53  ? -3.883  -12.955 -54.056  1.00 94.03  ?  51  ASN B CG  1 
ATOM   4776 O  OD1 . ASN B 1 53  ? -2.684  -12.896 -53.781  1.00 94.21  ?  51  ASN B OD1 1 
ATOM   4777 N  ND2 . ASN B 1 53  ? -4.760  -12.054 -53.630  1.00 88.55  ?  51  ASN B ND2 1 
ATOM   4778 N  N   . ALA B 1 54  ? -6.630  -17.054 -54.345  1.00 98.44  ?  52  ALA B N   1 
ATOM   4779 C  CA  . ALA B 1 54  ? -6.988  -18.323 -54.952  1.00 99.29  ?  52  ALA B CA  1 
ATOM   4780 C  C   . ALA B 1 54  ? -8.477  -18.359 -55.273  1.00 101.54 ?  52  ALA B C   1 
ATOM   4781 O  O   . ALA B 1 54  ? -9.291  -17.847 -54.497  1.00 100.42 ?  52  ALA B O   1 
ATOM   4782 C  CB  . ALA B 1 54  ? -6.639  -19.500 -54.030  1.00 98.41  ?  52  ALA B CB  1 
ATOM   4783 N  N   . PRO B 1 55  ? -8.863  -18.950 -56.408  1.00 109.57 ?  53  PRO B N   1 
ATOM   4784 C  CA  . PRO B 1 55  ? -10.282 -18.959 -56.793  1.00 112.57 ?  53  PRO B CA  1 
ATOM   4785 C  C   . PRO B 1 55  ? -11.186 -19.558 -55.728  1.00 111.63 ?  53  PRO B C   1 
ATOM   4786 O  O   . PRO B 1 55  ? -11.103 -20.753 -55.427  1.00 114.02 ?  53  PRO B O   1 
ATOM   4787 C  CB  . PRO B 1 55  ? -10.291 -19.804 -58.076  1.00 122.18 ?  53  PRO B CB  1 
ATOM   4788 C  CG  . PRO B 1 55  ? -9.002  -20.577 -58.042  1.00 121.13 ?  53  PRO B CG  1 
ATOM   4789 C  CD  . PRO B 1 55  ? -8.025  -19.658 -57.388  1.00 112.31 ?  53  PRO B CD  1 
ATOM   4790 N  N   . GLY B 1 56  ? -12.053 -18.731 -55.150  1.00 111.02 ?  54  GLY B N   1 
ATOM   4791 C  CA  . GLY B 1 56  ? -13.039 -19.194 -54.197  1.00 109.14 ?  54  GLY B CA  1 
ATOM   4792 C  C   . GLY B 1 56  ? -12.591 -19.254 -52.755  1.00 103.07 ?  54  GLY B C   1 
ATOM   4793 O  O   . GLY B 1 56  ? -13.322 -19.807 -51.925  1.00 109.47 ?  54  GLY B O   1 
ATOM   4794 N  N   . CYS B 1 57  ? -11.423 -18.713 -52.424  1.00 96.70  ?  55  CYS B N   1 
ATOM   4795 C  CA  . CYS B 1 57  ? -10.971 -18.679 -51.042  1.00 97.58  ?  55  CYS B CA  1 
ATOM   4796 C  C   . CYS B 1 57  ? -11.412 -17.392 -50.357  1.00 95.00  ?  55  CYS B C   1 
ATOM   4797 O  O   . CYS B 1 57  ? -11.591 -16.351 -50.995  1.00 95.98  ?  55  CYS B O   1 
ATOM   4798 C  CB  . CYS B 1 57  ? -9.453  -18.817 -50.947  1.00 95.80  ?  55  CYS B CB  1 
ATOM   4799 S  SG  . CYS B 1 57  ? -8.891  -19.188 -49.266  1.00 89.58  ?  55  CYS B SG  1 
ATOM   4800 N  N   . ASP B 1 58  ? -11.571 -17.474 -49.033  1.00 96.70  ?  56  ASP B N   1 
ATOM   4801 C  CA  . ASP B 1 58  ? -12.059 -16.357 -48.233  1.00 89.63  ?  56  ASP B CA  1 
ATOM   4802 C  C   . ASP B 1 58  ? -11.129 -16.029 -47.071  1.00 86.53  ?  56  ASP B C   1 
ATOM   4803 O  O   . ASP B 1 58  ? -11.568 -15.414 -46.094  1.00 91.15  ?  56  ASP B O   1 
ATOM   4804 C  CB  . ASP B 1 58  ? -13.459 -16.655 -47.693  1.00 94.40  ?  56  ASP B CB  1 
ATOM   4805 C  CG  . ASP B 1 58  ? -13.530 -17.988 -46.971  1.00 96.68  ?  56  ASP B CG  1 
ATOM   4806 O  OD1 . ASP B 1 58  ? -13.127 -19.011 -47.563  1.00 102.17 ?  56  ASP B OD1 1 
ATOM   4807 O  OD2 . ASP B 1 58  ? -13.975 -18.010 -45.804  1.00 98.69  -1 56  ASP B OD2 1 
ATOM   4808 N  N   . VAL B 1 59  ? -9.860  -16.415 -47.148  1.00 82.52  ?  57  VAL B N   1 
ATOM   4809 C  CA  . VAL B 1 59  ? -8.945  -16.253 -46.023  1.00 82.62  ?  57  VAL B CA  1 
ATOM   4810 C  C   . VAL B 1 59  ? -8.306  -14.874 -46.097  1.00 77.23  ?  57  VAL B C   1 
ATOM   4811 O  O   . VAL B 1 59  ? -7.693  -14.511 -47.107  1.00 70.80  ?  57  VAL B O   1 
ATOM   4812 C  CB  . VAL B 1 59  ? -7.875  -17.354 -46.009  1.00 78.14  ?  57  VAL B CB  1 
ATOM   4813 C  CG1 . VAL B 1 59  ? -6.878  -17.098 -44.888  1.00 80.78  ?  57  VAL B CG1 1 
ATOM   4814 C  CG2 . VAL B 1 59  ? -8.521  -18.719 -45.844  1.00 79.50  ?  57  VAL B CG2 1 
ATOM   4815 N  N   . THR B 1 60  ? -8.441  -14.112 -45.011  1.00 77.06  ?  58  THR B N   1 
ATOM   4816 C  CA  . THR B 1 60  ? -7.886  -12.771 -44.906  1.00 75.61  ?  58  THR B CA  1 
ATOM   4817 C  C   . THR B 1 60  ? -7.064  -12.568 -43.644  1.00 71.56  ?  58  THR B C   1 
ATOM   4818 O  O   . THR B 1 60  ? -6.428  -11.517 -43.507  1.00 70.38  ?  58  THR B O   1 
ATOM   4819 C  CB  . THR B 1 60  ? -9.001  -11.713 -44.944  1.00 76.42  ?  58  THR B CB  1 
ATOM   4820 O  OG1 . THR B 1 60  ? -9.977  -12.006 -43.936  1.00 77.91  ?  58  THR B OG1 1 
ATOM   4821 C  CG2 . THR B 1 60  ? -9.676  -11.697 -46.307  1.00 77.70  ?  58  THR B CG2 1 
ATOM   4822 N  N   . ASP B 1 61  ? -7.058  -13.529 -42.724  1.00 62.85  ?  59  ASP B N   1 
ATOM   4823 C  CA  . ASP B 1 61  ? -6.230  -13.433 -41.531  1.00 64.36  ?  59  ASP B CA  1 
ATOM   4824 C  C   . ASP B 1 61  ? -4.760  -13.542 -41.920  1.00 60.93  ?  59  ASP B C   1 
ATOM   4825 O  O   . ASP B 1 61  ? -4.363  -14.466 -42.638  1.00 65.84  ?  59  ASP B O   1 
ATOM   4826 C  CB  . ASP B 1 61  ? -6.623  -14.537 -40.547  1.00 61.60  ?  59  ASP B CB  1 
ATOM   4827 C  CG  . ASP B 1 61  ? -5.866  -14.463 -39.238  1.00 62.60  ?  59  ASP B CG  1 
ATOM   4828 O  OD1 . ASP B 1 61  ? -4.888  -13.695 -39.144  1.00 65.34  ?  59  ASP B OD1 1 
ATOM   4829 O  OD2 . ASP B 1 61  ? -6.261  -15.177 -38.292  1.00 67.31  -1 59  ASP B OD2 1 
ATOM   4830 N  N   . VAL B 1 62  ? -3.948  -12.598 -41.436  1.00 58.86  ?  60  VAL B N   1 
ATOM   4831 C  CA  . VAL B 1 62  ? -2.535  -12.584 -41.802  1.00 61.28  ?  60  VAL B CA  1 
ATOM   4832 C  C   . VAL B 1 62  ? -1.790  -13.733 -41.138  1.00 66.08  ?  60  VAL B C   1 
ATOM   4833 O  O   . VAL B 1 62  ? -0.772  -14.206 -41.660  1.00 66.71  ?  60  VAL B O   1 
ATOM   4834 C  CB  . VAL B 1 62  ? -1.904  -11.227 -41.443  1.00 57.94  ?  60  VAL B CB  1 
ATOM   4835 C  CG1 . VAL B 1 62  ? -1.983  -10.984 -39.942  1.00 53.24  ?  60  VAL B CG1 1 
ATOM   4836 C  CG2 . VAL B 1 62  ? -0.465  -11.163 -41.933  1.00 64.23  ?  60  VAL B CG2 1 
ATOM   4837 N  N   . THR B 1 63  ? -2.274  -14.205 -39.989  1.00 59.63  ?  61  THR B N   1 
ATOM   4838 C  CA  . THR B 1 63  ? -1.591  -15.282 -39.286  1.00 62.23  ?  61  THR B CA  1 
ATOM   4839 C  C   . THR B 1 63  ? -1.651  -16.591 -40.060  1.00 64.24  ?  61  THR B C   1 
ATOM   4840 O  O   . THR B 1 63  ? -0.805  -17.465 -39.843  1.00 66.81  ?  61  THR B O   1 
ATOM   4841 C  CB  . THR B 1 63  ? -2.185  -15.461 -37.888  1.00 63.65  ?  61  THR B CB  1 
ATOM   4842 O  OG1 . THR B 1 63  ? -3.563  -15.839 -37.994  1.00 69.87  ?  61  THR B OG1 1 
ATOM   4843 C  CG2 . THR B 1 63  ? -2.082  -14.161 -37.101  1.00 57.46  ?  61  THR B CG2 1 
ATOM   4844 N  N   . GLN B 1 64  ? -2.627  -16.743 -40.957  1.00 63.18  ?  62  GLN B N   1 
ATOM   4845 C  CA  . GLN B 1 64  ? -2.837  -17.975 -41.707  1.00 69.03  ?  62  GLN B CA  1 
ATOM   4846 C  C   . GLN B 1 64  ? -2.530  -17.794 -43.193  1.00 69.30  ?  62  GLN B C   1 
ATOM   4847 O  O   . GLN B 1 64  ? -3.104  -18.487 -44.037  1.00 72.34  ?  62  GLN B O   1 
ATOM   4848 C  CB  . GLN B 1 64  ? -4.275  -18.467 -41.534  1.00 62.85  ?  62  GLN B CB  1 
ATOM   4849 C  CG  . GLN B 1 64  ? -4.873  -18.251 -40.149  1.00 64.84  ?  62  GLN B CG  1 
ATOM   4850 C  CD  . GLN B 1 64  ? -4.263  -19.145 -39.088  1.00 71.88  ?  62  GLN B CD  1 
ATOM   4851 O  OE1 . GLN B 1 64  ? -4.338  -20.372 -39.173  1.00 62.82  ?  62  GLN B OE1 1 
ATOM   4852 N  NE2 . GLN B 1 64  ? -3.661  -18.532 -38.074  1.00 69.35  ?  62  GLN B NE2 1 
ATOM   4853 N  N   . LEU B 1 65  ? -1.617  -16.883 -43.532  1.00 65.02  ?  63  LEU B N   1 
ATOM   4854 C  CA  . LEU B 1 65  ? -1.340  -16.552 -44.923  1.00 68.25  ?  63  LEU B CA  1 
ATOM   4855 C  C   . LEU B 1 65  ? 0.156   -16.620 -45.196  1.00 66.18  ?  63  LEU B C   1 
ATOM   4856 O  O   . LEU B 1 65  ? 0.980   -16.411 -44.301  1.00 60.97  ?  63  LEU B O   1 
ATOM   4857 C  CB  . LEU B 1 65  ? -1.879  -15.159 -45.284  1.00 66.86  ?  63  LEU B CB  1 
ATOM   4858 C  CG  . LEU B 1 65  ? -3.389  -15.071 -45.521  1.00 69.34  ?  63  LEU B CG  1 
ATOM   4859 C  CD1 . LEU B 1 65  ? -3.818  -13.626 -45.733  1.00 71.30  ?  63  LEU B CD1 1 
ATOM   4860 C  CD2 . LEU B 1 65  ? -3.815  -15.940 -46.698  1.00 71.29  ?  63  LEU B CD2 1 
ATOM   4861 N  N   . TYR B 1 66  ? 0.495   -16.890 -46.458  1.00 72.67  ?  64  TYR B N   1 
ATOM   4862 C  CA  . TYR B 1 66  ? 1.873   -17.086 -46.887  1.00 72.45  ?  64  TYR B CA  1 
ATOM   4863 C  C   . TYR B 1 66  ? 2.095   -16.406 -48.230  1.00 71.45  ?  64  TYR B C   1 
ATOM   4864 O  O   . TYR B 1 66  ? 1.182   -16.320 -49.056  1.00 78.63  ?  64  TYR B O   1 
ATOM   4865 C  CB  . TYR B 1 66  ? 2.197   -18.583 -47.020  1.00 71.54  ?  64  TYR B CB  1 
ATOM   4866 C  CG  . TYR B 1 66  ? 1.906   -19.406 -45.783  1.00 74.45  ?  64  TYR B CG  1 
ATOM   4867 C  CD1 . TYR B 1 66  ? 0.608   -19.803 -45.483  1.00 71.70  ?  64  TYR B CD1 1 
ATOM   4868 C  CD2 . TYR B 1 66  ? 2.929   -19.831 -44.945  1.00 73.09  ?  64  TYR B CD2 1 
ATOM   4869 C  CE1 . TYR B 1 66  ? 0.332   -20.564 -44.364  1.00 78.09  ?  64  TYR B CE1 1 
ATOM   4870 C  CE2 . TYR B 1 66  ? 2.662   -20.600 -43.825  1.00 71.13  ?  64  TYR B CE2 1 
ATOM   4871 C  CZ  . TYR B 1 66  ? 1.362   -20.963 -43.540  1.00 75.66  ?  64  TYR B CZ  1 
ATOM   4872 O  OH  . TYR B 1 66  ? 1.086   -21.724 -42.428  1.00 78.11  ?  64  TYR B OH  1 
ATOM   4873 N  N   . LEU B 1 67  ? 3.319   -15.924 -48.444  1.00 76.21  ?  65  LEU B N   1 
ATOM   4874 C  CA  . LEU B 1 67  ? 3.705   -15.309 -49.709  1.00 80.50  ?  65  LEU B CA  1 
ATOM   4875 C  C   . LEU B 1 67  ? 4.311   -16.357 -50.638  1.00 85.32  ?  65  LEU B C   1 
ATOM   4876 O  O   . LEU B 1 67  ? 5.309   -16.998 -50.291  1.00 86.77  ?  65  LEU B O   1 
ATOM   4877 C  CB  . LEU B 1 67  ? 4.701   -14.171 -49.491  1.00 82.95  ?  65  LEU B CB  1 
ATOM   4878 C  CG  . LEU B 1 67  ? 5.295   -13.627 -50.796  1.00 90.41  ?  65  LEU B CG  1 
ATOM   4879 C  CD1 . LEU B 1 67  ? 4.304   -12.709 -51.503  1.00 89.91  ?  65  LEU B CD1 1 
ATOM   4880 C  CD2 . LEU B 1 67  ? 6.625   -12.922 -50.566  1.00 86.95  ?  65  LEU B CD2 1 
ATOM   4881 N  N   . GLY B 1 68  ? 3.704   -16.530 -51.811  1.00 89.42  ?  66  GLY B N   1 
ATOM   4882 C  CA  . GLY B 1 68  ? 4.222   -17.436 -52.820  1.00 90.00  ?  66  GLY B CA  1 
ATOM   4883 C  C   . GLY B 1 68  ? 4.450   -16.702 -54.127  1.00 97.56  ?  66  GLY B C   1 
ATOM   4884 O  O   . GLY B 1 68  ? 3.492   -16.222 -54.740  1.00 95.82  ?  66  GLY B O   1 
ATOM   4885 N  N   . GLY B 1 69  ? 5.704   -16.605 -54.568  1.00 101.22 ?  67  GLY B N   1 
ATOM   4886 C  CA  . GLY B 1 69  ? 5.999   -15.798 -55.737  1.00 93.75  ?  67  GLY B CA  1 
ATOM   4887 C  C   . GLY B 1 69  ? 5.832   -14.336 -55.377  1.00 100.79 ?  67  GLY B C   1 
ATOM   4888 O  O   . GLY B 1 69  ? 6.597   -13.796 -54.572  1.00 102.40 ?  67  GLY B O   1 
ATOM   4889 N  N   . MET B 1 70  ? 4.825   -13.688 -55.962  1.00 100.18 ?  68  MET B N   1 
ATOM   4890 C  CA  . MET B 1 70  ? 4.458   -12.323 -55.605  1.00 95.88  ?  68  MET B CA  1 
ATOM   4891 C  C   . MET B 1 70  ? 3.005   -12.261 -55.153  1.00 97.48  ?  68  MET B C   1 
ATOM   4892 O  O   . MET B 1 70  ? 2.479   -11.169 -54.907  1.00 96.29  ?  68  MET B O   1 
ATOM   4893 C  CB  . MET B 1 70  ? 4.681   -11.366 -56.781  1.00 99.86  ?  68  MET B CB  1 
ATOM   4894 C  CG  . MET B 1 70  ? 6.012   -11.528 -57.506  1.00 102.58 ?  68  MET B CG  1 
ATOM   4895 S  SD  . MET B 1 70  ? 7.432   -10.899 -56.588  1.00 123.27 ?  68  MET B SD  1 
ATOM   4896 C  CE  . MET B 1 70  ? 6.883   -9.240  -56.189  1.00 104.39 ?  68  MET B CE  1 
ATOM   4897 N  N   . SER B 1 71  ? 2.353   -13.414 -55.041  1.00 95.68  ?  69  SER B N   1 
ATOM   4898 C  CA  . SER B 1 71  ? 0.966   -13.562 -54.629  1.00 93.51  ?  69  SER B CA  1 
ATOM   4899 C  C   . SER B 1 71  ? 0.897   -14.078 -53.193  1.00 90.97  ?  69  SER B C   1 
ATOM   4900 O  O   . SER B 1 71  ? 1.898   -14.492 -52.604  1.00 89.50  ?  69  SER B O   1 
ATOM   4901 C  CB  . SER B 1 71  ? 0.224   -14.502 -55.582  1.00 92.01  ?  69  SER B CB  1 
ATOM   4902 O  OG  . SER B 1 71  ? 1.101   -15.480 -56.113  1.00 98.69  ?  69  SER B OG  1 
ATOM   4903 N  N   . TYR B 1 72  ? -0.309  -14.059 -52.632  1.00 87.90  ?  70  TYR B N   1 
ATOM   4904 C  CA  . TYR B 1 72  ? -0.532  -14.437 -51.244  1.00 86.70  ?  70  TYR B CA  1 
ATOM   4905 C  C   . TYR B 1 72  ? -1.565  -15.553 -51.184  1.00 85.15  ?  70  TYR B C   1 
ATOM   4906 O  O   . TYR B 1 72  ? -2.555  -15.536 -51.923  1.00 82.97  ?  70  TYR B O   1 
ATOM   4907 C  CB  . TYR B 1 72  ? -1.014  -13.245 -50.409  1.00 89.28  ?  70  TYR B CB  1 
ATOM   4908 C  CG  . TYR B 1 72  ? -0.204  -11.982 -50.601  1.00 85.76  ?  70  TYR B CG  1 
ATOM   4909 C  CD1 . TYR B 1 72  ? 1.027   -11.821 -49.981  1.00 84.14  ?  70  TYR B CD1 1 
ATOM   4910 C  CD2 . TYR B 1 72  ? -0.684  -10.942 -51.387  1.00 81.10  ?  70  TYR B CD2 1 
ATOM   4911 C  CE1 . TYR B 1 72  ? 1.768   -10.667 -50.156  1.00 85.99  ?  70  TYR B CE1 1 
ATOM   4912 C  CE2 . TYR B 1 72  ? 0.046   -9.783  -51.562  1.00 83.83  ?  70  TYR B CE2 1 
ATOM   4913 C  CZ  . TYR B 1 72  ? 1.272   -9.651  -50.946  1.00 83.38  ?  70  TYR B CZ  1 
ATOM   4914 O  OH  . TYR B 1 72  ? 2.002   -8.497  -51.113  1.00 82.17  ?  70  TYR B OH  1 
ATOM   4915 N  N   . TYR B 1 73  ? -1.335  -16.520 -50.296  1.00 82.81  ?  71  TYR B N   1 
ATOM   4916 C  CA  . TYR B 1 73  ? -2.203  -17.685 -50.203  1.00 83.27  ?  71  TYR B CA  1 
ATOM   4917 C  C   . TYR B 1 73  ? -2.285  -18.148 -48.756  1.00 79.38  ?  71  TYR B C   1 
ATOM   4918 O  O   . TYR B 1 73  ? -1.441  -17.807 -47.922  1.00 74.78  ?  71  TYR B O   1 
ATOM   4919 C  CB  . TYR B 1 73  ? -1.697  -18.844 -51.075  1.00 85.55  ?  71  TYR B CB  1 
ATOM   4920 C  CG  . TYR B 1 73  ? -1.438  -18.499 -52.526  1.00 88.69  ?  71  TYR B CG  1 
ATOM   4921 C  CD1 . TYR B 1 73  ? -2.452  -18.572 -53.472  1.00 88.87  ?  71  TYR B CD1 1 
ATOM   4922 C  CD2 . TYR B 1 73  ? -0.169  -18.126 -52.954  1.00 87.96  ?  71  TYR B CD2 1 
ATOM   4923 C  CE1 . TYR B 1 73  ? -2.214  -18.266 -54.800  1.00 93.96  ?  71  TYR B CE1 1 
ATOM   4924 C  CE2 . TYR B 1 73  ? 0.078   -17.820 -54.279  1.00 90.80  ?  71  TYR B CE2 1 
ATOM   4925 C  CZ  . TYR B 1 73  ? -0.948  -17.892 -55.199  1.00 96.46  ?  71  TYR B CZ  1 
ATOM   4926 O  OH  . TYR B 1 73  ? -0.709  -17.591 -56.521  1.00 94.33  ?  71  TYR B OH  1 
ATOM   4927 N  N   . CYS B 1 74  ? -3.321  -18.935 -48.469  1.00 81.41  ?  72  CYS B N   1 
ATOM   4928 C  CA  . CYS B 1 74  ? -3.500  -19.555 -47.166  1.00 81.26  ?  72  CYS B CA  1 
ATOM   4929 C  C   . CYS B 1 74  ? -2.730  -20.873 -47.124  1.00 82.56  ?  72  CYS B C   1 
ATOM   4930 O  O   . CYS B 1 74  ? -2.015  -21.231 -48.064  1.00 78.72  ?  72  CYS B O   1 
ATOM   4931 C  CB  . CYS B 1 74  ? -4.981  -19.787 -46.878  1.00 77.33  ?  72  CYS B CB  1 
ATOM   4932 S  SG  . CYS B 1 74  ? -5.759  -20.964 -48.011  1.00 87.67  ?  72  CYS B SG  1 
ATOM   4933 N  N   . LYS B 1 75  ? -2.876  -21.622 -46.028  1.00 80.13  ?  73  LYS B N   1 
ATOM   4934 C  CA  . LYS B 1 75  ? -2.174  -22.895 -45.920  1.00 85.44  ?  73  LYS B CA  1 
ATOM   4935 C  C   . LYS B 1 75  ? -2.737  -23.911 -46.902  1.00 86.53  ?  73  LYS B C   1 
ATOM   4936 O  O   . LYS B 1 75  ? -1.994  -24.756 -47.413  1.00 89.71  ?  73  LYS B O   1 
ATOM   4937 C  CB  . LYS B 1 75  ? -2.260  -23.437 -44.491  1.00 80.23  ?  73  LYS B CB  1 
ATOM   4938 C  CG  . LYS B 1 75  ? -2.330  -24.968 -44.380  1.00 83.06  ?  73  LYS B CG  1 
ATOM   4939 C  CD  . LYS B 1 75  ? -3.740  -25.470 -44.063  1.00 91.54  ?  73  LYS B CD  1 
ATOM   4940 C  CE  . LYS B 1 75  ? -3.800  -26.998 -43.951  1.00 91.12  ?  73  LYS B CE  1 
ATOM   4941 N  NZ  . LYS B 1 75  ? -3.614  -27.720 -45.243  1.00 97.06  ?  73  LYS B NZ  1 
ATOM   4942 N  N   . SER B 1 76  ? -4.038  -23.835 -47.186  1.00 89.19  ?  74  SER B N   1 
ATOM   4943 C  CA  . SER B 1 76  ? -4.709  -24.814 -48.029  1.00 89.54  ?  74  SER B CA  1 
ATOM   4944 C  C   . SER B 1 76  ? -4.488  -24.578 -49.516  1.00 92.41  ?  74  SER B C   1 
ATOM   4945 O  O   . SER B 1 76  ? -4.766  -25.479 -50.315  1.00 99.54  ?  74  SER B O   1 
ATOM   4946 C  CB  . SER B 1 76  ? -6.211  -24.815 -47.732  1.00 93.11  ?  74  SER B CB  1 
ATOM   4947 O  OG  . SER B 1 76  ? -6.468  -25.260 -46.412  1.00 96.54  ?  74  SER B OG  1 
ATOM   4948 N  N   . HIS B 1 77  ? -3.989  -23.404 -49.909  1.00 87.90  ?  75  HIS B N   1 
ATOM   4949 C  CA  . HIS B 1 77  ? -3.823  -23.076 -51.319  1.00 95.38  ?  75  HIS B CA  1 
ATOM   4950 C  C   . HIS B 1 77  ? -2.427  -22.530 -51.591  1.00 96.39  ?  75  HIS B C   1 
ATOM   4951 O  O   . HIS B 1 77  ? -2.228  -21.761 -52.536  1.00 100.68 ?  75  HIS B O   1 
ATOM   4952 C  CB  . HIS B 1 77  ? -4.875  -22.061 -51.769  1.00 93.29  ?  75  HIS B CB  1 
ATOM   4953 C  CG  . HIS B 1 77  ? -6.287  -22.532 -51.604  1.00 95.38  ?  75  HIS B CG  1 
ATOM   4954 N  ND1 . HIS B 1 77  ? -7.137  -22.009 -50.654  1.00 95.43  ?  75  HIS B ND1 1 
ATOM   4955 C  CD2 . HIS B 1 77  ? -7.000  -23.471 -52.271  1.00 100.90 ?  75  HIS B CD2 1 
ATOM   4956 C  CE1 . HIS B 1 77  ? -8.312  -22.608 -50.739  1.00 94.30  ?  75  HIS B CE1 1 
ATOM   4957 N  NE2 . HIS B 1 77  ? -8.255  -23.499 -51.713  1.00 101.51 ?  75  HIS B NE2 1 
ATOM   4958 N  N   . LYS B 1 78  ? -1.443  -22.929 -50.778  1.00 93.13  ?  76  LYS B N   1 
ATOM   4959 C  CA  . LYS B 1 78  ? -0.147  -22.293 -50.947  1.00 94.53  ?  76  LYS B CA  1 
ATOM   4960 C  C   . LYS B 1 78  ? 0.775   -23.142 -51.815  1.00 91.57  ?  76  LYS B C   1 
ATOM   4961 O  O   . LYS B 1 78  ? 0.677   -24.373 -51.826  1.00 96.63  ?  76  LYS B O   1 
ATOM   4962 C  CB  . LYS B 1 78  ? 0.501   -22.015 -49.582  1.00 87.46  ?  76  LYS B CB  1 
ATOM   4963 C  CG  . LYS B 1 78  ? 1.195   -23.183 -48.892  1.00 85.92  ?  76  LYS B CG  1 
ATOM   4964 C  CD  . LYS B 1 78  ? 1.705   -22.733 -47.518  1.00 77.49  ?  76  LYS B CD  1 
ATOM   4965 C  CE  . LYS B 1 78  ? 2.770   -23.658 -46.945  1.00 81.57  ?  76  LYS B CE  1 
ATOM   4966 N  NZ  . LYS B 1 78  ? 4.055   -23.590 -47.692  1.00 97.20  ?  76  LYS B NZ  1 
ATOM   4967 N  N   . PRO B 1 79  ? 1.666   -22.499 -52.563  1.00 92.25  ?  77  PRO B N   1 
ATOM   4968 C  CA  . PRO B 1 79  ? 2.704   -23.231 -53.293  1.00 98.52  ?  77  PRO B CA  1 
ATOM   4969 C  C   . PRO B 1 79  ? 3.726   -23.812 -52.335  1.00 98.15  ?  77  PRO B C   1 
ATOM   4970 O  O   . PRO B 1 79  ? 3.800   -23.399 -51.168  1.00 100.13 ?  77  PRO B O   1 
ATOM   4971 C  CB  . PRO B 1 79  ? 3.326   -22.147 -54.186  1.00 98.74  ?  77  PRO B CB  1 
ATOM   4972 C  CG  . PRO B 1 79  ? 3.134   -20.897 -53.384  1.00 95.99  ?  77  PRO B CG  1 
ATOM   4973 C  CD  . PRO B 1 79  ? 1.745   -21.051 -52.823  1.00 90.33  ?  77  PRO B CD  1 
ATOM   4974 N  N   . PRO B 1 80  ? 4.530   -24.782 -52.781  1.00 104.71 ?  78  PRO B N   1 
ATOM   4975 C  CA  . PRO B 1 80  ? 5.498   -25.386 -51.852  1.00 105.37 ?  78  PRO B CA  1 
ATOM   4976 C  C   . PRO B 1 80  ? 6.585   -24.425 -51.411  1.00 105.06 ?  78  PRO B C   1 
ATOM   4977 O  O   . PRO B 1 80  ? 6.988   -24.453 -50.241  1.00 105.08 ?  78  PRO B O   1 
ATOM   4978 C  CB  . PRO B 1 80  ? 6.067   -26.560 -52.667  1.00 114.44 ?  78  PRO B CB  1 
ATOM   4979 C  CG  . PRO B 1 80  ? 5.044   -26.796 -53.757  1.00 118.11 ?  78  PRO B CG  1 
ATOM   4980 C  CD  . PRO B 1 80  ? 4.587   -25.418 -54.105  1.00 112.64 ?  78  PRO B CD  1 
ATOM   4981 N  N   . ILE B 1 81  ? 7.073   -23.571 -52.308  1.00 102.37 ?  79  ILE B N   1 
ATOM   4982 C  CA  . ILE B 1 81  ? 8.051   -22.545 -51.959  1.00 100.92 ?  79  ILE B CA  1 
ATOM   4983 C  C   . ILE B 1 81  ? 7.282   -21.319 -51.476  1.00 98.55  ?  79  ILE B C   1 
ATOM   4984 O  O   . ILE B 1 81  ? 6.751   -20.546 -52.275  1.00 100.15 ?  79  ILE B O   1 
ATOM   4985 C  CB  . ILE B 1 81  ? 8.972   -22.213 -53.134  1.00 105.01 ?  79  ILE B CB  1 
ATOM   4986 C  CG1 . ILE B 1 81  ? 9.716   -23.466 -53.595  1.00 113.10 ?  79  ILE B CG1 1 
ATOM   4987 C  CG2 . ILE B 1 81  ? 9.953   -21.114 -52.749  1.00 102.87 ?  79  ILE B CG2 1 
ATOM   4988 C  CD1 . ILE B 1 81  ? 10.764  -23.198 -54.653  1.00 119.40 ?  79  ILE B CD1 1 
ATOM   4989 N  N   . SER B 1 82  ? 7.223   -21.140 -50.160  1.00 89.53  ?  80  SER B N   1 
ATOM   4990 C  CA  . SER B 1 82  ? 6.457   -20.049 -49.576  1.00 90.91  ?  80  SER B CA  1 
ATOM   4991 C  C   . SER B 1 82  ? 6.967   -19.801 -48.167  1.00 81.20  ?  80  SER B C   1 
ATOM   4992 O  O   . SER B 1 82  ? 7.542   -20.687 -47.530  1.00 86.43  ?  80  SER B O   1 
ATOM   4993 C  CB  . SER B 1 82  ? 4.955   -20.356 -49.559  1.00 87.06  ?  80  SER B CB  1 
ATOM   4994 O  OG  . SER B 1 82  ? 4.706   -21.668 -49.086  1.00 92.59  ?  80  SER B OG  1 
ATOM   4995 N  N   . PHE B 1 83  ? 6.751   -18.578 -47.686  1.00 75.25  ?  81  PHE B N   1 
ATOM   4996 C  CA  . PHE B 1 83  ? 7.144   -18.235 -46.332  1.00 73.90  ?  81  PHE B CA  1 
ATOM   4997 C  C   . PHE B 1 83  ? 6.021   -17.464 -45.651  1.00 76.55  ?  81  PHE B C   1 
ATOM   4998 O  O   . PHE B 1 83  ? 5.351   -16.637 -46.288  1.00 71.75  ?  81  PHE B O   1 
ATOM   4999 C  CB  . PHE B 1 83  ? 8.472   -17.450 -46.291  1.00 76.52  ?  81  PHE B CB  1 
ATOM   5000 C  CG  . PHE B 1 83  ? 8.385   -16.018 -46.758  1.00 75.56  ?  81  PHE B CG  1 
ATOM   5001 C  CD1 . PHE B 1 83  ? 7.936   -15.013 -45.915  1.00 82.31  ?  81  PHE B CD1 1 
ATOM   5002 C  CD2 . PHE B 1 83  ? 8.821   -15.671 -48.028  1.00 82.10  ?  81  PHE B CD2 1 
ATOM   5003 C  CE1 . PHE B 1 83  ? 7.885   -13.696 -46.346  1.00 82.69  ?  81  PHE B CE1 1 
ATOM   5004 C  CE2 . PHE B 1 83  ? 8.773   -14.358 -48.463  1.00 84.65  ?  81  PHE B CE2 1 
ATOM   5005 C  CZ  . PHE B 1 83  ? 8.306   -13.370 -47.621  1.00 80.85  ?  81  PHE B CZ  1 
ATOM   5006 N  N   . PRO B 1 84  ? 5.788   -17.731 -44.367  1.00 70.43  ?  82  PRO B N   1 
ATOM   5007 C  CA  . PRO B 1 84  ? 4.666   -17.096 -43.670  1.00 68.28  ?  82  PRO B CA  1 
ATOM   5008 C  C   . PRO B 1 84  ? 4.791   -15.583 -43.657  1.00 66.21  ?  82  PRO B C   1 
ATOM   5009 O  O   . PRO B 1 84  ? 5.886   -15.028 -43.539  1.00 65.87  ?  82  PRO B O   1 
ATOM   5010 C  CB  . PRO B 1 84  ? 4.760   -17.683 -42.257  1.00 65.95  ?  82  PRO B CB  1 
ATOM   5011 C  CG  . PRO B 1 84  ? 6.216   -17.992 -42.107  1.00 65.44  ?  82  PRO B CG  1 
ATOM   5012 C  CD  . PRO B 1 84  ? 6.592   -18.553 -43.450  1.00 67.58  ?  82  PRO B CD  1 
ATOM   5013 N  N   . LEU B 1 85  ? 3.648   -14.915 -43.799  1.00 62.09  ?  83  LEU B N   1 
ATOM   5014 C  CA  . LEU B 1 85  ? 3.638   -13.460 -43.773  1.00 67.31  ?  83  LEU B CA  1 
ATOM   5015 C  C   . LEU B 1 85  ? 3.800   -12.929 -42.356  1.00 64.51  ?  83  LEU B C   1 
ATOM   5016 O  O   . LEU B 1 85  ? 4.354   -11.842 -42.164  1.00 69.54  ?  83  LEU B O   1 
ATOM   5017 C  CB  . LEU B 1 85  ? 2.337   -12.931 -44.380  1.00 62.03  ?  83  LEU B CB  1 
ATOM   5018 C  CG  . LEU B 1 85  ? 2.136   -13.136 -45.881  1.00 69.75  ?  83  LEU B CG  1 
ATOM   5019 C  CD1 . LEU B 1 85  ? 0.759   -12.653 -46.304  1.00 70.72  ?  83  LEU B CD1 1 
ATOM   5020 C  CD2 . LEU B 1 85  ? 3.222   -12.424 -46.669  1.00 74.78  ?  83  LEU B CD2 1 
ATOM   5021 N  N   . CYS B 1 86  ? 3.327   -13.677 -41.362  1.00 61.88  ?  84  CYS B N   1 
ATOM   5022 C  CA  . CYS B 1 86  ? 3.326   -13.247 -39.966  1.00 66.79  ?  84  CYS B CA  1 
ATOM   5023 C  C   . CYS B 1 86  ? 4.138   -14.239 -39.133  1.00 67.30  ?  84  CYS B C   1 
ATOM   5024 O  O   . CYS B 1 86  ? 3.615   -15.276 -38.714  1.00 75.31  ?  84  CYS B O   1 
ATOM   5025 C  CB  . CYS B 1 86  ? 1.884   -13.130 -39.476  1.00 59.92  ?  84  CYS B CB  1 
ATOM   5026 S  SG  . CYS B 1 86  ? 1.662   -12.470 -37.825  1.00 63.08  ?  84  CYS B SG  1 
ATOM   5027 N  N   . ALA B 1 87  ? 5.410   -13.924 -38.879  1.00 64.78  ?  85  ALA B N   1 
ATOM   5028 C  CA  . ALA B 1 87  ? 6.255   -14.793 -38.064  1.00 56.55  ?  85  ALA B CA  1 
ATOM   5029 C  C   . ALA B 1 87  ? 7.506   -14.041 -37.628  1.00 65.14  ?  85  ALA B C   1 
ATOM   5030 O  O   . ALA B 1 87  ? 7.867   -13.010 -38.201  1.00 68.45  ?  85  ALA B O   1 
ATOM   5031 C  CB  . ALA B 1 87  ? 6.635   -16.072 -38.817  1.00 61.02  ?  85  ALA B CB  1 
ATOM   5032 N  N   . ASN B 1 88  ? 8.166   -14.582 -36.598  1.00 61.71  ?  86  ASN B N   1 
ATOM   5033 C  CA  . ASN B 1 88  ? 9.383   -13.999 -36.025  1.00 67.64  ?  86  ASN B CA  1 
ATOM   5034 C  C   . ASN B 1 88  ? 9.121   -12.631 -35.403  1.00 64.73  ?  86  ASN B C   1 
ATOM   5035 O  O   . ASN B 1 88  ? 10.020  -11.789 -35.330  1.00 71.42  ?  86  ASN B O   1 
ATOM   5036 C  CB  . ASN B 1 88  ? 10.500  -13.888 -37.068  1.00 69.05  ?  86  ASN B CB  1 
ATOM   5037 C  CG  . ASN B 1 88  ? 11.494  -15.031 -36.994  1.00 67.97  ?  86  ASN B CG  1 
ATOM   5038 O  OD1 . ASN B 1 88  ? 11.397  -15.905 -36.134  1.00 72.00  ?  86  ASN B OD1 1 
ATOM   5039 N  ND2 . ASN B 1 88  ? 12.469  -15.019 -37.894  1.00 71.75  ?  86  ASN B ND2 1 
ATOM   5040 N  N   . GLY B 1 89  ? 7.897   -12.401 -34.937  1.00 64.18  ?  87  GLY B N   1 
ATOM   5041 C  CA  . GLY B 1 89  ? 7.574   -11.122 -34.341  1.00 62.58  ?  87  GLY B CA  1 
ATOM   5042 C  C   . GLY B 1 89  ? 7.435   -10.006 -35.348  1.00 61.59  ?  87  GLY B C   1 
ATOM   5043 O  O   . GLY B 1 89  ? 7.542   -8.832  -34.983  1.00 60.04  ?  87  GLY B O   1 
ATOM   5044 N  N   . GLN B 1 90  ? 7.187   -10.342 -36.611  1.00 61.20  ?  88  GLN B N   1 
ATOM   5045 C  CA  . GLN B 1 90  ? 7.121   -9.363  -37.683  1.00 60.92  ?  88  GLN B CA  1 
ATOM   5046 C  C   . GLN B 1 90  ? 6.132   -9.835  -38.737  1.00 64.27  ?  88  GLN B C   1 
ATOM   5047 O  O   . GLN B 1 90  ? 6.026   -11.035 -39.005  1.00 63.69  ?  88  GLN B O   1 
ATOM   5048 C  CB  . GLN B 1 90  ? 8.496   -9.153  -38.336  1.00 62.17  ?  88  GLN B CB  1 
ATOM   5049 C  CG  . GLN B 1 90  ? 9.550   -8.497  -37.452  1.00 64.58  ?  88  GLN B CG  1 
ATOM   5050 C  CD  . GLN B 1 90  ? 10.758  -8.017  -38.245  1.00 71.46  ?  88  GLN B CD  1 
ATOM   5051 O  OE1 . GLN B 1 90  ? 11.372  -8.784  -38.987  1.00 71.61  ?  88  GLN B OE1 1 
ATOM   5052 N  NE2 . GLN B 1 90  ? 11.107  -6.745  -38.085  1.00 76.40  ?  88  GLN B NE2 1 
ATOM   5053 N  N   . VAL B 1 91  ? 5.412   -8.886  -39.326  1.00 53.91  ?  89  VAL B N   1 
ATOM   5054 C  CA  . VAL B 1 91  ? 4.532   -9.149  -40.457  1.00 56.63  ?  89  VAL B CA  1 
ATOM   5055 C  C   . VAL B 1 91  ? 5.313   -8.767  -41.704  1.00 66.19  ?  89  VAL B C   1 
ATOM   5056 O  O   . VAL B 1 91  ? 6.034   -7.761  -41.706  1.00 59.57  ?  89  VAL B O   1 
ATOM   5057 C  CB  . VAL B 1 91  ? 3.212   -8.360  -40.353  1.00 58.33  ?  89  VAL B CB  1 
ATOM   5058 C  CG1 . VAL B 1 91  ? 2.388   -8.523  -41.624  1.00 59.65  ?  89  VAL B CG1 1 
ATOM   5059 C  CG2 . VAL B 1 91  ? 2.419   -8.805  -39.135  1.00 58.88  ?  89  VAL B CG2 1 
ATOM   5060 N  N   . PHE B 1 92  ? 5.189   -9.562  -42.763  1.00 66.54  ?  90  PHE B N   1 
ATOM   5061 C  CA  . PHE B 1 92  ? 5.992   -9.301  -43.950  1.00 65.77  ?  90  PHE B CA  1 
ATOM   5062 C  C   . PHE B 1 92  ? 5.595   -7.983  -44.601  1.00 67.54  ?  90  PHE B C   1 
ATOM   5063 O  O   . PHE B 1 92  ? 4.418   -7.738  -44.883  1.00 63.47  ?  90  PHE B O   1 
ATOM   5064 C  CB  . PHE B 1 92  ? 5.868   -10.430 -44.967  1.00 67.30  ?  90  PHE B CB  1 
ATOM   5065 C  CG  . PHE B 1 92  ? 6.668   -10.186 -46.214  1.00 74.34  ?  90  PHE B CG  1 
ATOM   5066 C  CD1 . PHE B 1 92  ? 8.008   -9.837  -46.127  1.00 74.76  ?  90  PHE B CD1 1 
ATOM   5067 C  CD2 . PHE B 1 92  ? 6.082   -10.265 -47.465  1.00 76.81  ?  90  PHE B CD2 1 
ATOM   5068 C  CE1 . PHE B 1 92  ? 8.754   -9.595  -47.264  1.00 80.57  ?  90  PHE B CE1 1 
ATOM   5069 C  CE2 . PHE B 1 92  ? 6.824   -10.023 -48.609  1.00 82.39  ?  90  PHE B CE2 1 
ATOM   5070 C  CZ  . PHE B 1 92  ? 8.162   -9.688  -48.507  1.00 83.16  ?  90  PHE B CZ  1 
ATOM   5071 N  N   . GLY B 1 93  ? 6.593   -7.147  -44.851  1.00 69.92  ?  91  GLY B N   1 
ATOM   5072 C  CA  . GLY B 1 93  ? 6.399   -5.883  -45.536  1.00 66.82  ?  91  GLY B CA  1 
ATOM   5073 C  C   . GLY B 1 93  ? 7.747   -5.233  -45.746  1.00 75.19  ?  91  GLY B C   1 
ATOM   5074 O  O   . GLY B 1 93  ? 8.787   -5.761  -45.336  1.00 77.57  ?  91  GLY B O   1 
ATOM   5075 N  N   . LEU B 1 94  ? 7.724   -4.070  -46.389  1.00 70.93  ?  92  LEU B N   1 
ATOM   5076 C  CA  . LEU B 1 94  ? 8.981   -3.425  -46.724  1.00 80.15  ?  92  LEU B CA  1 
ATOM   5077 C  C   . LEU B 1 94  ? 9.638   -2.845  -45.473  1.00 81.99  ?  92  LEU B C   1 
ATOM   5078 O  O   . LEU B 1 94  ? 9.060   -2.817  -44.383  1.00 69.41  ?  92  LEU B O   1 
ATOM   5079 C  CB  . LEU B 1 94  ? 8.763   -2.328  -47.765  1.00 86.68  ?  92  LEU B CB  1 
ATOM   5080 C  CG  . LEU B 1 94  ? 8.605   -2.800  -49.209  1.00 85.06  ?  92  LEU B CG  1 
ATOM   5081 C  CD1 . LEU B 1 94  ? 8.500   -1.609  -50.147  1.00 84.21  ?  92  LEU B CD1 1 
ATOM   5082 C  CD2 . LEU B 1 94  ? 9.776   -3.690  -49.595  1.00 86.52  ?  92  LEU B CD2 1 
ATOM   5083 N  N   . TYR B 1 95  ? 10.877  -2.380  -45.649  1.00 82.58  ?  93  TYR B N   1 
ATOM   5084 C  CA  . TYR B 1 95  ? 11.644  -1.746  -44.574  1.00 84.51  ?  93  TYR B CA  1 
ATOM   5085 C  C   . TYR B 1 95  ? 11.704  -2.623  -43.325  1.00 87.93  ?  93  TYR B C   1 
ATOM   5086 O  O   . TYR B 1 95  ? 11.791  -2.123  -42.200  1.00 88.27  ?  93  TYR B O   1 
ATOM   5087 C  CB  . TYR B 1 95  ? 11.098  -0.353  -44.251  1.00 87.77  ?  93  TYR B CB  1 
ATOM   5088 C  CG  . TYR B 1 95  ? 10.823  0.476   -45.487  1.00 89.65  ?  93  TYR B CG  1 
ATOM   5089 C  CD1 . TYR B 1 95  ? 11.835  1.223   -46.079  1.00 93.22  ?  93  TYR B CD1 1 
ATOM   5090 C  CD2 . TYR B 1 95  ? 9.560   0.511   -46.063  1.00 89.87  ?  93  TYR B CD2 1 
ATOM   5091 C  CE1 . TYR B 1 95  ? 11.597  1.983   -47.207  1.00 97.76  ?  93  TYR B CE1 1 
ATOM   5092 C  CE2 . TYR B 1 95  ? 9.313   1.268   -47.194  1.00 92.65  ?  93  TYR B CE2 1 
ATOM   5093 C  CZ  . TYR B 1 95  ? 10.335  2.002   -47.761  1.00 94.06  ?  93  TYR B CZ  1 
ATOM   5094 O  OH  . TYR B 1 95  ? 10.099  2.755   -48.888  1.00 103.79 ?  93  TYR B OH  1 
ATOM   5095 N  N   . LYS B 1 96  ? 11.671  -3.944  -43.519  1.00 84.29  ?  94  LYS B N   1 
ATOM   5096 C  CA  . LYS B 1 96  ? 11.699  -4.898  -42.415  1.00 84.25  ?  94  LYS B CA  1 
ATOM   5097 C  C   . LYS B 1 96  ? 13.009  -4.860  -41.643  1.00 90.80  ?  94  LYS B C   1 
ATOM   5098 O  O   . LYS B 1 96  ? 13.183  -5.646  -40.704  1.00 92.05  ?  94  LYS B O   1 
ATOM   5099 C  CB  . LYS B 1 96  ? 11.447  -6.314  -42.936  1.00 80.46  ?  94  LYS B CB  1 
ATOM   5100 N  N   . ASN B 1 97  ? 13.924  -3.969  -42.020  1.00 89.22  ?  95  ASN B N   1 
ATOM   5101 C  CA  . ASN B 1 97  ? 15.242  -3.854  -41.414  1.00 91.82  ?  95  ASN B CA  1 
ATOM   5102 C  C   . ASN B 1 97  ? 15.401  -2.598  -40.578  1.00 96.72  ?  95  ASN B C   1 
ATOM   5103 O  O   . ASN B 1 97  ? 16.210  -2.586  -39.648  1.00 100.02 ?  95  ASN B O   1 
ATOM   5104 C  CB  . ASN B 1 97  ? 16.327  -3.873  -42.499  1.00 99.12  ?  95  ASN B CB  1 
ATOM   5105 C  CG  . ASN B 1 97  ? 15.899  -3.149  -43.764  1.00 103.04 ?  95  ASN B CG  1 
ATOM   5106 O  OD1 . ASN B 1 97  ? 14.926  -3.535  -44.414  1.00 94.87  ?  95  ASN B OD1 1 
ATOM   5107 N  ND2 . ASN B 1 97  ? 16.630  -2.099  -44.123  1.00 106.88 ?  95  ASN B ND2 1 
ATOM   5108 N  N   . THR B 1 98  ? 14.654  -1.540  -40.894  1.00 89.99  ?  96  THR B N   1 
ATOM   5109 C  CA  . THR B 1 98  ? 14.752  -0.264  -40.201  1.00 93.28  ?  96  THR B CA  1 
ATOM   5110 C  C   . THR B 1 98  ? 13.522  0.009   -39.340  1.00 92.66  ?  96  THR B C   1 
ATOM   5111 O  O   . THR B 1 98  ? 13.184  1.166   -39.076  1.00 90.15  ?  96  THR B O   1 
ATOM   5112 C  CB  . THR B 1 98  ? 14.960  0.868   -41.207  1.00 99.77  ?  96  THR B CB  1 
ATOM   5113 O  OG1 . THR B 1 98  ? 14.850  2.133   -40.543  1.00 105.49 ?  96  THR B OG1 1 
ATOM   5114 C  CG2 . THR B 1 98  ? 13.923  0.787   -42.320  1.00 95.26  ?  96  THR B CG2 1 
ATOM   5115 N  N   . CYS B 1 99  ? 12.850  -1.048  -38.886  1.00 91.66  ?  97  CYS B N   1 
ATOM   5116 C  CA  . CYS B 1 99  ? 11.704  -0.914  -37.996  1.00 82.63  ?  97  CYS B CA  1 
ATOM   5117 C  C   . CYS B 1 99  ? 12.193  -1.052  -36.558  1.00 86.73  ?  97  CYS B C   1 
ATOM   5118 O  O   . CYS B 1 99  ? 12.808  -2.061  -36.197  1.00 89.28  ?  97  CYS B O   1 
ATOM   5119 C  CB  . CYS B 1 99  ? 10.616  -1.941  -38.326  1.00 80.53  ?  97  CYS B CB  1 
ATOM   5120 S  SG  . CYS B 1 99  ? 10.774  -3.584  -37.581  1.00 102.11 ?  97  CYS B SG  1 
ATOM   5121 N  N   . VAL B 1 100 ? 11.944  -0.022  -35.750  1.00 82.79  ?  98  VAL B N   1 
ATOM   5122 C  CA  . VAL B 1 100 ? 12.434  -0.010  -34.377  1.00 81.41  ?  98  VAL B CA  1 
ATOM   5123 C  C   . VAL B 1 100 ? 11.513  -0.815  -33.472  1.00 83.60  ?  98  VAL B C   1 
ATOM   5124 O  O   . VAL B 1 100 ? 11.957  -1.698  -32.730  1.00 79.25  ?  98  VAL B O   1 
ATOM   5125 C  CB  . VAL B 1 100 ? 12.575  1.440   -33.878  1.00 86.60  ?  98  VAL B CB  1 
ATOM   5126 C  CG1 . VAL B 1 100 ? 13.215  1.470   -32.497  1.00 91.21  ?  98  VAL B CG1 1 
ATOM   5127 C  CG2 . VAL B 1 100 ? 13.370  2.273   -34.870  1.00 92.76  ?  98  VAL B CG2 1 
ATOM   5128 N  N   . GLY B 1 101 ? 10.225  -0.515  -33.517  1.00 81.61  ?  99  GLY B N   1 
ATOM   5129 C  CA  . GLY B 1 101 ? 9.248   -1.187  -32.692  1.00 76.01  ?  99  GLY B CA  1 
ATOM   5130 C  C   . GLY B 1 101 ? 8.854   -0.332  -31.508  1.00 79.12  ?  99  GLY B C   1 
ATOM   5131 O  O   . GLY B 1 101 ? 9.148   0.864   -31.427  1.00 75.10  ?  99  GLY B O   1 
ATOM   5132 N  N   . SER B 1 102 ? 8.184   -0.978  -30.560  1.00 73.26  ?  100 SER B N   1 
ATOM   5133 C  CA  . SER B 1 102 ? 7.703   -0.287  -29.375  1.00 79.72  ?  100 SER B CA  1 
ATOM   5134 C  C   . SER B 1 102 ? 7.385   -1.323  -28.310  1.00 84.54  ?  100 SER B C   1 
ATOM   5135 O  O   . SER B 1 102 ? 6.792   -2.363  -28.608  1.00 86.25  ?  100 SER B O   1 
ATOM   5136 C  CB  . SER B 1 102 ? 6.465   0.563   -29.688  1.00 82.84  ?  100 SER B CB  1 
ATOM   5137 O  OG  . SER B 1 102 ? 5.949   1.173   -28.517  1.00 93.44  ?  100 SER B OG  1 
ATOM   5138 N  N   . ASP B 1 103 ? 7.788   -1.035  -27.074  1.00 90.24  ?  101 ASP B N   1 
ATOM   5139 C  CA  . ASP B 1 103 ? 7.619   -1.995  -25.993  1.00 87.59  ?  101 ASP B CA  1 
ATOM   5140 C  C   . ASP B 1 103 ? 6.227   -1.940  -25.384  1.00 88.01  ?  101 ASP B C   1 
ATOM   5141 O  O   . ASP B 1 103 ? 5.881   -2.817  -24.585  1.00 96.43  ?  101 ASP B O   1 
ATOM   5142 C  CB  . ASP B 1 103 ? 8.667   -1.755  -24.903  1.00 87.32  ?  101 ASP B CB  1 
ATOM   5143 N  N   . ASN B 1 104 ? 5.429   -0.937  -25.744  1.00 83.60  ?  102 ASN B N   1 
ATOM   5144 C  CA  . ASN B 1 104 ? 4.082   -0.758  -25.208  1.00 85.05  ?  102 ASN B CA  1 
ATOM   5145 C  C   . ASN B 1 104 ? 3.112   -0.542  -26.366  1.00 85.63  ?  102 ASN B C   1 
ATOM   5146 O  O   . ASN B 1 104 ? 3.028   0.558   -26.921  1.00 85.30  ?  102 ASN B O   1 
ATOM   5147 C  CB  . ASN B 1 104 ? 4.034   0.409   -24.227  1.00 74.54  ?  102 ASN B CB  1 
ATOM   5148 N  N   . VAL B 1 105 ? 2.372   -1.592  -26.716  1.00 82.24  ?  103 VAL B N   1 
ATOM   5149 C  CA  . VAL B 1 105 ? 1.327   -1.526  -27.729  1.00 72.29  ?  103 VAL B CA  1 
ATOM   5150 C  C   . VAL B 1 105 ? -0.049  -1.612  -27.104  1.00 63.80  ?  103 VAL B C   1 
ATOM   5151 O  O   . VAL B 1 105 ? -1.061  -1.474  -27.807  1.00 63.25  ?  103 VAL B O   1 
ATOM   5152 C  CB  . VAL B 1 105 ? 1.511   -2.629  -28.791  1.00 67.91  ?  103 VAL B CB  1 
ATOM   5153 C  CG1 . VAL B 1 105 ? 0.516   -2.463  -29.931  1.00 66.81  ?  103 VAL B CG1 1 
ATOM   5154 C  CG2 . VAL B 1 105 ? 2.938   -2.623  -29.317  1.00 71.31  ?  103 VAL B CG2 1 
ATOM   5155 N  N   . THR B 1 106 ? -0.109  -1.799  -25.783  1.00 64.73  ?  104 THR B N   1 
ATOM   5156 C  CA  . THR B 1 106 ? -1.371  -1.963  -25.071  1.00 62.73  ?  104 THR B CA  1 
ATOM   5157 C  C   . THR B 1 106 ? -2.306  -0.778  -25.283  1.00 65.94  ?  104 THR B C   1 
ATOM   5158 O  O   . THR B 1 106 ? -3.514  -0.961  -25.470  1.00 66.03  ?  104 THR B O   1 
ATOM   5159 C  CB  . THR B 1 106 ? -1.091  -2.161  -23.582  1.00 64.24  ?  104 THR B CB  1 
ATOM   5160 O  OG1 . THR B 1 106 ? -0.215  -1.123  -23.123  1.00 84.93  ?  104 THR B OG1 1 
ATOM   5161 C  CG2 . THR B 1 106 ? -0.425  -3.507  -23.344  1.00 67.93  ?  104 THR B CG2 1 
ATOM   5162 N  N   . ASP B 1 107 ? -1.772  0.447   -25.251  1.00 63.15  ?  105 ASP B N   1 
ATOM   5163 C  CA  . ASP B 1 107 ? -2.638  1.618   -25.367  1.00 59.29  ?  105 ASP B CA  1 
ATOM   5164 C  C   . ASP B 1 107 ? -3.160  1.785   -26.787  1.00 54.63  ?  105 ASP B C   1 
ATOM   5165 O  O   . ASP B 1 107 ? -4.327  2.144   -26.982  1.00 51.85  ?  105 ASP B O   1 
ATOM   5166 C  CB  . ASP B 1 107 ? -1.904  2.877   -24.908  1.00 59.54  ?  105 ASP B CB  1 
ATOM   5167 C  CG  . ASP B 1 107 ? -1.639  2.882   -23.417  1.00 67.89  ?  105 ASP B CG  1 
ATOM   5168 O  OD1 . ASP B 1 107 ? -2.023  1.902   -22.744  1.00 75.21  ?  105 ASP B OD1 1 
ATOM   5169 O  OD2 . ASP B 1 107 ? -1.060  3.869   -22.916  1.00 67.66  -1 105 ASP B OD2 1 
ATOM   5170 N  N   . PHE B 1 108 ? -2.310  1.570   -27.794  1.00 55.48  ?  106 PHE B N   1 
ATOM   5171 C  CA  . PHE B 1 108 ? -2.807  1.620   -29.163  1.00 52.38  ?  106 PHE B CA  1 
ATOM   5172 C  C   . PHE B 1 108 ? -3.930  0.610   -29.355  1.00 49.97  ?  106 PHE B C   1 
ATOM   5173 O  O   . PHE B 1 108 ? -4.963  0.922   -29.958  1.00 49.59  ?  106 PHE B O   1 
ATOM   5174 C  CB  . PHE B 1 108 ? -1.678  1.365   -30.162  1.00 51.06  ?  106 PHE B CB  1 
ATOM   5175 C  CG  . PHE B 1 108 ? -2.151  1.238   -31.585  1.00 49.71  ?  106 PHE B CG  1 
ATOM   5176 C  CD1 . PHE B 1 108 ? -2.299  2.364   -32.379  1.00 46.96  ?  106 PHE B CD1 1 
ATOM   5177 C  CD2 . PHE B 1 108 ? -2.451  -0.002  -32.128  1.00 53.15  ?  106 PHE B CD2 1 
ATOM   5178 C  CE1 . PHE B 1 108 ? -2.739  2.258   -33.687  1.00 46.30  ?  106 PHE B CE1 1 
ATOM   5179 C  CE2 . PHE B 1 108 ? -2.891  -0.116  -33.437  1.00 52.16  ?  106 PHE B CE2 1 
ATOM   5180 C  CZ  . PHE B 1 108 ? -3.035  1.017   -34.217  1.00 50.27  ?  106 PHE B CZ  1 
ATOM   5181 N  N   . ASN B 1 109 ? -3.749  -0.605  -28.829  1.00 55.11  ?  107 ASN B N   1 
ATOM   5182 C  CA  . ASN B 1 109 ? -4.763  -1.643  -28.980  1.00 55.07  ?  107 ASN B CA  1 
ATOM   5183 C  C   . ASN B 1 109 ? -6.093  -1.198  -28.387  1.00 54.30  ?  107 ASN B C   1 
ATOM   5184 O  O   . ASN B 1 109 ? -7.152  -1.412  -28.987  1.00 55.63  ?  107 ASN B O   1 
ATOM   5185 C  CB  . ASN B 1 109 ? -4.288  -2.937  -28.318  1.00 54.87  ?  107 ASN B CB  1 
ATOM   5186 C  CG  . ASN B 1 109 ? -3.232  -3.658  -29.133  1.00 59.55  ?  107 ASN B CG  1 
ATOM   5187 O  OD1 . ASN B 1 109 ? -3.009  -3.342  -30.302  1.00 61.16  ?  107 ASN B OD1 1 
ATOM   5188 N  ND2 . ASN B 1 109 ? -2.573  -4.632  -28.517  1.00 65.06  ?  107 ASN B ND2 1 
ATOM   5189 N  N   . ALA B 1 110 ? -6.058  -0.578  -27.206  1.00 51.96  ?  108 ALA B N   1 
ATOM   5190 C  CA  . ALA B 1 110 ? -7.294  -0.161  -26.554  1.00 55.53  ?  108 ALA B CA  1 
ATOM   5191 C  C   . ALA B 1 110 ? -7.996  0.910   -27.376  1.00 54.24  ?  108 ALA B C   1 
ATOM   5192 O  O   . ALA B 1 110 ? -9.208  0.840   -27.611  1.00 54.31  ?  108 ALA B O   1 
ATOM   5193 C  CB  . ALA B 1 110 ? -7.000  0.343   -25.141  1.00 51.41  ?  108 ALA B CB  1 
ATOM   5194 N  N   . ILE B 1 111 ? -7.238  1.908   -27.835  1.00 46.46  ?  109 ILE B N   1 
ATOM   5195 C  CA  . ILE B 1 111 ? -7.816  2.974   -28.643  1.00 46.60  ?  109 ILE B CA  1 
ATOM   5196 C  C   . ILE B 1 111 ? -8.408  2.405   -29.921  1.00 47.02  ?  109 ILE B C   1 
ATOM   5197 O  O   . ILE B 1 111 ? -9.431  2.893   -30.416  1.00 43.58  ?  109 ILE B O   1 
ATOM   5198 C  CB  . ILE B 1 111 ? -6.747  4.042   -28.950  1.00 46.75  ?  109 ILE B CB  1 
ATOM   5199 C  CG1 . ILE B 1 111 ? -6.258  4.701   -27.658  1.00 45.99  ?  109 ILE B CG1 1 
ATOM   5200 C  CG2 . ILE B 1 111 ? -7.292  5.077   -29.921  1.00 39.63  ?  109 ILE B CG2 1 
ATOM   5201 C  CD1 . ILE B 1 111 ? -4.972  5.486   -27.822  1.00 43.59  ?  109 ILE B CD1 1 
ATOM   5202 N  N   . ALA B 1 112 ? -7.789  1.358   -30.468  1.00 50.38  ?  110 ALA B N   1 
ATOM   5203 C  CA  . ALA B 1 112 ? -8.218  0.810   -31.746  1.00 51.53  ?  110 ALA B CA  1 
ATOM   5204 C  C   . ALA B 1 112 ? -9.422  -0.111  -31.622  1.00 55.46  ?  110 ALA B C   1 
ATOM   5205 O  O   . ALA B 1 112 ? -10.109 -0.340  -32.623  1.00 52.80  ?  110 ALA B O   1 
ATOM   5206 C  CB  . ALA B 1 112 ? -7.062  0.056   -32.408  1.00 51.71  ?  110 ALA B CB  1 
ATOM   5207 N  N   . THR B 1 113 ? -9.704  -0.634  -30.426  1.00 51.98  ?  111 THR B N   1 
ATOM   5208 C  CA  . THR B 1 113 ? -10.767 -1.615  -30.257  1.00 52.34  ?  111 THR B CA  1 
ATOM   5209 C  C   . THR B 1 113 ? -11.950 -1.108  -29.444  1.00 52.70  ?  111 THR B C   1 
ATOM   5210 O  O   . THR B 1 113 ? -12.966 -1.808  -29.367  1.00 55.19  ?  111 THR B O   1 
ATOM   5211 C  CB  . THR B 1 113 ? -10.223 -2.888  -29.590  1.00 51.36  ?  111 THR B CB  1 
ATOM   5212 O  OG1 . THR B 1 113 ? -9.569  -2.546  -28.362  1.00 60.95  ?  111 THR B OG1 1 
ATOM   5213 C  CG2 . THR B 1 113 ? -9.234  -3.593  -30.508  1.00 50.56  ?  111 THR B CG2 1 
ATOM   5214 N  N   . CYS B 1 114 ? -11.853 0.068   -28.832  1.00 49.80  ?  112 CYS B N   1 
ATOM   5215 C  CA  . CYS B 1 114 ? -12.927 0.537   -27.971  1.00 48.45  ?  112 CYS B CA  1 
ATOM   5216 C  C   . CYS B 1 114 ? -14.083 1.076   -28.813  1.00 49.90  ?  112 CYS B C   1 
ATOM   5217 O  O   . CYS B 1 114 ? -13.918 1.441   -29.980  1.00 55.16  ?  112 CYS B O   1 
ATOM   5218 C  CB  . CYS B 1 114 ? -12.421 1.608   -27.002  1.00 47.96  ?  112 CYS B CB  1 
ATOM   5219 S  SG  . CYS B 1 114 ? -11.955 3.173   -27.770  1.00 48.36  ?  112 CYS B SG  1 
ATOM   5220 N  N   . ASP B 1 115 ? -15.265 1.136   -28.200  1.00 48.09  ?  113 ASP B N   1 
ATOM   5221 C  CA  . ASP B 1 115 ? -16.462 1.633   -28.868  1.00 37.48  ?  113 ASP B CA  1 
ATOM   5222 C  C   . ASP B 1 115 ? -16.783 3.075   -28.494  1.00 40.24  ?  113 ASP B C   1 
ATOM   5223 O  O   . ASP B 1 115 ? -17.791 3.616   -28.959  1.00 41.73  ?  113 ASP B O   1 
ATOM   5224 C  CB  . ASP B 1 115 ? -17.659 0.724   -28.569  1.00 46.27  ?  113 ASP B CB  1 
ATOM   5225 C  CG  . ASP B 1 115 ? -17.908 0.551   -27.088  1.00 41.89  ?  113 ASP B CG  1 
ATOM   5226 O  OD1 . ASP B 1 115 ? -17.174 1.161   -26.285  1.00 47.76  ?  113 ASP B OD1 1 
ATOM   5227 O  OD2 . ASP B 1 115 ? -18.835 -0.206  -26.729  1.00 62.21  -1 113 ASP B OD2 1 
ATOM   5228 N  N   . TRP B 1 116 ? -15.968 3.688   -27.636  1.00 41.43  ?  114 TRP B N   1 
ATOM   5229 C  CA  . TRP B 1 116 ? -16.121 5.081   -27.212  1.00 36.49  ?  114 TRP B CA  1 
ATOM   5230 C  C   . TRP B 1 116 ? -17.421 5.344   -26.452  1.00 46.49  ?  114 TRP B C   1 
ATOM   5231 O  O   . TRP B 1 116 ? -17.928 6.470   -26.448  1.00 39.10  ?  114 TRP B O   1 
ATOM   5232 C  CB  . TRP B 1 116 ? -15.985 6.023   -28.411  1.00 41.55  ?  114 TRP B CB  1 
ATOM   5233 C  CG  . TRP B 1 116 ? -14.673 5.827   -29.111  1.00 38.67  ?  114 TRP B CG  1 
ATOM   5234 C  CD1 . TRP B 1 116 ? -14.439 5.065   -30.219  1.00 41.06  ?  114 TRP B CD1 1 
ATOM   5235 C  CD2 . TRP B 1 116 ? -13.403 6.360   -28.716  1.00 41.59  ?  114 TRP B CD2 1 
ATOM   5236 N  NE1 . TRP B 1 116 ? -13.107 5.110   -30.552  1.00 46.60  ?  114 TRP B NE1 1 
ATOM   5237 C  CE2 . TRP B 1 116 ? -12.449 5.898   -29.645  1.00 42.91  ?  114 TRP B CE2 1 
ATOM   5238 C  CE3 . TRP B 1 116 ? -12.982 7.193   -27.675  1.00 39.76  ?  114 TRP B CE3 1 
ATOM   5239 C  CZ2 . TRP B 1 116 ? -11.102 6.240   -29.562  1.00 41.29  ?  114 TRP B CZ2 1 
ATOM   5240 C  CZ3 . TRP B 1 116 ? -11.644 7.530   -27.594  1.00 41.79  ?  114 TRP B CZ3 1 
ATOM   5241 C  CH2 . TRP B 1 116 ? -10.720 7.054   -28.532  1.00 45.99  ?  114 TRP B CH2 1 
ATOM   5242 N  N   . THR B 1 117 ? -17.961 4.321   -25.783  1.00 41.65  ?  115 THR B N   1 
ATOM   5243 C  CA  . THR B 1 117 ? -19.185 4.473   -25.003  1.00 48.00  ?  115 THR B CA  1 
ATOM   5244 C  C   . THR B 1 117 ? -18.908 4.697   -23.523  1.00 49.30  ?  115 THR B C   1 
ATOM   5245 O  O   . THR B 1 117 ? -19.818 5.100   -22.789  1.00 53.64  ?  115 THR B O   1 
ATOM   5246 C  CB  . THR B 1 117 ? -20.104 3.252   -25.163  1.00 43.40  ?  115 THR B CB  1 
ATOM   5247 O  OG1 . THR B 1 117 ? -19.475 2.093   -24.604  1.00 50.04  ?  115 THR B OG1 1 
ATOM   5248 C  CG2 . THR B 1 117 ? -20.420 3.002   -26.632  1.00 45.69  ?  115 THR B CG2 1 
ATOM   5249 N  N   . ASN B 1 118 ? -17.686 4.425   -23.070  1.00 46.24  ?  116 ASN B N   1 
ATOM   5250 C  CA  . ASN B 1 118 ? -17.284 4.585   -21.682  1.00 44.50  ?  116 ASN B CA  1 
ATOM   5251 C  C   . ASN B 1 118 ? -16.330 5.763   -21.546  1.00 48.97  ?  116 ASN B C   1 
ATOM   5252 O  O   . ASN B 1 118 ? -15.583 6.093   -22.472  1.00 46.35  ?  116 ASN B O   1 
ATOM   5253 C  CB  . ASN B 1 118 ? -16.599 3.323   -21.152  1.00 54.08  ?  116 ASN B CB  1 
ATOM   5254 C  CG  . ASN B 1 118 ? -17.464 2.094   -21.276  1.00 58.04  ?  116 ASN B CG  1 
ATOM   5255 O  OD1 . ASN B 1 118 ? -18.538 2.016   -20.684  1.00 66.26  ?  116 ASN B OD1 1 
ATOM   5256 N  ND2 . ASN B 1 118 ? -17.002 1.122   -22.053  1.00 66.08  ?  116 ASN B ND2 1 
ATOM   5257 N  N   . ALA B 1 119 ? -16.355 6.391   -20.370  1.00 45.79  ?  117 ALA B N   1 
ATOM   5258 C  CA  . ALA B 1 119 ? -15.528 7.572   -20.160  1.00 44.18  ?  117 ALA B CA  1 
ATOM   5259 C  C   . ALA B 1 119 ? -14.049 7.214   -20.094  1.00 45.04  ?  117 ALA B C   1 
ATOM   5260 O  O   . ALA B 1 119 ? -13.198 8.051   -20.416  1.00 42.09  ?  117 ALA B O   1 
ATOM   5261 C  CB  . ALA B 1 119 ? -15.961 8.297   -18.886  1.00 48.24  ?  117 ALA B CB  1 
ATOM   5262 N  N   . GLY B 1 120 ? -13.724 5.982   -19.694  1.00 40.40  ?  118 GLY B N   1 
ATOM   5263 C  CA  . GLY B 1 120 ? -12.331 5.566   -19.672  1.00 38.44  ?  118 GLY B CA  1 
ATOM   5264 C  C   . GLY B 1 120 ? -11.664 5.634   -21.032  1.00 43.57  ?  118 GLY B C   1 
ATOM   5265 O  O   . GLY B 1 120 ? -10.442 5.786   -21.122  1.00 44.55  ?  118 GLY B O   1 
ATOM   5266 N  N   . ASP B 1 121 ? -12.450 5.539   -22.107  1.00 39.97  ?  119 ASP B N   1 
ATOM   5267 C  CA  . ASP B 1 121 ? -11.871 5.628   -23.442  1.00 43.46  ?  119 ASP B CA  1 
ATOM   5268 C  C   . ASP B 1 121 ? -11.347 7.033   -23.698  1.00 43.75  ?  119 ASP B C   1 
ATOM   5269 O  O   . ASP B 1 121 ? -10.292 7.214   -24.317  1.00 38.06  ?  119 ASP B O   1 
ATOM   5270 C  CB  . ASP B 1 121 ? -12.910 5.235   -24.491  1.00 41.30  ?  119 ASP B CB  1 
ATOM   5271 C  CG  . ASP B 1 121 ? -13.398 3.811   -24.324  1.00 44.34  ?  119 ASP B CG  1 
ATOM   5272 O  OD1 . ASP B 1 121 ? -12.780 3.055   -23.545  1.00 50.69  ?  119 ASP B OD1 1 
ATOM   5273 O  OD2 . ASP B 1 121 ? -14.407 3.449   -24.966  1.00 49.24  -1 119 ASP B OD2 1 
ATOM   5274 N  N   . TYR B 1 122 ? -12.081 8.037   -23.222  1.00 41.34  ?  120 TYR B N   1 
ATOM   5275 C  CA  . TYR B 1 122 ? -11.708 9.430   -23.406  1.00 38.32  ?  120 TYR B CA  1 
ATOM   5276 C  C   . TYR B 1 122 ? -10.561 9.810   -22.482  1.00 41.80  ?  120 TYR B C   1 
ATOM   5277 O  O   . TYR B 1 122 ? -9.707  10.620  -22.858  1.00 40.08  ?  120 TYR B O   1 
ATOM   5278 C  CB  . TYR B 1 122 ? -12.936 10.310  -23.167  1.00 35.72  ?  120 TYR B CB  1 
ATOM   5279 C  CG  . TYR B 1 122 ? -14.037 10.009  -24.159  1.00 37.71  ?  120 TYR B CG  1 
ATOM   5280 C  CD1 . TYR B 1 122 ? -14.961 9.002   -23.909  1.00 37.03  ?  120 TYR B CD1 1 
ATOM   5281 C  CD2 . TYR B 1 122 ? -14.142 10.713  -25.352  1.00 38.51  ?  120 TYR B CD2 1 
ATOM   5282 C  CE1 . TYR B 1 122 ? -15.960 8.704   -24.813  1.00 36.71  ?  120 TYR B CE1 1 
ATOM   5283 C  CE2 . TYR B 1 122 ? -15.144 10.423  -26.265  1.00 37.59  ?  120 TYR B CE2 1 
ATOM   5284 C  CZ  . TYR B 1 122 ? -16.050 9.419   -25.989  1.00 41.54  ?  120 TYR B CZ  1 
ATOM   5285 O  OH  . TYR B 1 122 ? -17.048 9.126   -26.893  1.00 41.36  ?  120 TYR B OH  1 
ATOM   5286 N  N   . ILE B 1 123 ? -10.535 9.238   -21.276  1.00 38.75  ?  121 ILE B N   1 
ATOM   5287 C  CA  . ILE B 1 123 ? -9.430  9.472   -20.351  1.00 39.26  ?  121 ILE B CA  1 
ATOM   5288 C  C   . ILE B 1 123 ? -8.120  8.982   -20.952  1.00 40.46  ?  121 ILE B C   1 
ATOM   5289 O  O   . ILE B 1 123 ? -7.089  9.662   -20.874  1.00 42.86  ?  121 ILE B O   1 
ATOM   5290 C  CB  . ILE B 1 123 ? -9.713  8.787   -19.002  1.00 39.28  ?  121 ILE B CB  1 
ATOM   5291 C  CG1 . ILE B 1 123 ? -10.981 9.354   -18.363  1.00 41.36  ?  121 ILE B CG1 1 
ATOM   5292 C  CG2 . ILE B 1 123 ? -8.519  8.940   -18.075  1.00 41.63  ?  121 ILE B CG2 1 
ATOM   5293 C  CD1 . ILE B 1 123 ? -11.378 8.655   -17.074  1.00 43.14  ?  121 ILE B CD1 1 
ATOM   5294 N  N   . LEU B 1 124 ? -8.133  7.787   -21.548  1.00 37.32  ?  122 LEU B N   1 
ATOM   5295 C  CA  . LEU B 1 124 ? -6.919  7.254   -22.157  1.00 39.87  ?  122 LEU B CA  1 
ATOM   5296 C  C   . LEU B 1 124 ? -6.506  8.089   -23.362  1.00 43.02  ?  122 LEU B C   1 
ATOM   5297 O  O   . LEU B 1 124 ? -5.311  8.300   -23.602  1.00 43.35  ?  122 LEU B O   1 
ATOM   5298 C  CB  . LEU B 1 124 ? -7.131  5.794   -22.555  1.00 38.36  ?  122 LEU B CB  1 
ATOM   5299 C  CG  . LEU B 1 124 ? -6.038  5.123   -23.389  1.00 49.28  ?  122 LEU B CG  1 
ATOM   5300 C  CD1 . LEU B 1 124 ? -4.719  5.078   -22.632  1.00 47.21  ?  122 LEU B CD1 1 
ATOM   5301 C  CD2 . LEU B 1 124 ? -6.478  3.722   -23.786  1.00 44.02  ?  122 LEU B CD2 1 
ATOM   5302 N  N   . ALA B 1 125 ? -7.482  8.580   -24.126  1.00 39.78  ?  123 ALA B N   1 
ATOM   5303 C  CA  . ALA B 1 125 ? -7.183  9.347   -25.324  1.00 45.10  ?  123 ALA B CA  1 
ATOM   5304 C  C   . ALA B 1 125 ? -6.574  10.700  -24.994  1.00 37.93  ?  123 ALA B C   1 
ATOM   5305 O  O   . ALA B 1 125 ? -6.144  11.410  -25.910  1.00 41.75  ?  123 ALA B O   1 
ATOM   5306 C  CB  . ALA B 1 125 ? -8.451  9.532   -26.160  1.00 46.45  ?  123 ALA B CB  1 
ATOM   5307 N  N   . ASN B 1 126 ? -6.525  11.064  -23.712  1.00 42.35  ?  124 ASN B N   1 
ATOM   5308 C  CA  . ASN B 1 126 ? -5.965  12.332  -23.266  1.00 47.23  ?  124 ASN B CA  1 
ATOM   5309 C  C   . ASN B 1 126 ? -4.784  12.146  -22.321  1.00 44.35  ?  124 ASN B C   1 
ATOM   5310 O  O   . ASN B 1 126 ? -4.277  13.132  -21.775  1.00 47.34  ?  124 ASN B O   1 
ATOM   5311 C  CB  . ASN B 1 126 ? -7.051  13.180  -22.605  1.00 42.69  ?  124 ASN B CB  1 
ATOM   5312 C  CG  . ASN B 1 126 ? -7.666  14.170  -23.563  1.00 45.24  ?  124 ASN B CG  1 
ATOM   5313 O  OD1 . ASN B 1 126 ? -7.058  15.188  -23.896  1.00 44.14  ?  124 ASN B OD1 1 
ATOM   5314 N  ND2 . ASN B 1 126 ? -8.867  13.863  -24.040  1.00 50.88  ?  124 ASN B ND2 1 
ATOM   5315 N  N   . THR B 1 127 ? -4.336  10.908  -22.117  1.00 43.21  ?  125 THR B N   1 
ATOM   5316 C  CA  . THR B 1 127 ? -3.227  10.612  -21.224  1.00 46.02  ?  125 THR B CA  1 
ATOM   5317 C  C   . THR B 1 127 ? -2.124  9.827   -21.914  1.00 47.30  ?  125 THR B C   1 
ATOM   5318 O  O   . THR B 1 127 ? -1.074  9.604   -21.304  1.00 54.14  ?  125 THR B O   1 
ATOM   5319 C  CB  . THR B 1 127 ? -3.704  9.830   -19.989  1.00 48.45  ?  125 THR B CB  1 
ATOM   5320 O  OG1 . THR B 1 127 ? -4.411  8.656   -20.405  1.00 42.46  ?  125 THR B OG1 1 
ATOM   5321 C  CG2 . THR B 1 127 ? -4.615  10.693  -19.124  1.00 49.09  ?  125 THR B CG2 1 
ATOM   5322 N  N   . CYS B 1 128 ? -2.329  9.408   -23.157  1.00 51.37  ?  126 CYS B N   1 
ATOM   5323 C  CA  . CYS B 1 128 ? -1.354  8.630   -23.907  1.00 53.93  ?  126 CYS B CA  1 
ATOM   5324 C  C   . CYS B 1 128 ? -0.334  9.573   -24.543  1.00 59.64  ?  126 CYS B C   1 
ATOM   5325 O  O   . CYS B 1 128 ? -0.265  10.763  -24.226  1.00 55.29  ?  126 CYS B O   1 
ATOM   5326 C  CB  . CYS B 1 128 ? -2.064  7.779   -24.954  1.00 49.77  ?  126 CYS B CB  1 
ATOM   5327 S  SG  . CYS B 1 128 ? -3.148  8.734   -26.054  1.00 45.86  ?  126 CYS B SG  1 
ATOM   5328 N  N   . THR B 1 129 ? 0.468   9.045   -25.462  1.00 62.28  ?  127 THR B N   1 
ATOM   5329 C  CA  . THR B 1 129 ? 1.446   9.852   -26.176  1.00 61.29  ?  127 THR B CA  1 
ATOM   5330 C  C   . THR B 1 129 ? 0.764   10.730  -27.221  1.00 55.33  ?  127 THR B C   1 
ATOM   5331 O  O   . THR B 1 129 ? -0.367  10.475  -27.646  1.00 55.04  ?  127 THR B O   1 
ATOM   5332 C  CB  . THR B 1 129 ? 2.488   8.965   -26.855  1.00 61.88  ?  127 THR B CB  1 
ATOM   5333 O  OG1 . THR B 1 129 ? 1.837   8.068   -27.762  1.00 59.99  ?  127 THR B OG1 1 
ATOM   5334 C  CG2 . THR B 1 129 ? 3.257   8.162   -25.820  1.00 63.30  ?  127 THR B CG2 1 
ATOM   5335 N  N   . GLU B 1 130 ? 1.474   11.784  -27.632  1.00 52.07  ?  128 GLU B N   1 
ATOM   5336 C  CA  . GLU B 1 130 ? 0.882   12.766  -28.533  1.00 53.64  ?  128 GLU B CA  1 
ATOM   5337 C  C   . GLU B 1 130 ? 0.389   12.109  -29.817  1.00 48.88  ?  128 GLU B C   1 
ATOM   5338 O  O   . GLU B 1 130 ? -0.706  12.421  -30.299  1.00 43.76  ?  128 GLU B O   1 
ATOM   5339 C  CB  . GLU B 1 130 ? 1.897   13.866  -28.841  1.00 54.37  ?  128 GLU B CB  1 
ATOM   5340 C  CG  . GLU B 1 130 ? 1.315   15.116  -29.487  1.00 59.10  ?  128 GLU B CG  1 
ATOM   5341 C  CD  . GLU B 1 130 ? 0.253   15.782  -28.630  1.00 53.19  ?  128 GLU B CD  1 
ATOM   5342 O  OE1 . GLU B 1 130 ? 0.520   16.031  -27.435  1.00 52.07  ?  128 GLU B OE1 1 
ATOM   5343 O  OE2 . GLU B 1 130 ? -0.840  16.078  -29.159  1.00 48.33  -1 128 GLU B OE2 1 
ATOM   5344 N  N   . ARG B 1 131 ? 1.174   11.185  -30.383  1.00 49.84  ?  129 ARG B N   1 
ATOM   5345 C  CA  . ARG B 1 131 ? 0.771   10.603  -31.660  1.00 51.06  ?  129 ARG B CA  1 
ATOM   5346 C  C   . ARG B 1 131 ? -0.436  9.702   -31.462  1.00 47.91  ?  129 ARG B C   1 
ATOM   5347 O  O   . ARG B 1 131 ? -1.271  9.571   -32.363  1.00 45.14  ?  129 ARG B O   1 
ATOM   5348 C  CB  . ARG B 1 131 ? 1.908   9.816   -32.311  1.00 50.85  ?  129 ARG B CB  1 
ATOM   5349 C  CG  . ARG B 1 131 ? 1.548   9.271   -33.706  1.00 59.26  ?  129 ARG B CG  1 
ATOM   5350 C  CD  . ARG B 1 131 ? 1.238   10.429  -34.670  1.00 67.44  ?  129 ARG B CD  1 
ATOM   5351 N  NE  . ARG B 1 131 ? 0.530   10.060  -35.894  1.00 68.41  ?  129 ARG B NE  1 
ATOM   5352 C  CZ  . ARG B 1 131 ? -0.745  9.697   -35.969  1.00 62.88  ?  129 ARG B CZ  1 
ATOM   5353 N  NH1 . ARG B 1 131 ? -1.437  9.370   -34.890  1.00 57.82  ?  129 ARG B NH1 1 
ATOM   5354 N  NH2 . ARG B 1 131 ? -1.320  9.597   -37.164  1.00 74.14  ?  129 ARG B NH2 1 
ATOM   5355 N  N   . LEU B 1 132 ? -0.535  9.067   -30.293  1.00 49.96  ?  130 LEU B N   1 
ATOM   5356 C  CA  . LEU B 1 132 ? -1.716  8.272   -29.989  1.00 47.06  ?  130 LEU B CA  1 
ATOM   5357 C  C   . LEU B 1 132 ? -2.902  9.175   -29.684  1.00 42.89  ?  130 LEU B C   1 
ATOM   5358 O  O   . LEU B 1 132 ? -4.054  8.764   -29.869  1.00 44.60  ?  130 LEU B O   1 
ATOM   5359 C  CB  . LEU B 1 132 ? -1.432  7.319   -28.828  1.00 48.48  ?  130 LEU B CB  1 
ATOM   5360 C  CG  . LEU B 1 132 ? -0.626  6.075   -29.218  1.00 53.46  ?  130 LEU B CG  1 
ATOM   5361 C  CD1 . LEU B 1 132 ? -0.525  5.094   -28.058  1.00 49.31  ?  130 LEU B CD1 1 
ATOM   5362 C  CD2 . LEU B 1 132 ? -1.228  5.403   -30.446  1.00 45.00  ?  130 LEU B CD2 1 
ATOM   5363 N  N   . LYS B 1 133 ? -2.647  10.405  -29.225  1.00 43.15  ?  131 LYS B N   1 
ATOM   5364 C  CA  . LYS B 1 133 ? -3.743  11.354  -29.071  1.00 41.13  ?  131 LYS B CA  1 
ATOM   5365 C  C   . LYS B 1 133 ? -4.324  11.718  -30.431  1.00 39.96  ?  131 LYS B C   1 
ATOM   5366 O  O   . LYS B 1 133 ? -5.547  11.807  -30.587  1.00 43.58  ?  131 LYS B O   1 
ATOM   5367 C  CB  . LYS B 1 133 ? -3.270  12.622  -28.358  1.00 41.94  ?  131 LYS B CB  1 
ATOM   5368 C  CG  . LYS B 1 133 ? -2.922  12.480  -26.887  1.00 43.61  ?  131 LYS B CG  1 
ATOM   5369 C  CD  . LYS B 1 133 ? -2.568  13.849  -26.314  1.00 46.52  ?  131 LYS B CD  1 
ATOM   5370 C  CE  . LYS B 1 133 ? -2.254  13.793  -24.829  1.00 49.59  ?  131 LYS B CE  1 
ATOM   5371 N  NZ  . LYS B 1 133 ? -1.930  15.144  -24.289  1.00 49.93  ?  131 LYS B NZ  1 
ATOM   5372 N  N   . LEU B 1 134 ? -3.462  11.920  -31.430  1.00 38.77  ?  132 LEU B N   1 
ATOM   5373 C  CA  . LEU B 1 134 ? -3.956  12.172  -32.779  1.00 40.58  ?  132 LEU B CA  1 
ATOM   5374 C  C   . LEU B 1 134 ? -4.724  10.965  -33.302  1.00 41.52  ?  132 LEU B C   1 
ATOM   5375 O  O   . LEU B 1 134 ? -5.819  11.105  -33.859  1.00 39.48  ?  132 LEU B O   1 
ATOM   5376 C  CB  . LEU B 1 134 ? -2.794  12.522  -33.712  1.00 39.41  ?  132 LEU B CB  1 
ATOM   5377 C  CG  . LEU B 1 134 ? -1.894  13.678  -33.267  1.00 45.66  ?  132 LEU B CG  1 
ATOM   5378 C  CD1 . LEU B 1 134 ? -0.869  14.027  -34.344  1.00 48.16  ?  132 LEU B CD1 1 
ATOM   5379 C  CD2 . LEU B 1 134 ? -2.731  14.892  -32.893  1.00 39.16  ?  132 LEU B CD2 1 
ATOM   5380 N  N   . PHE B 1 135 ? -4.174  9.763   -33.111  1.00 38.34  ?  133 PHE B N   1 
ATOM   5381 C  CA  . PHE B 1 135 ? -4.849  8.561   -33.590  1.00 37.98  ?  133 PHE B CA  1 
ATOM   5382 C  C   . PHE B 1 135 ? -6.214  8.421   -32.930  1.00 39.15  ?  133 PHE B C   1 
ATOM   5383 O  O   . PHE B 1 135 ? -7.216  8.140   -33.598  1.00 41.51  ?  133 PHE B O   1 
ATOM   5384 C  CB  . PHE B 1 135 ? -3.984  7.323   -33.336  1.00 39.45  ?  133 PHE B CB  1 
ATOM   5385 C  CG  . PHE B 1 135 ? -4.653  6.025   -33.713  1.00 35.15  ?  133 PHE B CG  1 
ATOM   5386 C  CD1 . PHE B 1 135 ? -4.826  5.682   -35.045  1.00 34.86  ?  133 PHE B CD1 1 
ATOM   5387 C  CD2 . PHE B 1 135 ? -5.109  5.151   -32.740  1.00 42.28  ?  133 PHE B CD2 1 
ATOM   5388 C  CE1 . PHE B 1 135 ? -5.440  4.495   -35.400  1.00 42.28  ?  133 PHE B CE1 1 
ATOM   5389 C  CE2 . PHE B 1 135 ? -5.725  3.960   -33.090  1.00 38.37  ?  133 PHE B CE2 1 
ATOM   5390 C  CZ  . PHE B 1 135 ? -5.889  3.632   -34.421  1.00 45.56  ?  133 PHE B CZ  1 
ATOM   5391 N  N   . ALA B 1 136 ? -6.266  8.596   -31.606  1.00 31.67  ?  134 ALA B N   1 
ATOM   5392 C  CA  . ALA B 1 136 ? -7.533  8.470   -30.893  1.00 42.22  ?  134 ALA B CA  1 
ATOM   5393 C  C   . ALA B 1 136 ? -8.547  9.498   -31.384  1.00 41.95  ?  134 ALA B C   1 
ATOM   5394 O  O   . ALA B 1 136 ? -9.718  9.167   -31.606  1.00 41.89  ?  134 ALA B O   1 
ATOM   5395 C  CB  . ALA B 1 136 ? -7.304  8.610   -29.387  1.00 28.40  ?  134 ALA B CB  1 
ATOM   5396 N  N   . ALA B 1 137 ? -8.115  10.750  -31.565  1.00 38.99  ?  135 ALA B N   1 
ATOM   5397 C  CA  . ALA B 1 137 ? -9.031  11.793  -32.023  1.00 43.91  ?  135 ALA B CA  1 
ATOM   5398 C  C   . ALA B 1 137 ? -9.581  11.467  -33.405  1.00 40.20  ?  135 ALA B C   1 
ATOM   5399 O  O   . ALA B 1 137 ? -10.772 11.666  -33.670  1.00 37.89  ?  135 ALA B O   1 
ATOM   5400 C  CB  . ALA B 1 137 ? -8.333  13.154  -32.024  1.00 32.78  ?  135 ALA B CB  1 
ATOM   5401 N  N   . GLU B 1 138 ? -8.722  10.977  -34.306  1.00 43.65  ?  136 GLU B N   1 
ATOM   5402 C  CA  . GLU B 1 138 ? -9.190  10.566  -35.627  1.00 42.66  ?  136 GLU B CA  1 
ATOM   5403 C  C   . GLU B 1 138 ? -10.152 9.394   -35.510  1.00 46.41  ?  136 GLU B C   1 
ATOM   5404 O  O   . GLU B 1 138 ? -11.207 9.370   -36.155  1.00 42.86  ?  136 GLU B O   1 
ATOM   5405 C  CB  . GLU B 1 138 ? -8.009  10.153  -36.506  1.00 43.20  ?  136 GLU B CB  1 
ATOM   5406 C  CG  . GLU B 1 138 ? -7.288  11.249  -37.256  1.00 47.56  ?  136 GLU B CG  1 
ATOM   5407 C  CD  . GLU B 1 138 ? -6.205  10.681  -38.164  1.00 55.51  ?  136 GLU B CD  1 
ATOM   5408 O  OE1 . GLU B 1 138 ? -6.532  9.828   -39.018  1.00 53.39  ?  136 GLU B OE1 1 
ATOM   5409 O  OE2 . GLU B 1 138 ? -5.029  11.079  -38.024  1.00 52.50  -1 136 GLU B OE2 1 
ATOM   5410 N  N   . THR B 1 139 ? -9.795  8.409   -34.686  1.00 44.19  ?  137 THR B N   1 
ATOM   5411 C  CA  . THR B 1 139 ? -10.613 7.211   -34.555  1.00 48.34  ?  137 THR B CA  1 
ATOM   5412 C  C   . THR B 1 139 ? -11.977 7.547   -33.971  1.00 43.92  ?  137 THR B C   1 
ATOM   5413 O  O   . THR B 1 139 ? -13.007 7.067   -34.460  1.00 47.20  ?  137 THR B O   1 
ATOM   5414 C  CB  . THR B 1 139 ? -9.884  6.187   -33.687  1.00 44.31  ?  137 THR B CB  1 
ATOM   5415 O  OG1 . THR B 1 139 ? -8.665  5.798   -34.335  1.00 42.60  ?  137 THR B OG1 1 
ATOM   5416 C  CG2 . THR B 1 139 ? -10.749 4.962   -33.459  1.00 39.20  ?  137 THR B CG2 1 
ATOM   5417 N  N   . LEU B 1 140 ? -12.003 8.376   -32.926  1.00 39.38  ?  138 LEU B N   1 
ATOM   5418 C  CA  . LEU B 1 140 ? -13.271 8.748   -32.308  1.00 45.90  ?  138 LEU B CA  1 
ATOM   5419 C  C   . LEU B 1 140 ? -14.151 9.511   -33.289  1.00 40.80  ?  138 LEU B C   1 
ATOM   5420 O  O   . LEU B 1 140 ? -15.352 9.240   -33.405  1.00 43.65  ?  138 LEU B O   1 
ATOM   5421 C  CB  . LEU B 1 140 ? -13.018 9.578   -31.049  1.00 40.70  ?  138 LEU B CB  1 
ATOM   5422 C  CG  . LEU B 1 140 ? -14.247 10.278  -30.468  1.00 48.63  ?  138 LEU B CG  1 
ATOM   5423 C  CD1 . LEU B 1 140 ? -15.263 9.255   -29.981  1.00 34.89  ?  138 LEU B CD1 1 
ATOM   5424 C  CD2 . LEU B 1 140 ? -13.853 11.232  -29.344  1.00 38.05  ?  138 LEU B CD2 1 
ATOM   5425 N  N   . LYS B 1 141 ? -13.571 10.475  -34.007  1.00 36.94  ?  139 LYS B N   1 
ATOM   5426 C  CA  . LYS B 1 141 ? -14.381 11.299  -34.895  1.00 38.58  ?  139 LYS B CA  1 
ATOM   5427 C  C   . LYS B 1 141 ? -14.951 10.467  -36.035  1.00 46.44  ?  139 LYS B C   1 
ATOM   5428 O  O   . LYS B 1 141 ? -16.118 10.632  -36.411  1.00 44.27  ?  139 LYS B O   1 
ATOM   5429 C  CB  . LYS B 1 141 ? -13.555 12.467  -35.432  1.00 43.38  ?  139 LYS B CB  1 
ATOM   5430 C  CG  . LYS B 1 141 ? -14.387 13.630  -35.944  1.00 45.41  ?  139 LYS B CG  1 
ATOM   5431 C  CD  . LYS B 1 141 ? -13.511 14.687  -36.599  1.00 51.08  ?  139 LYS B CD  1 
ATOM   5432 C  CE  . LYS B 1 141 ? -14.200 16.042  -36.620  1.00 53.47  ?  139 LYS B CE  1 
ATOM   5433 N  NZ  . LYS B 1 141 ? -15.592 15.955  -37.141  1.00 64.96  ?  139 LYS B NZ  1 
ATOM   5434 N  N   . ALA B 1 142 ? -14.145 9.559   -36.593  1.00 42.90  ?  140 ALA B N   1 
ATOM   5435 C  CA  . ALA B 1 142 ? -14.646 8.691   -37.652  1.00 44.14  ?  140 ALA B CA  1 
ATOM   5436 C  C   . ALA B 1 142 ? -15.750 7.785   -37.127  1.00 42.79  ?  140 ALA B C   1 
ATOM   5437 O  O   . ALA B 1 142 ? -16.744 7.536   -37.819  1.00 41.22  ?  140 ALA B O   1 
ATOM   5438 C  CB  . ALA B 1 142 ? -13.504 7.866   -38.242  1.00 45.49  ?  140 ALA B CB  1 
ATOM   5439 N  N   . THR B 1 143 ? -15.589 7.276   -35.903  1.00 42.68  ?  141 THR B N   1 
ATOM   5440 C  CA  . THR B 1 143 ? -16.631 6.445   -35.310  1.00 43.56  ?  141 THR B CA  1 
ATOM   5441 C  C   . THR B 1 143 ? -17.905 7.254   -35.109  1.00 47.80  ?  141 THR B C   1 
ATOM   5442 O  O   . THR B 1 143 ? -19.008 6.778   -35.402  1.00 54.02  ?  141 THR B O   1 
ATOM   5443 C  CB  . THR B 1 143 ? -16.146 5.854   -33.985  1.00 45.98  ?  141 THR B CB  1 
ATOM   5444 O  OG1 . THR B 1 143 ? -14.906 5.165   -34.193  1.00 44.73  ?  141 THR B OG1 1 
ATOM   5445 C  CG2 . THR B 1 143 ? -17.170 4.876   -33.428  1.00 31.51  ?  141 THR B CG2 1 
ATOM   5446 N  N   . GLU B 1 144 ? -17.768 8.486   -34.611  1.00 42.04  ?  142 GLU B N   1 
ATOM   5447 C  CA  . GLU B 1 144 ? -18.924 9.358   -34.436  1.00 42.88  ?  142 GLU B CA  1 
ATOM   5448 C  C   . GLU B 1 144 ? -19.651 9.572   -35.756  1.00 45.52  ?  142 GLU B C   1 
ATOM   5449 O  O   . GLU B 1 144 ? -20.885 9.526   -35.810  1.00 47.99  ?  142 GLU B O   1 
ATOM   5450 C  CB  . GLU B 1 144 ? -18.477 10.704  -33.865  1.00 43.93  ?  142 GLU B CB  1 
ATOM   5451 C  CG  . GLU B 1 144 ? -18.171 10.720  -32.376  1.00 44.78  ?  142 GLU B CG  1 
ATOM   5452 C  CD  . GLU B 1 144 ? -17.371 11.949  -31.974  1.00 50.94  ?  142 GLU B CD  1 
ATOM   5453 O  OE1 . GLU B 1 144 ? -16.899 12.674  -32.878  1.00 49.74  ?  142 GLU B OE1 1 
ATOM   5454 O  OE2 . GLU B 1 144 ? -17.229 12.205  -30.759  1.00 44.82  -1 142 GLU B OE2 1 
ATOM   5455 N  N   . GLU B 1 145 ? -18.898 9.811   -36.832  1.00 48.85  ?  143 GLU B N   1 
ATOM   5456 C  CA  . GLU B 1 145 ? -19.516 10.067  -38.128  1.00 50.54  ?  143 GLU B CA  1 
ATOM   5457 C  C   . GLU B 1 145 ? -20.224 8.826   -38.653  1.00 54.63  ?  143 GLU B C   1 
ATOM   5458 O  O   . GLU B 1 145 ? -21.304 8.923   -39.249  1.00 56.60  ?  143 GLU B O   1 
ATOM   5459 C  CB  . GLU B 1 145 ? -18.458 10.545  -39.121  1.00 54.29  ?  143 GLU B CB  1 
ATOM   5460 C  CG  . GLU B 1 145 ? -17.900 11.922  -38.799  1.00 62.46  ?  143 GLU B CG  1 
ATOM   5461 C  CD  . GLU B 1 145 ? -18.835 13.046  -39.200  1.00 72.77  ?  143 GLU B CD  1 
ATOM   5462 O  OE1 . GLU B 1 145 ? -19.885 12.760  -39.813  1.00 74.97  ?  143 GLU B OE1 1 
ATOM   5463 O  OE2 . GLU B 1 145 ? -18.521 14.215  -38.894  1.00 77.74  -1 143 GLU B OE2 1 
ATOM   5464 N  N   . THR B 1 146 ? -19.635 7.648   -38.434  1.00 55.66  ?  144 THR B N   1 
ATOM   5465 C  CA  . THR B 1 146 ? -20.247 6.417   -38.921  1.00 60.94  ?  144 THR B CA  1 
ATOM   5466 C  C   . THR B 1 146 ? -21.503 6.088   -38.127  1.00 59.26  ?  144 THR B C   1 
ATOM   5467 O  O   . THR B 1 146 ? -22.501 5.626   -38.692  1.00 61.37  ?  144 THR B O   1 
ATOM   5468 C  CB  . THR B 1 146 ? -19.246 5.265   -38.847  1.00 61.16  ?  144 THR B CB  1 
ATOM   5469 O  OG1 . THR B 1 146 ? -18.344 5.343   -39.957  1.00 65.51  ?  144 THR B OG1 1 
ATOM   5470 C  CG2 . THR B 1 146 ? -19.972 3.926   -38.883  1.00 55.92  ?  144 THR B CG2 1 
ATOM   5471 N  N   . PHE B 1 147 ? -21.474 6.332   -36.814  1.00 54.63  ?  145 PHE B N   1 
ATOM   5472 C  CA  . PHE B 1 147 ? -22.635 6.038   -35.984  1.00 56.91  ?  145 PHE B CA  1 
ATOM   5473 C  C   . PHE B 1 147 ? -23.839 6.856   -36.426  1.00 59.69  ?  145 PHE B C   1 
ATOM   5474 O  O   . PHE B 1 147 ? -24.986 6.444   -36.214  1.00 53.99  ?  145 PHE B O   1 
ATOM   5475 C  CB  . PHE B 1 147 ? -22.302 6.314   -34.518  1.00 54.17  ?  145 PHE B CB  1 
ATOM   5476 C  CG  . PHE B 1 147 ? -23.436 6.043   -33.572  1.00 60.66  ?  145 PHE B CG  1 
ATOM   5477 C  CD1 . PHE B 1 147 ? -23.647 4.770   -33.069  1.00 61.43  ?  145 PHE B CD1 1 
ATOM   5478 C  CD2 . PHE B 1 147 ? -24.286 7.063   -33.177  1.00 57.71  ?  145 PHE B CD2 1 
ATOM   5479 C  CE1 . PHE B 1 147 ? -24.685 4.516   -32.195  1.00 63.71  ?  145 PHE B CE1 1 
ATOM   5480 C  CE2 . PHE B 1 147 ? -25.328 6.817   -32.302  1.00 70.90  ?  145 PHE B CE2 1 
ATOM   5481 C  CZ  . PHE B 1 147 ? -25.528 5.541   -31.811  1.00 67.27  ?  145 PHE B CZ  1 
ATOM   5482 N  N   . LYS B 1 148 ? -23.597 8.013   -37.043  1.00 60.60  ?  146 LYS B N   1 
ATOM   5483 C  CA  . LYS B 1 148 ? -24.692 8.841   -37.532  1.00 60.78  ?  146 LYS B CA  1 
ATOM   5484 C  C   . LYS B 1 148 ? -25.422 8.165   -38.686  1.00 58.21  ?  146 LYS B C   1 
ATOM   5485 O  O   . LYS B 1 148 ? -26.620 8.398   -38.880  1.00 62.91  ?  146 LYS B O   1 
ATOM   5486 C  CB  . LYS B 1 148 ? -24.157 10.216  -37.931  1.00 56.89  ?  146 LYS B CB  1 
ATOM   5487 C  CG  . LYS B 1 148 ? -23.836 11.085  -36.720  1.00 63.85  ?  146 LYS B CG  1 
ATOM   5488 C  CD  . LYS B 1 148 ? -23.585 12.538  -37.082  1.00 70.84  ?  146 LYS B CD  1 
ATOM   5489 C  CE  . LYS B 1 148 ? -22.477 12.670  -38.110  1.00 70.44  ?  146 LYS B CE  1 
ATOM   5490 N  NZ  . LYS B 1 148 ? -22.294 14.083  -38.544  1.00 77.09  ?  146 LYS B NZ  1 
ATOM   5491 N  N   . LEU B 1 149 ? -24.724 7.321   -39.452  1.00 57.35  ?  147 LEU B N   1 
ATOM   5492 C  CA  . LEU B 1 149 ? -25.351 6.600   -40.553  1.00 53.40  ?  147 LEU B CA  1 
ATOM   5493 C  C   . LEU B 1 149 ? -26.207 5.443   -40.061  1.00 65.28  ?  147 LEU B C   1 
ATOM   5494 O  O   . LEU B 1 149 ? -27.064 4.958   -40.808  1.00 73.89  ?  147 LEU B O   1 
ATOM   5495 C  CB  . LEU B 1 149 ? -24.289 6.068   -41.518  1.00 57.96  ?  147 LEU B CB  1 
ATOM   5496 C  CG  . LEU B 1 149 ? -23.259 7.064   -42.053  1.00 67.43  ?  147 LEU B CG  1 
ATOM   5497 C  CD1 . LEU B 1 149 ? -22.198 6.354   -42.887  1.00 60.54  ?  147 LEU B CD1 1 
ATOM   5498 C  CD2 . LEU B 1 149 ? -23.947 8.148   -42.868  1.00 66.94  ?  147 LEU B CD2 1 
ATOM   5499 N  N   . SER B 1 150 ? -25.984 4.990   -38.826  1.00 55.75  ?  148 SER B N   1 
ATOM   5500 C  CA  . SER B 1 150 ? -26.797 3.926   -38.249  1.00 61.79  ?  148 SER B CA  1 
ATOM   5501 C  C   . SER B 1 150 ? -28.249 4.348   -38.066  1.00 61.59  ?  148 SER B C   1 
ATOM   5502 O  O   . SER B 1 150 ? -29.121 3.483   -37.933  1.00 67.41  ?  148 SER B O   1 
ATOM   5503 C  CB  . SER B 1 150 ? -26.209 3.483   -36.910  1.00 58.40  ?  148 SER B CB  1 
ATOM   5504 O  OG  . SER B 1 150 ? -26.520 4.411   -35.885  1.00 67.68  ?  148 SER B OG  1 
ATOM   5505 N  N   . TYR B 1 151 ? -28.527 5.649   -38.052  1.00 61.92  ?  149 TYR B N   1 
ATOM   5506 C  CA  . TYR B 1 151 ? -29.876 6.138   -37.811  1.00 60.76  ?  149 TYR B CA  1 
ATOM   5507 C  C   . TYR B 1 151 ? -30.713 6.049   -39.081  1.00 60.18  ?  149 TYR B C   1 
ATOM   5508 O  O   . TYR B 1 151 ? -30.200 6.139   -40.200  1.00 62.50  ?  149 TYR B O   1 
ATOM   5509 C  CB  . TYR B 1 151 ? -29.839 7.589   -37.329  1.00 58.80  ?  149 TYR B CB  1 
ATOM   5510 C  CG  . TYR B 1 151 ? -29.403 7.771   -35.894  1.00 70.60  ?  149 TYR B CG  1 
ATOM   5511 C  CD1 . TYR B 1 151 ? -29.991 7.044   -34.866  1.00 65.87  ?  149 TYR B CD1 1 
ATOM   5512 C  CD2 . TYR B 1 151 ? -28.381 8.654   -35.571  1.00 68.85  ?  149 TYR B CD2 1 
ATOM   5513 C  CE1 . TYR B 1 151 ? -29.587 7.211   -33.553  1.00 69.97  ?  149 TYR B CE1 1 
ATOM   5514 C  CE2 . TYR B 1 151 ? -27.968 8.824   -34.265  1.00 72.33  ?  149 TYR B CE2 1 
ATOM   5515 C  CZ  . TYR B 1 151 ? -28.572 8.101   -33.260  1.00 74.14  ?  149 TYR B CZ  1 
ATOM   5516 O  OH  . TYR B 1 151 ? -28.160 8.273   -31.959  1.00 81.32  ?  149 TYR B OH  1 
ATOM   5517 N  N   . GLY B 1 152 ? -32.020 5.883   -38.896  1.00 59.07  ?  150 GLY B N   1 
ATOM   5518 C  CA  . GLY B 1 152 ? -32.908 5.736   -40.025  1.00 69.01  ?  150 GLY B CA  1 
ATOM   5519 C  C   . GLY B 1 152 ? -33.307 7.062   -40.642  1.00 70.72  ?  150 GLY B C   1 
ATOM   5520 O  O   . GLY B 1 152 ? -33.238 8.121   -40.018  1.00 75.67  ?  150 GLY B O   1 
ATOM   5521 N  N   . ILE B 1 153 ? -33.723 6.989   -41.902  1.00 62.39  ?  151 ILE B N   1 
ATOM   5522 C  CA  . ILE B 1 153 ? -34.170 8.167   -42.634  1.00 60.21  ?  151 ILE B CA  1 
ATOM   5523 C  C   . ILE B 1 153 ? -35.565 8.544   -42.162  1.00 61.41  ?  151 ILE B C   1 
ATOM   5524 O  O   . ILE B 1 153 ? -36.396 7.674   -41.874  1.00 62.63  ?  151 ILE B O   1 
ATOM   5525 C  CB  . ILE B 1 153 ? -34.158 7.904   -44.151  1.00 58.58  ?  151 ILE B CB  1 
ATOM   5526 C  CG1 . ILE B 1 153 ? -32.807 7.345   -44.599  1.00 65.78  ?  151 ILE B CG1 1 
ATOM   5527 C  CG2 . ILE B 1 153 ? -34.498 9.175   -44.916  1.00 62.54  ?  151 ILE B CG2 1 
ATOM   5528 C  CD1 . ILE B 1 153 ? -32.782 6.924   -46.055  1.00 63.12  ?  151 ILE B CD1 1 
ATOM   5529 N  N   . ALA B 1 154 ? -35.830 9.843   -42.080  1.00 62.80  ?  152 ALA B N   1 
ATOM   5530 C  CA  . ALA B 1 154 ? -37.150 10.359  -41.751  1.00 68.16  ?  152 ALA B CA  1 
ATOM   5531 C  C   . ALA B 1 154 ? -37.723 11.027  -42.992  1.00 68.14  ?  152 ALA B C   1 
ATOM   5532 O  O   . ALA B 1 154 ? -37.050 11.849  -43.623  1.00 69.88  ?  152 ALA B O   1 
ATOM   5533 C  CB  . ALA B 1 154 ? -37.088 11.346  -40.584  1.00 68.19  ?  152 ALA B CB  1 
ATOM   5534 N  N   . THR B 1 155 ? -38.960 10.683  -43.336  1.00 68.91  ?  153 THR B N   1 
ATOM   5535 C  CA  . THR B 1 155 ? -39.574 11.175  -44.559  1.00 74.60  ?  153 THR B CA  1 
ATOM   5536 C  C   . THR B 1 155 ? -40.916 11.816  -44.243  1.00 77.90  ?  153 THR B C   1 
ATOM   5537 O  O   . THR B 1 155 ? -41.700 11.281  -43.453  1.00 77.41  ?  153 THR B O   1 
ATOM   5538 C  CB  . THR B 1 155 ? -39.767 10.041  -45.575  1.00 72.98  ?  153 THR B CB  1 
ATOM   5539 O  OG1 . THR B 1 155 ? -38.509 9.405   -45.828  1.00 69.31  ?  153 THR B OG1 1 
ATOM   5540 C  CG2 . THR B 1 155 ? -40.320 10.584  -46.881  1.00 77.22  ?  153 THR B CG2 1 
ATOM   5541 N  N   . VAL B 1 156 ? -41.172 12.964  -44.868  1.00 81.39  ?  154 VAL B N   1 
ATOM   5542 C  CA  . VAL B 1 156 ? -42.415 13.687  -44.627  1.00 84.39  ?  154 VAL B CA  1 
ATOM   5543 C  C   . VAL B 1 156 ? -43.579 12.851  -45.139  1.00 82.55  ?  154 VAL B C   1 
ATOM   5544 O  O   . VAL B 1 156 ? -43.661 12.532  -46.331  1.00 80.22  ?  154 VAL B O   1 
ATOM   5545 C  CB  . VAL B 1 156 ? -42.391 15.069  -45.291  1.00 85.16  ?  154 VAL B CB  1 
ATOM   5546 C  CG1 . VAL B 1 156 ? -43.744 15.751  -45.137  1.00 86.40  ?  154 VAL B CG1 1 
ATOM   5547 C  CG2 . VAL B 1 156 ? -41.288 15.926  -44.693  1.00 85.01  ?  154 VAL B CG2 1 
ATOM   5548 N  N   . ARG B 1 157 ? -44.487 12.500  -44.236  1.00 79.93  ?  155 ARG B N   1 
ATOM   5549 C  CA  . ARG B 1 157 ? -45.684 11.751  -44.578  1.00 82.51  ?  155 ARG B CA  1 
ATOM   5550 C  C   . ARG B 1 157 ? -46.889 12.661  -44.730  1.00 90.55  ?  155 ARG B C   1 
ATOM   5551 O  O   . ARG B 1 157 ? -47.808 12.345  -45.492  1.00 88.63  ?  155 ARG B O   1 
ATOM   5552 C  CB  . ARG B 1 157 ? -45.925 10.680  -43.504  1.00 83.76  ?  155 ARG B CB  1 
ATOM   5553 C  CG  . ARG B 1 157 ? -47.280 9.987   -43.423  1.00 80.97  ?  155 ARG B CG  1 
ATOM   5554 C  CD  . ARG B 1 157 ? -47.290 9.218   -42.096  1.00 83.39  ?  155 ARG B CD  1 
ATOM   5555 N  NE  . ARG B 1 157 ? -48.288 8.161   -41.982  1.00 83.67  ?  155 ARG B NE  1 
ATOM   5556 C  CZ  . ARG B 1 157 ? -49.600 8.340   -41.944  1.00 85.41  ?  155 ARG B CZ  1 
ATOM   5557 N  NH1 . ARG B 1 157 ? -50.129 9.528   -41.702  1.00 87.59  ?  155 ARG B NH1 1 
ATOM   5558 N  NH2 . ARG B 1 157 ? -50.399 7.281   -42.038  1.00 84.25  ?  155 ARG B NH2 1 
ATOM   5559 N  N   . GLU B 1 158 ? -46.877 13.796  -44.034  1.00 89.61  ?  156 GLU B N   1 
ATOM   5560 C  CA  . GLU B 1 158 ? -47.987 14.736  -44.050  1.00 88.22  ?  156 GLU B CA  1 
ATOM   5561 C  C   . GLU B 1 158 ? -47.507 16.063  -43.481  1.00 91.13  ?  156 GLU B C   1 
ATOM   5562 O  O   . GLU B 1 158 ? -46.939 16.092  -42.386  1.00 96.53  ?  156 GLU B O   1 
ATOM   5563 C  CB  . GLU B 1 158 ? -49.147 14.183  -43.227  1.00 89.38  ?  156 GLU B CB  1 
ATOM   5564 C  CG  . GLU B 1 158 ? -50.372 15.050  -43.174  1.00 91.16  ?  156 GLU B CG  1 
ATOM   5565 C  CD  . GLU B 1 158 ? -51.567 14.266  -42.694  1.00 96.15  ?  156 GLU B CD  1 
ATOM   5566 O  OE1 . GLU B 1 158 ? -51.408 13.049  -42.457  1.00 91.83  ?  156 GLU B OE1 1 
ATOM   5567 O  OE2 . GLU B 1 158 ? -52.657 14.857  -42.551  1.00 97.97  -1 156 GLU B OE2 1 
ATOM   5568 N  N   . VAL B 1 159 ? -47.722 17.152  -44.218  1.00 92.90  ?  157 VAL B N   1 
ATOM   5569 C  CA  . VAL B 1 159 ? -47.441 18.495  -43.704  1.00 96.21  ?  157 VAL B CA  1 
ATOM   5570 C  C   . VAL B 1 159 ? -48.728 18.965  -43.032  1.00 97.78  ?  157 VAL B C   1 
ATOM   5571 O  O   . VAL B 1 159 ? -49.596 19.575  -43.658  1.00 95.76  ?  157 VAL B O   1 
ATOM   5572 C  CB  . VAL B 1 159 ? -46.970 19.449  -44.798  1.00 100.05 ?  157 VAL B CB  1 
ATOM   5573 C  CG1 . VAL B 1 159 ? -46.421 20.732  -44.179  1.00 100.06 ?  157 VAL B CG1 1 
ATOM   5574 C  CG2 . VAL B 1 159 ? -45.918 18.784  -45.673  1.00 95.23  ?  157 VAL B CG2 1 
ATOM   5575 N  N   . LEU B 1 160 ? -48.855 18.670  -41.737  1.00 97.60  ?  158 LEU B N   1 
ATOM   5576 C  CA  . LEU B 1 160 ? -50.053 19.057  -40.998  1.00 92.66  ?  158 LEU B CA  1 
ATOM   5577 C  C   . LEU B 1 160 ? -50.337 20.543  -41.169  1.00 103.02 ?  158 LEU B C   1 
ATOM   5578 O  O   . LEU B 1 160 ? -51.376 20.943  -41.707  1.00 104.51 ?  158 LEU B O   1 
ATOM   5579 C  CB  . LEU B 1 160 ? -49.888 18.710  -39.517  1.00 95.66  ?  158 LEU B CB  1 
ATOM   5580 C  CG  . LEU B 1 160 ? -50.195 17.273  -39.093  1.00 96.26  ?  158 LEU B CG  1 
ATOM   5581 C  CD1 . LEU B 1 160 ? -51.487 16.789  -39.733  1.00 95.08  ?  158 LEU B CD1 1 
ATOM   5582 C  CD2 . LEU B 1 160 ? -49.036 16.352  -39.440  1.00 94.03  ?  158 LEU B CD2 1 
ATOM   5583 N  N   . SER B 1 161 ? -49.410 21.373  -40.708  1.00 106.85 ?  159 SER B N   1 
ATOM   5584 C  CA  . SER B 1 161 ? -49.490 22.819  -40.839  1.00 98.42  ?  159 SER B CA  1 
ATOM   5585 C  C   . SER B 1 161 ? -48.073 23.351  -40.716  1.00 100.80 ?  159 SER B C   1 
ATOM   5586 O  O   . SER B 1 161 ? -47.153 22.624  -40.333  1.00 107.24 ?  159 SER B O   1 
ATOM   5587 C  CB  . SER B 1 161 ? -50.416 23.434  -39.786  1.00 102.44 ?  159 SER B CB  1 
ATOM   5588 O  OG  . SER B 1 161 ? -51.759 23.030  -39.991  1.00 104.66 ?  159 SER B OG  1 
ATOM   5589 N  N   . ASP B 1 162 ? -47.894 24.620  -41.068  1.00 107.81 ?  160 ASP B N   1 
ATOM   5590 C  CA  . ASP B 1 162 ? -46.552 25.182  -41.045  1.00 108.67 ?  160 ASP B CA  1 
ATOM   5591 C  C   . ASP B 1 162 ? -45.961 24.990  -39.654  1.00 105.91 ?  160 ASP B C   1 
ATOM   5592 O  O   . ASP B 1 162 ? -46.648 25.152  -38.642  1.00 108.72 ?  160 ASP B O   1 
ATOM   5593 C  CB  . ASP B 1 162 ? -46.592 26.662  -41.428  1.00 108.55 ?  160 ASP B CB  1 
ATOM   5594 C  CG  . ASP B 1 162 ? -45.224 27.212  -41.776  1.00 109.73 ?  160 ASP B CG  1 
ATOM   5595 O  OD1 . ASP B 1 162 ? -44.241 26.444  -41.721  1.00 111.29 ?  160 ASP B OD1 1 
ATOM   5596 O  OD2 . ASP B 1 162 ? -45.136 28.410  -42.119  1.00 114.91 -1 160 ASP B OD2 1 
ATOM   5597 N  N   . ARG B 1 163 ? -44.683 24.621  -39.604  1.00 102.57 ?  161 ARG B N   1 
ATOM   5598 C  CA  . ARG B 1 163 ? -43.911 24.357  -38.396  1.00 102.95 ?  161 ARG B CA  1 
ATOM   5599 C  C   . ARG B 1 163 ? -44.262 22.991  -37.804  1.00 105.09 ?  161 ARG B C   1 
ATOM   5600 O  O   . ARG B 1 163 ? -43.537 22.509  -36.932  1.00 104.08 ?  161 ARG B O   1 
ATOM   5601 C  CB  . ARG B 1 163 ? -44.089 25.436  -37.310  1.00 101.53 ?  161 ARG B CB  1 
ATOM   5602 N  N   . GLU B 1 164 ? -45.341 22.351  -38.250  1.00 104.62 ?  162 GLU B N   1 
ATOM   5603 C  CA  . GLU B 1 164 ? -45.749 21.029  -37.801  1.00 96.40  ?  162 GLU B CA  1 
ATOM   5604 C  C   . GLU B 1 164 ? -45.569 20.045  -38.950  1.00 99.32  ?  162 GLU B C   1 
ATOM   5605 O  O   . GLU B 1 164 ? -45.726 20.403  -40.121  1.00 99.39  ?  162 GLU B O   1 
ATOM   5606 C  CB  . GLU B 1 164 ? -47.208 21.037  -37.337  1.00 98.97  ?  162 GLU B CB  1 
ATOM   5607 C  CG  . GLU B 1 164 ? -47.544 22.188  -36.398  1.00 109.09 ?  162 GLU B CG  1 
ATOM   5608 C  CD  . GLU B 1 164 ? -49.030 22.302  -36.108  1.00 110.69 ?  162 GLU B CD  1 
ATOM   5609 O  OE1 . GLU B 1 164 ? -49.805 21.462  -36.614  1.00 111.43 ?  162 GLU B OE1 1 
ATOM   5610 O  OE2 . GLU B 1 164 ? -49.424 23.240  -35.383  1.00 106.14 -1 162 GLU B OE2 1 
ATOM   5611 N  N   . LEU B 1 165 ? -45.241 18.799  -38.617  1.00 95.89  ?  163 LEU B N   1 
ATOM   5612 C  CA  . LEU B 1 165 ? -44.930 17.839  -39.664  1.00 90.40  ?  163 LEU B CA  1 
ATOM   5613 C  C   . LEU B 1 165 ? -45.123 16.423  -39.143  1.00 88.85  ?  163 LEU B C   1 
ATOM   5614 O  O   . LEU B 1 165 ? -44.824 16.141  -37.980  1.00 89.58  ?  163 LEU B O   1 
ATOM   5615 C  CB  . LEU B 1 165 ? -43.489 18.040  -40.147  1.00 94.86  ?  163 LEU B CB  1 
ATOM   5616 C  CG  . LEU B 1 165 ? -43.111 17.620  -41.562  1.00 94.51  ?  163 LEU B CG  1 
ATOM   5617 C  CD1 . LEU B 1 165 ? -43.958 18.377  -42.568  1.00 93.47  ?  163 LEU B CD1 1 
ATOM   5618 C  CD2 . LEU B 1 165 ? -41.635 17.890  -41.793  1.00 94.27  ?  163 LEU B CD2 1 
ATOM   5619 N  N   . HIS B 1 166 ? -45.629 15.541  -40.002  1.00 87.22  ?  164 HIS B N   1 
ATOM   5620 C  CA  . HIS B 1 166 ? -45.753 14.126  -39.678  1.00 87.47  ?  164 HIS B CA  1 
ATOM   5621 C  C   . HIS B 1 166 ? -44.666 13.353  -40.418  1.00 87.73  ?  164 HIS B C   1 
ATOM   5622 O  O   . HIS B 1 166 ? -44.499 13.519  -41.631  1.00 86.62  ?  164 HIS B O   1 
ATOM   5623 C  CB  . HIS B 1 166 ? -47.136 13.586  -40.031  1.00 88.86  ?  164 HIS B CB  1 
ATOM   5624 C  CG  . HIS B 1 166 ? -47.573 12.476  -39.132  1.00 88.98  ?  164 HIS B CG  1 
ATOM   5625 N  ND1 . HIS B 1 166 ? -47.259 11.156  -39.372  1.00 92.03  ?  164 HIS B ND1 1 
ATOM   5626 C  CD2 . HIS B 1 166 ? -48.268 12.494  -37.970  1.00 88.67  ?  164 HIS B CD2 1 
ATOM   5627 C  CE1 . HIS B 1 166 ? -47.749 10.408  -38.400  1.00 93.17  ?  164 HIS B CE1 1 
ATOM   5628 N  NE2 . HIS B 1 166 ? -48.369 11.195  -37.539  1.00 98.15  ?  164 HIS B NE2 1 
ATOM   5629 N  N   . LEU B 1 167 ? -43.939 12.505  -39.691  1.00 82.36  ?  165 LEU B N   1 
ATOM   5630 C  CA  . LEU B 1 167 ? -42.771 11.818  -40.227  1.00 82.21  ?  165 LEU B CA  1 
ATOM   5631 C  C   . LEU B 1 167 ? -42.916 10.301  -40.198  1.00 81.08  ?  165 LEU B C   1 
ATOM   5632 O  O   . LEU B 1 167 ? -43.396 9.728   -39.214  1.00 78.10  ?  165 LEU B O   1 
ATOM   5633 C  CB  . LEU B 1 167 ? -41.518 12.210  -39.438  1.00 75.99  ?  165 LEU B CB  1 
ATOM   5634 C  CG  . LEU B 1 167 ? -41.069 13.667  -39.533  1.00 81.41  ?  165 LEU B CG  1 
ATOM   5635 C  CD1 . LEU B 1 167 ? -39.765 13.864  -38.779  1.00 81.63  ?  165 LEU B CD1 1 
ATOM   5636 C  CD2 . LEU B 1 167 ? -40.924 14.093  -40.985  1.00 83.87  ?  165 LEU B CD2 1 
ATOM   5637 N  N   . SER B 1 168 ? -42.494 9.662   -41.288  1.00 79.77  ?  166 SER B N   1 
ATOM   5638 C  CA  . SER B 1 168 ? -42.398 8.211   -41.392  1.00 77.21  ?  166 SER B CA  1 
ATOM   5639 C  C   . SER B 1 168 ? -40.924 7.833   -41.333  1.00 72.94  ?  166 SER B C   1 
ATOM   5640 O  O   . SER B 1 168 ? -40.104 8.421   -42.046  1.00 71.97  ?  166 SER B O   1 
ATOM   5641 C  CB  . SER B 1 168 ? -43.027 7.695   -42.689  1.00 78.02  ?  166 SER B CB  1 
ATOM   5642 O  OG  . SER B 1 168 ? -44.405 8.015   -42.763  1.00 79.22  ?  166 SER B OG  1 
ATOM   5643 N  N   . TRP B 1 169 ? -40.585 6.858   -40.497  1.00 69.17  ?  167 TRP B N   1 
ATOM   5644 C  CA  . TRP B 1 169 ? -39.192 6.513   -40.258  1.00 66.36  ?  167 TRP B CA  1 
ATOM   5645 C  C   . TRP B 1 169 ? -38.832 5.191   -40.924  1.00 60.58  ?  167 TRP B C   1 
ATOM   5646 O  O   . TRP B 1 169 ? -39.686 4.337   -41.177  1.00 59.97  ?  167 TRP B O   1 
ATOM   5647 C  CB  . TRP B 1 169 ? -38.897 6.438   -38.755  1.00 66.06  ?  167 TRP B CB  1 
ATOM   5648 C  CG  . TRP B 1 169 ? -39.011 7.760   -38.054  1.00 70.20  ?  167 TRP B CG  1 
ATOM   5649 C  CD1 . TRP B 1 169 ? -40.140 8.307   -37.517  1.00 72.94  ?  167 TRP B CD1 1 
ATOM   5650 C  CD2 . TRP B 1 169 ? -37.956 8.699   -37.811  1.00 71.44  ?  167 TRP B CD2 1 
ATOM   5651 N  NE1 . TRP B 1 169 ? -39.854 9.529   -36.957  1.00 71.16  ?  167 TRP B NE1 1 
ATOM   5652 C  CE2 . TRP B 1 169 ? -38.520 9.793   -37.124  1.00 74.42  ?  167 TRP B CE2 1 
ATOM   5653 C  CE3 . TRP B 1 169 ? -36.589 8.722   -38.109  1.00 71.43  ?  167 TRP B CE3 1 
ATOM   5654 C  CZ2 . TRP B 1 169 ? -37.766 10.897  -36.730  1.00 78.20  ?  167 TRP B CZ2 1 
ATOM   5655 C  CZ3 . TRP B 1 169 ? -35.842 9.820   -37.716  1.00 71.68  ?  167 TRP B CZ3 1 
ATOM   5656 C  CH2 . TRP B 1 169 ? -36.433 10.892  -37.035  1.00 71.87  ?  167 TRP B CH2 1 
ATOM   5657 N  N   . GLU B 1 170 ? -37.538 5.035   -41.194  1.00 56.15  ?  168 GLU B N   1 
ATOM   5658 C  CA  . GLU B 1 170 ? -37.035 3.835   -41.847  1.00 57.74  ?  168 GLU B CA  1 
ATOM   5659 C  C   . GLU B 1 170 ? -37.097 2.646   -40.895  1.00 58.77  ?  168 GLU B C   1 
ATOM   5660 O  O   . GLU B 1 170 ? -36.752 2.755   -39.715  1.00 54.99  ?  168 GLU B O   1 
ATOM   5661 C  CB  . GLU B 1 170 ? -35.600 4.076   -42.318  1.00 60.54  ?  168 GLU B CB  1 
ATOM   5662 C  CG  . GLU B 1 170 ? -34.934 2.921   -43.037  1.00 56.24  ?  168 GLU B CG  1 
ATOM   5663 C  CD  . GLU B 1 170 ? -33.543 3.288   -43.524  1.00 66.93  ?  168 GLU B CD  1 
ATOM   5664 O  OE1 . GLU B 1 170 ? -33.121 4.441   -43.290  1.00 66.02  ?  168 GLU B OE1 1 
ATOM   5665 O  OE2 . GLU B 1 170 ? -32.871 2.431   -44.135  1.00 70.90  -1 168 GLU B OE2 1 
ATOM   5666 N  N   . VAL B 1 171 ? -37.513 1.499   -41.425  1.00 61.36  ?  169 VAL B N   1 
ATOM   5667 C  CA  . VAL B 1 171 ? -37.657 0.282   -40.632  1.00 61.62  ?  169 VAL B CA  1 
ATOM   5668 C  C   . VAL B 1 171 ? -36.302 -0.391  -40.467  1.00 64.61  ?  169 VAL B C   1 
ATOM   5669 O  O   . VAL B 1 171 ? -35.486 -0.424  -41.397  1.00 66.28  ?  169 VAL B O   1 
ATOM   5670 C  CB  . VAL B 1 171 ? -38.679 -0.666  -41.284  1.00 70.69  ?  169 VAL B CB  1 
ATOM   5671 C  CG1 . VAL B 1 171 ? -38.465 -0.722  -42.789  1.00 72.47  ?  169 VAL B CG1 1 
ATOM   5672 C  CG2 . VAL B 1 171 ? -38.592 -2.054  -40.666  1.00 70.71  ?  169 VAL B CG2 1 
ATOM   5673 N  N   . GLY B 1 172 ? -36.053 -0.924  -39.272  1.00 64.12  ?  170 GLY B N   1 
ATOM   5674 C  CA  . GLY B 1 172 ? -34.845 -1.673  -39.005  1.00 59.27  ?  170 GLY B CA  1 
ATOM   5675 C  C   . GLY B 1 172 ? -33.699 -0.847  -38.473  1.00 60.72  ?  170 GLY B C   1 
ATOM   5676 O  O   . GLY B 1 172 ? -32.644 -1.412  -38.153  1.00 71.62  ?  170 GLY B O   1 
ATOM   5677 N  N   . LYS B 1 173 ? -33.866 0.470   -38.378  1.00 60.01  ?  171 LYS B N   1 
ATOM   5678 C  CA  . LYS B 1 173 ? -32.810 1.369   -37.965  1.00 64.79  ?  171 LYS B CA  1 
ATOM   5679 C  C   . LYS B 1 173 ? -33.262 2.212   -36.776  1.00 63.19  ?  171 LYS B C   1 
ATOM   5680 O  O   . LYS B 1 173 ? -34.423 2.629   -36.719  1.00 55.37  ?  171 LYS B O   1 
ATOM   5681 C  CB  . LYS B 1 173 ? -32.406 2.275   -39.135  1.00 60.21  ?  171 LYS B CB  1 
ATOM   5682 C  CG  . LYS B 1 173 ? -31.522 1.571   -40.158  1.00 65.77  ?  171 LYS B CG  1 
ATOM   5683 C  CD  . LYS B 1 173 ? -30.933 2.543   -41.165  1.00 64.98  ?  171 LYS B CD  1 
ATOM   5684 C  CE  . LYS B 1 173 ? -29.652 2.000   -41.771  1.00 62.04  ?  171 LYS B CE  1 
ATOM   5685 N  NZ  . LYS B 1 173 ? -28.824 3.090   -42.356  1.00 67.99  ?  171 LYS B NZ  1 
ATOM   5686 N  N   . PRO B 1 174 ? -32.380 2.462   -35.810  1.00 66.75  ?  172 PRO B N   1 
ATOM   5687 C  CA  . PRO B 1 174 ? -32.739 3.334   -34.685  1.00 68.05  ?  172 PRO B CA  1 
ATOM   5688 C  C   . PRO B 1 174 ? -33.084 4.746   -35.137  1.00 68.25  ?  172 PRO B C   1 
ATOM   5689 O  O   . PRO B 1 174 ? -32.620 5.224   -36.175  1.00 64.47  ?  172 PRO B O   1 
ATOM   5690 C  CB  . PRO B 1 174 ? -31.475 3.318   -33.815  1.00 65.71  ?  172 PRO B CB  1 
ATOM   5691 C  CG  . PRO B 1 174 ? -30.378 3.018   -34.798  1.00 69.39  ?  172 PRO B CG  1 
ATOM   5692 C  CD  . PRO B 1 174 ? -30.996 1.977   -35.687  1.00 67.30  ?  172 PRO B CD  1 
ATOM   5693 N  N   . ARG B 1 175 ? -33.933 5.421   -34.331  1.00 74.80  ?  173 ARG B N   1 
ATOM   5694 C  CA  . ARG B 1 175 ? -34.322 6.797   -34.629  1.00 74.57  ?  173 ARG B CA  1 
ATOM   5695 C  C   . ARG B 1 175 ? -33.458 7.767   -33.837  1.00 74.35  ?  173 ARG B C   1 
ATOM   5696 O  O   . ARG B 1 175 ? -33.252 7.567   -32.631  1.00 77.76  ?  173 ARG B O   1 
ATOM   5697 C  CB  . ARG B 1 175 ? -35.796 7.025   -34.303  1.00 76.02  ?  173 ARG B CB  1 
ATOM   5698 C  CG  . ARG B 1 175 ? -36.758 6.213   -35.163  1.00 74.00  ?  173 ARG B CG  1 
ATOM   5699 C  CD  . ARG B 1 175 ? -38.206 6.524   -34.812  1.00 78.20  ?  173 ARG B CD  1 
ATOM   5700 N  NE  . ARG B 1 175 ? -39.143 5.583   -35.415  1.00 77.84  ?  173 ARG B NE  1 
ATOM   5701 C  CZ  . ARG B 1 175 ? -40.460 5.638   -35.263  1.00 75.27  ?  173 ARG B CZ  1 
ATOM   5702 N  NH1 . ARG B 1 175 ? -41.036 6.612   -34.579  1.00 73.50  ?  173 ARG B NH1 1 
ATOM   5703 N  NH2 . ARG B 1 175 ? -41.218 4.701   -35.826  1.00 76.82  ?  173 ARG B NH2 1 
ATOM   5704 N  N   . PRO B 1 176 ? -32.940 8.813   -34.480  1.00 75.33  ?  174 PRO B N   1 
ATOM   5705 C  CA  . PRO B 1 176 ? -32.117 9.783   -33.762  1.00 74.98  ?  174 PRO B CA  1 
ATOM   5706 C  C   . PRO B 1 176 ? -32.916 10.518  -32.705  1.00 75.02  ?  174 PRO B C   1 
ATOM   5707 O  O   . PRO B 1 176 ? -34.150 10.650  -32.808  1.00 72.24  ?  174 PRO B O   1 
ATOM   5708 C  CB  . PRO B 1 176 ? -31.651 10.733  -34.875  1.00 73.07  ?  174 PRO B CB  1 
ATOM   5709 C  CG  . PRO B 1 176 ? -32.739 10.605  -35.909  1.00 71.16  ?  174 PRO B CG  1 
ATOM   5710 C  CD  . PRO B 1 176 ? -32.992 9.128   -35.916  1.00 72.40  ?  174 PRO B CD  1 
ATOM   5711 N  N   . PRO B 1 177 ? -32.249 11.011  -31.658  1.00 76.74  ?  175 PRO B N   1 
ATOM   5712 C  CA  . PRO B 1 177 ? -32.931 11.856  -30.667  1.00 78.53  ?  175 PRO B CA  1 
ATOM   5713 C  C   . PRO B 1 177 ? -33.228 13.229  -31.253  1.00 83.75  ?  175 PRO B C   1 
ATOM   5714 O  O   . PRO B 1 177 ? -32.369 13.849  -31.885  1.00 90.08  ?  175 PRO B O   1 
ATOM   5715 C  CB  . PRO B 1 177 ? -31.919 11.941  -29.515  1.00 80.53  ?  175 PRO B CB  1 
ATOM   5716 C  CG  . PRO B 1 177 ? -30.954 10.804  -29.768  1.00 86.89  ?  175 PRO B CG  1 
ATOM   5717 C  CD  . PRO B 1 177 ? -30.862 10.735  -31.259  1.00 77.96  ?  175 PRO B CD  1 
ATOM   5718 N  N   . LEU B 1 178 ? -34.458 13.698  -31.050  1.00 78.92  ?  176 LEU B N   1 
ATOM   5719 C  CA  . LEU B 1 178 ? -34.918 14.957  -31.638  1.00 80.52  ?  176 LEU B CA  1 
ATOM   5720 C  C   . LEU B 1 178 ? -34.599 16.144  -30.722  1.00 89.43  ?  176 LEU B C   1 
ATOM   5721 O  O   . LEU B 1 178 ? -35.474 16.757  -30.109  1.00 87.08  ?  176 LEU B O   1 
ATOM   5722 C  CB  . LEU B 1 178 ? -36.408 14.875  -31.943  1.00 80.76  ?  176 LEU B CB  1 
ATOM   5723 C  CG  . LEU B 1 178 ? -36.847 13.663  -32.770  1.00 79.03  ?  176 LEU B CG  1 
ATOM   5724 C  CD1 . LEU B 1 178 ? -38.319 13.768  -33.141  1.00 72.14  ?  176 LEU B CD1 1 
ATOM   5725 C  CD2 . LEU B 1 178 ? -35.980 13.497  -34.012  1.00 81.15  ?  176 LEU B CD2 1 
ATOM   5726 N  N   . ASN B 1 179 ? -33.308 16.465  -30.634  1.00 91.78  ?  177 ASN B N   1 
ATOM   5727 C  CA  . ASN B 1 179 ? -32.835 17.601  -29.846  1.00 85.23  ?  177 ASN B CA  1 
ATOM   5728 C  C   . ASN B 1 179 ? -31.892 18.434  -30.712  1.00 90.72  ?  177 ASN B C   1 
ATOM   5729 O  O   . ASN B 1 179 ? -31.679 18.138  -31.892  1.00 99.31  ?  177 ASN B O   1 
ATOM   5730 C  CB  . ASN B 1 179 ? -32.178 17.152  -28.530  1.00 89.61  ?  177 ASN B CB  1 
ATOM   5731 C  CG  . ASN B 1 179 ? -30.902 16.365  -28.740  1.00 96.28  ?  177 ASN B CG  1 
ATOM   5732 O  OD1 . ASN B 1 179 ? -29.905 16.893  -29.232  1.00 98.73  ?  177 ASN B OD1 1 
ATOM   5733 N  ND2 . ASN B 1 179 ? -30.921 15.095  -28.351  1.00 97.40  ?  177 ASN B ND2 1 
ATOM   5734 N  N   . ARG B 1 180 ? -31.317 19.489  -30.127  1.00 93.26  ?  178 ARG B N   1 
ATOM   5735 C  CA  . ARG B 1 180 ? -30.510 20.414  -30.916  1.00 98.73  ?  178 ARG B CA  1 
ATOM   5736 C  C   . ARG B 1 180 ? -29.078 19.944  -31.133  1.00 104.50 ?  178 ARG B C   1 
ATOM   5737 O  O   . ARG B 1 180 ? -28.335 20.603  -31.868  1.00 107.99 ?  178 ARG B O   1 
ATOM   5738 C  CB  . ARG B 1 180 ? -30.494 21.795  -30.255  1.00 103.64 ?  178 ARG B CB  1 
ATOM   5739 N  N   . ASN B 1 181 ? -28.669 18.835  -30.520  1.00 103.75 ?  179 ASN B N   1 
ATOM   5740 C  CA  . ASN B 1 181 ? -27.380 18.237  -30.840  1.00 99.55  ?  179 ASN B CA  1 
ATOM   5741 C  C   . ASN B 1 181 ? -27.459 17.360  -32.081  1.00 95.14  ?  179 ASN B C   1 
ATOM   5742 O  O   . ASN B 1 181 ? -26.439 16.802  -32.501  1.00 93.42  ?  179 ASN B O   1 
ATOM   5743 C  CB  . ASN B 1 181 ? -26.854 17.419  -29.655  1.00 95.57  ?  179 ASN B CB  1 
ATOM   5744 C  CG  . ASN B 1 181 ? -26.417 18.288  -28.490  1.00 104.37 ?  179 ASN B CG  1 
ATOM   5745 O  OD1 . ASN B 1 181 ? -26.341 19.512  -28.607  1.00 108.90 ?  179 ASN B OD1 1 
ATOM   5746 N  ND2 . ASN B 1 181 ? -26.121 17.657  -27.359  1.00 107.60 ?  179 ASN B ND2 1 
ATOM   5747 N  N   . TYR B 1 182 ? -28.649 17.224  -32.661  1.00 93.47  ?  180 TYR B N   1 
ATOM   5748 C  CA  . TYR B 1 182 ? -28.892 16.416  -33.853  1.00 91.17  ?  180 TYR B CA  1 
ATOM   5749 C  C   . TYR B 1 182 ? -29.507 17.315  -34.923  1.00 88.60  ?  180 TYR B C   1 
ATOM   5750 O  O   . TYR B 1 182 ? -30.698 17.636  -34.868  1.00 89.66  ?  180 TYR B O   1 
ATOM   5751 C  CB  . TYR B 1 182 ? -29.783 15.234  -33.496  1.00 84.87  ?  180 TYR B CB  1 
ATOM   5752 C  CG  . TYR B 1 182 ? -29.096 14.300  -32.529  1.00 86.86  ?  180 TYR B CG  1 
ATOM   5753 C  CD1 . TYR B 1 182 ? -28.243 13.304  -32.980  1.00 85.60  ?  180 TYR B CD1 1 
ATOM   5754 C  CD2 . TYR B 1 182 ? -29.251 14.458  -31.157  1.00 85.92  ?  180 TYR B CD2 1 
ATOM   5755 C  CE1 . TYR B 1 182 ? -27.593 12.464  -32.094  1.00 84.51  ?  180 TYR B CE1 1 
ATOM   5756 C  CE2 . TYR B 1 182 ? -28.607 13.624  -30.263  1.00 88.30  ?  180 TYR B CE2 1 
ATOM   5757 C  CZ  . TYR B 1 182 ? -27.778 12.629  -30.737  1.00 89.52  ?  180 TYR B CZ  1 
ATOM   5758 O  OH  . TYR B 1 182 ? -27.137 11.794  -29.850  1.00 87.75  ?  180 TYR B OH  1 
ATOM   5759 N  N   . VAL B 1 183 ? -28.689 17.716  -35.894  1.00 86.96  ?  181 VAL B N   1 
ATOM   5760 C  CA  . VAL B 1 183 ? -29.099 18.609  -36.974  1.00 83.62  ?  181 VAL B CA  1 
ATOM   5761 C  C   . VAL B 1 183 ? -29.302 17.789  -38.240  1.00 78.29  ?  181 VAL B C   1 
ATOM   5762 O  O   . VAL B 1 183 ? -28.451 16.964  -38.597  1.00 79.18  ?  181 VAL B O   1 
ATOM   5763 C  CB  . VAL B 1 183 ? -28.056 19.718  -37.197  1.00 84.00  ?  181 VAL B CB  1 
ATOM   5764 C  CG1 . VAL B 1 183 ? -28.557 20.730  -38.218  1.00 84.14  ?  181 VAL B CG1 1 
ATOM   5765 C  CG2 . VAL B 1 183 ? -27.711 20.398  -35.878  1.00 88.01  ?  181 VAL B CG2 1 
ATOM   5766 N  N   . PHE B 1 184 ? -30.417 18.028  -38.931  1.00 80.26  ?  182 PHE B N   1 
ATOM   5767 C  CA  . PHE B 1 184 ? -30.825 17.239  -40.084  1.00 80.55  ?  182 PHE B CA  1 
ATOM   5768 C  C   . PHE B 1 184 ? -30.710 18.067  -41.356  1.00 83.31  ?  182 PHE B C   1 
ATOM   5769 O  O   . PHE B 1 184 ? -30.835 19.295  -41.330  1.00 90.21  ?  182 PHE B O   1 
ATOM   5770 C  CB  . PHE B 1 184 ? -32.277 16.766  -39.954  1.00 79.28  ?  182 PHE B CB  1 
ATOM   5771 C  CG  . PHE B 1 184 ? -32.493 15.726  -38.899  1.00 77.03  ?  182 PHE B CG  1 
ATOM   5772 C  CD1 . PHE B 1 184 ? -32.708 16.096  -37.582  1.00 81.05  ?  182 PHE B CD1 1 
ATOM   5773 C  CD2 . PHE B 1 184 ? -32.506 14.381  -39.224  1.00 66.37  ?  182 PHE B CD2 1 
ATOM   5774 C  CE1 . PHE B 1 184 ? -32.918 15.144  -36.607  1.00 74.57  ?  182 PHE B CE1 1 
ATOM   5775 C  CE2 . PHE B 1 184 ? -32.715 13.424  -38.253  1.00 70.63  ?  182 PHE B CE2 1 
ATOM   5776 C  CZ  . PHE B 1 184 ? -32.922 13.806  -36.942  1.00 75.97  ?  182 PHE B CZ  1 
ATOM   5777 N  N   . THR B 1 185 ? -30.482 17.382  -42.474  1.00 81.59  ?  183 THR B N   1 
ATOM   5778 C  CA  . THR B 1 185 ? -30.454 18.009  -43.790  1.00 78.83  ?  183 THR B CA  1 
ATOM   5779 C  C   . THR B 1 185 ? -31.600 17.466  -44.631  1.00 72.91  ?  183 THR B C   1 
ATOM   5780 O  O   . THR B 1 185 ? -31.702 16.252  -44.838  1.00 76.78  ?  183 THR B O   1 
ATOM   5781 C  CB  . THR B 1 185 ? -29.117 17.767  -44.493  1.00 82.53  ?  183 THR B CB  1 
ATOM   5782 O  OG1 . THR B 1 185 ? -28.046 18.244  -43.668  1.00 82.05  ?  183 THR B OG1 1 
ATOM   5783 C  CG2 . THR B 1 185 ? -29.085 18.497  -45.829  1.00 81.38  ?  183 THR B CG2 1 
ATOM   5784 N  N   . GLY B 1 186 ? -32.456 18.365  -45.117  1.00 75.44  ?  184 GLY B N   1 
ATOM   5785 C  CA  . GLY B 1 186 ? -33.559 17.955  -45.956  1.00 78.64  ?  184 GLY B CA  1 
ATOM   5786 C  C   . GLY B 1 186 ? -33.119 17.647  -47.376  1.00 79.83  ?  184 GLY B C   1 
ATOM   5787 O  O   . GLY B 1 186 ? -32.040 18.036  -47.819  1.00 85.50  ?  184 GLY B O   1 
ATOM   5788 N  N   . TYR B 1 187 ? -33.986 16.944  -48.103  1.00 77.69  ?  185 TYR B N   1 
ATOM   5789 C  CA  . TYR B 1 187 ? -33.690 16.520  -49.465  1.00 81.02  ?  185 TYR B CA  1 
ATOM   5790 C  C   . TYR B 1 187 ? -34.998 16.345  -50.223  1.00 80.41  ?  185 TYR B C   1 
ATOM   5791 O  O   . TYR B 1 187 ? -36.001 15.915  -49.647  1.00 73.46  ?  185 TYR B O   1 
ATOM   5792 C  CB  . TYR B 1 187 ? -32.904 15.202  -49.487  1.00 70.35  ?  185 TYR B CB  1 
ATOM   5793 C  CG  . TYR B 1 187 ? -31.457 15.296  -49.045  1.00 74.06  ?  185 TYR B CG  1 
ATOM   5794 C  CD1 . TYR B 1 187 ? -30.460 15.678  -49.934  1.00 78.34  ?  185 TYR B CD1 1 
ATOM   5795 C  CD2 . TYR B 1 187 ? -31.087 14.982  -47.744  1.00 71.29  ?  185 TYR B CD2 1 
ATOM   5796 C  CE1 . TYR B 1 187 ? -29.136 15.755  -49.535  1.00 78.45  ?  185 TYR B CE1 1 
ATOM   5797 C  CE2 . TYR B 1 187 ? -29.767 15.057  -47.337  1.00 76.11  ?  185 TYR B CE2 1 
ATOM   5798 C  CZ  . TYR B 1 187 ? -28.796 15.443  -48.235  1.00 79.11  ?  185 TYR B CZ  1 
ATOM   5799 O  OH  . TYR B 1 187 ? -27.482 15.517  -47.833  1.00 88.35  ?  185 TYR B OH  1 
ATOM   5800 N  N   . ARG B 1 188 ? -34.984 16.678  -51.514  1.00 82.38  ?  186 ARG B N   1 
ATOM   5801 C  CA  . ARG B 1 188 ? -36.138 16.504  -52.386  1.00 85.73  ?  186 ARG B CA  1 
ATOM   5802 C  C   . ARG B 1 188 ? -35.803 15.531  -53.510  1.00 86.20  ?  186 ARG B C   1 
ATOM   5803 O  O   . ARG B 1 188 ? -34.720 15.597  -54.100  1.00 86.37  ?  186 ARG B O   1 
ATOM   5804 C  CB  . ARG B 1 188 ? -36.594 17.844  -52.975  1.00 84.81  ?  186 ARG B CB  1 
ATOM   5805 N  N   . VAL B 1 189 ? -36.744 14.640  -53.811  1.00 85.32  ?  187 VAL B N   1 
ATOM   5806 C  CA  . VAL B 1 189 ? -36.523 13.588  -54.800  1.00 90.59  ?  187 VAL B CA  1 
ATOM   5807 C  C   . VAL B 1 189 ? -36.640 14.170  -56.203  1.00 91.89  ?  187 VAL B C   1 
ATOM   5808 O  O   . VAL B 1 189 ? -37.644 14.807  -56.543  1.00 95.62  ?  187 VAL B O   1 
ATOM   5809 C  CB  . VAL B 1 189 ? -37.516 12.432  -54.596  1.00 87.01  ?  187 VAL B CB  1 
ATOM   5810 C  CG1 . VAL B 1 189 ? -37.417 11.441  -55.745  1.00 81.13  ?  187 VAL B CG1 1 
ATOM   5811 C  CG2 . VAL B 1 189 ? -37.257 11.737  -53.267  1.00 83.71  ?  187 VAL B CG2 1 
ATOM   5812 N  N   . THR B 1 190 ? -35.616 13.946  -57.021  1.00 91.20  ?  188 THR B N   1 
ATOM   5813 C  CA  . THR B 1 190 ? -35.609 14.330  -58.426  1.00 97.00  ?  188 THR B CA  1 
ATOM   5814 C  C   . THR B 1 190 ? -35.560 13.081  -59.298  1.00 102.47 ?  188 THR B C   1 
ATOM   5815 O  O   . THR B 1 190 ? -35.451 11.953  -58.808  1.00 100.43 ?  188 THR B O   1 
ATOM   5816 C  CB  . THR B 1 190 ? -34.428 15.254  -58.751  1.00 99.12  ?  188 THR B CB  1 
ATOM   5817 O  OG1 . THR B 1 190 ? -33.233 14.477  -58.906  1.00 99.44  ?  188 THR B OG1 1 
ATOM   5818 C  CG2 . THR B 1 190 ? -34.228 16.285  -57.649  1.00 96.60  ?  188 THR B CG2 1 
ATOM   5819 N  N   . LYS B 1 191 ? -35.664 13.300  -60.612  1.00 103.55 ?  189 LYS B N   1 
ATOM   5820 C  CA  . LYS B 1 191 ? -35.702 12.197  -61.569  1.00 110.60 ?  189 LYS B CA  1 
ATOM   5821 C  C   . LYS B 1 191 ? -34.655 11.131  -61.266  1.00 112.56 ?  189 LYS B C   1 
ATOM   5822 O  O   . LYS B 1 191 ? -34.977 9.944   -61.144  1.00 114.54 ?  189 LYS B O   1 
ATOM   5823 C  CB  . LYS B 1 191 ? -35.514 12.740  -62.989  1.00 117.47 ?  189 LYS B CB  1 
ATOM   5824 N  N   . ASN B 1 192 ? -33.388 11.535  -61.145  1.00 110.98 ?  190 ASN B N   1 
ATOM   5825 C  CA  . ASN B 1 192 ? -32.302 10.585  -60.939  1.00 104.95 ?  190 ASN B CA  1 
ATOM   5826 C  C   . ASN B 1 192 ? -31.422 10.915  -59.738  1.00 104.22 ?  190 ASN B C   1 
ATOM   5827 O  O   . ASN B 1 192 ? -30.391 10.259  -59.552  1.00 104.03 ?  190 ASN B O   1 
ATOM   5828 C  CB  . ASN B 1 192 ? -31.430 10.484  -62.197  1.00 114.07 ?  190 ASN B CB  1 
ATOM   5829 C  CG  . ASN B 1 192 ? -31.839 9.337   -63.102  1.00 118.42 ?  190 ASN B CG  1 
ATOM   5830 O  OD1 . ASN B 1 192 ? -32.708 8.537   -62.754  1.00 119.41 ?  190 ASN B OD1 1 
ATOM   5831 N  ND2 . ASN B 1 192 ? -31.208 9.248   -64.267  1.00 126.64 ?  190 ASN B ND2 1 
ATOM   5832 N  N   . SER B 1 193 ? -31.787 11.896  -58.919  1.00 97.03  ?  191 SER B N   1 
ATOM   5833 C  CA  . SER B 1 193 ? -30.986 12.164  -57.730  1.00 91.66  ?  191 SER B CA  1 
ATOM   5834 C  C   . SER B 1 193 ? -31.804 12.976  -56.726  1.00 89.66  ?  191 SER B C   1 
ATOM   5835 O  O   . SER B 1 193 ? -33.040 12.982  -56.772  1.00 87.39  ?  191 SER B O   1 
ATOM   5836 C  CB  . SER B 1 193 ? -29.677 12.871  -58.120  1.00 97.92  ?  191 SER B CB  1 
ATOM   5837 O  OG  . SER B 1 193 ? -28.814 12.995  -57.003  1.00 101.80 ?  191 SER B OG  1 
ATOM   5838 N  N   . LYS B 1 194 ? -31.100 13.656  -55.822  1.00 93.73  ?  192 LYS B N   1 
ATOM   5839 C  CA  . LYS B 1 194 ? -31.669 14.442  -54.738  1.00 89.60  ?  192 LYS B CA  1 
ATOM   5840 C  C   . LYS B 1 194 ? -31.087 15.849  -54.783  1.00 96.46  ?  192 LYS B C   1 
ATOM   5841 O  O   . LYS B 1 194 ? -29.998 16.070  -55.318  1.00 92.16  ?  192 LYS B O   1 
ATOM   5842 C  CB  . LYS B 1 194 ? -31.355 13.797  -53.385  1.00 83.12  ?  192 LYS B CB  1 
ATOM   5843 C  CG  . LYS B 1 194 ? -29.862 13.533  -53.209  1.00 86.73  ?  192 LYS B CG  1 
ATOM   5844 C  CD  . LYS B 1 194 ? -29.521 12.989  -51.835  1.00 86.42  ?  192 LYS B CD  1 
ATOM   5845 C  CE  . LYS B 1 194 ? -28.021 12.755  -51.698  1.00 92.12  ?  192 LYS B CE  1 
ATOM   5846 N  NZ  . LYS B 1 194 ? -27.664 12.240  -50.345  1.00 83.27  ?  192 LYS B NZ  1 
ATOM   5847 N  N   . VAL B 1 195 ? -31.819 16.809  -54.217  1.00 96.06  ?  193 VAL B N   1 
ATOM   5848 C  CA  . VAL B 1 195 ? -31.320 18.171  -54.054  1.00 98.38  ?  193 VAL B CA  1 
ATOM   5849 C  C   . VAL B 1 195 ? -31.489 18.594  -52.600  1.00 89.61  ?  193 VAL B C   1 
ATOM   5850 O  O   . VAL B 1 195 ? -32.572 18.435  -52.025  1.00 90.18  ?  193 VAL B O   1 
ATOM   5851 C  CB  . VAL B 1 195 ? -32.033 19.162  -54.996  1.00 98.81  ?  193 VAL B CB  1 
ATOM   5852 C  CG1 . VAL B 1 195 ? -33.539 18.944  -54.967  1.00 102.87 ?  193 VAL B CG1 1 
ATOM   5853 C  CG2 . VAL B 1 195 ? -31.682 20.595  -54.623  1.00 102.05 ?  193 VAL B CG2 1 
ATOM   5854 N  N   . GLN B 1 196 ? -30.417 19.124  -52.008  1.00 92.65  ?  194 GLN B N   1 
ATOM   5855 C  CA  . GLN B 1 196 ? -30.489 19.662  -50.655  1.00 92.53  ?  194 GLN B CA  1 
ATOM   5856 C  C   . GLN B 1 196 ? -31.549 20.753  -50.569  1.00 91.96  ?  194 GLN B C   1 
ATOM   5857 O  O   . GLN B 1 196 ? -31.656 21.609  -51.451  1.00 95.07  ?  194 GLN B O   1 
ATOM   5858 C  CB  . GLN B 1 196 ? -29.131 20.220  -50.222  1.00 90.83  ?  194 GLN B CB  1 
ATOM   5859 C  CG  . GLN B 1 196 ? -28.068 19.166  -49.947  1.00 91.93  ?  194 GLN B CG  1 
ATOM   5860 C  CD  . GLN B 1 196 ? -27.017 19.641  -48.957  1.00 101.28 ?  194 GLN B CD  1 
ATOM   5861 O  OE1 . GLN B 1 196 ? -27.101 20.750  -48.428  1.00 97.71  ?  194 GLN B OE1 1 
ATOM   5862 N  NE2 . GLN B 1 196 ? -26.019 18.801  -48.704  1.00 101.18 ?  194 GLN B NE2 1 
ATOM   5863 N  N   . ILE B 1 197 ? -32.331 20.725  -49.493  1.00 90.68  ?  195 ILE B N   1 
ATOM   5864 C  CA  . ILE B 1 197 ? -33.418 21.681  -49.325  1.00 91.67  ?  195 ILE B CA  1 
ATOM   5865 C  C   . ILE B 1 197 ? -33.276 22.403  -47.990  1.00 103.47 ?  195 ILE B C   1 
ATOM   5866 O  O   . ILE B 1 197 ? -34.197 23.098  -47.548  1.00 108.31 ?  195 ILE B O   1 
ATOM   5867 C  CB  . ILE B 1 197 ? -34.787 20.981  -49.439  1.00 94.13  ?  195 ILE B CB  1 
ATOM   5868 C  CG1 . ILE B 1 197 ? -35.875 21.985  -49.833  1.00 101.31 ?  195 ILE B CG1 1 
ATOM   5869 C  CG2 . ILE B 1 197 ? -35.134 20.258  -48.145  1.00 85.73  ?  195 ILE B CG2 1 
ATOM   5870 C  CD1 . ILE B 1 197 ? -35.609 22.697  -51.142  1.00 99.53  ?  195 ILE B CD1 1 
ATOM   5871 N  N   . GLY B 1 198 ? -32.123 22.247  -47.341  1.00 101.05 ?  196 GLY B N   1 
ATOM   5872 C  CA  . GLY B 1 198 ? -31.853 22.995  -46.129  1.00 96.89  ?  196 GLY B CA  1 
ATOM   5873 C  C   . GLY B 1 198 ? -31.538 22.127  -44.929  1.00 92.00  ?  196 GLY B C   1 
ATOM   5874 O  O   . GLY B 1 198 ? -31.849 20.933  -44.921  1.00 91.27  ?  196 GLY B O   1 
ATOM   5875 N  N   . GLU B 1 199 ? -30.914 22.712  -43.910  1.00 91.39  ?  197 GLU B N   1 
ATOM   5876 C  CA  . GLU B 1 199 ? -30.680 22.011  -42.657  1.00 89.97  ?  197 GLU B CA  1 
ATOM   5877 C  C   . GLU B 1 199 ? -31.875 22.223  -41.736  1.00 89.45  ?  197 GLU B C   1 
ATOM   5878 O  O   . GLU B 1 199 ? -32.593 23.222  -41.840  1.00 91.46  ?  197 GLU B O   1 
ATOM   5879 C  CB  . GLU B 1 199 ? -29.386 22.487  -41.992  1.00 94.78  ?  197 GLU B CB  1 
ATOM   5880 C  CG  . GLU B 1 199 ? -28.132 21.856  -42.595  1.00 96.32  ?  197 GLU B CG  1 
ATOM   5881 C  CD  . GLU B 1 199 ? -26.854 22.244  -41.869  1.00 101.50 ?  197 GLU B CD  1 
ATOM   5882 O  OE1 . GLU B 1 199 ? -26.540 23.452  -41.807  1.00 100.27 ?  197 GLU B OE1 1 
ATOM   5883 O  OE2 . GLU B 1 199 ? -26.158 21.335  -41.366  1.00 101.72 -1 197 GLU B OE2 1 
ATOM   5884 N  N   . TYR B 1 200 ? -32.081 21.276  -40.824  1.00 89.61  ?  198 TYR B N   1 
ATOM   5885 C  CA  . TYR B 1 200 ? -33.284 21.288  -40.007  1.00 89.97  ?  198 TYR B CA  1 
ATOM   5886 C  C   . TYR B 1 200 ? -32.993 20.690  -38.640  1.00 90.06  ?  198 TYR B C   1 
ATOM   5887 O  O   . TYR B 1 200 ? -32.065 19.896  -38.464  1.00 91.42  ?  198 TYR B O   1 
ATOM   5888 C  CB  . TYR B 1 200 ? -34.420 20.482  -40.656  1.00 92.44  ?  198 TYR B CB  1 
ATOM   5889 C  CG  . TYR B 1 200 ? -35.087 21.123  -41.852  1.00 91.76  ?  198 TYR B CG  1 
ATOM   5890 C  CD1 . TYR B 1 200 ? -34.496 21.071  -43.107  1.00 94.66  ?  198 TYR B CD1 1 
ATOM   5891 C  CD2 . TYR B 1 200 ? -36.322 21.748  -41.736  1.00 93.74  ?  198 TYR B CD2 1 
ATOM   5892 C  CE1 . TYR B 1 200 ? -35.101 21.641  -44.208  1.00 94.92  ?  198 TYR B CE1 1 
ATOM   5893 C  CE2 . TYR B 1 200 ? -36.938 22.321  -42.834  1.00 100.44 ?  198 TYR B CE2 1 
ATOM   5894 C  CZ  . TYR B 1 200 ? -36.321 22.264  -44.068  1.00 99.63  ?  198 TYR B CZ  1 
ATOM   5895 O  OH  . TYR B 1 200 ? -36.922 22.832  -45.168  1.00 105.21 ?  198 TYR B OH  1 
ATOM   5896 N  N   . THR B 1 201 ? -33.811 21.092  -37.674  1.00 92.17  ?  199 THR B N   1 
ATOM   5897 C  CA  . THR B 1 201 ? -33.766 20.595  -36.308  1.00 91.36  ?  199 THR B CA  1 
ATOM   5898 C  C   . THR B 1 201 ? -35.206 20.332  -35.896  1.00 91.73  ?  199 THR B C   1 
ATOM   5899 O  O   . THR B 1 201 ? -36.089 21.148  -36.177  1.00 97.46  ?  199 THR B O   1 
ATOM   5900 C  CB  . THR B 1 201 ? -33.082 21.595  -35.362  1.00 88.79  ?  199 THR B CB  1 
ATOM   5901 O  OG1 . THR B 1 201 ? -31.673 21.331  -35.324  1.00 94.53  ?  199 THR B OG1 1 
ATOM   5902 C  CG2 . THR B 1 201 ? -33.652 21.492  -33.955  1.00 95.77  ?  199 THR B CG2 1 
ATOM   5903 N  N   . PHE B 1 202 ? -35.450 19.202  -35.239  1.00 84.46  ?  200 PHE B N   1 
ATOM   5904 C  CA  . PHE B 1 202 ? -36.811 18.790  -34.933  1.00 86.89  ?  200 PHE B CA  1 
ATOM   5905 C  C   . PHE B 1 202 ? -36.996 18.607  -33.434  1.00 87.59  ?  200 PHE B C   1 
ATOM   5906 O  O   . PHE B 1 202 ? -36.032 18.471  -32.675  1.00 89.79  ?  200 PHE B O   1 
ATOM   5907 C  CB  . PHE B 1 202 ? -37.167 17.459  -35.619  1.00 85.78  ?  200 PHE B CB  1 
ATOM   5908 C  CG  . PHE B 1 202 ? -37.102 17.493  -37.120  1.00 81.77  ?  200 PHE B CG  1 
ATOM   5909 C  CD1 . PHE B 1 202 ? -35.902 17.276  -37.775  1.00 81.89  ?  200 PHE B CD1 1 
ATOM   5910 C  CD2 . PHE B 1 202 ? -38.244 17.703  -37.876  1.00 87.15  ?  200 PHE B CD2 1 
ATOM   5911 C  CE1 . PHE B 1 202 ? -35.835 17.288  -39.155  1.00 87.34  ?  200 PHE B CE1 1 
ATOM   5912 C  CE2 . PHE B 1 202 ? -38.183 17.716  -39.259  1.00 90.26  ?  200 PHE B CE2 1 
ATOM   5913 C  CZ  . PHE B 1 202 ? -36.977 17.508  -39.898  1.00 87.55  ?  200 PHE B CZ  1 
ATOM   5914 N  N   . GLU B 1 203 ? -38.261 18.604  -33.019  1.00 88.56  ?  201 GLU B N   1 
ATOM   5915 C  CA  . GLU B 1 203 ? -38.626 18.278  -31.647  1.00 90.09  ?  201 GLU B CA  1 
ATOM   5916 C  C   . GLU B 1 203 ? -40.063 17.776  -31.633  1.00 88.96  ?  201 GLU B C   1 
ATOM   5917 O  O   . GLU B 1 203 ? -40.861 18.092  -32.518  1.00 90.38  ?  201 GLU B O   1 
ATOM   5918 C  CB  . GLU B 1 203 ? -38.444 19.464  -30.694  1.00 87.04  ?  201 GLU B CB  1 
ATOM   5919 C  CG  . GLU B 1 203 ? -38.487 19.035  -29.233  1.00 91.07  ?  201 GLU B CG  1 
ATOM   5920 C  CD  . GLU B 1 203 ? -37.836 20.027  -28.291  1.00 98.69  ?  201 GLU B CD  1 
ATOM   5921 O  OE1 . GLU B 1 203 ? -37.405 21.104  -28.753  1.00 101.08 ?  201 GLU B OE1 1 
ATOM   5922 O  OE2 . GLU B 1 203 ? -37.749 19.720  -27.082  1.00 102.98 -1 201 GLU B OE2 1 
ATOM   5923 N  N   . LYS B 1 204 ? -40.378 16.994  -30.603  1.00 88.62  ?  202 LYS B N   1 
ATOM   5924 C  CA  . LYS B 1 204 ? -41.695 16.385  -30.482  1.00 88.11  ?  202 LYS B CA  1 
ATOM   5925 C  C   . LYS B 1 204 ? -42.779 17.451  -30.359  1.00 93.84  ?  202 LYS B C   1 
ATOM   5926 O  O   . LYS B 1 204 ? -42.534 18.571  -29.902  1.00 96.34  ?  202 LYS B O   1 
ATOM   5927 C  CB  . LYS B 1 204 ? -41.723 15.461  -29.264  1.00 89.75  ?  202 LYS B CB  1 
ATOM   5928 C  CG  . LYS B 1 204 ? -42.967 14.605  -29.116  1.00 88.53  ?  202 LYS B CG  1 
ATOM   5929 C  CD  . LYS B 1 204 ? -42.945 13.885  -27.774  1.00 92.17  ?  202 LYS B CD  1 
ATOM   5930 C  CE  . LYS B 1 204 ? -44.138 12.962  -27.601  1.00 90.07  ?  202 LYS B CE  1 
ATOM   5931 N  NZ  . LYS B 1 204 ? -44.111 12.272  -26.280  1.00 100.84 ?  202 LYS B NZ  1 
ATOM   5932 N  N   . GLY B 1 205 ? -43.993 17.088  -30.763  1.00 92.92  ?  203 GLY B N   1 
ATOM   5933 C  CA  . GLY B 1 205 ? -45.124 17.994  -30.677  1.00 93.41  ?  203 GLY B CA  1 
ATOM   5934 C  C   . GLY B 1 205 ? -46.471 17.304  -30.580  1.00 90.59  ?  203 GLY B C   1 
ATOM   5935 O  O   . GLY B 1 205 ? -47.482 17.938  -30.276  1.00 101.91 ?  203 GLY B O   1 
ATOM   5936 N  N   . ALA B 1 210 ? -45.984 14.404  -36.183  1.00 85.97  ?  208 ALA B N   1 
ATOM   5937 C  CA  . ALA B 1 210 ? -46.134 14.798  -34.788  1.00 85.69  ?  208 ALA B CA  1 
ATOM   5938 C  C   . ALA B 1 210 ? -44.868 15.477  -34.270  1.00 91.10  ?  208 ALA B C   1 
ATOM   5939 O  O   . ALA B 1 210 ? -44.534 15.364  -33.090  1.00 91.42  ?  208 ALA B O   1 
ATOM   5940 C  CB  . ALA B 1 210 ? -46.478 13.587  -33.929  1.00 82.57  ?  208 ALA B CB  1 
ATOM   5941 N  N   . VAL B 1 211 ? -44.165 16.182  -35.159  1.00 89.47  ?  209 VAL B N   1 
ATOM   5942 C  CA  . VAL B 1 211 ? -42.907 16.833  -34.821  1.00 91.22  ?  209 VAL B CA  1 
ATOM   5943 C  C   . VAL B 1 211 ? -42.965 18.297  -35.236  1.00 91.73  ?  209 VAL B C   1 
ATOM   5944 O  O   . VAL B 1 211 ? -43.752 18.697  -36.096  1.00 91.81  ?  209 VAL B O   1 
ATOM   5945 C  CB  . VAL B 1 211 ? -41.692 16.145  -35.480  1.00 85.86  ?  209 VAL B CB  1 
ATOM   5946 C  CG1 . VAL B 1 211 ? -41.644 14.673  -35.103  1.00 81.12  ?  209 VAL B CG1 1 
ATOM   5947 C  CG2 . VAL B 1 211 ? -41.733 16.324  -36.991  1.00 85.67  ?  209 VAL B CG2 1 
ATOM   5948 N  N   . VAL B 1 212 ? -42.115 19.096  -34.599  1.00 91.41  ?  210 VAL B N   1 
ATOM   5949 C  CA  . VAL B 1 212 ? -41.968 20.518  -34.890  1.00 95.65  ?  210 VAL B CA  1 
ATOM   5950 C  C   . VAL B 1 212 ? -40.606 20.718  -35.541  1.00 98.83  ?  210 VAL B C   1 
ATOM   5951 O  O   . VAL B 1 212 ? -39.581 20.324  -34.971  1.00 97.02  ?  210 VAL B O   1 
ATOM   5952 C  CB  . VAL B 1 212 ? -42.098 21.366  -33.615  1.00 97.69  ?  210 VAL B CB  1 
ATOM   5953 C  CG1 . VAL B 1 212 ? -41.497 22.747  -33.825  1.00 101.25 ?  210 VAL B CG1 1 
ATOM   5954 C  CG2 . VAL B 1 212 ? -43.553 21.458  -33.177  1.00 95.52  ?  210 VAL B CG2 1 
ATOM   5955 N  N   . TYR B 1 213 ? -40.581 21.324  -36.729  1.00 106.22 ?  211 TYR B N   1 
ATOM   5956 C  CA  . TYR B 1 213 ? -39.338 21.485  -37.471  1.00 105.88 ?  211 TYR B CA  1 
ATOM   5957 C  C   . TYR B 1 213 ? -38.867 22.932  -37.398  1.00 106.09 ?  211 TYR B C   1 
ATOM   5958 O  O   . TYR B 1 213 ? -39.669 23.865  -37.509  1.00 105.50 ?  211 TYR B O   1 
ATOM   5959 C  CB  . TYR B 1 213 ? -39.477 21.044  -38.937  1.00 104.13 ?  211 TYR B CB  1 
ATOM   5960 C  CG  . TYR B 1 213 ? -40.552 21.725  -39.765  1.00 106.31 ?  211 TYR B CG  1 
ATOM   5961 C  CD1 . TYR B 1 213 ? -41.841 21.212  -39.832  1.00 104.12 ?  211 TYR B CD1 1 
ATOM   5962 C  CD2 . TYR B 1 213 ? -40.259 22.854  -40.522  1.00 108.46 ?  211 TYR B CD2 1 
ATOM   5963 C  CE1 . TYR B 1 213 ? -42.816 21.822  -40.606  1.00 104.70 ?  211 TYR B CE1 1 
ATOM   5964 C  CE2 . TYR B 1 213 ? -41.227 23.470  -41.298  1.00 110.62 ?  211 TYR B CE2 1 
ATOM   5965 C  CZ  . TYR B 1 213 ? -42.503 22.950  -41.336  1.00 109.58 ?  211 TYR B CZ  1 
ATOM   5966 O  OH  . TYR B 1 213 ? -43.468 23.560  -42.106  1.00 106.36 ?  211 TYR B OH  1 
ATOM   5967 N  N   . ARG B 1 214 ? -37.560 23.109  -37.209  1.00 107.29 ?  212 ARG B N   1 
ATOM   5968 C  CA  . ARG B 1 214 ? -36.910 24.418  -37.156  1.00 112.08 ?  212 ARG B CA  1 
ATOM   5969 C  C   . ARG B 1 214 ? -35.820 24.480  -38.225  1.00 109.92 ?  212 ARG B C   1 
ATOM   5970 O  O   . ARG B 1 214 ? -34.647 24.220  -37.947  1.00 107.57 ?  212 ARG B O   1 
ATOM   5971 C  CB  . ARG B 1 214 ? -36.338 24.682  -35.762  1.00 107.75 ?  212 ARG B CB  1 
ATOM   5972 N  N   . GLY B 1 215 ? -36.208 24.836  -39.447  1.00 109.82 ?  213 GLY B N   1 
ATOM   5973 C  CA  . GLY B 1 215 ? -35.277 24.865  -40.557  1.00 108.65 ?  213 GLY B CA  1 
ATOM   5974 C  C   . GLY B 1 215 ? -34.633 26.229  -40.746  1.00 117.33 ?  213 GLY B C   1 
ATOM   5975 O  O   . GLY B 1 215 ? -35.240 27.266  -40.492  1.00 118.38 ?  213 GLY B O   1 
ATOM   5976 N  N   . THR B 1 216 ? -33.376 26.211  -41.198  1.00 115.99 ?  214 THR B N   1 
ATOM   5977 C  CA  . THR B 1 216 ? -32.662 27.460  -41.445  1.00 120.48 ?  214 THR B CA  1 
ATOM   5978 C  C   . THR B 1 216 ? -33.370 28.286  -42.511  1.00 126.82 ?  214 THR B C   1 
ATOM   5979 O  O   . THR B 1 216 ? -33.698 29.458  -42.292  1.00 131.85 ?  214 THR B O   1 
ATOM   5980 C  CB  . THR B 1 216 ? -31.218 27.169  -41.858  1.00 117.53 ?  214 THR B CB  1 
ATOM   5981 N  N   . THR B 1 217 ? -33.609 27.691  -43.676  1.00 125.31 ?  215 THR B N   1 
ATOM   5982 C  CA  . THR B 1 217 ? -34.347 28.354  -44.735  1.00 123.50 ?  215 THR B CA  1 
ATOM   5983 C  C   . THR B 1 217 ? -35.822 27.980  -44.610  1.00 127.77 ?  215 THR B C   1 
ATOM   5984 O  O   . THR B 1 217 ? -36.213 27.175  -43.760  1.00 122.66 ?  215 THR B O   1 
ATOM   5985 C  CB  . THR B 1 217 ? -33.783 27.977  -46.104  1.00 124.54 ?  215 THR B CB  1 
ATOM   5986 O  OG1 . THR B 1 217 ? -34.576 28.581  -47.134  1.00 129.66 ?  215 THR B OG1 1 
ATOM   5987 C  CG2 . THR B 1 217 ? -33.789 26.466  -46.286  1.00 118.34 ?  215 THR B CG2 1 
ATOM   5988 N  N   . THR B 1 218 ? -36.660 28.563  -45.462  1.00 125.16 ?  216 THR B N   1 
ATOM   5989 C  CA  . THR B 1 218 ? -38.082 28.251  -45.477  1.00 125.33 ?  216 THR B CA  1 
ATOM   5990 C  C   . THR B 1 218 ? -38.481 27.743  -46.854  1.00 122.64 ?  216 THR B C   1 
ATOM   5991 O  O   . THR B 1 218 ? -38.236 28.411  -47.864  1.00 126.45 ?  216 THR B O   1 
ATOM   5992 C  CB  . THR B 1 218 ? -38.922 29.475  -45.095  1.00 126.99 ?  216 THR B CB  1 
ATOM   5993 O  OG1 . THR B 1 218 ? -40.287 29.260  -45.477  1.00 130.98 ?  216 THR B OG1 1 
ATOM   5994 C  CG2 . THR B 1 218 ? -38.393 30.724  -45.782  1.00 136.88 ?  216 THR B CG2 1 
ATOM   5995 N  N   . TYR B 1 219 ? -39.096 26.562  -46.885  1.00 119.67 ?  217 TYR B N   1 
ATOM   5996 C  CA  . TYR B 1 219 ? -39.596 25.958  -48.110  1.00 116.48 ?  217 TYR B CA  1 
ATOM   5997 C  C   . TYR B 1 219 ? -40.905 25.245  -47.806  1.00 113.46 ?  217 TYR B C   1 
ATOM   5998 O  O   . TYR B 1 219 ? -41.094 24.700  -46.716  1.00 117.88 ?  217 TYR B O   1 
ATOM   5999 C  CB  . TYR B 1 219 ? -38.586 24.975  -48.720  1.00 113.72 ?  217 TYR B CB  1 
ATOM   6000 C  CG  . TYR B 1 219 ? -37.503 25.640  -49.541  1.00 119.25 ?  217 TYR B CG  1 
ATOM   6001 C  CD1 . TYR B 1 219 ? -37.695 25.906  -50.892  1.00 122.92 ?  217 TYR B CD1 1 
ATOM   6002 C  CD2 . TYR B 1 219 ? -36.292 26.002  -48.968  1.00 119.99 ?  217 TYR B CD2 1 
ATOM   6003 C  CE1 . TYR B 1 219 ? -36.711 26.518  -51.647  1.00 121.53 ?  217 TYR B CE1 1 
ATOM   6004 C  CE2 . TYR B 1 219 ? -35.300 26.612  -49.717  1.00 119.25 ?  217 TYR B CE2 1 
ATOM   6005 C  CZ  . TYR B 1 219 ? -35.516 26.868  -51.055  1.00 123.40 ?  217 TYR B CZ  1 
ATOM   6006 O  OH  . TYR B 1 219 ? -34.532 27.472  -51.805  1.00 130.05 ?  217 TYR B OH  1 
ATOM   6007 N  N   . LYS B 1 220 ? -41.812 25.262  -48.782  1.00 112.16 ?  218 LYS B N   1 
ATOM   6008 C  CA  . LYS B 1 220 ? -43.098 24.575  -48.665  1.00 105.33 ?  218 LYS B CA  1 
ATOM   6009 C  C   . LYS B 1 220 ? -42.872 23.068  -48.764  1.00 106.19 ?  218 LYS B C   1 
ATOM   6010 O  O   . LYS B 1 220 ? -43.111 22.434  -49.794  1.00 108.58 ?  218 LYS B O   1 
ATOM   6011 C  CB  . LYS B 1 220 ? -44.067 25.065  -49.735  1.00 109.39 ?  218 LYS B CB  1 
ATOM   6012 N  N   . LEU B 1 221 ? -42.385 22.488  -47.666  1.00 108.37 ?  219 LEU B N   1 
ATOM   6013 C  CA  . LEU B 1 221 ? -42.097 21.059  -47.641  1.00 104.57 ?  219 LEU B CA  1 
ATOM   6014 C  C   . LEU B 1 221 ? -43.325 20.264  -48.061  1.00 101.62 ?  219 LEU B C   1 
ATOM   6015 O  O   . LEU B 1 221 ? -44.465 20.639  -47.772  1.00 102.92 ?  219 LEU B O   1 
ATOM   6016 C  CB  . LEU B 1 221 ? -41.644 20.622  -46.246  1.00 97.67  ?  219 LEU B CB  1 
ATOM   6017 C  CG  . LEU B 1 221 ? -40.159 20.770  -45.912  1.00 101.67 ?  219 LEU B CG  1 
ATOM   6018 C  CD1 . LEU B 1 221 ? -39.756 22.232  -45.871  1.00 107.38 ?  219 LEU B CD1 1 
ATOM   6019 C  CD2 . LEU B 1 221 ? -39.849 20.092  -44.588  1.00 103.57 ?  219 LEU B CD2 1 
ATOM   6020 N  N   . ASN B 1 222 ? -43.085 19.149  -48.746  1.00 98.15  ?  220 ASN B N   1 
ATOM   6021 C  CA  . ASN B 1 222 ? -44.160 18.308  -49.245  1.00 92.85  ?  220 ASN B CA  1 
ATOM   6022 C  C   . ASN B 1 222 ? -43.823 16.844  -49.004  1.00 90.90  ?  220 ASN B C   1 
ATOM   6023 O  O   . ASN B 1 222 ? -42.682 16.485  -48.699  1.00 92.01  ?  220 ASN B O   1 
ATOM   6024 C  CB  . ASN B 1 222 ? -44.414 18.574  -50.734  1.00 97.57  ?  220 ASN B CB  1 
ATOM   6025 C  CG  . ASN B 1 222 ? -43.128 18.774  -51.517  1.00 105.35 ?  220 ASN B CG  1 
ATOM   6026 O  OD1 . ASN B 1 222 ? -42.332 19.662  -51.208  1.00 103.44 ?  220 ASN B OD1 1 
ATOM   6027 N  ND2 . ASN B 1 222 ? -42.923 17.954  -52.541  1.00 108.52 ?  220 ASN B ND2 1 
ATOM   6028 N  N   . VAL B 1 223 ? -44.849 15.999  -49.128  1.00 89.58  ?  221 VAL B N   1 
ATOM   6029 C  CA  . VAL B 1 223 ? -44.677 14.568  -48.921  1.00 78.33  ?  221 VAL B CA  1 
ATOM   6030 C  C   . VAL B 1 223 ? -43.546 14.058  -49.801  1.00 87.54  ?  221 VAL B C   1 
ATOM   6031 O  O   . VAL B 1 223 ? -43.448 14.401  -50.984  1.00 89.10  ?  221 VAL B O   1 
ATOM   6032 C  CB  . VAL B 1 223 ? -45.992 13.821  -49.207  1.00 81.98  ?  221 VAL B CB  1 
ATOM   6033 C  CG1 . VAL B 1 223 ? -45.795 12.321  -49.053  1.00 80.27  ?  221 VAL B CG1 1 
ATOM   6034 C  CG2 . VAL B 1 223 ? -47.093 14.319  -48.283  1.00 83.03  ?  221 VAL B CG2 1 
ATOM   6035 N  N   . GLY B 1 224 ? -42.681 13.234  -49.217  1.00 79.41  ?  222 GLY B N   1 
ATOM   6036 C  CA  . GLY B 1 224 ? -41.570 12.635  -49.920  1.00 83.20  ?  222 GLY B CA  1 
ATOM   6037 C  C   . GLY B 1 224 ? -40.228 13.215  -49.541  1.00 82.66  ?  222 GLY B C   1 
ATOM   6038 O  O   . GLY B 1 224 ? -39.201 12.553  -49.744  1.00 79.52  ?  222 GLY B O   1 
ATOM   6039 N  N   . ASP B 1 225 ? -40.204 14.430  -49.002  1.00 86.10  ?  223 ASP B N   1 
ATOM   6040 C  CA  . ASP B 1 225 ? -38.953 15.018  -48.552  1.00 84.86  ?  223 ASP B CA  1 
ATOM   6041 C  C   . ASP B 1 225 ? -38.434 14.241  -47.351  1.00 78.01  ?  223 ASP B C   1 
ATOM   6042 O  O   . ASP B 1 225 ? -39.197 13.869  -46.456  1.00 77.39  ?  223 ASP B O   1 
ATOM   6043 C  CB  . ASP B 1 225 ? -39.153 16.488  -48.181  1.00 89.54  ?  223 ASP B CB  1 
ATOM   6044 C  CG  . ASP B 1 225 ? -39.569 17.340  -49.364  1.00 91.72  ?  223 ASP B CG  1 
ATOM   6045 O  OD1 . ASP B 1 225 ? -38.902 17.264  -50.417  1.00 96.39  ?  223 ASP B OD1 1 
ATOM   6046 O  OD2 . ASP B 1 225 ? -40.560 18.091  -49.239  1.00 93.83  -1 223 ASP B OD2 1 
ATOM   6047 N  N   . TYR B 1 226 ? -37.130 13.986  -47.336  1.00 76.17  ?  224 TYR B N   1 
ATOM   6048 C  CA  . TYR B 1 226 ? -36.534 13.151  -46.307  1.00 74.65  ?  224 TYR B CA  1 
ATOM   6049 C  C   . TYR B 1 226 ? -35.385 13.894  -45.640  1.00 75.67  ?  224 TYR B C   1 
ATOM   6050 O  O   . TYR B 1 226 ? -34.813 14.836  -46.197  1.00 75.12  ?  224 TYR B O   1 
ATOM   6051 C  CB  . TYR B 1 226 ? -36.113 11.778  -46.872  1.00 69.44  ?  224 TYR B CB  1 
ATOM   6052 C  CG  . TYR B 1 226 ? -34.976 11.749  -47.873  1.00 64.85  ?  224 TYR B CG  1 
ATOM   6053 C  CD1 . TYR B 1 226 ? -35.225 11.883  -49.234  1.00 68.58  ?  224 TYR B CD1 1 
ATOM   6054 C  CD2 . TYR B 1 226 ? -33.669 11.514  -47.470  1.00 65.97  ?  224 TYR B CD2 1 
ATOM   6055 C  CE1 . TYR B 1 226 ? -34.199 11.833  -50.159  1.00 68.50  ?  224 TYR B CE1 1 
ATOM   6056 C  CE2 . TYR B 1 226 ? -32.635 11.457  -48.390  1.00 67.27  ?  224 TYR B CE2 1 
ATOM   6057 C  CZ  . TYR B 1 226 ? -32.907 11.617  -49.732  1.00 68.18  ?  224 TYR B CZ  1 
ATOM   6058 O  OH  . TYR B 1 226 ? -31.883 11.558  -50.652  1.00 70.17  ?  224 TYR B OH  1 
ATOM   6059 N  N   . PHE B 1 227 ? -35.068 13.462  -44.420  1.00 73.06  ?  225 PHE B N   1 
ATOM   6060 C  CA  . PHE B 1 227 ? -34.085 14.124  -43.575  1.00 74.83  ?  225 PHE B CA  1 
ATOM   6061 C  C   . PHE B 1 227 ? -33.085 13.101  -43.063  1.00 67.50  ?  225 PHE B C   1 
ATOM   6062 O  O   . PHE B 1 227 ? -33.475 12.027  -42.595  1.00 66.56  ?  225 PHE B O   1 
ATOM   6063 C  CB  . PHE B 1 227 ? -34.772 14.819  -42.395  1.00 79.63  ?  225 PHE B CB  1 
ATOM   6064 C  CG  . PHE B 1 227 ? -35.789 15.844  -42.806  1.00 88.96  ?  225 PHE B CG  1 
ATOM   6065 C  CD1 . PHE B 1 227 ? -35.414 17.149  -43.071  1.00 90.89  ?  225 PHE B CD1 1 
ATOM   6066 C  CD2 . PHE B 1 227 ? -37.122 15.495  -42.939  1.00 91.12  ?  225 PHE B CD2 1 
ATOM   6067 C  CE1 . PHE B 1 227 ? -36.352 18.088  -43.453  1.00 95.90  ?  225 PHE B CE1 1 
ATOM   6068 C  CE2 . PHE B 1 227 ? -38.063 16.428  -43.321  1.00 94.84  ?  225 PHE B CE2 1 
ATOM   6069 C  CZ  . PHE B 1 227 ? -37.678 17.727  -43.578  1.00 97.63  ?  225 PHE B CZ  1 
ATOM   6070 N  N   . VAL B 1 228 ? -31.803 13.438  -43.147  1.00 73.09  ?  226 VAL B N   1 
ATOM   6071 C  CA  . VAL B 1 228 ? -30.727 12.564  -42.696  1.00 75.01  ?  226 VAL B CA  1 
ATOM   6072 C  C   . VAL B 1 228 ? -29.687 13.406  -41.972  1.00 79.30  ?  226 VAL B C   1 
ATOM   6073 O  O   . VAL B 1 228 ? -29.364 14.517  -42.405  1.00 76.68  ?  226 VAL B O   1 
ATOM   6074 C  CB  . VAL B 1 228 ? -30.089 11.800  -43.877  1.00 72.62  ?  226 VAL B CB  1 
ATOM   6075 C  CG1 . VAL B 1 228 ? -28.828 11.078  -43.427  1.00 74.95  ?  226 VAL B CG1 1 
ATOM   6076 C  CG2 . VAL B 1 228 ? -31.087 10.823  -44.481  1.00 60.81  ?  226 VAL B CG2 1 
ATOM   6077 N  N   . LEU B 1 229 ? -29.171 12.883  -40.861  1.00 86.69  ?  227 LEU B N   1 
ATOM   6078 C  CA  . LEU B 1 229 ? -28.098 13.565  -40.145  1.00 81.26  ?  227 LEU B CA  1 
ATOM   6079 C  C   . LEU B 1 229 ? -26.864 13.588  -41.037  1.00 81.19  ?  227 LEU B C   1 
ATOM   6080 O  O   . LEU B 1 229 ? -26.297 12.536  -41.352  1.00 82.20  ?  227 LEU B O   1 
ATOM   6081 C  CB  . LEU B 1 229 ? -27.803 12.865  -38.823  1.00 78.99  ?  227 LEU B CB  1 
ATOM   6082 C  CG  . LEU B 1 229 ? -28.922 12.811  -37.782  1.00 83.84  ?  227 LEU B CG  1 
ATOM   6083 C  CD1 . LEU B 1 229 ? -28.452 12.056  -36.549  1.00 83.51  ?  227 LEU B CD1 1 
ATOM   6084 C  CD2 . LEU B 1 229 ? -29.389 14.210  -37.416  1.00 84.06  ?  227 LEU B CD2 1 
ATOM   6085 N  N   . THR B 1 230 ? -26.445 14.781  -41.447  1.00 81.74  ?  228 THR B N   1 
ATOM   6086 C  CA  . THR B 1 230 ? -25.358 14.892  -42.408  1.00 79.69  ?  228 THR B CA  1 
ATOM   6087 C  C   . THR B 1 230 ? -24.034 14.462  -41.788  1.00 79.46  ?  228 THR B C   1 
ATOM   6088 O  O   . THR B 1 230 ? -23.662 14.917  -40.701  1.00 69.80  ?  228 THR B O   1 
ATOM   6089 C  CB  . THR B 1 230 ? -25.251 16.323  -42.933  1.00 81.84  ?  228 THR B CB  1 
ATOM   6090 O  OG1 . THR B 1 230 ? -26.435 16.651  -43.671  1.00 85.72  ?  228 THR B OG1 1 
ATOM   6091 C  CG2 . THR B 1 230 ? -24.040 16.461  -43.846  1.00 85.62  ?  228 THR B CG2 1 
ATOM   6092 N  N   . SER B 1 231 ? -23.328 13.586  -42.490  1.00 77.39  ?  229 SER B N   1 
ATOM   6093 C  CA  . SER B 1 231 ? -22.014 13.107  -42.097  1.00 78.57  ?  229 SER B CA  1 
ATOM   6094 C  C   . SER B 1 231 ? -20.953 13.826  -42.923  1.00 77.35  ?  229 SER B C   1 
ATOM   6095 O  O   . SER B 1 231 ? -21.242 14.413  -43.968  1.00 81.96  ?  229 SER B O   1 
ATOM   6096 C  CB  . SER B 1 231 ? -21.910 11.590  -42.287  1.00 72.61  ?  229 SER B CB  1 
ATOM   6097 O  OG  . SER B 1 231 ? -20.572 11.142  -42.154  1.00 81.52  ?  229 SER B OG  1 
ATOM   6098 N  N   . HIS B 1 232 ? -19.715 13.785  -42.438  1.00 77.84  ?  230 HIS B N   1 
ATOM   6099 C  CA  . HIS B 1 232 ? -18.605 14.379  -43.166  1.00 81.12  ?  230 HIS B CA  1 
ATOM   6100 C  C   . HIS B 1 232 ? -17.393 13.465  -43.086  1.00 78.80  ?  230 HIS B C   1 
ATOM   6101 O  O   . HIS B 1 232 ? -17.233 12.702  -42.130  1.00 79.10  ?  230 HIS B O   1 
ATOM   6102 C  CB  . HIS B 1 232 ? -18.246 15.767  -42.614  1.00 80.16  ?  230 HIS B CB  1 
ATOM   6103 C  CG  . HIS B 1 232 ? -19.415 16.696  -42.508  1.00 88.34  ?  230 HIS B CG  1 
ATOM   6104 N  ND1 . HIS B 1 232 ? -19.882 17.431  -43.576  1.00 92.86  ?  230 HIS B ND1 1 
ATOM   6105 C  CD2 . HIS B 1 232 ? -20.207 17.015  -41.457  1.00 84.66  ?  230 HIS B CD2 1 
ATOM   6106 C  CE1 . HIS B 1 232 ? -20.916 18.159  -43.189  1.00 88.13  ?  230 HIS B CE1 1 
ATOM   6107 N  NE2 . HIS B 1 232 ? -21.132 17.925  -41.907  1.00 96.10  ?  230 HIS B NE2 1 
ATOM   6108 N  N   . THR B 1 233 ? -16.539 13.550  -44.102  1.00 75.38  ?  231 THR B N   1 
ATOM   6109 C  CA  . THR B 1 233 ? -15.308 12.777  -44.092  1.00 67.51  ?  231 THR B CA  1 
ATOM   6110 C  C   . THR B 1 233 ? -14.348 13.360  -43.062  1.00 60.86  ?  231 THR B C   1 
ATOM   6111 O  O   . THR B 1 233 ? -14.309 14.571  -42.831  1.00 64.51  ?  231 THR B O   1 
ATOM   6112 C  CB  . THR B 1 233 ? -14.665 12.770  -45.480  1.00 72.38  ?  231 THR B CB  1 
ATOM   6113 O  OG1 . THR B 1 233 ? -15.532 12.100  -46.405  1.00 82.91  ?  231 THR B OG1 1 
ATOM   6114 C  CG2 . THR B 1 233 ? -13.325 12.051  -45.444  1.00 70.60  ?  231 THR B CG2 1 
ATOM   6115 N  N   . VAL B 1 234 ? -13.576 12.482  -42.429  1.00 60.61  ?  232 VAL B N   1 
ATOM   6116 C  CA  . VAL B 1 234 ? -12.599 12.879  -41.422  1.00 58.74  ?  232 VAL B CA  1 
ATOM   6117 C  C   . VAL B 1 234 ? -11.204 12.800  -42.029  1.00 53.33  ?  232 VAL B C   1 
ATOM   6118 O  O   . VAL B 1 234 ? -10.795 11.749  -42.536  1.00 50.06  ?  232 VAL B O   1 
ATOM   6119 C  CB  . VAL B 1 234 ? -12.710 11.997  -40.169  1.00 54.00  ?  232 VAL B CB  1 
ATOM   6120 C  CG1 . VAL B 1 234 ? -11.645 12.374  -39.156  1.00 51.49  ?  232 VAL B CG1 1 
ATOM   6121 C  CG2 . VAL B 1 234 ? -14.106 12.106  -39.570  1.00 54.69  ?  232 VAL B CG2 1 
ATOM   6122 N  N   . MET B 1 235 ? -10.465 13.915  -41.970  1.00 53.15  ?  233 MET B N   1 
ATOM   6123 C  CA  . MET B 1 235 ? -9.133  13.941  -42.553  1.00 55.54  ?  233 MET B CA  1 
ATOM   6124 C  C   . MET B 1 235 ? -8.089  13.474  -41.542  1.00 52.28  ?  233 MET B C   1 
ATOM   6125 O  O   . MET B 1 235 ? -8.267  13.645  -40.332  1.00 48.62  ?  233 MET B O   1 
ATOM   6126 C  CB  . MET B 1 235 ? -8.790  15.346  -43.035  1.00 52.73  ?  233 MET B CB  1 
ATOM   6127 C  CG  . MET B 1 235 ? -9.602  15.782  -44.242  1.00 55.39  ?  233 MET B CG  1 
ATOM   6128 S  SD  . MET B 1 235 ? -9.383  14.680  -45.653  1.00 71.67  ?  233 MET B SD  1 
ATOM   6129 C  CE  . MET B 1 235 ? -10.977 14.844  -46.455  1.00 78.52  ?  233 MET B CE  1 
ATOM   6130 N  N   . PRO B 1 236 ? -6.990  12.882  -42.007  1.00 53.09  ?  234 PRO B N   1 
ATOM   6131 C  CA  . PRO B 1 236 ? -5.929  12.474  -41.083  1.00 45.53  ?  234 PRO B CA  1 
ATOM   6132 C  C   . PRO B 1 236 ? -5.301  13.678  -40.397  1.00 50.13  ?  234 PRO B C   1 
ATOM   6133 O  O   . PRO B 1 236 ? -5.319  14.800  -40.907  1.00 50.74  ?  234 PRO B O   1 
ATOM   6134 C  CB  . PRO B 1 236 ? -4.924  11.765  -41.999  1.00 54.00  ?  234 PRO B CB  1 
ATOM   6135 C  CG  . PRO B 1 236 ? -5.135  12.444  -43.326  1.00 52.15  ?  234 PRO B CG  1 
ATOM   6136 C  CD  . PRO B 1 236 ? -6.634  12.569  -43.402  1.00 61.20  ?  234 PRO B CD  1 
ATOM   6137 N  N   . LEU B 1 237 ? -4.731  13.427  -39.222  1.00 45.63  ?  235 LEU B N   1 
ATOM   6138 C  CA  . LEU B 1 237 ? -4.100  14.463  -38.419  1.00 45.70  ?  235 LEU B CA  1 
ATOM   6139 C  C   . LEU B 1 237 ? -2.586  14.320  -38.491  1.00 45.82  ?  235 LEU B C   1 
ATOM   6140 O  O   . LEU B 1 237 ? -2.060  13.230  -38.735  1.00 45.86  ?  235 LEU B O   1 
ATOM   6141 C  CB  . LEU B 1 237 ? -4.557  14.386  -36.957  1.00 42.27  ?  235 LEU B CB  1 
ATOM   6142 C  CG  . LEU B 1 237 ? -6.022  14.719  -36.660  1.00 42.77  ?  235 LEU B CG  1 
ATOM   6143 C  CD1 . LEU B 1 237 ? -6.352  14.478  -35.187  1.00 40.77  ?  235 LEU B CD1 1 
ATOM   6144 C  CD2 . LEU B 1 237 ? -6.339  16.152  -37.058  1.00 38.70  ?  235 LEU B CD2 1 
ATOM   6145 N  N   . SER B 1 238 ? -1.887  15.433  -38.272  1.00 40.62  ?  236 SER B N   1 
ATOM   6146 C  CA  . SER B 1 238 ? -0.432  15.437  -38.355  1.00 45.20  ?  236 SER B CA  1 
ATOM   6147 C  C   . SER B 1 238 ? 0.175   16.250  -37.218  1.00 49.99  ?  236 SER B C   1 
ATOM   6148 O  O   . SER B 1 238 ? 1.161   15.829  -36.605  1.00 49.73  ?  236 SER B O   1 
ATOM   6149 C  CB  . SER B 1 238 ? 0.030   15.987  -39.708  1.00 43.88  ?  236 SER B CB  1 
ATOM   6150 O  OG  . SER B 1 238 ? -0.524  17.268  -39.960  1.00 56.93  ?  236 SER B OG  1 
ATOM   6151 N  N   . ALA B 1 239 ? -0.409  17.416  -36.930  1.00 45.75  ?  237 ALA B N   1 
ATOM   6152 C  CA  . ALA B 1 239 ? 0.152   18.327  -35.947  1.00 47.82  ?  237 ALA B CA  1 
ATOM   6153 C  C   . ALA B 1 239 ? -0.228  17.909  -34.526  1.00 43.84  ?  237 ALA B C   1 
ATOM   6154 O  O   . ALA B 1 239 ? -1.299  17.342  -34.300  1.00 41.69  ?  237 ALA B O   1 
ATOM   6155 C  CB  . ALA B 1 239 ? -0.328  19.750  -36.209  1.00 49.59  ?  237 ALA B CB  1 
ATOM   6156 N  N   . PRO B 1 240 ? 0.640   18.180  -33.554  1.00 44.78  ?  238 PRO B N   1 
ATOM   6157 C  CA  . PRO B 1 240 ? 0.304   17.896  -32.155  1.00 41.23  ?  238 PRO B CA  1 
ATOM   6158 C  C   . PRO B 1 240 ? -0.843  18.765  -31.656  1.00 37.97  ?  238 PRO B C   1 
ATOM   6159 O  O   . PRO B 1 240 ? -1.143  19.829  -32.201  1.00 38.95  ?  238 PRO B O   1 
ATOM   6160 C  CB  . PRO B 1 240 ? 1.608   18.214  -31.416  1.00 39.42  ?  238 PRO B CB  1 
ATOM   6161 C  CG  . PRO B 1 240 ? 2.260   19.251  -32.288  1.00 51.64  ?  238 PRO B CG  1 
ATOM   6162 C  CD  . PRO B 1 240 ? 1.991   18.753  -33.681  1.00 51.91  ?  238 PRO B CD  1 
ATOM   6163 N  N   . THR B 1 241 ? -1.502  18.283  -30.599  1.00 33.66  ?  239 THR B N   1 
ATOM   6164 C  CA  . THR B 1 241 ? -2.588  19.058  -30.005  1.00 37.76  ?  239 THR B CA  1 
ATOM   6165 C  C   . THR B 1 241 ? -2.063  20.353  -29.403  1.00 40.64  ?  239 THR B C   1 
ATOM   6166 O  O   . THR B 1 241 ? -2.799  21.344  -29.318  1.00 38.98  ?  239 THR B O   1 
ATOM   6167 C  CB  . THR B 1 241 ? -3.323  18.234  -28.948  1.00 34.67  ?  239 THR B CB  1 
ATOM   6168 O  OG1 . THR B 1 241 ? -2.411  17.850  -27.914  1.00 38.39  ?  239 THR B OG1 1 
ATOM   6169 C  CG2 . THR B 1 241 ? -3.914  16.988  -29.580  1.00 36.91  ?  239 THR B CG2 1 
ATOM   6170 N  N   . LEU B 1 242 ? -0.811  20.346  -28.950  1.00 36.07  ?  240 LEU B N   1 
ATOM   6171 C  CA  . LEU B 1 242 ? -0.144  21.511  -28.393  1.00 36.85  ?  240 LEU B CA  1 
ATOM   6172 C  C   . LEU B 1 242 ? 1.267   21.553  -28.957  1.00 38.70  ?  240 LEU B C   1 
ATOM   6173 O  O   . LEU B 1 242 ? 1.925   20.516  -29.071  1.00 38.36  ?  240 LEU B O   1 
ATOM   6174 C  CB  . LEU B 1 242 ? -0.100  21.464  -26.860  1.00 35.16  ?  240 LEU B CB  1 
ATOM   6175 C  CG  . LEU B 1 242 ? -1.394  21.861  -26.149  1.00 38.77  ?  240 LEU B CG  1 
ATOM   6176 C  CD1 . LEU B 1 242 ? -1.317  21.551  -24.661  1.00 36.65  ?  240 LEU B CD1 1 
ATOM   6177 C  CD2 . LEU B 1 242 ? -1.679  23.335  -26.377  1.00 40.44  ?  240 LEU B CD2 1 
ATOM   6178 N  N   . VAL B 1 243 ? 1.725   22.745  -29.320  1.00 45.30  ?  241 VAL B N   1 
ATOM   6179 C  CA  . VAL B 1 243 ? 3.084   22.914  -29.827  1.00 45.39  ?  241 VAL B CA  1 
ATOM   6180 C  C   . VAL B 1 243 ? 4.036   22.788  -28.643  1.00 38.57  ?  241 VAL B C   1 
ATOM   6181 O  O   . VAL B 1 243 ? 3.591   22.862  -27.488  1.00 40.51  ?  241 VAL B O   1 
ATOM   6182 C  CB  . VAL B 1 243 ? 3.250   24.252  -30.564  1.00 52.94  ?  241 VAL B CB  1 
ATOM   6183 C  CG1 . VAL B 1 243 ? 2.349   24.290  -31.790  1.00 60.41  ?  241 VAL B CG1 1 
ATOM   6184 C  CG2 . VAL B 1 243 ? 2.947   25.416  -29.637  1.00 43.57  ?  241 VAL B CG2 1 
ATOM   6185 N  N   . PRO B 1 244 ? 5.330   22.568  -28.863  1.00 40.45  ?  242 PRO B N   1 
ATOM   6186 C  CA  . PRO B 1 244 ? 6.266   22.558  -27.732  1.00 39.13  ?  242 PRO B CA  1 
ATOM   6187 C  C   . PRO B 1 244 ? 6.335   23.933  -27.082  1.00 45.27  ?  242 PRO B C   1 
ATOM   6188 O  O   . PRO B 1 244 ? 6.534   24.949  -27.752  1.00 44.40  ?  242 PRO B O   1 
ATOM   6189 C  CB  . PRO B 1 244 ? 7.602   22.156  -28.373  1.00 44.48  ?  242 PRO B CB  1 
ATOM   6190 C  CG  . PRO B 1 244 ? 7.256   21.667  -29.762  1.00 41.95  ?  242 PRO B CG  1 
ATOM   6191 C  CD  . PRO B 1 244 ? 6.022   22.407  -30.151  1.00 43.76  ?  242 PRO B CD  1 
ATOM   6192 N  N   . GLN B 1 245 ? 6.142   23.959  -25.766  1.00 40.67  ?  243 GLN B N   1 
ATOM   6193 C  CA  . GLN B 1 245 ? 6.149   25.214  -25.027  1.00 39.85  ?  243 GLN B CA  1 
ATOM   6194 C  C   . GLN B 1 245 ? 7.536   25.844  -25.013  1.00 42.61  ?  243 GLN B C   1 
ATOM   6195 O  O   . GLN B 1 245 ? 8.556   25.153  -24.956  1.00 43.66  ?  243 GLN B O   1 
ATOM   6196 C  CB  . GLN B 1 245 ? 5.666   24.991  -23.594  1.00 33.71  ?  243 GLN B CB  1 
ATOM   6197 C  CG  . GLN B 1 245 ? 5.577   26.271  -22.773  1.00 38.71  ?  243 GLN B CG  1 
ATOM   6198 C  CD  . GLN B 1 245 ? 4.588   27.268  -23.345  1.00 35.32  ?  243 GLN B CD  1 
ATOM   6199 O  OE1 . GLN B 1 245 ? 4.817   27.847  -24.410  1.00 37.73  ?  243 GLN B OE1 1 
ATOM   6200 N  NE2 . GLN B 1 245 ? 3.482   27.476  -22.641  1.00 35.55  ?  243 GLN B NE2 1 
ATOM   6201 N  N   . GLU B 1 246 ? 7.563   27.172  -25.085  1.00 38.09  ?  244 GLU B N   1 
ATOM   6202 C  CA  . GLU B 1 246 ? 8.790   27.945  -24.968  1.00 42.40  ?  244 GLU B CA  1 
ATOM   6203 C  C   . GLU B 1 246 ? 8.514   29.153  -24.089  1.00 38.44  ?  244 GLU B C   1 
ATOM   6204 O  O   . GLU B 1 246 ? 7.546   29.882  -24.326  1.00 42.14  ?  244 GLU B O   1 
ATOM   6205 C  CB  . GLU B 1 246 ? 9.298   28.394  -26.343  1.00 43.59  ?  244 GLU B CB  1 
ATOM   6206 C  CG  . GLU B 1 246 ? 9.593   27.250  -27.297  1.00 49.44  ?  244 GLU B CG  1 
ATOM   6207 C  CD  . GLU B 1 246 ? 10.023  27.733  -28.669  1.00 60.60  ?  244 GLU B CD  1 
ATOM   6208 O  OE1 . GLU B 1 246 ? 10.077  28.963  -28.882  1.00 59.58  ?  244 GLU B OE1 1 
ATOM   6209 O  OE2 . GLU B 1 246 ? 10.306  26.882  -29.537  1.00 65.69  -1 244 GLU B OE2 1 
ATOM   6210 N  N   . HIS B 1 247 ? 9.329   29.345  -23.058  1.00 43.99  ?  245 HIS B N   1 
ATOM   6211 C  CA  . HIS B 1 247 ? 9.242   30.540  -22.234  1.00 41.31  ?  245 HIS B CA  1 
ATOM   6212 C  C   . HIS B 1 247 ? 10.375  31.489  -22.605  1.00 44.75  ?  245 HIS B C   1 
ATOM   6213 O  O   . HIS B 1 247 ? 11.503  31.056  -22.856  1.00 43.83  ?  245 HIS B O   1 
ATOM   6214 C  CB  . HIS B 1 247 ? 9.282   30.183  -20.748  1.00 43.44  ?  245 HIS B CB  1 
ATOM   6215 C  CG  . HIS B 1 247 ? 8.081   29.413  -20.292  1.00 52.11  ?  245 HIS B CG  1 
ATOM   6216 N  ND1 . HIS B 1 247 ? 6.973   30.018  -19.739  1.00 45.36  ?  245 HIS B ND1 1 
ATOM   6217 C  CD2 . HIS B 1 247 ? 7.811   28.086  -20.319  1.00 47.75  ?  245 HIS B CD2 1 
ATOM   6218 C  CE1 . HIS B 1 247 ? 6.074   29.097  -19.442  1.00 49.65  ?  245 HIS B CE1 1 
ATOM   6219 N  NE2 . HIS B 1 247 ? 6.558   27.916  -19.782  1.00 53.84  ?  245 HIS B NE2 1 
ATOM   6220 N  N   . TYR B 1 248 ? 10.071  32.782  -22.635  1.00 44.30  ?  246 TYR B N   1 
ATOM   6221 C  CA  . TYR B 1 248 ? 11.023  33.800  -23.049  1.00 45.92  ?  246 TYR B CA  1 
ATOM   6222 C  C   . TYR B 1 248 ? 11.279  34.793  -21.922  1.00 45.90  ?  246 TYR B C   1 
ATOM   6223 O  O   . TYR B 1 248 ? 10.442  34.994  -21.038  1.00 48.05  ?  246 TYR B O   1 
ATOM   6224 C  CB  . TYR B 1 248 ? 10.509  34.556  -24.284  1.00 44.91  ?  246 TYR B CB  1 
ATOM   6225 C  CG  . TYR B 1 248 ? 10.036  33.665  -25.413  1.00 44.13  ?  246 TYR B CG  1 
ATOM   6226 C  CD1 . TYR B 1 248 ? 10.829  32.629  -25.888  1.00 44.14  ?  246 TYR B CD1 1 
ATOM   6227 C  CD2 . TYR B 1 248 ? 8.780   33.846  -25.985  1.00 46.48  ?  246 TYR B CD2 1 
ATOM   6228 C  CE1 . TYR B 1 248 ? 10.394  31.808  -26.918  1.00 47.42  ?  246 TYR B CE1 1 
ATOM   6229 C  CE2 . TYR B 1 248 ? 8.336   33.030  -27.013  1.00 46.08  ?  246 TYR B CE2 1 
ATOM   6230 C  CZ  . TYR B 1 248 ? 9.147   32.013  -27.474  1.00 49.99  ?  246 TYR B CZ  1 
ATOM   6231 O  OH  . TYR B 1 248 ? 8.711   31.201  -28.497  1.00 49.70  ?  246 TYR B OH  1 
ATOM   6232 N  N   . VAL B 1 249 ? 12.455  35.430  -21.975  1.00 52.37  ?  247 VAL B N   1 
ATOM   6233 C  CA  . VAL B 1 249 ? 12.836  36.413  -20.963  1.00 48.61  ?  247 VAL B CA  1 
ATOM   6234 C  C   . VAL B 1 249 ? 12.348  37.805  -21.333  1.00 56.81  ?  247 VAL B C   1 
ATOM   6235 O  O   . VAL B 1 249 ? 12.364  38.707  -20.481  1.00 63.02  ?  247 VAL B O   1 
ATOM   6236 C  CB  . VAL B 1 249 ? 14.361  36.458  -20.727  1.00 55.24  ?  247 VAL B CB  1 
ATOM   6237 C  CG1 . VAL B 1 249 ? 14.832  35.193  -20.025  1.00 52.70  ?  247 VAL B CG1 1 
ATOM   6238 C  CG2 . VAL B 1 249 ? 15.112  36.670  -22.035  1.00 55.14  ?  247 VAL B CG2 1 
ATOM   6239 N  N   . ARG B 1 250 ? 11.919  38.006  -22.578  1.00 52.23  ?  248 ARG B N   1 
ATOM   6240 C  CA  . ARG B 1 250 ? 11.429  39.285  -23.067  1.00 52.80  ?  248 ARG B CA  1 
ATOM   6241 C  C   . ARG B 1 250 ? 10.246  39.022  -23.985  1.00 43.18  ?  248 ARG B C   1 
ATOM   6242 O  O   . ARG B 1 250 ? 10.071  37.912  -24.494  1.00 44.27  ?  248 ARG B O   1 
ATOM   6243 C  CB  . ARG B 1 250 ? 12.503  40.037  -23.865  1.00 53.50  ?  248 ARG B CB  1 
ATOM   6244 C  CG  . ARG B 1 250 ? 13.513  40.818  -23.060  1.00 67.32  ?  248 ARG B CG  1 
ATOM   6245 C  CD  . ARG B 1 250 ? 14.646  41.261  -23.979  1.00 73.78  ?  248 ARG B CD  1 
ATOM   6246 N  NE  . ARG B 1 250 ? 15.119  40.165  -24.817  1.00 78.47  ?  248 ARG B NE  1 
ATOM   6247 C  CZ  . ARG B 1 250 ? 16.046  39.286  -24.460  1.00 70.69  ?  248 ARG B CZ  1 
ATOM   6248 N  NH1 . ARG B 1 250 ? 16.760  39.445  -23.358  1.00 65.82  ?  248 ARG B NH1 1 
ATOM   6249 N  NH2 . ARG B 1 250 ? 16.298  38.249  -25.254  1.00 67.93  ?  248 ARG B NH2 1 
ATOM   6250 N  N   . ILE B 1 251 ? 9.437   40.059  -24.211  1.00 44.24  ?  249 ILE B N   1 
ATOM   6251 C  CA  . ILE B 1 251 ? 8.372   39.941  -25.198  1.00 40.76  ?  249 ILE B CA  1 
ATOM   6252 C  C   . ILE B 1 251 ? 9.022   39.717  -26.553  1.00 43.12  ?  249 ILE B C   1 
ATOM   6253 O  O   . ILE B 1 251 ? 9.875   40.502  -26.985  1.00 43.70  ?  249 ILE B O   1 
ATOM   6254 C  CB  . ILE B 1 251 ? 7.486   41.195  -25.194  1.00 43.89  ?  249 ILE B CB  1 
ATOM   6255 C  CG1 . ILE B 1 251 ? 6.950   41.466  -23.787  1.00 46.10  ?  249 ILE B CG1 1 
ATOM   6256 C  CG2 . ILE B 1 251 ? 6.329   41.027  -26.167  1.00 38.80  ?  249 ILE B CG2 1 
ATOM   6257 C  CD1 . ILE B 1 251 ? 6.050   42.678  -23.703  1.00 45.20  ?  249 ILE B CD1 1 
ATOM   6258 N  N   . THR B 1 252 ? 8.620   38.651  -27.239  1.00 47.35  ?  250 THR B N   1 
ATOM   6259 C  CA  . THR B 1 252 ? 9.262   38.256  -28.486  1.00 47.91  ?  250 THR B CA  1 
ATOM   6260 C  C   . THR B 1 252 ? 8.278   38.309  -29.645  1.00 51.15  ?  250 THR B C   1 
ATOM   6261 O  O   . THR B 1 252 ? 7.181   37.746  -29.562  1.00 52.91  ?  250 THR B O   1 
ATOM   6262 C  CB  . THR B 1 252 ? 9.859   36.852  -28.359  1.00 54.62  ?  250 THR B CB  1 
ATOM   6263 O  OG1 . THR B 1 252 ? 10.625  36.773  -27.150  1.00 53.68  ?  250 THR B OG1 1 
ATOM   6264 C  CG2 . THR B 1 252 ? 10.768  36.557  -29.539  1.00 57.11  ?  250 THR B CG2 1 
ATOM   6265 N  N   . GLY B 1 253 ? 8.678   38.987  -30.720  1.00 44.96  ?  251 GLY B N   1 
ATOM   6266 C  CA  . GLY B 1 253 ? 7.899   39.049  -31.937  1.00 52.21  ?  251 GLY B CA  1 
ATOM   6267 C  C   . GLY B 1 253 ? 6.764   40.045  -31.913  1.00 55.27  ?  251 GLY B C   1 
ATOM   6268 O  O   . GLY B 1 253 ? 6.036   40.155  -32.908  1.00 67.04  ?  251 GLY B O   1 
ATOM   6269 N  N   . LEU B 1 254 ? 6.600   40.783  -30.820  1.00 50.33  ?  252 LEU B N   1 
ATOM   6270 C  CA  . LEU B 1 254 ? 5.475   41.683  -30.635  1.00 48.50  ?  252 LEU B CA  1 
ATOM   6271 C  C   . LEU B 1 254 ? 5.994   43.023  -30.143  1.00 54.50  ?  252 LEU B C   1 
ATOM   6272 O  O   . LEU B 1 254 ? 6.972   43.092  -29.394  1.00 54.30  ?  252 LEU B O   1 
ATOM   6273 C  CB  . LEU B 1 254 ? 4.461   41.113  -29.628  1.00 40.68  ?  252 LEU B CB  1 
ATOM   6274 C  CG  . LEU B 1 254 ? 3.755   39.817  -30.028  1.00 43.23  ?  252 LEU B CG  1 
ATOM   6275 C  CD1 . LEU B 1 254 ? 2.878   39.305  -28.890  1.00 34.93  ?  252 LEU B CD1 1 
ATOM   6276 C  CD2 . LEU B 1 254 ? 2.939   40.011  -31.299  1.00 38.66  ?  252 LEU B CD2 1 
ATOM   6277 N  N   . TYR B 1 255 ? 5.330   44.090  -30.570  1.00 50.97  ?  253 TYR B N   1 
ATOM   6278 C  CA  . TYR B 1 255 ? 5.742   45.446  -30.216  1.00 40.72  ?  253 TYR B CA  1 
ATOM   6279 C  C   . TYR B 1 255 ? 4.632   46.111  -29.421  1.00 44.31  ?  253 TYR B C   1 
ATOM   6280 O  O   . TYR B 1 255 ? 3.629   46.568  -30.000  1.00 40.61  ?  253 TYR B O   1 
ATOM   6281 C  CB  . TYR B 1 255 ? 6.094   46.224  -31.480  1.00 53.16  ?  253 TYR B CB  1 
ATOM   6282 C  CG  . TYR B 1 255 ? 7.181   45.501  -32.241  1.00 59.53  ?  253 TYR B CG  1 
ATOM   6283 C  CD1 . TYR B 1 255 ? 8.515   45.636  -31.877  1.00 60.08  ?  253 TYR B CD1 1 
ATOM   6284 C  CD2 . TYR B 1 255 ? 6.870   44.623  -33.271  1.00 63.44  ?  253 TYR B CD2 1 
ATOM   6285 C  CE1 . TYR B 1 255 ? 9.512   44.955  -32.549  1.00 65.63  ?  253 TYR B CE1 1 
ATOM   6286 C  CE2 . TYR B 1 255 ? 7.861   43.936  -33.950  1.00 65.23  ?  253 TYR B CE2 1 
ATOM   6287 C  CZ  . TYR B 1 255 ? 9.180   44.105  -33.583  1.00 69.04  ?  253 TYR B CZ  1 
ATOM   6288 O  OH  . TYR B 1 255 ? 10.170  43.425  -34.255  1.00 85.82  ?  253 TYR B OH  1 
ATOM   6289 N  N   . PRO B 1 256 ? 4.771   46.199  -28.101  1.00 43.12  ?  254 PRO B N   1 
ATOM   6290 C  CA  . PRO B 1 256 ? 3.705   46.771  -27.280  1.00 42.84  ?  254 PRO B CA  1 
ATOM   6291 C  C   . PRO B 1 256 ? 3.507   48.250  -27.544  1.00 44.12  ?  254 PRO B C   1 
ATOM   6292 O  O   . PRO B 1 256 ? 4.449   48.997  -27.818  1.00 48.20  ?  254 PRO B O   1 
ATOM   6293 C  CB  . PRO B 1 256 ? 4.204   46.525  -25.851  1.00 45.06  ?  254 PRO B CB  1 
ATOM   6294 C  CG  . PRO B 1 256 ? 5.687   46.579  -26.004  1.00 46.61  ?  254 PRO B CG  1 
ATOM   6295 C  CD  . PRO B 1 256 ? 5.922   45.800  -27.274  1.00 45.40  ?  254 PRO B CD  1 
ATOM   6296 N  N   . THR B 1 257 ? 2.250   48.664  -27.455  1.00 42.78  ?  255 THR B N   1 
ATOM   6297 C  CA  . THR B 1 257 ? 1.900   50.055  -27.649  1.00 43.30  ?  255 THR B CA  1 
ATOM   6298 C  C   . THR B 1 257 ? 2.346   50.873  -26.446  1.00 44.05  ?  255 THR B C   1 
ATOM   6299 O  O   . THR B 1 257 ? 2.684   50.344  -25.382  1.00 45.75  ?  255 THR B O   1 
ATOM   6300 C  CB  . THR B 1 257 ? 0.394   50.216  -27.844  1.00 46.32  ?  255 THR B CB  1 
ATOM   6301 O  OG1 . THR B 1 257 ? 0.088   51.596  -28.074  1.00 47.87  ?  255 THR B OG1 1 
ATOM   6302 C  CG2 . THR B 1 257 ? -0.350  49.746  -26.600  1.00 41.65  ?  255 THR B CG2 1 
ATOM   6303 N  N   . LEU B 1 258 ? 2.337   52.186  -26.622  1.00 51.14  ?  256 LEU B N   1 
ATOM   6304 C  CA  . LEU B 1 258 ? 2.734   53.083  -25.552  1.00 63.21  ?  256 LEU B CA  1 
ATOM   6305 C  C   . LEU B 1 258 ? 1.518   53.682  -24.869  1.00 58.91  ?  256 LEU B C   1 
ATOM   6306 O  O   . LEU B 1 258 ? 1.524   53.881  -23.650  1.00 55.95  ?  256 LEU B O   1 
ATOM   6307 C  CB  . LEU B 1 258 ? 3.621   54.198  -26.118  1.00 60.40  ?  256 LEU B CB  1 
ATOM   6308 C  CG  . LEU B 1 258 ? 5.012   53.763  -26.591  1.00 68.20  ?  256 LEU B CG  1 
ATOM   6309 C  CD1 . LEU B 1 258 ? 5.639   54.828  -27.479  1.00 62.01  ?  256 LEU B CD1 1 
ATOM   6310 C  CD2 . LEU B 1 258 ? 5.922   53.441  -25.415  1.00 57.83  ?  256 LEU B CD2 1 
ATOM   6311 N  N   . ASN B 1 259 ? 0.468   53.945  -25.641  1.00 57.21  ?  257 ASN B N   1 
ATOM   6312 C  CA  . ASN B 1 259 ? -0.775  54.521  -25.154  1.00 53.59  ?  257 ASN B CA  1 
ATOM   6313 C  C   . ASN B 1 259 ? -1.867  53.458  -25.231  1.00 54.05  ?  257 ASN B C   1 
ATOM   6314 O  O   . ASN B 1 259 ? -2.071  52.854  -26.290  1.00 57.44  ?  257 ASN B O   1 
ATOM   6315 C  CB  . ASN B 1 259 ? -1.145  55.756  -25.974  1.00 46.72  ?  257 ASN B CB  1 
ATOM   6316 C  CG  . ASN B 1 259 ? -2.477  56.339  -25.577  1.00 64.12  ?  257 ASN B CG  1 
ATOM   6317 O  OD1 . ASN B 1 259 ? -2.634  56.856  -24.471  1.00 70.38  ?  257 ASN B OD1 1 
ATOM   6318 N  ND2 . ASN B 1 259 ? -3.447  56.273  -26.483  1.00 74.49  ?  257 ASN B ND2 1 
ATOM   6319 N  N   . ILE B 1 260 ? -2.562  53.225  -24.119  1.00 46.49  ?  258 ILE B N   1 
ATOM   6320 C  CA  . ILE B 1 260 ? -3.641  52.244  -24.074  1.00 46.21  ?  258 ILE B CA  1 
ATOM   6321 C  C   . ILE B 1 260 ? -4.831  52.862  -23.347  1.00 43.57  ?  258 ILE B C   1 
ATOM   6322 O  O   . ILE B 1 260 ? -4.672  53.734  -22.488  1.00 47.40  ?  258 ILE B O   1 
ATOM   6323 C  CB  . ILE B 1 260 ? -3.182  50.926  -23.401  1.00 46.99  ?  258 ILE B CB  1 
ATOM   6324 C  CG1 . ILE B 1 260 ? -4.274  49.852  -23.471  1.00 55.39  ?  258 ILE B CG1 1 
ATOM   6325 C  CG2 . ILE B 1 260 ? -2.742  51.170  -21.965  1.00 48.17  ?  258 ILE B CG2 1 
ATOM   6326 C  CD1 . ILE B 1 260 ? -4.648  49.438  -24.880  1.00 44.17  ?  258 ILE B CD1 1 
ATOM   6327 N  N   . SER B 1 261 ? -6.034  52.410  -23.704  1.00 44.10  ?  259 SER B N   1 
ATOM   6328 C  CA  . SER B 1 261 ? -7.247  52.864  -23.032  1.00 46.67  ?  259 SER B CA  1 
ATOM   6329 C  C   . SER B 1 261 ? -7.393  52.230  -21.652  1.00 46.21  ?  259 SER B C   1 
ATOM   6330 O  O   . SER B 1 261 ? -6.993  51.085  -21.425  1.00 43.82  ?  259 SER B O   1 
ATOM   6331 C  CB  . SER B 1 261 ? -8.475  52.539  -23.883  1.00 47.88  ?  259 SER B CB  1 
ATOM   6332 O  OG  . SER B 1 261 ? -9.669  52.633  -23.123  1.00 53.12  ?  259 SER B OG  1 
ATOM   6333 N  N   . ASP B 1 262 ? -8.005  52.979  -20.727  1.00 48.41  ?  260 ASP B N   1 
ATOM   6334 C  CA  . ASP B 1 262 ? -8.252  52.444  -19.391  1.00 51.31  ?  260 ASP B CA  1 
ATOM   6335 C  C   . ASP B 1 262 ? -9.261  51.304  -19.404  1.00 53.63  ?  260 ASP B C   1 
ATOM   6336 O  O   . ASP B 1 262 ? -9.480  50.681  -18.359  1.00 49.48  ?  260 ASP B O   1 
ATOM   6337 C  CB  . ASP B 1 262 ? -8.710  53.544  -18.423  1.00 54.04  ?  260 ASP B CB  1 
ATOM   6338 C  CG  . ASP B 1 262 ? -10.004 54.210  -18.846  1.00 61.31  ?  260 ASP B CG  1 
ATOM   6339 O  OD1 . ASP B 1 262 ? -10.529 53.881  -19.929  1.00 70.89  ?  260 ASP B OD1 1 
ATOM   6340 O  OD2 . ASP B 1 262 ? -10.502 55.064  -18.081  1.00 71.29  -1 260 ASP B OD2 1 
ATOM   6341 N  N   . GLU B 1 263 ? -9.894  51.038  -20.549  1.00 55.35  ?  261 GLU B N   1 
ATOM   6342 C  CA  . GLU B 1 263 ? -10.802 49.907  -20.686  1.00 56.28  ?  261 GLU B CA  1 
ATOM   6343 C  C   . GLU B 1 263 ? -10.064 48.583  -20.741  1.00 48.26  ?  261 GLU B C   1 
ATOM   6344 O  O   . GLU B 1 263 ? -10.699 47.530  -20.619  1.00 50.58  ?  261 GLU B O   1 
ATOM   6345 C  CB  . GLU B 1 263 ? -11.632 50.038  -21.958  1.00 52.02  ?  261 GLU B CB  1 
ATOM   6346 C  CG  . GLU B 1 263 ? -12.565 51.214  -22.006  1.00 69.98  ?  261 GLU B CG  1 
ATOM   6347 C  CD  . GLU B 1 263 ? -13.530 51.097  -23.160  1.00 77.60  ?  261 GLU B CD  1 
ATOM   6348 O  OE1 . GLU B 1 263 ? -14.321 50.129  -23.172  1.00 78.01  ?  261 GLU B OE1 1 
ATOM   6349 O  OE2 . GLU B 1 263 ? -13.489 51.962  -24.060  1.00 77.39  -1 261 GLU B OE2 1 
ATOM   6350 N  N   . PHE B 1 264 ? -8.749  48.613  -20.931  1.00 46.18  ?  262 PHE B N   1 
ATOM   6351 C  CA  . PHE B 1 264 ? -7.962  47.405  -21.083  1.00 46.82  ?  262 PHE B CA  1 
ATOM   6352 C  C   . PHE B 1 264 ? -6.747  47.409  -20.168  1.00 44.73  ?  262 PHE B C   1 
ATOM   6353 O  O   . PHE B 1 264 ? -5.952  46.464  -20.212  1.00 43.31  ?  262 PHE B O   1 
ATOM   6354 C  CB  . PHE B 1 264 ? -7.514  47.253  -22.545  1.00 47.16  ?  262 PHE B CB  1 
ATOM   6355 C  CG  . PHE B 1 264 ? -8.657  47.149  -23.519  1.00 47.57  ?  262 PHE B CG  1 
ATOM   6356 C  CD1 . PHE B 1 264 ? -9.326  45.952  -23.707  1.00 46.34  ?  262 PHE B CD1 1 
ATOM   6357 C  CD2 . PHE B 1 264 ? -9.068  48.259  -24.242  1.00 50.71  ?  262 PHE B CD2 1 
ATOM   6358 C  CE1 . PHE B 1 264 ? -10.380 45.862  -24.599  1.00 43.87  ?  262 PHE B CE1 1 
ATOM   6359 C  CE2 . PHE B 1 264 ? -10.119 48.175  -25.137  1.00 49.63  ?  262 PHE B CE2 1 
ATOM   6360 C  CZ  . PHE B 1 264 ? -10.775 46.975  -25.315  1.00 51.91  ?  262 PHE B CZ  1 
ATOM   6361 N  N   . SER B 1 265 ? -6.603  48.432  -19.321  1.00 45.67  ?  263 SER B N   1 
ATOM   6362 C  CA  . SER B 1 265 ? -5.476  48.507  -18.399  1.00 46.77  ?  263 SER B CA  1 
ATOM   6363 C  C   . SER B 1 265 ? -5.422  47.300  -17.470  1.00 44.72  ?  263 SER B C   1 
ATOM   6364 O  O   . SER B 1 265 ? -4.338  46.915  -17.018  1.00 40.46  ?  263 SER B O   1 
ATOM   6365 C  CB  . SER B 1 265 ? -5.541  49.810  -17.601  1.00 42.67  ?  263 SER B CB  1 
ATOM   6366 O  OG  . SER B 1 265 ? -6.697  49.866  -16.787  1.00 53.36  ?  263 SER B OG  1 
ATOM   6367 N  N   . SER B 1 266 ? -6.576  46.709  -17.149  1.00 39.91  ?  264 SER B N   1 
ATOM   6368 C  CA  . SER B 1 266 ? -6.590  45.571  -16.237  1.00 47.17  ?  264 SER B CA  1 
ATOM   6369 C  C   . SER B 1 266 ? -5.857  44.359  -16.806  1.00 43.40  ?  264 SER B C   1 
ATOM   6370 O  O   . SER B 1 266 ? -5.407  43.506  -16.034  1.00 42.59  ?  264 SER B O   1 
ATOM   6371 C  CB  . SER B 1 266 ? -8.032  45.192  -15.887  1.00 42.62  ?  264 SER B CB  1 
ATOM   6372 O  OG  . SER B 1 266 ? -8.786  44.908  -17.055  1.00 47.66  ?  264 SER B OG  1 
ATOM   6373 N  N   . ASN B 1 267 ? -5.735  44.254  -18.129  1.00 36.81  ?  265 ASN B N   1 
ATOM   6374 C  CA  . ASN B 1 267 ? -5.153  43.082  -18.774  1.00 41.31  ?  265 ASN B CA  1 
ATOM   6375 C  C   . ASN B 1 267 ? -3.722  43.303  -19.250  1.00 41.41  ?  265 ASN B C   1 
ATOM   6376 O  O   . ASN B 1 267 ? -3.180  42.442  -19.950  1.00 42.31  ?  265 ASN B O   1 
ATOM   6377 C  CB  . ASN B 1 267 ? -6.007  42.640  -19.966  1.00 40.77  ?  265 ASN B CB  1 
ATOM   6378 C  CG  . ASN B 1 267 ? -7.404  42.223  -19.566  1.00 40.54  ?  265 ASN B CG  1 
ATOM   6379 O  OD1 . ASN B 1 267 ? -7.594  41.527  -18.571  1.00 39.61  ?  265 ASN B OD1 1 
ATOM   6380 N  ND2 . ASN B 1 267 ? -8.390  42.626  -20.358  1.00 39.21  ?  265 ASN B ND2 1 
ATOM   6381 N  N   . VAL B 1 268 ? -3.101  44.431  -18.901  1.00 35.84  ?  266 VAL B N   1 
ATOM   6382 C  CA  . VAL B 1 268 ? -1.797  44.759  -19.472  1.00 44.90  ?  266 VAL B CA  1 
ATOM   6383 C  C   . VAL B 1 268 ? -0.728  43.768  -19.022  1.00 43.12  ?  266 VAL B C   1 
ATOM   6384 O  O   . VAL B 1 268 ? 0.117   43.348  -19.822  1.00 41.90  ?  266 VAL B O   1 
ATOM   6385 C  CB  . VAL B 1 268 ? -1.413  46.210  -19.135  1.00 42.47  ?  266 VAL B CB  1 
ATOM   6386 C  CG1 . VAL B 1 268 ? 0.053   46.463  -19.466  1.00 38.20  ?  266 VAL B CG1 1 
ATOM   6387 C  CG2 . VAL B 1 268 ? -2.295  47.171  -19.915  1.00 45.72  ?  266 VAL B CG2 1 
ATOM   6388 N  N   . ALA B 1 269 ? -0.727  43.384  -17.743  1.00 42.35  ?  267 ALA B N   1 
ATOM   6389 C  CA  . ALA B 1 269 ? 0.234   42.379  -17.295  1.00 47.52  ?  267 ALA B CA  1 
ATOM   6390 C  C   . ALA B 1 269 ? 0.026   41.058  -18.030  1.00 43.67  ?  267 ALA B C   1 
ATOM   6391 O  O   . ALA B 1 269 ? 0.985   40.442  -18.511  1.00 41.17  ?  267 ALA B O   1 
ATOM   6392 C  CB  . ALA B 1 269 ? 0.129   42.182  -15.782  1.00 43.20  ?  267 ALA B CB  1 
ATOM   6393 N  N   . ASN B 1 270 ? -1.228  40.609  -18.132  1.00 39.65  ?  268 ASN B N   1 
ATOM   6394 C  CA  . ASN B 1 270 ? -1.511  39.361  -18.836  1.00 41.12  ?  268 ASN B CA  1 
ATOM   6395 C  C   . ASN B 1 270 ? -1.152  39.461  -20.315  1.00 40.97  ?  268 ASN B C   1 
ATOM   6396 O  O   . ASN B 1 270 ? -0.780  38.456  -20.931  1.00 39.67  ?  268 ASN B O   1 
ATOM   6397 C  CB  . ASN B 1 270 ? -2.974  38.964  -18.646  1.00 35.85  ?  268 ASN B CB  1 
ATOM   6398 C  CG  . ASN B 1 270 ? -3.240  38.366  -17.272  1.00 35.76  ?  268 ASN B CG  1 
ATOM   6399 O  OD1 . ASN B 1 270 ? -2.317  37.947  -16.574  1.00 47.33  ?  268 ASN B OD1 1 
ATOM   6400 N  ND2 . ASN B 1 270 ? -4.503  38.334  -16.875  1.00 39.60  ?  268 ASN B ND2 1 
ATOM   6401 N  N   . TYR B 1 271 ? -1.271  40.653  -20.907  1.00 38.31  ?  269 TYR B N   1 
ATOM   6402 C  CA  . TYR B 1 271 ? -0.938  40.797  -22.320  1.00 36.48  ?  269 TYR B CA  1 
ATOM   6403 C  C   . TYR B 1 271 ? 0.565   40.706  -22.532  1.00 44.19  ?  269 TYR B C   1 
ATOM   6404 O  O   . TYR B 1 271 ? 1.019   40.275  -23.598  1.00 33.60  ?  269 TYR B O   1 
ATOM   6405 C  CB  . TYR B 1 271 ? -1.433  42.137  -22.866  1.00 39.43  ?  269 TYR B CB  1 
ATOM   6406 C  CG  . TYR B 1 271 ? -2.926  42.280  -23.017  1.00 42.64  ?  269 TYR B CG  1 
ATOM   6407 C  CD1 . TYR B 1 271 ? -3.740  41.172  -23.203  1.00 36.30  ?  269 TYR B CD1 1 
ATOM   6408 C  CD2 . TYR B 1 271 ? -3.519  43.536  -23.007  1.00 45.23  ?  269 TYR B CD2 1 
ATOM   6409 C  CE1 . TYR B 1 271 ? -5.104  41.310  -23.362  1.00 36.05  ?  269 TYR B CE1 1 
ATOM   6410 C  CE2 . TYR B 1 271 ? -4.882  43.684  -23.160  1.00 41.47  ?  269 TYR B CE2 1 
ATOM   6411 C  CZ  . TYR B 1 271 ? -5.670  42.567  -23.340  1.00 39.28  ?  269 TYR B CZ  1 
ATOM   6412 O  OH  . TYR B 1 271 ? -7.030  42.705  -23.488  1.00 44.45  ?  269 TYR B OH  1 
ATOM   6413 N  N   . GLN B 1 272 ? 1.347   41.127  -21.537  1.00 38.83  ?  270 GLN B N   1 
ATOM   6414 C  CA  . GLN B 1 272 ? 2.793   40.979  -21.621  1.00 45.73  ?  270 GLN B CA  1 
ATOM   6415 C  C   . GLN B 1 272 ? 3.184   39.518  -21.444  1.00 43.55  ?  270 GLN B C   1 
ATOM   6416 O  O   . GLN B 1 272 ? 4.097   39.025  -22.115  1.00 40.27  ?  270 GLN B O   1 
ATOM   6417 C  CB  . GLN B 1 272 ? 3.466   41.874  -20.581  1.00 46.60  ?  270 GLN B CB  1 
ATOM   6418 C  CG  . GLN B 1 272 ? 3.213   43.359  -20.826  1.00 46.49  ?  270 GLN B CG  1 
ATOM   6419 C  CD  . GLN B 1 272 ? 4.176   44.262  -20.084  1.00 54.73  ?  270 GLN B CD  1 
ATOM   6420 O  OE1 . GLN B 1 272 ? 5.091   43.793  -19.408  1.00 68.74  ?  270 GLN B OE1 1 
ATOM   6421 N  NE2 . GLN B 1 272 ? 3.971   45.569  -20.204  1.00 59.42  ?  270 GLN B NE2 1 
ATOM   6422 N  N   . LYS B 1 273 ? 2.496   38.813  -20.543  1.00 41.44  ?  271 LYS B N   1 
ATOM   6423 C  CA  . LYS B 1 273 ? 2.750   37.389  -20.360  1.00 41.98  ?  271 LYS B CA  1 
ATOM   6424 C  C   . LYS B 1 273 ? 2.495   36.624  -21.654  1.00 37.06  ?  271 LYS B C   1 
ATOM   6425 O  O   . LYS B 1 273 ? 3.221   35.676  -21.975  1.00 39.54  ?  271 LYS B O   1 
ATOM   6426 C  CB  . LYS B 1 273 ? 1.874   36.848  -19.227  1.00 46.35  ?  271 LYS B CB  1 
ATOM   6427 C  CG  . LYS B 1 273 ? 2.238   35.448  -18.738  1.00 54.81  ?  271 LYS B CG  1 
ATOM   6428 C  CD  . LYS B 1 273 ? 1.382   35.050  -17.536  1.00 48.98  ?  271 LYS B CD  1 
ATOM   6429 C  CE  . LYS B 1 273 ? 2.064   33.996  -16.670  1.00 56.65  ?  271 LYS B CE  1 
ATOM   6430 N  NZ  . LYS B 1 273 ? 2.555   32.818  -17.440  1.00 58.41  ?  271 LYS B NZ  1 
ATOM   6431 N  N   . VAL B 1 274 ? 1.473   37.029  -22.415  1.00 34.87  ?  272 VAL B N   1 
ATOM   6432 C  CA  . VAL B 1 274 ? 1.184   36.373  -23.690  1.00 39.16  ?  272 VAL B CA  1 
ATOM   6433 C  C   . VAL B 1 274 ? 2.392   36.449  -24.616  1.00 44.70  ?  272 VAL B C   1 
ATOM   6434 O  O   . VAL B 1 274 ? 2.665   35.520  -25.386  1.00 36.26  ?  272 VAL B O   1 
ATOM   6435 C  CB  . VAL B 1 274 ? -0.064  36.993  -24.345  1.00 36.77  ?  272 VAL B CB  1 
ATOM   6436 C  CG1 . VAL B 1 274 ? -0.085  36.684  -25.834  1.00 37.60  ?  272 VAL B CG1 1 
ATOM   6437 C  CG2 . VAL B 1 274 ? -1.328  36.480  -23.675  1.00 35.05  ?  272 VAL B CG2 1 
ATOM   6438 N  N   . GLY B 1 275 ? 3.135   37.547  -24.556  1.00 38.15  ?  273 GLY B N   1 
ATOM   6439 C  CA  . GLY B 1 275 ? 4.259   37.730  -25.445  1.00 46.98  ?  273 GLY B CA  1 
ATOM   6440 C  C   . GLY B 1 275 ? 5.552   37.130  -24.954  1.00 40.05  ?  273 GLY B C   1 
ATOM   6441 O  O   . GLY B 1 275 ? 6.553   37.155  -25.677  1.00 48.62  ?  273 GLY B O   1 
ATOM   6442 N  N   . MET B 1 276 ? 5.569   36.585  -23.739  1.00 41.85  ?  274 MET B N   1 
ATOM   6443 C  CA  . MET B 1 276 ? 6.781   36.021  -23.162  1.00 44.88  ?  274 MET B CA  1 
ATOM   6444 C  C   . MET B 1 276 ? 6.766   34.497  -23.112  1.00 41.08  ?  274 MET B C   1 
ATOM   6445 O  O   . MET B 1 276 ? 7.613   33.902  -22.439  1.00 47.39  ?  274 MET B O   1 
ATOM   6446 C  CB  . MET B 1 276 ? 7.004   36.599  -21.764  1.00 47.84  ?  274 MET B CB  1 
ATOM   6447 C  CG  . MET B 1 276 ? 7.230   38.103  -21.774  1.00 51.21  ?  274 MET B CG  1 
ATOM   6448 S  SD  . MET B 1 276 ? 7.706   38.778  -20.175  1.00 62.24  ?  274 MET B SD  1 
ATOM   6449 C  CE  . MET B 1 276 ? 9.183   37.828  -19.837  1.00 54.96  ?  274 MET B CE  1 
ATOM   6450 N  N   . GLN B 1 277 ? 5.836   33.851  -23.813  1.00 39.19  ?  275 GLN B N   1 
ATOM   6451 C  CA  . GLN B 1 277 ? 5.806   32.395  -23.890  1.00 43.21  ?  275 GLN B CA  1 
ATOM   6452 C  C   . GLN B 1 277 ? 5.067   32.002  -25.162  1.00 35.42  ?  275 GLN B C   1 
ATOM   6453 O  O   . GLN B 1 277 ? 4.209   32.742  -25.649  1.00 37.60  ?  275 GLN B O   1 
ATOM   6454 C  CB  . GLN B 1 277 ? 5.194   31.761  -22.630  1.00 41.72  ?  275 GLN B CB  1 
ATOM   6455 C  CG  . GLN B 1 277 ? 3.726   32.030  -22.363  1.00 36.85  ?  275 GLN B CG  1 
ATOM   6456 C  CD  . GLN B 1 277 ? 3.300   31.487  -21.002  1.00 48.46  ?  275 GLN B CD  1 
ATOM   6457 O  OE1 . GLN B 1 277 ? 3.745   31.975  -19.961  1.00 39.56  ?  275 GLN B OE1 1 
ATOM   6458 N  NE2 . GLN B 1 277 ? 2.455   30.463  -21.006  1.00 37.89  ?  275 GLN B NE2 1 
ATOM   6459 N  N   . LYS B 1 278 ? 5.418   30.829  -25.698  1.00 41.33  ?  276 LYS B N   1 
ATOM   6460 C  CA  . LYS B 1 278 ? 4.859   30.398  -26.979  1.00 37.95  ?  276 LYS B CA  1 
ATOM   6461 C  C   . LYS B 1 278 ? 3.342   30.242  -26.914  1.00 37.76  ?  276 LYS B C   1 
ATOM   6462 O  O   . LYS B 1 278 ? 2.622   30.744  -27.785  1.00 38.22  ?  276 LYS B O   1 
ATOM   6463 C  CB  . LYS B 1 278 ? 5.529   29.088  -27.404  1.00 39.20  ?  276 LYS B CB  1 
ATOM   6464 C  CG  . LYS B 1 278 ? 4.797   28.305  -28.485  1.00 51.53  ?  276 LYS B CG  1 
ATOM   6465 C  CD  . LYS B 1 278 ? 4.823   28.996  -29.838  1.00 47.02  ?  276 LYS B CD  1 
ATOM   6466 C  CE  . LYS B 1 278 ? 6.219   29.031  -30.426  1.00 49.85  ?  276 LYS B CE  1 
ATOM   6467 N  NZ  . LYS B 1 278 ? 6.166   29.290  -31.891  1.00 71.62  ?  276 LYS B NZ  1 
ATOM   6468 N  N   . TYR B 1 279 ? 2.830   29.561  -25.894  1.00 38.21  ?  277 TYR B N   1 
ATOM   6469 C  CA  . TYR B 1 279 ? 1.389   29.403  -25.754  1.00 33.74  ?  277 TYR B CA  1 
ATOM   6470 C  C   . TYR B 1 279 ? 0.991   29.677  -24.311  1.00 39.76  ?  277 TYR B C   1 
ATOM   6471 O  O   . TYR B 1 279 ? 1.730   29.348  -23.377  1.00 36.17  ?  277 TYR B O   1 
ATOM   6472 C  CB  . TYR B 1 279 ? 0.888   28.025  -26.250  1.00 31.21  ?  277 TYR B CB  1 
ATOM   6473 C  CG  . TYR B 1 279 ? 1.221   26.806  -25.424  1.00 38.88  ?  277 TYR B CG  1 
ATOM   6474 C  CD1 . TYR B 1 279 ? 0.467   26.466  -24.308  1.00 36.22  ?  277 TYR B CD1 1 
ATOM   6475 C  CD2 . TYR B 1 279 ? 2.251   25.957  -25.800  1.00 33.93  ?  277 TYR B CD2 1 
ATOM   6476 C  CE1 . TYR B 1 279 ? 0.761   25.336  -23.570  1.00 32.91  ?  277 TYR B CE1 1 
ATOM   6477 C  CE2 . TYR B 1 279 ? 2.546   24.831  -25.074  1.00 41.43  ?  277 TYR B CE2 1 
ATOM   6478 C  CZ  . TYR B 1 279 ? 1.801   24.522  -23.960  1.00 36.85  ?  277 TYR B CZ  1 
ATOM   6479 O  OH  . TYR B 1 279 ? 2.107   23.392  -23.240  1.00 51.13  ?  277 TYR B OH  1 
ATOM   6480 N  N   . SER B 1 280 ? -0.151  30.338  -24.145  1.00 39.42  ?  278 SER B N   1 
ATOM   6481 C  CA  . SER B 1 280 ? -0.675  30.718  -22.843  1.00 36.66  ?  278 SER B CA  1 
ATOM   6482 C  C   . SER B 1 280 ? -2.153  30.357  -22.738  1.00 36.17  ?  278 SER B C   1 
ATOM   6483 O  O   . SER B 1 280 ? -2.879  30.357  -23.736  1.00 30.06  ?  278 SER B O   1 
ATOM   6484 C  CB  . SER B 1 280 ? -0.467  32.219  -22.604  1.00 34.37  ?  278 SER B CB  1 
ATOM   6485 O  OG  . SER B 1 280 ? -0.881  32.969  -23.731  1.00 44.36  ?  278 SER B OG  1 
ATOM   6486 N  N   . THR B 1 281 ? -2.586  29.993  -21.530  1.00 34.04  ?  279 THR B N   1 
ATOM   6487 C  CA  . THR B 1 281 ? -3.977  29.638  -21.276  1.00 31.86  ?  279 THR B CA  1 
ATOM   6488 C  C   . THR B 1 281 ? -4.645  30.690  -20.395  1.00 38.56  ?  279 THR B C   1 
ATOM   6489 O  O   . THR B 1 281 ? -4.060  31.139  -19.404  1.00 37.42  ?  279 THR B O   1 
ATOM   6490 C  CB  . THR B 1 281 ? -4.070  28.272  -20.583  1.00 35.62  ?  279 THR B CB  1 
ATOM   6491 O  OG1 . THR B 1 281 ? -3.412  28.337  -19.311  1.00 35.16  ?  279 THR B OG1 1 
ATOM   6492 C  CG2 . THR B 1 281 ? -3.411  27.189  -21.425  1.00 31.34  ?  279 THR B CG2 1 
ATOM   6493 N  N   . LEU B 1 282 ? -5.870  31.093  -20.760  1.00 30.86  ?  280 LEU B N   1 
ATOM   6494 C  CA  . LEU B 1 282 ? -6.649  32.065  -19.987  1.00 34.95  ?  280 LEU B CA  1 
ATOM   6495 C  C   . LEU B 1 282 ? -7.973  31.453  -19.545  1.00 35.20  ?  280 LEU B C   1 
ATOM   6496 O  O   . LEU B 1 282 ? -8.824  31.148  -20.388  1.00 33.53  ?  280 LEU B O   1 
ATOM   6497 C  CB  . LEU B 1 282 ? -6.911  33.356  -20.766  1.00 34.63  ?  280 LEU B CB  1 
ATOM   6498 C  CG  . LEU B 1 282 ? -7.847  34.333  -20.028  1.00 38.07  ?  280 LEU B CG  1 
ATOM   6499 C  CD1 . LEU B 1 282 ? -7.178  34.965  -18.811  1.00 36.05  ?  280 LEU B CD1 1 
ATOM   6500 C  CD2 . LEU B 1 282 ? -8.390  35.418  -20.948  1.00 37.61  ?  280 LEU B CD2 1 
ATOM   6501 N  N   . GLN B 1 283 ? -8.149  31.262  -18.238  1.00 34.24  ?  281 GLN B N   1 
ATOM   6502 C  CA  . GLN B 1 283 ? -9.420  30.789  -17.691  1.00 33.62  ?  281 GLN B CA  1 
ATOM   6503 C  C   . GLN B 1 283 ? -10.309 32.001  -17.433  1.00 34.85  ?  281 GLN B C   1 
ATOM   6504 O  O   . GLN B 1 283 ? -10.028 32.803  -16.537  1.00 33.98  ?  281 GLN B O   1 
ATOM   6505 C  CB  . GLN B 1 283 ? -9.248  29.986  -16.405  1.00 30.23  ?  281 GLN B CB  1 
ATOM   6506 C  CG  . GLN B 1 283 ? -10.601 29.510  -15.852  1.00 31.59  ?  281 GLN B CG  1 
ATOM   6507 C  CD  . GLN B 1 283 ? -10.479 28.495  -14.735  1.00 38.27  ?  281 GLN B CD  1 
ATOM   6508 O  OE1 . GLN B 1 283 ? -9.384  28.211  -14.257  1.00 44.76  ?  281 GLN B OE1 1 
ATOM   6509 N  NE2 . GLN B 1 283 ? -11.612 27.941  -14.312  1.00 36.56  ?  281 GLN B NE2 1 
ATOM   6510 N  N   . GLY B 1 284 ? -11.361 32.146  -18.231  1.00 35.56  ?  282 GLY B N   1 
ATOM   6511 C  CA  . GLY B 1 284 ? -12.292 33.243  -18.095  1.00 30.25  ?  282 GLY B CA  1 
ATOM   6512 C  C   . GLY B 1 284 ? -13.631 32.753  -17.576  1.00 37.67  ?  282 GLY B C   1 
ATOM   6513 O  O   . GLY B 1 284 ? -14.459 32.250  -18.340  1.00 40.24  ?  282 GLY B O   1 
ATOM   6514 N  N   . PRO B 1 285 ? -13.856 32.851  -16.267  1.00 33.13  ?  283 PRO B N   1 
ATOM   6515 C  CA  . PRO B 1 285 ? -15.177 32.506  -15.696  1.00 36.39  ?  283 PRO B CA  1 
ATOM   6516 C  C   . PRO B 1 285 ? -16.299 33.318  -16.320  1.00 37.30  ?  283 PRO B C   1 
ATOM   6517 O  O   . PRO B 1 285 ? -16.052 34.338  -16.979  1.00 40.29  ?  283 PRO B O   1 
ATOM   6518 C  CB  . PRO B 1 285 ? -15.012 32.839  -14.204  1.00 38.62  ?  283 PRO B CB  1 
ATOM   6519 C  CG  . PRO B 1 285 ? -13.545 32.687  -13.967  1.00 36.74  ?  283 PRO B CG  1 
ATOM   6520 C  CD  . PRO B 1 285 ? -12.921 33.282  -15.214  1.00 33.47  ?  283 PRO B CD  1 
ATOM   6521 N  N   . PRO B 1 286 ? -17.552 32.909  -16.114  1.00 42.69  ?  284 PRO B N   1 
ATOM   6522 C  CA  . PRO B 1 286 ? -18.682 33.667  -16.670  1.00 42.12  ?  284 PRO B CA  1 
ATOM   6523 C  C   . PRO B 1 286 ? -18.673 35.129  -16.248  1.00 44.26  ?  284 PRO B C   1 
ATOM   6524 O  O   . PRO B 1 286 ? -18.489 35.459  -15.074  1.00 44.59  ?  284 PRO B O   1 
ATOM   6525 C  CB  . PRO B 1 286 ? -19.900 32.923  -16.107  1.00 46.24  ?  284 PRO B CB  1 
ATOM   6526 C  CG  . PRO B 1 286 ? -19.384 31.527  -15.911  1.00 45.44  ?  284 PRO B CG  1 
ATOM   6527 C  CD  . PRO B 1 286 ? -18.027 31.769  -15.315  1.00 43.03  ?  284 PRO B CD  1 
ATOM   6528 N  N   . GLY B 1 287 ? -18.856 36.007  -17.232  1.00 50.15  ?  285 GLY B N   1 
ATOM   6529 C  CA  . GLY B 1 287 ? -18.972 37.433  -16.991  1.00 47.66  ?  285 GLY B CA  1 
ATOM   6530 C  C   . GLY B 1 287 ? -17.690 38.132  -16.604  1.00 45.14  ?  285 GLY B C   1 
ATOM   6531 O  O   . GLY B 1 287 ? -17.738 39.167  -15.932  1.00 46.94  ?  285 GLY B O   1 
ATOM   6532 N  N   . THR B 1 288 ? -16.542 37.609  -17.031  1.00 41.03  ?  286 THR B N   1 
ATOM   6533 C  CA  . THR B 1 288 ? -15.250 38.168  -16.655  1.00 39.30  ?  286 THR B CA  1 
ATOM   6534 C  C   . THR B 1 288 ? -14.608 38.976  -17.774  1.00 43.22  ?  286 THR B C   1 
ATOM   6535 O  O   . THR B 1 288 ? -13.684 39.752  -17.506  1.00 41.64  ?  286 THR B O   1 
ATOM   6536 C  CB  . THR B 1 288 ? -14.284 37.061  -16.210  1.00 35.74  ?  286 THR B CB  1 
ATOM   6537 O  OG1 . THR B 1 288 ? -14.180 36.065  -17.234  1.00 35.22  ?  286 THR B OG1 1 
ATOM   6538 C  CG2 . THR B 1 288 ? -14.777 36.412  -14.920  1.00 37.27  ?  286 THR B CG2 1 
ATOM   6539 N  N   . GLY B 1 289 ? -15.050 38.784  -19.016  1.00 40.36  ?  287 GLY B N   1 
ATOM   6540 C  CA  . GLY B 1 289 ? -14.584 39.577  -20.136  1.00 38.70  ?  287 GLY B CA  1 
ATOM   6541 C  C   . GLY B 1 289 ? -13.612 38.881  -21.065  1.00 41.83  ?  287 GLY B C   1 
ATOM   6542 O  O   . GLY B 1 289 ? -12.583 39.454  -21.437  1.00 42.52  ?  287 GLY B O   1 
ATOM   6543 N  N   . LYS B 1 290 ? -13.940 37.653  -21.472  1.00 36.99  ?  288 LYS B N   1 
ATOM   6544 C  CA  . LYS B 1 290 ? -13.038 36.899  -22.337  1.00 34.24  ?  288 LYS B CA  1 
ATOM   6545 C  C   . LYS B 1 290 ? -12.871 37.590  -23.685  1.00 39.87  ?  288 LYS B C   1 
ATOM   6546 O  O   . LYS B 1 290 ? -11.746 37.776  -24.166  1.00 40.89  ?  288 LYS B O   1 
ATOM   6547 C  CB  . LYS B 1 290 ? -13.552 35.470  -22.502  1.00 38.55  ?  288 LYS B CB  1 
ATOM   6548 C  CG  . LYS B 1 290 ? -13.526 34.677  -21.202  1.00 40.09  ?  288 LYS B CG  1 
ATOM   6549 C  CD  . LYS B 1 290 ? -14.127 33.291  -21.360  1.00 34.30  ?  288 LYS B CD  1 
ATOM   6550 C  CE  . LYS B 1 290 ? -15.639 33.351  -21.353  1.00 41.12  ?  288 LYS B CE  1 
ATOM   6551 N  NZ  . LYS B 1 290 ? -16.123 33.698  -19.991  1.00 35.11  ?  288 LYS B NZ  1 
ATOM   6552 N  N   . SER B 1 291 ? -13.984 37.980  -24.313  1.00 34.51  ?  289 SER B N   1 
ATOM   6553 C  CA  . SER B 1 291 ? -13.899 38.635  -25.615  1.00 42.68  ?  289 SER B CA  1 
ATOM   6554 C  C   . SER B 1 291 ? -13.257 40.009  -25.488  1.00 40.15  ?  289 SER B C   1 
ATOM   6555 O  O   . SER B 1 291 ? -12.551 40.455  -26.399  1.00 36.24  ?  289 SER B O   1 
ATOM   6556 C  CB  . SER B 1 291 ? -15.287 38.743  -26.248  1.00 37.11  ?  289 SER B CB  1 
ATOM   6557 O  OG  . SER B 1 291 ? -16.172 39.468  -25.412  1.00 59.45  ?  289 SER B OG  1 
ATOM   6558 N  N   . HIS B 1 292 ? -13.499 40.691  -24.367  1.00 40.02  ?  290 HIS B N   1 
ATOM   6559 C  CA  . HIS B 1 292 ? -12.854 41.974  -24.122  1.00 39.93  ?  290 HIS B CA  1 
ATOM   6560 C  C   . HIS B 1 292 ? -11.340 41.802  -24.076  1.00 39.52  ?  290 HIS B C   1 
ATOM   6561 O  O   . HIS B 1 292 ? -10.594 42.591  -24.668  1.00 39.29  ?  290 HIS B O   1 
ATOM   6562 C  CB  . HIS B 1 292 ? -13.390 42.566  -22.817  1.00 40.14  ?  290 HIS B CB  1 
ATOM   6563 C  CG  . HIS B 1 292 ? -13.058 44.010  -22.614  1.00 42.96  ?  290 HIS B CG  1 
ATOM   6564 N  ND1 . HIS B 1 292 ? -13.798 45.027  -23.174  1.00 43.47  ?  290 HIS B ND1 1 
ATOM   6565 C  CD2 . HIS B 1 292 ? -12.078 44.608  -21.896  1.00 43.91  ?  290 HIS B CD2 1 
ATOM   6566 C  CE1 . HIS B 1 292 ? -13.283 46.191  -22.819  1.00 51.02  ?  290 HIS B CE1 1 
ATOM   6567 N  NE2 . HIS B 1 292 ? -12.239 45.964  -22.043  1.00 52.41  ?  290 HIS B NE2 1 
ATOM   6568 N  N   . PHE B 1 293 ? -10.873 40.751  -23.397  1.00 41.15  ?  291 PHE B N   1 
ATOM   6569 C  CA  . PHE B 1 293 ? -9.447  40.444  -23.359  1.00 39.41  ?  291 PHE B CA  1 
ATOM   6570 C  C   . PHE B 1 293 ? -8.913  40.176  -24.762  1.00 33.86  ?  291 PHE B C   1 
ATOM   6571 O  O   . PHE B 1 293 ? -7.867  40.704  -25.155  1.00 37.24  ?  291 PHE B O   1 
ATOM   6572 C  CB  . PHE B 1 293 ? -9.217  39.234  -22.448  1.00 35.81  ?  291 PHE B CB  1 
ATOM   6573 C  CG  . PHE B 1 293 ? -7.779  38.799  -22.338  1.00 36.24  ?  291 PHE B CG  1 
ATOM   6574 C  CD1 . PHE B 1 293 ? -7.224  37.944  -23.277  1.00 38.23  ?  291 PHE B CD1 1 
ATOM   6575 C  CD2 . PHE B 1 293 ? -6.994  39.215  -21.274  1.00 35.47  ?  291 PHE B CD2 1 
ATOM   6576 C  CE1 . PHE B 1 293 ? -5.904  37.533  -23.172  1.00 38.21  ?  291 PHE B CE1 1 
ATOM   6577 C  CE2 . PHE B 1 293 ? -5.676  38.805  -21.163  1.00 40.99  ?  291 PHE B CE2 1 
ATOM   6578 C  CZ  . PHE B 1 293 ? -5.132  37.961  -22.114  1.00 35.70  ?  291 PHE B CZ  1 
ATOM   6579 N  N   . ALA B 1 294 ? -9.634  39.360  -25.535  1.00 33.30  ?  292 ALA B N   1 
ATOM   6580 C  CA  . ALA B 1 294 ? -9.155  38.945  -26.851  1.00 34.13  ?  292 ALA B CA  1 
ATOM   6581 C  C   . ALA B 1 294 ? -8.958  40.140  -27.777  1.00 35.04  ?  292 ALA B C   1 
ATOM   6582 O  O   . ALA B 1 294 ? -7.943  40.235  -28.477  1.00 35.55  ?  292 ALA B O   1 
ATOM   6583 C  CB  . ALA B 1 294 ? -10.128 37.936  -27.462  1.00 33.57  ?  292 ALA B CB  1 
ATOM   6584 N  N   . ILE B 1 295 ? -9.929  41.059  -27.806  1.00 38.58  ?  293 ILE B N   1 
ATOM   6585 C  CA  . ILE B 1 295 ? -9.819  42.221  -28.684  1.00 35.13  ?  293 ILE B CA  1 
ATOM   6586 C  C   . ILE B 1 295 ? -8.810  43.220  -28.137  1.00 39.49  ?  293 ILE B C   1 
ATOM   6587 O  O   . ILE B 1 295 ? -8.102  43.881  -28.906  1.00 39.52  ?  293 ILE B O   1 
ATOM   6588 C  CB  . ILE B 1 295 ? -11.197 42.877  -28.889  1.00 40.08  ?  293 ILE B CB  1 
ATOM   6589 C  CG1 . ILE B 1 295 ? -12.191 41.875  -29.485  1.00 43.11  ?  293 ILE B CG1 1 
ATOM   6590 C  CG2 . ILE B 1 295 ? -11.076 44.115  -29.766  1.00 37.64  ?  293 ILE B CG2 1 
ATOM   6591 C  CD1 . ILE B 1 295 ? -11.662 41.128  -30.690  1.00 44.97  ?  293 ILE B CD1 1 
ATOM   6592 N  N   . GLY B 1 296 ? -8.718  43.347  -26.812  1.00 35.63  ?  294 GLY B N   1 
ATOM   6593 C  CA  . GLY B 1 296 ? -7.731  44.242  -26.233  1.00 37.33  ?  294 GLY B CA  1 
ATOM   6594 C  C   . GLY B 1 296 ? -6.312  43.859  -26.601  1.00 40.41  ?  294 GLY B C   1 
ATOM   6595 O  O   . GLY B 1 296 ? -5.443  44.725  -26.733  1.00 48.32  ?  294 GLY B O   1 
ATOM   6596 N  N   . LEU B 1 297 ? -6.057  42.558  -26.767  1.00 37.74  ?  295 LEU B N   1 
ATOM   6597 C  CA  . LEU B 1 297 ? -4.730  42.103  -27.166  1.00 38.05  ?  295 LEU B CA  1 
ATOM   6598 C  C   . LEU B 1 297 ? -4.294  42.784  -28.458  1.00 41.41  ?  295 LEU B C   1 
ATOM   6599 O  O   . LEU B 1 297 ? -3.115  43.115  -28.631  1.00 41.17  ?  295 LEU B O   1 
ATOM   6600 C  CB  . LEU B 1 297 ? -4.742  40.582  -27.320  1.00 39.99  ?  295 LEU B CB  1 
ATOM   6601 C  CG  . LEU B 1 297 ? -3.435  39.811  -27.477  1.00 42.03  ?  295 LEU B CG  1 
ATOM   6602 C  CD1 . LEU B 1 297 ? -2.509  40.072  -26.301  1.00 41.70  ?  295 LEU B CD1 1 
ATOM   6603 C  CD2 . LEU B 1 297 ? -3.734  38.325  -27.603  1.00 52.07  ?  295 LEU B CD2 1 
ATOM   6604 N  N   . ALA B 1 298 ? -5.236  42.992  -29.383  1.00 42.19  ?  296 ALA B N   1 
ATOM   6605 C  CA  . ALA B 1 298 ? -4.914  43.632  -30.653  1.00 38.69  ?  296 ALA B CA  1 
ATOM   6606 C  C   . ALA B 1 298 ? -4.547  45.094  -30.449  1.00 39.92  ?  296 ALA B C   1 
ATOM   6607 O  O   . ALA B 1 298 ? -3.710  45.637  -31.180  1.00 43.87  ?  296 ALA B O   1 
ATOM   6608 C  CB  . ALA B 1 298 ? -6.091  43.509  -31.618  1.00 39.19  ?  296 ALA B CB  1 
ATOM   6609 N  N   . LEU B 1 299 ? -5.178  45.748  -29.475  1.00 42.24  ?  297 LEU B N   1 
ATOM   6610 C  CA  . LEU B 1 299 ? -4.867  47.140  -29.186  1.00 42.59  ?  297 LEU B CA  1 
ATOM   6611 C  C   . LEU B 1 299 ? -3.524  47.269  -28.482  1.00 35.61  ?  297 LEU B C   1 
ATOM   6612 O  O   . LEU B 1 299 ? -2.800  48.248  -28.699  1.00 36.05  ?  297 LEU B O   1 
ATOM   6613 C  CB  . LEU B 1 299 ? -5.979  47.748  -28.331  1.00 46.02  ?  297 LEU B CB  1 
ATOM   6614 C  CG  . LEU B 1 299 ? -7.338  47.861  -29.027  1.00 50.28  ?  297 LEU B CG  1 
ATOM   6615 C  CD1 . LEU B 1 299 ? -8.406  48.379  -28.073  1.00 43.95  ?  297 LEU B CD1 1 
ATOM   6616 C  CD2 . LEU B 1 299 ? -7.227  48.760  -30.244  1.00 43.64  ?  297 LEU B CD2 1 
ATOM   6617 N  N   . TYR B 1 300 ? -3.172  46.295  -27.640  1.00 45.00  ?  298 TYR B N   1 
ATOM   6618 C  CA  . TYR B 1 300 ? -1.891  46.365  -26.949  1.00 43.82  ?  298 TYR B CA  1 
ATOM   6619 C  C   . TYR B 1 300 ? -0.729  46.050  -27.884  1.00 35.63  ?  298 TYR B C   1 
ATOM   6620 O  O   . TYR B 1 300 ? 0.383   46.544  -27.670  1.00 37.25  ?  298 TYR B O   1 
ATOM   6621 C  CB  . TYR B 1 300 ? -1.884  45.437  -25.734  1.00 35.86  ?  298 TYR B CB  1 
ATOM   6622 C  CG  . TYR B 1 300 ? -0.678  45.675  -24.859  1.00 33.91  ?  298 TYR B CG  1 
ATOM   6623 C  CD1 . TYR B 1 300 ? -0.642  46.756  -23.990  1.00 36.54  ?  298 TYR B CD1 1 
ATOM   6624 C  CD2 . TYR B 1 300 ? 0.421   44.826  -24.899  1.00 33.83  ?  298 TYR B CD2 1 
ATOM   6625 C  CE1 . TYR B 1 300 ? 0.453   46.997  -23.193  1.00 42.78  ?  298 TYR B CE1 1 
ATOM   6626 C  CE2 . TYR B 1 300 ? 1.528   45.058  -24.098  1.00 37.19  ?  298 TYR B CE2 1 
ATOM   6627 C  CZ  . TYR B 1 300 ? 1.535   46.146  -23.245  1.00 39.62  ?  298 TYR B CZ  1 
ATOM   6628 O  OH  . TYR B 1 300 ? 2.626   46.398  -22.441  1.00 41.74  ?  298 TYR B OH  1 
ATOM   6629 N  N   . TYR B 1 301 ? -0.961  45.243  -28.920  1.00 38.83  ?  299 TYR B N   1 
ATOM   6630 C  CA  . TYR B 1 301 ? 0.047   44.922  -29.930  1.00 44.02  ?  299 TYR B CA  1 
ATOM   6631 C  C   . TYR B 1 301 ? -0.474  45.419  -31.277  1.00 40.40  ?  299 TYR B C   1 
ATOM   6632 O  O   . TYR B 1 301 ? -0.800  44.625  -32.171  1.00 42.94  ?  299 TYR B O   1 
ATOM   6633 C  CB  . TYR B 1 301 ? 0.354   43.425  -29.948  1.00 41.82  ?  299 TYR B CB  1 
ATOM   6634 C  CG  . TYR B 1 301 ? 0.970   42.915  -28.655  1.00 41.58  ?  299 TYR B CG  1 
ATOM   6635 C  CD1 . TYR B 1 301 ? 2.260   43.281  -28.284  1.00 47.04  ?  299 TYR B CD1 1 
ATOM   6636 C  CD2 . TYR B 1 301 ? 0.258   42.079  -27.801  1.00 39.00  ?  299 TYR B CD2 1 
ATOM   6637 C  CE1 . TYR B 1 301 ? 2.827   42.820  -27.103  1.00 43.42  ?  299 TYR B CE1 1 
ATOM   6638 C  CE2 . TYR B 1 301 ? 0.816   41.614  -26.618  1.00 35.48  ?  299 TYR B CE2 1 
ATOM   6639 C  CZ  . TYR B 1 301 ? 2.099   41.986  -26.274  1.00 43.02  ?  299 TYR B CZ  1 
ATOM   6640 O  OH  . TYR B 1 301 ? 2.658   41.530  -25.099  1.00 34.55  ?  299 TYR B OH  1 
ATOM   6641 N  N   . PRO B 1 302 ? -0.535  46.741  -31.459  1.00 36.81  ?  300 PRO B N   1 
ATOM   6642 C  CA  . PRO B 1 302 ? -1.214  47.310  -32.639  1.00 44.07  ?  300 PRO B CA  1 
ATOM   6643 C  C   . PRO B 1 302 ? -0.723  46.823  -33.998  1.00 44.24  ?  300 PRO B C   1 
ATOM   6644 O  O   . PRO B 1 302 ? -1.517  46.819  -34.946  1.00 50.77  ?  300 PRO B O   1 
ATOM   6645 C  CB  . PRO B 1 302 ? -0.986  48.820  -32.455  1.00 42.27  ?  300 PRO B CB  1 
ATOM   6646 C  CG  . PRO B 1 302 ? 0.264   48.897  -31.624  1.00 44.29  ?  300 PRO B CG  1 
ATOM   6647 C  CD  . PRO B 1 302 ? 0.056   47.799  -30.624  1.00 37.60  ?  300 PRO B CD  1 
ATOM   6648 N  N   . SER B 1 303 ? 0.541   46.434  -34.149  1.00 38.60  ?  301 SER B N   1 
ATOM   6649 C  CA  . SER B 1 303 ? 1.037   46.066  -35.472  1.00 49.49  ?  301 SER B CA  1 
ATOM   6650 C  C   . SER B 1 303 ? 0.909   44.575  -35.764  1.00 48.43  ?  301 SER B C   1 
ATOM   6651 O  O   . SER B 1 303 ? 1.243   44.143  -36.872  1.00 53.60  ?  301 SER B O   1 
ATOM   6652 C  CB  . SER B 1 303 ? 2.501   46.494  -35.634  1.00 42.78  ?  301 SER B CB  1 
ATOM   6653 O  OG  . SER B 1 303 ? 3.336   45.823  -34.706  1.00 55.81  ?  301 SER B OG  1 
ATOM   6654 N  N   . ALA B 1 304 ? 0.430   43.787  -34.807  1.00 37.71  ?  302 ALA B N   1 
ATOM   6655 C  CA  . ALA B 1 304 ? 0.427   42.337  -34.930  1.00 44.47  ?  302 ALA B CA  1 
ATOM   6656 C  C   . ALA B 1 304 ? -0.747  41.842  -35.767  1.00 38.13  ?  302 ALA B C   1 
ATOM   6657 O  O   . ALA B 1 304 ? -1.857  42.377  -35.690  1.00 41.70  ?  302 ALA B O   1 
ATOM   6658 C  CB  . ALA B 1 304 ? 0.382   41.689  -33.544  1.00 35.87  ?  302 ALA B CB  1 
ATOM   6659 N  N   . ARG B 1 305 ? -0.485  40.820  -36.579  1.00 35.39  ?  303 ARG B N   1 
ATOM   6660 C  CA  . ARG B 1 305 ? -1.515  40.114  -37.332  1.00 40.70  ?  303 ARG B CA  1 
ATOM   6661 C  C   . ARG B 1 305 ? -2.102  39.034  -36.428  1.00 34.76  ?  303 ARG B C   1 
ATOM   6662 O  O   . ARG B 1 305 ? -1.368  38.172  -35.933  1.00 35.40  ?  303 ARG B O   1 
ATOM   6663 C  CB  . ARG B 1 305 ? -0.915  39.514  -38.604  1.00 43.03  ?  303 ARG B CB  1 
ATOM   6664 C  CG  . ARG B 1 305 ? -1.760  38.482  -39.347  1.00 41.84  ?  303 ARG B CG  1 
ATOM   6665 C  CD  . ARG B 1 305 ? -1.017  38.077  -40.624  1.00 53.37  ?  303 ARG B CD  1 
ATOM   6666 N  NE  . ARG B 1 305 ? -1.508  36.850  -41.243  1.00 53.55  ?  303 ARG B NE  1 
ATOM   6667 C  CZ  . ARG B 1 305 ? -2.707  36.704  -41.790  1.00 51.43  ?  303 ARG B CZ  1 
ATOM   6668 N  NH1 . ARG B 1 305 ? -3.518  37.735  -41.963  1.00 51.57  ?  303 ARG B NH1 1 
ATOM   6669 N  NH2 . ARG B 1 305 ? -3.074  35.506  -42.235  1.00 52.10  ?  303 ARG B NH2 1 
ATOM   6670 N  N   . ILE B 1 306 ? -3.410  39.088  -36.193  1.00 34.58  ?  304 ILE B N   1 
ATOM   6671 C  CA  . ILE B 1 306 ? -4.064  38.179  -35.259  1.00 37.39  ?  304 ILE B CA  1 
ATOM   6672 C  C   . ILE B 1 306 ? -5.170  37.414  -35.966  1.00 37.15  ?  304 ILE B C   1 
ATOM   6673 O  O   . ILE B 1 306 ? -5.973  38.002  -36.699  1.00 40.25  ?  304 ILE B O   1 
ATOM   6674 C  CB  . ILE B 1 306 ? -4.624  38.921  -34.034  1.00 34.13  ?  304 ILE B CB  1 
ATOM   6675 C  CG1 . ILE B 1 306 ? -3.519  39.727  -33.354  1.00 36.39  ?  304 ILE B CG1 1 
ATOM   6676 C  CG2 . ILE B 1 306 ? -5.269  37.932  -33.070  1.00 33.04  ?  304 ILE B CG2 1 
ATOM   6677 C  CD1 . ILE B 1 306 ? -3.976  40.466  -32.118  1.00 40.64  ?  304 ILE B CD1 1 
ATOM   6678 N  N   . VAL B 1 307 ? -5.201  36.104  -35.743  1.00 39.48  ?  305 VAL B N   1 
ATOM   6679 C  CA  . VAL B 1 307 ? -6.263  35.230  -36.219  1.00 40.21  ?  305 VAL B CA  1 
ATOM   6680 C  C   . VAL B 1 307 ? -7.095  34.816  -35.013  1.00 36.38  ?  305 VAL B C   1 
ATOM   6681 O  O   . VAL B 1 307 ? -6.571  34.228  -34.060  1.00 38.69  ?  305 VAL B O   1 
ATOM   6682 C  CB  . VAL B 1 307 ? -5.704  34.006  -36.960  1.00 44.79  ?  305 VAL B CB  1 
ATOM   6683 C  CG1 . VAL B 1 307 ? -6.823  33.033  -37.294  1.00 40.46  ?  305 VAL B CG1 1 
ATOM   6684 C  CG2 . VAL B 1 307 ? -4.983  34.449  -38.226  1.00 42.54  ?  305 VAL B CG2 1 
ATOM   6685 N  N   . TYR B 1 308 ? -8.380  35.156  -35.038  1.00 34.57  ?  306 TYR B N   1 
ATOM   6686 C  CA  . TYR B 1 308 ? -9.322  34.769  -33.997  1.00 36.63  ?  306 TYR B CA  1 
ATOM   6687 C  C   . TYR B 1 308 ? -10.084 33.539  -34.477  1.00 35.41  ?  306 TYR B C   1 
ATOM   6688 O  O   . TYR B 1 308 ? -10.711 33.572  -35.540  1.00 39.21  ?  306 TYR B O   1 
ATOM   6689 C  CB  . TYR B 1 308 ? -10.283 35.916  -33.680  1.00 35.56  ?  306 TYR B CB  1 
ATOM   6690 C  CG  . TYR B 1 308 ? -9.610  37.120  -33.054  1.00 37.39  ?  306 TYR B CG  1 
ATOM   6691 C  CD1 . TYR B 1 308 ? -9.449  37.213  -31.678  1.00 32.34  ?  306 TYR B CD1 1 
ATOM   6692 C  CD2 . TYR B 1 308 ? -9.141  38.165  -33.840  1.00 29.88  ?  306 TYR B CD2 1 
ATOM   6693 C  CE1 . TYR B 1 308 ? -8.833  38.312  -31.101  1.00 32.49  ?  306 TYR B CE1 1 
ATOM   6694 C  CE2 . TYR B 1 308 ? -8.527  39.271  -33.270  1.00 35.88  ?  306 TYR B CE2 1 
ATOM   6695 C  CZ  . TYR B 1 308 ? -8.375  39.337  -31.901  1.00 37.80  ?  306 TYR B CZ  1 
ATOM   6696 O  OH  . TYR B 1 308 ? -7.762  40.430  -31.326  1.00 33.59  ?  306 TYR B OH  1 
ATOM   6697 N  N   . THR B 1 309 ? -10.028 32.458  -33.704  1.00 35.01  ?  307 THR B N   1 
ATOM   6698 C  CA  . THR B 1 309 ? -10.664 31.211  -34.101  1.00 35.71  ?  307 THR B CA  1 
ATOM   6699 C  C   . THR B 1 309 ? -11.441 30.607  -32.938  1.00 34.77  ?  307 THR B C   1 
ATOM   6700 O  O   . THR B 1 309 ? -11.133 30.844  -31.768  1.00 36.82  ?  307 THR B O   1 
ATOM   6701 C  CB  . THR B 1 309 ? -9.632  30.199  -34.630  1.00 40.93  ?  307 THR B CB  1 
ATOM   6702 O  OG1 . THR B 1 309 ? -10.312 29.124  -35.290  1.00 43.28  ?  307 THR B OG1 1 
ATOM   6703 C  CG2 . THR B 1 309 ? -8.780  29.646  -33.497  1.00 31.98  ?  307 THR B CG2 1 
ATOM   6704 N  N   . ALA B 1 310 ? -12.469 29.837  -33.288  1.00 39.07  ?  308 ALA B N   1 
ATOM   6705 C  CA  . ALA B 1 310 ? -13.278 29.082  -32.341  1.00 36.60  ?  308 ALA B CA  1 
ATOM   6706 C  C   . ALA B 1 310 ? -13.945 27.947  -33.107  1.00 40.91  ?  308 ALA B C   1 
ATOM   6707 O  O   . ALA B 1 310 ? -13.917 27.908  -34.339  1.00 40.92  ?  308 ALA B O   1 
ATOM   6708 C  CB  . ALA B 1 310 ? -14.313 29.970  -31.644  1.00 35.92  ?  308 ALA B CB  1 
ATOM   6709 N  N   . CYS B 1 311 ? -14.528 27.002  -32.364  1.00 39.23  ?  309 CYS B N   1 
ATOM   6710 C  CA  . CYS B 1 311 ? -15.160 25.865  -33.028  1.00 45.78  ?  309 CYS B CA  1 
ATOM   6711 C  C   . CYS B 1 311 ? -16.501 26.229  -33.659  1.00 44.47  ?  309 CYS B C   1 
ATOM   6712 O  O   . CYS B 1 311 ? -16.812 25.769  -34.763  1.00 46.67  ?  309 CYS B O   1 
ATOM   6713 C  CB  . CYS B 1 311 ? -15.349 24.715  -32.036  1.00 51.06  ?  309 CYS B CB  1 
ATOM   6714 S  SG  . CYS B 1 311 ? -13.816 23.919  -31.500  1.00 52.51  ?  309 CYS B SG  1 
ATOM   6715 N  N   . SER B 1 312 ? -17.299 27.056  -32.990  1.00 41.33  ?  310 SER B N   1 
ATOM   6716 C  CA  . SER B 1 312 ? -18.645 27.387  -33.437  1.00 49.56  ?  310 SER B CA  1 
ATOM   6717 C  C   . SER B 1 312 ? -18.697 28.738  -34.145  1.00 43.60  ?  310 SER B C   1 
ATOM   6718 O  O   . SER B 1 312 ? -17.904 29.639  -33.862  1.00 44.34  ?  310 SER B O   1 
ATOM   6719 C  CB  . SER B 1 312 ? -19.617 27.387  -32.253  1.00 44.01  ?  310 SER B CB  1 
ATOM   6720 O  OG  . SER B 1 312 ? -19.604 28.634  -31.580  1.00 52.41  ?  310 SER B OG  1 
ATOM   6721 N  N   . HIS B 1 313 ? -19.650 28.871  -35.074  1.00 52.48  ?  311 HIS B N   1 
ATOM   6722 C  CA  . HIS B 1 313 ? -19.814 30.150  -35.757  1.00 51.44  ?  311 HIS B CA  1 
ATOM   6723 C  C   . HIS B 1 313 ? -20.289 31.224  -34.790  1.00 54.23  ?  311 HIS B C   1 
ATOM   6724 O  O   . HIS B 1 313 ? -19.896 32.389  -34.916  1.00 53.79  ?  311 HIS B O   1 
ATOM   6725 C  CB  . HIS B 1 313 ? -20.810 30.031  -36.915  1.00 54.29  ?  311 HIS B CB  1 
ATOM   6726 C  CG  . HIS B 1 313 ? -20.267 29.331  -38.121  1.00 52.16  ?  311 HIS B CG  1 
ATOM   6727 N  ND1 . HIS B 1 313 ? -19.461 29.960  -39.045  1.00 56.69  ?  311 HIS B ND1 1 
ATOM   6728 C  CD2 . HIS B 1 313 ? -20.447 28.069  -38.577  1.00 52.52  ?  311 HIS B CD2 1 
ATOM   6729 C  CE1 . HIS B 1 313 ? -19.148 29.109  -40.006  1.00 57.95  ?  311 HIS B CE1 1 
ATOM   6730 N  NE2 . HIS B 1 313 ? -19.735 27.954  -39.746  1.00 54.55  ?  311 HIS B NE2 1 
ATOM   6731 N  N   . ALA B 1 314 ? -21.119 30.848  -33.813  1.00 55.36  ?  312 ALA B N   1 
ATOM   6732 C  CA  . ALA B 1 314 ? -21.602 31.811  -32.829  1.00 56.73  ?  312 ALA B CA  1 
ATOM   6733 C  C   . ALA B 1 314 ? -20.438 32.427  -32.064  1.00 52.26  ?  312 ALA B C   1 
ATOM   6734 O  O   . ALA B 1 314 ? -20.370 33.649  -31.886  1.00 56.57  ?  312 ALA B O   1 
ATOM   6735 C  CB  . ALA B 1 314 ? -22.591 31.138  -31.875  1.00 46.77  ?  312 ALA B CB  1 
ATOM   6736 N  N   . ALA B 1 315 ? -19.512 31.590  -31.592  1.00 52.78  ?  313 ALA B N   1 
ATOM   6737 C  CA  . ALA B 1 315 ? -18.384 32.101  -30.824  1.00 50.13  ?  313 ALA B CA  1 
ATOM   6738 C  C   . ALA B 1 315 ? -17.518 33.021  -31.675  1.00 51.45  ?  313 ALA B C   1 
ATOM   6739 O  O   . ALA B 1 315 ? -17.057 34.066  -31.201  1.00 52.52  ?  313 ALA B O   1 
ATOM   6740 C  CB  . ALA B 1 315 ? -17.558 30.942  -30.267  1.00 47.82  ?  313 ALA B CB  1 
ATOM   6741 N  N   . VAL B 1 316 ? -17.270 32.640  -32.931  1.00 43.02  ?  314 VAL B N   1 
ATOM   6742 C  CA  . VAL B 1 316 ? -16.503 33.504  -33.824  1.00 42.27  ?  314 VAL B CA  1 
ATOM   6743 C  C   . VAL B 1 316 ? -17.225 34.833  -34.026  1.00 47.59  ?  314 VAL B C   1 
ATOM   6744 O  O   . VAL B 1 316 ? -16.608 35.904  -33.993  1.00 45.98  ?  314 VAL B O   1 
ATOM   6745 C  CB  . VAL B 1 316 ? -16.239 32.793  -35.164  1.00 42.43  ?  314 VAL B CB  1 
ATOM   6746 C  CG1 . VAL B 1 316 ? -15.635 33.765  -36.173  1.00 43.41  ?  314 VAL B CG1 1 
ATOM   6747 C  CG2 . VAL B 1 316 ? -15.333 31.588  -34.960  1.00 38.85  ?  314 VAL B CG2 1 
ATOM   6748 N  N   . ASP B 1 317 ? -18.546 34.786  -34.227  1.00 49.35  ?  315 ASP B N   1 
ATOM   6749 C  CA  . ASP B 1 317 ? -19.297 36.008  -34.499  1.00 50.16  ?  315 ASP B CA  1 
ATOM   6750 C  C   . ASP B 1 317 ? -19.304 36.943  -33.297  1.00 52.18  ?  315 ASP B C   1 
ATOM   6751 O  O   . ASP B 1 317 ? -19.327 38.168  -33.468  1.00 52.24  ?  315 ASP B O   1 
ATOM   6752 C  CB  . ASP B 1 317 ? -20.726 35.673  -34.926  1.00 56.37  ?  315 ASP B CB  1 
ATOM   6753 C  CG  . ASP B 1 317 ? -20.784 34.992  -36.281  1.00 54.78  ?  315 ASP B CG  1 
ATOM   6754 O  OD1 . ASP B 1 317 ? -19.744 34.958  -36.973  1.00 58.22  ?  315 ASP B OD1 1 
ATOM   6755 O  OD2 . ASP B 1 317 ? -21.867 34.499  -36.657  1.00 61.65  -1 315 ASP B OD2 1 
ATOM   6756 N  N   . ALA B 1 318 ? -19.291 36.394  -32.080  1.00 50.64  ?  316 ALA B N   1 
ATOM   6757 C  CA  . ALA B 1 318 ? -19.214 37.242  -30.896  1.00 56.37  ?  316 ALA B CA  1 
ATOM   6758 C  C   . ALA B 1 318 ? -17.892 37.999  -30.861  1.00 51.92  ?  316 ALA B C   1 
ATOM   6759 O  O   . ALA B 1 318 ? -17.839 39.159  -30.435  1.00 54.49  ?  316 ALA B O   1 
ATOM   6760 C  CB  . ALA B 1 318 ? -19.393 36.403  -29.633  1.00 54.00  ?  316 ALA B CB  1 
ATOM   6761 N  N   . LEU B 1 319 ? -16.809 37.357  -31.306  1.00 44.81  ?  317 LEU B N   1 
ATOM   6762 C  CA  . LEU B 1 319 ? -15.532 38.054  -31.394  1.00 51.05  ?  317 LEU B CA  1 
ATOM   6763 C  C   . LEU B 1 319 ? -15.585 39.134  -32.468  1.00 45.63  ?  317 LEU B C   1 
ATOM   6764 O  O   . LEU B 1 319 ? -15.018 40.218  -32.297  1.00 46.05  ?  317 LEU B O   1 
ATOM   6765 C  CB  . LEU B 1 319 ? -14.404 37.059  -31.671  1.00 44.17  ?  317 LEU B CB  1 
ATOM   6766 C  CG  . LEU B 1 319 ? -13.997 36.165  -30.498  1.00 50.42  ?  317 LEU B CG  1 
ATOM   6767 C  CD1 . LEU B 1 319 ? -13.273 34.920  -30.987  1.00 48.41  ?  317 LEU B CD1 1 
ATOM   6768 C  CD2 . LEU B 1 319 ? -13.128 36.935  -29.520  1.00 42.75  ?  317 LEU B CD2 1 
ATOM   6769 N  N   . CYS B 1 320 ? -16.249 38.843  -33.592  1.00 46.19  ?  318 CYS B N   1 
ATOM   6770 C  CA  . CYS B 1 320 ? -16.438 39.851  -34.630  1.00 49.62  ?  318 CYS B CA  1 
ATOM   6771 C  C   . CYS B 1 320 ? -17.203 41.055  -34.097  1.00 53.36  ?  318 CYS B C   1 
ATOM   6772 O  O   . CYS B 1 320 ? -16.895 42.200  -34.447  1.00 53.50  ?  318 CYS B O   1 
ATOM   6773 C  CB  . CYS B 1 320 ? -17.187 39.252  -35.820  1.00 47.33  ?  318 CYS B CB  1 
ATOM   6774 S  SG  . CYS B 1 320 ? -16.311 37.971  -36.729  1.00 53.44  ?  318 CYS B SG  1 
ATOM   6775 N  N   . GLU B 1 321 ? -18.200 40.816  -33.241  1.00 50.53  ?  319 GLU B N   1 
ATOM   6776 C  CA  . GLU B 1 321 ? -19.016 41.916  -32.739  1.00 51.51  ?  319 GLU B CA  1 
ATOM   6777 C  C   . GLU B 1 321 ? -18.220 42.790  -31.782  1.00 52.32  ?  319 GLU B C   1 
ATOM   6778 O  O   . GLU B 1 321 ? -18.294 44.023  -31.851  1.00 58.58  ?  319 GLU B O   1 
ATOM   6779 C  CB  . GLU B 1 321 ? -20.271 41.375  -32.058  1.00 56.37  ?  319 GLU B CB  1 
ATOM   6780 C  CG  . GLU B 1 321 ? -21.307 40.796  -33.017  1.00 55.86  ?  319 GLU B CG  1 
ATOM   6781 C  CD  . GLU B 1 321 ? -22.169 41.860  -33.665  1.00 67.06  ?  319 GLU B CD  1 
ATOM   6782 O  OE1 . GLU B 1 321 ? -21.983 43.054  -33.348  1.00 78.77  ?  319 GLU B OE1 1 
ATOM   6783 O  OE2 . GLU B 1 321 ? -23.042 41.502  -34.486  1.00 77.21  -1 319 GLU B OE2 1 
ATOM   6784 N  N   . LYS B 1 322 ? -17.451 42.172  -30.882  1.00 47.42  ?  320 LYS B N   1 
ATOM   6785 C  CA  . LYS B 1 322 ? -16.657 42.958  -29.948  1.00 52.37  ?  320 LYS B CA  1 
ATOM   6786 C  C   . LYS B 1 322 ? -15.551 43.693  -30.690  1.00 51.26  ?  320 LYS B C   1 
ATOM   6787 O  O   . LYS B 1 322 ? -15.155 44.793  -30.289  1.00 55.73  ?  320 LYS B O   1 
ATOM   6788 C  CB  . LYS B 1 322 ? -16.084 42.050  -28.854  1.00 49.49  ?  320 LYS B CB  1 
ATOM   6789 C  CG  . LYS B 1 322 ? -15.151 42.733  -27.858  1.00 47.36  ?  320 LYS B CG  1 
ATOM   6790 C  CD  . LYS B 1 322 ? -15.908 43.598  -26.851  1.00 42.67  ?  320 LYS B CD  1 
ATOM   6791 C  CE  . LYS B 1 322 ? -16.854 42.762  -26.003  1.00 53.09  ?  320 LYS B CE  1 
ATOM   6792 N  NZ  . LYS B 1 322 ? -17.468 43.552  -24.896  1.00 62.03  ?  320 LYS B NZ  1 
ATOM   6793 N  N   . ALA B 1 323 ? -15.062 43.110  -31.788  1.00 46.57  ?  321 ALA B N   1 
ATOM   6794 C  CA  . ALA B 1 323 ? -14.042 43.773  -32.588  1.00 50.20  ?  321 ALA B CA  1 
ATOM   6795 C  C   . ALA B 1 323 ? -14.626 44.983  -33.300  1.00 52.39  ?  321 ALA B C   1 
ATOM   6796 O  O   . ALA B 1 323 ? -13.928 45.982  -33.507  1.00 58.45  ?  321 ALA B O   1 
ATOM   6797 C  CB  . ALA B 1 323 ? -13.435 42.795  -33.593  1.00 46.27  ?  321 ALA B CB  1 
ATOM   6798 N  N   . LEU B 1 324 ? -15.902 44.903  -33.685  1.00 54.66  ?  322 LEU B N   1 
ATOM   6799 C  CA  . LEU B 1 324 ? -16.543 46.006  -34.388  1.00 52.88  ?  322 LEU B CA  1 
ATOM   6800 C  C   . LEU B 1 324 ? -16.547 47.268  -33.536  1.00 58.22  ?  322 LEU B C   1 
ATOM   6801 O  O   . LEU B 1 324 ? -16.587 48.381  -34.073  1.00 59.42  ?  322 LEU B O   1 
ATOM   6802 C  CB  . LEU B 1 324 ? -17.970 45.615  -34.779  1.00 51.70  ?  322 LEU B CB  1 
ATOM   6803 C  CG  . LEU B 1 324 ? -18.569 46.241  -36.041  1.00 65.67  ?  322 LEU B CG  1 
ATOM   6804 C  CD1 . LEU B 1 324 ? -17.657 46.028  -37.239  1.00 59.73  ?  322 LEU B CD1 1 
ATOM   6805 C  CD2 . LEU B 1 324 ? -19.956 45.677  -36.312  1.00 65.14  ?  322 LEU B CD2 1 
ATOM   6806 N  N   . LYS B 1 325 ? -16.515 47.115  -32.209  1.00 59.44  ?  323 LYS B N   1 
ATOM   6807 C  CA  . LYS B 1 325 ? -16.529 48.257  -31.303  1.00 58.19  ?  323 LYS B CA  1 
ATOM   6808 C  C   . LYS B 1 325 ? -15.152 48.860  -31.067  1.00 56.89  ?  323 LYS B C   1 
ATOM   6809 O  O   . LYS B 1 325 ? -15.068 49.998  -30.592  1.00 58.88  ?  323 LYS B O   1 
ATOM   6810 C  CB  . LYS B 1 325 ? -17.095 47.856  -29.938  1.00 53.42  ?  323 LYS B CB  1 
ATOM   6811 C  CG  . LYS B 1 325 ? -18.531 47.384  -29.919  1.00 67.69  ?  323 LYS B CG  1 
ATOM   6812 C  CD  . LYS B 1 325 ? -18.983 47.249  -28.473  1.00 77.90  ?  323 LYS B CD  1 
ATOM   6813 C  CE  . LYS B 1 325 ? -20.464 46.948  -28.358  1.00 73.35  ?  323 LYS B CE  1 
ATOM   6814 N  NZ  . LYS B 1 325 ? -20.895 46.977  -26.933  1.00 75.15  ?  323 LYS B NZ  1 
ATOM   6815 N  N   . TYR B 1 326 ? -14.076 48.141  -31.383  1.00 53.50  ?  324 TYR B N   1 
ATOM   6816 C  CA  . TYR B 1 326 ? -12.740 48.593  -31.015  1.00 54.34  ?  324 TYR B CA  1 
ATOM   6817 C  C   . TYR B 1 326 ? -11.719 48.555  -32.143  1.00 58.29  ?  324 TYR B C   1 
ATOM   6818 O  O   . TYR B 1 326 ? -10.728 49.291  -32.066  1.00 54.76  ?  324 TYR B O   1 
ATOM   6819 C  CB  . TYR B 1 326 ? -12.199 47.748  -29.848  1.00 46.09  ?  324 TYR B CB  1 
ATOM   6820 C  CG  . TYR B 1 326 ? -12.969 47.906  -28.554  1.00 54.53  ?  324 TYR B CG  1 
ATOM   6821 C  CD1 . TYR B 1 326 ? -12.746 48.989  -27.714  1.00 56.00  ?  324 TYR B CD1 1 
ATOM   6822 C  CD2 . TYR B 1 326 ? -13.909 46.958  -28.166  1.00 53.50  ?  324 TYR B CD2 1 
ATOM   6823 C  CE1 . TYR B 1 326 ? -13.450 49.134  -26.530  1.00 58.78  ?  324 TYR B CE1 1 
ATOM   6824 C  CE2 . TYR B 1 326 ? -14.617 47.093  -26.985  1.00 53.79  ?  324 TYR B CE2 1 
ATOM   6825 C  CZ  . TYR B 1 326 ? -14.383 48.181  -26.171  1.00 55.38  ?  324 TYR B CZ  1 
ATOM   6826 O  OH  . TYR B 1 326 ? -15.080 48.318  -24.993  1.00 57.04  ?  324 TYR B OH  1 
ATOM   6827 N  N   . LEU B 1 327 ? -11.929 47.757  -33.192  1.00 56.96  ?  325 LEU B N   1 
ATOM   6828 C  CA  . LEU B 1 327 ? -10.932 47.570  -34.234  1.00 52.21  ?  325 LEU B CA  1 
ATOM   6829 C  C   . LEU B 1 327 ? -11.418 48.138  -35.567  1.00 55.69  ?  325 LEU B C   1 
ATOM   6830 O  O   . LEU B 1 327 ? -12.621 48.144  -35.845  1.00 64.02  ?  325 LEU B O   1 
ATOM   6831 C  CB  . LEU B 1 327 ? -10.615 46.078  -34.395  1.00 47.57  ?  325 LEU B CB  1 
ATOM   6832 C  CG  . LEU B 1 327 ? -9.985  45.385  -33.179  1.00 51.45  ?  325 LEU B CG  1 
ATOM   6833 C  CD1 . LEU B 1 327 ? -9.617  43.945  -33.499  1.00 46.75  ?  325 LEU B CD1 1 
ATOM   6834 C  CD2 . LEU B 1 327 ? -8.769  46.148  -32.668  1.00 45.51  ?  325 LEU B CD2 1 
ATOM   6835 N  N   . PRO B 1 328 ? -10.508 48.617  -36.417  1.00 56.38  ?  326 PRO B N   1 
ATOM   6836 C  CA  . PRO B 1 328 ? -10.920 49.132  -37.731  1.00 57.40  ?  326 PRO B CA  1 
ATOM   6837 C  C   . PRO B 1 328 ? -11.512 48.041  -38.612  1.00 56.48  ?  326 PRO B C   1 
ATOM   6838 O  O   . PRO B 1 328 ? -10.917 46.978  -38.804  1.00 54.68  ?  326 PRO B O   1 
ATOM   6839 C  CB  . PRO B 1 328 ? -9.613  49.687  -38.313  1.00 56.23  ?  326 PRO B CB  1 
ATOM   6840 C  CG  . PRO B 1 328 ? -8.741  49.918  -37.101  1.00 61.23  ?  326 PRO B CG  1 
ATOM   6841 C  CD  . PRO B 1 328 ? -9.055  48.742  -36.232  1.00 54.00  ?  326 PRO B CD  1 
ATOM   6842 N  N   . ILE B 1 329 ? -12.694 48.327  -39.168  1.00 66.43  ?  327 ILE B N   1 
ATOM   6843 C  CA  . ILE B 1 329 ? -13.416 47.336  -39.962  1.00 65.33  ?  327 ILE B CA  1 
ATOM   6844 C  C   . ILE B 1 329 ? -12.665 46.997  -41.245  1.00 57.26  ?  327 ILE B C   1 
ATOM   6845 O  O   . ILE B 1 329 ? -12.796 45.884  -41.770  1.00 54.77  ?  327 ILE B O   1 
ATOM   6846 C  CB  . ILE B 1 329 ? -14.842 47.844  -40.248  1.00 60.69  ?  327 ILE B CB  1 
ATOM   6847 C  CG1 . ILE B 1 329 ? -15.726 46.721  -40.789  1.00 61.47  ?  327 ILE B CG1 1 
ATOM   6848 C  CG2 . ILE B 1 329 ? -14.814 49.023  -41.212  1.00 59.41  ?  327 ILE B CG2 1 
ATOM   6849 C  CD1 . ILE B 1 329 ? -17.196 47.086  -40.822  1.00 64.54  ?  327 ILE B CD1 1 
ATOM   6850 N  N   . ASP B 1 330 ? -11.836 47.914  -41.747  1.00 62.84  ?  328 ASP B N   1 
ATOM   6851 C  CA  . ASP B 1 330 ? -11.136 47.692  -43.007  1.00 57.88  ?  328 ASP B CA  1 
ATOM   6852 C  C   . ASP B 1 330 ? -9.952  46.756  -42.840  1.00 60.03  ?  328 ASP B C   1 
ATOM   6853 O  O   . ASP B 1 330 ? -9.386  46.304  -43.841  1.00 61.59  ?  328 ASP B O   1 
ATOM   6854 C  CB  . ASP B 1 330 ? -10.646 49.017  -43.594  1.00 58.35  ?  328 ASP B CB  1 
ATOM   6855 C  CG  . ASP B 1 330 ? -11.778 49.898  -44.067  1.00 78.01  ?  328 ASP B CG  1 
ATOM   6856 O  OD1 . ASP B 1 330 ? -12.943 49.454  -44.003  1.00 89.32  ?  328 ASP B OD1 1 
ATOM   6857 O  OD2 . ASP B 1 330 ? -11.502 51.034  -44.507  1.00 89.43  -1 328 ASP B OD2 1 
ATOM   6858 N  N   . LYS B 1 331 ? -9.574  46.470  -41.599  1.00 47.42  ?  329 LYS B N   1 
ATOM   6859 C  CA  . LYS B 1 331 ? -8.435  45.630  -41.273  1.00 49.52  ?  329 LYS B CA  1 
ATOM   6860 C  C   . LYS B 1 331 ? -8.888  44.267  -40.766  1.00 46.69  ?  329 LYS B C   1 
ATOM   6861 O  O   . LYS B 1 331 ? -8.059  43.464  -40.327  1.00 49.56  ?  329 LYS B O   1 
ATOM   6862 C  CB  . LYS B 1 331 ? -7.562  46.359  -40.249  1.00 48.93  ?  329 LYS B CB  1 
ATOM   6863 C  CG  . LYS B 1 331 ? -6.778  47.510  -40.879  1.00 59.31  ?  329 LYS B CG  1 
ATOM   6864 C  CD  . LYS B 1 331 ? -6.281  48.536  -39.866  1.00 61.41  ?  329 LYS B CD  1 
ATOM   6865 C  CE  . LYS B 1 331 ? -5.492  47.914  -38.731  1.00 62.68  ?  329 LYS B CE  1 
ATOM   6866 N  NZ  . LYS B 1 331 ? -4.995  48.966  -37.796  1.00 70.96  ?  329 LYS B NZ  1 
ATOM   6867 N  N   . CYS B 1 332 ? -10.191 43.994  -40.837  1.00 46.31  ?  330 CYS B N   1 
ATOM   6868 C  CA  . CYS B 1 332 ? -10.814 42.760  -40.384  1.00 52.34  ?  330 CYS B CA  1 
ATOM   6869 C  C   . CYS B 1 332 ? -11.391 42.004  -41.573  1.00 51.24  ?  330 CYS B C   1 
ATOM   6870 O  O   . CYS B 1 332 ? -11.785 42.604  -42.577  1.00 51.69  ?  330 CYS B O   1 
ATOM   6871 C  CB  . CYS B 1 332 ? -11.939 43.041  -39.385  1.00 47.26  ?  330 CYS B CB  1 
ATOM   6872 S  SG  . CYS B 1 332 ? -11.449 43.960  -37.925  1.00 52.85  ?  330 CYS B SG  1 
ATOM   6873 N  N   . SER B 1 333 ? -11.449 40.679  -41.452  1.00 49.46  ?  331 SER B N   1 
ATOM   6874 C  CA  . SER B 1 333 ? -12.067 39.860  -42.486  1.00 53.61  ?  331 SER B CA  1 
ATOM   6875 C  C   . SER B 1 333 ? -12.648 38.599  -41.862  1.00 50.53  ?  331 SER B C   1 
ATOM   6876 O  O   . SER B 1 333 ? -11.988 37.945  -41.050  1.00 53.11  ?  331 SER B O   1 
ATOM   6877 C  CB  . SER B 1 333 ? -11.054 39.500  -43.580  1.00 59.18  ?  331 SER B CB  1 
ATOM   6878 O  OG  . SER B 1 333 ? -11.628 38.633  -44.543  1.00 55.38  ?  331 SER B OG  1 
ATOM   6879 N  N   . ARG B 1 334 ? -13.883 38.271  -42.240  1.00 54.55  ?  332 ARG B N   1 
ATOM   6880 C  CA  . ARG B 1 334 ? -14.552 37.048  -41.815  1.00 49.49  ?  332 ARG B CA  1 
ATOM   6881 C  C   . ARG B 1 334 ? -14.386 35.999  -42.908  1.00 55.21  ?  332 ARG B C   1 
ATOM   6882 O  O   . ARG B 1 334 ? -14.776 36.233  -44.057  1.00 54.44  ?  332 ARG B O   1 
ATOM   6883 C  CB  . ARG B 1 334 ? -16.037 37.300  -41.545  1.00 50.83  ?  332 ARG B CB  1 
ATOM   6884 C  CG  . ARG B 1 334 ? -16.813 36.076  -41.059  1.00 55.58  ?  332 ARG B CG  1 
ATOM   6885 C  CD  . ARG B 1 334 ? -16.643 35.894  -39.556  1.00 54.01  ?  332 ARG B CD  1 
ATOM   6886 N  NE  . ARG B 1 334 ? -17.583 34.938  -38.980  1.00 57.47  ?  332 ARG B NE  1 
ATOM   6887 C  CZ  . ARG B 1 334 ? -17.571 33.632  -39.216  1.00 61.57  ?  332 ARG B CZ  1 
ATOM   6888 N  NH1 . ARG B 1 334 ? -16.616 33.069  -39.937  1.00 60.18  ?  332 ARG B NH1 1 
ATOM   6889 N  NH2 . ARG B 1 334 ? -18.516 32.867  -38.675  1.00 57.50  ?  332 ARG B NH2 1 
ATOM   6890 N  N   . ILE B 1 335 ? -13.812 34.851  -42.556  1.00 51.34  ?  333 ILE B N   1 
ATOM   6891 C  CA  . ILE B 1 335 ? -13.627 33.759  -43.507  1.00 53.45  ?  333 ILE B CA  1 
ATOM   6892 C  C   . ILE B 1 335 ? -14.829 32.828  -43.441  1.00 52.34  ?  333 ILE B C   1 
ATOM   6893 O  O   . ILE B 1 335 ? -15.215 32.369  -42.359  1.00 54.85  ?  333 ILE B O   1 
ATOM   6894 C  CB  . ILE B 1 335 ? -12.323 32.994  -43.231  1.00 48.33  ?  333 ILE B CB  1 
ATOM   6895 C  CG1 . ILE B 1 335 ? -11.124 33.937  -43.315  1.00 52.34  ?  333 ILE B CG1 1 
ATOM   6896 C  CG2 . ILE B 1 335 ? -12.172 31.835  -44.205  1.00 52.21  ?  333 ILE B CG2 1 
ATOM   6897 C  CD1 . ILE B 1 335 ? -9.796  33.219  -43.382  1.00 60.78  ?  333 ILE B CD1 1 
ATOM   6898 N  N   . ILE B 1 336 ? -15.423 32.556  -44.599  1.00 54.27  ?  334 ILE B N   1 
ATOM   6899 C  CA  . ILE B 1 336 ? -16.637 31.748  -44.687  1.00 64.09  ?  334 ILE B CA  1 
ATOM   6900 C  C   . ILE B 1 336 ? -16.473 30.649  -45.729  1.00 64.43  ?  334 ILE B C   1 
ATOM   6901 O  O   . ILE B 1 336 ? -16.149 30.940  -46.890  1.00 70.30  ?  334 ILE B O   1 
ATOM   6902 C  CB  . ILE B 1 336 ? -17.858 32.622  -45.011  1.00 63.65  ?  334 ILE B CB  1 
ATOM   6903 C  CG1 . ILE B 1 336 ? -18.075 33.634  -43.891  1.00 66.05  ?  334 ILE B CG1 1 
ATOM   6904 C  CG2 . ILE B 1 336 ? -19.094 31.761  -45.205  1.00 71.72  ?  334 ILE B CG2 1 
ATOM   6905 C  CD1 . ILE B 1 336 ? -18.301 32.975  -42.551  1.00 69.24  ?  334 ILE B CD1 1 
ATOM   6906 N  N   . PRO B 1 337 ? -16.685 29.383  -45.369  1.00 67.51  ?  335 PRO B N   1 
ATOM   6907 C  CA  . PRO B 1 337 ? -16.658 28.308  -46.372  1.00 71.25  ?  335 PRO B CA  1 
ATOM   6908 C  C   . PRO B 1 337 ? -17.840 28.446  -47.321  1.00 73.20  ?  335 PRO B C   1 
ATOM   6909 O  O   . PRO B 1 337 ? -18.997 28.322  -46.913  1.00 82.47  ?  335 PRO B O   1 
ATOM   6910 C  CB  . PRO B 1 337 ? -16.752 27.036  -45.524  1.00 68.64  ?  335 PRO B CB  1 
ATOM   6911 C  CG  . PRO B 1 337 ? -17.516 27.480  -44.313  1.00 70.73  ?  335 PRO B CG  1 
ATOM   6912 C  CD  . PRO B 1 337 ? -16.989 28.864  -44.024  1.00 59.18  ?  335 PRO B CD  1 
ATOM   6913 N  N   . ALA B 1 338 ? -17.546 28.698  -48.592  1.00 82.57  ?  336 ALA B N   1 
ATOM   6914 C  CA  . ALA B 1 338 ? -18.595 28.941  -49.574  1.00 79.87  ?  336 ALA B CA  1 
ATOM   6915 C  C   . ALA B 1 338 ? -19.242 27.636  -50.019  1.00 74.83  ?  336 ALA B C   1 
ATOM   6916 O  O   . ALA B 1 338 ? -20.234 27.646  -50.748  1.00 90.92  ?  336 ALA B O   1 
ATOM   6917 C  CB  . ALA B 1 338 ? -18.036 29.690  -50.774  1.00 84.14  ?  336 ALA B CB  1 
ATOM   6918 N  N   . VAL B 1 342 ? -25.367 28.093  -42.672  1.00 90.59  ?  340 VAL B N   1 
ATOM   6919 C  CA  . VAL B 1 342 ? -25.809 28.939  -41.572  1.00 80.62  ?  340 VAL B CA  1 
ATOM   6920 C  C   . VAL B 1 342 ? -25.354 30.378  -41.819  1.00 82.34  ?  340 VAL B C   1 
ATOM   6921 O  O   . VAL B 1 342 ? -24.262 30.611  -42.339  1.00 86.27  ?  340 VAL B O   1 
ATOM   6922 C  CB  . VAL B 1 342 ? -25.280 28.398  -40.224  1.00 82.32  ?  340 VAL B CB  1 
ATOM   6923 C  CG1 . VAL B 1 342 ? -25.412 29.440  -39.125  1.00 87.78  ?  340 VAL B CG1 1 
ATOM   6924 C  CG2 . VAL B 1 342 ? -26.010 27.115  -39.847  1.00 78.30  ?  340 VAL B CG2 1 
ATOM   6925 N  N   . GLU B 1 343 ? -26.195 31.340  -41.446  1.00 80.56  ?  341 GLU B N   1 
ATOM   6926 C  CA  . GLU B 1 343 ? -25.865 32.748  -41.623  1.00 74.95  ?  341 GLU B CA  1 
ATOM   6927 C  C   . GLU B 1 343 ? -24.945 33.219  -40.504  1.00 75.86  ?  341 GLU B C   1 
ATOM   6928 O  O   . GLU B 1 343 ? -25.120 32.850  -39.339  1.00 83.00  ?  341 GLU B O   1 
ATOM   6929 C  CB  . GLU B 1 343 ? -27.139 33.591  -41.670  1.00 74.05  ?  341 GLU B CB  1 
ATOM   6930 C  CG  . GLU B 1 343 ? -27.998 33.299  -42.892  1.00 76.24  ?  341 GLU B CG  1 
ATOM   6931 C  CD  . GLU B 1 343 ? -29.433 33.750  -42.727  1.00 84.63  ?  341 GLU B CD  1 
ATOM   6932 O  OE1 . GLU B 1 343 ? -29.770 34.287  -41.651  1.00 93.30  ?  341 GLU B OE1 1 
ATOM   6933 O  OE2 . GLU B 1 343 ? -30.228 33.560  -43.672  1.00 91.47  -1 341 GLU B OE2 1 
ATOM   6934 N  N   . CYS B 1 344 ? -23.961 34.037  -40.862  1.00 68.84  ?  342 CYS B N   1 
ATOM   6935 C  CA  . CYS B 1 344 ? -22.969 34.511  -39.905  1.00 66.38  ?  342 CYS B CA  1 
ATOM   6936 C  C   . CYS B 1 344 ? -22.851 36.033  -39.945  1.00 60.75  ?  342 CYS B C   1 
ATOM   6937 O  O   . CYS B 1 344 ? -23.703 36.751  -40.484  1.00 67.36  ?  342 CYS B O   1 
ATOM   6938 C  CB  . CYS B 1 344 ? -21.620 33.852  -40.203  1.00 70.66  ?  342 CYS B CB  1 
ATOM   6939 S  SG  . CYS B 1 344 ? -20.857 34.526  -41.692  1.00 97.42  ?  342 CYS B SG  1 
ATOM   6940 N  N   . PHE B 1 345 ? -21.767 36.536  -39.356  1.00 68.30  ?  343 PHE B N   1 
ATOM   6941 C  CA  . PHE B 1 345 ? -21.478 37.962  -39.334  1.00 62.87  ?  343 PHE B CA  1 
ATOM   6942 C  C   . PHE B 1 345 ? -21.194 38.416  -40.764  1.00 64.52  ?  343 PHE B C   1 
ATOM   6943 O  O   . PHE B 1 345 ? -20.391 37.795  -41.468  1.00 71.07  ?  343 PHE B O   1 
ATOM   6944 C  CB  . PHE B 1 345 ? -20.281 38.196  -38.405  1.00 62.01  ?  343 PHE B CB  1 
ATOM   6945 C  CG  . PHE B 1 345 ? -19.953 39.636  -38.138  1.00 64.80  ?  343 PHE B CG  1 
ATOM   6946 C  CD1 . PHE B 1 345 ? -20.544 40.305  -37.077  1.00 66.09  ?  343 PHE B CD1 1 
ATOM   6947 C  CD2 . PHE B 1 345 ? -18.998 40.298  -38.891  1.00 61.11  ?  343 PHE B CD2 1 
ATOM   6948 C  CE1 . PHE B 1 345 ? -20.230 41.623  -36.806  1.00 63.12  ?  343 PHE B CE1 1 
ATOM   6949 C  CE2 . PHE B 1 345 ? -18.677 41.617  -38.624  1.00 65.13  ?  343 PHE B CE2 1 
ATOM   6950 C  CZ  . PHE B 1 345 ? -19.294 42.280  -37.580  1.00 62.69  ?  343 PHE B CZ  1 
ATOM   6951 N  N   . ASP B 1 346 ? -21.837 39.505  -41.199  1.00 59.36  ?  344 ASP B N   1 
ATOM   6952 C  CA  . ASP B 1 346 ? -21.734 39.920  -42.596  1.00 60.05  ?  344 ASP B CA  1 
ATOM   6953 C  C   . ASP B 1 346 ? -21.273 41.365  -42.744  1.00 62.76  ?  344 ASP B C   1 
ATOM   6954 O  O   . ASP B 1 346 ? -21.590 42.022  -43.740  1.00 73.58  ?  344 ASP B O   1 
ATOM   6955 C  CB  . ASP B 1 346 ? -23.060 39.718  -43.332  1.00 68.11  ?  344 ASP B CB  1 
ATOM   6956 C  CG  . ASP B 1 346 ? -24.246 40.268  -42.566  1.00 76.45  ?  344 ASP B CG  1 
ATOM   6957 O  OD1 . ASP B 1 346 ? -24.042 40.820  -41.464  1.00 81.87  ?  344 ASP B OD1 1 
ATOM   6958 O  OD2 . ASP B 1 346 ? -25.382 40.159  -43.076  1.00 76.06  -1 344 ASP B OD2 1 
ATOM   6959 N  N   . LYS B 1 347 ? -20.532 41.883  -41.770  1.00 64.28  ?  345 LYS B N   1 
ATOM   6960 C  CA  . LYS B 1 347 ? -20.127 43.279  -41.795  1.00 66.67  ?  345 LYS B CA  1 
ATOM   6961 C  C   . LYS B 1 347 ? -18.646 43.458  -42.099  1.00 65.95  ?  345 LYS B C   1 
ATOM   6962 O  O   . LYS B 1 347 ? -18.203 44.597  -42.287  1.00 70.62  ?  345 LYS B O   1 
ATOM   6963 C  CB  . LYS B 1 347 ? -20.494 43.958  -40.467  1.00 68.97  ?  345 LYS B CB  1 
ATOM   6964 C  CG  . LYS B 1 347 ? -21.992 43.891  -40.188  1.00 69.24  ?  345 LYS B CG  1 
ATOM   6965 C  CD  . LYS B 1 347 ? -22.403 44.713  -38.981  1.00 70.11  ?  345 LYS B CD  1 
ATOM   6966 C  CE  . LYS B 1 347 ? -23.919 44.793  -38.876  1.00 61.43  ?  345 LYS B CE  1 
ATOM   6967 N  NZ  . LYS B 1 347 ? -24.355 45.815  -37.886  1.00 66.28  ?  345 LYS B NZ  1 
ATOM   6968 N  N   . PHE B 1 348 ? -17.886 42.371  -42.178  1.00 57.43  ?  346 PHE B N   1 
ATOM   6969 C  CA  . PHE B 1 348 ? -16.492 42.386  -42.591  1.00 56.49  ?  346 PHE B CA  1 
ATOM   6970 C  C   . PHE B 1 348 ? -16.391 41.863  -44.018  1.00 62.28  ?  346 PHE B C   1 
ATOM   6971 O  O   . PHE B 1 348 ? -17.273 41.152  -44.505  1.00 65.59  ?  346 PHE B O   1 
ATOM   6972 C  CB  . PHE B 1 348 ? -15.616 41.504  -41.693  1.00 56.20  ?  346 PHE B CB  1 
ATOM   6973 C  CG  . PHE B 1 348 ? -15.499 41.972  -40.274  1.00 49.11  ?  346 PHE B CG  1 
ATOM   6974 C  CD1 . PHE B 1 348 ? -15.548 43.315  -39.954  1.00 49.86  ?  346 PHE B CD1 1 
ATOM   6975 C  CD2 . PHE B 1 348 ? -15.295 41.052  -39.257  1.00 52.35  ?  346 PHE B CD2 1 
ATOM   6976 C  CE1 . PHE B 1 348 ? -15.425 43.731  -38.638  1.00 54.04  ?  346 PHE B CE1 1 
ATOM   6977 C  CE2 . PHE B 1 348 ? -15.167 41.459  -37.947  1.00 48.90  ?  346 PHE B CE2 1 
ATOM   6978 C  CZ  . PHE B 1 348 ? -15.234 42.801  -37.636  1.00 46.11  ?  346 PHE B CZ  1 
ATOM   6979 N  N   . LYS B 1 349 ? -15.310 42.235  -44.696  1.00 61.30  ?  347 LYS B N   1 
ATOM   6980 C  CA  . LYS B 1 349 ? -15.055 41.651  -46.004  1.00 63.99  ?  347 LYS B CA  1 
ATOM   6981 C  C   . LYS B 1 349 ? -14.844 40.150  -45.827  1.00 54.53  ?  347 LYS B C   1 
ATOM   6982 O  O   . LYS B 1 349 ? -14.282 39.703  -44.823  1.00 64.20  ?  347 LYS B O   1 
ATOM   6983 C  CB  . LYS B 1 349 ? -13.844 42.318  -46.657  1.00 65.58  ?  347 LYS B CB  1 
ATOM   6984 C  CG  . LYS B 1 349 ? -12.601 42.361  -45.782  1.00 64.38  ?  347 LYS B CG  1 
ATOM   6985 C  CD  . LYS B 1 349 ? -11.551 43.285  -46.384  1.00 76.28  ?  347 LYS B CD  1 
ATOM   6986 C  CE  . LYS B 1 349 ? -11.341 42.998  -47.862  1.00 70.68  ?  347 LYS B CE  1 
ATOM   6987 N  NZ  . LYS B 1 349 ? -10.195 43.768  -48.424  1.00 75.43  ?  347 LYS B NZ  1 
ATOM   6988 N  N   . VAL B 1 350 ? -15.302 39.366  -46.799  1.00 56.59  ?  348 VAL B N   1 
ATOM   6989 C  CA  . VAL B 1 350 ? -15.291 37.909  -46.698  1.00 58.39  ?  348 VAL B CA  1 
ATOM   6990 C  C   . VAL B 1 350 ? -14.089 37.330  -47.434  1.00 55.03  ?  348 VAL B C   1 
ATOM   6991 O  O   . VAL B 1 350 ? -13.809 37.704  -48.580  1.00 60.61  ?  348 VAL B O   1 
ATOM   6992 C  CB  . VAL B 1 350 ? -16.603 37.316  -47.239  1.00 61.49  ?  348 VAL B CB  1 
ATOM   6993 C  CG1 . VAL B 1 350 ? -16.457 35.823  -47.480  1.00 66.03  ?  348 VAL B CG1 1 
ATOM   6994 C  CG2 . VAL B 1 350 ? -17.750 37.600  -46.278  1.00 65.92  ?  348 VAL B CG2 1 
ATOM   6995 N  N   . ASN B 1 351 ? -13.369 36.423  -46.764  1.00 54.27  ?  349 ASN B N   1 
ATOM   6996 C  CA  . ASN B 1 351 ? -12.316 35.611  -47.385  1.00 61.65  ?  349 ASN B CA  1 
ATOM   6997 C  C   . ASN B 1 351 ? -11.136 36.450  -47.878  1.00 64.06  ?  349 ASN B C   1 
ATOM   6998 O  O   . ASN B 1 351 ? -10.665 36.300  -49.008  1.00 63.32  ?  349 ASN B O   1 
ATOM   6999 C  CB  . ASN B 1 351 ? -12.878 34.728  -48.505  1.00 65.59  ?  349 ASN B CB  1 
ATOM   7000 C  CG  . ASN B 1 351 ? -13.936 33.755  -48.006  1.00 57.46  ?  349 ASN B CG  1 
ATOM   7001 O  OD1 . ASN B 1 351 ? -14.176 33.643  -46.803  1.00 57.49  ?  349 ASN B OD1 1 
ATOM   7002 N  ND2 . ASN B 1 351 ? -14.559 33.032  -48.929  1.00 54.48  ?  349 ASN B ND2 1 
ATOM   7003 N  N   . SER B 1 352 ? -10.660 37.346  -47.022  1.00 58.76  ?  350 SER B N   1 
ATOM   7004 C  CA  . SER B 1 352 ? -9.440  38.108  -47.281  1.00 61.18  ?  350 SER B CA  1 
ATOM   7005 C  C   . SER B 1 352 ? -8.435  37.657  -46.223  1.00 60.85  ?  350 SER B C   1 
ATOM   7006 O  O   . SER B 1 352 ? -8.317  38.259  -45.154  1.00 65.64  ?  350 SER B O   1 
ATOM   7007 C  CB  . SER B 1 352 ? -9.697  39.613  -47.237  1.00 63.36  ?  350 SER B CB  1 
ATOM   7008 O  OG  . SER B 1 352 ? -8.534  40.344  -47.588  1.00 70.77  ?  350 SER B OG  1 
ATOM   7009 N  N   . THR B 1 353 ? -7.708  36.582  -46.537  1.00 53.60  ?  351 THR B N   1 
ATOM   7010 C  CA  . THR B 1 353 ? -6.797  35.971  -45.576  1.00 54.96  ?  351 THR B CA  1 
ATOM   7011 C  C   . THR B 1 353 ? -5.629  36.874  -45.207  1.00 57.49  ?  351 THR B C   1 
ATOM   7012 O  O   . THR B 1 353 ? -4.987  36.638  -44.177  1.00 57.69  ?  351 THR B O   1 
ATOM   7013 C  CB  . THR B 1 353 ? -6.281  34.638  -46.126  1.00 60.74  ?  351 THR B CB  1 
ATOM   7014 O  OG1 . THR B 1 353 ? -7.393  33.817  -46.503  1.00 62.92  ?  351 THR B OG1 1 
ATOM   7015 C  CG2 . THR B 1 353 ? -5.457  33.902  -45.077  1.00 63.47  ?  351 THR B CG2 1 
ATOM   7016 N  N   . LEU B 1 354 ? -5.336  37.901  -46.002  1.00 62.49  ?  352 LEU B N   1 
ATOM   7017 C  CA  . LEU B 1 354 ? -4.170  38.730  -45.735  1.00 66.42  ?  352 LEU B CA  1 
ATOM   7018 C  C   . LEU B 1 354 ? -4.499  39.944  -44.876  1.00 62.69  ?  352 LEU B C   1 
ATOM   7019 O  O   . LEU B 1 354 ? -3.624  40.787  -44.650  1.00 62.56  ?  352 LEU B O   1 
ATOM   7020 C  CB  . LEU B 1 354 ? -3.524  39.177  -47.049  1.00 63.22  ?  352 LEU B CB  1 
ATOM   7021 C  CG  . LEU B 1 354 ? -2.651  38.121  -47.733  1.00 72.13  ?  352 LEU B CG  1 
ATOM   7022 C  CD1 . LEU B 1 354 ? -1.884  37.322  -46.686  1.00 59.42  ?  352 LEU B CD1 1 
ATOM   7023 C  CD2 . LEU B 1 354 ? -3.468  37.204  -48.638  1.00 67.83  ?  352 LEU B CD2 1 
ATOM   7024 N  N   . GLU B 1 355 ? -5.733  40.051  -44.396  1.00 60.11  ?  353 GLU B N   1 
ATOM   7025 C  CA  . GLU B 1 355 ? -6.113  41.144  -43.516  1.00 61.25  ?  353 GLU B CA  1 
ATOM   7026 C  C   . GLU B 1 355 ? -5.444  40.946  -42.156  1.00 51.31  ?  353 GLU B C   1 
ATOM   7027 O  O   . GLU B 1 355 ? -5.181  39.816  -41.732  1.00 54.43  ?  353 GLU B O   1 
ATOM   7028 C  CB  . GLU B 1 355 ? -7.632  41.227  -43.386  1.00 59.60  ?  353 GLU B CB  1 
ATOM   7029 C  CG  . GLU B 1 355 ? -8.317  41.730  -44.662  1.00 60.75  ?  353 GLU B CG  1 
ATOM   7030 C  CD  . GLU B 1 355 ? -8.005  43.180  -45.002  1.00 67.90  ?  353 GLU B CD  1 
ATOM   7031 O  OE1 . GLU B 1 355 ? -7.375  43.876  -44.177  1.00 69.88  ?  353 GLU B OE1 1 
ATOM   7032 O  OE2 . GLU B 1 355 ? -8.375  43.615  -46.115  1.00 70.51  -1 353 GLU B OE2 1 
ATOM   7033 N  N   . GLN B 1 356 ? -5.164  42.055  -41.467  1.00 46.71  ?  354 GLN B N   1 
ATOM   7034 C  CA  . GLN B 1 356 ? -4.485  41.955  -40.176  1.00 47.06  ?  354 GLN B CA  1 
ATOM   7035 C  C   . GLN B 1 356 ? -5.313  41.165  -39.168  1.00 44.55  ?  354 GLN B C   1 
ATOM   7036 O  O   . GLN B 1 356 ? -4.762  40.400  -38.367  1.00 44.87  ?  354 GLN B O   1 
ATOM   7037 C  CB  . GLN B 1 356 ? -4.186  43.357  -39.634  1.00 45.91  ?  354 GLN B CB  1 
ATOM   7038 C  CG  . GLN B 1 356 ? -3.462  43.384  -38.281  1.00 47.40  ?  354 GLN B CG  1 
ATOM   7039 C  CD  . GLN B 1 356 ? -2.965  44.776  -37.897  1.00 44.46  ?  354 GLN B CD  1 
ATOM   7040 O  OE1 . GLN B 1 356 ? -3.114  45.733  -38.656  1.00 50.07  ?  354 GLN B OE1 1 
ATOM   7041 N  NE2 . GLN B 1 356 ? -2.366  44.886  -36.717  1.00 46.09  ?  354 GLN B NE2 1 
ATOM   7042 N  N   . TYR B 1 357 ? -6.629  41.342  -39.182  1.00 43.66  ?  355 TYR B N   1 
ATOM   7043 C  CA  . TYR B 1 357 ? -7.530  40.689  -38.236  1.00 42.57  ?  355 TYR B CA  1 
ATOM   7044 C  C   . TYR B 1 357 ? -8.422  39.712  -39.001  1.00 42.86  ?  355 TYR B C   1 
ATOM   7045 O  O   . TYR B 1 357 ? -9.353  40.130  -39.698  1.00 44.14  ?  355 TYR B O   1 
ATOM   7046 C  CB  . TYR B 1 357 ? -8.324  41.753  -37.483  1.00 41.38  ?  355 TYR B CB  1 
ATOM   7047 C  CG  . TYR B 1 357 ? -7.416  42.717  -36.734  1.00 40.06  ?  355 TYR B CG  1 
ATOM   7048 C  CD1 . TYR B 1 357 ? -6.340  42.246  -35.992  1.00 40.75  ?  355 TYR B CD1 1 
ATOM   7049 C  CD2 . TYR B 1 357 ? -7.595  44.094  -36.821  1.00 47.40  ?  355 TYR B CD2 1 
ATOM   7050 C  CE1 . TYR B 1 357 ? -5.495  43.115  -35.318  1.00 44.45  ?  355 TYR B CE1 1 
ATOM   7051 C  CE2 . TYR B 1 357 ? -6.750  44.972  -36.151  1.00 49.29  ?  355 TYR B CE2 1 
ATOM   7052 C  CZ  . TYR B 1 357 ? -5.702  44.475  -35.402  1.00 41.67  ?  355 TYR B CZ  1 
ATOM   7053 O  OH  . TYR B 1 357 ? -4.860  45.337  -34.735  1.00 43.04  ?  355 TYR B OH  1 
ATOM   7054 N  N   . VAL B 1 358 ? -8.143  38.415  -38.871  1.00 45.18  ?  356 VAL B N   1 
ATOM   7055 C  CA  . VAL B 1 358 ? -8.906  37.365  -39.541  1.00 45.53  ?  356 VAL B CA  1 
ATOM   7056 C  C   . VAL B 1 358 ? -9.738  36.601  -38.518  1.00 41.01  ?  356 VAL B C   1 
ATOM   7057 O  O   . VAL B 1 358 ? -9.205  36.114  -37.514  1.00 43.31  ?  356 VAL B O   1 
ATOM   7058 C  CB  . VAL B 1 358 ? -7.973  36.410  -40.307  1.00 45.99  ?  356 VAL B CB  1 
ATOM   7059 C  CG1 . VAL B 1 358 ? -8.692  35.112  -40.649  1.00 52.00  ?  356 VAL B CG1 1 
ATOM   7060 C  CG2 . VAL B 1 358 ? -7.431  37.085  -41.559  1.00 51.51  ?  356 VAL B CG2 1 
ATOM   7061 N  N   . PHE B 1 359 ? -11.037 36.472  -38.789  1.00 44.75  ?  357 PHE B N   1 
ATOM   7062 C  CA  . PHE B 1 359 ? -11.976 35.773  -37.916  1.00 46.02  ?  357 PHE B CA  1 
ATOM   7063 C  C   . PHE B 1 359 ? -12.498 34.562  -38.677  1.00 49.83  ?  357 PHE B C   1 
ATOM   7064 O  O   . PHE B 1 359 ? -13.016 34.708  -39.789  1.00 46.98  ?  357 PHE B O   1 
ATOM   7065 C  CB  . PHE B 1 359 ? -13.128 36.685  -37.481  1.00 43.80  ?  357 PHE B CB  1 
ATOM   7066 C  CG  . PHE B 1 359 ? -12.684 37.919  -36.740  1.00 43.26  ?  357 PHE B CG  1 
ATOM   7067 C  CD1 . PHE B 1 359 ? -12.143 38.997  -37.420  1.00 42.13  ?  357 PHE B CD1 1 
ATOM   7068 C  CD2 . PHE B 1 359 ? -12.805 37.997  -35.361  1.00 39.80  ?  357 PHE B CD2 1 
ATOM   7069 C  CE1 . PHE B 1 359 ? -11.734 40.131  -36.742  1.00 43.09  ?  357 PHE B CE1 1 
ATOM   7070 C  CE2 . PHE B 1 359 ? -12.397 39.129  -34.677  1.00 44.38  ?  357 PHE B CE2 1 
ATOM   7071 C  CZ  . PHE B 1 359 ? -11.860 40.197  -35.370  1.00 37.28  ?  357 PHE B CZ  1 
ATOM   7072 N  N   . CYS B 1 360 ? -12.352 33.373  -38.095  1.00 43.49  ?  358 CYS B N   1 
ATOM   7073 C  CA  . CYS B 1 360 ? -12.708 32.167  -38.829  1.00 44.59  ?  358 CYS B CA  1 
ATOM   7074 C  C   . CYS B 1 360 ? -12.902 30.996  -37.875  1.00 42.32  ?  358 CYS B C   1 
ATOM   7075 O  O   . CYS B 1 360 ? -12.302 30.949  -36.798  1.00 46.78  ?  358 CYS B O   1 
ATOM   7076 C  CB  . CYS B 1 360 ? -11.623 31.837  -39.861  1.00 51.02  ?  358 CYS B CB  1 
ATOM   7077 S  SG  . CYS B 1 360 ? -11.902 30.340  -40.818  1.00 52.78  ?  358 CYS B SG  1 
ATOM   7078 N  N   . THR B 1 361 ? -13.728 30.039  -38.298  1.00 39.46  ?  359 THR B N   1 
ATOM   7079 C  CA  . THR B 1 361 ? -13.916 28.817  -37.533  1.00 45.20  ?  359 THR B CA  1 
ATOM   7080 C  C   . THR B 1 361 ? -12.769 27.848  -37.803  1.00 41.89  ?  359 THR B C   1 
ATOM   7081 O  O   . THR B 1 361 ? -12.035 27.970  -38.787  1.00 44.63  ?  359 THR B O   1 
ATOM   7082 C  CB  . THR B 1 361 ? -15.245 28.141  -37.879  1.00 42.91  ?  359 THR B CB  1 
ATOM   7083 O  OG1 . THR B 1 361 ? -15.462 28.200  -39.296  1.00 49.13  ?  359 THR B OG1 1 
ATOM   7084 C  CG2 . THR B 1 361 ? -16.404 28.804  -37.149  1.00 40.34  ?  359 THR B CG2 1 
ATOM   7085 N  N   . VAL B 1 362 ? -12.624 26.866  -36.912  1.00 37.48  ?  360 VAL B N   1 
ATOM   7086 C  CA  . VAL B 1 362 ? -11.495 25.947  -37.021  1.00 41.39  ?  360 VAL B CA  1 
ATOM   7087 C  C   . VAL B 1 362 ? -11.559 25.167  -38.329  1.00 46.83  ?  360 VAL B C   1 
ATOM   7088 O  O   . VAL B 1 362 ? -10.533 24.939  -38.981  1.00 51.67  ?  360 VAL B O   1 
ATOM   7089 C  CB  . VAL B 1 362 ? -11.450 25.005  -35.804  1.00 42.39  ?  360 VAL B CB  1 
ATOM   7090 C  CG1 . VAL B 1 362 ? -10.393 23.928  -36.009  1.00 43.20  ?  360 VAL B CG1 1 
ATOM   7091 C  CG2 . VAL B 1 362 ? -11.189 25.791  -34.524  1.00 40.98  ?  360 VAL B CG2 1 
ATOM   7092 N  N   . ASN B 1 363 ? -12.765 24.765  -38.748  1.00 42.79  ?  361 ASN B N   1 
ATOM   7093 C  CA  . ASN B 1 363 ? -12.885 23.922  -39.936  1.00 51.96  ?  361 ASN B CA  1 
ATOM   7094 C  C   . ASN B 1 363 ? -12.586 24.684  -41.220  1.00 52.80  ?  361 ASN B C   1 
ATOM   7095 O  O   . ASN B 1 363 ? -12.181 24.075  -42.216  1.00 56.53  ?  361 ASN B O   1 
ATOM   7096 C  CB  . ASN B 1 363 ? -14.274 23.288  -40.014  1.00 57.87  ?  361 ASN B CB  1 
ATOM   7097 C  CG  . ASN B 1 363 ? -14.394 22.045  -39.154  1.00 69.27  ?  361 ASN B CG  1 
ATOM   7098 O  OD1 . ASN B 1 363 ? -15.272 21.946  -38.298  1.00 74.91  ?  361 ASN B OD1 1 
ATOM   7099 N  ND2 . ASN B 1 363 ? -13.499 21.086  -39.377  1.00 70.61  ?  361 ASN B ND2 1 
ATOM   7100 N  N   . ALA B 1 364 ? -12.791 25.998  -41.228  1.00 49.11  ?  362 ALA B N   1 
ATOM   7101 C  CA  . ALA B 1 364 ? -12.592 26.806  -42.422  1.00 47.80  ?  362 ALA B CA  1 
ATOM   7102 C  C   . ALA B 1 364 ? -11.242 27.509  -42.429  1.00 46.94  ?  362 ALA B C   1 
ATOM   7103 O  O   . ALA B 1 364 ? -10.977 28.309  -43.332  1.00 47.45  ?  362 ALA B O   1 
ATOM   7104 C  CB  . ALA B 1 364 ? -13.717 27.837  -42.560  1.00 50.63  ?  362 ALA B CB  1 
ATOM   7105 N  N   . LEU B 1 365 ? -10.397 27.237  -41.444  1.00 42.50  ?  363 LEU B N   1 
ATOM   7106 C  CA  . LEU B 1 365 ? -9.118  27.921  -41.333  1.00 45.57  ?  363 LEU B CA  1 
ATOM   7107 C  C   . LEU B 1 365 ? -8.271  27.702  -42.583  1.00 45.93  ?  363 LEU B C   1 
ATOM   7108 O  O   . LEU B 1 365 ? -8.156  26.564  -43.060  1.00 43.19  ?  363 LEU B O   1 
ATOM   7109 C  CB  . LEU B 1 365 ? -8.354  27.425  -40.107  1.00 44.14  ?  363 LEU B CB  1 
ATOM   7110 C  CG  . LEU B 1 365 ? -8.742  28.008  -38.750  1.00 51.67  ?  363 LEU B CG  1 
ATOM   7111 C  CD1 . LEU B 1 365 ? -7.903  27.369  -37.657  1.00 43.63  ?  363 LEU B CD1 1 
ATOM   7112 C  CD2 . LEU B 1 365 ? -8.585  29.521  -38.745  1.00 52.70  ?  363 LEU B CD2 1 
ATOM   7113 N  N   . PRO B 1 366 ? -7.660  28.742  -43.129  1.00 51.53  ?  364 PRO B N   1 
ATOM   7114 C  CA  . PRO B 1 366 ? -6.723  28.567  -44.236  1.00 52.00  ?  364 PRO B CA  1 
ATOM   7115 C  C   . PRO B 1 366 ? -5.321  28.301  -43.697  1.00 50.43  ?  364 PRO B C   1 
ATOM   7116 O  O   . PRO B 1 366 ? -5.027  28.510  -42.518  1.00 52.20  ?  364 PRO B O   1 
ATOM   7117 C  CB  . PRO B 1 366 ? -6.796  29.923  -44.937  1.00 50.26  ?  364 PRO B CB  1 
ATOM   7118 C  CG  . PRO B 1 366 ? -6.883  30.867  -43.774  1.00 53.92  ?  364 PRO B CG  1 
ATOM   7119 C  CD  . PRO B 1 366 ? -7.834  30.169  -42.800  1.00 53.37  ?  364 PRO B CD  1 
ATOM   7120 N  N   . GLU B 1 367 ? -4.457  27.823  -44.586  1.00 46.84  ?  365 GLU B N   1 
ATOM   7121 C  CA  . GLU B 1 367 ? -3.054  27.649  -44.231  1.00 50.50  ?  365 GLU B CA  1 
ATOM   7122 C  C   . GLU B 1 367 ? -2.387  29.014  -44.327  1.00 56.53  ?  365 GLU B C   1 
ATOM   7123 O  O   . GLU B 1 367 ? -2.231  29.562  -45.423  1.00 61.73  ?  365 GLU B O   1 
ATOM   7124 C  CB  . GLU B 1 367 ? -2.391  26.627  -45.147  1.00 50.87  ?  365 GLU B CB  1 
ATOM   7125 C  CG  . GLU B 1 367 ? -2.125  25.289  -44.479  1.00 56.47  ?  365 GLU B CG  1 
ATOM   7126 C  CD  . GLU B 1 367 ? -1.891  24.176  -45.477  1.00 70.80  ?  365 GLU B CD  1 
ATOM   7127 O  OE1 . GLU B 1 367 ? -1.007  24.331  -46.346  1.00 73.52  ?  365 GLU B OE1 1 
ATOM   7128 O  OE2 . GLU B 1 367 ? -2.591  23.144  -45.392  1.00 75.17  -1 365 GLU B OE2 1 
ATOM   7129 N  N   . THR B 1 368 ? -2.001  29.572  -43.184  1.00 52.26  ?  366 THR B N   1 
ATOM   7130 C  CA  . THR B 1 368 ? -1.394  30.894  -43.155  1.00 46.90  ?  366 THR B CA  1 
ATOM   7131 C  C   . THR B 1 368 ? -0.539  31.015  -41.900  1.00 47.25  ?  366 THR B C   1 
ATOM   7132 O  O   . THR B 1 368 ? -0.403  30.070  -41.118  1.00 48.37  ?  366 THR B O   1 
ATOM   7133 C  CB  . THR B 1 368 ? -2.466  31.988  -43.214  1.00 50.56  ?  366 THR B CB  1 
ATOM   7134 O  OG1 . THR B 1 368 ? -1.842  33.278  -43.248  1.00 53.01  ?  366 THR B OG1 1 
ATOM   7135 C  CG2 . THR B 1 368 ? -3.387  31.904  -42.003  1.00 49.75  ?  366 THR B CG2 1 
ATOM   7136 N  N   . THR B 1 369 ? 0.051   32.190  -41.724  1.00 47.04  ?  367 THR B N   1 
ATOM   7137 C  CA  . THR B 1 369 ? 0.869   32.512  -40.569  1.00 44.81  ?  367 THR B CA  1 
ATOM   7138 C  C   . THR B 1 369 ? 0.237   33.689  -39.842  1.00 46.90  ?  367 THR B C   1 
ATOM   7139 O  O   . THR B 1 369 ? -0.681  34.341  -40.346  1.00 47.78  ?  367 THR B O   1 
ATOM   7140 C  CB  . THR B 1 369 ? 2.309   32.851  -40.975  1.00 47.95  ?  367 THR B CB  1 
ATOM   7141 O  OG1 . THR B 1 369 ? 2.299   33.927  -41.921  1.00 50.61  ?  367 THR B OG1 1 
ATOM   7142 C  CG2 . THR B 1 369 ? 2.981   31.643  -41.603  1.00 48.02  ?  367 THR B CG2 1 
ATOM   7143 N  N   . ALA B 1 370 ? 0.732   33.959  -38.640  1.00 44.62  ?  368 ALA B N   1 
ATOM   7144 C  CA  . ALA B 1 370 ? 0.220   35.083  -37.873  1.00 45.23  ?  368 ALA B CA  1 
ATOM   7145 C  C   . ALA B 1 370 ? 1.139   35.325  -36.689  1.00 43.74  ?  368 ALA B C   1 
ATOM   7146 O  O   . ALA B 1 370 ? 1.919   34.454  -36.297  1.00 40.97  ?  368 ALA B O   1 
ATOM   7147 C  CB  . ALA B 1 370 ? -1.216  34.834  -37.398  1.00 44.76  ?  368 ALA B CB  1 
ATOM   7148 N  N   . ASP B 1 371 ? 1.045   36.532  -36.135  1.00 43.92  ?  369 ASP B N   1 
ATOM   7149 C  CA  . ASP B 1 371 ? 1.804   36.845  -34.932  1.00 46.32  ?  369 ASP B CA  1 
ATOM   7150 C  C   . ASP B 1 371 ? 1.164   36.206  -33.704  1.00 41.43  ?  369 ASP B C   1 
ATOM   7151 O  O   . ASP B 1 371 ? 1.865   35.633  -32.863  1.00 44.03  ?  369 ASP B O   1 
ATOM   7152 C  CB  . ASP B 1 371 ? 1.933   38.360  -34.764  1.00 41.76  ?  369 ASP B CB  1 
ATOM   7153 C  CG  . ASP B 1 371 ? 2.593   39.027  -35.963  1.00 49.48  ?  369 ASP B CG  1 
ATOM   7154 O  OD1 . ASP B 1 371 ? 3.730   38.638  -36.307  1.00 58.72  ?  369 ASP B OD1 1 
ATOM   7155 O  OD2 . ASP B 1 371 ? 1.988   39.951  -36.550  1.00 44.04  -1 369 ASP B OD2 1 
ATOM   7156 N  N   . ILE B 1 372 ? -0.161  36.296  -33.582  1.00 39.88  ?  370 ILE B N   1 
ATOM   7157 C  CA  . ILE B 1 372 ? -0.896  35.741  -32.451  1.00 36.01  ?  370 ILE B CA  1 
ATOM   7158 C  C   . ILE B 1 372 ? -2.120  34.995  -32.964  1.00 39.95  ?  370 ILE B C   1 
ATOM   7159 O  O   . ILE B 1 372 ? -2.816  35.471  -33.868  1.00 41.78  ?  370 ILE B O   1 
ATOM   7160 C  CB  . ILE B 1 372 ? -1.339  36.827  -31.449  1.00 38.78  ?  370 ILE B CB  1 
ATOM   7161 C  CG1 . ILE B 1 372 ? -0.151  37.660  -30.968  1.00 40.44  ?  370 ILE B CG1 1 
ATOM   7162 C  CG2 . ILE B 1 372 ? -2.067  36.189  -30.273  1.00 41.47  ?  370 ILE B CG2 1 
ATOM   7163 C  CD1 . ILE B 1 372 ? -0.560  38.863  -30.138  1.00 35.82  ?  370 ILE B CD1 1 
ATOM   7164 N  N   . VAL B 1 373 ? -2.382  33.827  -32.384  1.00 39.29  ?  371 VAL B N   1 
ATOM   7165 C  CA  . VAL B 1 373 ? -3.604  33.068  -32.632  1.00 34.06  ?  371 VAL B CA  1 
ATOM   7166 C  C   . VAL B 1 373 ? -4.404  33.040  -31.335  1.00 35.41  ?  371 VAL B C   1 
ATOM   7167 O  O   . VAL B 1 373 ? -3.892  32.614  -30.292  1.00 35.55  ?  371 VAL B O   1 
ATOM   7168 C  CB  . VAL B 1 373 ? -3.310  31.645  -33.129  1.00 38.47  ?  371 VAL B CB  1 
ATOM   7169 C  CG1 . VAL B 1 373 ? -4.594  30.829  -33.165  1.00 30.36  ?  371 VAL B CG1 1 
ATOM   7170 C  CG2 . VAL B 1 373 ? -2.666  31.682  -34.505  1.00 34.26  ?  371 VAL B CG2 1 
ATOM   7171 N  N   . VAL B 1 374 ? -5.646  33.517  -31.391  1.00 36.26  ?  372 VAL B N   1 
ATOM   7172 C  CA  . VAL B 1 374 ? -6.566  33.495  -30.258  1.00 36.40  ?  372 VAL B CA  1 
ATOM   7173 C  C   . VAL B 1 374 ? -7.606  32.413  -30.525  1.00 41.00  ?  372 VAL B C   1 
ATOM   7174 O  O   . VAL B 1 374 ? -8.328  32.473  -31.528  1.00 36.02  ?  372 VAL B O   1 
ATOM   7175 C  CB  . VAL B 1 374 ? -7.233  34.863  -30.041  1.00 35.75  ?  372 VAL B CB  1 
ATOM   7176 C  CG1 . VAL B 1 374 ? -8.208  34.797  -28.874  1.00 37.41  ?  372 VAL B CG1 1 
ATOM   7177 C  CG2 . VAL B 1 374 ? -6.182  35.930  -29.801  1.00 38.13  ?  372 VAL B CG2 1 
ATOM   7178 N  N   . PHE B 1 375 ? -7.672  31.416  -29.643  1.00 40.72  ?  373 PHE B N   1 
ATOM   7179 C  CA  . PHE B 1 375 ? -8.612  30.305  -29.771  1.00 37.62  ?  373 PHE B CA  1 
ATOM   7180 C  C   . PHE B 1 375 ? -9.559  30.394  -28.574  1.00 42.26  ?  373 PHE B C   1 
ATOM   7181 O  O   . PHE B 1 375 ? -9.157  30.108  -27.441  1.00 36.08  ?  373 PHE B O   1 
ATOM   7182 C  CB  . PHE B 1 375 ? -7.823  28.989  -29.807  1.00 33.67  ?  373 PHE B CB  1 
ATOM   7183 C  CG  . PHE B 1 375 ? -8.612  27.771  -30.235  1.00 34.09  ?  373 PHE B CG  1 
ATOM   7184 C  CD1 . PHE B 1 375 ? -9.993  27.717  -30.148  1.00 35.77  ?  373 PHE B CD1 1 
ATOM   7185 C  CD2 . PHE B 1 375 ? -7.935  26.657  -30.720  1.00 32.99  ?  373 PHE B CD2 1 
ATOM   7186 C  CE1 . PHE B 1 375 ? -10.682 26.576  -30.551  1.00 39.27  ?  373 PHE B CE1 1 
ATOM   7187 C  CE2 . PHE B 1 375 ? -8.614  25.520  -31.121  1.00 33.24  ?  373 PHE B CE2 1 
ATOM   7188 C  CZ  . PHE B 1 375 ? -9.988  25.479  -31.036  1.00 35.44  ?  373 PHE B CZ  1 
ATOM   7189 N  N   . ASP B 1 376 ? -10.816 30.770  -28.818  1.00 41.12  ?  374 ASP B N   1 
ATOM   7190 C  CA  . ASP B 1 376 ? -11.783 30.983  -27.747  1.00 43.98  ?  374 ASP B CA  1 
ATOM   7191 C  C   . ASP B 1 376 ? -12.656 29.743  -27.551  1.00 42.92  ?  374 ASP B C   1 
ATOM   7192 O  O   . ASP B 1 376 ? -12.651 28.814  -28.361  1.00 41.27  ?  374 ASP B O   1 
ATOM   7193 C  CB  . ASP B 1 376 ? -12.644 32.217  -28.060  1.00 42.53  ?  374 ASP B CB  1 
ATOM   7194 C  CG  . ASP B 1 376 ? -13.309 32.815  -26.823  1.00 55.38  ?  374 ASP B CG  1 
ATOM   7195 O  OD1 . ASP B 1 376 ? -13.093 32.310  -25.699  1.00 47.99  ?  374 ASP B OD1 1 
ATOM   7196 O  OD2 . ASP B 1 376 ? -14.051 33.808  -26.985  1.00 62.72  -1 374 ASP B OD2 1 
ATOM   7197 N  N   . GLU B 1 377 ? -13.427 29.745  -26.462  1.00 45.78  ?  375 GLU B N   1 
ATOM   7198 C  CA  . GLU B 1 377 ? -14.309 28.626  -26.120  1.00 45.18  ?  375 GLU B CA  1 
ATOM   7199 C  C   . GLU B 1 377 ? -13.534 27.311  -26.167  1.00 37.30  ?  375 GLU B C   1 
ATOM   7200 O  O   . GLU B 1 377 ? -13.911 26.360  -26.854  1.00 39.15  ?  375 GLU B O   1 
ATOM   7201 C  CB  . GLU B 1 377 ? -15.542 28.575  -27.032  1.00 45.82  ?  375 GLU B CB  1 
ATOM   7202 C  CG  . GLU B 1 377 ? -16.586 29.642  -26.744  1.00 55.10  ?  375 GLU B CG  1 
ATOM   7203 C  CD  . GLU B 1 377 ? -17.974 29.269  -27.253  1.00 65.27  ?  375 GLU B CD  1 
ATOM   7204 O  OE1 . GLU B 1 377 ? -18.135 28.165  -27.816  1.00 66.96  ?  375 GLU B OE1 1 
ATOM   7205 O  OE2 . GLU B 1 377 ? -18.909 30.081  -27.078  1.00 78.00  -1 375 GLU B OE2 1 
ATOM   7206 N  N   . ILE B 1 378 ? -12.459 27.257  -25.376  1.00 38.49  ?  376 ILE B N   1 
ATOM   7207 C  CA  . ILE B 1 378 ? -11.564 26.103  -25.415  1.00 39.46  ?  376 ILE B CA  1 
ATOM   7208 C  C   . ILE B 1 378 ? -12.200 24.882  -24.765  1.00 38.61  ?  376 ILE B C   1 
ATOM   7209 O  O   . ILE B 1 378 ? -11.861 23.745  -25.112  1.00 37.79  ?  376 ILE B O   1 
ATOM   7210 C  CB  . ILE B 1 378 ? -10.202 26.459  -24.785  1.00 39.68  ?  376 ILE B CB  1 
ATOM   7211 C  CG1 . ILE B 1 378 ? -9.093  25.593  -25.388  1.00 41.90  ?  376 ILE B CG1 1 
ATOM   7212 C  CG2 . ILE B 1 378 ? -10.238 26.341  -23.268  1.00 38.41  ?  376 ILE B CG2 1 
ATOM   7213 C  CD1 . ILE B 1 378 ? -8.968  25.711  -26.892  1.00 39.25  ?  376 ILE B CD1 1 
ATOM   7214 N  N   . SER B 1 379 ? -13.117 25.077  -23.814  1.00 41.42  ?  377 SER B N   1 
ATOM   7215 C  CA  . SER B 1 379 ? -13.782 23.920  -23.227  1.00 37.61  ?  377 SER B CA  1 
ATOM   7216 C  C   . SER B 1 379 ? -14.548 23.140  -24.290  1.00 43.53  ?  377 SER B C   1 
ATOM   7217 O  O   . SER B 1 379 ? -14.707 21.919  -24.172  1.00 45.50  ?  377 SER B O   1 
ATOM   7218 C  CB  . SER B 1 379 ? -14.716 24.353  -22.095  1.00 38.18  ?  377 SER B CB  1 
ATOM   7219 O  OG  . SER B 1 379 ? -15.819 25.094  -22.589  1.00 45.20  ?  377 SER B OG  1 
ATOM   7220 N  N   . MET B 1 380 ? -15.020 23.825  -25.335  1.00 43.55  ?  378 MET B N   1 
ATOM   7221 C  CA  . MET B 1 380 ? -15.831 23.232  -26.393  1.00 41.20  ?  378 MET B CA  1 
ATOM   7222 C  C   . MET B 1 380 ? -15.004 22.582  -27.491  1.00 42.96  ?  378 MET B C   1 
ATOM   7223 O  O   . MET B 1 380 ? -15.577 22.064  -28.454  1.00 42.72  ?  378 MET B O   1 
ATOM   7224 C  CB  . MET B 1 380 ? -16.729 24.294  -27.037  1.00 45.26  ?  378 MET B CB  1 
ATOM   7225 C  CG  . MET B 1 380 ? -17.817 24.841  -26.145  1.00 49.68  ?  378 MET B CG  1 
ATOM   7226 S  SD  . MET B 1 380 ? -19.054 23.590  -25.771  1.00 54.74  ?  378 MET B SD  1 
ATOM   7227 C  CE  . MET B 1 380 ? -19.681 23.218  -27.410  1.00 51.97  ?  378 MET B CE  1 
ATOM   7228 N  N   . ALA B 1 381 ? -13.685 22.590  -27.377  1.00 40.15  ?  379 ALA B N   1 
ATOM   7229 C  CA  . ALA B 1 381 ? -12.826 22.059  -28.420  1.00 41.43  ?  379 ALA B CA  1 
ATOM   7230 C  C   . ALA B 1 381 ? -12.456 20.617  -28.110  1.00 37.19  ?  379 ALA B C   1 
ATOM   7231 O  O   . ALA B 1 381 ? -12.484 20.179  -26.957  1.00 35.19  ?  379 ALA B O   1 
ATOM   7232 C  CB  . ALA B 1 381 ? -11.558 22.903  -28.573  1.00 42.15  ?  379 ALA B CB  1 
ATOM   7233 N  N   . THR B 1 382 ? -12.144 19.873  -29.161  1.00 39.18  ?  380 THR B N   1 
ATOM   7234 C  CA  . THR B 1 382 ? -11.663 18.508  -29.045  1.00 37.79  ?  380 THR B CA  1 
ATOM   7235 C  C   . THR B 1 382 ? -10.187 18.488  -29.407  1.00 35.49  ?  380 THR B C   1 
ATOM   7236 O  O   . THR B 1 382 ? -9.647  19.449  -29.962  1.00 34.12  ?  380 THR B O   1 
ATOM   7237 C  CB  . THR B 1 382 ? -12.443 17.566  -29.968  1.00 37.66  ?  380 THR B CB  1 
ATOM   7238 O  OG1 . THR B 1 382 ? -12.081 17.831  -31.329  1.00 42.35  ?  380 THR B OG1 1 
ATOM   7239 C  CG2 . THR B 1 382 ? -13.938 17.779  -29.807  1.00 42.21  ?  380 THR B CG2 1 
ATOM   7240 N  N   . ASN B 1 383 ? -9.520  17.384  -29.075  1.00 32.57  ?  381 ASN B N   1 
ATOM   7241 C  CA  . ASN B 1 383 ? -8.138  17.247  -29.511  1.00 31.50  ?  381 ASN B CA  1 
ATOM   7242 C  C   . ASN B 1 383 ? -8.031  17.284  -31.029  1.00 32.50  ?  381 ASN B C   1 
ATOM   7243 O  O   . ASN B 1 383 ? -6.979  17.657  -31.557  1.00 35.98  ?  381 ASN B O   1 
ATOM   7244 C  CB  . ASN B 1 383 ? -7.530  15.972  -28.931  1.00 31.66  ?  381 ASN B CB  1 
ATOM   7245 C  CG  . ASN B 1 383 ? -7.137  16.139  -27.475  1.00 30.68  ?  381 ASN B CG  1 
ATOM   7246 O  OD1 . ASN B 1 383 ? -7.125  17.254  -26.956  1.00 33.20  ?  381 ASN B OD1 1 
ATOM   7247 N  ND2 . ASN B 1 383 ? -6.824  15.037  -26.809  1.00 36.02  ?  381 ASN B ND2 1 
ATOM   7248 N  N   . TYR B 1 384 ? -9.103  16.926  -31.741  1.00 31.89  ?  382 TYR B N   1 
ATOM   7249 C  CA  . TYR B 1 384 ? -9.096  17.046  -33.194  1.00 32.77  ?  382 TYR B CA  1 
ATOM   7250 C  C   . TYR B 1 384 ? -8.966  18.506  -33.617  1.00 37.83  ?  382 TYR B C   1 
ATOM   7251 O  O   . TYR B 1 384 ? -8.149  18.842  -34.482  1.00 37.88  ?  382 TYR B O   1 
ATOM   7252 C  CB  . TYR B 1 384 ? -10.358 16.418  -33.790  1.00 35.68  ?  382 TYR B CB  1 
ATOM   7253 C  CG  . TYR B 1 384 ? -10.244 16.163  -35.278  1.00 38.81  ?  382 TYR B CG  1 
ATOM   7254 C  CD1 . TYR B 1 384 ? -10.547 17.161  -36.196  1.00 36.81  ?  382 TYR B CD1 1 
ATOM   7255 C  CD2 . TYR B 1 384 ? -9.821  14.931  -35.766  1.00 39.93  ?  382 TYR B CD2 1 
ATOM   7256 C  CE1 . TYR B 1 384 ? -10.436 16.942  -37.556  1.00 42.14  ?  382 TYR B CE1 1 
ATOM   7257 C  CE2 . TYR B 1 384 ? -9.709  14.701  -37.131  1.00 41.55  ?  382 TYR B CE2 1 
ATOM   7258 C  CZ  . TYR B 1 384 ? -10.020 15.712  -38.019  1.00 43.06  ?  382 TYR B CZ  1 
ATOM   7259 O  OH  . TYR B 1 384 ? -9.912  15.500  -39.373  1.00 48.68  ?  382 TYR B OH  1 
ATOM   7260 N  N   . ASP B 1 385 ? -9.774  19.391  -33.022  1.00 35.45  ?  383 ASP B N   1 
ATOM   7261 C  CA  . ASP B 1 385 ? -9.694  20.810  -33.365  1.00 40.22  ?  383 ASP B CA  1 
ATOM   7262 C  C   . ASP B 1 385 ? -8.324  21.392  -33.038  1.00 36.40  ?  383 ASP B C   1 
ATOM   7263 O  O   . ASP B 1 385 ? -7.764  22.158  -33.833  1.00 38.38  ?  383 ASP B O   1 
ATOM   7264 C  CB  . ASP B 1 385 ? -10.794 21.601  -32.653  1.00 33.38  ?  383 ASP B CB  1 
ATOM   7265 C  CG  . ASP B 1 385 ? -12.171 21.003  -32.861  1.00 45.89  ?  383 ASP B CG  1 
ATOM   7266 O  OD1 . ASP B 1 385 ? -12.560 20.820  -34.034  1.00 53.85  ?  383 ASP B OD1 1 
ATOM   7267 O  OD2 . ASP B 1 385 ? -12.872 20.738  -31.861  1.00 49.19  -1 383 ASP B OD2 1 
ATOM   7268 N  N   . LEU B 1 386 ? -7.766  21.051  -31.873  1.00 34.15  ?  384 LEU B N   1 
ATOM   7269 C  CA  . LEU B 1 386 ? -6.470  21.611  -31.498  1.00 35.64  ?  384 LEU B CA  1 
ATOM   7270 C  C   . LEU B 1 386 ? -5.411  21.265  -32.533  1.00 36.77  ?  384 LEU B C   1 
ATOM   7271 O  O   . LEU B 1 386 ? -4.549  22.092  -32.854  1.00 34.65  ?  384 LEU B O   1 
ATOM   7272 C  CB  . LEU B 1 386 ? -6.049  21.103  -30.123  1.00 28.65  ?  384 LEU B CB  1 
ATOM   7273 C  CG  . LEU B 1 386 ? -6.950  21.426  -28.934  1.00 34.67  ?  384 LEU B CG  1 
ATOM   7274 C  CD1 . LEU B 1 386 ? -6.406  20.755  -27.689  1.00 34.19  ?  384 LEU B CD1 1 
ATOM   7275 C  CD2 . LEU B 1 386 ? -7.016  22.927  -28.733  1.00 33.88  ?  384 LEU B CD2 1 
ATOM   7276 N  N   . SER B 1 387 ? -5.459  20.043  -33.066  1.00 38.89  ?  385 SER B N   1 
ATOM   7277 C  CA  . SER B 1 387 ? -4.452  19.618  -34.030  1.00 36.90  ?  385 SER B CA  1 
ATOM   7278 C  C   . SER B 1 387 ? -4.619  20.353  -35.353  1.00 39.34  ?  385 SER B C   1 
ATOM   7279 O  O   . SER B 1 387 ? -3.628  20.724  -35.995  1.00 36.78  ?  385 SER B O   1 
ATOM   7280 C  CB  . SER B 1 387 ? -4.533  18.104  -34.230  1.00 36.83  ?  385 SER B CB  1 
ATOM   7281 O  OG  . SER B 1 387 ? -3.759  17.690  -35.339  1.00 38.32  ?  385 SER B OG  1 
ATOM   7282 N  N   . VAL B 1 388 ? -5.867  20.570  -35.776  1.00 35.68  ?  386 VAL B N   1 
ATOM   7283 C  CA  . VAL B 1 388 ? -6.122  21.261  -37.038  1.00 37.01  ?  386 VAL B CA  1 
ATOM   7284 C  C   . VAL B 1 388 ? -5.574  22.680  -36.981  1.00 39.76  ?  386 VAL B C   1 
ATOM   7285 O  O   . VAL B 1 388 ? -4.948  23.162  -37.935  1.00 41.08  ?  386 VAL B O   1 
ATOM   7286 C  CB  . VAL B 1 388 ? -7.627  21.248  -37.363  1.00 38.13  ?  386 VAL B CB  1 
ATOM   7287 C  CG1 . VAL B 1 388 ? -7.929  22.186  -38.524  1.00 41.43  ?  386 VAL B CG1 1 
ATOM   7288 C  CG2 . VAL B 1 388 ? -8.091  19.834  -37.674  1.00 36.62  ?  386 VAL B CG2 1 
ATOM   7289 N  N   . VAL B 1 389 ? -5.810  23.375  -35.867  1.00 35.50  ?  387 VAL B N   1 
ATOM   7290 C  CA  . VAL B 1 389 ? -5.311  24.739  -35.722  1.00 36.23  ?  387 VAL B CA  1 
ATOM   7291 C  C   . VAL B 1 389 ? -3.792  24.752  -35.822  1.00 38.05  ?  387 VAL B C   1 
ATOM   7292 O  O   . VAL B 1 389 ? -3.203  25.570  -36.540  1.00 37.83  ?  387 VAL B O   1 
ATOM   7293 C  CB  . VAL B 1 389 ? -5.790  25.345  -34.390  1.00 32.30  ?  387 VAL B CB  1 
ATOM   7294 C  CG1 . VAL B 1 389 ? -5.094  26.674  -34.127  1.00 39.81  ?  387 VAL B CG1 1 
ATOM   7295 C  CG2 . VAL B 1 389 ? -7.301  25.513  -34.389  1.00 33.87  ?  387 VAL B CG2 1 
ATOM   7296 N  N   . ASN B 1 390 ? -3.134  23.835  -35.106  1.00 38.83  ?  388 ASN B N   1 
ATOM   7297 C  CA  . ASN B 1 390 ? -1.677  23.783  -35.137  1.00 40.88  ?  388 ASN B CA  1 
ATOM   7298 C  C   . ASN B 1 390 ? -1.156  23.416  -36.520  1.00 45.64  ?  388 ASN B C   1 
ATOM   7299 O  O   . ASN B 1 390 ? -0.035  23.794  -36.881  1.00 54.98  ?  388 ASN B O   1 
ATOM   7300 C  CB  . ASN B 1 390 ? -1.170  22.801  -34.082  1.00 40.64  ?  388 ASN B CB  1 
ATOM   7301 C  CG  . ASN B 1 390 ? -1.321  23.341  -32.672  1.00 45.61  ?  388 ASN B CG  1 
ATOM   7302 O  OD1 . ASN B 1 390 ? -1.184  24.542  -32.442  1.00 52.35  ?  388 ASN B OD1 1 
ATOM   7303 N  ND2 . ASN B 1 390 ? -1.606  22.457  -31.721  1.00 41.66  ?  388 ASN B ND2 1 
ATOM   7304 N  N   . ALA B 1 391 ? -1.950  22.693  -37.311  1.00 44.63  ?  389 ALA B N   1 
ATOM   7305 C  CA  . ALA B 1 391 ? -1.487  22.274  -38.626  1.00 42.45  ?  389 ALA B CA  1 
ATOM   7306 C  C   . ALA B 1 391 ? -1.701  23.363  -39.664  1.00 39.29  ?  389 ALA B C   1 
ATOM   7307 O  O   . ALA B 1 391 ? -0.900  23.495  -40.597  1.00 44.31  ?  389 ALA B O   1 
ATOM   7308 C  CB  . ALA B 1 391 ? -2.201  20.994  -39.060  1.00 40.54  ?  389 ALA B CB  1 
ATOM   7309 N  N   . ARG B 1 392 ? -2.777  24.138  -39.529  1.00 37.66  ?  390 ARG B N   1 
ATOM   7310 C  CA  . ARG B 1 392 ? -3.084  25.159  -40.515  1.00 41.83  ?  390 ARG B CA  1 
ATOM   7311 C  C   . ARG B 1 392 ? -2.524  26.522  -40.147  1.00 45.50  ?  390 ARG B C   1 
ATOM   7312 O  O   . ARG B 1 392 ? -2.337  27.359  -41.037  1.00 48.51  ?  390 ARG B O   1 
ATOM   7313 C  CB  . ARG B 1 392 ? -4.602  25.254  -40.652  1.00 40.04  ?  390 ARG B CB  1 
ATOM   7314 C  CG  . ARG B 1 392 ? -5.207  24.038  -41.318  1.00 44.65  ?  390 ARG B CG  1 
ATOM   7315 C  CD  . ARG B 1 392 ? -6.705  24.159  -41.446  1.00 50.75  ?  390 ARG B CD  1 
ATOM   7316 N  NE  . ARG B 1 392 ? -7.290  22.907  -41.907  1.00 52.97  ?  390 ARG B NE  1 
ATOM   7317 C  CZ  . ARG B 1 392 ? -8.588  22.708  -42.085  1.00 55.63  ?  390 ARG B CZ  1 
ATOM   7318 N  NH1 . ARG B 1 392 ? -9.464  23.690  -41.935  1.00 57.11  ?  390 ARG B NH1 1 
ATOM   7319 N  NH2 . ARG B 1 392 ? -9.016  21.503  -42.451  1.00 55.10  ?  390 ARG B NH2 1 
ATOM   7320 N  N   . LEU B 1 393 ? -2.226  26.757  -38.871  1.00 40.17  ?  391 LEU B N   1 
ATOM   7321 C  CA  . LEU B 1 393 ? -1.841  28.084  -38.396  1.00 44.74  ?  391 LEU B CA  1 
ATOM   7322 C  C   . LEU B 1 393 ? -0.470  28.018  -37.739  1.00 52.69  ?  391 LEU B C   1 
ATOM   7323 O  O   . LEU B 1 393 ? -0.329  27.456  -36.647  1.00 52.52  ?  391 LEU B O   1 
ATOM   7324 C  CB  . LEU B 1 393 ? -2.882  28.656  -37.430  1.00 40.35  ?  391 LEU B CB  1 
ATOM   7325 C  CG  . LEU B 1 393 ? -4.267  28.927  -38.019  1.00 47.03  ?  391 LEU B CG  1 
ATOM   7326 C  CD1 . LEU B 1 393 ? -5.129  29.674  -37.020  1.00 48.24  ?  391 LEU B CD1 1 
ATOM   7327 C  CD2 . LEU B 1 393 ? -4.147  29.720  -39.310  1.00 49.27  ?  391 LEU B CD2 1 
ATOM   7328 N  N   . ARG B 1 394 ? 0.538   28.562  -38.409  1.00 37.41  ?  392 ARG B N   1 
ATOM   7329 C  CA  . ARG B 1 394 ? 1.864   28.717  -37.828  1.00 46.07  ?  392 ARG B CA  1 
ATOM   7330 C  C   . ARG B 1 394 ? 1.846   30.117  -37.229  1.00 42.11  ?  392 ARG B C   1 
ATOM   7331 O  O   . ARG B 1 394 ? 1.435   31.078  -37.888  1.00 55.73  ?  392 ARG B O   1 
ATOM   7332 C  CB  . ARG B 1 394 ? 2.968   28.540  -38.867  1.00 51.12  ?  392 ARG B CB  1 
ATOM   7333 C  CG  . ARG B 1 394 ? 3.080   27.089  -39.363  1.00 57.56  ?  392 ARG B CG  1 
ATOM   7334 C  CD  . ARG B 1 394 ? 2.608   26.096  -38.291  1.00 70.42  ?  392 ARG B CD  1 
ATOM   7335 N  NE  . ARG B 1 394 ? 3.236   24.787  -38.416  1.00 77.06  ?  392 ARG B NE  1 
ATOM   7336 C  CZ  . ARG B 1 394 ? 4.533   24.568  -38.262  1.00 86.97  ?  392 ARG B CZ  1 
ATOM   7337 N  NH1 . ARG B 1 394 ? 5.339   25.485  -37.747  1.00 86.55  ?  392 ARG B NH1 1 
ATOM   7338 N  NH2 . ARG B 1 394 ? 5.027   23.378  -38.592  1.00 76.90  ?  392 ARG B NH2 1 
ATOM   7339 N  N   . ALA B 1 395 ? 2.286   30.234  -35.981  1.00 37.55  ?  393 ALA B N   1 
ATOM   7340 C  CA  . ALA B 1 395 ? 2.179   31.490  -35.244  1.00 38.97  ?  393 ALA B CA  1 
ATOM   7341 C  C   . ALA B 1 395 ? 3.332   31.637  -34.259  1.00 40.14  ?  393 ALA B C   1 
ATOM   7342 O  O   . ALA B 1 395 ? 3.950   30.654  -33.842  1.00 41.33  ?  393 ALA B O   1 
ATOM   7343 C  CB  . ALA B 1 395 ? 0.836   31.570  -34.495  1.00 39.76  ?  393 ALA B CB  1 
ATOM   7344 N  N   . LYS B 1 396 ? 3.611   32.888  -33.876  1.00 41.26  ?  394 LYS B N   1 
ATOM   7345 C  CA  . LYS B 1 396 ? 4.621   33.148  -32.855  1.00 42.56  ?  394 LYS B CA  1 
ATOM   7346 C  C   . LYS B 1 396 ? 4.067   32.927  -31.454  1.00 41.37  ?  394 LYS B C   1 
ATOM   7347 O  O   . LYS B 1 396 ? 4.811   32.527  -30.553  1.00 45.03  ?  394 LYS B O   1 
ATOM   7348 C  CB  . LYS B 1 396 ? 5.115   34.592  -32.956  1.00 45.22  ?  394 LYS B CB  1 
ATOM   7349 C  CG  . LYS B 1 396 ? 5.629   35.027  -34.319  1.00 50.84  ?  394 LYS B CG  1 
ATOM   7350 C  CD  . LYS B 1 396 ? 6.011   36.502  -34.259  1.00 56.80  ?  394 LYS B CD  1 
ATOM   7351 C  CE  . LYS B 1 396 ? 6.652   36.997  -35.543  1.00 52.52  ?  394 LYS B CE  1 
ATOM   7352 N  NZ  . LYS B 1 396 ? 6.935   38.460  -35.451  1.00 59.56  ?  394 LYS B NZ  1 
ATOM   7353 N  N   . HIS B 1 397 ? 2.774   33.176  -31.258  1.00 41.74  ?  395 HIS B N   1 
ATOM   7354 C  CA  . HIS B 1 397 ? 2.136   33.059  -29.957  1.00 41.88  ?  395 HIS B CA  1 
ATOM   7355 C  C   . HIS B 1 397 ? 0.727   32.509  -30.125  1.00 38.16  ?  395 HIS B C   1 
ATOM   7356 O  O   . HIS B 1 397 ? 0.023   32.863  -31.076  1.00 41.96  ?  395 HIS B O   1 
ATOM   7357 C  CB  . HIS B 1 397 ? 2.104   34.412  -29.240  1.00 39.37  ?  395 HIS B CB  1 
ATOM   7358 C  CG  . HIS B 1 397 ? 3.463   34.966  -28.949  1.00 35.56  ?  395 HIS B CG  1 
ATOM   7359 N  ND1 . HIS B 1 397 ? 4.158   34.662  -27.800  1.00 40.85  ?  395 HIS B ND1 1 
ATOM   7360 C  CD2 . HIS B 1 397 ? 4.266   35.785  -29.670  1.00 40.06  ?  395 HIS B CD2 1 
ATOM   7361 C  CE1 . HIS B 1 397 ? 5.327   35.278  -27.819  1.00 43.51  ?  395 HIS B CE1 1 
ATOM   7362 N  NE2 . HIS B 1 397 ? 5.417   35.965  -28.943  1.00 41.92  ?  395 HIS B NE2 1 
ATOM   7363 N  N   . TYR B 1 398 ? 0.324   31.643  -29.201  1.00 43.67  ?  396 TYR B N   1 
ATOM   7364 C  CA  . TYR B 1 398 ? -0.994  31.022  -29.218  1.00 40.72  ?  396 TYR B CA  1 
ATOM   7365 C  C   . TYR B 1 398 ? -1.654  31.303  -27.879  1.00 40.71  ?  396 TYR B C   1 
ATOM   7366 O  O   . TYR B 1 398 ? -1.063  31.033  -26.828  1.00 46.78  ?  396 TYR B O   1 
ATOM   7367 C  CB  . TYR B 1 398 ? -0.893  29.508  -29.439  1.00 36.43  ?  396 TYR B CB  1 
ATOM   7368 C  CG  . TYR B 1 398 ? -0.318  29.104  -30.778  1.00 40.04  ?  396 TYR B CG  1 
ATOM   7369 C  CD1 . TYR B 1 398 ? 1.055   29.025  -30.955  1.00 42.85  ?  396 TYR B CD1 1 
ATOM   7370 C  CD2 . TYR B 1 398 ? -1.138  28.768  -31.850  1.00 43.24  ?  396 TYR B CD2 1 
ATOM   7371 C  CE1 . TYR B 1 398 ? 1.603   28.651  -32.164  1.00 53.41  ?  396 TYR B CE1 1 
ATOM   7372 C  CE2 . TYR B 1 398 ? -0.596  28.385  -33.071  1.00 46.19  ?  396 TYR B CE2 1 
ATOM   7373 C  CZ  . TYR B 1 398 ? 0.779   28.330  -33.217  1.00 51.68  ?  396 TYR B CZ  1 
ATOM   7374 O  OH  . TYR B 1 398 ? 1.342   27.955  -34.415  1.00 46.43  ?  396 TYR B OH  1 
ATOM   7375 N  N   . VAL B 1 399 ? -2.868  31.843  -27.912  1.00 37.08  ?  397 VAL B N   1 
ATOM   7376 C  CA  . VAL B 1 399 ? -3.629  32.129  -26.702  1.00 36.80  ?  397 VAL B CA  1 
ATOM   7377 C  C   . VAL B 1 399 ? -4.904  31.299  -26.728  1.00 37.99  ?  397 VAL B C   1 
ATOM   7378 O  O   . VAL B 1 399 ? -5.717  31.426  -27.652  1.00 36.87  ?  397 VAL B O   1 
ATOM   7379 C  CB  . VAL B 1 399 ? -3.947  33.626  -26.571  1.00 35.46  ?  397 VAL B CB  1 
ATOM   7380 C  CG1 . VAL B 1 399 ? -4.523  33.926  -25.198  1.00 33.74  ?  397 VAL B CG1 1 
ATOM   7381 C  CG2 . VAL B 1 399 ? -2.685  34.445  -26.809  1.00 35.42  ?  397 VAL B CG2 1 
ATOM   7382 N  N   . TYR B 1 400 ? -5.088  30.475  -25.703  1.00 34.46  ?  398 TYR B N   1 
ATOM   7383 C  CA  . TYR B 1 400 ? -6.277  29.649  -25.542  1.00 36.67  ?  398 TYR B CA  1 
ATOM   7384 C  C   . TYR B 1 400 ? -7.142  30.255  -24.446  1.00 34.45  ?  398 TYR B C   1 
ATOM   7385 O  O   . TYR B 1 400 ? -6.715  30.345  -23.291  1.00 33.68  ?  398 TYR B O   1 
ATOM   7386 C  CB  . TYR B 1 400 ? -5.897  28.204  -25.214  1.00 34.04  ?  398 TYR B CB  1 
ATOM   7387 C  CG  . TYR B 1 400 ? -4.992  27.579  -26.253  1.00 38.12  ?  398 TYR B CG  1 
ATOM   7388 C  CD1 . TYR B 1 400 ? -5.515  27.088  -27.442  1.00 37.62  ?  398 TYR B CD1 1 
ATOM   7389 C  CD2 . TYR B 1 400 ? -3.619  27.477  -26.049  1.00 35.95  ?  398 TYR B CD2 1 
ATOM   7390 C  CE1 . TYR B 1 400 ? -4.705  26.515  -28.398  1.00 37.85  ?  398 TYR B CE1 1 
ATOM   7391 C  CE2 . TYR B 1 400 ? -2.797  26.904  -27.004  1.00 41.88  ?  398 TYR B CE2 1 
ATOM   7392 C  CZ  . TYR B 1 400 ? -3.349  26.424  -28.177  1.00 36.07  ?  398 TYR B CZ  1 
ATOM   7393 O  OH  . TYR B 1 400 ? -2.550  25.855  -29.140  1.00 52.16  ?  398 TYR B OH  1 
ATOM   7394 N  N   . ILE B 1 401 ? -8.340  30.695  -24.820  1.00 38.09  ?  399 ILE B N   1 
ATOM   7395 C  CA  . ILE B 1 401 ? -9.286  31.317  -23.903  1.00 38.29  ?  399 ILE B CA  1 
ATOM   7396 C  C   . ILE B 1 401 ? -10.487 30.397  -23.732  1.00 38.97  ?  399 ILE B C   1 
ATOM   7397 O  O   . ILE B 1 401 ? -11.040 29.893  -24.717  1.00 35.69  ?  399 ILE B O   1 
ATOM   7398 C  CB  . ILE B 1 401 ? -9.712  32.708  -24.404  1.00 38.08  ?  399 ILE B CB  1 
ATOM   7399 C  CG1 . ILE B 1 401 ? -8.472  33.589  -24.600  1.00 35.89  ?  399 ILE B CG1 1 
ATOM   7400 C  CG2 . ILE B 1 401 ? -10.703 33.347  -23.447  1.00 37.41  ?  399 ILE B CG2 1 
ATOM   7401 C  CD1 . ILE B 1 401 ? -8.759  34.933  -25.236  1.00 35.47  ?  399 ILE B CD1 1 
ATOM   7402 N  N   . GLY B 1 402 ? -10.883 30.183  -22.484  1.00 37.31  ?  400 GLY B N   1 
ATOM   7403 C  CA  . GLY B 1 402 ? -12.020 29.335  -22.198  1.00 35.52  ?  400 GLY B CA  1 
ATOM   7404 C  C   . GLY B 1 402 ? -12.226 29.205  -20.707  1.00 39.31  ?  400 GLY B C   1 
ATOM   7405 O  O   . GLY B 1 402 ? -11.764 30.040  -19.927  1.00 38.58  ?  400 GLY B O   1 
ATOM   7406 N  N   . ASP B 1 403 ? -12.930 28.145  -20.315  1.00 38.45  ?  401 ASP B N   1 
ATOM   7407 C  CA  . ASP B 1 403 ? -13.184 27.854  -18.909  1.00 37.81  ?  401 ASP B CA  1 
ATOM   7408 C  C   . ASP B 1 403 ? -13.424 26.360  -18.720  1.00 36.04  ?  401 ASP B C   1 
ATOM   7409 O  O   . ASP B 1 403 ? -14.496 25.857  -19.080  1.00 36.85  ?  401 ASP B O   1 
ATOM   7410 C  CB  . ASP B 1 403 ? -14.382 28.664  -18.410  1.00 39.61  ?  401 ASP B CB  1 
ATOM   7411 C  CG  . ASP B 1 403 ? -14.631 28.489  -16.925  1.00 35.78  ?  401 ASP B CG  1 
ATOM   7412 O  OD1 . ASP B 1 403 ? -13.851 27.769  -16.269  1.00 38.85  ?  401 ASP B OD1 1 
ATOM   7413 O  OD2 . ASP B 1 403 ? -15.605 29.083  -16.413  1.00 37.94  -1 401 ASP B OD2 1 
ATOM   7414 N  N   . PRO B 1 404 ? -12.460 25.613  -18.159  1.00 36.19  ?  402 PRO B N   1 
ATOM   7415 C  CA  . PRO B 1 404 ? -12.679 24.176  -17.934  1.00 40.90  ?  402 PRO B CA  1 
ATOM   7416 C  C   . PRO B 1 404 ? -13.832 23.875  -16.987  1.00 32.17  ?  402 PRO B C   1 
ATOM   7417 O  O   . PRO B 1 404 ? -14.180 22.710  -16.777  1.00 35.38  ?  402 PRO B O   1 
ATOM   7418 C  CB  . PRO B 1 404 ? -11.333 23.716  -17.358  1.00 39.74  ?  402 PRO B CB  1 
ATOM   7419 C  CG  . PRO B 1 404 ? -10.820 24.941  -16.673  1.00 42.25  ?  402 PRO B CG  1 
ATOM   7420 C  CD  . PRO B 1 404 ? -11.134 26.026  -17.672  1.00 38.25  ?  402 PRO B CD  1 
ATOM   7421 N  N   . ALA B 1 405 ? -14.438 24.908  -16.411  1.00 34.08  ?  403 ALA B N   1 
ATOM   7422 C  CA  . ALA B 1 405 ? -15.533 24.723  -15.473  1.00 31.35  ?  403 ALA B CA  1 
ATOM   7423 C  C   . ALA B 1 405 ? -16.882 24.856  -16.158  1.00 30.38  ?  403 ALA B C   1 
ATOM   7424 O  O   . ALA B 1 405 ? -17.920 24.709  -15.503  1.00 31.73  ?  403 ALA B O   1 
ATOM   7425 C  CB  . ALA B 1 405 ? -15.430 25.728  -14.320  1.00 35.45  ?  403 ALA B CB  1 
ATOM   7426 N  N   . GLN B 1 406 ? -16.889 25.146  -17.452  1.00 32.84  ?  404 GLN B N   1 
ATOM   7427 C  CA  . GLN B 1 406 ? -18.111 25.225  -18.228  1.00 33.85  ?  404 GLN B CA  1 
ATOM   7428 C  C   . GLN B 1 406 ? -18.251 23.944  -19.058  1.00 36.11  ?  404 GLN B C   1 
ATOM   7429 O  O   . GLN B 1 406 ? -17.505 22.976  -18.876  1.00 37.27  ?  404 GLN B O   1 
ATOM   7430 C  CB  . GLN B 1 406 ? -18.120 26.525  -19.031  1.00 36.77  ?  404 GLN B CB  1 
ATOM   7431 C  CG  . GLN B 1 406 ? -18.255 27.731  -18.098  1.00 37.61  ?  404 GLN B CG  1 
ATOM   7432 C  CD  . GLN B 1 406 ? -18.449 29.052  -18.812  1.00 43.18  ?  404 GLN B CD  1 
ATOM   7433 O  OE1 . GLN B 1 406 ? -17.671 29.991  -18.628  1.00 41.69  ?  404 GLN B OE1 1 
ATOM   7434 N  NE2 . GLN B 1 406 ? -19.514 29.148  -19.597  1.00 40.80  ?  404 GLN B NE2 1 
ATOM   7435 N  N   . LEU B 1 407 ? -19.191 23.942  -19.995  1.00 36.07  ?  405 LEU B N   1 
ATOM   7436 C  CA  . LEU B 1 407 ? -19.563 22.726  -20.709  1.00 35.18  ?  405 LEU B CA  1 
ATOM   7437 C  C   . LEU B 1 407 ? -18.591 22.390  -21.840  1.00 47.16  ?  405 LEU B C   1 
ATOM   7438 O  O   . LEU B 1 407 ? -18.070 23.288  -22.508  1.00 43.40  ?  405 LEU B O   1 
ATOM   7439 C  CB  . LEU B 1 407 ? -20.971 22.860  -21.271  1.00 33.85  ?  405 LEU B CB  1 
ATOM   7440 C  CG  . LEU B 1 407 ? -22.024 22.896  -20.166  1.00 42.74  ?  405 LEU B CG  1 
ATOM   7441 C  CD1 . LEU B 1 407 ? -23.391 23.230  -20.729  1.00 39.31  ?  405 LEU B CD1 1 
ATOM   7442 C  CD2 . LEU B 1 407 ? -22.042 21.570  -19.419  1.00 40.57  ?  405 LEU B CD2 1 
ATOM   7443 N  N   . PRO B 1 408 ? -18.340 21.103  -22.064  1.00 41.78  ?  406 PRO B N   1 
ATOM   7444 C  CA  . PRO B 1 408 ? -17.530 20.660  -23.197  1.00 43.65  ?  406 PRO B CA  1 
ATOM   7445 C  C   . PRO B 1 408 ? -18.417 20.361  -24.402  1.00 43.00  ?  406 PRO B C   1 
ATOM   7446 O  O   . PRO B 1 408 ? -19.646 20.389  -24.327  1.00 45.67  ?  406 PRO B O   1 
ATOM   7447 C  CB  . PRO B 1 408 ? -16.901 19.374  -22.660  1.00 46.00  ?  406 PRO B CB  1 
ATOM   7448 C  CG  . PRO B 1 408 ? -18.052 18.774  -21.886  1.00 43.96  ?  406 PRO B CG  1 
ATOM   7449 C  CD  . PRO B 1 408 ? -18.747 19.964  -21.221  1.00 40.16  ?  406 PRO B CD  1 
ATOM   7450 N  N   . ALA B 1 409 ? -17.765 20.055  -25.517  1.00 47.80  ?  407 ALA B N   1 
ATOM   7451 C  CA  . ALA B 1 409 ? -18.505 19.617  -26.689  1.00 49.87  ?  407 ALA B CA  1 
ATOM   7452 C  C   . ALA B 1 409 ? -19.250 18.320  -26.380  1.00 44.75  ?  407 ALA B C   1 
ATOM   7453 O  O   . ALA B 1 409 ? -18.733 17.464  -25.653  1.00 45.91  ?  407 ALA B O   1 
ATOM   7454 C  CB  . ALA B 1 409 ? -17.565 19.410  -27.878  1.00 48.90  ?  407 ALA B CB  1 
ATOM   7455 N  N   . PRO B 1 410 ? -20.465 18.150  -26.899  1.00 46.56  ?  408 PRO B N   1 
ATOM   7456 C  CA  . PRO B 1 410 ? -21.189 16.891  -26.700  1.00 51.65  ?  408 PRO B CA  1 
ATOM   7457 C  C   . PRO B 1 410 ? -20.437 15.705  -27.284  1.00 57.78  ?  408 PRO B C   1 
ATOM   7458 O  O   . PRO B 1 410 ? -19.909 15.768  -28.397  1.00 55.42  ?  408 PRO B O   1 
ATOM   7459 C  CB  . PRO B 1 410 ? -22.513 17.130  -27.436  1.00 49.42  ?  408 PRO B CB  1 
ATOM   7460 C  CG  . PRO B 1 410 ? -22.162 18.171  -28.462  1.00 56.49  ?  408 PRO B CG  1 
ATOM   7461 C  CD  . PRO B 1 410 ? -21.255 19.094  -27.705  1.00 50.52  ?  408 PRO B CD  1 
ATOM   7462 N  N   . ARG B 1 411 ? -20.379 14.621  -26.518  1.00 52.58  ?  409 ARG B N   1 
ATOM   7463 C  CA  . ARG B 1 411 ? -19.829 13.352  -26.989  1.00 54.05  ?  409 ARG B CA  1 
ATOM   7464 C  C   . ARG B 1 411 ? -21.021 12.423  -27.200  1.00 53.91  ?  409 ARG B C   1 
ATOM   7465 O  O   . ARG B 1 411 ? -21.490 11.759  -26.274  1.00 53.83  ?  409 ARG B O   1 
ATOM   7466 C  CB  . ARG B 1 411 ? -18.808 12.778  -26.013  1.00 61.43  ?  409 ARG B CB  1 
ATOM   7467 C  CG  . ARG B 1 411 ? -17.378 13.154  -26.355  1.00 48.53  ?  409 ARG B CG  1 
ATOM   7468 C  CD  . ARG B 1 411 ? -17.067 14.580  -25.964  1.00 54.79  ?  409 ARG B CD  1 
ATOM   7469 N  NE  . ARG B 1 411 ? -15.631 14.801  -25.848  1.00 48.35  ?  409 ARG B NE  1 
ATOM   7470 C  CZ  . ARG B 1 411 ? -15.077 15.940  -25.457  1.00 45.14  ?  409 ARG B CZ  1 
ATOM   7471 N  NH1 . ARG B 1 411 ? -15.795 17.039  -25.294  1.00 53.81  ?  409 ARG B NH1 1 
ATOM   7472 N  NH2 . ARG B 1 411 ? -13.761 15.990  -25.275  1.00 44.64  ?  409 ARG B NH2 1 
ATOM   7473 N  N   . THR B 1 412 ? -21.504 12.388  -28.447  1.00 53.70  ?  410 THR B N   1 
ATOM   7474 C  CA  . THR B 1 412 ? -22.720 11.660  -28.794  1.00 50.92  ?  410 THR B CA  1 
ATOM   7475 C  C   . THR B 1 412 ? -22.642 10.176  -28.467  1.00 49.46  ?  410 THR B C   1 
ATOM   7476 O  O   . THR B 1 412 ? -23.686 9.528   -28.345  1.00 54.35  ?  410 THR B O   1 
ATOM   7477 C  CB  . THR B 1 412 ? -23.024 11.841  -30.283  1.00 63.30  ?  410 THR B CB  1 
ATOM   7478 O  OG1 . THR B 1 412 ? -21.876 11.461  -31.053  1.00 65.87  ?  410 THR B OG1 1 
ATOM   7479 C  CG2 . THR B 1 412 ? -23.364 13.293  -30.583  1.00 66.15  ?  410 THR B CG2 1 
ATOM   7480 N  N   . LEU B 1 413 ? -21.439 9.623   -28.319  1.00 51.33  ?  411 LEU B N   1 
ATOM   7481 C  CA  . LEU B 1 413 ? -21.279 8.191   -28.112  1.00 48.21  ?  411 LEU B CA  1 
ATOM   7482 C  C   . LEU B 1 413 ? -21.070 7.828   -26.654  1.00 47.88  ?  411 LEU B C   1 
ATOM   7483 O  O   . LEU B 1 413 ? -21.304 6.675   -26.277  1.00 52.92  ?  411 LEU B O   1 
ATOM   7484 C  CB  . LEU B 1 413 ? -20.091 7.661   -28.925  1.00 52.99  ?  411 LEU B CB  1 
ATOM   7485 C  CG  . LEU B 1 413 ? -20.090 7.924   -30.429  1.00 52.80  ?  411 LEU B CG  1 
ATOM   7486 C  CD1 . LEU B 1 413 ? -18.865 7.293   -31.070  1.00 52.47  ?  411 LEU B CD1 1 
ATOM   7487 C  CD2 . LEU B 1 413 ? -21.362 7.381   -31.055  1.00 51.20  ?  411 LEU B CD2 1 
ATOM   7488 N  N   . LEU B 1 414 ? -20.623 8.776   -25.838  1.00 47.26  ?  412 LEU B N   1 
ATOM   7489 C  CA  . LEU B 1 414 ? -20.367 8.525   -24.427  1.00 49.22  ?  412 LEU B CA  1 
ATOM   7490 C  C   . LEU B 1 414 ? -21.692 8.469   -23.677  1.00 54.76  ?  412 LEU B C   1 
ATOM   7491 O  O   . LEU B 1 414 ? -22.387 9.482   -23.544  1.00 57.47  ?  412 LEU B O   1 
ATOM   7492 C  CB  . LEU B 1 414 ? -19.455 9.604   -23.856  1.00 53.73  ?  412 LEU B CB  1 
ATOM   7493 C  CG  . LEU B 1 414 ? -19.374 9.679   -22.332  1.00 51.85  ?  412 LEU B CG  1 
ATOM   7494 C  CD1 . LEU B 1 414 ? -18.757 8.417   -21.751  1.00 43.45  ?  412 LEU B CD1 1 
ATOM   7495 C  CD2 . LEU B 1 414 ? -18.577 10.909  -21.930  1.00 47.19  ?  412 LEU B CD2 1 
ATOM   7496 N  N   . THR B 1 415 ? -22.035 7.283   -23.180  1.00 50.45  ?  413 THR B N   1 
ATOM   7497 C  CA  . THR B 1 415 ? -23.280 7.057   -22.464  1.00 57.62  ?  413 THR B CA  1 
ATOM   7498 C  C   . THR B 1 415 ? -23.057 6.562   -21.046  1.00 63.14  ?  413 THR B C   1 
ATOM   7499 O  O   . THR B 1 415 ? -23.972 6.668   -20.222  1.00 72.79  ?  413 THR B O   1 
ATOM   7500 C  CB  . THR B 1 415 ? -24.170 6.050   -23.211  1.00 58.31  ?  413 THR B CB  1 
ATOM   7501 O  OG1 . THR B 1 415 ? -23.447 4.832   -23.433  1.00 58.42  ?  413 THR B OG1 1 
ATOM   7502 C  CG2 . THR B 1 415 ? -24.607 6.626   -24.551  1.00 57.71  ?  413 THR B CG2 1 
ATOM   7503 N  N   . LYS B 1 416 ? -21.876 6.028   -20.743  1.00 58.86  ?  414 LYS B N   1 
ATOM   7504 C  CA  . LYS B 1 416 ? -21.565 5.426   -19.453  1.00 52.81  ?  414 LYS B CA  1 
ATOM   7505 C  C   . LYS B 1 416 ? -20.369 6.174   -18.883  1.00 60.17  ?  414 LYS B C   1 
ATOM   7506 O  O   . LYS B 1 416 ? -19.267 6.105   -19.438  1.00 64.16  ?  414 LYS B O   1 
ATOM   7507 C  CB  . LYS B 1 416 ? -21.254 3.941   -19.610  1.00 56.76  ?  414 LYS B CB  1 
ATOM   7508 C  CG  . LYS B 1 416 ? -22.206 3.209   -20.539  1.00 57.32  ?  414 LYS B CG  1 
ATOM   7509 C  CD  . LYS B 1 416 ? -21.688 1.821   -20.870  1.00 60.18  ?  414 LYS B CD  1 
ATOM   7510 C  CE  . LYS B 1 416 ? -22.269 1.318   -22.180  1.00 66.42  ?  414 LYS B CE  1 
ATOM   7511 N  NZ  . LYS B 1 416 ? -21.583 0.086   -22.656  1.00 73.53  ?  414 LYS B NZ  1 
ATOM   7512 N  N   . GLY B 1 417 ? -20.577 6.881   -17.784  1.00 55.81  ?  415 GLY B N   1 
ATOM   7513 C  CA  . GLY B 1 417 ? -19.479 7.562   -17.138  1.00 52.25  ?  415 GLY B CA  1 
ATOM   7514 C  C   . GLY B 1 417 ? -19.580 9.071   -17.298  1.00 54.89  ?  415 GLY B C   1 
ATOM   7515 O  O   . GLY B 1 417 ? -20.296 9.595   -18.156  1.00 65.84  ?  415 GLY B O   1 
ATOM   7516 N  N   . THR B 1 418 ? -18.838 9.774   -16.450  1.00 54.91  ?  416 THR B N   1 
ATOM   7517 C  CA  . THR B 1 418 ? -18.738 11.225  -16.508  1.00 47.20  ?  416 THR B CA  1 
ATOM   7518 C  C   . THR B 1 418 ? -17.334 11.609  -16.951  1.00 53.38  ?  416 THR B C   1 
ATOM   7519 O  O   . THR B 1 418 ? -16.347 11.079  -16.431  1.00 56.07  ?  416 THR B O   1 
ATOM   7520 C  CB  . THR B 1 418 ? -19.056 11.859  -15.153  1.00 51.82  ?  416 THR B CB  1 
ATOM   7521 O  OG1 . THR B 1 418 ? -20.439 11.650  -14.843  1.00 63.87  ?  416 THR B OG1 1 
ATOM   7522 C  CG2 . THR B 1 418 ? -18.772 13.352  -15.191  1.00 54.44  ?  416 THR B CG2 1 
ATOM   7523 N  N   . LEU B 1 419 ? -17.254 12.512  -17.925  1.00 47.36  ?  417 LEU B N   1 
ATOM   7524 C  CA  . LEU B 1 419 ? -15.982 13.020  -18.429  1.00 47.51  ?  417 LEU B CA  1 
ATOM   7525 C  C   . LEU B 1 419 ? -15.582 14.248  -17.614  1.00 49.76  ?  417 LEU B C   1 
ATOM   7526 O  O   . LEU B 1 419 ? -16.242 15.290  -17.684  1.00 48.51  ?  417 LEU B O   1 
ATOM   7527 C  CB  . LEU B 1 419 ? -16.105 13.348  -19.915  1.00 42.66  ?  417 LEU B CB  1 
ATOM   7528 C  CG  . LEU B 1 419 ? -14.840 13.767  -20.657  1.00 57.68  ?  417 LEU B CG  1 
ATOM   7529 C  CD1 . LEU B 1 419 ? -13.889 12.587  -20.752  1.00 53.07  ?  417 LEU B CD1 1 
ATOM   7530 C  CD2 . LEU B 1 419 ? -15.186 14.293  -22.040  1.00 49.54  ?  417 LEU B CD2 1 
ATOM   7531 N  N   . GLU B 1 420 ? -14.499 14.127  -16.846  1.00 48.85  ?  418 GLU B N   1 
ATOM   7532 C  CA  . GLU B 1 420 ? -14.032 15.236  -16.028  1.00 43.30  ?  418 GLU B CA  1 
ATOM   7533 C  C   . GLU B 1 420 ? -13.354 16.311  -16.879  1.00 44.29  ?  418 GLU B C   1 
ATOM   7534 O  O   . GLU B 1 420 ? -12.825 16.024  -17.957  1.00 40.09  ?  418 GLU B O   1 
ATOM   7535 C  CB  . GLU B 1 420 ? -13.064 14.739  -14.959  1.00 47.51  ?  418 GLU B CB  1 
ATOM   7536 C  CG  . GLU B 1 420 ? -13.757 14.065  -13.790  1.00 60.54  ?  418 GLU B CG  1 
ATOM   7537 C  CD  . GLU B 1 420 ? -14.684 15.010  -13.050  1.00 67.59  ?  418 GLU B CD  1 
ATOM   7538 O  OE1 . GLU B 1 420 ? -14.196 16.035  -12.523  1.00 69.60  ?  418 GLU B OE1 1 
ATOM   7539 O  OE2 . GLU B 1 420 ? -15.901 14.733  -13.005  1.00 70.35  -1 418 GLU B OE2 1 
ATOM   7540 N  N   . PRO B 1 421 ? -13.351 17.561  -16.405  1.00 43.65  ?  419 PRO B N   1 
ATOM   7541 C  CA  . PRO B 1 421 ? -12.786 18.656  -17.214  1.00 31.49  ?  419 PRO B CA  1 
ATOM   7542 C  C   . PRO B 1 421 ? -11.330 18.456  -17.606  1.00 38.73  ?  419 PRO B C   1 
ATOM   7543 O  O   . PRO B 1 421 ? -10.922 18.911  -18.682  1.00 35.29  ?  419 PRO B O   1 
ATOM   7544 C  CB  . PRO B 1 421 ? -12.962 19.871  -16.292  1.00 34.46  ?  419 PRO B CB  1 
ATOM   7545 C  CG  . PRO B 1 421 ? -14.175 19.504  -15.475  1.00 36.99  ?  419 PRO B CG  1 
ATOM   7546 C  CD  . PRO B 1 421 ? -13.893 18.069  -15.133  1.00 41.12  ?  419 PRO B CD  1 
ATOM   7547 N  N   . GLU B 1 422 ? -10.535 17.777  -16.780  1.00 39.27  ?  420 GLU B N   1 
ATOM   7548 C  CA  . GLU B 1 422 ? -9.137  17.534  -17.119  1.00 42.07  ?  420 GLU B CA  1 
ATOM   7549 C  C   . GLU B 1 422 ? -8.981  16.607  -18.315  1.00 43.44  ?  420 GLU B C   1 
ATOM   7550 O  O   . GLU B 1 422 ? -7.851  16.374  -18.759  1.00 46.71  ?  420 GLU B O   1 
ATOM   7551 C  CB  . GLU B 1 422 ? -8.392  16.979  -15.901  1.00 37.18  ?  420 GLU B CB  1 
ATOM   7552 C  CG  . GLU B 1 422 ? -8.718  15.541  -15.558  1.00 48.66  ?  420 GLU B CG  1 
ATOM   7553 C  CD  . GLU B 1 422 ? -7.779  14.973  -14.510  1.00 60.79  ?  420 GLU B CD  1 
ATOM   7554 O  OE1 . GLU B 1 422 ? -6.562  14.877  -14.780  1.00 48.43  ?  420 GLU B OE1 1 
ATOM   7555 O  OE2 . GLU B 1 422 ? -8.260  14.631  -13.409  1.00 72.21  -1 420 GLU B OE2 1 
ATOM   7556 N  N   . TYR B 1 423 ? -10.089 16.101  -18.854  1.00 35.51  ?  421 TYR B N   1 
ATOM   7557 C  CA  . TYR B 1 423 ? -10.088 15.145  -19.952  1.00 35.74  ?  421 TYR B CA  1 
ATOM   7558 C  C   . TYR B 1 423 ? -10.838 15.678  -21.167  1.00 40.67  ?  421 TYR B C   1 
ATOM   7559 O  O   . TYR B 1 423 ? -11.035 14.933  -22.132  1.00 42.25  ?  421 TYR B O   1 
ATOM   7560 C  CB  . TYR B 1 423 ? -10.700 13.813  -19.500  1.00 38.72  ?  421 TYR B CB  1 
ATOM   7561 C  CG  . TYR B 1 423 ? -9.974  13.140  -18.352  1.00 43.84  ?  421 TYR B CG  1 
ATOM   7562 C  CD1 . TYR B 1 423 ? -8.601  12.935  -18.394  1.00 39.46  ?  421 TYR B CD1 1 
ATOM   7563 C  CD2 . TYR B 1 423 ? -10.664 12.717  -17.221  1.00 49.51  ?  421 TYR B CD2 1 
ATOM   7564 C  CE1 . TYR B 1 423 ? -7.936  12.320  -17.349  1.00 43.90  ?  421 TYR B CE1 1 
ATOM   7565 C  CE2 . TYR B 1 423 ? -10.006 12.103  -16.170  1.00 43.15  ?  421 TYR B CE2 1 
ATOM   7566 C  CZ  . TYR B 1 423 ? -8.643  11.907  -16.238  1.00 42.18  ?  421 TYR B CZ  1 
ATOM   7567 O  OH  . TYR B 1 423 ? -7.984  11.298  -15.194  1.00 52.36  ?  421 TYR B OH  1 
ATOM   7568 N  N   . PHE B 1 424 ? -11.267 16.948  -21.141  1.00 43.22  ?  422 PHE B N   1 
ATOM   7569 C  CA  . PHE B 1 424 ? -11.975 17.524  -22.282  1.00 35.21  ?  422 PHE B CA  1 
ATOM   7570 C  C   . PHE B 1 424 ? -11.062 17.617  -23.498  1.00 31.25  ?  422 PHE B C   1 
ATOM   7571 O  O   . PHE B 1 424 ? -11.452 17.248  -24.611  1.00 40.92  ?  422 PHE B O   1 
ATOM   7572 C  CB  . PHE B 1 424 ? -12.515 18.919  -21.942  1.00 36.80  ?  422 PHE B CB  1 
ATOM   7573 C  CG  . PHE B 1 424 ? -13.631 18.933  -20.934  1.00 39.03  ?  422 PHE B CG  1 
ATOM   7574 C  CD1 . PHE B 1 424 ? -14.205 17.760  -20.475  1.00 37.07  ?  422 PHE B CD1 1 
ATOM   7575 C  CD2 . PHE B 1 424 ? -14.129 20.141  -20.468  1.00 44.31  ?  422 PHE B CD2 1 
ATOM   7576 C  CE1 . PHE B 1 424 ? -15.237 17.792  -19.552  1.00 38.50  ?  422 PHE B CE1 1 
ATOM   7577 C  CE2 . PHE B 1 424 ? -15.165 20.181  -19.550  1.00 34.01  ?  422 PHE B CE2 1 
ATOM   7578 C  CZ  . PHE B 1 424 ? -15.719 19.004  -19.092  1.00 37.80  ?  422 PHE B CZ  1 
ATOM   7579 N  N   . ASN B 1 425 ? -9.854  18.144  -23.307  1.00 33.45  ?  423 ASN B N   1 
ATOM   7580 C  CA  . ASN B 1 425 ? -8.843  18.250  -24.353  1.00 33.81  ?  423 ASN B CA  1 
ATOM   7581 C  C   . ASN B 1 425 ? -7.505  18.539  -23.679  1.00 34.97  ?  423 ASN B C   1 
ATOM   7582 O  O   . ASN B 1 425 ? -7.429  18.702  -22.458  1.00 37.40  ?  423 ASN B O   1 
ATOM   7583 C  CB  . ASN B 1 425 ? -9.213  19.315  -25.391  1.00 32.44  ?  423 ASN B CB  1 
ATOM   7584 C  CG  . ASN B 1 425 ? -9.384  20.692  -24.782  1.00 32.95  ?  423 ASN B CG  1 
ATOM   7585 O  OD1 . ASN B 1 425 ? -8.447  21.251  -24.213  1.00 35.34  ?  423 ASN B OD1 1 
ATOM   7586 N  ND2 . ASN B 1 425 ? -10.582 21.254  -24.913  1.00 34.14  ?  423 ASN B ND2 1 
ATOM   7587 N  N   . SER B 1 426 ? -6.445  18.623  -24.488  1.00 34.05  ?  424 SER B N   1 
ATOM   7588 C  CA  . SER B 1 426 ? -5.109  18.835  -23.934  1.00 35.71  ?  424 SER B CA  1 
ATOM   7589 C  C   . SER B 1 426 ? -5.000  20.164  -23.195  1.00 32.75  ?  424 SER B C   1 
ATOM   7590 O  O   . SER B 1 426 ? -4.327  20.249  -22.161  1.00 35.30  ?  424 SER B O   1 
ATOM   7591 C  CB  . SER B 1 426 ? -4.054  18.759  -25.040  1.00 34.36  ?  424 SER B CB  1 
ATOM   7592 O  OG  . SER B 1 426 ? -4.066  17.495  -25.677  1.00 35.70  ?  424 SER B OG  1 
ATOM   7593 N  N   . VAL B 1 427 ? -5.638  21.216  -23.709  1.00 29.30  ?  425 VAL B N   1 
ATOM   7594 C  CA  . VAL B 1 427 ? -5.511  22.516  -23.058  1.00 28.35  ?  425 VAL B CA  1 
ATOM   7595 C  C   . VAL B 1 427 ? -6.220  22.505  -21.710  1.00 36.79  ?  425 VAL B C   1 
ATOM   7596 O  O   . VAL B 1 427 ? -5.695  23.014  -20.713  1.00 36.73  ?  425 VAL B O   1 
ATOM   7597 C  CB  . VAL B 1 427 ? -6.039  23.631  -23.979  1.00 35.63  ?  425 VAL B CB  1 
ATOM   7598 C  CG1 . VAL B 1 427 ? -6.126  24.948  -23.226  1.00 34.80  ?  425 VAL B CG1 1 
ATOM   7599 C  CG2 . VAL B 1 427 ? -5.135  23.776  -25.194  1.00 34.10  ?  425 VAL B CG2 1 
ATOM   7600 N  N   . CYS B 1 428 ? -7.408  21.900  -21.645  1.00 35.84  ?  426 CYS B N   1 
ATOM   7601 C  CA  . CYS B 1 428 ? -8.107  21.836  -20.368  1.00 40.19  ?  426 CYS B CA  1 
ATOM   7602 C  C   . CYS B 1 428 ? -7.352  20.961  -19.380  1.00 36.41  ?  426 CYS B C   1 
ATOM   7603 O  O   . CYS B 1 428 ? -7.344  21.248  -18.178  1.00 37.47  ?  426 CYS B O   1 
ATOM   7604 C  CB  . CYS B 1 428 ? -9.538  21.339  -20.564  1.00 40.78  ?  426 CYS B CB  1 
ATOM   7605 S  SG  . CYS B 1 428 ? -10.599 22.533  -21.420  1.00 57.94  ?  426 CYS B SG  1 
ATOM   7606 N  N   . ARG B 1 429 ? -6.709  19.897  -19.862  1.00 33.46  ?  427 ARG B N   1 
ATOM   7607 C  CA  . ARG B 1 429 ? -5.877  19.091  -18.978  1.00 36.14  ?  427 ARG B CA  1 
ATOM   7608 C  C   . ARG B 1 429 ? -4.816  19.958  -18.309  1.00 35.55  ?  427 ARG B C   1 
ATOM   7609 O  O   . ARG B 1 429 ? -4.637  19.906  -17.087  1.00 36.94  ?  427 ARG B O   1 
ATOM   7610 C  CB  . ARG B 1 429 ? -5.243  17.936  -19.751  1.00 34.97  ?  427 ARG B CB  1 
ATOM   7611 C  CG  . ARG B 1 429 ? -4.451  16.985  -18.874  1.00 36.92  ?  427 ARG B CG  1 
ATOM   7612 C  CD  . ARG B 1 429 ? -4.272  15.633  -19.541  1.00 42.68  ?  427 ARG B CD  1 
ATOM   7613 N  NE  . ARG B 1 429 ? -3.520  14.706  -18.704  1.00 53.35  ?  427 ARG B NE  1 
ATOM   7614 C  CZ  . ARG B 1 429 ? -3.918  14.277  -17.513  1.00 61.04  ?  427 ARG B CZ  1 
ATOM   7615 N  NH1 . ARG B 1 429 ? -5.142  14.513  -17.066  1.00 55.37  ?  427 ARG B NH1 1 
ATOM   7616 N  NH2 . ARG B 1 429 ? -3.091  13.535  -16.782  1.00 59.52  ?  427 ARG B NH2 1 
ATOM   7617 N  N   . LEU B 1 430 ? -4.096  20.761  -19.099  1.00 34.68  ?  428 LEU B N   1 
ATOM   7618 C  CA  . LEU B 1 430 ? -3.081  21.641  -18.527  1.00 35.24  ?  428 LEU B CA  1 
ATOM   7619 C  C   . LEU B 1 430 ? -3.688  22.569  -17.485  1.00 37.39  ?  428 LEU B C   1 
ATOM   7620 O  O   . LEU B 1 430 ? -3.169  22.699  -16.370  1.00 36.82  ?  428 LEU B O   1 
ATOM   7621 C  CB  . LEU B 1 430 ? -2.411  22.464  -19.627  1.00 41.04  ?  428 LEU B CB  1 
ATOM   7622 C  CG  . LEU B 1 430 ? -1.351  21.813  -20.508  1.00 42.26  ?  428 LEU B CG  1 
ATOM   7623 C  CD1 . LEU B 1 430 ? -0.822  22.834  -21.497  1.00 51.71  ?  428 LEU B CD1 1 
ATOM   7624 C  CD2 . LEU B 1 430 ? -0.222  21.268  -19.651  1.00 49.50  ?  428 LEU B CD2 1 
ATOM   7625 N  N   . MET B 1 431 ? -4.801  23.218  -17.830  1.00 36.13  ?  429 MET B N   1 
ATOM   7626 C  CA  . MET B 1 431 ? -5.397  24.192  -16.925  1.00 36.68  ?  429 MET B CA  1 
ATOM   7627 C  C   . MET B 1 431 ? -5.833  23.545  -15.618  1.00 35.50  ?  429 MET B C   1 
ATOM   7628 O  O   . MET B 1 431 ? -5.860  24.210  -14.576  1.00 43.75  ?  429 MET B O   1 
ATOM   7629 C  CB  . MET B 1 431 ? -6.573  24.885  -17.613  1.00 40.29  ?  429 MET B CB  1 
ATOM   7630 C  CG  . MET B 1 431 ? -6.179  25.590  -18.903  1.00 35.24  ?  429 MET B CG  1 
ATOM   7631 S  SD  . MET B 1 431 ? -7.568  26.354  -19.755  1.00 46.49  ?  429 MET B SD  1 
ATOM   7632 C  CE  . MET B 1 431 ? -7.855  27.776  -18.711  1.00 45.18  ?  429 MET B CE  1 
ATOM   7633 N  N   . LYS B 1 432 ? -6.162  22.256  -15.645  1.00 38.77  ?  430 LYS B N   1 
ATOM   7634 C  CA  . LYS B 1 432 ? -6.619  21.578  -14.441  1.00 39.65  ?  430 LYS B CA  1 
ATOM   7635 C  C   . LYS B 1 432 ? -5.486  20.915  -13.668  1.00 45.16  ?  430 LYS B C   1 
ATOM   7636 O  O   . LYS B 1 432 ? -5.641  20.656  -12.468  1.00 43.76  ?  430 LYS B O   1 
ATOM   7637 C  CB  . LYS B 1 432 ? -7.686  20.537  -14.795  1.00 35.82  ?  430 LYS B CB  1 
ATOM   7638 C  CG  . LYS B 1 432 ? -8.975  21.153  -15.315  1.00 33.61  ?  430 LYS B CG  1 
ATOM   7639 C  CD  . LYS B 1 432 ? -9.754  21.875  -14.219  1.00 34.84  ?  430 LYS B CD  1 
ATOM   7640 C  CE  . LYS B 1 432 ? -10.223 20.925  -13.130  1.00 40.39  ?  430 LYS B CE  1 
ATOM   7641 N  NZ  . LYS B 1 432 ? -11.056 21.626  -12.112  1.00 39.47  ?  430 LYS B NZ  1 
ATOM   7642 N  N   . THR B 1 433 ? -4.354  20.637  -14.318  1.00 39.97  ?  431 THR B N   1 
ATOM   7643 C  CA  . THR B 1 433 ? -3.229  19.969  -13.669  1.00 44.21  ?  431 THR B CA  1 
ATOM   7644 C  C   . THR B 1 433 ? -2.185  20.983  -13.211  1.00 43.33  ?  431 THR B C   1 
ATOM   7645 O  O   . THR B 1 433 ? -1.889  21.076  -12.017  1.00 53.23  ?  431 THR B O   1 
ATOM   7646 C  CB  . THR B 1 433 ? -2.603  18.920  -14.601  1.00 42.96  ?  431 THR B CB  1 
ATOM   7647 O  OG1 . THR B 1 433 ? -2.197  19.535  -15.829  1.00 44.98  ?  431 THR B OG1 1 
ATOM   7648 C  CG2 . THR B 1 433 ? -3.602  17.811  -14.899  1.00 43.17  ?  431 THR B CG2 1 
ATOM   7649 N  N   . ILE B 1 434 ? -1.612  21.745  -14.148  1.00 42.75  ?  432 ILE B N   1 
ATOM   7650 C  CA  . ILE B 1 434 ? -0.602  22.743  -13.800  1.00 45.07  ?  432 ILE B CA  1 
ATOM   7651 C  C   . ILE B 1 434 ? -1.225  24.103  -13.520  1.00 43.54  ?  432 ILE B C   1 
ATOM   7652 O  O   . ILE B 1 434 ? -0.538  24.992  -12.994  1.00 44.03  ?  432 ILE B O   1 
ATOM   7653 C  CB  . ILE B 1 434 ? 0.473   22.890  -14.896  1.00 47.38  ?  432 ILE B CB  1 
ATOM   7654 C  CG1 . ILE B 1 434 ? -0.078  23.647  -16.104  1.00 40.12  ?  432 ILE B CG1 1 
ATOM   7655 C  CG2 . ILE B 1 434 ? 1.005   21.526  -15.311  1.00 55.10  ?  432 ILE B CG2 1 
ATOM   7656 C  CD1 . ILE B 1 434 ? 0.970   23.954  -17.149  1.00 52.19  ?  432 ILE B CD1 1 
ATOM   7657 N  N   . GLY B 1 435 ? -2.498  24.296  -13.860  1.00 41.84  ?  433 GLY B N   1 
ATOM   7658 C  CA  . GLY B 1 435 ? -3.181  25.551  -13.657  1.00 36.65  ?  433 GLY B CA  1 
ATOM   7659 C  C   . GLY B 1 435 ? -3.180  26.448  -14.878  1.00 38.71  ?  433 GLY B C   1 
ATOM   7660 O  O   . GLY B 1 435 ? -2.387  26.280  -15.808  1.00 34.82  ?  433 GLY B O   1 
ATOM   7661 N  N   . PRO B 1 436 ? -4.087  27.423  -14.895  1.00 37.63  ?  434 PRO B N   1 
ATOM   7662 C  CA  . PRO B 1 436 ? -4.104  28.406  -15.983  1.00 37.28  ?  434 PRO B CA  1 
ATOM   7663 C  C   . PRO B 1 436 ? -2.984  29.424  -15.842  1.00 40.04  ?  434 PRO B C   1 
ATOM   7664 O  O   . PRO B 1 436 ? -2.640  29.852  -14.737  1.00 39.46  ?  434 PRO B O   1 
ATOM   7665 C  CB  . PRO B 1 436 ? -5.475  29.075  -15.823  1.00 38.04  ?  434 PRO B CB  1 
ATOM   7666 C  CG  . PRO B 1 436 ? -5.726  28.991  -14.349  1.00 43.59  ?  434 PRO B CG  1 
ATOM   7667 C  CD  . PRO B 1 436 ? -5.191  27.639  -13.944  1.00 39.36  ?  434 PRO B CD  1 
ATOM   7668 N  N   . ASP B 1 437 ? -2.406  29.809  -16.980  1.00 37.81  ?  435 ASP B N   1 
ATOM   7669 C  CA  . ASP B 1 437 ? -1.410  30.873  -16.958  1.00 38.29  ?  435 ASP B CA  1 
ATOM   7670 C  C   . ASP B 1 437 ? -2.025  32.185  -16.484  1.00 42.16  ?  435 ASP B C   1 
ATOM   7671 O  O   . ASP B 1 437 ? -1.396  32.942  -15.734  1.00 43.95  ?  435 ASP B O   1 
ATOM   7672 C  CB  . ASP B 1 437 ? -0.796  31.051  -18.347  1.00 44.18  ?  435 ASP B CB  1 
ATOM   7673 C  CG  . ASP B 1 437 ? 0.003   29.845  -18.791  1.00 46.99  ?  435 ASP B CG  1 
ATOM   7674 O  OD1 . ASP B 1 437 ? 0.983   29.492  -18.102  1.00 56.94  ?  435 ASP B OD1 1 
ATOM   7675 O  OD2 . ASP B 1 437 ? -0.349  29.251  -19.833  1.00 48.73  -1 435 ASP B OD2 1 
ATOM   7676 N  N   . MET B 1 438 ? -3.257  32.467  -16.908  1.00 41.01  ?  436 MET B N   1 
ATOM   7677 C  CA  . MET B 1 438 ? -3.931  33.721  -16.606  1.00 35.01  ?  436 MET B CA  1 
ATOM   7678 C  C   . MET B 1 438 ? -5.355  33.449  -16.143  1.00 37.70  ?  436 MET B C   1 
ATOM   7679 O  O   . MET B 1 438 ? -6.005  32.506  -16.603  1.00 37.03  ?  436 MET B O   1 
ATOM   7680 C  CB  . MET B 1 438 ? -3.933  34.636  -17.832  1.00 30.96  ?  436 MET B CB  1 
ATOM   7681 C  CG  . MET B 1 438 ? -2.531  35.013  -18.288  1.00 41.67  ?  436 MET B CG  1 
ATOM   7682 S  SD  . MET B 1 438 ? -2.492  35.708  -19.944  1.00 41.17  ?  436 MET B SD  1 
ATOM   7683 C  CE  . MET B 1 438 ? -3.010  34.298  -20.923  1.00 38.72  ?  436 MET B CE  1 
ATOM   7684 N  N   . PHE B 1 439 ? -5.844  34.296  -15.241  1.00 32.91  ?  437 PHE B N   1 
ATOM   7685 C  CA  . PHE B 1 439 ? -7.169  34.112  -14.666  1.00 35.46  ?  437 PHE B CA  1 
ATOM   7686 C  C   . PHE B 1 439 ? -7.873  35.457  -14.585  1.00 38.18  ?  437 PHE B C   1 
ATOM   7687 O  O   . PHE B 1 439 ? -7.308  36.427  -14.073  1.00 39.07  ?  437 PHE B O   1 
ATOM   7688 C  CB  . PHE B 1 439 ? -7.054  33.473  -13.274  1.00 36.82  ?  437 PHE B CB  1 
ATOM   7689 C  CG  . PHE B 1 439 ? -8.367  33.051  -12.672  1.00 41.79  ?  437 PHE B CG  1 
ATOM   7690 C  CD1 . PHE B 1 439 ? -8.939  31.835  -13.006  1.00 43.04  ?  437 PHE B CD1 1 
ATOM   7691 C  CD2 . PHE B 1 439 ? -9.007  33.851  -11.740  1.00 44.14  ?  437 PHE B CD2 1 
ATOM   7692 C  CE1 . PHE B 1 439 ? -10.138 31.437  -12.441  1.00 39.81  ?  437 PHE B CE1 1 
ATOM   7693 C  CE2 . PHE B 1 439 ? -10.206 33.458  -11.173  1.00 39.52  ?  437 PHE B CE2 1 
ATOM   7694 C  CZ  . PHE B 1 439 ? -10.771 32.250  -11.525  1.00 42.92  ?  437 PHE B CZ  1 
ATOM   7695 N  N   . LEU B 1 440 ? -9.106  35.508  -15.086  1.00 40.27  ?  438 LEU B N   1 
ATOM   7696 C  CA  . LEU B 1 440 ? -9.945  36.701  -14.985  1.00 35.06  ?  438 LEU B CA  1 
ATOM   7697 C  C   . LEU B 1 440 ? -10.763 36.536  -13.711  1.00 40.49  ?  438 LEU B C   1 
ATOM   7698 O  O   . LEU B 1 440 ? -11.727 35.769  -13.673  1.00 38.24  ?  438 LEU B O   1 
ATOM   7699 C  CB  . LEU B 1 440 ? -10.819 36.858  -16.223  1.00 32.37  ?  438 LEU B CB  1 
ATOM   7700 C  CG  . LEU B 1 440 ? -10.065 36.919  -17.558  1.00 38.22  ?  438 LEU B CG  1 
ATOM   7701 C  CD1 . LEU B 1 440 ? -11.024 37.080  -18.730  1.00 35.66  ?  438 LEU B CD1 1 
ATOM   7702 C  CD2 . LEU B 1 440 ? -9.015  38.028  -17.560  1.00 37.62  ?  438 LEU B CD2 1 
ATOM   7703 N  N   . GLY B 1 441 ? -10.370 37.244  -12.658  1.00 39.39  ?  439 GLY B N   1 
ATOM   7704 C  CA  . GLY B 1 441 ? -10.957 36.993  -11.362  1.00 40.54  ?  439 GLY B CA  1 
ATOM   7705 C  C   . GLY B 1 441 ? -12.169 37.789  -10.947  1.00 43.73  ?  439 GLY B C   1 
ATOM   7706 O  O   . GLY B 1 441 ? -12.674 37.558  -9.844   1.00 39.18  ?  439 GLY B O   1 
ATOM   7707 N  N   . THR B 1 442 ? -12.687 38.699  -11.766  1.00 37.58  ?  440 THR B N   1 
ATOM   7708 C  CA  . THR B 1 442 ? -13.809 39.528  -11.333  1.00 46.35  ?  440 THR B CA  1 
ATOM   7709 C  C   . THR B 1 442 ? -14.999 39.343  -12.265  1.00 43.55  ?  440 THR B C   1 
ATOM   7710 O  O   . THR B 1 442 ? -14.952 39.735  -13.436  1.00 40.44  ?  440 THR B O   1 
ATOM   7711 C  CB  . THR B 1 442 ? -13.398 40.997  -11.246  1.00 41.83  ?  440 THR B CB  1 
ATOM   7712 O  OG1 . THR B 1 442 ? -12.427 41.148  -10.204  1.00 56.30  ?  440 THR B OG1 1 
ATOM   7713 C  CG2 . THR B 1 442 ? -14.605 41.867  -10.916  1.00 48.43  ?  440 THR B CG2 1 
ATOM   7714 N  N   . CYS B 1 443 ? -16.064 38.750  -11.734  1.00 41.34  ?  441 CYS B N   1 
ATOM   7715 C  CA  . CYS B 1 443 ? -17.306 38.585  -12.472  1.00 39.59  ?  441 CYS B CA  1 
ATOM   7716 C  C   . CYS B 1 443 ? -18.082 39.892  -12.405  1.00 40.55  ?  441 CYS B C   1 
ATOM   7717 O  O   . CYS B 1 443 ? -18.210 40.491  -11.334  1.00 47.71  ?  441 CYS B O   1 
ATOM   7718 C  CB  . CYS B 1 443 ? -18.124 37.433  -11.885  1.00 49.22  ?  441 CYS B CB  1 
ATOM   7719 S  SG  . CYS B 1 443 ? -19.773 37.191  -12.601  1.00 43.66  ?  441 CYS B SG  1 
ATOM   7720 N  N   . ARG B 1 444 ? -18.598 40.339  -13.547  1.00 42.87  ?  442 ARG B N   1 
ATOM   7721 C  CA  . ARG B 1 444 ? -19.278 41.622  -13.615  1.00 43.08  ?  442 ARG B CA  1 
ATOM   7722 C  C   . ARG B 1 444 ? -20.757 41.490  -13.933  1.00 40.79  ?  442 ARG B C   1 
ATOM   7723 O  O   . ARG B 1 444 ? -21.471 42.497  -13.917  1.00 42.97  ?  442 ARG B O   1 
ATOM   7724 C  CB  . ARG B 1 444 ? -18.610 42.517  -14.668  1.00 45.82  ?  442 ARG B CB  1 
ATOM   7725 C  CG  . ARG B 1 444 ? -17.154 42.819  -14.366  1.00 55.74  ?  442 ARG B CG  1 
ATOM   7726 C  CD  . ARG B 1 444 ? -16.597 43.889  -15.283  1.00 61.95  ?  442 ARG B CD  1 
ATOM   7727 N  NE  . ARG B 1 444 ? -17.283 45.163  -15.114  1.00 67.30  ?  442 ARG B NE  1 
ATOM   7728 C  CZ  . ARG B 1 444 ? -16.692 46.276  -14.702  1.00 64.40  ?  442 ARG B CZ  1 
ATOM   7729 N  NH1 . ARG B 1 444 ? -15.377 46.356  -14.585  1.00 64.38  ?  442 ARG B NH1 1 
ATOM   7730 N  NH2 . ARG B 1 444 ? -17.435 47.351  -14.455  1.00 70.98  ?  442 ARG B NH2 1 
ATOM   7731 N  N   . ARG B 1 445 ? -21.234 40.282  -14.209  1.00 37.68  ?  443 ARG B N   1 
ATOM   7732 C  CA  . ARG B 1 445 ? -22.602 40.057  -14.648  1.00 42.19  ?  443 ARG B CA  1 
ATOM   7733 C  C   . ARG B 1 445 ? -23.536 39.618  -13.528  1.00 40.48  ?  443 ARG B C   1 
ATOM   7734 O  O   . ARG B 1 445 ? -24.688 40.058  -13.483  1.00 35.57  ?  443 ARG B O   1 
ATOM   7735 C  CB  . ARG B 1 445 ? -22.602 38.991  -15.753  1.00 34.87  ?  443 ARG B CB  1 
ATOM   7736 C  CG  . ARG B 1 445 ? -23.957 38.388  -16.093  1.00 40.62  ?  443 ARG B CG  1 
ATOM   7737 C  CD  . ARG B 1 445 ? -23.765 37.015  -16.735  1.00 34.87  ?  443 ARG B CD  1 
ATOM   7738 N  NE  . ARG B 1 445 ? -22.939 37.105  -17.932  1.00 35.46  ?  443 ARG B NE  1 
ATOM   7739 C  CZ  . ARG B 1 445 ? -22.461 36.066  -18.606  1.00 41.15  ?  443 ARG B CZ  1 
ATOM   7740 N  NH1 . ARG B 1 445 ? -22.561 34.834  -18.138  1.00 29.98  ?  443 ARG B NH1 1 
ATOM   7741 N  NH2 . ARG B 1 445 ? -21.813 36.278  -19.750  1.00 35.00  ?  443 ARG B NH2 1 
ATOM   7742 N  N   . CYS B 1 446 ? -23.051 38.800  -12.596  1.00 36.57  ?  444 CYS B N   1 
ATOM   7743 C  CA  . CYS B 1 446 ? -23.925 38.093  -11.666  1.00 36.12  ?  444 CYS B CA  1 
ATOM   7744 C  C   . CYS B 1 446 ? -24.016 38.760  -10.298  1.00 41.08  ?  444 CYS B C   1 
ATOM   7745 O  O   . CYS B 1 446 ? -23.031 39.321  -9.807   1.00 37.86  ?  444 CYS B O   1 
ATOM   7746 C  CB  . CYS B 1 446 ? -23.430 36.659  -11.483  1.00 32.19  ?  444 CYS B CB  1 
ATOM   7747 S  SG  . CYS B 1 446 ? -23.420 35.699  -13.007  1.00 36.40  ?  444 CYS B SG  1 
ATOM   7748 N  N   . PRO B 1 447 ? -25.200 38.700  -9.686   1.00 41.59  ?  445 PRO B N   1 
ATOM   7749 C  CA  . PRO B 1 447 ? -25.334 39.124  -8.288   1.00 43.63  ?  445 PRO B CA  1 
ATOM   7750 C  C   . PRO B 1 447 ? -24.340 38.370  -7.413   1.00 40.49  ?  445 PRO B C   1 
ATOM   7751 O  O   . PRO B 1 447 ? -23.942 37.245  -7.722   1.00 37.78  ?  445 PRO B O   1 
ATOM   7752 C  CB  . PRO B 1 447 ? -26.785 38.763  -7.940   1.00 42.48  ?  445 PRO B CB  1 
ATOM   7753 C  CG  . PRO B 1 447 ? -27.254 37.861  -9.059   1.00 38.23  ?  445 PRO B CG  1 
ATOM   7754 C  CD  . PRO B 1 447 ? -26.490 38.298  -10.264  1.00 39.62  ?  445 PRO B CD  1 
ATOM   7755 N  N   . ALA B 1 448 ? -23.953 38.996  -6.299   1.00 40.98  ?  446 ALA B N   1 
ATOM   7756 C  CA  . ALA B 1 448 ? -22.945 38.396  -5.427   1.00 43.29  ?  446 ALA B CA  1 
ATOM   7757 C  C   . ALA B 1 448 ? -23.325 36.990  -4.971   1.00 44.10  ?  446 ALA B C   1 
ATOM   7758 O  O   . ALA B 1 448 ? -22.441 36.145  -4.783   1.00 41.09  ?  446 ALA B O   1 
ATOM   7759 C  CB  . ALA B 1 448 ? -22.702 39.297  -4.215   1.00 40.59  ?  446 ALA B CB  1 
ATOM   7760 N  N   . GLU B 1 449 ? -24.619 36.712  -4.795   1.00 39.17  ?  447 GLU B N   1 
ATOM   7761 C  CA  . GLU B 1 449 ? -25.023 35.390  -4.318   1.00 44.04  ?  447 GLU B CA  1 
ATOM   7762 C  C   . GLU B 1 449 ? -24.627 34.303  -5.307   1.00 43.48  ?  447 GLU B C   1 
ATOM   7763 O  O   . GLU B 1 449 ? -24.254 33.193  -4.907   1.00 46.22  ?  447 GLU B O   1 
ATOM   7764 C  CB  . GLU B 1 449 ? -26.526 35.365  -4.051   1.00 41.11  ?  447 GLU B CB  1 
ATOM   7765 C  CG  . GLU B 1 449 ? -26.965 36.483  -3.130   1.00 48.54  ?  447 GLU B CG  1 
ATOM   7766 C  CD  . GLU B 1 449 ? -27.658 37.605  -3.869   1.00 53.61  ?  447 GLU B CD  1 
ATOM   7767 O  OE1 . GLU B 1 449 ? -27.052 38.156  -4.814   1.00 52.64  ?  447 GLU B OE1 1 
ATOM   7768 O  OE2 . GLU B 1 449 ? -28.792 37.959  -3.485   1.00 58.80  -1 447 GLU B OE2 1 
ATOM   7769 N  N   . ILE B 1 450 ? -24.721 34.594  -6.603   1.00 42.26  ?  448 ILE B N   1 
ATOM   7770 C  CA  . ILE B 1 450 ? -24.353 33.602  -7.604   1.00 33.97  ?  448 ILE B CA  1 
ATOM   7771 C  C   . ILE B 1 450 ? -22.838 33.469  -7.678   1.00 34.74  ?  448 ILE B C   1 
ATOM   7772 O  O   . ILE B 1 450 ? -22.302 32.358  -7.775   1.00 37.36  ?  448 ILE B O   1 
ATOM   7773 C  CB  . ILE B 1 450 ? -24.965 33.964  -8.967   1.00 34.30  ?  448 ILE B CB  1 
ATOM   7774 C  CG1 . ILE B 1 450 ? -26.490 33.929  -8.881   1.00 38.46  ?  448 ILE B CG1 1 
ATOM   7775 C  CG2 . ILE B 1 450 ? -24.464 33.017  -10.040  1.00 37.41  ?  448 ILE B CG2 1 
ATOM   7776 C  CD1 . ILE B 1 450 ? -27.176 34.389  -10.142  1.00 31.58  ?  448 ILE B CD1 1 
ATOM   7777 N  N   . VAL B 1 451 ? -22.123 34.596  -7.633   1.00 32.24  ?  449 VAL B N   1 
ATOM   7778 C  CA  . VAL B 1 451 ? -20.665 34.554  -7.715   1.00 39.91  ?  449 VAL B CA  1 
ATOM   7779 C  C   . VAL B 1 451 ? -20.088 33.801  -6.524   1.00 38.64  ?  449 VAL B C   1 
ATOM   7780 O  O   . VAL B 1 451 ? -19.157 32.998  -6.668   1.00 41.06  ?  449 VAL B O   1 
ATOM   7781 C  CB  . VAL B 1 451 ? -20.091 35.979  -7.813   1.00 43.63  ?  449 VAL B CB  1 
ATOM   7782 C  CG1 . VAL B 1 451 ? -18.573 35.932  -7.933   1.00 37.77  ?  449 VAL B CG1 1 
ATOM   7783 C  CG2 . VAL B 1 451 ? -20.705 36.715  -8.992   1.00 40.03  ?  449 VAL B CG2 1 
ATOM   7784 N  N   . ASP B 1 452 ? -20.643 34.027  -5.332   1.00 40.26  ?  450 ASP B N   1 
ATOM   7785 C  CA  . ASP B 1 452 ? -20.119 33.342  -4.158   1.00 45.79  ?  450 ASP B CA  1 
ATOM   7786 C  C   . ASP B 1 452 ? -20.347 31.840  -4.257   1.00 41.44  ?  450 ASP B C   1 
ATOM   7787 O  O   . ASP B 1 452 ? -19.516 31.056  -3.785   1.00 39.23  ?  450 ASP B O   1 
ATOM   7788 C  CB  . ASP B 1 452 ? -20.760 33.901  -2.885   1.00 43.67  ?  450 ASP B CB  1 
ATOM   7789 C  CG  . ASP B 1 452 ? -20.286 35.309  -2.556   1.00 57.24  ?  450 ASP B CG  1 
ATOM   7790 O  OD1 . ASP B 1 452 ? -19.319 35.783  -3.191   1.00 61.06  ?  450 ASP B OD1 1 
ATOM   7791 O  OD2 . ASP B 1 452 ? -20.888 35.945  -1.665   1.00 65.65  -1 450 ASP B OD2 1 
ATOM   7792 N  N   . THR B 1 453 ? -21.458 31.418  -4.865   1.00 38.82  ?  451 THR B N   1 
ATOM   7793 C  CA  . THR B 1 453 ? -21.736 29.990  -4.953   1.00 40.72  ?  451 THR B CA  1 
ATOM   7794 C  C   . THR B 1 453 ? -20.757 29.301  -5.898   1.00 38.34  ?  451 THR B C   1 
ATOM   7795 O  O   . THR B 1 453 ? -20.187 28.257  -5.563   1.00 41.00  ?  451 THR B O   1 
ATOM   7796 C  CB  . THR B 1 453 ? -23.177 29.761  -5.412   1.00 40.12  ?  451 THR B CB  1 
ATOM   7797 O  OG1 . THR B 1 453 ? -24.082 30.406  -4.506   1.00 41.09  ?  451 THR B OG1 1 
ATOM   7798 C  CG2 . THR B 1 453 ? -23.490 28.274  -5.455   1.00 35.85  ?  451 THR B CG2 1 
ATOM   7799 N  N   . VAL B 1 454 ? -20.530 29.886  -7.077   1.00 38.99  ?  452 VAL B N   1 
ATOM   7800 C  CA  . VAL B 1 454 ? -19.695 29.216  -8.070   1.00 38.93  ?  452 VAL B CA  1 
ATOM   7801 C  C   . VAL B 1 454 ? -18.218 29.395  -7.744   1.00 41.66  ?  452 VAL B C   1 
ATOM   7802 O  O   . VAL B 1 454 ? -17.401 28.522  -8.060   1.00 43.75  ?  452 VAL B O   1 
ATOM   7803 C  CB  . VAL B 1 454 ? -20.040 29.694  -9.490   1.00 40.15  ?  452 VAL B CB  1 
ATOM   7804 C  CG1 . VAL B 1 454 ? -21.497 29.371  -9.802   1.00 35.70  ?  452 VAL B CG1 1 
ATOM   7805 C  CG2 . VAL B 1 454 ? -19.771 31.182  -9.643   1.00 36.17  ?  452 VAL B CG2 1 
ATOM   7806 N  N   . SER B 1 455 ? -17.846 30.511  -7.110   1.00 44.10  ?  453 SER B N   1 
ATOM   7807 C  CA  . SER B 1 455 ? -16.457 30.681  -6.701   1.00 44.96  ?  453 SER B CA  1 
ATOM   7808 C  C   . SER B 1 455 ? -16.034 29.523  -5.812   1.00 47.38  ?  453 SER B C   1 
ATOM   7809 O  O   . SER B 1 455 ? -14.950 28.953  -5.985   1.00 50.68  ?  453 SER B O   1 
ATOM   7810 C  CB  . SER B 1 455 ? -16.279 32.012  -5.974   1.00 42.27  ?  453 SER B CB  1 
ATOM   7811 O  OG  . SER B 1 455 ? -14.908 32.306  -5.779   1.00 43.92  ?  453 SER B OG  1 
ATOM   7812 N  N   . ALA B 1 456 ? -16.891 29.154  -4.863   1.00 45.46  ?  454 ALA B N   1 
ATOM   7813 C  CA  . ALA B 1 456 ? -16.577 28.081  -3.932   1.00 51.59  ?  454 ALA B CA  1 
ATOM   7814 C  C   . ALA B 1 456 ? -16.773 26.719  -4.582   1.00 51.71  ?  454 ALA B C   1 
ATOM   7815 O  O   . ALA B 1 456 ? -16.065 25.764  -4.243   1.00 53.60  ?  454 ALA B O   1 
ATOM   7816 C  CB  . ALA B 1 456 ? -17.443 28.201  -2.678   1.00 45.86  ?  454 ALA B CB  1 
ATOM   7817 N  N   . LEU B 1 457 ? -17.719 26.618  -5.518   1.00 46.98  ?  455 LEU B N   1 
ATOM   7818 C  CA  . LEU B 1 457 ? -18.072 25.330  -6.103   1.00 47.68  ?  455 LEU B CA  1 
ATOM   7819 C  C   . LEU B 1 457 ? -17.062 24.863  -7.148   1.00 48.50  ?  455 LEU B C   1 
ATOM   7820 O  O   . LEU B 1 457 ? -16.781 23.662  -7.234   1.00 46.65  ?  455 LEU B O   1 
ATOM   7821 C  CB  . LEU B 1 457 ? -19.471 25.412  -6.719   1.00 46.03  ?  455 LEU B CB  1 
ATOM   7822 C  CG  . LEU B 1 457 ? -19.998 24.181  -7.460   1.00 51.65  ?  455 LEU B CG  1 
ATOM   7823 C  CD1 . LEU B 1 457 ? -20.206 23.021  -6.498   1.00 53.21  ?  455 LEU B CD1 1 
ATOM   7824 C  CD2 . LEU B 1 457 ? -21.285 24.505  -8.207   1.00 46.73  ?  455 LEU B CD2 1 
ATOM   7825 N  N   . VAL B 1 458 ? -16.498 25.775  -7.947   1.00 46.72  ?  456 VAL B N   1 
ATOM   7826 C  CA  . VAL B 1 458 ? -15.654 25.340  -9.060   1.00 45.45  ?  456 VAL B CA  1 
ATOM   7827 C  C   . VAL B 1 458 ? -14.428 26.219  -9.293   1.00 47.15  ?  456 VAL B C   1 
ATOM   7828 O  O   . VAL B 1 458 ? -13.627 25.933  -10.190  1.00 51.13  ?  456 VAL B O   1 
ATOM   7829 C  CB  . VAL B 1 458 ? -16.473 25.252  -10.364  1.00 49.33  ?  456 VAL B CB  1 
ATOM   7830 C  CG1 . VAL B 1 458 ? -17.442 24.072  -10.319  1.00 43.96  ?  456 VAL B CG1 1 
ATOM   7831 C  CG2 . VAL B 1 458 ? -17.199 26.564  -10.642  1.00 42.69  ?  456 VAL B CG2 1 
ATOM   7832 N  N   . TYR B 1 459 ? -14.252 27.285  -8.509   1.00 46.32  ?  457 TYR B N   1 
ATOM   7833 C  CA  . TYR B 1 459 ? -13.162 28.223  -8.772   1.00 45.39  ?  457 TYR B CA  1 
ATOM   7834 C  C   . TYR B 1 459 ? -12.243 28.429  -7.571   1.00 52.23  ?  457 TYR B C   1 
ATOM   7835 O  O   . TYR B 1 459 ? -11.522 29.430  -7.514   1.00 49.51  ?  457 TYR B O   1 
ATOM   7836 C  CB  . TYR B 1 459 ? -13.722 29.564  -9.251   1.00 44.51  ?  457 TYR B CB  1 
ATOM   7837 C  CG  . TYR B 1 459 ? -14.469 29.470  -10.563  1.00 45.70  ?  457 TYR B CG  1 
ATOM   7838 C  CD1 . TYR B 1 459 ? -13.852 28.963  -11.700  1.00 41.80  ?  457 TYR B CD1 1 
ATOM   7839 C  CD2 . TYR B 1 459 ? -15.793 29.878  -10.663  1.00 41.16  ?  457 TYR B CD2 1 
ATOM   7840 C  CE1 . TYR B 1 459 ? -14.530 28.872  -12.902  1.00 39.42  ?  457 TYR B CE1 1 
ATOM   7841 C  CE2 . TYR B 1 459 ? -16.480 29.787  -11.861  1.00 39.50  ?  457 TYR B CE2 1 
ATOM   7842 C  CZ  . TYR B 1 459 ? -15.842 29.287  -12.978  1.00 38.47  ?  457 TYR B CZ  1 
ATOM   7843 O  OH  . TYR B 1 459 ? -16.517 29.191  -14.172  1.00 35.80  ?  457 TYR B OH  1 
ATOM   7844 N  N   . ASP B 1 460 ? -12.243 27.494  -6.620   1.00 55.59  ?  458 ASP B N   1 
ATOM   7845 C  CA  . ASP B 1 460 ? -11.366 27.546  -5.446   1.00 53.49  ?  458 ASP B CA  1 
ATOM   7846 C  C   . ASP B 1 460 ? -11.413 28.904  -4.749   1.00 55.76  ?  458 ASP B C   1 
ATOM   7847 O  O   . ASP B 1 460 ? -10.407 29.395  -4.231   1.00 51.23  ?  458 ASP B O   1 
ATOM   7848 C  CB  . ASP B 1 460 ? -9.929  27.189  -5.826   1.00 62.60  ?  458 ASP B CB  1 
ATOM   7849 C  CG  . ASP B 1 460 ? -9.804  25.783  -6.369   1.00 75.84  ?  458 ASP B CG  1 
ATOM   7850 O  OD1 . ASP B 1 460 ? -10.218 24.836  -5.666   1.00 81.77  ?  458 ASP B OD1 1 
ATOM   7851 O  OD2 . ASP B 1 460 ? -9.290  25.624  -7.495   1.00 87.72  -1 458 ASP B OD2 1 
ATOM   7852 N  N   . ASN B 1 461 ? -12.593 29.520  -4.737   1.00 51.38  ?  459 ASN B N   1 
ATOM   7853 C  CA  . ASN B 1 461 ? -12.816 30.769  -4.009   1.00 55.47  ?  459 ASN B CA  1 
ATOM   7854 C  C   . ASN B 1 461 ? -11.954 31.906  -4.546   1.00 50.36  ?  459 ASN B C   1 
ATOM   7855 O  O   . ASN B 1 461 ? -11.533 32.787  -3.793   1.00 55.67  ?  459 ASN B O   1 
ATOM   7856 C  CB  . ASN B 1 461 ? -12.576 30.585  -2.508   1.00 54.49  ?  459 ASN B CB  1 
ATOM   7857 C  CG  . ASN B 1 461 ? -13.596 29.668  -1.866   1.00 59.20  ?  459 ASN B CG  1 
ATOM   7858 O  OD1 . ASN B 1 461 ? -14.772 30.014  -1.750   1.00 54.20  ?  459 ASN B OD1 1 
ATOM   7859 N  ND2 . ASN B 1 461 ? -13.153 28.488  -1.451   1.00 61.71  ?  459 ASN B ND2 1 
ATOM   7860 N  N   . LYS B 1 462 ? -11.700 31.915  -5.854   1.00 51.94  ?  460 LYS B N   1 
ATOM   7861 C  CA  . LYS B 1 462 ? -10.858 32.935  -6.459   1.00 50.88  ?  460 LYS B CA  1 
ATOM   7862 C  C   . LYS B 1 462 ? -11.627 33.869  -7.375   1.00 51.81  ?  460 LYS B C   1 
ATOM   7863 O  O   . LYS B 1 462 ? -11.054 34.857  -7.845   1.00 52.23  ?  460 LYS B O   1 
ATOM   7864 C  CB  . LYS B 1 462 ? -9.708  32.298  -7.255   1.00 55.13  ?  460 LYS B CB  1 
ATOM   7865 C  CG  . LYS B 1 462 ? -8.831  31.345  -6.464   1.00 59.32  ?  460 LYS B CG  1 
ATOM   7866 C  CD  . LYS B 1 462 ? -7.508  31.107  -7.178   1.00 59.20  ?  460 LYS B CD  1 
ATOM   7867 C  CE  . LYS B 1 462 ? -7.708  30.861  -8.668   1.00 57.84  ?  460 LYS B CE  1 
ATOM   7868 N  NZ  . LYS B 1 462 ? -8.494  29.627  -8.947   1.00 66.25  ?  460 LYS B NZ  1 
ATOM   7869 N  N   . LEU B 1 463 ? -12.894 33.583  -7.652   1.00 43.92  ?  461 LEU B N   1 
ATOM   7870 C  CA  . LEU B 1 463 ? -13.719 34.479  -8.444   1.00 45.50  ?  461 LEU B CA  1 
ATOM   7871 C  C   . LEU B 1 463 ? -14.374 35.480  -7.503   1.00 46.12  ?  461 LEU B C   1 
ATOM   7872 O  O   . LEU B 1 463 ? -15.032 35.091  -6.533   1.00 41.47  ?  461 LEU B O   1 
ATOM   7873 C  CB  . LEU B 1 463 ? -14.774 33.703  -9.233   1.00 42.18  ?  461 LEU B CB  1 
ATOM   7874 C  CG  . LEU B 1 463 ? -15.700 34.540  -10.119  1.00 41.08  ?  461 LEU B CG  1 
ATOM   7875 C  CD1 . LEU B 1 463 ? -14.901 35.320  -11.152  1.00 39.79  ?  461 LEU B CD1 1 
ATOM   7876 C  CD2 . LEU B 1 463 ? -16.744 33.660  -10.795  1.00 40.31  ?  461 LEU B CD2 1 
ATOM   7877 N  N   . LYS B 1 464 ? -14.193 36.761  -7.793   1.00 41.56  ?  462 LYS B N   1 
ATOM   7878 C  CA  . LYS B 1 464 ? -14.741 37.830  -6.976   1.00 47.36  ?  462 LYS B CA  1 
ATOM   7879 C  C   . LYS B 1 464 ? -15.894 38.496  -7.711   1.00 43.50  ?  462 LYS B C   1 
ATOM   7880 O  O   . LYS B 1 464 ? -15.956 38.487  -8.944   1.00 39.97  ?  462 LYS B O   1 
ATOM   7881 C  CB  . LYS B 1 464 ? -13.666 38.862  -6.625   1.00 45.00  ?  462 LYS B CB  1 
ATOM   7882 C  CG  . LYS B 1 464 ? -12.373 38.251  -6.101   1.00 58.96  ?  462 LYS B CG  1 
ATOM   7883 C  CD  . LYS B 1 464 ? -12.601 37.496  -4.798   1.00 61.14  ?  462 LYS B CD  1 
ATOM   7884 C  CE  . LYS B 1 464 ? -11.380 36.673  -4.410   1.00 68.19  ?  462 LYS B CE  1 
ATOM   7885 N  NZ  . LYS B 1 464 ? -11.525 36.047  -3.065   1.00 77.56  ?  462 LYS B NZ  1 
ATOM   7886 N  N   . ALA B 1 465 ? -16.812 39.065  -6.944   1.00 43.08  ?  463 ALA B N   1 
ATOM   7887 C  CA  . ALA B 1 465 ? -17.981 39.716  -7.509   1.00 43.46  ?  463 ALA B CA  1 
ATOM   7888 C  C   . ALA B 1 465 ? -17.759 41.216  -7.628   1.00 46.81  ?  463 ALA B C   1 
ATOM   7889 O  O   . ALA B 1 465 ? -17.058 41.832  -6.820   1.00 51.60  ?  463 ALA B O   1 
ATOM   7890 C  CB  . ALA B 1 465 ? -19.222 39.447  -6.654   1.00 44.33  ?  463 ALA B CB  1 
ATOM   7891 N  N   . HIS B 1 466 ? -18.370 41.798  -8.656   1.00 49.66  ?  464 HIS B N   1 
ATOM   7892 C  CA  . HIS B 1 466 ? -18.379 43.240  -8.847   1.00 56.14  ?  464 HIS B CA  1 
ATOM   7893 C  C   . HIS B 1 466 ? -19.659 43.823  -8.271   1.00 57.26  ?  464 HIS B C   1 
ATOM   7894 O  O   . HIS B 1 466 ? -19.625 44.808  -7.528   1.00 60.36  ?  464 HIS B O   1 
ATOM   7895 C  CB  . HIS B 1 466 ? -18.250 43.583  -10.337  1.00 54.99  ?  464 HIS B CB  1 
ATOM   7896 C  CG  . HIS B 1 466 ? -18.142 45.049  -10.617  1.00 55.38  ?  464 HIS B CG  1 
ATOM   7897 N  ND1 . HIS B 1 466 ? -17.392 45.903  -9.837   1.00 65.65  ?  464 HIS B ND1 1 
ATOM   7898 C  CD2 . HIS B 1 466 ? -18.682 45.812  -11.596  1.00 59.97  ?  464 HIS B CD2 1 
ATOM   7899 C  CE1 . HIS B 1 466 ? -17.475 47.128  -10.322  1.00 62.34  ?  464 HIS B CE1 1 
ATOM   7900 N  NE2 . HIS B 1 466 ? -18.253 47.101  -11.390  1.00 59.26  ?  464 HIS B NE2 1 
ATOM   7901 N  N   . LYS B 1 467 ? -20.790 43.206  -8.597   1.00 51.28  ?  465 LYS B N   1 
ATOM   7902 C  CA  . LYS B 1 467 ? -22.085 43.648  -8.123   1.00 54.79  ?  465 LYS B CA  1 
ATOM   7903 C  C   . LYS B 1 467 ? -22.249 43.214  -6.671   1.00 56.46  ?  465 LYS B C   1 
ATOM   7904 O  O   . LYS B 1 467 ? -21.559 42.311  -6.188   1.00 54.96  ?  465 LYS B O   1 
ATOM   7905 C  CB  . LYS B 1 467 ? -23.206 43.040  -8.968   1.00 45.69  ?  465 LYS B CB  1 
ATOM   7906 C  CG  . LYS B 1 467 ? -23.192 43.412  -10.440  1.00 50.45  ?  465 LYS B CG  1 
ATOM   7907 C  CD  . LYS B 1 467 ? -24.403 42.816  -11.151  1.00 45.76  ?  465 LYS B CD  1 
ATOM   7908 C  CE  . LYS B 1 467 ? -24.509 43.301  -12.589  1.00 51.22  ?  465 LYS B CE  1 
ATOM   7909 N  NZ  . LYS B 1 467 ? -25.787 42.874  -13.229  1.00 47.54  ?  465 LYS B NZ  1 
ATOM   7910 N  N   . ASP B 1 468 ? -23.193 43.838  -5.979   1.00 49.30  ?  466 ASP B N   1 
ATOM   7911 C  CA  . ASP B 1 468 ? -23.478 43.432  -4.615   1.00 49.98  ?  466 ASP B CA  1 
ATOM   7912 C  C   . ASP B 1 468 ? -24.578 42.372  -4.630   1.00 54.45  ?  466 ASP B C   1 
ATOM   7913 O  O   . ASP B 1 468 ? -25.007 41.900  -5.686   1.00 54.37  ?  466 ASP B O   1 
ATOM   7914 C  CB  . ASP B 1 468 ? -23.874 44.633  -3.758   1.00 56.66  ?  466 ASP B CB  1 
ATOM   7915 C  CG  . ASP B 1 468 ? -22.800 45.705  -3.720   1.00 73.40  ?  466 ASP B CG  1 
ATOM   7916 O  OD1 . ASP B 1 468 ? -21.656 45.395  -3.322   1.00 71.95  ?  466 ASP B OD1 1 
ATOM   7917 O  OD2 . ASP B 1 468 ? -23.106 46.863  -4.078   1.00 79.39  -1 466 ASP B OD2 1 
ATOM   7918 N  N   . LYS B 1 469 ? -25.027 41.969  -3.446   1.00 54.94  ?  467 LYS B N   1 
ATOM   7919 C  CA  . LYS B 1 469 ? -26.135 41.031  -3.383   1.00 51.98  ?  467 LYS B CA  1 
ATOM   7920 C  C   . LYS B 1 469 ? -27.382 41.688  -3.959   1.00 51.45  ?  467 LYS B C   1 
ATOM   7921 O  O   . LYS B 1 469 ? -27.613 42.886  -3.774   1.00 50.44  ?  467 LYS B O   1 
ATOM   7922 C  CB  . LYS B 1 469 ? -26.387 40.591  -1.939   1.00 57.64  ?  467 LYS B CB  1 
ATOM   7923 C  CG  . LYS B 1 469 ? -25.402 39.564  -1.396   1.00 56.71  ?  467 LYS B CG  1 
ATOM   7924 C  CD  . LYS B 1 469 ? -25.725 39.230  0.058    1.00 62.62  ?  467 LYS B CD  1 
ATOM   7925 C  CE  . LYS B 1 469 ? -24.841 38.115  0.601    1.00 64.76  ?  467 LYS B CE  1 
ATOM   7926 N  NZ  . LYS B 1 469 ? -25.256 36.774  0.098    1.00 73.32  ?  467 LYS B NZ  1 
ATOM   7927 N  N   . SER B 1 470 ? -28.181 40.900  -4.677   1.00 51.35  ?  468 SER B N   1 
ATOM   7928 C  CA  . SER B 1 470 ? -29.389 41.413  -5.308   1.00 51.81  ?  468 SER B CA  1 
ATOM   7929 C  C   . SER B 1 470 ? -30.638 41.175  -4.475   1.00 45.99  ?  468 SER B C   1 
ATOM   7930 O  O   . SER B 1 470 ? -31.620 41.907  -4.637   1.00 48.39  ?  468 SER B O   1 
ATOM   7931 C  CB  . SER B 1 470 ? -29.587 40.779  -6.691   1.00 49.27  ?  468 SER B CB  1 
ATOM   7932 O  OG  . SER B 1 470 ? -29.780 39.378  -6.591   1.00 50.16  ?  468 SER B OG  1 
ATOM   7933 N  N   . ALA B 1 471 ? -30.621 40.171  -3.600   1.00 50.00  ?  469 ALA B N   1 
ATOM   7934 C  CA  . ALA B 1 471 ? -31.776 39.740  -2.820   1.00 50.70  ?  469 ALA B CA  1 
ATOM   7935 C  C   . ALA B 1 471 ? -32.878 39.156  -3.693   1.00 53.11  ?  469 ALA B C   1 
ATOM   7936 O  O   . ALA B 1 471 ? -34.034 39.072  -3.262   1.00 61.50  ?  469 ALA B O   1 
ATOM   7937 C  CB  . ALA B 1 471 ? -32.333 40.885  -1.965   1.00 51.70  ?  469 ALA B CB  1 
ATOM   7938 N  N   . GLN B 1 472 ? -32.543 38.754  -4.921   1.00 47.74  ?  470 GLN B N   1 
ATOM   7939 C  CA  . GLN B 1 472 ? -33.493 38.140  -5.843   1.00 49.00  ?  470 GLN B CA  1 
ATOM   7940 C  C   . GLN B 1 472 ? -33.015 36.774  -6.332   1.00 42.71  ?  470 GLN B C   1 
ATOM   7941 O  O   . GLN B 1 472 ? -33.389 36.340  -7.425   1.00 42.61  ?  470 GLN B O   1 
ATOM   7942 C  CB  . GLN B 1 472 ? -33.778 39.081  -7.015   1.00 50.87  ?  470 GLN B CB  1 
ATOM   7943 C  CG  . GLN B 1 472 ? -34.360 40.417  -6.566   1.00 54.01  ?  470 GLN B CG  1 
ATOM   7944 C  CD  . GLN B 1 472 ? -34.772 41.312  -7.720   1.00 59.93  ?  470 GLN B CD  1 
ATOM   7945 O  OE1 . GLN B 1 472 ? -35.704 41.000  -8.461   1.00 61.35  ?  470 GLN B OE1 1 
ATOM   7946 N  NE2 . GLN B 1 472 ? -34.089 42.441  -7.866   1.00 59.64  ?  470 GLN B NE2 1 
ATOM   7947 N  N   . CYS B 1 473 ? -32.165 36.109  -5.554   1.00 42.51  ?  471 CYS B N   1 
ATOM   7948 C  CA  . CYS B 1 473 ? -31.661 34.771  -5.846   1.00 40.86  ?  471 CYS B CA  1 
ATOM   7949 C  C   . CYS B 1 473 ? -32.305 33.799  -4.860   1.00 41.21  ?  471 CYS B C   1 
ATOM   7950 O  O   . CYS B 1 473 ? -32.006 33.838  -3.661   1.00 40.79  ?  471 CYS B O   1 
ATOM   7951 C  CB  . CYS B 1 473 ? -30.139 34.742  -5.753   1.00 40.63  ?  471 CYS B CB  1 
ATOM   7952 S  SG  . CYS B 1 473 ? -29.349 35.867  -6.918   1.00 41.17  ?  471 CYS B SG  1 
ATOM   7953 N  N   . PHE B 1 474 ? -33.205 32.948  -5.355   1.00 42.67  ?  472 PHE B N   1 
ATOM   7954 C  CA  . PHE B 1 474 ? -34.001 32.082  -4.497   1.00 40.28  ?  472 PHE B CA  1 
ATOM   7955 C  C   . PHE B 1 474 ? -33.828 30.619  -4.891   1.00 39.17  ?  472 PHE B C   1 
ATOM   7956 O  O   . PHE B 1 474 ? -33.422 30.299  -6.012   1.00 29.35  ?  472 PHE B O   1 
ATOM   7957 C  CB  . PHE B 1 474 ? -35.484 32.460  -4.578   1.00 34.25  ?  472 PHE B CB  1 
ATOM   7958 C  CG  . PHE B 1 474 ? -35.760 33.892  -4.234   1.00 38.55  ?  472 PHE B CG  1 
ATOM   7959 C  CD1 . PHE B 1 474 ? -35.821 34.307  -2.914   1.00 39.36  ?  472 PHE B CD1 1 
ATOM   7960 C  CD2 . PHE B 1 474 ? -35.959 34.827  -5.235   1.00 36.44  ?  472 PHE B CD2 1 
ATOM   7961 C  CE1 . PHE B 1 474 ? -36.073 35.629  -2.600   1.00 49.09  ?  472 PHE B CE1 1 
ATOM   7962 C  CE2 . PHE B 1 474 ? -36.213 36.149  -4.929   1.00 40.87  ?  472 PHE B CE2 1 
ATOM   7963 C  CZ  . PHE B 1 474 ? -36.270 36.552  -3.609   1.00 50.37  ?  472 PHE B CZ  1 
ATOM   7964 N  N   . LYS B 1 475 ? -34.141 29.728  -3.948   1.00 32.79  ?  473 LYS B N   1 
ATOM   7965 C  CA  . LYS B 1 475 ? -34.021 28.293  -4.170   1.00 29.76  ?  473 LYS B CA  1 
ATOM   7966 C  C   . LYS B 1 475 ? -35.131 27.560  -3.430   1.00 42.43  ?  473 LYS B C   1 
ATOM   7967 O  O   . LYS B 1 475 ? -35.518 27.954  -2.326   1.00 35.00  ?  473 LYS B O   1 
ATOM   7968 C  CB  . LYS B 1 475 ? -32.662 27.744  -3.709   1.00 30.39  ?  473 LYS B CB  1 
ATOM   7969 C  CG  . LYS B 1 475 ? -32.368 27.925  -2.213   1.00 35.58  ?  473 LYS B CG  1 
ATOM   7970 C  CD  . LYS B 1 475 ? -31.032 27.287  -1.816   1.00 33.59  ?  473 LYS B CD  1 
ATOM   7971 C  CE  . LYS B 1 475 ? -30.838 27.272  -0.300   1.00 40.15  ?  473 LYS B CE  1 
ATOM   7972 N  NZ  . LYS B 1 475 ? -29.524 26.689  0.104    1.00 38.40  ?  473 LYS B NZ  1 
ATOM   7973 N  N   . MET B 1 476 ? -35.628 26.488  -4.043   1.00 38.01  ?  474 MET B N   1 
ATOM   7974 C  CA  . MET B 1 476 ? -36.620 25.625  -3.422   1.00 43.58  ?  474 MET B CA  1 
ATOM   7975 C  C   . MET B 1 476 ? -36.197 24.186  -3.662   1.00 46.58  ?  474 MET B C   1 
ATOM   7976 O  O   . MET B 1 476 ? -35.614 23.866  -4.700   1.00 34.26  ?  474 MET B O   1 
ATOM   7977 C  CB  . MET B 1 476 ? -38.019 25.853  -4.002   1.00 42.15  ?  474 MET B CB  1 
ATOM   7978 C  CG  . MET B 1 476 ? -38.581 27.244  -3.791   1.00 59.12  ?  474 MET B CG  1 
ATOM   7979 S  SD  . MET B 1 476 ? -40.173 27.387  -4.619   1.00 84.59  ?  474 MET B SD  1 
ATOM   7980 C  CE  . MET B 1 476 ? -40.874 25.788  -4.207   1.00 35.86  ?  474 MET B CE  1 
ATOM   7981 N  N   . PHE B 1 477 ? -36.484 23.317  -2.698   1.00 35.77  ?  475 PHE B N   1 
ATOM   7982 C  CA  . PHE B 1 477 ? -36.210 21.892  -2.845   1.00 36.39  ?  475 PHE B CA  1 
ATOM   7983 C  C   . PHE B 1 477 ? -37.546 21.186  -3.052   1.00 44.66  ?  475 PHE B C   1 
ATOM   7984 O  O   . PHE B 1 477 ? -38.365 21.102  -2.128   1.00 40.48  ?  475 PHE B O   1 
ATOM   7985 C  CB  . PHE B 1 477 ? -35.428 21.389  -1.631   1.00 39.23  ?  475 PHE B CB  1 
ATOM   7986 C  CG  . PHE B 1 477 ? -35.044 19.938  -1.690   1.00 45.34  ?  475 PHE B CG  1 
ATOM   7987 C  CD1 . PHE B 1 477 ? -33.945 19.537  -2.433   1.00 38.57  ?  475 PHE B CD1 1 
ATOM   7988 C  CD2 . PHE B 1 477 ? -35.701 18.994  -0.915   1.00 44.38  ?  475 PHE B CD2 1 
ATOM   7989 C  CE1 . PHE B 1 477 ? -33.559 18.211  -2.475   1.00 45.63  ?  475 PHE B CE1 1 
ATOM   7990 C  CE2 . PHE B 1 477 ? -35.313 17.664  -0.944   1.00 46.20  ?  475 PHE B CE2 1 
ATOM   7991 C  CZ  . PHE B 1 477 ? -34.239 17.272  -1.721   1.00 46.08  ?  475 PHE B CZ  1 
ATOM   7992 N  N   . TYR B 1 478 ? -37.757 20.671  -4.262   1.00 36.04  ?  476 TYR B N   1 
ATOM   7993 C  CA  . TYR B 1 478 ? -39.010 20.003  -4.605   1.00 44.95  ?  476 TYR B CA  1 
ATOM   7994 C  C   . TYR B 1 478 ? -38.730 18.920  -5.640   1.00 39.87  ?  476 TYR B C   1 
ATOM   7995 O  O   . TYR B 1 478 ? -38.415 19.232  -6.795   1.00 39.12  ?  476 TYR B O   1 
ATOM   7996 C  CB  . TYR B 1 478 ? -40.019 21.027  -5.118   1.00 37.42  ?  476 TYR B CB  1 
ATOM   7997 C  CG  . TYR B 1 478 ? -41.390 20.488  -5.437   1.00 36.23  ?  476 TYR B CG  1 
ATOM   7998 C  CD1 . TYR B 1 478 ? -42.276 20.135  -4.427   1.00 46.10  ?  476 TYR B CD1 1 
ATOM   7999 C  CD2 . TYR B 1 478 ? -41.817 20.382  -6.748   1.00 35.77  ?  476 TYR B CD2 1 
ATOM   8000 C  CE1 . TYR B 1 478 ? -43.536 19.660  -4.726   1.00 42.82  ?  476 TYR B CE1 1 
ATOM   8001 C  CE2 . TYR B 1 478 ? -43.068 19.913  -7.055   1.00 39.64  ?  476 TYR B CE2 1 
ATOM   8002 C  CZ  . TYR B 1 478 ? -43.926 19.553  -6.045   1.00 39.12  ?  476 TYR B CZ  1 
ATOM   8003 O  OH  . TYR B 1 478 ? -45.176 19.082  -6.366   1.00 52.74  ?  476 TYR B OH  1 
ATOM   8004 N  N   . LYS B 1 479 ? -38.845 17.655  -5.228   1.00 37.76  ?  477 LYS B N   1 
ATOM   8005 C  CA  . LYS B 1 479 ? -38.530 16.549  -6.128   1.00 45.86  ?  477 LYS B CA  1 
ATOM   8006 C  C   . LYS B 1 479 ? -39.563 16.431  -7.244   1.00 47.78  ?  477 LYS B C   1 
ATOM   8007 O  O   . LYS B 1 479 ? -39.210 16.167  -8.400   1.00 42.20  ?  477 LYS B O   1 
ATOM   8008 C  CB  . LYS B 1 479 ? -38.444 15.244  -5.339   1.00 51.87  ?  477 LYS B CB  1 
ATOM   8009 C  CG  . LYS B 1 479 ? -37.435 15.265  -4.198   1.00 57.02  ?  477 LYS B CG  1 
ATOM   8010 C  CD  . LYS B 1 479 ? -36.193 14.442  -4.494   1.00 51.26  ?  477 LYS B CD  1 
ATOM   8011 C  CE  . LYS B 1 479 ? -35.265 14.432  -3.288   1.00 52.26  ?  477 LYS B CE  1 
ATOM   8012 N  NZ  . LYS B 1 479 ? -33.967 13.754  -3.556   1.00 60.82  ?  477 LYS B NZ  1 
ATOM   8013 N  N   . GLY B 1 480 ? -40.837 16.658  -6.924   1.00 44.67  ?  478 GLY B N   1 
ATOM   8014 C  CA  . GLY B 1 480 ? -41.907 16.594  -7.904   1.00 37.18  ?  478 GLY B CA  1 
ATOM   8015 C  C   . GLY B 1 480 ? -42.155 15.186  -8.423   1.00 39.09  ?  478 GLY B C   1 
ATOM   8016 O  O   . GLY B 1 480 ? -42.037 14.192  -7.700   1.00 42.17  ?  478 GLY B O   1 
ATOM   8017 N  N   . VAL B 1 481 ? -42.551 15.107  -9.692   1.00 43.15  ?  479 VAL B N   1 
ATOM   8018 C  CA  . VAL B 1 481 ? -42.840 13.841  -10.360  1.00 42.87  ?  479 VAL B CA  1 
ATOM   8019 C  C   . VAL B 1 481 ? -42.060 13.810  -11.666  1.00 40.04  ?  479 VAL B C   1 
ATOM   8020 O  O   . VAL B 1 481 ? -42.207 14.711  -12.500  1.00 36.10  ?  479 VAL B O   1 
ATOM   8021 C  CB  . VAL B 1 481 ? -44.344 13.648  -10.617  1.00 41.42  ?  479 VAL B CB  1 
ATOM   8022 C  CG1 . VAL B 1 481 ? -44.576 12.501  -11.590  1.00 47.34  ?  479 VAL B CG1 1 
ATOM   8023 C  CG2 . VAL B 1 481 ? -45.071 13.383  -9.306   1.00 47.71  ?  479 VAL B CG2 1 
ATOM   8024 N  N   . ILE B 1 482 ? -41.236 12.782  -11.844  1.00 46.46  ?  480 ILE B N   1 
ATOM   8025 C  CA  . ILE B 1 482 ? -40.397 12.641  -13.028  1.00 44.67  ?  480 ILE B CA  1 
ATOM   8026 C  C   . ILE B 1 482 ? -41.064 11.690  -14.010  1.00 40.28  ?  480 ILE B C   1 
ATOM   8027 O  O   . ILE B 1 482 ? -41.398 10.552  -13.661  1.00 43.67  ?  480 ILE B O   1 
ATOM   8028 C  CB  . ILE B 1 482 ? -38.991 12.139  -12.663  1.00 45.86  ?  480 ILE B CB  1 
ATOM   8029 C  CG1 . ILE B 1 482 ? -38.299 13.116  -11.711  1.00 40.52  ?  480 ILE B CG1 1 
ATOM   8030 C  CG2 . ILE B 1 482 ? -38.164 11.914  -13.920  1.00 41.24  ?  480 ILE B CG2 1 
ATOM   8031 C  CD1 . ILE B 1 482 ? -37.003 12.585  -11.141  1.00 48.34  ?  480 ILE B CD1 1 
ATOM   8032 N  N   . THR B 1 483 ? -41.265 12.157  -15.237  1.00 38.85  ?  481 THR B N   1 
ATOM   8033 C  CA  . THR B 1 483 ? -41.751 11.323  -16.322  1.00 44.10  ?  481 THR B CA  1 
ATOM   8034 C  C   . THR B 1 483 ? -40.678 11.282  -17.400  1.00 47.05  ?  481 THR B C   1 
ATOM   8035 O  O   . THR B 1 483 ? -39.837 12.180  -17.502  1.00 39.51  ?  481 THR B O   1 
ATOM   8036 C  CB  . THR B 1 483 ? -43.079 11.835  -16.904  1.00 41.96  ?  481 THR B CB  1 
ATOM   8037 O  OG1 . THR B 1 483 ? -43.007 13.252  -17.106  1.00 44.02  ?  481 THR B OG1 1 
ATOM   8038 C  CG2 . THR B 1 483 ? -44.233 11.508  -15.964  1.00 42.58  ?  481 THR B CG2 1 
ATOM   8039 N  N   . HIS B 1 484 ? -40.704 10.227  -18.202  1.00 50.32  ?  482 HIS B N   1 
ATOM   8040 C  CA  . HIS B 1 484 ? -39.682 10.013  -19.211  1.00 50.77  ?  482 HIS B CA  1 
ATOM   8041 C  C   . HIS B 1 484 ? -40.338 9.817   -20.567  1.00 58.86  ?  482 HIS B C   1 
ATOM   8042 O  O   . HIS B 1 484 ? -41.355 9.128   -20.678  1.00 55.61  ?  482 HIS B O   1 
ATOM   8043 C  CB  . HIS B 1 484 ? -38.822 8.780   -18.886  1.00 56.18  ?  482 HIS B CB  1 
ATOM   8044 C  CG  . HIS B 1 484 ? -38.110 8.862   -17.571  1.00 57.09  ?  482 HIS B CG  1 
ATOM   8045 N  ND1 . HIS B 1 484 ? -36.841 9.384   -17.439  1.00 49.58  ?  482 HIS B ND1 1 
ATOM   8046 C  CD2 . HIS B 1 484 ? -38.480 8.458   -16.333  1.00 50.59  ?  482 HIS B CD2 1 
ATOM   8047 C  CE1 . HIS B 1 484 ? -36.468 9.314   -16.174  1.00 54.59  ?  482 HIS B CE1 1 
ATOM   8048 N  NE2 . HIS B 1 484 ? -37.444 8.754   -15.482  1.00 53.04  ?  482 HIS B NE2 1 
ATOM   8049 N  N   . ASP B 1 485 ? -39.759 10.432  -21.596  1.00 65.78  ?  483 ASP B N   1 
ATOM   8050 C  CA  . ASP B 1 485 ? -40.174 10.196  -22.964  1.00 69.49  ?  483 ASP B CA  1 
ATOM   8051 C  C   . ASP B 1 485 ? -39.071 9.370   -23.631  1.00 67.69  ?  483 ASP B C   1 
ATOM   8052 O  O   . ASP B 1 485 ? -38.327 8.657   -22.934  1.00 74.61  ?  483 ASP B O   1 
ATOM   8053 C  CB  . ASP B 1 485 ? -40.475 11.525  -23.656  1.00 62.55  ?  483 ASP B CB  1 
ATOM   8054 C  CG  . ASP B 1 485 ? -39.368 12.535  -23.493  1.00 63.48  ?  483 ASP B CG  1 
ATOM   8055 O  OD1 . ASP B 1 485 ? -38.235 12.249  -23.934  1.00 70.61  ?  483 ASP B OD1 1 
ATOM   8056 O  OD2 . ASP B 1 485 ? -39.634 13.622  -22.939  1.00 72.26  -1 483 ASP B OD2 1 
ATOM   8057 N  N   . VAL B 1 486 ? -38.954 9.459   -24.953  1.00 69.38  ?  484 VAL B N   1 
ATOM   8058 C  CA  . VAL B 1 486 ? -38.004 8.597   -25.649  1.00 64.38  ?  484 VAL B CA  1 
ATOM   8059 C  C   . VAL B 1 486 ? -36.570 8.939   -25.256  1.00 66.34  ?  484 VAL B C   1 
ATOM   8060 O  O   . VAL B 1 486 ? -35.779 8.051   -24.915  1.00 77.37  ?  484 VAL B O   1 
ATOM   8061 C  CB  . VAL B 1 486 ? -38.213 8.684   -27.171  1.00 68.88  ?  484 VAL B CB  1 
ATOM   8062 C  CG1 . VAL B 1 486 ? -37.158 7.864   -27.894  1.00 64.86  ?  484 VAL B CG1 1 
ATOM   8063 C  CG2 . VAL B 1 486 ? -39.607 8.199   -27.536  1.00 71.41  ?  484 VAL B CG2 1 
ATOM   8064 N  N   . SER B 1 487 ? -36.206 10.225  -25.298  1.00 68.09  ?  485 SER B N   1 
ATOM   8065 C  CA  . SER B 1 487 ? -34.822 10.617  -25.050  1.00 65.27  ?  485 SER B CA  1 
ATOM   8066 C  C   . SER B 1 487 ? -34.650 11.715  -24.003  1.00 67.06  ?  485 SER B C   1 
ATOM   8067 O  O   . SER B 1 487 ? -33.526 12.199  -23.821  1.00 72.51  ?  485 SER B O   1 
ATOM   8068 C  CB  . SER B 1 487 ? -34.154 11.058  -26.359  1.00 73.59  ?  485 SER B CB  1 
ATOM   8069 O  OG  . SER B 1 487 ? -34.802 12.194  -26.905  1.00 84.54  ?  485 SER B OG  1 
ATOM   8070 N  N   . SER B 1 488 ? -35.710 12.133  -23.313  1.00 59.63  ?  486 SER B N   1 
ATOM   8071 C  CA  . SER B 1 488 ? -35.595 13.257  -22.392  1.00 56.29  ?  486 SER B CA  1 
ATOM   8072 C  C   . SER B 1 488 ? -36.408 12.987  -21.130  1.00 50.57  ?  486 SER B C   1 
ATOM   8073 O  O   . SER B 1 488 ? -37.016 11.925  -20.965  1.00 57.30  ?  486 SER B O   1 
ATOM   8074 C  CB  . SER B 1 488 ? -36.037 14.558  -23.076  1.00 52.33  ?  486 SER B CB  1 
ATOM   8075 O  OG  . SER B 1 488 ? -35.843 15.682  -22.233  1.00 49.06  ?  486 SER B OG  1 
ATOM   8076 N  N   . ALA B 1 489 ? -36.412 13.972  -20.231  1.00 46.53  ?  487 ALA B N   1 
ATOM   8077 C  CA  . ALA B 1 489 ? -37.122 13.900  -18.964  1.00 45.67  ?  487 ALA B CA  1 
ATOM   8078 C  C   . ALA B 1 489 ? -38.032 15.111  -18.820  1.00 43.29  ?  487 ALA B C   1 
ATOM   8079 O  O   . ALA B 1 489 ? -37.781 16.172  -19.401  1.00 34.73  ?  487 ALA B O   1 
ATOM   8080 C  CB  . ALA B 1 489 ? -36.155 13.829  -17.773  1.00 37.18  ?  487 ALA B CB  1 
ATOM   8081 N  N   . ILE B 1 490 ? -39.093 14.938  -18.035  1.00 34.19  ?  488 ILE B N   1 
ATOM   8082 C  CA  . ILE B 1 490 ? -40.096 15.970  -17.797  1.00 35.49  ?  488 ILE B CA  1 
ATOM   8083 C  C   . ILE B 1 490 ? -40.460 15.960  -16.318  1.00 37.26  ?  488 ILE B C   1 
ATOM   8084 O  O   . ILE B 1 490 ? -40.542 14.893  -15.700  1.00 38.93  ?  488 ILE B O   1 
ATOM   8085 C  CB  . ILE B 1 490 ? -41.356 15.743  -18.662  1.00 42.09  ?  488 ILE B CB  1 
ATOM   8086 C  CG1 . ILE B 1 490 ? -41.020 15.851  -20.151  1.00 40.57  ?  488 ILE B CG1 1 
ATOM   8087 C  CG2 . ILE B 1 490 ? -42.459 16.721  -18.274  1.00 38.80  ?  488 ILE B CG2 1 
ATOM   8088 C  CD1 . ILE B 1 490 ? -42.191 15.532  -21.060  1.00 46.08  ?  488 ILE B CD1 1 
ATOM   8089 N  N   . ASN B 1 491 ? -40.651 17.150  -15.739  1.00 31.56  ?  489 ASN B N   1 
ATOM   8090 C  CA  . ASN B 1 491 ? -41.100 17.276  -14.346  1.00 40.17  ?  489 ASN B CA  1 
ATOM   8091 C  C   . ASN B 1 491 ? -42.194 18.344  -14.301  1.00 37.27  ?  489 ASN B C   1 
ATOM   8092 O  O   . ASN B 1 491 ? -41.921 19.521  -14.048  1.00 37.11  ?  489 ASN B O   1 
ATOM   8093 C  CB  . ASN B 1 491 ? -39.957 17.608  -13.395  1.00 33.61  ?  489 ASN B CB  1 
ATOM   8094 C  CG  . ASN B 1 491 ? -40.293 17.266  -11.947  1.00 34.17  ?  489 ASN B CG  1 
ATOM   8095 O  OD1 . ASN B 1 491 ? -41.353 17.636  -11.439  1.00 34.68  ?  489 ASN B OD1 1 
ATOM   8096 N  ND2 . ASN B 1 491 ? -39.388 16.560  -11.278  1.00 33.07  ?  489 ASN B ND2 1 
ATOM   8097 N  N   . ARG B 1 492 ? -43.428 17.927  -14.574  1.00 36.09  ?  490 ARG B N   1 
ATOM   8098 C  CA  . ARG B 1 492 ? -44.540 18.873  -14.606  1.00 33.77  ?  490 ARG B CA  1 
ATOM   8099 C  C   . ARG B 1 492 ? -44.795 19.518  -13.248  1.00 30.85  ?  490 ARG B C   1 
ATOM   8100 O  O   . ARG B 1 492 ? -45.062 20.731  -13.214  1.00 32.66  ?  490 ARG B O   1 
ATOM   8101 C  CB  . ARG B 1 492 ? -45.780 18.160  -15.162  1.00 34.03  ?  490 ARG B CB  1 
ATOM   8102 C  CG  . ARG B 1 492 ? -45.590 17.872  -16.646  1.00 46.99  ?  490 ARG B CG  1 
ATOM   8103 C  CD  . ARG B 1 492 ? -46.759 17.230  -17.378  1.00 51.72  ?  490 ARG B CD  1 
ATOM   8104 N  NE  . ARG B 1 492 ? -46.392 17.121  -18.786  1.00 58.05  ?  490 ARG B NE  1 
ATOM   8105 C  CZ  . ARG B 1 492 ? -47.134 16.580  -19.741  1.00 62.82  ?  490 ARG B CZ  1 
ATOM   8106 N  NH1 . ARG B 1 492 ? -48.391 16.227  -19.526  1.00 82.02  ?  490 ARG B NH1 1 
ATOM   8107 N  NH2 . ARG B 1 492 ? -46.615 16.433  -20.958  1.00 67.54  ?  490 ARG B NH2 1 
ATOM   8108 N  N   . PRO B 1 493 ? -44.745 18.798  -12.123  1.00 32.10  ?  491 PRO B N   1 
ATOM   8109 C  CA  . PRO B 1 493 ? -44.877 19.474  -10.818  1.00 32.92  ?  491 PRO B CA  1 
ATOM   8110 C  C   . PRO B 1 493 ? -43.920 20.647  -10.649  1.00 34.12  ?  491 PRO B C   1 
ATOM   8111 O  O   . PRO B 1 493 ? -44.337 21.717  -10.188  1.00 36.74  ?  491 PRO B O   1 
ATOM   8112 C  CB  . PRO B 1 493 ? -44.616 18.335  -9.825   1.00 38.00  ?  491 PRO B CB  1 
ATOM   8113 C  CG  . PRO B 1 493 ? -45.111 17.121  -10.563  1.00 39.23  ?  491 PRO B CG  1 
ATOM   8114 C  CD  . PRO B 1 493 ? -44.610 17.340  -11.964  1.00 35.90  ?  491 PRO B CD  1 
ATOM   8115 N  N   . GLN B 1 494 ? -42.639 20.479  -10.997  1.00 37.16  ?  492 GLN B N   1 
ATOM   8116 C  CA  . GLN B 1 494 ? -41.706 21.585  -10.817  1.00 35.79  ?  492 GLN B CA  1 
ATOM   8117 C  C   . GLN B 1 494 ? -42.125 22.771  -11.667  1.00 33.17  ?  492 GLN B C   1 
ATOM   8118 O  O   . GLN B 1 494 ? -41.919 23.926  -11.275  1.00 32.21  ?  492 GLN B O   1 
ATOM   8119 C  CB  . GLN B 1 494 ? -40.280 21.164  -11.180  1.00 31.26  ?  492 GLN B CB  1 
ATOM   8120 C  CG  . GLN B 1 494 ? -39.560 20.326  -10.136  1.00 28.98  ?  492 GLN B CG  1 
ATOM   8121 C  CD  . GLN B 1 494 ? -38.141 19.982  -10.548  1.00 33.27  ?  492 GLN B CD  1 
ATOM   8122 O  OE1 . GLN B 1 494 ? -37.698 20.317  -11.653  1.00 28.71  ?  492 GLN B OE1 1 
ATOM   8123 N  NE2 . GLN B 1 494 ? -37.413 19.325  -9.654   1.00 27.17  ?  492 GLN B NE2 1 
ATOM   8124 N  N   . ILE B 1 495 ? -42.711 22.502  -12.834  1.00 34.78  ?  493 ILE B N   1 
ATOM   8125 C  CA  . ILE B 1 495 ? -43.261 23.573  -13.652  1.00 36.29  ?  493 ILE B CA  1 
ATOM   8126 C  C   . ILE B 1 495 ? -44.477 24.182  -12.966  1.00 31.55  ?  493 ILE B C   1 
ATOM   8127 O  O   . ILE B 1 495 ? -44.670 25.403  -12.980  1.00 33.77  ?  493 ILE B O   1 
ATOM   8128 C  CB  . ILE B 1 495 ? -43.592 23.045  -15.058  1.00 35.54  ?  493 ILE B CB  1 
ATOM   8129 C  CG1 . ILE B 1 495 ? -42.296 22.689  -15.794  1.00 34.14  ?  493 ILE B CG1 1 
ATOM   8130 C  CG2 . ILE B 1 495 ? -44.404 24.067  -15.834  1.00 36.63  ?  493 ILE B CG2 1 
ATOM   8131 C  CD1 . ILE B 1 495 ? -42.506 22.055  -17.151  1.00 38.33  ?  493 ILE B CD1 1 
ATOM   8132 N  N   . GLY B 1 496 ? -45.298 23.350  -12.327  1.00 33.05  ?  494 GLY B N   1 
ATOM   8133 C  CA  . GLY B 1 496 ? -46.416 23.891  -11.576  1.00 32.69  ?  494 GLY B CA  1 
ATOM   8134 C  C   . GLY B 1 496 ? -45.949 24.843  -10.494  1.00 32.42  ?  494 GLY B C   1 
ATOM   8135 O  O   . GLY B 1 496 ? -46.553 25.896  -10.274  1.00 37.17  ?  494 GLY B O   1 
ATOM   8136 N  N   . VAL B 1 497 ? -44.855 24.495  -9.815   1.00 31.49  ?  495 VAL B N   1 
ATOM   8137 C  CA  . VAL B 1 497 ? -44.320 25.380  -8.787   1.00 36.37  ?  495 VAL B CA  1 
ATOM   8138 C  C   . VAL B 1 497 ? -43.966 26.728  -9.395   1.00 36.17  ?  495 VAL B C   1 
ATOM   8139 O  O   . VAL B 1 497 ? -44.232 27.782  -8.803   1.00 32.75  ?  495 VAL B O   1 
ATOM   8140 C  CB  . VAL B 1 497 ? -43.123 24.721  -8.079   1.00 40.25  ?  495 VAL B CB  1 
ATOM   8141 C  CG1 . VAL B 1 497 ? -42.347 25.748  -7.281   1.00 31.66  ?  495 VAL B CG1 1 
ATOM   8142 C  CG2 . VAL B 1 497 ? -43.621 23.608  -7.157   1.00 36.82  ?  495 VAL B CG2 1 
ATOM   8143 N  N   . VAL B 1 498 ? -43.380 26.722  -10.597  1.00 34.17  ?  496 VAL B N   1 
ATOM   8144 C  CA  . VAL B 1 498 ? -42.973 27.980  -11.211  1.00 30.78  ?  496 VAL B CA  1 
ATOM   8145 C  C   . VAL B 1 498 ? -44.205 28.811  -11.542  1.00 35.23  ?  496 VAL B C   1 
ATOM   8146 O  O   . VAL B 1 498 ? -44.230 30.027  -11.316  1.00 41.78  ?  496 VAL B O   1 
ATOM   8147 C  CB  . VAL B 1 498 ? -42.100 27.723  -12.454  1.00 30.24  ?  496 VAL B CB  1 
ATOM   8148 C  CG1 . VAL B 1 498 ? -41.743 29.036  -13.133  1.00 36.94  ?  496 VAL B CG1 1 
ATOM   8149 C  CG2 . VAL B 1 498 ? -40.839 26.958  -12.064  1.00 24.38  ?  496 VAL B CG2 1 
ATOM   8150 N  N   . ARG B 1 499 ? -45.253 28.167  -12.065  1.00 36.25  ?  497 ARG B N   1 
ATOM   8151 C  CA  . ARG B 1 499 ? -46.449 28.905  -12.451  1.00 33.39  ?  497 ARG B CA  1 
ATOM   8152 C  C   . ARG B 1 499 ? -47.001 29.669  -11.257  1.00 37.98  ?  497 ARG B C   1 
ATOM   8153 O  O   . ARG B 1 499 ? -47.376 30.840  -11.375  1.00 41.67  ?  497 ARG B O   1 
ATOM   8154 C  CB  . ARG B 1 499 ? -47.499 27.950  -13.019  1.00 34.12  ?  497 ARG B CB  1 
ATOM   8155 C  CG  . ARG B 1 499 ? -48.772 28.628  -13.507  1.00 36.82  ?  497 ARG B CG  1 
ATOM   8156 C  CD  . ARG B 1 499 ? -49.634 27.662  -14.305  1.00 55.59  ?  497 ARG B CD  1 
ATOM   8157 N  NE  . ARG B 1 499 ? -49.834 26.408  -13.587  1.00 73.20  ?  497 ARG B NE  1 
ATOM   8158 C  CZ  . ARG B 1 499 ? -50.499 25.363  -14.064  1.00 81.03  ?  497 ARG B CZ  1 
ATOM   8159 N  NH1 . ARG B 1 499 ? -51.039 25.379  -15.273  1.00 67.97  ?  497 ARG B NH1 1 
ATOM   8160 N  NH2 . ARG B 1 499 ? -50.617 24.272  -13.312  1.00 76.39  ?  497 ARG B NH2 1 
ATOM   8161 N  N   . GLU B 1 500 ? -47.053 29.016  -10.091  1.00 41.42  ?  498 GLU B N   1 
ATOM   8162 C  CA  . GLU B 1 500 ? -47.558 29.679  -8.894   1.00 46.15  ?  498 GLU B CA  1 
ATOM   8163 C  C   . GLU B 1 500 ? -46.638 30.824  -8.498   1.00 47.75  ?  498 GLU B C   1 
ATOM   8164 O  O   . GLU B 1 500 ? -47.107 31.903  -8.119   1.00 52.74  ?  498 GLU B O   1 
ATOM   8165 C  CB  . GLU B 1 500 ? -47.704 28.678  -7.749   1.00 45.00  ?  498 GLU B CB  1 
ATOM   8166 C  CG  . GLU B 1 500 ? -48.495 29.206  -6.567   1.00 57.73  ?  498 GLU B CG  1 
ATOM   8167 C  CD  . GLU B 1 500 ? -49.870 29.717  -6.964   1.00 74.48  ?  498 GLU B CD  1 
ATOM   8168 O  OE1 . GLU B 1 500 ? -50.681 28.911  -7.470   1.00 75.28  ?  498 GLU B OE1 1 
ATOM   8169 O  OE2 . GLU B 1 500 ? -50.142 30.922  -6.769   1.00 78.72  -1 498 GLU B OE2 1 
ATOM   8170 N  N   . PHE B 1 501 ? -45.321 30.595  -8.551   1.00 45.23  ?  499 PHE B N   1 
ATOM   8171 C  CA  . PHE B 1 501 ? -44.377 31.651  -8.205   1.00 46.31  ?  499 PHE B CA  1 
ATOM   8172 C  C   . PHE B 1 501 ? -44.585 32.851  -9.116   1.00 46.32  ?  499 PHE B C   1 
ATOM   8173 O  O   . PHE B 1 501 ? -44.544 34.002  -8.665   1.00 46.91  ?  499 PHE B O   1 
ATOM   8174 C  CB  . PHE B 1 501 ? -42.944 31.121  -8.308   1.00 43.50  ?  499 PHE B CB  1 
ATOM   8175 C  CG  . PHE B 1 501 ? -41.881 32.177  -8.154   1.00 42.55  ?  499 PHE B CG  1 
ATOM   8176 C  CD1 . PHE B 1 501 ? -41.370 32.491  -6.906   1.00 43.54  ?  499 PHE B CD1 1 
ATOM   8177 C  CD2 . PHE B 1 501 ? -41.375 32.836  -9.263   1.00 46.33  ?  499 PHE B CD2 1 
ATOM   8178 C  CE1 . PHE B 1 501 ? -40.386 33.454  -6.764   1.00 47.72  ?  499 PHE B CE1 1 
ATOM   8179 C  CE2 . PHE B 1 501 ? -40.390 33.801  -9.128   1.00 44.32  ?  499 PHE B CE2 1 
ATOM   8180 C  CZ  . PHE B 1 501 ? -39.895 34.109  -7.878   1.00 43.45  ?  499 PHE B CZ  1 
ATOM   8181 N  N   . LEU B 1 502 ? -44.832 32.597  -10.404  1.00 44.62  ?  500 LEU B N   1 
ATOM   8182 C  CA  . LEU B 1 502 ? -45.042 33.686  -11.348  1.00 46.67  ?  500 LEU B CA  1 
ATOM   8183 C  C   . LEU B 1 502 ? -46.342 34.405  -11.030  1.00 53.29  ?  500 LEU B C   1 
ATOM   8184 O  O   . LEU B 1 502 ? -46.443 35.629  -11.182  1.00 56.69  ?  500 LEU B O   1 
ATOM   8185 C  CB  . LEU B 1 502 ? -45.066 33.149  -12.779  1.00 36.14  ?  500 LEU B CB  1 
ATOM   8186 C  CG  . LEU B 1 502 ? -43.727 32.828  -13.443  1.00 47.14  ?  500 LEU B CG  1 
ATOM   8187 C  CD1 . LEU B 1 502 ? -43.947 32.328  -14.862  1.00 45.33  ?  500 LEU B CD1 1 
ATOM   8188 C  CD2 . LEU B 1 502 ? -42.830 34.052  -13.442  1.00 41.21  ?  500 LEU B CD2 1 
ATOM   8189 N  N   . THR B 1 503 ? -47.346 33.653  -10.576  1.00 51.27  ?  501 THR B N   1 
ATOM   8190 C  CA  . THR B 1 503 ? -48.637 34.249  -10.270  1.00 49.27  ?  501 THR B CA  1 
ATOM   8191 C  C   . THR B 1 503 ? -48.512 35.188  -9.078   1.00 50.53  ?  501 THR B C   1 
ATOM   8192 O  O   . THR B 1 503 ? -49.152 36.245  -9.040   1.00 54.42  ?  501 THR B O   1 
ATOM   8193 C  CB  . THR B 1 503 ? -49.670 33.151  -10.012  1.00 52.48  ?  501 THR B CB  1 
ATOM   8194 O  OG1 . THR B 1 503 ? -50.032 32.541  -11.258  1.00 60.74  ?  501 THR B OG1 1 
ATOM   8195 C  CG2 . THR B 1 503 ? -50.916 33.732  -9.377   1.00 52.93  ?  501 THR B CG2 1 
ATOM   8196 N  N   . ARG B 1 504 ? -47.684 34.821  -8.097   1.00 51.17  ?  502 ARG B N   1 
ATOM   8197 C  CA  . ARG B 1 504 ? -47.478 35.637  -6.908   1.00 55.22  ?  502 ARG B CA  1 
ATOM   8198 C  C   . ARG B 1 504 ? -46.345 36.638  -7.088   1.00 55.29  ?  502 ARG B C   1 
ATOM   8199 O  O   . ARG B 1 504 ? -46.157 37.502  -6.224   1.00 57.78  ?  502 ARG B O   1 
ATOM   8200 C  CB  . ARG B 1 504 ? -47.143 34.758  -5.695   1.00 60.21  ?  502 ARG B CB  1 
ATOM   8201 C  CG  . ARG B 1 504 ? -48.153 33.688  -5.319   1.00 63.97  ?  502 ARG B CG  1 
ATOM   8202 C  CD  . ARG B 1 504 ? -47.640 32.936  -4.093   1.00 70.06  ?  502 ARG B CD  1 
ATOM   8203 N  NE  . ARG B 1 504 ? -48.251 31.624  -3.918   1.00 81.06  ?  502 ARG B NE  1 
ATOM   8204 C  CZ  . ARG B 1 504 ? -49.540 31.407  -3.698   1.00 73.47  ?  502 ARG B CZ  1 
ATOM   8205 N  NH1 . ARG B 1 504 ? -50.353 32.384  -3.333   1.00 81.55  ?  502 ARG B NH1 1 
ATOM   8206 N  NH2 . ARG B 1 504 ? -50.007 30.162  -3.764   1.00 82.72  ?  502 ARG B NH2 1 
ATOM   8207 N  N   . ASN B 1 505 ? -45.604 36.550  -8.194   1.00 48.52  ?  503 ASN B N   1 
ATOM   8208 C  CA  . ASN B 1 505 ? -44.447 37.410  -8.456   1.00 52.15  ?  503 ASN B CA  1 
ATOM   8209 C  C   . ASN B 1 505 ? -44.431 37.760  -9.939   1.00 52.05  ?  503 ASN B C   1 
ATOM   8210 O  O   . ASN B 1 505 ? -43.499 37.414  -10.669  1.00 43.93  ?  503 ASN B O   1 
ATOM   8211 C  CB  . ASN B 1 505 ? -43.148 36.718  -8.041   1.00 50.13  ?  503 ASN B CB  1 
ATOM   8212 C  CG  . ASN B 1 505 ? -43.033 36.531  -6.539   1.00 57.79  ?  503 ASN B CG  1 
ATOM   8213 O  OD1 . ASN B 1 505 ? -42.811 37.488  -5.797   1.00 60.46  ?  503 ASN B OD1 1 
ATOM   8214 N  ND2 . ASN B 1 505 ? -43.176 35.291  -6.086   1.00 53.79  ?  503 ASN B ND2 1 
ATOM   8215 N  N   . PRO B 1 506 ? -45.458 38.470  -10.413  1.00 51.60  ?  504 PRO B N   1 
ATOM   8216 C  CA  . PRO B 1 506 ? -45.595 38.701  -11.861  1.00 53.42  ?  504 PRO B CA  1 
ATOM   8217 C  C   . PRO B 1 506 ? -44.400 39.370  -12.517  1.00 56.33  ?  504 PRO B C   1 
ATOM   8218 O  O   . PRO B 1 506 ? -44.257 39.265  -13.741  1.00 56.89  ?  504 PRO B O   1 
ATOM   8219 C  CB  . PRO B 1 506 ? -46.850 39.581  -11.948  1.00 54.87  ?  504 PRO B CB  1 
ATOM   8220 C  CG  . PRO B 1 506 ? -46.910 40.246  -10.598  1.00 58.13  ?  504 PRO B CG  1 
ATOM   8221 C  CD  . PRO B 1 506 ? -46.541 39.129  -9.668   1.00 55.06  ?  504 PRO B CD  1 
ATOM   8222 N  N   . ALA B 1 507 ? -43.535 40.052  -11.764  1.00 58.86  ?  505 ALA B N   1 
ATOM   8223 C  CA  . ALA B 1 507 ? -42.411 40.711  -12.415  1.00 54.45  ?  505 ALA B CA  1 
ATOM   8224 C  C   . ALA B 1 507 ? -41.462 39.701  -13.040  1.00 56.04  ?  505 ALA B C   1 
ATOM   8225 O  O   . ALA B 1 507 ? -40.708 40.053  -13.953  1.00 54.70  ?  505 ALA B O   1 
ATOM   8226 C  CB  . ALA B 1 507 ? -41.657 41.593  -11.420  1.00 51.82  ?  505 ALA B CB  1 
ATOM   8227 N  N   . TRP B 1 508 ? -41.497 38.452  -12.583  1.00 50.49  ?  506 TRP B N   1 
ATOM   8228 C  CA  . TRP B 1 508 ? -40.587 37.430  -13.072  1.00 47.98  ?  506 TRP B CA  1 
ATOM   8229 C  C   . TRP B 1 508 ? -41.026 36.865  -14.415  1.00 44.87  ?  506 TRP B C   1 
ATOM   8230 O  O   . TRP B 1 508 ? -40.442 35.880  -14.876  1.00 41.19  ?  506 TRP B O   1 
ATOM   8231 C  CB  . TRP B 1 508 ? -40.459 36.314  -12.030  1.00 41.42  ?  506 TRP B CB  1 
ATOM   8232 C  CG  . TRP B 1 508 ? -39.521 36.652  -10.906  1.00 42.05  ?  506 TRP B CG  1 
ATOM   8233 C  CD1 . TRP B 1 508 ? -39.765 37.488  -9.854   1.00 41.93  ?  506 TRP B CD1 1 
ATOM   8234 C  CD2 . TRP B 1 508 ? -38.216 36.098  -10.682  1.00 33.05  ?  506 TRP B CD2 1 
ATOM   8235 N  NE1 . TRP B 1 508 ? -38.676 37.525  -9.017   1.00 42.31  ?  506 TRP B NE1 1 
ATOM   8236 C  CE2 . TRP B 1 508 ? -37.715 36.676  -9.498   1.00 34.69  ?  506 TRP B CE2 1 
ATOM   8237 C  CE3 . TRP B 1 508 ? -37.420 35.182  -11.374  1.00 31.88  ?  506 TRP B CE3 1 
ATOM   8238 C  CZ2 . TRP B 1 508 ? -36.454 36.369  -8.994   1.00 40.07  ?  506 TRP B CZ2 1 
ATOM   8239 C  CZ3 . TRP B 1 508 ? -36.166 34.878  -10.872  1.00 36.95  ?  506 TRP B CZ3 1 
ATOM   8240 C  CH2 . TRP B 1 508 ? -35.695 35.471  -9.695   1.00 33.25  ?  506 TRP B CH2 1 
ATOM   8241 N  N   . ARG B 1 509 ? -42.019 37.485  -15.059  1.00 48.80  ?  507 ARG B N   1 
ATOM   8242 C  CA  . ARG B 1 509 ? -42.507 37.013  -16.347  1.00 49.32  ?  507 ARG B CA  1 
ATOM   8243 C  C   . ARG B 1 509 ? -41.598 37.447  -17.484  1.00 52.92  ?  507 ARG B C   1 
ATOM   8244 O  O   . ARG B 1 509 ? -41.845 37.077  -18.637  1.00 46.94  ?  507 ARG B O   1 
ATOM   8245 C  CB  . ARG B 1 509 ? -43.938 37.503  -16.605  1.00 58.05  ?  507 ARG B CB  1 
ATOM   8246 C  CG  . ARG B 1 509 ? -44.065 38.997  -16.855  1.00 63.62  ?  507 ARG B CG  1 
ATOM   8247 C  CD  . ARG B 1 509 ? -45.500 39.387  -17.209  1.00 76.79  ?  507 ARG B CD  1 
ATOM   8248 N  NE  . ARG B 1 509 ? -46.470 38.964  -16.205  1.00 78.15  ?  507 ARG B NE  1 
ATOM   8249 C  CZ  . ARG B 1 509 ? -47.777 39.175  -16.291  1.00 74.04  ?  507 ARG B CZ  1 
ATOM   8250 N  NH1 . ARG B 1 509 ? -48.321 39.713  -17.371  1.00 73.57  ?  507 ARG B NH1 1 
ATOM   8251 N  NH2 . ARG B 1 509 ? -48.561 38.810  -15.281  1.00 74.28  ?  507 ARG B NH2 1 
ATOM   8252 N  N   . LYS B 1 510 ? -40.559 38.226  -17.180  1.00 54.05  ?  508 LYS B N   1 
ATOM   8253 C  CA  . LYS B 1 510 ? -39.558 38.630  -18.154  1.00 50.06  ?  508 LYS B CA  1 
ATOM   8254 C  C   . LYS B 1 510 ? -38.324 37.747  -18.060  1.00 47.45  ?  508 LYS B C   1 
ATOM   8255 O  O   . LYS B 1 510 ? -37.253 38.116  -18.553  1.00 54.83  ?  508 LYS B O   1 
ATOM   8256 C  CB  . LYS B 1 510 ? -39.179 40.103  -17.963  1.00 57.57  ?  508 LYS B CB  1 
ATOM   8257 C  CG  . LYS B 1 510 ? -38.717 40.486  -16.554  1.00 57.71  ?  508 LYS B CG  1 
ATOM   8258 C  CD  . LYS B 1 510 ? -38.420 41.986  -16.471  1.00 63.99  ?  508 LYS B CD  1 
ATOM   8259 C  CE  . LYS B 1 510 ? -38.051 42.435  -15.059  1.00 72.76  ?  508 LYS B CE  1 
ATOM   8260 N  NZ  . LYS B 1 510 ? -39.160 42.251  -14.080  1.00 75.52  ?  508 LYS B NZ  1 
ATOM   8261 N  N   . ALA B 1 511 ? -38.464 36.581  -17.442  1.00 38.23  ?  509 ALA B N   1 
ATOM   8262 C  CA  . ALA B 1 511 ? -37.359 35.671  -17.209  1.00 43.95  ?  509 ALA B CA  1 
ATOM   8263 C  C   . ALA B 1 511 ? -37.226 34.667  -18.346  1.00 42.96  ?  509 ALA B C   1 
ATOM   8264 O  O   . ALA B 1 511 ? -38.122 34.488  -19.176  1.00 35.29  ?  509 ALA B O   1 
ATOM   8265 C  CB  . ALA B 1 511 ? -37.545 34.931  -15.884  1.00 39.23  ?  509 ALA B CB  1 
ATOM   8266 N  N   . VAL B 1 512 ? -36.083 33.995  -18.360  1.00 37.91  ?  510 VAL B N   1 
ATOM   8267 C  CA  . VAL B 1 512 ? -35.813 32.900  -19.277  1.00 36.10  ?  510 VAL B CA  1 
ATOM   8268 C  C   . VAL B 1 512 ? -35.911 31.616  -18.473  1.00 27.85  ?  510 VAL B C   1 
ATOM   8269 O  O   . VAL B 1 512 ? -35.420 31.546  -17.340  1.00 33.85  ?  510 VAL B O   1 
ATOM   8270 C  CB  . VAL B 1 512 ? -34.428 33.037  -19.938  1.00 37.99  ?  510 VAL B CB  1 
ATOM   8271 C  CG1 . VAL B 1 512 ? -34.128 31.820  -20.798  1.00 40.01  ?  510 VAL B CG1 1 
ATOM   8272 C  CG2 . VAL B 1 512 ? -34.361 34.309  -20.766  1.00 41.87  ?  510 VAL B CG2 1 
ATOM   8273 N  N   . PHE B 1 513 ? -36.561 30.610  -19.047  1.00 29.80  ?  511 PHE B N   1 
ATOM   8274 C  CA  . PHE B 1 513 ? -36.676 29.311  -18.402  1.00 31.48  ?  511 PHE B CA  1 
ATOM   8275 C  C   . PHE B 1 513 ? -35.535 28.421  -18.877  1.00 30.35  ?  511 PHE B C   1 
ATOM   8276 O  O   . PHE B 1 513 ? -35.314 28.274  -20.085  1.00 26.77  ?  511 PHE B O   1 
ATOM   8277 C  CB  . PHE B 1 513 ? -38.028 28.667  -18.712  1.00 30.06  ?  511 PHE B CB  1 
ATOM   8278 C  CG  . PHE B 1 513 ? -38.204 27.324  -18.080  1.00 29.15  ?  511 PHE B CG  1 
ATOM   8279 C  CD1 . PHE B 1 513 ? -37.727 26.184  -18.701  1.00 27.84  ?  511 PHE B CD1 1 
ATOM   8280 C  CD2 . PHE B 1 513 ? -38.833 27.201  -16.852  1.00 28.37  ?  511 PHE B CD2 1 
ATOM   8281 C  CE1 . PHE B 1 513 ? -37.874 24.948  -18.114  1.00 27.85  ?  511 PHE B CE1 1 
ATOM   8282 C  CE2 . PHE B 1 513 ? -38.985 25.967  -16.264  1.00 28.04  ?  511 PHE B CE2 1 
ATOM   8283 C  CZ  . PHE B 1 513 ? -38.507 24.837  -16.894  1.00 25.90  ?  511 PHE B CZ  1 
ATOM   8284 N  N   . ILE B 1 514 ? -34.780 27.873  -17.928  1.00 22.87  ?  512 ILE B N   1 
ATOM   8285 C  CA  . ILE B 1 514 ? -33.667 26.978  -18.223  1.00 29.47  ?  512 ILE B CA  1 
ATOM   8286 C  C   . ILE B 1 514 ? -33.852 25.652  -17.491  1.00 33.33  ?  512 ILE B C   1 
ATOM   8287 O  O   . ILE B 1 514 ? -34.206 25.633  -16.305  1.00 33.34  ?  512 ILE B O   1 
ATOM   8288 C  CB  . ILE B 1 514 ? -32.320 27.630  -17.860  1.00 29.18  ?  512 ILE B CB  1 
ATOM   8289 C  CG1 . ILE B 1 514 ? -32.173 28.963  -18.601  1.00 30.56  ?  512 ILE B CG1 1 
ATOM   8290 C  CG2 . ILE B 1 514 ? -31.170 26.691  -18.188  1.00 30.18  ?  512 ILE B CG2 1 
ATOM   8291 C  CD1 . ILE B 1 514 ? -30.829 29.657  -18.397  1.00 30.33  ?  512 ILE B CD1 1 
ATOM   8292 N  N   . SER B 1 515 ? -33.689 24.545  -18.224  1.00 32.13  ?  513 SER B N   1 
ATOM   8293 C  CA  . SER B 1 515 ? -33.700 23.202  -17.650  1.00 31.43  ?  513 SER B CA  1 
ATOM   8294 C  C   . SER B 1 515 ? -32.607 22.374  -18.319  1.00 33.57  ?  513 SER B C   1 
ATOM   8295 O  O   . SER B 1 515 ? -32.072 22.786  -19.356  1.00 33.26  ?  513 SER B O   1 
ATOM   8296 C  CB  . SER B 1 515 ? -35.063 22.521  -17.806  1.00 29.70  ?  513 SER B CB  1 
ATOM   8297 O  OG  . SER B 1 515 ? -35.090 21.667  -18.931  1.00 32.67  ?  513 SER B OG  1 
ATOM   8298 N  N   . PRO B 1 516 ? -32.232 21.221  -17.759  1.00 31.13  ?  514 PRO B N   1 
ATOM   8299 C  CA  . PRO B 1 516 ? -31.244 20.361  -18.418  1.00 34.50  ?  514 PRO B CA  1 
ATOM   8300 C  C   . PRO B 1 516 ? -31.825 19.466  -19.507  1.00 38.92  ?  514 PRO B C   1 
ATOM   8301 O  O   . PRO B 1 516 ? -31.074 18.662  -20.070  1.00 36.53  ?  514 PRO B O   1 
ATOM   8302 C  CB  . PRO B 1 516 ? -30.697 19.519  -17.251  1.00 36.51  ?  514 PRO B CB  1 
ATOM   8303 C  CG  . PRO B 1 516 ? -31.293 20.147  -15.991  1.00 35.50  ?  514 PRO B CG  1 
ATOM   8304 C  CD  . PRO B 1 516 ? -32.596 20.678  -16.437  1.00 34.23  ?  514 PRO B CD  1 
ATOM   8305 N  N   . TYR B 1 517 ? -33.132 19.555  -19.800  1.00 40.28  ?  515 TYR B N   1 
ATOM   8306 C  CA  . TYR B 1 517 ? -33.801 18.670  -20.759  1.00 43.16  ?  515 TYR B CA  1 
ATOM   8307 C  C   . TYR B 1 517 ? -34.718 19.461  -21.703  1.00 40.96  ?  515 TYR B C   1 
ATOM   8308 O  O   . TYR B 1 517 ? -35.500 20.303  -21.254  1.00 36.44  ?  515 TYR B O   1 
ATOM   8309 C  CB  . TYR B 1 517 ? -34.624 17.617  -19.994  1.00 37.87  ?  515 TYR B CB  1 
ATOM   8310 C  CG  . TYR B 1 517 ? -33.868 16.702  -19.028  1.00 38.12  ?  515 TYR B CG  1 
ATOM   8311 C  CD1 . TYR B 1 517 ? -33.312 15.506  -19.467  1.00 41.28  ?  515 TYR B CD1 1 
ATOM   8312 C  CD2 . TYR B 1 517 ? -33.752 17.016  -17.671  1.00 35.01  ?  515 TYR B CD2 1 
ATOM   8313 C  CE1 . TYR B 1 517 ? -32.643 14.657  -18.594  1.00 42.76  ?  515 TYR B CE1 1 
ATOM   8314 C  CE2 . TYR B 1 517 ? -33.085 16.171  -16.791  1.00 36.92  ?  515 TYR B CE2 1 
ATOM   8315 C  CZ  . TYR B 1 517 ? -32.534 14.994  -17.259  1.00 41.45  ?  515 TYR B CZ  1 
ATOM   8316 O  OH  . TYR B 1 517 ? -31.875 14.148  -16.397  1.00 48.66  ?  515 TYR B OH  1 
ATOM   8317 N  N   . ASN B 1 518 ? -34.599 19.189  -23.017  1.00 47.11  ?  516 ASN B N   1 
ATOM   8318 C  CA  A ASN B 1 518 ? -35.453 19.803  -24.042  0.58 44.25  ?  516 ASN B CA  1 
ATOM   8319 C  CA  B ASN B 1 518 ? -35.453 19.826  -24.031  0.42 54.53  ?  516 ASN B CA  1 
ATOM   8320 C  C   . ASN B 1 518 ? -36.949 19.552  -23.847  1.00 48.91  ?  516 ASN B C   1 
ATOM   8321 O  O   . ASN B 1 518 ? -37.778 20.422  -24.153  1.00 43.17  ?  516 ASN B O   1 
ATOM   8322 C  CB  A ASN B 1 518 ? -35.050 19.304  -25.427  0.58 58.76  ?  516 ASN B CB  1 
ATOM   8323 C  CB  B ASN B 1 518 ? -34.965 19.470  -25.446  0.42 61.09  ?  516 ASN B CB  1 
ATOM   8324 C  CG  A ASN B 1 518 ? -33.943 20.119  -26.035  0.58 61.49  ?  516 ASN B CG  1 
ATOM   8325 C  CG  B ASN B 1 518 ? -35.266 18.044  -25.856  0.42 60.70  ?  516 ASN B CG  1 
ATOM   8326 O  OD1 A ASN B 1 518 ? -32.851 19.612  -26.288  0.58 63.04  ?  516 ASN B OD1 1 
ATOM   8327 O  OD1 B ASN B 1 518 ? -34.350 17.236  -25.992  0.42 67.53  ?  516 ASN B OD1 1 
ATOM   8328 N  ND2 A ASN B 1 518 ? -34.211 21.399  -26.269  0.58 60.05  ?  516 ASN B ND2 1 
ATOM   8329 N  ND2 B ASN B 1 518 ? -36.537 17.733  -26.091  0.42 60.76  ?  516 ASN B ND2 1 
ATOM   8330 N  N   . SER B 1 519 ? -37.327 18.380  -23.340  1.00 40.54  ?  517 SER B N   1 
ATOM   8331 C  CA  . SER B 1 519 ? -38.752 18.088  -23.147  1.00 42.00  ?  517 SER B CA  1 
ATOM   8332 C  C   . SER B 1 519 ? -39.333 18.905  -22.002  1.00 36.19  ?  517 SER B C   1 
ATOM   8333 O  O   . SER B 1 519 ? -40.443 19.435  -22.118  1.00 38.45  ?  517 SER B O   1 
ATOM   8334 C  CB  . SER B 1 519 ? -38.980 16.592  -22.960  1.00 40.66  ?  517 SER B CB  1 
ATOM   8335 O  OG  . SER B 1 519 ? -38.866 15.928  -24.208  1.00 51.06  ?  517 SER B OG  1 
ATOM   8336 N  N   . GLN B 1 520 ? -38.602 19.034  -20.897  1.00 34.55  ?  518 GLN B N   1 
ATOM   8337 C  CA  . GLN B 1 520 ? -39.074 19.918  -19.839  1.00 37.96  ?  518 GLN B CA  1 
ATOM   8338 C  C   . GLN B 1 520 ? -39.256 21.323  -20.402  1.00 36.88  ?  518 GLN B C   1 
ATOM   8339 O  O   . GLN B 1 520 ? -40.261 21.986  -20.122  1.00 37.94  ?  518 GLN B O   1 
ATOM   8340 C  CB  . GLN B 1 520 ? -38.090 19.931  -18.667  1.00 32.60  ?  518 GLN B CB  1 
ATOM   8341 C  CG  . GLN B 1 520 ? -38.481 20.873  -17.526  1.00 31.49  ?  518 GLN B CG  1 
ATOM   8342 C  CD  . GLN B 1 520 ? -39.448 20.227  -16.545  1.00 32.94  ?  518 GLN B CD  1 
ATOM   8343 O  OE1 . GLN B 1 520 ? -40.397 19.554  -16.943  1.00 35.39  ?  518 GLN B OE1 1 
ATOM   8344 N  NE2 . GLN B 1 520 ? -39.216 20.445  -15.255  1.00 29.23  ?  518 GLN B NE2 1 
ATOM   8345 N  N   . ASN B 1 521 ? -38.301 21.785  -21.214  1.00 34.41  ?  519 ASN B N   1 
ATOM   8346 C  CA  . ASN B 1 521 ? -38.401 23.122  -21.789  1.00 38.50  ?  519 ASN B CA  1 
ATOM   8347 C  C   . ASN B 1 521 ? -39.663 23.251  -22.635  1.00 39.05  ?  519 ASN B C   1 
ATOM   8348 O  O   . ASN B 1 521 ? -40.397 24.240  -22.528  1.00 41.28  ?  519 ASN B O   1 
ATOM   8349 C  CB  . ASN B 1 521 ? -37.169 23.428  -22.643  1.00 34.55  ?  519 ASN B CB  1 
ATOM   8350 C  CG  . ASN B 1 521 ? -35.932 23.671  -21.818  1.00 41.68  ?  519 ASN B CG  1 
ATOM   8351 O  OD1 . ASN B 1 521 ? -35.965 23.602  -20.589  1.00 30.53  ?  519 ASN B OD1 1 
ATOM   8352 N  ND2 . ASN B 1 521 ? -34.827 23.976  -22.490  1.00 30.39  ?  519 ASN B ND2 1 
ATOM   8353 N  N   . ALA B 1 522 ? -39.923 22.265  -23.500  1.00 39.38  ?  520 ALA B N   1 
ATOM   8354 C  CA  . ALA B 1 522 ? -41.100 22.332  -24.360  1.00 41.58  ?  520 ALA B CA  1 
ATOM   8355 C  C   . ALA B 1 522 ? -42.382 22.393  -23.537  1.00 43.88  ?  520 ALA B C   1 
ATOM   8356 O  O   . ALA B 1 522 ? -43.300 23.157  -23.859  1.00 45.42  ?  520 ALA B O   1 
ATOM   8357 C  CB  . ALA B 1 522 ? -41.129 21.136  -25.313  1.00 40.69  ?  520 ALA B CB  1 
ATOM   8358 N  N   . VAL B 1 523 ? -42.477 21.579  -22.482  1.00 43.05  ?  521 VAL B N   1 
ATOM   8359 C  CA  . VAL B 1 523 ? -43.656 21.639  -21.621  1.00 43.33  ?  521 VAL B CA  1 
ATOM   8360 C  C   . VAL B 1 523 ? -43.741 23.001  -20.943  1.00 44.51  ?  521 VAL B C   1 
ATOM   8361 O  O   . VAL B 1 523 ? -44.811 23.619  -20.887  1.00 44.80  ?  521 VAL B O   1 
ATOM   8362 C  CB  . VAL B 1 523 ? -43.625 20.497  -20.587  1.00 41.26  ?  521 VAL B CB  1 
ATOM   8363 C  CG1 . VAL B 1 523 ? -44.820 20.594  -19.647  1.00 40.21  ?  521 VAL B CG1 1 
ATOM   8364 C  CG2 . VAL B 1 523 ? -43.588 19.142  -21.279  1.00 40.78  ?  521 VAL B CG2 1 
ATOM   8365 N  N   . ALA B 1 524 ? -42.605 23.505  -20.449  1.00 42.36  ?  522 ALA B N   1 
ATOM   8366 C  CA  . ALA B 1 524 ? -42.592 24.795  -19.765  1.00 41.70  ?  522 ALA B CA  1 
ATOM   8367 C  C   . ALA B 1 524 ? -42.994 25.922  -20.705  1.00 45.01  ?  522 ALA B C   1 
ATOM   8368 O  O   . ALA B 1 524 ? -43.692 26.860  -20.300  1.00 44.69  ?  522 ALA B O   1 
ATOM   8369 C  CB  . ALA B 1 524 ? -41.210 25.062  -19.172  1.00 37.72  ?  522 ALA B CB  1 
ATOM   8370 N  N   . SER B 1 525 ? -42.552 25.852  -21.962  1.00 45.69  ?  523 SER B N   1 
ATOM   8371 C  CA  . SER B 1 525 ? -42.899 26.882  -22.933  1.00 45.15  ?  523 SER B CA  1 
ATOM   8372 C  C   . SER B 1 525 ? -44.410 27.031  -23.062  1.00 47.47  ?  523 SER B C   1 
ATOM   8373 O  O   . SER B 1 525 ? -44.930 28.152  -23.112  1.00 46.01  ?  523 SER B O   1 
ATOM   8374 C  CB  . SER B 1 525 ? -42.270 26.551  -24.286  1.00 43.76  ?  523 SER B CB  1 
ATOM   8375 O  OG  . SER B 1 525 ? -42.601 27.525  -25.260  1.00 47.03  ?  523 SER B OG  1 
ATOM   8376 N  N   . LYS B 1 526 ? -45.131 25.910  -23.128  1.00 47.42  ?  524 LYS B N   1 
ATOM   8377 C  CA  . LYS B 1 526 ? -46.575 25.971  -23.328  1.00 49.57  ?  524 LYS B CA  1 
ATOM   8378 C  C   . LYS B 1 526 ? -47.300 26.402  -22.057  1.00 47.23  ?  524 LYS B C   1 
ATOM   8379 O  O   . LYS B 1 526 ? -48.276 27.157  -22.122  1.00 49.33  ?  524 LYS B O   1 
ATOM   8380 C  CB  . LYS B 1 526 ? -47.093 24.616  -23.811  1.00 48.75  ?  524 LYS B CB  1 
ATOM   8381 N  N   . ILE B 1 527 ? -46.832 25.950  -20.892  1.00 45.86  ?  525 ILE B N   1 
ATOM   8382 C  CA  . ILE B 1 527 ? -47.549 26.220  -19.649  1.00 46.71  ?  525 ILE B CA  1 
ATOM   8383 C  C   . ILE B 1 527 ? -47.234 27.612  -19.113  1.00 44.50  ?  525 ILE B C   1 
ATOM   8384 O  O   . ILE B 1 527 ? -48.113 28.286  -18.567  1.00 42.31  ?  525 ILE B O   1 
ATOM   8385 C  CB  . ILE B 1 527 ? -47.234 25.133  -18.604  1.00 45.15  ?  525 ILE B CB  1 
ATOM   8386 C  CG1 . ILE B 1 527 ? -47.701 23.762  -19.097  1.00 46.28  ?  525 ILE B CG1 1 
ATOM   8387 C  CG2 . ILE B 1 527 ? -47.872 25.476  -17.264  1.00 40.53  ?  525 ILE B CG2 1 
ATOM   8388 C  CD1 . ILE B 1 527 ? -47.575 22.666  -18.059  1.00 45.04  ?  525 ILE B CD1 1 
ATOM   8389 N  N   . LEU B 1 528 ? -45.992 28.072  -19.270  1.00 46.68  ?  526 LEU B N   1 
ATOM   8390 C  CA  . LEU B 1 528 ? -45.541 29.324  -18.673  1.00 41.24  ?  526 LEU B CA  1 
ATOM   8391 C  C   . LEU B 1 528 ? -45.390 30.465  -19.664  1.00 41.67  ?  526 LEU B C   1 
ATOM   8392 O  O   . LEU B 1 528 ? -45.476 31.626  -19.261  1.00 43.60  ?  526 LEU B O   1 
ATOM   8393 C  CB  . LEU B 1 528 ? -44.199 29.129  -17.952  1.00 39.31  ?  526 LEU B CB  1 
ATOM   8394 C  CG  . LEU B 1 528 ? -44.062 27.983  -16.949  1.00 39.79  ?  526 LEU B CG  1 
ATOM   8395 C  CD1 . LEU B 1 528 ? -42.627 27.894  -16.438  1.00 35.90  ?  526 LEU B CD1 1 
ATOM   8396 C  CD2 . LEU B 1 528 ? -45.038 28.155  -15.795  1.00 39.58  ?  526 LEU B CD2 1 
ATOM   8397 N  N   . GLY B 1 529 ? -45.141 30.172  -20.937  1.00 43.06  ?  527 GLY B N   1 
ATOM   8398 C  CA  . GLY B 1 529 ? -44.991 31.214  -21.930  1.00 42.60  ?  527 GLY B CA  1 
ATOM   8399 C  C   . GLY B 1 529 ? -43.670 31.942  -21.884  1.00 40.55  ?  527 GLY B C   1 
ATOM   8400 O  O   . GLY B 1 529 ? -43.510 32.956  -22.571  1.00 41.02  ?  527 GLY B O   1 
ATOM   8401 N  N   . LEU B 1 530 ? -42.761 31.481  -21.134  1.00 39.54  ?  528 LEU B N   1 
ATOM   8402 C  CA  . LEU B 1 530 ? -41.447 32.085  -21.029  1.00 41.34  ?  528 LEU B CA  1 
ATOM   8403 C  C   . LEU B 1 530 ? -40.532 31.533  -22.114  1.00 41.09  ?  528 LEU B C   1 
ATOM   8404 O  O   . LEU B 1 530 ? -40.670 30.374  -22.520  1.00 38.22  ?  528 LEU B O   1 
ATOM   8405 C  CB  . LEU B 1 530 ? -40.830 31.786  -19.666  1.00 35.91  ?  528 LEU B CB  1 
ATOM   8406 C  CG  . LEU B 1 530 ? -41.506 32.268  -18.384  1.00 42.43  ?  528 LEU B CG  1 
ATOM   8407 C  CD1 . LEU B 1 530 ? -40.758 31.708  -17.183  1.00 39.17  ?  528 LEU B CD1 1 
ATOM   8408 C  CD2 . LEU B 1 530 ? -41.553 33.784  -18.331  1.00 47.46  ?  528 LEU B CD2 1 
ATOM   8409 N  N   . PRO B 1 531 ? -39.595 32.335  -22.613  1.00 43.43  ?  529 PRO B N   1 
ATOM   8410 C  CA  . PRO B 1 531 ? -38.575 31.781  -23.507  1.00 42.14  ?  529 PRO B CA  1 
ATOM   8411 C  C   . PRO B 1 531 ? -37.817 30.681  -22.780  1.00 35.36  ?  529 PRO B C   1 
ATOM   8412 O  O   . PRO B 1 531 ? -37.603 30.753  -21.568  1.00 37.11  ?  529 PRO B O   1 
ATOM   8413 C  CB  . PRO B 1 531 ? -37.679 32.985  -23.821  1.00 46.95  ?  529 PRO B CB  1 
ATOM   8414 C  CG  . PRO B 1 531 ? -37.968 33.981  -22.731  1.00 52.04  ?  529 PRO B CG  1 
ATOM   8415 C  CD  . PRO B 1 531 ? -39.411 33.777  -22.386  1.00 47.66  ?  529 PRO B CD  1 
ATOM   8416 N  N   . THR B 1 532 ? -37.431 29.646  -23.522  1.00 37.71  ?  530 THR B N   1 
ATOM   8417 C  CA  . THR B 1 532 ? -36.756 28.494  -22.942  1.00 34.92  ?  530 THR B CA  1 
ATOM   8418 C  C   . THR B 1 532 ? -35.383 28.295  -23.565  1.00 41.19  ?  530 THR B C   1 
ATOM   8419 O  O   . THR B 1 532 ? -35.136 28.670  -24.716  1.00 41.25  ?  530 THR B O   1 
ATOM   8420 C  CB  . THR B 1 532 ? -37.571 27.206  -23.114  1.00 32.27  ?  530 THR B CB  1 
ATOM   8421 O  OG1 . THR B 1 532 ? -37.760 26.933  -24.508  1.00 47.44  ?  530 THR B OG1 1 
ATOM   8422 C  CG2 . THR B 1 532 ? -38.924 27.324  -22.421  1.00 37.55  ?  530 THR B CG2 1 
ATOM   8423 N  N   . GLN B 1 533 ? -34.494 27.698  -22.779  1.00 39.94  ?  531 GLN B N   1 
ATOM   8424 C  CA  . GLN B 1 533 ? -33.154 27.346  -23.216  1.00 43.97  ?  531 GLN B CA  1 
ATOM   8425 C  C   . GLN B 1 533 ? -32.665 26.166  -22.395  1.00 34.88  ?  531 GLN B C   1 
ATOM   8426 O  O   . GLN B 1 533 ? -32.897 26.109  -21.182  1.00 36.66  ?  531 GLN B O   1 
ATOM   8427 C  CB  . GLN B 1 533 ? -32.170 28.512  -23.042  1.00 43.44  ?  531 GLN B CB  1 
ATOM   8428 C  CG  . GLN B 1 533 ? -32.345 29.664  -24.007  1.00 43.62  ?  531 GLN B CG  1 
ATOM   8429 C  CD  . GLN B 1 533 ? -31.504 29.505  -25.253  1.00 50.64  ?  531 GLN B CD  1 
ATOM   8430 O  OE1 . GLN B 1 533 ? -30.284 29.356  -25.178  1.00 51.84  ?  531 GLN B OE1 1 
ATOM   8431 N  NE2 . GLN B 1 533 ? -32.150 29.548  -26.410  1.00 47.96  ?  531 GLN B NE2 1 
ATOM   8432 N  N   . THR B 1 534 ? -32.012 25.217  -23.058  1.00 33.09  ?  532 THR B N   1 
ATOM   8433 C  CA  . THR B 1 534 ? -31.307 24.204  -22.296  1.00 40.40  ?  532 THR B CA  1 
ATOM   8434 C  C   . THR B 1 534 ? -30.038 24.836  -21.743  1.00 41.46  ?  532 THR B C   1 
ATOM   8435 O  O   . THR B 1 534 ? -29.544 25.841  -22.262  1.00 40.54  ?  532 THR B O   1 
ATOM   8436 C  CB  . THR B 1 534 ? -30.939 22.996  -23.159  1.00 41.94  ?  532 THR B CB  1 
ATOM   8437 O  OG1 . THR B 1 534 ? -30.071 23.415  -24.218  1.00 42.00  ?  532 THR B OG1 1 
ATOM   8438 C  CG2 . THR B 1 534 ? -32.180 22.353  -23.752  1.00 44.90  ?  532 THR B CG2 1 
ATOM   8439 N  N   . VAL B 1 535 ? -29.501 24.239  -20.680  1.00 38.54  ?  533 VAL B N   1 
ATOM   8440 C  CA  . VAL B 1 535 ? -28.275 24.784  -20.108  1.00 41.29  ?  533 VAL B CA  1 
ATOM   8441 C  C   . VAL B 1 535 ? -27.185 24.859  -21.168  1.00 39.02  ?  533 VAL B C   1 
ATOM   8442 O  O   . VAL B 1 535 ? -26.472 25.864  -21.277  1.00 36.04  ?  533 VAL B O   1 
ATOM   8443 C  CB  . VAL B 1 535 ? -27.822 23.953  -18.896  1.00 36.35  ?  533 VAL B CB  1 
ATOM   8444 C  CG1 . VAL B 1 535 ? -26.649 24.637  -18.211  1.00 35.17  ?  533 VAL B CG1 1 
ATOM   8445 C  CG2 . VAL B 1 535 ? -28.974 23.748  -17.923  1.00 36.92  ?  533 VAL B CG2 1 
ATOM   8446 N  N   . ASP B 1 536 ? -27.049 23.803  -21.976  1.00 40.30  ?  534 ASP B N   1 
ATOM   8447 C  CA  . ASP B 1 536 ? -25.994 23.759  -22.985  1.00 49.29  ?  534 ASP B CA  1 
ATOM   8448 C  C   . ASP B 1 536 ? -26.180 24.833  -24.053  1.00 45.25  ?  534 ASP B C   1 
ATOM   8449 O  O   . ASP B 1 536 ? -25.198 25.394  -24.551  1.00 54.66  ?  534 ASP B O   1 
ATOM   8450 C  CB  . ASP B 1 536 ? -25.931 22.366  -23.614  1.00 48.63  ?  534 ASP B CB  1 
ATOM   8451 C  CG  . ASP B 1 536 ? -25.608 21.279  -22.595  1.00 60.23  ?  534 ASP B CG  1 
ATOM   8452 O  OD1 . ASP B 1 536 ? -26.360 21.134  -21.606  1.00 51.92  ?  534 ASP B OD1 1 
ATOM   8453 O  OD2 . ASP B 1 536 ? -24.596 20.570  -22.782  1.00 69.40  -1 534 ASP B OD2 1 
ATOM   8454 N  N   . SER B 1 537 ? -27.426 25.118  -24.440  1.00 40.32  ?  535 SER B N   1 
ATOM   8455 C  CA  . SER B 1 537 ? -27.658 26.167  -25.426  1.00 46.11  ?  535 SER B CA  1 
ATOM   8456 C  C   . SER B 1 537 ? -27.503 27.561  -24.831  1.00 45.80  ?  535 SER B C   1 
ATOM   8457 O  O   . SER B 1 537 ? -27.241 28.513  -25.575  1.00 40.30  ?  535 SER B O   1 
ATOM   8458 C  CB  . SER B 1 537 ? -29.045 26.012  -26.063  1.00 46.73  ?  535 SER B CB  1 
ATOM   8459 O  OG  . SER B 1 537 ? -30.076 26.377  -25.162  1.00 54.56  ?  535 SER B OG  1 
ATOM   8460 N  N   . SER B 1 538 ? -27.659 27.698  -23.510  1.00 31.94  ?  536 SER B N   1 
ATOM   8461 C  CA  . SER B 1 538 ? -27.579 28.989  -22.835  1.00 29.34  ?  536 SER B CA  1 
ATOM   8462 C  C   . SER B 1 538 ? -26.145 29.479  -22.668  1.00 29.73  ?  536 SER B C   1 
ATOM   8463 O  O   . SER B 1 538 ? -25.939 30.677  -22.446  1.00 31.59  ?  536 SER B O   1 
ATOM   8464 C  CB  . SER B 1 538 ? -28.253 28.924  -21.459  1.00 26.11  ?  536 SER B CB  1 
ATOM   8465 O  OG  . SER B 1 538 ? -27.406 28.299  -20.519  1.00 24.47  ?  536 SER B OG  1 
ATOM   8466 N  N   . GLN B 1 539 ? -25.162 28.579  -22.708  1.00 34.06  ?  537 GLN B N   1 
ATOM   8467 C  CA  . GLN B 1 539 ? -23.770 28.965  -22.494  1.00 38.68  ?  537 GLN B CA  1 
ATOM   8468 C  C   . GLN B 1 539 ? -23.369 30.076  -23.454  1.00 41.95  ?  537 GLN B C   1 
ATOM   8469 O  O   . GLN B 1 539 ? -23.571 29.971  -24.667  1.00 36.35  ?  537 GLN B O   1 
ATOM   8470 C  CB  . GLN B 1 539 ? -22.853 27.752  -22.684  1.00 32.00  ?  537 GLN B CB  1 
ATOM   8471 C  CG  . GLN B 1 539 ? -21.385 28.002  -22.350  1.00 39.75  ?  537 GLN B CG  1 
ATOM   8472 C  CD  . GLN B 1 539 ? -20.584 26.716  -22.229  1.00 42.50  ?  537 GLN B CD  1 
ATOM   8473 O  OE1 . GLN B 1 539 ? -20.744 25.956  -21.276  1.00 40.55  ?  537 GLN B OE1 1 
ATOM   8474 N  NE2 . GLN B 1 539 ? -19.740 26.452  -23.221  1.00 41.24  ?  537 GLN B NE2 1 
ATOM   8475 N  N   . GLY B 1 540 ? -22.805 31.148  -22.900  1.00 40.10  ?  538 GLY B N   1 
ATOM   8476 C  CA  . GLY B 1 540 ? -22.398 32.302  -23.669  1.00 50.71  ?  538 GLY B CA  1 
ATOM   8477 C  C   . GLY B 1 540 ? -23.401 33.436  -23.666  1.00 52.28  ?  538 GLY B C   1 
ATOM   8478 O  O   . GLY B 1 540 ? -23.061 34.543  -24.104  1.00 41.61  ?  538 GLY B O   1 
ATOM   8479 N  N   . SER B 1 541 ? -24.624 33.185  -23.209  1.00 43.28  ?  539 SER B N   1 
ATOM   8480 C  CA  . SER B 1 541 ? -25.702 34.161  -23.173  1.00 47.18  ?  539 SER B CA  1 
ATOM   8481 C  C   . SER B 1 541 ? -25.972 34.598  -21.738  1.00 38.86  ?  539 SER B C   1 
ATOM   8482 O  O   . SER B 1 541 ? -25.629 33.904  -20.776  1.00 35.72  ?  539 SER B O   1 
ATOM   8483 C  CB  . SER B 1 541 ? -26.981 33.590  -23.799  1.00 36.19  ?  539 SER B CB  1 
ATOM   8484 O  OG  . SER B 1 541 ? -26.821 33.396  -25.194  1.00 55.32  ?  539 SER B OG  1 
ATOM   8485 N  N   . GLU B 1 542 ? -26.584 35.775  -21.603  1.00 39.28  ?  540 GLU B N   1 
ATOM   8486 C  CA  . GLU B 1 542 ? -26.933 36.323  -20.299  1.00 45.45  ?  540 GLU B CA  1 
ATOM   8487 C  C   . GLU B 1 542 ? -28.353 36.874  -20.334  1.00 41.55  ?  540 GLU B C   1 
ATOM   8488 O  O   . GLU B 1 542 ? -28.844 37.307  -21.379  1.00 37.19  ?  540 GLU B O   1 
ATOM   8489 C  CB  . GLU B 1 542 ? -25.934 37.404  -19.857  1.00 34.47  ?  540 GLU B CB  1 
ATOM   8490 C  CG  . GLU B 1 542 ? -25.888 38.641  -20.737  1.00 42.29  ?  540 GLU B CG  1 
ATOM   8491 C  CD  . GLU B 1 542 ? -24.862 39.651  -20.253  1.00 49.57  ?  540 GLU B CD  1 
ATOM   8492 O  OE1 . GLU B 1 542 ? -24.211 39.389  -19.219  1.00 50.77  ?  540 GLU B OE1 1 
ATOM   8493 O  OE2 . GLU B 1 542 ? -24.697 40.700  -20.912  1.00 53.91  -1 540 GLU B OE2 1 
ATOM   8494 N  N   . TYR B 1 543 ? -29.009 36.850  -19.174  1.00 40.63  ?  541 TYR B N   1 
ATOM   8495 C  CA  . TYR B 1 543 ? -30.387 37.301  -19.041  1.00 39.13  ?  541 TYR B CA  1 
ATOM   8496 C  C   . TYR B 1 543 ? -30.572 37.892  -17.651  1.00 37.57  ?  541 TYR B C   1 
ATOM   8497 O  O   . TYR B 1 543 ? -29.882 37.505  -16.705  1.00 36.38  ?  541 TYR B O   1 
ATOM   8498 C  CB  . TYR B 1 543 ? -31.392 36.155  -19.240  1.00 40.79  ?  541 TYR B CB  1 
ATOM   8499 C  CG  . TYR B 1 543 ? -31.099 35.221  -20.396  1.00 39.77  ?  541 TYR B CG  1 
ATOM   8500 C  CD1 . TYR B 1 543 ? -31.448 35.561  -21.696  1.00 41.43  ?  541 TYR B CD1 1 
ATOM   8501 C  CD2 . TYR B 1 543 ? -30.493 33.988  -20.183  1.00 42.15  ?  541 TYR B CD2 1 
ATOM   8502 C  CE1 . TYR B 1 543 ? -31.190 34.706  -22.753  1.00 51.23  ?  541 TYR B CE1 1 
ATOM   8503 C  CE2 . TYR B 1 543 ? -30.230 33.127  -21.234  1.00 46.72  ?  541 TYR B CE2 1 
ATOM   8504 C  CZ  . TYR B 1 543 ? -30.581 33.492  -22.517  1.00 50.76  ?  541 TYR B CZ  1 
ATOM   8505 O  OH  . TYR B 1 543 ? -30.322 32.642  -23.568  1.00 58.42  ?  541 TYR B OH  1 
ATOM   8506 N  N   . ASP B 1 544 ? -31.531 38.814  -17.521  1.00 37.00  ?  542 ASP B N   1 
ATOM   8507 C  CA  . ASP B 1 544 ? -31.722 39.468  -16.230  1.00 37.70  ?  542 ASP B CA  1 
ATOM   8508 C  C   . ASP B 1 544 ? -32.275 38.495  -15.199  1.00 38.16  ?  542 ASP B C   1 
ATOM   8509 O  O   . ASP B 1 544 ? -31.774 38.421  -14.071  1.00 40.51  ?  542 ASP B O   1 
ATOM   8510 C  CB  . ASP B 1 544 ? -32.650 40.679  -16.361  1.00 38.86  ?  542 ASP B CB  1 
ATOM   8511 C  CG  . ASP B 1 544 ? -32.054 41.788  -17.202  1.00 59.71  ?  542 ASP B CG  1 
ATOM   8512 O  OD1 . ASP B 1 544 ? -30.908 42.195  -16.918  1.00 58.34  ?  542 ASP B OD1 1 
ATOM   8513 O  OD2 . ASP B 1 544 ? -32.743 42.279  -18.122  1.00 67.01  -1 542 ASP B OD2 1 
ATOM   8514 N  N   . TYR B 1 545 ? -33.315 37.750  -15.560  1.00 31.53  ?  543 TYR B N   1 
ATOM   8515 C  CA  . TYR B 1 545 ? -33.961 36.817  -14.650  1.00 34.22  ?  543 TYR B CA  1 
ATOM   8516 C  C   . TYR B 1 545 ? -33.958 35.421  -15.257  1.00 31.26  ?  543 TYR B C   1 
ATOM   8517 O  O   . TYR B 1 545 ? -34.267 35.253  -16.442  1.00 38.19  ?  543 TYR B O   1 
ATOM   8518 C  CB  . TYR B 1 545 ? -35.383 37.282  -14.331  1.00 32.64  ?  543 TYR B CB  1 
ATOM   8519 C  CG  . TYR B 1 545 ? -35.398 38.511  -13.445  1.00 41.59  ?  543 TYR B CG  1 
ATOM   8520 C  CD1 . TYR B 1 545 ? -35.337 38.401  -12.061  1.00 42.75  ?  543 TYR B CD1 1 
ATOM   8521 C  CD2 . TYR B 1 545 ? -35.461 39.785  -13.997  1.00 45.15  ?  543 TYR B CD2 1 
ATOM   8522 C  CE1 . TYR B 1 545 ? -35.343 39.528  -11.252  1.00 45.84  ?  543 TYR B CE1 1 
ATOM   8523 C  CE2 . TYR B 1 545 ? -35.471 40.914  -13.198  1.00 49.89  ?  543 TYR B CE2 1 
ATOM   8524 C  CZ  . TYR B 1 545 ? -35.411 40.781  -11.828  1.00 50.57  ?  543 TYR B CZ  1 
ATOM   8525 O  OH  . TYR B 1 545 ? -35.422 41.908  -11.036  1.00 57.80  ?  543 TYR B OH  1 
ATOM   8526 N  N   . VAL B 1 546 ? -33.604 34.429  -14.449  1.00 27.02  ?  544 VAL B N   1 
ATOM   8527 C  CA  . VAL B 1 546 ? -33.527 33.042  -14.885  1.00 26.12  ?  544 VAL B CA  1 
ATOM   8528 C  C   . VAL B 1 546 ? -34.337 32.192  -13.920  1.00 32.34  ?  544 VAL B C   1 
ATOM   8529 O  O   . VAL B 1 546 ? -34.258 32.373  -12.699  1.00 33.20  ?  544 VAL B O   1 
ATOM   8530 C  CB  . VAL B 1 546 ? -32.068 32.539  -14.965  1.00 28.75  ?  544 VAL B CB  1 
ATOM   8531 C  CG1 . VAL B 1 546 ? -32.031 31.039  -15.234  1.00 27.16  ?  544 VAL B CG1 1 
ATOM   8532 C  CG2 . VAL B 1 546 ? -31.298 33.291  -16.050  1.00 24.60  ?  544 VAL B CG2 1 
ATOM   8533 N  N   . ILE B 1 547 ? -35.136 31.283  -14.470  1.00 31.55  ?  545 ILE B N   1 
ATOM   8534 C  CA  . ILE B 1 547 ? -35.852 30.277  -13.693  1.00 29.89  ?  545 ILE B CA  1 
ATOM   8535 C  C   . ILE B 1 547 ? -35.357 28.916  -14.155  1.00 29.47  ?  545 ILE B C   1 
ATOM   8536 O  O   . ILE B 1 547 ? -35.473 28.572  -15.339  1.00 29.87  ?  545 ILE B O   1 
ATOM   8537 C  CB  . ILE B 1 547 ? -37.375 30.408  -13.836  1.00 28.99  ?  545 ILE B CB  1 
ATOM   8538 C  CG1 . ILE B 1 547 ? -37.815 31.799  -13.370  1.00 30.70  ?  545 ILE B CG1 1 
ATOM   8539 C  CG2 . ILE B 1 547 ? -38.079 29.315  -13.038  1.00 32.59  ?  545 ILE B CG2 1 
ATOM   8540 C  CD1 . ILE B 1 547 ? -39.309 32.041  -13.435  1.00 34.54  ?  545 ILE B CD1 1 
ATOM   8541 N  N   . PHE B 1 548 ? -34.779 28.159  -13.229  1.00 23.62  ?  546 PHE B N   1 
ATOM   8542 C  CA  . PHE B 1 548 ? -34.181 26.866  -13.521  1.00 26.02  ?  546 PHE B CA  1 
ATOM   8543 C  C   . PHE B 1 548 ? -34.896 25.772  -12.744  1.00 30.81  ?  546 PHE B C   1 
ATOM   8544 O  O   . PHE B 1 548 ? -35.052 25.878  -11.523  1.00 24.13  ?  546 PHE B O   1 
ATOM   8545 C  CB  . PHE B 1 548 ? -32.694 26.899  -13.145  1.00 28.51  ?  546 PHE B CB  1 
ATOM   8546 C  CG  . PHE B 1 548 ? -31.996 25.574  -13.249  1.00 36.22  ?  546 PHE B CG  1 
ATOM   8547 C  CD1 . PHE B 1 548 ? -31.459 25.155  -14.455  1.00 27.12  ?  546 PHE B CD1 1 
ATOM   8548 C  CD2 . PHE B 1 548 ? -31.865 24.752  -12.142  1.00 27.75  ?  546 PHE B CD2 1 
ATOM   8549 C  CE1 . PHE B 1 548 ? -30.804 23.943  -14.559  1.00 25.36  ?  546 PHE B CE1 1 
ATOM   8550 C  CE2 . PHE B 1 548 ? -31.213 23.534  -12.240  1.00 27.03  ?  546 PHE B CE2 1 
ATOM   8551 C  CZ  . PHE B 1 548 ? -30.685 23.129  -13.449  1.00 35.49  ?  546 PHE B CZ  1 
ATOM   8552 N  N   . THR B 1 549 ? -35.308 24.719  -13.447  1.00 23.03  ?  547 THR B N   1 
ATOM   8553 C  CA  . THR B 1 549 ? -35.807 23.498  -12.823  1.00 36.80  ?  547 THR B CA  1 
ATOM   8554 C  C   . THR B 1 549 ? -34.821 22.387  -13.149  1.00 30.70  ?  547 THR B C   1 
ATOM   8555 O  O   . THR B 1 549 ? -34.565 22.103  -14.325  1.00 31.02  ?  547 THR B O   1 
ATOM   8556 C  CB  . THR B 1 549 ? -37.216 23.130  -13.296  1.00 27.50  ?  547 THR B CB  1 
ATOM   8557 O  OG1 . THR B 1 549 ? -37.214 22.901  -14.712  1.00 32.06  ?  547 THR B OG1 1 
ATOM   8558 C  CG2 . THR B 1 549 ? -38.208 24.232  -12.948  1.00 24.12  ?  547 THR B CG2 1 
ATOM   8559 N  N   . GLN B 1 550 ? -34.249 21.782  -12.108  1.00 28.14  ?  548 GLN B N   1 
ATOM   8560 C  CA  . GLN B 1 550 ? -33.284 20.709  -12.313  1.00 31.30  ?  548 GLN B CA  1 
ATOM   8561 C  C   . GLN B 1 550 ? -33.914 19.490  -12.981  1.00 34.08  ?  548 GLN B C   1 
ATOM   8562 O  O   . GLN B 1 550 ? -33.219 18.734  -13.672  1.00 30.12  ?  548 GLN B O   1 
ATOM   8563 C  CB  . GLN B 1 550 ? -32.651 20.341  -10.977  1.00 29.05  ?  548 GLN B CB  1 
ATOM   8564 C  CG  . GLN B 1 550 ? -31.285 19.715  -11.105  1.00 30.56  ?  548 GLN B CG  1 
ATOM   8565 C  CD  . GLN B 1 550 ? -30.681 19.394  -9.762   1.00 37.81  ?  548 GLN B CD  1 
ATOM   8566 O  OE1 . GLN B 1 550 ? -31.338 19.524  -8.726   1.00 35.89  ?  548 GLN B OE1 1 
ATOM   8567 N  NE2 . GLN B 1 550 ? -29.411 19.005  -9.763   1.00 30.43  ?  548 GLN B NE2 1 
ATOM   8568 N  N   . THR B 1 551 ? -35.214 19.271  -12.764  1.00 34.16  ?  549 THR B N   1 
ATOM   8569 C  CA  . THR B 1 551 ? -36.011 18.223  -13.404  1.00 34.07  ?  549 THR B CA  1 
ATOM   8570 C  C   . THR B 1 551 ? -35.767 16.835  -12.815  1.00 35.39  ?  549 THR B C   1 
ATOM   8571 O  O   . THR B 1 551 ? -36.726 16.129  -12.485  1.00 38.01  ?  549 THR B O   1 
ATOM   8572 C  CB  . THR B 1 551 ? -35.755 18.175  -14.914  1.00 33.55  ?  549 THR B CB  1 
ATOM   8573 O  OG1 . THR B 1 551 ? -35.728 19.504  -15.448  1.00 31.64  ?  549 THR B OG1 1 
ATOM   8574 C  CG2 . THR B 1 551 ? -36.854 17.369  -15.612  1.00 28.64  ?  549 THR B CG2 1 
ATOM   8575 N  N   . THR B 1 552 ? -34.504 16.429  -12.680  1.00 32.49  ?  550 THR B N   1 
ATOM   8576 C  CA  . THR B 1 552 ? -34.157 15.111  -12.157  1.00 35.55  ?  550 THR B CA  1 
ATOM   8577 C  C   . THR B 1 552 ? -32.921 15.240  -11.280  1.00 39.66  ?  550 THR B C   1 
ATOM   8578 O  O   . THR B 1 552 ? -32.364 16.329  -11.103  1.00 34.13  ?  550 THR B O   1 
ATOM   8579 C  CB  . THR B 1 552 ? -33.893 14.071  -13.259  1.00 42.70  ?  550 THR B CB  1 
ATOM   8580 O  OG1 . THR B 1 552 ? -32.659 14.371  -13.923  1.00 42.58  ?  550 THR B OG1 1 
ATOM   8581 C  CG2 . THR B 1 552 ? -35.026 14.030  -14.270  1.00 36.19  ?  550 THR B CG2 1 
ATOM   8582 N  N   . GLU B 1 553 ? -32.491 14.100  -10.738  1.00 44.43  ?  551 GLU B N   1 
ATOM   8583 C  CA  . GLU B 1 553 ? -31.289 13.982  -9.922   1.00 46.09  ?  551 GLU B CA  1 
ATOM   8584 C  C   . GLU B 1 553 ? -30.244 13.095  -10.594  1.00 47.89  ?  551 GLU B C   1 
ATOM   8585 O  O   . GLU B 1 553 ? -29.421 12.474  -9.919   1.00 56.87  ?  551 GLU B O   1 
ATOM   8586 C  CB  . GLU B 1 553 ? -31.643 13.412  -8.549   1.00 46.74  ?  551 GLU B CB  1 
ATOM   8587 C  CG  . GLU B 1 553 ? -31.509 14.361  -7.381   1.00 48.02  ?  551 GLU B CG  1 
ATOM   8588 C  CD  . GLU B 1 553 ? -31.997 13.724  -6.093   1.00 55.71  ?  551 GLU B CD  1 
ATOM   8589 O  OE1 . GLU B 1 553 ? -33.199 13.381  -6.018   1.00 55.66  ?  551 GLU B OE1 1 
ATOM   8590 O  OE2 . GLU B 1 553 ? -31.178 13.543  -5.167   1.00 57.39  -1 551 GLU B OE2 1 
ATOM   8591 N  N   . THR B 1 554 ? -30.265 13.026  -11.923  1.00 50.28  ?  552 THR B N   1 
ATOM   8592 C  CA  . THR B 1 554 ? -29.307 12.211  -12.657  1.00 53.42  ?  552 THR B CA  1 
ATOM   8593 C  C   . THR B 1 554 ? -27.919 12.851  -12.638  1.00 48.08  ?  552 THR B C   1 
ATOM   8594 O  O   . THR B 1 554 ? -27.718 13.972  -12.163  1.00 41.59  ?  552 THR B O   1 
ATOM   8595 C  CB  . THR B 1 554 ? -29.757 12.009  -14.105  1.00 51.01  ?  552 THR B CB  1 
ATOM   8596 O  OG1 . THR B 1 554 ? -29.742 13.268  -14.793  1.00 47.20  ?  552 THR B OG1 1 
ATOM   8597 C  CG2 . THR B 1 554 ? -31.159 11.416  -14.159  1.00 40.29  ?  552 THR B CG2 1 
ATOM   8598 N  N   . ALA B 1 555 ? -26.944 12.107  -13.164  1.00 44.54  ?  553 ALA B N   1 
ATOM   8599 C  CA  . ALA B 1 555 ? -25.606 12.665  -13.306  1.00 44.51  ?  553 ALA B CA  1 
ATOM   8600 C  C   . ALA B 1 555 ? -25.623 13.832  -14.284  1.00 45.91  ?  553 ALA B C   1 
ATOM   8601 O  O   . ALA B 1 555 ? -24.910 14.824  -14.096  1.00 45.24  ?  553 ALA B O   1 
ATOM   8602 C  CB  . ALA B 1 555 ? -24.628 11.584  -13.764  1.00 45.23  ?  553 ALA B CB  1 
ATOM   8603 N  N   . HIS B 1 556 ? -26.440 13.728  -15.335  1.00 49.44  ?  554 HIS B N   1 
ATOM   8604 C  CA  . HIS B 1 556 ? -26.574 14.817  -16.297  1.00 48.20  ?  554 HIS B CA  1 
ATOM   8605 C  C   . HIS B 1 556 ? -27.067 16.095  -15.627  1.00 42.07  ?  554 HIS B C   1 
ATOM   8606 O  O   . HIS B 1 556 ? -26.545 17.184  -15.892  1.00 41.82  ?  554 HIS B O   1 
ATOM   8607 C  CB  . HIS B 1 556 ? -27.527 14.395  -17.417  1.00 40.91  ?  554 HIS B CB  1 
ATOM   8608 C  CG  . HIS B 1 556 ? -27.895 15.502  -18.355  1.00 47.70  ?  554 HIS B CG  1 
ATOM   8609 N  ND1 . HIS B 1 556 ? -27.091 15.888  -19.406  1.00 45.31  ?  554 HIS B ND1 1 
ATOM   8610 C  CD2 . HIS B 1 556 ? -28.983 16.307  -18.399  1.00 44.07  ?  554 HIS B CD2 1 
ATOM   8611 C  CE1 . HIS B 1 556 ? -27.668 16.882  -20.058  1.00 42.27  ?  554 HIS B CE1 1 
ATOM   8612 N  NE2 . HIS B 1 556 ? -28.818 17.155  -19.467  1.00 42.32  ?  554 HIS B NE2 1 
ATOM   8613 N  N   . SER B 1 557 ? -28.055 15.982  -14.734  1.00 36.33  ?  555 SER B N   1 
ATOM   8614 C  CA  . SER B 1 557 ? -28.650 17.159  -14.110  1.00 36.70  ?  555 SER B CA  1 
ATOM   8615 C  C   . SER B 1 557 ? -27.848 17.667  -12.918  1.00 37.37  ?  555 SER B C   1 
ATOM   8616 O  O   . SER B 1 557 ? -28.091 18.789  -12.461  1.00 33.16  ?  555 SER B O   1 
ATOM   8617 C  CB  . SER B 1 557 ? -30.092 16.866  -13.677  1.00 38.75  ?  555 SER B CB  1 
ATOM   8618 O  OG  . SER B 1 557 ? -30.129 16.181  -12.436  1.00 48.65  ?  555 SER B OG  1 
ATOM   8619 N  N   . CYS B 1 558 ? -26.935 16.859  -12.380  1.00 38.08  ?  556 CYS B N   1 
ATOM   8620 C  CA  . CYS B 1 558 ? -26.134 17.239  -11.225  1.00 31.47  ?  556 CYS B CA  1 
ATOM   8621 C  C   . CYS B 1 558 ? -24.692 17.560  -11.592  1.00 33.15  ?  556 CYS B C   1 
ATOM   8622 O  O   . CYS B 1 558 ? -23.881 17.816  -10.697  1.00 36.50  ?  556 CYS B O   1 
ATOM   8623 C  CB  . CYS B 1 558 ? -26.156 16.123  -10.173  1.00 38.83  ?  556 CYS B CB  1 
ATOM   8624 S  SG  . CYS B 1 558 ? -27.784 15.767  -9.468   1.00 48.21  ?  556 CYS B SG  1 
ATOM   8625 N  N   . ASN B 1 559 ? -24.354 17.559  -12.878  1.00 33.07  ?  557 ASN B N   1 
ATOM   8626 C  CA  . ASN B 1 559 ? -23.006 17.898  -13.322  1.00 37.42  ?  557 ASN B CA  1 
ATOM   8627 C  C   . ASN B 1 559 ? -22.648 19.324  -12.907  1.00 33.59  ?  557 ASN B C   1 
ATOM   8628 O  O   . ASN B 1 559 ? -23.329 20.280  -13.290  1.00 29.64  ?  557 ASN B O   1 
ATOM   8629 C  CB  . ASN B 1 559 ? -22.915 17.724  -14.839  1.00 35.88  ?  557 ASN B CB  1 
ATOM   8630 C  CG  . ASN B 1 559 ? -21.524 17.985  -15.377  1.00 39.83  ?  557 ASN B CG  1 
ATOM   8631 O  OD1 . ASN B 1 559 ? -21.072 19.127  -15.430  1.00 41.74  ?  557 ASN B OD1 1 
ATOM   8632 N  ND2 . ASN B 1 559 ? -20.834 16.921  -15.774  1.00 39.07  ?  557 ASN B ND2 1 
ATOM   8633 N  N   . VAL B 1 560 ? -21.593 19.458  -12.093  1.00 33.07  ?  558 VAL B N   1 
ATOM   8634 C  CA  . VAL B 1 560 ? -21.208 20.767  -11.561  1.00 36.97  ?  558 VAL B CA  1 
ATOM   8635 C  C   . VAL B 1 560 ? -20.961 21.772  -12.682  1.00 33.09  ?  558 VAL B C   1 
ATOM   8636 O  O   . VAL B 1 560 ? -21.279 22.959  -12.546  1.00 33.18  ?  558 VAL B O   1 
ATOM   8637 C  CB  . VAL B 1 560 ? -19.982 20.642  -10.635  1.00 39.58  ?  558 VAL B CB  1 
ATOM   8638 C  CG1 . VAL B 1 560 ? -20.354 19.904  -9.357   1.00 47.37  ?  558 VAL B CG1 1 
ATOM   8639 C  CG2 . VAL B 1 560 ? -18.828 19.955  -11.352  1.00 38.00  ?  558 VAL B CG2 1 
ATOM   8640 N  N   . ASN B 1 561 ? -20.372 21.328  -13.795  1.00 34.43  ?  559 ASN B N   1 
ATOM   8641 C  CA  . ASN B 1 561 ? -20.127 22.255  -14.898  1.00 34.35  ?  559 ASN B CA  1 
ATOM   8642 C  C   . ASN B 1 561 ? -21.441 22.748  -15.488  1.00 34.48  ?  559 ASN B C   1 
ATOM   8643 O  O   . ASN B 1 561 ? -21.616 23.950  -15.728  1.00 34.34  ?  559 ASN B O   1 
ATOM   8644 C  CB  . ASN B 1 561 ? -19.264 21.590  -15.970  1.00 37.20  ?  559 ASN B CB  1 
ATOM   8645 C  CG  . ASN B 1 561 ? -17.841 21.355  -15.507  1.00 41.57  ?  559 ASN B CG  1 
ATOM   8646 O  OD1 . ASN B 1 561 ? -17.610 20.914  -14.381  1.00 42.77  ?  559 ASN B OD1 1 
ATOM   8647 N  ND2 . ASN B 1 561 ? -16.878 21.636  -16.379  1.00 35.57  ?  559 ASN B ND2 1 
ATOM   8648 N  N   . ARG B 1 562 ? -22.384 21.834  -15.716  1.00 34.19  ?  560 ARG B N   1 
ATOM   8649 C  CA  . ARG B 1 562 ? -23.694 22.243  -16.203  1.00 29.77  ?  560 ARG B CA  1 
ATOM   8650 C  C   . ARG B 1 562 ? -24.372 23.165  -15.202  1.00 32.07  ?  560 ARG B C   1 
ATOM   8651 O  O   . ARG B 1 562 ? -24.921 24.208  -15.576  1.00 33.66  ?  560 ARG B O   1 
ATOM   8652 C  CB  . ARG B 1 562 ? -24.552 21.006  -16.470  1.00 30.71  ?  560 ARG B CB  1 
ATOM   8653 C  CG  . ARG B 1 562 ? -25.975 21.291  -16.926  1.00 33.16  ?  560 ARG B CG  1 
ATOM   8654 C  CD  . ARG B 1 562 ? -26.557 20.052  -17.586  1.00 43.49  ?  560 ARG B CD  1 
ATOM   8655 N  NE  . ARG B 1 562 ? -25.914 19.792  -18.868  1.00 39.68  ?  560 ARG B NE  1 
ATOM   8656 C  CZ  . ARG B 1 562 ? -25.123 18.757  -19.109  1.00 44.09  ?  560 ARG B CZ  1 
ATOM   8657 N  NH1 . ARG B 1 562 ? -24.812 17.890  -18.159  1.00 43.17  ?  560 ARG B NH1 1 
ATOM   8658 N  NH2 . ARG B 1 562 ? -24.608 18.604  -20.326  1.00 46.31  ?  560 ARG B NH2 1 
ATOM   8659 N  N   . PHE B 1 563 ? -24.315 22.813  -13.916  1.00 33.45  ?  561 PHE B N   1 
ATOM   8660 C  CA  . PHE B 1 563 ? -24.926 23.656  -12.896  1.00 28.93  ?  561 PHE B CA  1 
ATOM   8661 C  C   . PHE B 1 563 ? -24.274 25.029  -12.862  1.00 36.21  ?  561 PHE B C   1 
ATOM   8662 O  O   . PHE B 1 563 ? -24.959 26.052  -12.747  1.00 38.02  ?  561 PHE B O   1 
ATOM   8663 C  CB  . PHE B 1 563 ? -24.823 22.986  -11.527  1.00 32.81  ?  561 PHE B CB  1 
ATOM   8664 C  CG  . PHE B 1 563 ? -25.752 23.567  -10.506  1.00 31.09  ?  561 PHE B CG  1 
ATOM   8665 C  CD1 . PHE B 1 563 ? -27.100 23.710  -10.790  1.00 35.26  ?  561 PHE B CD1 1 
ATOM   8666 C  CD2 . PHE B 1 563 ? -25.284 23.975  -9.269   1.00 37.84  ?  561 PHE B CD2 1 
ATOM   8667 C  CE1 . PHE B 1 563 ? -27.968 24.242  -9.857   1.00 42.31  ?  561 PHE B CE1 1 
ATOM   8668 C  CE2 . PHE B 1 563 ? -26.149 24.510  -8.329   1.00 31.25  ?  561 PHE B CE2 1 
ATOM   8669 C  CZ  . PHE B 1 563 ? -27.492 24.644  -8.624   1.00 33.05  ?  561 PHE B CZ  1 
ATOM   8670 N  N   . ASN B 1 564 ? -22.944 25.068  -12.959  1.00 33.06  ?  562 ASN B N   1 
ATOM   8671 C  CA  . ASN B 1 564 ? -22.230 26.339  -12.982  1.00 34.44  ?  562 ASN B CA  1 
ATOM   8672 C  C   . ASN B 1 564 ? -22.742 27.233  -14.109  1.00 31.92  ?  562 ASN B C   1 
ATOM   8673 O  O   . ASN B 1 564 ? -23.009 28.423  -13.901  1.00 34.36  ?  562 ASN B O   1 
ATOM   8674 C  CB  . ASN B 1 564 ? -20.726 26.074  -13.098  1.00 31.01  ?  562 ASN B CB  1 
ATOM   8675 C  CG  . ASN B 1 564 ? -19.921 27.337  -13.273  1.00 37.07  ?  562 ASN B CG  1 
ATOM   8676 O  OD1 . ASN B 1 564 ? -20.057 28.283  -12.498  1.00 38.52  ?  562 ASN B OD1 1 
ATOM   8677 N  ND2 . ASN B 1 564 ? -19.042 27.344  -14.268  1.00 33.02  ?  562 ASN B ND2 1 
ATOM   8678 N  N   . VAL B 1 565 ? -22.862 26.683  -15.320  1.00 34.47  ?  563 VAL B N   1 
ATOM   8679 C  CA  . VAL B 1 565 ? -23.337 27.479  -16.450  1.00 35.49  ?  563 VAL B CA  1 
ATOM   8680 C  C   . VAL B 1 565 ? -24.768 27.944  -16.213  1.00 29.72  ?  563 VAL B C   1 
ATOM   8681 O  O   . VAL B 1 565 ? -25.112 29.106  -16.467  1.00 30.81  ?  563 VAL B O   1 
ATOM   8682 C  CB  . VAL B 1 565 ? -23.220 26.684  -17.764  1.00 30.32  ?  563 VAL B CB  1 
ATOM   8683 C  CG1 . VAL B 1 565 ? -23.944 27.418  -18.880  1.00 32.87  ?  563 VAL B CG1 1 
ATOM   8684 C  CG2 . VAL B 1 565 ? -21.755 26.477  -18.137  1.00 31.31  ?  563 VAL B CG2 1 
ATOM   8685 N  N   . ALA B 1 566 ? -25.626 27.047  -15.729  1.00 32.75  ?  564 ALA B N   1 
ATOM   8686 C  CA  . ALA B 1 566 ? -27.035 27.387  -15.567  1.00 30.65  ?  564 ALA B CA  1 
ATOM   8687 C  C   . ALA B 1 566 ? -27.218 28.637  -14.714  1.00 29.41  ?  564 ALA B C   1 
ATOM   8688 O  O   . ALA B 1 566 ? -27.905 29.581  -15.120  1.00 29.07  ?  564 ALA B O   1 
ATOM   8689 C  CB  . ALA B 1 566 ? -27.790 26.204  -14.956  1.00 31.60  ?  564 ALA B CB  1 
ATOM   8690 N  N   . ILE B 1 567 ? -26.597 28.674  -13.532  1.00 34.58  ?  565 ILE B N   1 
ATOM   8691 C  CA  . ILE B 1 567 ? -26.865 29.789  -12.626  1.00 32.01  ?  565 ILE B CA  1 
ATOM   8692 C  C   . ILE B 1 567 ? -26.072 31.046  -12.975  1.00 36.72  ?  565 ILE B C   1 
ATOM   8693 O  O   . ILE B 1 567 ? -26.437 32.135  -12.515  1.00 40.06  ?  565 ILE B O   1 
ATOM   8694 C  CB  . ILE B 1 567 ? -26.635 29.389  -11.158  1.00 39.10  ?  565 ILE B CB  1 
ATOM   8695 C  CG1 . ILE B 1 567 ? -25.160 29.121  -10.864  1.00 38.91  ?  565 ILE B CG1 1 
ATOM   8696 C  CG2 . ILE B 1 567 ? -27.477 28.173  -10.798  1.00 35.61  ?  565 ILE B CG2 1 
ATOM   8697 C  CD1 . ILE B 1 567 ? -24.910 28.811  -9.401   1.00 42.56  ?  565 ILE B CD1 1 
ATOM   8698 N  N   . THR B 1 568 ? -25.008 30.943  -13.774  1.00 34.38  ?  566 THR B N   1 
ATOM   8699 C  CA  . THR B 1 568 ? -24.222 32.124  -14.128  1.00 32.41  ?  566 THR B CA  1 
ATOM   8700 C  C   . THR B 1 568 ? -24.814 32.889  -15.303  1.00 29.92  ?  566 THR B C   1 
ATOM   8701 O  O   . THR B 1 568 ? -24.175 33.821  -15.807  1.00 35.97  ?  566 THR B O   1 
ATOM   8702 C  CB  . THR B 1 568 ? -22.766 31.752  -14.442  1.00 27.82  ?  566 THR B CB  1 
ATOM   8703 O  OG1 . THR B 1 568 ? -22.727 30.664  -15.371  1.00 34.84  ?  566 THR B OG1 1 
ATOM   8704 C  CG2 . THR B 1 568 ? -22.019 31.375  -13.168  1.00 33.72  ?  566 THR B CG2 1 
ATOM   8705 N  N   . ARG B 1 569 ? -25.999 32.496  -15.772  1.00 31.25  ?  567 ARG B N   1 
ATOM   8706 C  CA  . ARG B 1 569 ? -26.652 33.201  -16.866  1.00 30.80  ?  567 ARG B CA  1 
ATOM   8707 C  C   . ARG B 1 569 ? -27.388 34.446  -16.390  1.00 31.59  ?  567 ARG B C   1 
ATOM   8708 O  O   . ARG B 1 569 ? -27.697 35.322  -17.206  1.00 31.50  ?  567 ARG B O   1 
ATOM   8709 C  CB  . ARG B 1 569 ? -27.672 32.282  -17.553  1.00 33.87  ?  567 ARG B CB  1 
ATOM   8710 C  CG  . ARG B 1 569 ? -27.158 30.957  -18.111  1.00 35.37  ?  567 ARG B CG  1 
ATOM   8711 C  CD  . ARG B 1 569 ? -25.957 31.123  -19.039  1.00 24.77  ?  567 ARG B CD  1 
ATOM   8712 N  NE  . ARG B 1 569 ? -24.691 31.119  -18.318  1.00 24.73  ?  567 ARG B NE  1 
ATOM   8713 C  CZ  . ARG B 1 569 ? -23.528 31.447  -18.862  1.00 35.03  ?  567 ARG B CZ  1 
ATOM   8714 N  NH1 . ARG B 1 569 ? -23.458 31.966  -20.077  1.00 28.70  ?  567 ARG B NH1 1 
ATOM   8715 N  NH2 . ARG B 1 569 ? -22.414 31.294  -18.152  1.00 36.86  ?  567 ARG B NH2 1 
ATOM   8716 N  N   . ALA B 1 570 ? -27.650 34.552  -15.089  1.00 30.61  ?  568 ALA B N   1 
ATOM   8717 C  CA  . ALA B 1 570 ? -28.462 35.623  -14.528  1.00 33.55  ?  568 ALA B CA  1 
ATOM   8718 C  C   . ALA B 1 570 ? -27.650 36.873  -14.220  1.00 33.57  ?  568 ALA B C   1 
ATOM   8719 O  O   . ALA B 1 570 ? -26.554 36.799  -13.656  1.00 33.09  ?  568 ALA B O   1 
ATOM   8720 C  CB  . ALA B 1 570 ? -29.159 35.147  -13.254  1.00 27.97  ?  568 ALA B CB  1 
ATOM   8721 N  N   . LYS B 1 571 ? -28.212 38.025  -14.580  1.00 35.06  ?  569 LYS B N   1 
ATOM   8722 C  CA  . LYS B 1 571 ? -27.626 39.317  -14.255  1.00 39.17  ?  569 LYS B CA  1 
ATOM   8723 C  C   . LYS B 1 571 ? -28.242 39.939  -13.011  1.00 40.49  ?  569 LYS B C   1 
ATOM   8724 O  O   . LYS B 1 571 ? -27.577 40.732  -12.336  1.00 43.11  ?  569 LYS B O   1 
ATOM   8725 C  CB  . LYS B 1 571 ? -27.772 40.298  -15.428  1.00 38.04  ?  569 LYS B CB  1 
ATOM   8726 C  CG  . LYS B 1 571 ? -27.097 39.848  -16.717  1.00 42.80  ?  569 LYS B CG  1 
ATOM   8727 C  CD  . LYS B 1 571 ? -27.128 40.941  -17.786  1.00 51.98  ?  569 LYS B CD  1 
ATOM   8728 C  CE  . LYS B 1 571 ? -28.492 41.063  -18.447  1.00 47.79  ?  569 LYS B CE  1 
ATOM   8729 N  NZ  . LYS B 1 571 ? -28.502 42.136  -19.485  1.00 65.35  ?  569 LYS B NZ  1 
ATOM   8730 N  N   . VAL B 1 572 ? -29.494 39.603  -12.689  1.00 41.40  ?  570 VAL B N   1 
ATOM   8731 C  CA  . VAL B 1 572 ? -30.192 40.243  -11.579  1.00 42.04  ?  570 VAL B CA  1 
ATOM   8732 C  C   . VAL B 1 572 ? -30.754 39.219  -10.597  1.00 43.53  ?  570 VAL B C   1 
ATOM   8733 O  O   . VAL B 1 572 ? -30.401 39.230  -9.413   1.00 43.08  ?  570 VAL B O   1 
ATOM   8734 C  CB  . VAL B 1 572 ? -31.311 41.165  -12.097  1.00 45.04  ?  570 VAL B CB  1 
ATOM   8735 C  CG1 . VAL B 1 572 ? -32.064 41.780  -10.930  1.00 48.29  ?  570 VAL B CG1 1 
ATOM   8736 C  CG2 . VAL B 1 572 ? -30.727 42.253  -12.986  1.00 47.20  ?  570 VAL B CG2 1 
ATOM   8737 N  N   . GLY B 1 573 ? -31.651 38.347  -11.066  1.00 40.67  ?  571 GLY B N   1 
ATOM   8738 C  CA  . GLY B 1 573 ? -32.295 37.387  -10.197  1.00 36.12  ?  571 GLY B CA  1 
ATOM   8739 C  C   . GLY B 1 573 ? -32.316 35.994  -10.798  1.00 36.73  ?  571 GLY B C   1 
ATOM   8740 O  O   . GLY B 1 573 ? -32.165 35.808  -12.005  1.00 33.13  ?  571 GLY B O   1 
ATOM   8741 N  N   . ILE B 1 574 ? -32.490 35.006  -9.921   1.00 33.11  ?  572 ILE B N   1 
ATOM   8742 C  CA  . ILE B 1 574 ? -32.579 33.609  -10.340  1.00 29.72  ?  572 ILE B CA  1 
ATOM   8743 C  C   . ILE B 1 574 ? -33.447 32.843  -9.347   1.00 34.27  ?  572 ILE B C   1 
ATOM   8744 O  O   . ILE B 1 574 ? -33.387 33.074  -8.136   1.00 31.10  ?  572 ILE B O   1 
ATOM   8745 C  CB  . ILE B 1 574 ? -31.186 32.957  -10.489  1.00 35.32  ?  572 ILE B CB  1 
ATOM   8746 C  CG1 . ILE B 1 574 ? -31.335 31.533  -11.033  1.00 37.40  ?  572 ILE B CG1 1 
ATOM   8747 C  CG2 . ILE B 1 574 ? -30.435 32.962  -9.163   1.00 32.94  ?  572 ILE B CG2 1 
ATOM   8748 C  CD1 . ILE B 1 574 ? -30.059 30.944  -11.591  1.00 31.87  ?  572 ILE B CD1 1 
ATOM   8749 N  N   . LEU B 1 575 ? -34.276 31.945  -9.881   1.00 32.37  ?  573 LEU B N   1 
ATOM   8750 C  CA  . LEU B 1 575 ? -35.035 30.966  -9.108   1.00 31.00  ?  573 LEU B CA  1 
ATOM   8751 C  C   . LEU B 1 575 ? -34.608 29.568  -9.542   1.00 26.34  ?  573 LEU B C   1 
ATOM   8752 O  O   . LEU B 1 575 ? -34.747 29.212  -10.716  1.00 31.05  ?  573 LEU B O   1 
ATOM   8753 C  CB  . LEU B 1 575 ? -36.541 31.158  -9.295   1.00 30.10  ?  573 LEU B CB  1 
ATOM   8754 C  CG  . LEU B 1 575 ? -37.421 30.106  -8.624   1.00 36.53  ?  573 LEU B CG  1 
ATOM   8755 C  CD1 . LEU B 1 575 ? -37.218 30.136  -7.118   1.00 31.35  ?  573 LEU B CD1 1 
ATOM   8756 C  CD2 . LEU B 1 575 ? -38.881 30.340  -8.971   1.00 29.24  ?  573 LEU B CD2 1 
ATOM   8757 N  N   . CYS B 1 576 ? -34.068 28.791  -8.605   1.00 22.74  ?  574 CYS B N   1 
ATOM   8758 C  CA  . CYS B 1 576 ? -33.700 27.393  -8.825   1.00 27.24  ?  574 CYS B CA  1 
ATOM   8759 C  C   . CYS B 1 576 ? -34.647 26.449  -8.090   1.00 37.07  ?  574 CYS B C   1 
ATOM   8760 O  O   . CYS B 1 576 ? -34.708 26.469  -6.855   1.00 27.55  ?  574 CYS B O   1 
ATOM   8761 C  CB  . CYS B 1 576 ? -32.269 27.135  -8.354   1.00 28.64  ?  574 CYS B CB  1 
ATOM   8762 S  SG  . CYS B 1 576 ? -30.986 27.925  -9.329   1.00 37.41  ?  574 CYS B SG  1 
ATOM   8763 N  N   . ILE B 1 577 ? -35.382 25.629  -8.844   1.00 28.85  ?  575 ILE B N   1 
ATOM   8764 C  CA  . ILE B 1 577 ? -36.196 24.554  -8.272   1.00 40.63  ?  575 ILE B CA  1 
ATOM   8765 C  C   . ILE B 1 577 ? -35.329 23.296  -8.284   1.00 39.77  ?  575 ILE B C   1 
ATOM   8766 O  O   . ILE B 1 577 ? -35.141 22.671  -9.327   1.00 33.98  ?  575 ILE B O   1 
ATOM   8767 C  CB  . ILE B 1 577 ? -37.499 24.343  -9.048   1.00 38.18  ?  575 ILE B CB  1 
ATOM   8768 C  CG1 . ILE B 1 577 ? -38.168 25.680  -9.395   1.00 37.67  ?  575 ILE B CG1 1 
ATOM   8769 C  CG2 . ILE B 1 577 ? -38.437 23.423  -8.274   1.00 37.75  ?  575 ILE B CG2 1 
ATOM   8770 C  CD1 . ILE B 1 577 ? -38.547 26.526  -8.204   1.00 25.90  ?  575 ILE B CD1 1 
ATOM   8771 N  N   . MET B 1 578 ? -34.798 22.921  -7.119   1.00 40.48  ?  576 MET B N   1 
ATOM   8772 C  CA  . MET B 1 578 ? -33.831 21.833  -7.012   1.00 33.55  ?  576 MET B CA  1 
ATOM   8773 C  C   . MET B 1 578 ? -34.444 20.468  -6.725   1.00 42.43  ?  576 MET B C   1 
ATOM   8774 O  O   . MET B 1 578 ? -35.478 20.341  -6.062   1.00 42.81  ?  576 MET B O   1 
ATOM   8775 C  CB  . MET B 1 578 ? -32.802 22.136  -5.922   1.00 27.69  ?  576 MET B CB  1 
ATOM   8776 C  CG  . MET B 1 578 ? -32.108 23.441  -6.127   1.00 44.81  ?  576 MET B CG  1 
ATOM   8777 S  SD  . MET B 1 578 ? -31.415 23.418  -7.776   1.00 35.04  ?  576 MET B SD  1 
ATOM   8778 C  CE  . MET B 1 578 ? -30.059 22.268  -7.564   1.00 37.53  ?  576 MET B CE  1 
ATOM   8779 N  N   . SER B 1 579 ? -33.748 19.436  -7.204   1.00 45.36  ?  577 SER B N   1 
ATOM   8780 C  CA  . SER B 1 579 ? -34.069 18.041  -6.943   1.00 38.50  ?  577 SER B CA  1 
ATOM   8781 C  C   . SER B 1 579 ? -32.988 17.352  -6.132   1.00 38.37  ?  577 SER B C   1 
ATOM   8782 O  O   . SER B 1 579 ? -33.293 16.463  -5.333   1.00 49.21  ?  577 SER B O   1 
ATOM   8783 C  CB  . SER B 1 579 ? -34.238 17.267  -8.259   1.00 36.72  ?  577 SER B CB  1 
ATOM   8784 O  OG  . SER B 1 579 ? -35.299 17.774  -9.043   1.00 36.85  ?  577 SER B OG  1 
ATOM   8785 N  N   . ASP B 1 580 ? -31.739 17.776  -6.301   1.00 41.62  ?  578 ASP B N   1 
ATOM   8786 C  CA  . ASP B 1 580 ? -30.601 17.202  -5.600   1.00 41.32  ?  578 ASP B CA  1 
ATOM   8787 C  C   . ASP B 1 580 ? -30.324 18.015  -4.342   1.00 44.94  ?  578 ASP B C   1 
ATOM   8788 O  O   . ASP B 1 580 ? -30.067 19.222  -4.418   1.00 37.61  ?  578 ASP B O   1 
ATOM   8789 C  CB  . ASP B 1 580 ? -29.383 17.173  -6.524   1.00 47.83  ?  578 ASP B CB  1 
ATOM   8790 C  CG  . ASP B 1 580 ? -28.114 16.751  -5.814   1.00 49.91  ?  578 ASP B CG  1 
ATOM   8791 O  OD1 . ASP B 1 580 ? -28.137 15.722  -5.108   1.00 54.78  ?  578 ASP B OD1 1 
ATOM   8792 O  OD2 . ASP B 1 580 ? -27.081 17.435  -5.990   1.00 50.81  -1 578 ASP B OD2 1 
ATOM   8793 N  N   . ARG B 1 581 ? -30.362 17.348  -3.188   1.00 44.57  ?  579 ARG B N   1 
ATOM   8794 C  CA  . ARG B 1 581 ? -30.082 18.028  -1.929   1.00 47.99  ?  579 ARG B CA  1 
ATOM   8795 C  C   . ARG B 1 581 ? -28.661 18.577  -1.902   1.00 48.46  ?  579 ARG B C   1 
ATOM   8796 O  O   . ARG B 1 581 ? -28.412 19.651  -1.340   1.00 48.92  ?  579 ARG B O   1 
ATOM   8797 C  CB  . ARG B 1 581 ? -30.313 17.069  -0.761   1.00 46.56  ?  579 ARG B CB  1 
ATOM   8798 C  CG  . ARG B 1 581 ? -30.036 17.679  0.595    1.00 55.39  ?  579 ARG B CG  1 
ATOM   8799 C  CD  . ARG B 1 581 ? -31.007 18.802  0.902    1.00 60.79  ?  579 ARG B CD  1 
ATOM   8800 N  NE  . ARG B 1 581 ? -30.634 19.501  2.124    1.00 70.09  ?  579 ARG B NE  1 
ATOM   8801 C  CZ  . ARG B 1 581 ? -30.586 18.941  3.325    1.00 67.89  ?  579 ARG B CZ  1 
ATOM   8802 N  NH1 . ARG B 1 581 ? -31.163 17.775  3.567    1.00 66.94  ?  579 ARG B NH1 1 
ATOM   8803 N  NH2 . ARG B 1 581 ? -30.018 19.606  4.328    1.00 71.54  ?  579 ARG B NH2 1 
ATOM   8804 N  N   . ASP B 1 582 ? -27.716 17.856  -2.508   1.00 54.49  ?  580 ASP B N   1 
ATOM   8805 C  CA  . ASP B 1 582 ? -26.318 18.276  -2.494   1.00 48.75  ?  580 ASP B CA  1 
ATOM   8806 C  C   . ASP B 1 582 ? -26.163 19.669  -3.096   1.00 41.51  ?  580 ASP B C   1 
ATOM   8807 O  O   . ASP B 1 582 ? -25.652 20.588  -2.444   1.00 37.35  ?  580 ASP B O   1 
ATOM   8808 C  CB  . ASP B 1 582 ? -25.468 17.237  -3.235   1.00 55.15  ?  580 ASP B CB  1 
ATOM   8809 C  CG  . ASP B 1 582 ? -23.989 17.586  -3.270   1.00 60.21  ?  580 ASP B CG  1 
ATOM   8810 O  OD1 . ASP B 1 582 ? -23.599 18.666  -2.779   1.00 60.51  ?  580 ASP B OD1 1 
ATOM   8811 O  OD2 . ASP B 1 582 ? -23.206 16.752  -3.773   1.00 66.84  -1 580 ASP B OD2 1 
ATOM   8812 N  N   . LEU B 1 583 ? -26.582 19.843  -4.353   1.00 40.29  ?  581 LEU B N   1 
ATOM   8813 C  CA  . LEU B 1 583 ? -26.438 21.149  -4.988   1.00 43.82  ?  581 LEU B CA  1 
ATOM   8814 C  C   . LEU B 1 583 ? -27.341 22.190  -4.337   1.00 40.40  ?  581 LEU B C   1 
ATOM   8815 O  O   . LEU B 1 583 ? -26.978 23.370  -4.270   1.00 40.43  ?  581 LEU B O   1 
ATOM   8816 C  CB  . LEU B 1 583 ? -26.729 21.052  -6.485   1.00 31.72  ?  581 LEU B CB  1 
ATOM   8817 C  CG  . LEU B 1 583 ? -25.642 20.343  -7.296   1.00 41.82  ?  581 LEU B CG  1 
ATOM   8818 C  CD1 . LEU B 1 583 ? -26.071 20.165  -8.743   1.00 43.02  ?  581 LEU B CD1 1 
ATOM   8819 C  CD2 . LEU B 1 583 ? -24.331 21.113  -7.211   1.00 40.06  ?  581 LEU B CD2 1 
ATOM   8820 N  N   . TYR B 1 584 ? -28.507 21.776  -3.838   1.00 37.05  ?  582 TYR B N   1 
ATOM   8821 C  CA  . TYR B 1 584 ? -29.385 22.726  -3.167   1.00 42.00  ?  582 TYR B CA  1 
ATOM   8822 C  C   . TYR B 1 584 ? -28.694 23.324  -1.951   1.00 35.33  ?  582 TYR B C   1 
ATOM   8823 O  O   . TYR B 1 584 ? -28.850 24.515  -1.660   1.00 34.46  ?  582 TYR B O   1 
ATOM   8824 C  CB  . TYR B 1 584 ? -30.693 22.043  -2.769   1.00 33.89  ?  582 TYR B CB  1 
ATOM   8825 C  CG  . TYR B 1 584 ? -31.597 22.899  -1.914   1.00 41.23  ?  582 TYR B CG  1 
ATOM   8826 C  CD1 . TYR B 1 584 ? -32.540 23.734  -2.492   1.00 41.83  ?  582 TYR B CD1 1 
ATOM   8827 C  CD2 . TYR B 1 584 ? -31.508 22.870  -0.525   1.00 39.11  ?  582 TYR B CD2 1 
ATOM   8828 C  CE1 . TYR B 1 584 ? -33.371 24.517  -1.719   1.00 43.46  ?  582 TYR B CE1 1 
ATOM   8829 C  CE2 . TYR B 1 584 ? -32.337 23.652  0.260    1.00 49.55  ?  582 TYR B CE2 1 
ATOM   8830 C  CZ  . TYR B 1 584 ? -33.267 24.472  -0.343   1.00 39.27  ?  582 TYR B CZ  1 
ATOM   8831 O  OH  . TYR B 1 584 ? -34.094 25.255  0.425    1.00 42.59  ?  582 TYR B OH  1 
ATOM   8832 N  N   . ASP B 1 585 ? -27.919 22.512  -1.230   1.00 37.26  ?  583 ASP B N   1 
ATOM   8833 C  CA  . ASP B 1 585 ? -27.250 23.004  -0.032   1.00 44.69  ?  583 ASP B CA  1 
ATOM   8834 C  C   . ASP B 1 585 ? -26.059 23.879  -0.392   1.00 40.50  ?  583 ASP B C   1 
ATOM   8835 O  O   . ASP B 1 585 ? -25.644 24.721  0.412    1.00 40.30  ?  583 ASP B O   1 
ATOM   8836 C  CB  . ASP B 1 585 ? -26.803 21.843  0.855    1.00 44.04  ?  583 ASP B CB  1 
ATOM   8837 C  CG  . ASP B 1 585 ? -27.950 21.230  1.639    1.00 61.51  ?  583 ASP B CG  1 
ATOM   8838 O  OD1 . ASP B 1 585 ? -29.089 21.729  1.522    1.00 60.91  ?  583 ASP B OD1 1 
ATOM   8839 O  OD2 . ASP B 1 585 ? -27.709 20.259  2.389    1.00 56.76  -1 583 ASP B OD2 1 
ATOM   8840 N  N   . LYS B 1 586 ? -25.484 23.670  -1.577   1.00 42.17  ?  584 LYS B N   1 
ATOM   8841 C  CA  . LYS B 1 586 ? -24.371 24.478  -2.053   1.00 35.01  ?  584 LYS B CA  1 
ATOM   8842 C  C   . LYS B 1 586 ? -24.813 25.859  -2.525   1.00 37.99  ?  584 LYS B C   1 
ATOM   8843 O  O   . LYS B 1 586 ? -23.983 26.771  -2.596   1.00 44.51  ?  584 LYS B O   1 
ATOM   8844 C  CB  . LYS B 1 586 ? -23.648 23.734  -3.179   1.00 36.53  ?  584 LYS B CB  1 
ATOM   8845 C  CG  . LYS B 1 586 ? -22.679 22.679  -2.667   1.00 41.74  ?  584 LYS B CG  1 
ATOM   8846 C  CD  . LYS B 1 586 ? -22.196 21.753  -3.770   1.00 46.86  ?  584 LYS B CD  1 
ATOM   8847 C  CE  . LYS B 1 586 ? -21.093 20.832  -3.262   1.00 53.46  ?  584 LYS B CE  1 
ATOM   8848 N  NZ  . LYS B 1 586 ? -20.938 19.619  -4.113   1.00 66.34  ?  584 LYS B NZ  1 
ATOM   8849 N  N   . LEU B 1 587 ? -26.094 26.031  -2.846   1.00 38.53  ?  585 LEU B N   1 
ATOM   8850 C  CA  . LEU B 1 587 ? -26.596 27.311  -3.332   1.00 34.13  ?  585 LEU B CA  1 
ATOM   8851 C  C   . LEU B 1 587 ? -26.691 28.311  -2.187   1.00 37.52  ?  585 LEU B C   1 
ATOM   8852 O  O   . LEU B 1 587 ? -27.363 28.056  -1.180   1.00 37.44  ?  585 LEU B O   1 
ATOM   8853 C  CB  . LEU B 1 587 ? -27.957 27.131  -3.995   1.00 34.88  ?  585 LEU B CB  1 
ATOM   8854 C  CG  . LEU B 1 587 ? -27.951 26.555  -5.409   1.00 34.20  ?  585 LEU B CG  1 
ATOM   8855 C  CD1 . LEU B 1 587 ? -29.367 26.501  -5.959   1.00 30.36  ?  585 LEU B CD1 1 
ATOM   8856 C  CD2 . LEU B 1 587 ? -27.052 27.379  -6.312   1.00 36.37  ?  585 LEU B CD2 1 
ATOM   8857 N  N   . GLN B 1 588 ? -26.011 29.445  -2.335   1.00 34.81  ?  586 GLN B N   1 
ATOM   8858 C  CA  . GLN B 1 588 ? -26.032 30.492  -1.315   1.00 39.77  ?  586 GLN B CA  1 
ATOM   8859 C  C   . GLN B 1 588 ? -27.174 31.473  -1.589   1.00 45.19  ?  586 GLN B C   1 
ATOM   8860 O  O   . GLN B 1 588 ? -26.989 32.682  -1.719   1.00 43.29  ?  586 GLN B O   1 
ATOM   8861 C  CB  . GLN B 1 588 ? -24.681 31.194  -1.253   1.00 35.63  ?  586 GLN B CB  1 
ATOM   8862 C  CG  . GLN B 1 588 ? -23.513 30.227  -1.144   1.00 37.92  ?  586 GLN B CG  1 
ATOM   8863 C  CD  . GLN B 1 588 ? -22.197 30.920  -0.859   1.00 51.57  ?  586 GLN B CD  1 
ATOM   8864 O  OE1 . GLN B 1 588 ? -22.164 32.105  -0.524   1.00 49.21  ?  586 GLN B OE1 1 
ATOM   8865 N  NE2 . GLN B 1 588 ? -21.099 30.185  -1.004   1.00 44.20  ?  586 GLN B NE2 1 
ATOM   8866 N  N   . PHE B 1 589 ? -28.383 30.919  -1.653   1.00 38.85  ?  587 PHE B N   1 
ATOM   8867 C  CA  . PHE B 1 589 ? -29.582 31.662  -2.003   1.00 34.34  ?  587 PHE B CA  1 
ATOM   8868 C  C   . PHE B 1 589 ? -30.580 31.594  -0.858   1.00 45.44  ?  587 PHE B C   1 
ATOM   8869 O  O   . PHE B 1 589 ? -30.410 30.852  0.113    1.00 43.86  ?  587 PHE B O   1 
ATOM   8870 C  CB  . PHE B 1 589 ? -30.284 31.104  -3.253   1.00 35.40  ?  587 PHE B CB  1 
ATOM   8871 C  CG  . PHE B 1 589 ? -29.466 31.130  -4.510   1.00 39.40  ?  587 PHE B CG  1 
ATOM   8872 C  CD1 . PHE B 1 589 ? -28.329 31.910  -4.625   1.00 43.12  ?  587 PHE B CD1 1 
ATOM   8873 C  CD2 . PHE B 1 589 ? -29.880 30.392  -5.608   1.00 37.66  ?  587 PHE B CD2 1 
ATOM   8874 C  CE1 . PHE B 1 589 ? -27.602 31.921  -5.811   1.00 35.29  ?  587 PHE B CE1 1 
ATOM   8875 C  CE2 . PHE B 1 589 ? -29.165 30.401  -6.787   1.00 39.26  ?  587 PHE B CE2 1 
ATOM   8876 C  CZ  . PHE B 1 589 ? -28.024 31.167  -6.888   1.00 40.35  ?  587 PHE B CZ  1 
ATOM   8877 N  N   . THR B 1 590 ? -31.634 32.390  -0.996   1.00 45.40  ?  588 THR B N   1 
ATOM   8878 C  CA  . THR B 1 590 ? -32.683 32.446  0.007    1.00 44.03  ?  588 THR B CA  1 
ATOM   8879 C  C   . THR B 1 590 ? -33.622 31.268  -0.216   1.00 42.56  ?  588 THR B C   1 
ATOM   8880 O  O   . THR B 1 590 ? -34.109 31.055  -1.331   1.00 38.04  ?  588 THR B O   1 
ATOM   8881 C  CB  . THR B 1 590 ? -33.436 33.772  -0.086   1.00 44.75  ?  588 THR B CB  1 
ATOM   8882 O  OG1 . THR B 1 590 ? -32.549 34.846  0.250    1.00 45.41  ?  588 THR B OG1 1 
ATOM   8883 C  CG2 . THR B 1 590 ? -34.628 33.785  0.864    1.00 47.64  ?  588 THR B CG2 1 
ATOM   8884 N  N   . SER B 1 591 ? -33.847 30.483  0.834    1.00 43.63  ?  589 SER B N   1 
ATOM   8885 C  CA  . SER B 1 591 ? -34.736 29.336  0.738    1.00 43.44  ?  589 SER B CA  1 
ATOM   8886 C  C   . SER B 1 591 ? -36.191 29.788  0.748    1.00 50.23  ?  589 SER B C   1 
ATOM   8887 O  O   . SER B 1 591 ? -36.588 30.620  1.571    1.00 53.74  ?  589 SER B O   1 
ATOM   8888 C  CB  . SER B 1 591 ? -34.469 28.357  1.882    1.00 47.15  ?  589 SER B CB  1 
ATOM   8889 O  OG  . SER B 1 591 ? -34.557 29.002  3.137    1.00 58.03  ?  589 SER B OG  1 
ATOM   8890 N  N   . LEU B 1 592 ? -36.988 29.227  -0.157   1.00 51.43  ?  590 LEU B N   1 
ATOM   8891 C  CA  . LEU B 1 592 ? -38.417 29.495  -0.224   1.00 47.38  ?  590 LEU B CA  1 
ATOM   8892 C  C   . LEU B 1 592 ? -39.187 28.212  0.051    1.00 49.86  ?  590 LEU B C   1 
ATOM   8893 O  O   . LEU B 1 592 ? -38.791 27.129  -0.392   1.00 51.11  ?  590 LEU B O   1 
ATOM   8894 C  CB  . LEU B 1 592 ? -38.823 30.059  -1.591   1.00 51.95  ?  590 LEU B CB  1 
ATOM   8895 C  CG  . LEU B 1 592 ? -38.143 31.351  -2.040   1.00 57.87  ?  590 LEU B CG  1 
ATOM   8896 C  CD1 . LEU B 1 592 ? -38.633 31.759  -3.421   1.00 41.90  ?  590 LEU B CD1 1 
ATOM   8897 C  CD2 . LEU B 1 592 ? -38.415 32.453  -1.027   1.00 44.81  ?  590 LEU B CD2 1 
ATOM   8898 N  N   . GLU B 1 593 ? -40.287 28.342  0.786    1.00 49.60  ?  591 GLU B N   1 
ATOM   8899 C  CA  . GLU B 1 593 ? -41.087 27.188  1.161    1.00 56.26  ?  591 GLU B CA  1 
ATOM   8900 C  C   . GLU B 1 593 ? -42.049 26.829  0.037    1.00 55.22  ?  591 GLU B C   1 
ATOM   8901 O  O   . GLU B 1 593 ? -42.593 27.707  -0.639   1.00 66.24  ?  591 GLU B O   1 
ATOM   8902 C  CB  . GLU B 1 593 ? -41.863 27.469  2.449    1.00 57.51  ?  591 GLU B CB  1 
ATOM   8903 N  N   . ILE B 1 594 ? -42.254 25.533  -0.159   1.00 60.67  ?  592 ILE B N   1 
ATOM   8904 C  CA  . ILE B 1 594 ? -43.181 25.066  -1.196   1.00 70.70  ?  592 ILE B CA  1 
ATOM   8905 C  C   . ILE B 1 594 ? -44.611 25.385  -0.774   1.00 64.70  ?  592 ILE B C   1 
ATOM   8906 O  O   . ILE B 1 594 ? -45.035 24.984  0.326    1.00 61.69  ?  592 ILE B O   1 
ATOM   8907 C  CB  . ILE B 1 594 ? -43.007 23.566  -1.441   1.00 69.70  ?  592 ILE B CB  1 
ATOM   8908 C  CG1 . ILE B 1 594 ? -41.537 23.221  -1.708   1.00 65.07  ?  592 ILE B CG1 1 
ATOM   8909 C  CG2 . ILE B 1 594 ? -43.910 23.112  -2.581   1.00 52.76  ?  592 ILE B CG2 1 
ATOM   8910 C  CD1 . ILE B 1 594 ? -40.736 22.910  -0.453   1.00 71.47  ?  592 ILE B CD1 1 
ATOM   8911 N  N   . PRO B 1 595 ? -45.395 26.089  -1.604   1.00 67.54  ?  593 PRO B N   1 
ATOM   8912 C  CA  . PRO B 1 595 ? -46.804 26.374  -1.312   1.00 69.99  ?  593 PRO B CA  1 
ATOM   8913 C  C   . PRO B 1 595 ? -47.659 25.109  -1.247   1.00 72.67  ?  593 PRO B C   1 
ATOM   8914 O  O   . PRO B 1 595 ? -47.170 24.034  -1.598   1.00 78.61  ?  593 PRO B O   1 
ATOM   8915 C  CB  . PRO B 1 595 ? -47.233 27.256  -2.492   1.00 68.00  ?  593 PRO B CB  1 
ATOM   8916 C  CG  . PRO B 1 595 ? -45.950 27.831  -3.018   1.00 65.46  ?  593 PRO B CG  1 
ATOM   8917 C  CD  . PRO B 1 595 ? -44.964 26.717  -2.864   1.00 67.53  ?  593 PRO B CD  1 
HETATM 8918 ZN ZN  . ZN  C 2 .   ? -2.597  70.549  -52.789  1.00 57.54  ?  701 ZN  A ZN  1 
HETATM 8919 ZN ZN  . ZN  D 2 .   ? -2.711  50.799  -62.854  1.00 72.37  ?  702 ZN  A ZN  1 
HETATM 8920 ZN ZN  . ZN  E 2 .   ? 9.833   46.526  -61.508  1.00 119.33 ?  703 ZN  A ZN  1 
HETATM 8921 P  P   . PO4 F 3 .   ? -11.222 10.103  -77.253  1.00 43.51  ?  704 PO4 A P   1 
HETATM 8922 O  O1  . PO4 F 3 .   ? -11.258 10.134  -75.744  1.00 58.11  ?  704 PO4 A O1  1 
HETATM 8923 O  O2  . PO4 F 3 .   ? -9.897  10.639  -77.743  1.00 47.54  ?  704 PO4 A O2  1 
HETATM 8924 O  O3  . PO4 F 3 .   ? -11.378 8.680   -77.730  1.00 55.71  -1 704 PO4 A O3  1 
HETATM 8925 O  O4  . PO4 F 3 .   ? -12.344 10.954  -77.796  1.00 47.96  ?  704 PO4 A O4  1 
HETATM 8926 P  P   . PO4 G 3 .   ? -13.422 14.656  -78.526  1.00 42.80  ?  705 PO4 A P   1 
HETATM 8927 O  O1  . PO4 G 3 .   ? -11.979 14.792  -78.949  1.00 38.96  ?  705 PO4 A O1  1 
HETATM 8928 O  O2  . PO4 G 3 .   ? -14.084 16.014  -78.508  1.00 47.32  ?  705 PO4 A O2  1 
HETATM 8929 O  O3  . PO4 G 3 .   ? -14.145 13.764  -79.509  1.00 44.44  -1 705 PO4 A O3  1 
HETATM 8930 O  O4  . PO4 G 3 .   ? -13.488 14.058  -77.140  1.00 51.74  ?  705 PO4 A O4  1 
HETATM 8931 S  S1  . MPO H 4 .   ? -26.224 30.835  -79.646  0.72 67.97  ?  706 MPO A S1  1 
HETATM 8932 O  O1  . MPO H 4 .   ? -26.587 29.440  -79.722  0.72 56.76  ?  706 MPO A O1  1 
HETATM 8933 O  O2  . MPO H 4 .   ? -25.949 31.342  -78.323  0.72 68.93  ?  706 MPO A O2  1 
HETATM 8934 O  O4  . MPO H 4 .   ? -20.145 35.603  -81.315  0.72 65.41  ?  706 MPO A O4  1 
HETATM 8935 N  N1  . MPO H 4 .   ? -22.540 34.046  -81.453  0.72 55.25  ?  706 MPO A N1  1 
HETATM 8936 C  C1  . MPO H 4 .   ? -24.748 31.040  -80.596  0.72 56.03  ?  706 MPO A C1  1 
HETATM 8937 O  O3  . MPO H 4 .   ? -27.247 31.664  -80.325  0.72 60.81  ?  706 MPO A O3  1 
HETATM 8938 C  C2  . MPO H 4 .   ? -24.214 32.459  -80.513  0.72 55.45  ?  706 MPO A C2  1 
HETATM 8939 C  C3  . MPO H 4 .   ? -23.235 32.765  -81.630  0.72 52.68  ?  706 MPO A C3  1 
HETATM 8940 C  C4  . MPO H 4 .   ? -21.767 34.393  -82.649  0.72 57.63  ?  706 MPO A C4  1 
HETATM 8941 C  C5  . MPO H 4 .   ? -21.024 35.685  -82.431  0.72 62.72  ?  706 MPO A C5  1 
HETATM 8942 C  C6  . MPO H 4 .   ? -20.886 35.271  -80.148  0.72 61.91  ?  706 MPO A C6  1 
HETATM 8943 C  C7  . MPO H 4 .   ? -21.623 33.968  -80.312  0.72 56.75  ?  706 MPO A C7  1 
HETATM 8944 ZN ZN  . ZN  I 2 .   ? -6.220  -2.564  -36.023  1.00 47.17  ?  701 ZN  B ZN  1 
HETATM 8945 ZN ZN  . ZN  J 2 .   ? 6.224   0.619   -35.413  1.00 62.51  ?  702 ZN  B ZN  1 
HETATM 8946 ZN ZN  . ZN  K 2 .   ? -6.844  -20.083 -49.855  1.00 84.27  ?  703 ZN  B ZN  1 
HETATM 8947 P  P   . PO4 L 3 .   ? -17.622 36.918  -20.775  0.93 43.57  ?  704 PO4 B P   1 
HETATM 8948 O  O1  . PO4 L 3 .   ? -16.353 36.436  -20.114  0.93 40.71  ?  704 PO4 B O1  1 
HETATM 8949 O  O2  . PO4 L 3 .   ? -17.848 38.372  -20.437  0.93 55.49  ?  704 PO4 B O2  1 
HETATM 8950 O  O3  . PO4 L 3 .   ? -17.504 36.768  -22.271  0.93 40.75  -1 704 PO4 B O3  1 
HETATM 8951 O  O4  . PO4 L 3 .   ? -18.784 36.098  -20.265  0.93 44.96  ?  704 PO4 B O4  1 
HETATM 8952 P  P   . PO4 M 3 .   ? -19.809 32.607  -20.326  1.00 44.36  ?  705 PO4 B P   1 
HETATM 8953 O  O1  . PO4 M 3 .   ? -18.418 32.435  -19.767  1.00 36.74  ?  705 PO4 B O1  1 
HETATM 8954 O  O2  . PO4 M 3 .   ? -19.749 33.435  -21.588  1.00 41.68  ?  705 PO4 B O2  1 
HETATM 8955 O  O3  . PO4 M 3 .   ? -20.416 31.256  -20.638  1.00 43.52  -1 705 PO4 B O3  1 
HETATM 8956 O  O4  . PO4 M 3 .   ? -20.669 33.310  -19.308  1.00 42.40  ?  705 PO4 B O4  1 
HETATM 8957 S  S1  . MPO N 4 .   ? -32.246 16.373  -23.721  0.84 58.89  ?  706 MPO B S1  1 
HETATM 8958 O  O1  . MPO N 4 .   ? -33.205 15.887  -22.757  0.84 53.23  ?  706 MPO B O1  1 
HETATM 8959 O  O2  . MPO N 4 .   ? -32.386 17.756  -24.110  0.84 55.84  ?  706 MPO B O2  1 
HETATM 8960 O  O4  . MPO N 4 .   ? -28.131 10.844  -20.857  0.84 62.92  ?  706 MPO B O4  1 
HETATM 8961 N  N1  . MPO N 4 .   ? -28.593 13.299  -21.595  0.84 60.73  ?  706 MPO B N1  1 
HETATM 8962 C  C1  . MPO N 4 .   ? -30.648 16.202  -22.989  0.84 53.35  ?  706 MPO B C1  1 
HETATM 8963 O  O3  . MPO N 4 .   ? -32.231 15.487  -24.908  0.84 66.31  ?  706 MPO B O3  1 
HETATM 8964 C  C2  . MPO N 4 .   ? -30.365 14.779  -22.544  0.84 55.23  ?  706 MPO B C2  1 
HETATM 8965 C  C3  . MPO N 4 .   ? -28.943 14.646  -22.054  0.84 54.35  ?  706 MPO B C3  1 
HETATM 8966 C  C4  . MPO N 4 .   ? -29.541 12.796  -20.598  0.84 56.12  ?  706 MPO B C4  1 
HETATM 8967 C  C5  . MPO N 4 .   ? -29.440 11.295  -20.514  0.84 65.47  ?  706 MPO B C5  1 
HETATM 8968 C  C6  . MPO N 4 .   ? -27.899 11.064  -22.245  0.84 66.30  ?  706 MPO B C6  1 
HETATM 8969 C  C7  . MPO N 4 .   ? -28.528 12.350  -22.709  0.84 63.88  ?  706 MPO B C7  1 
HETATM 8970 C  C1  . MYC O 5 .   ? 5.739   16.483  -35.411  0.76 81.22  ?  707 MYC B C1  1 
HETATM 8971 C  C2  . MYC O 5 .   ? 4.946   17.137  -36.361  0.76 78.42  ?  707 MYC B C2  1 
HETATM 8972 C  C3  . MYC O 5 .   ? 4.694   18.534  -36.202  0.76 74.65  ?  707 MYC B C3  1 
HETATM 8973 C  C4  . MYC O 5 .   ? 5.250   19.192  -35.087  0.76 76.24  ?  707 MYC B C4  1 
HETATM 8974 C  C5  . MYC O 5 .   ? 6.036   18.534  -34.142  0.76 80.18  ?  707 MYC B C5  1 
HETATM 8975 C  C6  . MYC O 5 .   ? 6.282   17.163  -34.307  0.76 81.85  ?  707 MYC B C6  1 
HETATM 8976 C  C9  . MYC O 5 .   ? 3.893   19.275  -37.135  0.76 72.39  ?  707 MYC B C9  1 
HETATM 8977 C  C10 . MYC O 5 .   ? 3.704   20.693  -36.858  0.76 72.12  ?  707 MYC B C10 1 
HETATM 8978 C  C11 . MYC O 5 .   ? 4.281   21.255  -35.750  0.76 73.69  ?  707 MYC B C11 1 
HETATM 8979 C  C14 . MYC O 5 .   ? 4.192   22.673  -35.357  0.76 73.78  ?  707 MYC B C14 1 
HETATM 8980 C  C15 . MYC O 5 .   ? 3.001   23.380  -35.550  0.76 69.29  ?  707 MYC B C15 1 
HETATM 8981 C  C16 . MYC O 5 .   ? 2.899   24.717  -35.196  0.76 69.52  ?  707 MYC B C16 1 
HETATM 8982 C  C17 . MYC O 5 .   ? 4.003   25.389  -34.634  0.76 76.13  ?  707 MYC B C17 1 
HETATM 8983 C  C18 . MYC O 5 .   ? 5.214   24.687  -34.434  0.76 78.18  ?  707 MYC B C18 1 
HETATM 8984 C  C19 . MYC O 5 .   ? 5.296   23.333  -34.802  0.76 77.01  ?  707 MYC B C19 1 
HETATM 8985 O  O12 . MYC O 5 .   ? 5.031   20.504  -34.903  0.76 76.64  ?  707 MYC B O12 1 
HETATM 8986 O  O13 . MYC O 5 .   ? 3.360   18.786  -38.144  0.76 81.27  ?  707 MYC B O13 1 
HETATM 8987 O  O23 . MYC O 5 .   ? 6.323   25.274  -33.896  0.76 97.12  ?  707 MYC B O23 1 
HETATM 8988 O  O24 . MYC O 5 .   ? 3.990   26.697  -34.256  0.76 99.20  ?  707 MYC B O24 1 
HETATM 8989 O  O25 . MYC O 5 .   ? 1.766   25.453  -35.358  0.76 82.37  ?  707 MYC B O25 1 
HETATM 8990 O  O27 . MYC O 5 .   ? 2.961   21.456  -37.711  0.76 74.08  ?  707 MYC B O27 1 
HETATM 8991 O  O29 . MYC O 5 .   ? 7.047   16.550  -33.377  0.76 86.89  ?  707 MYC B O29 1 
HETATM 8992 O  O30 . MYC O 5 .   ? 4.477   16.403  -37.389  0.76 90.70  ?  707 MYC B O30 1 
HETATM 8993 H  H1  . MYC O 5 .   ? 5.906   15.575  -35.520  0.76 97.49  ?  707 MYC B H1  1 
HETATM 8994 H  H5  . MYC O 5 .   ? 6.389   18.995  -33.416  0.76 96.24  ?  707 MYC B H5  1 
HETATM 8995 H  H15 . MYC O 5 .   ? 2.257   22.962  -35.920  0.76 83.17  ?  707 MYC B H15 1 
HETATM 8996 H  H19 . MYC O 5 .   ? 6.103   22.890  -34.665  0.76 92.43  ?  707 MYC B H19 1 
HETATM 8997 H  HO3 . MYC O 5 .   ? 6.207   26.090  -33.659  0.76 116.57 ?  707 MYC B HO3 1 
HETATM 8998 H  HO4 . MYC O 5 .   ? 3.257   27.102  -34.435  0.76 119.06 ?  707 MYC B HO4 1 
HETATM 8999 H  HO5 . MYC O 5 .   ? 1.115   25.017  -35.715  0.76 98.87  ?  707 MYC B HO5 1 
HETATM 9000 H  HO7 . MYC O 5 .   ? 2.598   21.005  -38.346  0.76 88.92  ?  707 MYC B HO7 1 
HETATM 9001 H  HO9 . MYC O 5 .   ? 7.157   15.707  -33.501  0.76 104.30 ?  707 MYC B HO9 1 
HETATM 9002 H  HO0 . MYC O 5 .   ? 3.867   16.794  -37.852  0.76 108.86 ?  707 MYC B HO0 1 
HETATM 9003 O  O   . HOH P 6 .   ? -21.748 19.530  -104.824 1.00 45.44  ?  801 HOH A O   1 
HETATM 9004 O  O   . HOH P 6 .   ? 3.850   32.015  -59.162  1.00 77.06  ?  802 HOH A O   1 
HETATM 9005 O  O   . HOH P 6 .   ? -16.523 20.073  -74.149  1.00 61.30  ?  803 HOH A O   1 
HETATM 9006 O  O   . HOH P 6 .   ? -24.858 13.719  -75.929  1.00 54.88  ?  804 HOH A O   1 
HETATM 9007 O  O   . HOH P 6 .   ? -27.207 30.280  -94.893  1.00 33.87  ?  805 HOH A O   1 
HETATM 9008 O  O   . HOH P 6 .   ? -19.900 9.154   -57.841  1.00 83.36  ?  806 HOH A O   1 
HETATM 9009 O  O   . HOH P 6 .   ? -6.959  45.363  -68.137  1.00 58.70  ?  807 HOH A O   1 
HETATM 9010 O  O   . HOH P 6 .   ? -9.922  27.921  -73.638  1.00 46.66  ?  808 HOH A O   1 
HETATM 9011 O  O   . HOH P 6 .   ? 5.755   66.642  -43.583  1.00 72.02  ?  809 HOH A O   1 
HETATM 9012 O  O   . HOH P 6 .   ? -2.782  4.390   -60.150  1.00 78.63  ?  810 HOH A O   1 
HETATM 9013 O  O   . HOH P 6 .   ? -20.855 5.064   -78.445  1.00 56.95  ?  811 HOH A O   1 
HETATM 9014 O  O   . HOH P 6 .   ? -20.717 8.665   -103.943 1.00 36.51  ?  812 HOH A O   1 
HETATM 9015 O  O   . HOH P 6 .   ? -31.286 28.394  -100.593 1.00 41.87  ?  813 HOH A O   1 
HETATM 9016 O  O   . HOH P 6 .   ? -13.709 28.132  -92.540  1.00 40.96  ?  814 HOH A O   1 
HETATM 9017 O  O   . HOH P 6 .   ? -30.540 22.928  -74.583  1.00 85.29  ?  815 HOH A O   1 
HETATM 9018 O  O   . HOH P 6 .   ? -9.316  33.557  -70.722  1.00 52.29  ?  816 HOH A O   1 
HETATM 9019 O  O   . HOH P 6 .   ? -12.880 30.263  -96.517  1.00 47.18  ?  817 HOH A O   1 
HETATM 9020 O  O   . HOH P 6 .   ? -9.350  19.939  -75.876  1.00 45.33  ?  818 HOH A O   1 
HETATM 9021 O  O   . HOH P 6 .   ? -40.714 26.251  -90.539  1.00 58.13  ?  819 HOH A O   1 
HETATM 9022 O  O   . HOH P 6 .   ? -12.086 10.614  -98.865  1.00 47.98  ?  820 HOH A O   1 
HETATM 9023 O  O   . HOH P 6 .   ? -10.030 45.929  -82.294  1.00 57.61  ?  821 HOH A O   1 
HETATM 9024 O  O   . HOH P 6 .   ? -17.804 18.772  -103.977 1.00 39.10  ?  822 HOH A O   1 
HETATM 9025 O  O   . HOH P 6 .   ? -14.560 23.782  -62.897  1.00 59.78  ?  823 HOH A O   1 
HETATM 9026 O  O   . HOH P 6 .   ? -4.935  23.987  -84.121  1.00 52.55  ?  824 HOH A O   1 
HETATM 9027 O  O   . HOH P 6 .   ? -6.365  7.344   -92.998  1.00 50.23  ?  825 HOH A O   1 
HETATM 9028 O  O   . HOH P 6 .   ? -12.830 1.451   -84.604  1.00 54.30  ?  826 HOH A O   1 
HETATM 9029 O  O   . HOH P 6 .   ? -2.376  21.575  -93.407  1.00 51.82  ?  827 HOH A O   1 
HETATM 9030 O  O   . HOH P 6 .   ? -4.209  21.182  -91.357  1.00 39.72  ?  828 HOH A O   1 
HETATM 9031 O  O   . HOH P 6 .   ? -43.782 7.379   -85.786  1.00 61.51  ?  829 HOH A O   1 
HETATM 9032 O  O   . HOH P 6 .   ? -13.710 37.466  -71.808  1.00 52.95  ?  830 HOH A O   1 
HETATM 9033 O  O   . HOH P 6 .   ? -38.846 29.409  -79.786  1.00 74.61  ?  831 HOH A O   1 
HETATM 9034 O  O   . HOH P 6 .   ? -10.584 19.317  -95.580  1.00 39.17  ?  832 HOH A O   1 
HETATM 9035 O  O   . HOH P 6 .   ? -8.798  48.080  -74.902  1.00 53.79  ?  833 HOH A O   1 
HETATM 9036 O  O   . HOH P 6 .   ? 3.415   4.956   -76.498  1.00 66.82  ?  834 HOH A O   1 
HETATM 9037 O  O   . HOH P 6 .   ? -11.183 21.180  -68.996  1.00 52.93  ?  835 HOH A O   1 
HETATM 9038 O  O   . HOH P 6 .   ? -10.759 18.234  -97.904  1.00 39.33  ?  836 HOH A O   1 
HETATM 9039 O  O   . HOH P 6 .   ? -12.803 26.981  -67.986  1.00 57.75  ?  837 HOH A O   1 
HETATM 9040 O  O   . HOH P 6 .   ? 3.009   74.040  -46.997  1.00 60.37  ?  838 HOH A O   1 
HETATM 9041 O  O   . HOH P 6 .   ? -16.624 30.140  -98.611  1.00 45.66  ?  839 HOH A O   1 
HETATM 9042 O  O   . HOH P 6 .   ? -2.913  29.020  -83.516  1.00 49.25  ?  840 HOH A O   1 
HETATM 9043 O  O   . HOH P 6 .   ? -28.213 27.615  -101.988 1.00 38.62  ?  841 HOH A O   1 
HETATM 9044 O  O   . HOH P 6 .   ? -18.338 25.436  -87.757  1.00 40.23  ?  842 HOH A O   1 
HETATM 9045 O  O   . HOH P 6 .   ? -5.934  31.680  -71.252  1.00 45.57  ?  843 HOH A O   1 
HETATM 9046 O  O   . HOH P 6 .   ? -7.654  0.136   -90.724  1.00 52.04  ?  844 HOH A O   1 
HETATM 9047 O  O   . HOH P 6 .   ? -12.887 13.926  -70.294  1.00 61.76  ?  845 HOH A O   1 
HETATM 9048 O  O   . HOH P 6 .   ? -11.335 48.644  -77.026  1.00 48.02  ?  846 HOH A O   1 
HETATM 9049 O  O   . HOH P 6 .   ? -25.053 34.145  -93.702  1.00 44.48  ?  847 HOH A O   1 
HETATM 9050 O  O   . HOH P 6 .   ? -35.288 31.039  -91.252  1.00 40.32  ?  848 HOH A O   1 
HETATM 9051 O  O   . HOH P 6 .   ? -27.396 6.201   -94.946  1.00 49.38  ?  849 HOH A O   1 
HETATM 9052 O  O   . HOH P 6 .   ? -20.479 30.657  -99.638  1.00 46.16  ?  850 HOH A O   1 
HETATM 9053 O  O   . HOH P 6 .   ? -21.582 1.646   -93.649  1.00 41.10  ?  851 HOH A O   1 
HETATM 9054 O  O   . HOH P 6 .   ? -20.022 21.881  -65.945  1.00 60.60  ?  852 HOH A O   1 
HETATM 9055 O  O   . HOH P 6 .   ? 6.594   28.710  -63.707  1.00 71.13  ?  853 HOH A O   1 
HETATM 9056 O  O   . HOH P 6 .   ? -11.488 29.300  -88.865  1.00 41.79  ?  854 HOH A O   1 
HETATM 9057 O  O   . HOH P 6 .   ? -25.949 7.099   -81.236  1.00 47.61  ?  855 HOH A O   1 
HETATM 9058 O  O   . HOH P 6 .   ? -4.176  54.526  -70.233  1.00 66.13  ?  856 HOH A O   1 
HETATM 9059 O  O   . HOH P 6 .   ? -5.755  5.202   -92.991  1.00 54.60  ?  857 HOH A O   1 
HETATM 9060 O  O   . HOH P 6 .   ? -22.331 10.374  -76.344  1.00 60.52  ?  858 HOH A O   1 
HETATM 9061 O  O   . HOH P 6 .   ? -7.224  42.949  -81.754  1.00 50.46  ?  859 HOH A O   1 
HETATM 9062 O  O   . HOH P 6 .   ? -17.237 3.075   -91.410  1.00 42.56  ?  860 HOH A O   1 
HETATM 9063 O  O   . HOH P 6 .   ? -6.263  10.597  -93.716  1.00 56.42  ?  861 HOH A O   1 
HETATM 9064 O  O   . HOH P 6 .   ? -4.538  7.094   -81.839  1.00 50.61  ?  862 HOH A O   1 
HETATM 9065 O  O   . HOH P 6 .   ? -4.676  12.321  -93.810  1.00 49.54  ?  863 HOH A O   1 
HETATM 9066 O  O   . HOH P 6 .   ? -14.381 10.204  -99.238  1.00 49.95  ?  864 HOH A O   1 
HETATM 9067 O  O   . HOH P 6 .   ? -8.569  -3.659  -64.935  1.00 63.57  ?  865 HOH A O   1 
HETATM 9068 O  O   . HOH P 6 .   ? -6.667  47.237  -76.160  1.00 57.85  ?  866 HOH A O   1 
HETATM 9069 O  O   . HOH P 6 .   ? -5.161  64.453  -59.903  1.00 65.48  ?  867 HOH A O   1 
HETATM 9070 O  O   . HOH P 6 .   ? -11.642 33.984  -69.830  1.00 60.19  ?  868 HOH A O   1 
HETATM 9071 O  O   . HOH P 6 .   ? -24.033 15.808  -74.620  1.00 58.82  ?  869 HOH A O   1 
HETATM 9072 O  O   . HOH P 6 .   ? -14.332 9.656   -73.955  1.00 65.10  ?  870 HOH A O   1 
HETATM 9073 O  O   . HOH P 6 .   ? -14.638 29.293  -94.721  1.00 39.66  ?  871 HOH A O   1 
HETATM 9074 O  O   . HOH P 6 .   ? -37.852 32.258  -88.175  1.00 49.48  ?  872 HOH A O   1 
HETATM 9075 O  O   . HOH P 6 .   ? -38.948 24.026  -91.723  1.00 52.20  ?  873 HOH A O   1 
HETATM 9076 O  O   . HOH P 6 .   ? -20.020 35.366  -85.848  1.00 45.58  ?  874 HOH A O   1 
HETATM 9077 O  O   . HOH P 6 .   ? 12.173  7.696   -57.446  1.00 67.69  ?  875 HOH A O   1 
HETATM 9078 O  O   . HOH P 6 .   ? -21.252 31.797  -102.246 1.00 51.37  ?  876 HOH A O   1 
HETATM 9079 O  O   . HOH P 6 .   ? -26.413 1.953   -95.079  1.00 51.93  ?  877 HOH A O   1 
HETATM 9080 O  O   . HOH P 6 .   ? -28.304 1.495   -93.353  1.00 50.49  ?  878 HOH A O   1 
HETATM 9081 O  O   . HOH P 6 .   ? -8.192  21.451  -96.607  1.00 43.94  ?  879 HOH A O   1 
HETATM 9082 O  O   . HOH P 6 .   ? -10.655 17.433  -75.948  1.00 51.30  ?  880 HOH A O   1 
HETATM 9083 O  O   . HOH P 6 .   ? -37.707 31.315  -93.500  1.00 44.78  ?  881 HOH A O   1 
HETATM 9084 O  O   . HOH Q 6 .   ? 1.076   1.618   -27.068  1.00 64.05  ?  801 HOH B O   1 
HETATM 9085 O  O   . HOH Q 6 .   ? -28.494 20.896  -20.838  1.00 44.88  ?  802 HOH B O   1 
HETATM 9086 O  O   . HOH Q 6 .   ? -8.277  28.301  -10.803  1.00 56.05  ?  803 HOH B O   1 
HETATM 9087 O  O   . HOH Q 6 .   ? -1.093  35.041  -14.741  1.00 44.75  ?  804 HOH B O   1 
HETATM 9088 O  O   . HOH Q 6 .   ? -18.789 38.040  -2.818   1.00 54.09  ?  805 HOH B O   1 
HETATM 9089 O  O   . HOH Q 6 .   ? -27.810 12.381  -8.181   1.00 48.58  ?  806 HOH B O   1 
HETATM 9090 O  O   . HOH Q 6 .   ? 2.479   46.143  -32.058  1.00 47.94  ?  807 HOH B O   1 
HETATM 9091 O  O   . HOH Q 6 .   ? -31.011 14.245  -2.851   1.00 45.22  ?  808 HOH B O   1 
HETATM 9092 O  O   . HOH Q 6 .   ? -38.155 3.543   -36.389  1.00 65.47  ?  809 HOH B O   1 
HETATM 9093 O  O   . HOH Q 6 .   ? -36.026 11.848  -29.023  1.00 68.81  ?  810 HOH B O   1 
HETATM 9094 O  O   . HOH Q 6 .   ? -4.654  15.641  -23.494  1.00 45.24  ?  811 HOH B O   1 
HETATM 9095 O  O   . HOH Q 6 .   ? -23.771 40.553  -39.006  1.00 59.83  ?  812 HOH B O   1 
HETATM 9096 O  O   . HOH Q 6 .   ? -37.400 12.792  -26.217  1.00 55.98  ?  813 HOH B O   1 
HETATM 9097 O  O   . HOH Q 6 .   ? -15.736 30.313  -40.594  1.00 50.96  ?  814 HOH B O   1 
HETATM 9098 O  O   . HOH Q 6 .   ? 7.306   32.471  -30.536  1.00 48.18  ?  815 HOH B O   1 
HETATM 9099 O  O   . HOH Q 6 .   ? -35.763 9.690   -31.137  1.00 65.82  ?  816 HOH B O   1 
HETATM 9100 O  O   . HOH Q 6 .   ? -11.321 -2.549  -26.546  1.00 50.47  ?  817 HOH B O   1 
HETATM 9101 O  O   . HOH Q 6 .   ? -40.093 36.175  -20.226  1.00 41.38  ?  818 HOH B O   1 
HETATM 9102 O  O   . HOH Q 6 .   ? -22.460 12.007  -23.362  1.00 58.15  ?  819 HOH B O   1 
HETATM 9103 O  O   . HOH Q 6 .   ? -27.453 35.866  0.977    1.00 55.10  ?  820 HOH B O   1 
HETATM 9104 O  O   . HOH Q 6 .   ? -28.974 12.440  -5.769   1.00 44.43  ?  821 HOH B O   1 
HETATM 9105 O  O   . HOH Q 6 .   ? 9.358   22.764  -25.324  1.00 49.51  ?  822 HOH B O   1 
HETATM 9106 O  O   . HOH Q 6 .   ? -25.826 30.952  -25.352  1.00 45.78  ?  823 HOH B O   1 
HETATM 9107 O  O   . HOH Q 6 .   ? 3.110   28.080  -18.210  1.00 52.21  ?  824 HOH B O   1 
HETATM 9108 O  O   . HOH Q 6 .   ? -16.991 27.030  -29.801  1.00 46.08  ?  825 HOH B O   1 
HETATM 9109 O  O   . HOH Q 6 .   ? -14.518 19.548  -25.539  1.00 42.45  ?  826 HOH B O   1 
HETATM 9110 O  O   . HOH Q 6 .   ? -1.635  14.328  -20.403  1.00 50.20  ?  827 HOH B O   1 
HETATM 9111 O  O   . HOH Q 6 .   ? -17.778 41.918  -22.928  1.00 53.26  ?  828 HOH B O   1 
HETATM 9112 O  O   . HOH Q 6 .   ? -26.510 43.028  -7.455   1.00 46.48  ?  829 HOH B O   1 
HETATM 9113 O  O   . HOH Q 6 .   ? -4.409  -9.933  -43.818  1.00 58.21  ?  830 HOH B O   1 
HETATM 9114 O  O   . HOH Q 6 .   ? -41.081 29.611  -25.050  1.00 46.60  ?  831 HOH B O   1 
HETATM 9115 O  O   . HOH Q 6 .   ? -34.707 38.348  -18.081  1.00 42.18  ?  832 HOH B O   1 
HETATM 9116 O  O   . HOH Q 6 .   ? 1.254   33.051  -25.214  1.00 36.79  ?  833 HOH B O   1 
HETATM 9117 O  O   . HOH Q 6 .   ? -46.706 29.285  -24.647  1.00 39.49  ?  834 HOH B O   1 
HETATM 9118 O  O   . HOH Q 6 .   ? -16.141 40.039  -22.866  1.00 40.45  ?  835 HOH B O   1 
HETATM 9119 O  O   . HOH Q 6 .   ? -20.848 40.732  -10.042  1.00 47.29  ?  836 HOH B O   1 
HETATM 9120 O  O   . HOH Q 6 .   ? -39.309 17.274  -2.687   1.00 45.25  ?  837 HOH B O   1 
HETATM 9121 O  O   . HOH Q 6 .   ? -2.068  26.236  -18.529  1.00 37.92  ?  838 HOH B O   1 
HETATM 9122 O  O   . HOH Q 6 .   ? -9.052  42.002  -16.454  1.00 46.82  ?  839 HOH B O   1 
HETATM 9123 O  O   . HOH Q 6 .   ? 5.775   -21.818 -45.964  1.00 70.38  ?  840 HOH B O   1 
HETATM 9124 O  O   . HOH Q 6 .   ? 3.418   21.607  -25.192  1.00 46.05  ?  841 HOH B O   1 
HETATM 9125 O  O   . HOH Q 6 .   ? -21.227 26.943  -35.904  1.00 54.05  ?  842 HOH B O   1 
HETATM 9126 O  O   . HOH Q 6 .   ? -17.410 16.240  -29.083  1.00 50.54  ?  843 HOH B O   1 
HETATM 9127 O  O   . HOH Q 6 .   ? -14.042 26.813  -29.782  1.00 44.17  ?  844 HOH B O   1 
HETATM 9128 O  O   . HOH Q 6 .   ? -13.801 25.427  -6.117   1.00 45.85  ?  845 HOH B O   1 
HETATM 9129 O  O   . HOH Q 6 .   ? -3.050  43.807  -33.546  1.00 38.17  ?  846 HOH B O   1 
HETATM 9130 O  O   . HOH Q 6 .   ? -15.264 31.802  -24.263  1.00 42.53  ?  847 HOH B O   1 
HETATM 9131 O  O   . HOH Q 6 .   ? -10.602 15.916  -26.750  1.00 37.29  ?  848 HOH B O   1 
HETATM 9132 O  O   . HOH Q 6 .   ? -14.603 27.459  -22.525  1.00 40.02  ?  849 HOH B O   1 
HETATM 9133 O  O   . HOH Q 6 .   ? -30.638 12.036  -17.439  1.00 48.95  ?  850 HOH B O   1 
HETATM 9134 O  O   . HOH Q 6 .   ? -6.847  12.533  -28.370  1.00 34.51  ?  851 HOH B O   1 
HETATM 9135 O  O   . HOH Q 6 .   ? -12.229 2.606   -31.721  1.00 44.96  ?  852 HOH B O   1 
HETATM 9136 O  O   . HOH Q 6 .   ? 3.166   41.193  -38.640  1.00 57.40  ?  853 HOH B O   1 
HETATM 9137 O  O   . HOH Q 6 .   ? -21.781 19.139  -23.241  1.00 47.38  ?  854 HOH B O   1 
HETATM 9138 O  O   . HOH Q 6 .   ? -42.470 8.207   -17.803  1.00 37.85  ?  855 HOH B O   1 
HETATM 9139 O  O   . HOH Q 6 .   ? -4.696  48.042  -34.953  1.00 53.28  ?  856 HOH B O   1 
HETATM 9140 O  O   . HOH Q 6 .   ? -10.896 17.497  -14.077  1.00 47.04  ?  857 HOH B O   1 
HETATM 9141 O  O   . HOH Q 6 .   ? -30.383 5.301   -42.807  1.00 60.85  ?  858 HOH B O   1 
HETATM 9142 O  O   . HOH Q 6 .   ? -11.566 25.804  -12.592  1.00 46.83  ?  859 HOH B O   1 
HETATM 9143 O  O   . HOH Q 6 .   ? -35.084 24.651  -25.139  1.00 40.56  ?  860 HOH B O   1 
HETATM 9144 O  O   . HOH Q 6 .   ? -18.454 10.819  -28.728  1.00 46.22  ?  861 HOH B O   1 
HETATM 9145 O  O   . HOH Q 6 .   ? -21.342 13.940  -24.031  1.00 56.38  ?  862 HOH B O   1 
HETATM 9146 O  O   . HOH Q 6 .   ? -21.664 9.429   -13.758  1.00 49.65  ?  863 HOH B O   1 
HETATM 9147 O  O   . HOH Q 6 .   ? -22.812 34.741  -31.187  1.00 46.68  ?  864 HOH B O   1 
HETATM 9148 O  O   . HOH Q 6 .   ? -3.158  18.016  -38.019  1.00 39.86  ?  865 HOH B O   1 
HETATM 9149 O  O   . HOH Q 6 .   ? -43.657 15.183  -14.944  1.00 37.88  ?  866 HOH B O   1 
HETATM 9150 O  O   . HOH Q 6 .   ? -20.840 45.143  -31.835  1.00 56.73  ?  867 HOH B O   1 
HETATM 9151 O  O   . HOH Q 6 .   ? -36.602 15.281  -8.858   1.00 40.05  ?  868 HOH B O   1 
HETATM 9152 O  O   . HOH Q 6 .   ? -15.607 20.711  -31.270  1.00 45.26  ?  869 HOH B O   1 
HETATM 9153 O  O   . HOH Q 6 .   ? -8.595  3.450   -36.489  1.00 44.02  ?  870 HOH B O   1 
HETATM 9154 O  O   . HOH Q 6 .   ? -45.556 16.320  -6.090   1.00 53.98  ?  871 HOH B O   1 
HETATM 9155 O  O   . HOH Q 6 .   ? -13.601 11.499  -16.025  1.00 47.40  ?  872 HOH B O   1 
HETATM 9156 O  O   . HOH Q 6 .   ? -24.801 15.912  -6.598   1.00 46.63  ?  873 HOH B O   1 
HETATM 9157 O  O   . HOH Q 6 .   ? -22.540 10.385  -33.706  1.00 52.65  ?  874 HOH B O   1 
HETATM 9158 O  O   . HOH Q 6 .   ? 1.346   19.471  -39.991  1.00 53.63  ?  875 HOH B O   1 
HETATM 9159 O  O   . HOH Q 6 .   ? 11.180  42.933  -26.402  1.00 52.10  ?  876 HOH B O   1 
HETATM 9160 O  O   . HOH Q 6 .   ? -23.799 28.112  -26.777  1.00 49.74  ?  877 HOH B O   1 
HETATM 9161 O  O   . HOH Q 6 .   ? -3.142  41.780  -16.420  1.00 43.54  ?  878 HOH B O   1 
HETATM 9162 O  O   . HOH Q 6 .   ? 9.144   44.432  -28.165  1.00 53.10  ?  879 HOH B O   1 
HETATM 9163 O  O   . HOH Q 6 .   ? -4.812  27.484  -47.377  1.00 59.76  ?  880 HOH B O   1 
HETATM 9164 O  O   . HOH Q 6 .   ? -23.079 6.224   -16.614  1.00 44.22  ?  881 HOH B O   1 
HETATM 9165 O  O   . HOH Q 6 .   ? 3.060   43.618  -32.218  1.00 44.19  ?  882 HOH B O   1 
HETATM 9166 O  O   . HOH Q 6 .   ? -27.471 11.247  -16.283  1.00 37.23  ?  883 HOH B O   1 
HETATM 9167 O  O   . HOH Q 6 .   ? -14.746 14.396  -32.157  1.00 46.98  ?  884 HOH B O   1 
HETATM 9168 O  O   . HOH Q 6 .   ? -2.448  45.355  -15.536  1.00 46.99  ?  885 HOH B O   1 
HETATM 9169 O  O   . HOH Q 6 .   ? -16.594 34.110  -28.362  1.00 49.15  ?  886 HOH B O   1 
HETATM 9170 O  O   . HOH Q 6 .   ? -19.721 13.646  -30.631  1.00 49.65  ?  887 HOH B O   1 
HETATM 9171 O  O   . HOH Q 6 .   ? 2.825   25.943  -20.279  1.00 45.39  ?  888 HOH B O   1 
HETATM 9172 O  O   . HOH Q 6 .   ? -9.829  1.321   -34.977  1.00 52.62  ?  889 HOH B O   1 
HETATM 9173 O  O   . HOH Q 6 .   ? -4.276  24.209  -30.807  1.00 40.39  ?  890 HOH B O   1 
HETATM 9174 O  O   . HOH Q 6 .   ? 2.271   36.494  -40.547  1.00 55.86  ?  891 HOH B O   1 
HETATM 9175 O  O   . HOH Q 6 .   ? -0.511  17.390  -16.871  1.00 61.29  ?  892 HOH B O   1 
HETATM 9176 O  O   . HOH Q 6 .   ? -9.243  47.814  -17.783  1.00 40.46  ?  893 HOH B O   1 
HETATM 9177 O  O   . HOH Q 6 .   ? -13.364 14.736  -27.911  1.00 48.64  ?  894 HOH B O   1 
HETATM 9178 O  O   . HOH Q 6 .   ? 0.266   26.361  -19.752  1.00 47.35  ?  895 HOH B O   1 
HETATM 9179 O  O   . HOH Q 6 .   ? -33.816 37.322  -0.752   1.00 48.21  ?  896 HOH B O   1 
HETATM 9180 O  O   . HOH Q 6 .   ? -7.026  17.186  -40.481  1.00 52.53  ?  897 HOH B O   1 
HETATM 9181 O  O   . HOH Q 6 .   ? 4.218   42.108  -34.211  1.00 51.37  ?  898 HOH B O   1 
HETATM 9182 O  O   . HOH Q 6 .   ? -8.338  39.363  -12.191  1.00 47.58  ?  899 HOH B O   1 
HETATM 9183 O  O   . HOH Q 6 .   ? -4.133  36.541  -14.289  1.00 45.88  ?  900 HOH B O   1 
HETATM 9184 O  O   . HOH Q 6 .   ? 8.302   4.327   -30.216  1.00 73.57  ?  901 HOH B O   1 
HETATM 9185 O  O   . HOH Q 6 .   ? -12.800 43.014  -7.900   1.00 56.71  ?  902 HOH B O   1 
HETATM 9186 O  O   . HOH Q 6 .   ? -19.874 18.382  -18.203  1.00 43.84  ?  903 HOH B O   1 
HETATM 9187 O  O   . HOH Q 6 .   ? -17.793 17.266  -16.054  1.00 44.41  ?  904 HOH B O   1 
HETATM 9188 O  O   . HOH Q 6 .   ? -37.098 24.655  -0.084   1.00 50.17  ?  905 HOH B O   1 
HETATM 9189 O  O   . HOH Q 6 .   ? -15.491 22.054  -12.587  1.00 43.45  ?  906 HOH B O   1 
HETATM 9190 O  O   . HOH Q 6 .   ? -31.098 43.982  -19.992  1.00 57.65  ?  907 HOH B O   1 
HETATM 9191 O  O   . HOH Q 6 .   ? -22.167 14.188  -15.203  1.00 50.29  ?  908 HOH B O   1 
HETATM 9192 O  O   . HOH Q 6 .   ? -27.445 44.884  -11.682  1.00 47.03  ?  909 HOH B O   1 
HETATM 9193 O  O   . HOH Q 6 .   ? -22.903 41.695  -17.746  1.00 50.38  ?  910 HOH B O   1 
HETATM 9194 O  O   . HOH Q 6 .   ? -12.910 22.782  -9.995   1.00 42.43  ?  911 HOH B O   1 
HETATM 9195 O  O   . HOH Q 6 .   ? -32.646 31.347  3.526    1.00 53.75  ?  912 HOH B O   1 
HETATM 9196 O  O   . HOH Q 6 .   ? 1.082   27.693  -42.379  1.00 53.02  ?  913 HOH B O   1 
HETATM 9197 O  O   . HOH Q 6 .   ? -31.290 36.544  -2.383   1.00 38.70  ?  914 HOH B O   1 
HETATM 9198 O  O   . HOH Q 6 .   ? -34.483 10.817  -4.340   1.00 51.20  ?  915 HOH B O   1 
HETATM 9199 O  O   . HOH Q 6 .   ? -18.949 18.242  -2.187   1.00 59.34  ?  916 HOH B O   1 
HETATM 9200 O  O   . HOH Q 6 .   ? -3.222  51.097  -29.840  1.00 53.04  ?  917 HOH B O   1 
HETATM 9201 O  O   . HOH Q 6 .   ? -26.651 20.520  5.302    1.00 61.43  ?  918 HOH B O   1 
HETATM 9202 O  O   . HOH Q 6 .   ? -20.074 16.837  -11.369  1.00 37.22  ?  919 HOH B O   1 
HETATM 9203 O  O   . HOH Q 6 .   ? -22.888 28.294  -34.052  1.00 53.94  ?  920 HOH B O   1 
HETATM 9204 O  O   . HOH Q 6 .   ? 6.529   -15.764 -34.167  1.00 63.60  ?  921 HOH B O   1 
HETATM 9205 O  O   . HOH Q 6 .   ? -11.280 41.627  -19.430  1.00 46.51  ?  922 HOH B O   1 
HETATM 9206 O  O   . HOH Q 6 .   ? -35.001 12.963  -8.640   1.00 48.08  ?  923 HOH B O   1 
HETATM 9207 O  O   . HOH Q 6 .   ? -9.759  -8.732  -39.501  1.00 54.21  ?  924 HOH B O   1 
HETATM 9208 O  O   . HOH Q 6 .   ? -32.473 13.844  -0.674   1.00 57.10  ?  925 HOH B O   1 
HETATM 9209 O  O   . HOH Q 6 .   ? 4.255   10.927  -29.374  1.00 55.41  ?  926 HOH B O   1 
HETATM 9210 O  O   . HOH Q 6 .   ? -33.013 39.727  -20.273  1.00 47.54  ?  927 HOH B O   1 
HETATM 9211 O  O   . HOH Q 6 .   ? 4.351   12.102  -26.084  1.00 58.51  ?  928 HOH B O   1 
HETATM 9212 O  O   . HOH Q 6 .   ? -32.633 25.205  -26.868  1.00 45.80  ?  929 HOH B O   1 
HETATM 9213 O  O   . HOH Q 6 .   ? -34.128 11.253  -10.089  1.00 42.68  ?  930 HOH B O   1 
HETATM 9214 O  O   . HOH Q 6 .   ? -45.069 28.678  -27.357  1.00 58.98  ?  931 HOH B O   1 
HETATM 9215 O  O   . HOH Q 6 .   ? 2.360   3.510   -25.282  1.00 62.51  ?  932 HOH B O   1 
HETATM 9216 O  O   . HOH Q 6 .   ? -41.317 5.731   -19.634  1.00 56.12  ?  933 HOH B O   1 
HETATM 9217 O  O   . HOH Q 6 .   ? -35.415 10.937  -7.390   1.00 51.39  ?  934 HOH B O   1 
HETATM 9218 O  O   . HOH Q 6 .   ? -39.092 18.094  -0.284   1.00 50.13  ?  935 HOH B O   1 
HETATM 9219 O  O   . HOH Q 6 .   ? -21.440 27.257  -26.441  1.00 51.75  ?  936 HOH B O   1 
HETATM 9220 O  O   . HOH Q 6 .   ? -11.044 12.721  -26.796  1.00 44.15  ?  937 HOH B O   1 
HETATM 9221 O  O   . HOH Q 6 .   ? -22.760 37.386  -30.821  1.00 51.11  ?  938 HOH B O   1 
HETATM 9222 O  O   . HOH Q 6 .   ? 3.285   4.365   -27.373  1.00 61.06  ?  939 HOH B O   1 
HETATM 9223 O  O   . HOH Q 6 .   ? -5.151  18.655  -40.191  1.00 47.33  ?  940 HOH B O   1 
HETATM 9224 O  O   . HOH Q 6 .   ? -10.048 12.865  -28.829  1.00 42.73  ?  941 HOH B O   1 
HETATM 9225 O  O   . HOH Q 6 .   ? -19.774 41.057  -2.871   1.00 53.56  ?  942 HOH B O   1 
HETATM 9226 O  O   . HOH Q 6 .   ? -47.608 16.054  -7.380   1.00 52.57  ?  943 HOH B O   1 
HETATM 9227 O  O   . HOH Q 6 .   ? -16.134 29.872  -22.370  1.00 44.61  ?  944 HOH B O   1 
HETATM 9228 O  O   . HOH Q 6 .   ? -8.376  40.557  -14.365  1.00 44.10  ?  945 HOH B O   1 
HETATM 9229 O  O   . HOH Q 6 .   ? -46.489 14.107  -14.229  1.00 45.50  ?  946 HOH B O   1 
HETATM 9230 O  O   . HOH Q 6 .   ? -17.868 16.773  -9.239   1.00 56.45  ?  947 HOH B O   1 
HETATM 9231 O  O   . HOH Q 6 .   ? -3.974  51.195  -32.273  1.00 55.55  ?  948 HOH B O   1 
HETATM 9232 O  O   . HOH Q 6 .   ? -47.853 15.123  -12.078  1.00 51.22  ?  949 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ALA A 3   ? 2.6152 0.7571 1.1091 -0.1085 -0.8237 0.0475  1   ALA A N   
2    C CA  . ALA A 3   ? 2.5484 0.7974 1.1818 -0.0673 -0.8275 0.0319  1   ALA A CA  
3    C C   . ALA A 3   ? 2.5423 0.8038 1.2637 0.0032  -0.9026 -0.0029 1   ALA A C   
4    O O   . ALA A 3   ? 2.4869 0.8244 1.3249 0.0437  -0.9121 -0.0203 1   ALA A O   
5    C CB  . ALA A 3   ? 2.4512 0.7241 1.0769 -0.0974 -0.7926 0.0453  1   ALA A CB  
6    N N   . VAL A 4   ? 2.6223 0.8014 1.2908 0.0193  -0.9533 -0.0137 2   VAL A N   
7    C CA  . VAL A 4   ? 2.6372 0.8198 1.3882 0.0854  -1.0263 -0.0540 2   VAL A CA  
8    C C   . VAL A 4   ? 2.6110 0.8189 1.4056 0.1137  -1.0405 -0.0690 2   VAL A C   
9    O O   . VAL A 4   ? 2.6991 0.8366 1.3931 0.0835  -1.0295 -0.0482 2   VAL A O   
10   C CB  . VAL A 4   ? 2.8110 0.8674 1.4641 0.0869  -1.0842 -0.0570 2   VAL A CB  
11   C CG1 . VAL A 4   ? 2.8444 0.9088 1.5902 0.1585  -1.1628 -0.1035 2   VAL A CG1 
12   C CG2 . VAL A 4   ? 2.8361 0.8624 1.4416 0.0562  -1.0677 -0.0396 2   VAL A CG2 
13   N N   . GLY A 5   ? 2.5459 0.8539 1.4904 0.1699  -1.0618 -0.1082 3   GLY A N   
14   C CA  . GLY A 5   ? 2.4828 0.8247 1.4844 0.1995  -1.0749 -0.1283 3   GLY A CA  
15   C C   . GLY A 5   ? 2.3782 0.8409 1.5573 0.2611  -1.0976 -0.1818 3   GLY A C   
16   O O   . GLY A 5   ? 2.3375 0.8522 1.5924 0.2825  -1.1067 -0.2053 3   GLY A O   
17   N N   . ALA A 6   ? 2.3372 0.8487 1.5894 0.2874  -1.0968 -0.2034 4   ALA A N   
18   C CA  . ALA A 6   ? 2.2565 0.8928 1.6862 0.3410  -1.1048 -0.2607 4   ALA A CA  
19   C C   . ALA A 6   ? 2.1784 0.9056 1.6887 0.3286  -1.0200 -0.2627 4   ALA A C   
20   O O   . ALA A 6   ? 2.1654 0.8523 1.5990 0.2878  -0.9719 -0.2244 4   ALA A O   
21   C CB  . ALA A 6   ? 2.3257 0.9408 1.7894 0.3845  -1.1777 -0.3037 4   ALA A CB  
22   N N   . CYS A 7   ? 2.0873 0.9394 1.7513 0.3578  -0.9987 -0.3167 5   CYS A N   
23   C CA  . CYS A 7   ? 1.9308 0.8706 1.6615 0.3366  -0.9152 -0.3305 5   CYS A CA  
24   C C   . CYS A 7   ? 1.8979 0.8098 1.6108 0.3366  -0.9066 -0.3220 5   CYS A C   
25   O O   . CYS A 7   ? 1.9741 0.8544 1.6964 0.3704  -0.9640 -0.3371 5   CYS A O   
26   C CB  . CYS A 7   ? 1.7788 0.8559 1.6691 0.3624  -0.8938 -0.3993 5   CYS A CB  
27   S SG  . CYS A 7   ? 1.6641 0.8495 1.6051 0.3212  -0.7834 -0.4096 5   CYS A SG  
28   N N   . VAL A 8   ? 1.8356 0.7610 1.5222 0.2972  -0.8370 -0.3008 6   VAL A N   
29   C CA  . VAL A 8   ? 1.8807 0.7816 1.5485 0.2925  -0.8231 -0.2925 6   VAL A CA  
30   C C   . VAL A 8   ? 1.8193 0.8240 1.6152 0.3144  -0.7923 -0.3461 6   VAL A C   
31   O O   . VAL A 8   ? 1.8348 0.8404 1.6290 0.3047  -0.7632 -0.3444 6   VAL A O   
32   C CB  . VAL A 8   ? 1.8536 0.7134 1.4268 0.2382  -0.7689 -0.2456 6   VAL A CB  
33   C CG1 . VAL A 8   ? 1.9452 0.6971 1.3853 0.2097  -0.7931 -0.1964 6   VAL A CG1 
34   C CG2 . VAL A 8   ? 1.7876 0.7306 1.4033 0.2113  -0.7030 -0.2544 6   VAL A CG2 
35   N N   . LEU A 9   ? 1.7736 0.8667 1.6792 0.3399  -0.7950 -0.3965 7   LEU A N   
36   C CA  . LEU A 9   ? 1.6869 0.8851 1.7158 0.3533  -0.7571 -0.4545 7   LEU A CA  
37   C C   . LEU A 9   ? 1.7026 0.9540 1.8456 0.4024  -0.8086 -0.5125 7   LEU A C   
38   O O   . LEU A 9   ? 1.6755 0.9774 1.9013 0.4200  -0.8012 -0.5544 7   LEU A O   
39   C CB  . LEU A 9   ? 1.5569 0.8379 1.6196 0.3208  -0.6832 -0.4710 7   LEU A CB  
40   C CG  . LEU A 9   ? 1.5238 0.7721 1.4916 0.2734  -0.6309 -0.4223 7   LEU A CG  
41   C CD1 . LEU A 9   ? 1.4988 0.8392 1.4957 0.2425  -0.5601 -0.4312 7   LEU A CD1 
42   C CD2 . LEU A 9   ? 1.5510 0.7721 1.4971 0.2671  -0.6138 -0.4141 7   LEU A CD2 
43   N N   . CYS A 10  ? 1.7173 0.9603 1.8686 0.4236  -0.8619 -0.5185 8   CYS A N   
44   C CA  . CYS A 10  ? 1.7463 1.0461 2.0128 0.4712  -0.9197 -0.5784 8   CYS A CA  
45   C C   . CYS A 10  ? 1.8676 1.0657 2.0580 0.4983  -1.0197 -0.5539 8   CYS A C   
46   O O   . CYS A 10  ? 1.9163 1.1467 2.1881 0.5385  -1.0853 -0.6038 8   CYS A O   
47   C CB  . CYS A 10  ? 1.6646 1.0837 2.0448 0.4696  -0.8838 -0.6318 8   CYS A CB  
48   S SG  . CYS A 10  ? 1.7174 1.0996 2.0173 0.4477  -0.8878 -0.5935 8   CYS A SG  
49   N N   . ASN A 11  ? 1.9302 1.0052 1.9606 0.4711  -1.0315 -0.4829 9   ASN A N   
50   C CA  . ASN A 11  ? 2.0685 1.0218 1.9832 0.4796  -1.1164 -0.4530 9   ASN A CA  
51   C C   . ASN A 11  ? 2.0928 1.0543 2.0252 0.4951  -1.1650 -0.4728 9   ASN A C   
52   O O   . ASN A 11  ? 2.2203 1.0963 2.0904 0.5095  -1.2460 -0.4802 9   ASN A O   
53   C CB  . ASN A 11  ? 2.1681 1.0821 2.0904 0.5115  -1.1814 -0.4794 9   ASN A CB  
54   C CG  . ASN A 11  ? 2.3283 1.0790 2.0738 0.4973  -1.2419 -0.4339 9   ASN A CG  
55   O OD1 . ASN A 11  ? 2.3528 1.0220 1.9701 0.4563  -1.2066 -0.3742 9   ASN A OD1 
56   N ND2 . ASN A 11  ? 2.4476 1.1459 2.1829 0.5270  -1.3298 -0.4681 9   ASN A ND2 
57   N N   . SER A 12  ? 2.0340 1.0865 2.0415 0.4875  -1.1138 -0.4870 10  SER A N   
58   C CA  . SER A 12  ? 2.0000 1.0611 2.0210 0.4988  -1.1534 -0.5020 10  SER A CA  
59   C C   . SER A 12  ? 2.0574 0.9988 1.9074 0.4577  -1.1517 -0.4289 10  SER A C   
60   O O   . SER A 12  ? 2.0806 1.0193 1.8803 0.4152  -1.0756 -0.3869 10  SER A O   
61   C CB  . SER A 12  ? 1.8653 1.0768 2.0374 0.5019  -1.0898 -0.5534 10  SER A CB  
62   O OG  . SER A 12  ? 1.8238 1.1516 2.1570 0.5330  -1.0875 -0.6283 10  SER A OG  
63   N N   . GLN A 13  ? 2.1867 1.0210 1.9477 0.4569  -1.2012 -0.4174 11  GLN A N   
64   C CA  . GLN A 13  ? 2.2597 0.9704 1.8542 0.4111  -1.1902 -0.3512 11  GLN A CA  
65   C C   . GLN A 13  ? 2.2004 0.9671 1.8194 0.3934  -1.1395 -0.3335 11  GLN A C   
66   O O   . GLN A 13  ? 2.1399 1.0233 1.8906 0.4209  -1.1355 -0.3789 11  GLN A O   
67   C CB  . GLN A 13  ? 2.4234 1.0158 1.9378 0.4216  -1.2572 -0.3533 11  GLN A CB  
68   C CG  . GLN A 13  ? 2.5536 1.0562 2.0014 0.4322  -1.3102 -0.3574 11  GLN A CG  
69   C CD  . GLN A 13  ? 2.6872 1.0472 1.9395 0.3791  -1.3000 -0.2923 11  GLN A CD  
70   O OE1 . GLN A 13  ? 2.6783 1.0021 1.8418 0.3319  -1.2557 -0.2460 11  GLN A OE1 
71   N NE2 . GLN A 13  ? 2.7709 1.0524 1.9569 0.3847  -1.3380 -0.2919 11  GLN A NE2 
72   N N   . THR A 14  ? 2.2366 0.9399 1.7299 0.3403  -1.0979 -0.2706 12  THR A N   
73   C CA  . THR A 14  ? 2.1088 0.8962 1.6056 0.2990  -1.0375 -0.2528 12  THR A CA  
74   C C   . THR A 14  ? 2.1621 0.8328 1.4892 0.2392  -1.0098 -0.1849 12  THR A C   
75   O O   . THR A 14  ? 2.2746 0.8008 1.4845 0.2289  -1.0398 -0.1579 12  THR A O   
76   C CB  . THR A 14  ? 2.0427 0.9831 1.6558 0.2853  -0.9592 -0.2842 12  THR A CB  
77   O OG1 . THR A 14  ? 2.0312 1.0717 1.7991 0.3354  -0.9820 -0.3543 12  THR A OG1 
78   C CG2 . THR A 14  ? 1.9647 0.9893 1.5858 0.2423  -0.8864 -0.2688 12  THR A CG2 
79   N N   . SER A 15  ? 2.1095 0.8444 1.4251 0.1917  -0.9444 -0.1673 13  SER A N   
80   C CA  . SER A 15  ? 2.1296 0.7815 1.3074 0.1293  -0.9031 -0.1133 13  SER A CA  
81   C C   . SER A 15  ? 2.1236 0.8754 1.3429 0.0890  -0.8072 -0.1062 13  SER A C   
82   O O   . SER A 15  ? 2.1253 0.8378 1.2587 0.0357  -0.7610 -0.0709 13  SER A O   
83   C CB  . SER A 15  ? 2.1548 0.7688 1.2731 0.1103  -0.9099 -0.0916 13  SER A CB  
84   O OG  . SER A 15  ? 2.2725 0.8160 1.2667 0.0452  -0.8616 -0.0463 13  SER A OG  
85   N N   . LEU A 16  ? 1.9623 0.8405 1.3127 0.1130  -0.7737 -0.1405 14  LEU A N   
86   C CA  . LEU A 16  ? 1.8668 0.8399 1.2622 0.0830  -0.6878 -0.1359 14  LEU A CA  
87   C C   . LEU A 16  ? 1.8641 0.8027 1.2344 0.0722  -0.6677 -0.1247 14  LEU A C   
88   O O   . LEU A 16  ? 1.8676 0.7896 1.2704 0.1061  -0.7022 -0.1455 14  LEU A O   
89   C CB  . LEU A 16  ? 1.7849 0.8956 1.3157 0.1087  -0.6606 -0.1801 14  LEU A CB  
90   C CG  . LEU A 16  ? 1.6367 0.8004 1.2092 0.1171  -0.6717 -0.1992 14  LEU A CG  
91   C CD1 . LEU A 16  ? 1.5484 0.8440 1.2463 0.1309  -0.6296 -0.2460 14  LEU A CD1 
92   C CD2 . LEU A 16  ? 1.6507 0.7910 1.1429 0.0719  -0.6391 -0.1598 14  LEU A CD2 
93   N N   . ARG A 17  ? 1.8754 0.8047 1.1928 0.0252  -0.6132 -0.0959 15  ARG A N   
94   C CA  . ARG A 17  ? 1.7863 0.6937 1.0840 0.0082  -0.5865 -0.0873 15  ARG A CA  
95   C C   . ARG A 17  ? 1.6931 0.7036 1.0491 -0.0112 -0.5167 -0.0907 15  ARG A C   
96   O O   . ARG A 17  ? 1.6174 0.6711 0.9765 -0.0319 -0.4843 -0.0832 15  ARG A O   
97   C CB  . ARG A 17  ? 1.8288 0.6128 0.9985 -0.0355 -0.5900 -0.0549 15  ARG A CB  
98   C CG  . ARG A 17  ? 2.0388 0.6852 1.1165 -0.0219 -0.6622 -0.0464 15  ARG A CG  
99   C CD  . ARG A 17  ? 2.1461 0.7016 1.0963 -0.0766 -0.6392 -0.0099 15  ARG A CD  
100  N NE  . ARG A 17  ? 2.2231 0.7935 1.1444 -0.1162 -0.6028 0.0027  15  ARG A NE  
101  C CZ  . ARG A 17  ? 2.2074 0.7271 1.0340 -0.1711 -0.5661 0.0269  15  ARG A CZ  
102  N NH1 . ARG A 17  ? 2.1805 0.6497 0.9430 -0.2007 -0.5453 0.0371  15  ARG A NH1 
103  N NH2 . ARG A 17  ? 2.1123 0.6435 0.9159 -0.2000 -0.5417 0.0354  15  ARG A NH2 
104  N N   . CYS A 18  ? 1.6520 0.6948 1.0485 -0.0037 -0.4968 -0.1025 16  CYS A N   
105  C CA  . CYS A 18  ? 1.4934 0.6150 0.9300 -0.0205 -0.4397 -0.1051 16  CYS A CA  
106  C C   . CYS A 18  ? 1.5253 0.6089 0.9024 -0.0650 -0.4112 -0.0829 16  CYS A C   
107  O O   . CYS A 18  ? 1.5467 0.5587 0.8730 -0.0796 -0.4230 -0.0749 16  CYS A O   
108  C CB  . CYS A 18  ? 1.4258 0.5911 0.9216 0.0025  -0.4306 -0.1284 16  CYS A CB  
109  S SG  . CYS A 18  ? 1.3461 0.5890 0.8747 -0.0140 -0.3722 -0.1320 16  CYS A SG  
110  N N   . GLY A 19  ? 1.5182 0.6501 0.9047 -0.0878 -0.3718 -0.0776 17  GLY A N   
111  C CA  . GLY A 19  ? 1.5302 0.6417 0.8791 -0.1308 -0.3404 -0.0669 17  GLY A CA  
112  C C   . GLY A 19  ? 1.5175 0.6801 0.9112 -0.1338 -0.3109 -0.0798 17  GLY A C   
113  O O   . GLY A 19  ? 1.5897 0.7520 0.9733 -0.1673 -0.2833 -0.0807 17  GLY A O   
114  N N   . ALA A 20  ? 1.3845 0.5896 0.8284 -0.1006 -0.3166 -0.0941 18  ALA A N   
115  C CA  . ALA A 20  ? 1.4398 0.6813 0.9171 -0.0989 -0.2983 -0.1069 18  ALA A CA  
116  C C   . ALA A 20  ? 1.3983 0.6002 0.8669 -0.0933 -0.3161 -0.1126 18  ALA A C   
117  O O   . ALA A 20  ? 1.4343 0.6431 0.9116 -0.1065 -0.3031 -0.1206 18  ALA A O   
118  C CB  . ALA A 20  ? 1.3498 0.6525 0.8711 -0.0725 -0.2878 -0.1197 18  ALA A CB  
119  N N   . CYS A 21  ? 1.3888 0.5502 0.8446 -0.0725 -0.3480 -0.1121 19  CYS A N   
120  C CA  . CYS A 21  ? 1.4659 0.5762 0.9040 -0.0685 -0.3676 -0.1160 19  CYS A CA  
121  C C   . CYS A 21  ? 1.4879 0.5300 0.8631 -0.1095 -0.3623 -0.1039 19  CYS A C   
122  O O   . CYS A 21  ? 1.6273 0.6249 0.9509 -0.1333 -0.3634 -0.0893 19  CYS A O   
123  C CB  . CYS A 21  ? 1.4631 0.5354 0.8990 -0.0361 -0.4090 -0.1205 19  CYS A CB  
124  S SG  . CYS A 21  ? 1.4016 0.5468 0.9186 0.0078  -0.4116 -0.1499 19  CYS A SG  
125  N N   . ILE A 22  ? 1.5520 0.5816 0.9266 -0.1219 -0.3540 -0.1127 20  ILE A N   
126  C CA  . ILE A 22  ? 1.6064 0.5751 0.9243 -0.1688 -0.3396 -0.1091 20  ILE A CA  
127  C C   . ILE A 22  ? 1.7317 0.5980 0.9667 -0.1754 -0.3669 -0.0904 20  ILE A C   
128  O O   . ILE A 22  ? 1.7456 0.5656 0.9201 -0.2167 -0.3470 -0.0795 20  ILE A O   
129  C CB  . ILE A 22  ? 1.5595 0.5454 0.9034 -0.1797 -0.3247 -0.1275 20  ILE A CB  
130  C CG1 . ILE A 22  ? 1.6555 0.6237 0.9726 -0.2339 -0.2901 -0.1333 20  ILE A CG1 
131  C CG2 . ILE A 22  ? 1.6048 0.5417 0.9314 -0.1570 -0.3529 -0.1272 20  ILE A CG2 
132  C CD1 . ILE A 22  ? 1.6620 0.6797 1.0045 -0.2588 -0.2605 -0.1418 20  ILE A CD1 
133  N N   . ARG A 23  ? 1.7003 0.5388 0.9350 -0.1334 -0.4097 -0.0877 21  ARG A N   
134  C CA  . ARG A 23  ? 1.8087 0.5549 0.9682 -0.1283 -0.4455 -0.0695 21  ARG A CA  
135  C C   . ARG A 23  ? 1.8753 0.6002 1.0145 -0.1106 -0.4773 -0.0595 21  ARG A C   
136  O O   . ARG A 23  ? 1.9700 0.6157 1.0457 -0.0985 -0.5191 -0.0462 21  ARG A O   
137  C CB  . ARG A 23  ? 1.8340 0.5585 1.0099 -0.0906 -0.4790 -0.0784 21  ARG A CB  
138  C CG  . ARG A 23  ? 1.8290 0.5614 1.0135 -0.1090 -0.4522 -0.0870 21  ARG A CG  
139  C CD  . ARG A 23  ? 1.8868 0.5800 1.0056 -0.1665 -0.4157 -0.0761 21  ARG A CD  
140  N NE  . ARG A 23  ? 2.0160 0.6044 1.0292 -0.1807 -0.4373 -0.0538 21  ARG A NE  
141  C CZ  . ARG A 23  ? 2.0963 0.6320 1.0324 -0.2326 -0.4064 -0.0450 21  ARG A CZ  
142  N NH1 . ARG A 23  ? 2.0514 0.6400 1.0180 -0.2758 -0.3512 -0.0592 21  ARG A NH1 
143  N NH2 . ARG A 23  ? 2.2314 0.6594 1.0567 -0.2414 -0.4324 -0.0251 21  ARG A NH2 
144  N N   . ARG A 24  ? 1.7747 0.5653 0.9621 -0.1087 -0.4614 -0.0671 22  ARG A N   
145  C CA  . ARG A 24  ? 1.7642 0.5489 0.9415 -0.0962 -0.4849 -0.0611 22  ARG A CA  
146  C C   . ARG A 24  ? 1.8498 0.5836 1.0191 -0.0505 -0.5490 -0.0649 22  ARG A C   
147  O O   . ARG A 24  ? 1.9216 0.5763 1.0134 -0.0543 -0.5826 -0.0463 22  ARG A O   
148  C CB  . ARG A 24  ? 1.8185 0.5544 0.9133 -0.1445 -0.4640 -0.0379 22  ARG A CB  
149  C CG  . ARG A 24  ? 1.8201 0.6197 0.9437 -0.1849 -0.4030 -0.0437 22  ARG A CG  
150  C CD  . ARG A 24  ? 1.8715 0.6370 0.9263 -0.2347 -0.3730 -0.0275 22  ARG A CD  
151  N NE  . ARG A 24  ? 1.8318 0.6671 0.9323 -0.2691 -0.3161 -0.0418 22  ARG A NE  
152  C CZ  . ARG A 24  ? 1.9610 0.7946 1.0297 -0.3154 -0.2753 -0.0389 22  ARG A CZ  
153  N NH1 . ARG A 24  ? 1.9556 0.7197 0.9363 -0.3354 -0.2823 -0.0182 22  ARG A NH1 
154  N NH2 . ARG A 24  ? 1.8751 0.7798 1.0038 -0.3402 -0.2285 -0.0606 22  ARG A NH2 
155  N N   . PRO A 25  ? 1.7730 0.5598 1.0252 -0.0061 -0.5657 -0.0908 23  PRO A N   
156  C CA  . PRO A 25  ? 1.8323 0.5807 1.0966 0.0415  -0.6288 -0.1049 23  PRO A CA  
157  C C   . PRO A 25  ? 1.8728 0.6462 1.1648 0.0641  -0.6575 -0.1140 23  PRO A C   
158  O O   . PRO A 25  ? 1.8076 0.6518 1.1255 0.0469  -0.6205 -0.1098 23  PRO A O   
159  C CB  . PRO A 25  ? 1.7624 0.5826 1.1232 0.0739  -0.6205 -0.1376 23  PRO A CB  
160  C CG  . PRO A 25  ? 1.6570 0.5875 1.0748 0.0543  -0.5565 -0.1408 23  PRO A CG  
161  C CD  . PRO A 25  ? 1.6599 0.5553 1.0035 0.0032  -0.5242 -0.1103 23  PRO A CD  
162  N N   . PHE A 26  ? 1.9827 0.7067 1.2747 0.1057  -0.7248 -0.1270 24  PHE A N   
163  C CA  . PHE A 26  ? 1.9025 0.6482 1.2320 0.1349  -0.7647 -0.1452 24  PHE A CA  
164  C C   . PHE A 26  ? 1.8317 0.7051 1.3085 0.1762  -0.7562 -0.1944 24  PHE A C   
165  O O   . PHE A 26  ? 1.9662 0.8460 1.4926 0.2046  -0.7703 -0.2206 24  PHE A O   
166  C CB  . PHE A 26  ? 2.0829 0.7230 1.3403 0.1602  -0.8447 -0.1348 24  PHE A CB  
167  C CG  . PHE A 26  ? 2.1865 0.7288 1.3052 0.1181  -0.8511 -0.0914 24  PHE A CG  
168  C CD1 . PHE A 26  ? 2.2227 0.7620 1.3304 0.1179  -0.8703 -0.0901 24  PHE A CD1 
169  C CD2 . PHE A 26  ? 2.2526 0.7087 1.2507 0.0750  -0.8335 -0.0565 24  PHE A CD2 
170  C CE1 . PHE A 26  ? 2.3354 0.7831 1.3089 0.0752  -0.8721 -0.0517 24  PHE A CE1 
171  C CE2 . PHE A 26  ? 2.3215 0.6919 1.1885 0.0297  -0.8308 -0.0238 24  PHE A CE2 
172  C CZ  . PHE A 26  ? 2.3914 0.7565 1.2434 0.0293  -0.8503 -0.0206 24  PHE A CZ  
173  N N   . LEU A 27  ? 1.7835 0.7545 1.3263 0.1754  -0.7290 -0.2096 25  LEU A N   
174  C CA  . LEU A 27  ? 1.7306 0.8216 1.4061 0.2039  -0.7104 -0.2611 25  LEU A CA  
175  C C   . LEU A 27  ? 1.7080 0.8352 1.4366 0.2295  -0.7480 -0.2898 25  LEU A C   
176  O O   . LEU A 27  ? 1.7034 0.8021 1.3728 0.2102  -0.7549 -0.2625 25  LEU A O   
177  C CB  . LEU A 27  ? 1.5883 0.7730 1.2962 0.1710  -0.6257 -0.2588 25  LEU A CB  
178  C CG  . LEU A 27  ? 1.6021 0.7866 1.2965 0.1535  -0.5844 -0.2489 25  LEU A CG  
179  C CD1 . LEU A 27  ? 1.6241 0.8017 1.3699 0.1876  -0.6110 -0.2837 25  LEU A CD1 
180  C CD2 . LEU A 27  ? 1.6174 0.7177 1.2043 0.1182  -0.5790 -0.1993 25  LEU A CD2 
181  N N   . CYS A 28  ? 1.7021 0.8954 1.5469 0.2712  -0.7707 -0.3494 26  CYS A N   
182  C CA  . CYS A 28  ? 1.6683 0.9180 1.5870 0.2950  -0.8009 -0.3885 26  CYS A CA  
183  C C   . CYS A 28  ? 1.6291 0.9878 1.5923 0.2615  -0.7223 -0.3966 26  CYS A C   
184  O O   . CYS A 28  ? 1.5691 0.9476 1.4970 0.2235  -0.6535 -0.3688 26  CYS A O   
185  C CB  . CYS A 28  ? 1.6266 0.9254 1.6734 0.3485  -0.8457 -0.4617 26  CYS A CB  
186  S SG  . CYS A 28  ? 1.7108 1.1171 1.8661 0.3428  -0.7700 -0.5115 26  CYS A SG  
187  N N   . CYS A 29  ? 1.5112 0.9381 1.5525 0.2767  -0.7357 -0.4384 27  CYS A N   
188  C CA  . CYS A 29  ? 1.4489 0.9666 1.5202 0.2428  -0.6641 -0.4460 27  CYS A CA  
189  C C   . CYS A 29  ? 1.3619 0.9747 1.5230 0.2343  -0.5967 -0.4950 27  CYS A C   
190  O O   . CYS A 29  ? 1.3216 0.9777 1.4655 0.1960  -0.5238 -0.4846 27  CYS A O   
191  C CB  . CYS A 29  ? 1.4803 1.0356 1.6001 0.2576  -0.6999 -0.4760 27  CYS A CB  
192  S SG  . CYS A 29  ? 1.6235 1.0541 1.6173 0.2601  -0.7768 -0.4184 27  CYS A SG  
193  N N   . LYS A 30  ? 1.3441 0.9809 1.5923 0.2676  -0.6195 -0.5490 28  LYS A N   
194  C CA  . LYS A 30  ? 1.2883 1.0102 1.6179 0.2543  -0.5520 -0.6028 28  LYS A CA  
195  C C   . LYS A 30  ? 1.4131 1.0974 1.6720 0.2283  -0.5040 -0.5654 28  LYS A C   
196  O O   . LYS A 30  ? 1.3267 1.0568 1.5911 0.1961  -0.4308 -0.5806 28  LYS A O   
197  C CB  . LYS A 30  ? 1.3115 1.0819 1.7741 0.2980  -0.5904 -0.6850 28  LYS A CB  
198  N N   . CYS A 31  ? 1.4665 1.0610 1.6510 0.2393  -0.5448 -0.5178 29  CYS A N   
199  C CA  . CYS A 31  ? 1.4044 0.9628 1.5298 0.2189  -0.5087 -0.4871 29  CYS A CA  
200  C C   . CYS A 31  ? 1.3670 0.8948 1.3893 0.1786  -0.4709 -0.4229 29  CYS A C   
201  O O   . CYS A 31  ? 1.3346 0.8708 1.3269 0.1523  -0.4179 -0.4115 29  CYS A O   
202  C CB  . CYS A 31  ? 1.4602 0.9389 1.5615 0.2481  -0.5676 -0.4746 29  CYS A CB  
203  S SG  . CYS A 31  ? 1.5726 1.0821 1.8038 0.3034  -0.6203 -0.5560 29  CYS A SG  
204  N N   . CYS A 32  ? 1.3847 0.8726 1.3512 0.1738  -0.5004 -0.3837 30  CYS A N   
205  C CA  . CYS A 32  ? 1.3978 0.8666 1.2814 0.1358  -0.4634 -0.3317 30  CYS A CA  
206  C C   . CYS A 32  ? 1.3299 0.8689 1.2346 0.1104  -0.3950 -0.3475 30  CYS A C   
207  O O   . CYS A 32  ? 1.2335 0.7608 1.0818 0.0832  -0.3561 -0.3159 30  CYS A O   
208  C CB  . CYS A 32  ? 1.3774 0.8080 1.2141 0.1323  -0.4986 -0.3024 30  CYS A CB  
209  S SG  . CYS A 32  ? 1.4363 0.8094 1.1596 0.0890  -0.4727 -0.2359 30  CYS A SG  
210  N N   . TYR A 33  ? 1.3241 0.9319 1.3085 0.1184  -0.3809 -0.4005 31  TYR A N   
211  C CA  . TYR A 33  ? 1.2910 0.9520 1.2822 0.0894  -0.3137 -0.4193 31  TYR A CA  
212  C C   . TYR A 33  ? 1.2328 0.8855 1.2028 0.0749  -0.2713 -0.4252 31  TYR A C   
213  O O   . TYR A 33  ? 1.2153 0.8668 1.1348 0.0458  -0.2222 -0.4121 31  TYR A O   
214  C CB  . TYR A 33  ? 1.2365 0.9719 1.3233 0.0974  -0.3062 -0.4845 31  TYR A CB  
215  C CG  . TYR A 33  ? 1.2174 1.0000 1.3060 0.0621  -0.2328 -0.5122 31  TYR A CG  
216  C CD1 . TYR A 33  ? 1.2089 0.9978 1.2535 0.0373  -0.2069 -0.4884 31  TYR A CD1 
217  C CD2 . TYR A 33  ? 1.2239 1.0364 1.3506 0.0504  -0.1876 -0.5646 31  TYR A CD2 
218  C CE1 . TYR A 33  ? 1.1993 1.0164 1.2313 0.0029  -0.1403 -0.5135 31  TYR A CE1 
219  C CE2 . TYR A 33  ? 1.2065 1.0439 1.3154 0.0118  -0.1179 -0.5912 31  TYR A CE2 
220  C CZ  . TYR A 33  ? 1.1915 1.0281 1.2502 -0.0112 -0.0958 -0.5645 31  TYR A CZ  
221  O OH  . TYR A 33  ? 1.2092 1.0561 1.2362 -0.0517 -0.0269 -0.5905 31  TYR A OH  
222  N N   . ASP A 34  ? 1.2757 0.9137 1.2759 0.0956  -0.2932 -0.4441 32  ASP A N   
223  C CA  . ASP A 34  ? 1.2744 0.9010 1.2535 0.0818  -0.2555 -0.4537 32  ASP A CA  
224  C C   . ASP A 34  ? 1.2781 0.8424 1.1727 0.0734  -0.2635 -0.3960 32  ASP A C   
225  O O   . ASP A 34  ? 1.3823 0.9311 1.2300 0.0531  -0.2274 -0.3887 32  ASP A O   
226  C CB  . ASP A 34  ? 1.2996 0.9455 1.3570 0.1051  -0.2686 -0.5080 32  ASP A CB  
227  C CG  . ASP A 34  ? 1.3374 1.0582 1.4856 0.1020  -0.2385 -0.5808 32  ASP A CG  
228  O OD1 . ASP A 34  ? 1.3409 1.0815 1.4653 0.0663  -0.1750 -0.5986 32  ASP A OD1 
229  O OD2 . ASP A 34  ? 1.2983 1.0541 1.5389 0.1338  -0.2786 -0.6234 32  ASP A OD2 
230  N N   . HIS A 35  ? 1.2582 0.7814 1.1285 0.0863  -0.3106 -0.3583 33  HIS A N   
231  C CA  . HIS A 35  ? 1.3232 0.7961 1.1204 0.0718  -0.3117 -0.3098 33  HIS A CA  
232  C C   . HIS A 35  ? 1.2214 0.7055 0.9733 0.0451  -0.2748 -0.2864 33  HIS A C   
233  O O   . HIS A 35  ? 1.2086 0.6774 0.9194 0.0306  -0.2517 -0.2732 33  HIS A O   
234  C CB  . HIS A 35  ? 1.2930 0.7134 1.0635 0.0816  -0.3618 -0.2786 33  HIS A CB  
235  C CG  . HIS A 35  ? 1.2444 0.6154 0.9511 0.0637  -0.3612 -0.2396 33  HIS A CG  
236  N ND1 . HIS A 35  ? 1.2345 0.6025 0.9277 0.0552  -0.3383 -0.2401 33  HIS A ND1 
237  C CD2 . HIS A 35  ? 1.2728 0.5949 0.9270 0.0498  -0.3794 -0.2042 33  HIS A CD2 
238  C CE1 . HIS A 35  ? 1.2483 0.5773 0.8952 0.0393  -0.3439 -0.2096 33  HIS A CE1 
239  N NE2 . HIS A 35  ? 1.2721 0.5726 0.8941 0.0331  -0.3649 -0.1886 33  HIS A NE2 
240  N N   . VAL A 36  ? 1.2127 0.7216 0.9724 0.0402  -0.2720 -0.2840 34  VAL A N   
241  C CA  . VAL A 36  ? 1.2294 0.7429 0.9449 0.0168  -0.2423 -0.2597 34  VAL A CA  
242  C C   . VAL A 36  ? 1.1753 0.7104 0.8815 0.0022  -0.1946 -0.2833 34  VAL A C   
243  O O   . VAL A 36  ? 1.1536 0.6703 0.8072 -0.0135 -0.1732 -0.2632 34  VAL A O   
244  C CB  . VAL A 36  ? 1.1985 0.7252 0.9191 0.0143  -0.2548 -0.2490 34  VAL A CB  
245  C CG1 . VAL A 36  ? 1.2564 0.7913 0.9372 -0.0092 -0.2204 -0.2297 34  VAL A CG1 
246  C CG2 . VAL A 36  ? 1.2444 0.7248 0.9424 0.0201  -0.2993 -0.2202 34  VAL A CG2 
247  N N   . ILE A 37  ? 1.1761 0.7443 0.9289 0.0052  -0.1773 -0.3296 35  ILE A N   
248  C CA  . ILE A 37  ? 1.2416 0.8177 0.9697 -0.0178 -0.1255 -0.3553 35  ILE A CA  
249  C C   . ILE A 37  ? 1.3143 0.8567 1.0089 -0.0241 -0.1077 -0.3674 35  ILE A C   
250  O O   . ILE A 37  ? 1.3695 0.8958 1.0190 -0.0479 -0.0646 -0.3866 35  ILE A O   
251  C CB  . ILE A 37  ? 1.2704 0.9021 1.0634 -0.0221 -0.1035 -0.4078 35  ILE A CB  
252  C CG1 . ILE A 37  ? 1.2966 0.9286 1.0412 -0.0543 -0.0519 -0.4152 35  ILE A CG1 
253  C CG2 . ILE A 37  ? 1.3027 0.9533 1.1505 -0.0165 -0.0928 -0.4612 35  ILE A CG2 
254  C CD1 . ILE A 37  ? 1.3333 1.0238 1.1414 -0.0661 -0.0222 -0.4718 35  ILE A CD1 
255  N N   . SER A 38  ? 1.2934 0.8151 0.9977 -0.0066 -0.1390 -0.3566 36  SER A N   
256  C CA  . SER A 38  ? 1.2971 0.7845 0.9692 -0.0119 -0.1264 -0.3674 36  SER A CA  
257  C C   . SER A 38  ? 1.3580 0.8010 0.9791 -0.0079 -0.1510 -0.3253 36  SER A C   
258  O O   . SER A 38  ? 1.4056 0.8122 0.9830 -0.0148 -0.1416 -0.3293 36  SER A O   
259  C CB  . SER A 38  ? 1.2317 0.7385 0.9722 0.0045  -0.1368 -0.4068 36  SER A CB  
260  O OG  . SER A 38  ? 1.3715 0.9325 1.1850 0.0071  -0.1243 -0.4527 36  SER A OG  
261  N N   . THR A 39  ? 1.2828 0.7263 0.9082 0.0003  -0.1808 -0.2900 37  THR A N   
262  C CA  . THR A 39  ? 1.2632 0.6753 0.8552 0.0008  -0.2016 -0.2578 37  THR A CA  
263  C C   . THR A 39  ? 1.2672 0.6792 0.8277 -0.0098 -0.1966 -0.2315 37  THR A C   
264  O O   . THR A 39  ? 1.2149 0.6417 0.7655 -0.0184 -0.1747 -0.2358 37  THR A O   
265  C CB  . THR A 39  ? 1.2378 0.6425 0.8603 0.0136  -0.2373 -0.2457 37  THR A CB  
266  O OG1 . THR A 39  ? 1.2760 0.6919 0.9102 0.0130  -0.2508 -0.2282 37  THR A OG1 
267  C CG2 . THR A 39  ? 1.2013 0.6105 0.8667 0.0294  -0.2463 -0.2763 37  THR A CG2 
268  N N   . SER A 40  ? 1.2823 0.6790 0.8312 -0.0107 -0.2154 -0.2085 38  SER A N   
269  C CA  . SER A 40  ? 1.2660 0.6670 0.7989 -0.0195 -0.2135 -0.1886 38  SER A CA  
270  C C   . SER A 40  ? 1.2277 0.6421 0.7842 -0.0251 -0.2244 -0.1719 38  SER A C   
271  O O   . SER A 40  ? 1.1849 0.6057 0.7346 -0.0360 -0.2201 -0.1579 38  SER A O   
272  C CB  . SER A 40  ? 1.2908 0.6719 0.8054 -0.0192 -0.2258 -0.1834 38  SER A CB  
273  O OG  . SER A 40  ? 1.1718 0.5472 0.7087 -0.0191 -0.2450 -0.1802 38  SER A OG  
274  N N   . HIS A 41  ? 1.1576 0.5691 0.7367 -0.0181 -0.2403 -0.1755 39  HIS A N   
275  C CA  . HIS A 41  ? 1.2302 0.6315 0.8120 -0.0242 -0.2576 -0.1593 39  HIS A CA  
276  C C   . HIS A 41  ? 1.1970 0.6227 0.7874 -0.0248 -0.2500 -0.1608 39  HIS A C   
277  O O   . HIS A 41  ? 1.1536 0.5975 0.7718 -0.0111 -0.2524 -0.1818 39  HIS A O   
278  C CB  . HIS A 41  ? 1.2304 0.6022 0.8216 -0.0121 -0.2866 -0.1641 39  HIS A CB  
279  C CG  . HIS A 41  ? 1.2645 0.6077 0.8432 -0.0164 -0.2941 -0.1607 39  HIS A CG  
280  N ND1 . HIS A 41  ? 1.3089 0.6068 0.8744 -0.0168 -0.3195 -0.1546 39  HIS A ND1 
281  C CD2 . HIS A 41  ? 1.2723 0.6211 0.8461 -0.0209 -0.2820 -0.1645 39  HIS A CD2 
282  C CE1 . HIS A 41  ? 1.2703 0.5538 0.8282 -0.0241 -0.3173 -0.1558 39  HIS A CE1 
283  N NE2 . HIS A 41  ? 1.3169 0.6340 0.8838 -0.0252 -0.2969 -0.1626 39  HIS A NE2 
284  N N   . LYS A 42  ? 1.1846 0.6143 0.7572 -0.0417 -0.2398 -0.1434 40  LYS A N   
285  C CA  . LYS A 42  ? 1.2379 0.6914 0.8149 -0.0451 -0.2297 -0.1443 40  LYS A CA  
286  C C   . LYS A 42  ? 1.2337 0.6658 0.7922 -0.0584 -0.2453 -0.1251 40  LYS A C   
287  O O   . LYS A 42  ? 1.1744 0.6216 0.7381 -0.0584 -0.2463 -0.1273 40  LYS A O   
288  C CB  . LYS A 42  ? 1.1869 0.6609 0.7497 -0.0546 -0.1977 -0.1438 40  LYS A CB  
289  C CG  . LYS A 42  ? 1.1364 0.6086 0.6906 -0.0467 -0.1836 -0.1596 40  LYS A CG  
290  C CD  . LYS A 42  ? 1.2117 0.6998 0.7817 -0.0393 -0.1714 -0.1872 40  LYS A CD  
291  C CE  . LYS A 42  ? 1.2291 0.6974 0.7700 -0.0388 -0.1545 -0.2023 40  LYS A CE  
292  N NZ  . LYS A 42  ? 1.3068 0.7883 0.8615 -0.0398 -0.1333 -0.2368 40  LYS A NZ  
293  N N   . LEU A 43  ? 1.2967 0.6896 0.8284 -0.0733 -0.2557 -0.1091 41  LEU A N   
294  C CA  . LEU A 43  ? 1.3590 0.7106 0.8523 -0.0928 -0.2693 -0.0915 41  LEU A CA  
295  C C   . LEU A 43  ? 1.3929 0.7017 0.8755 -0.0757 -0.3123 -0.0931 41  LEU A C   
296  O O   . LEU A 43  ? 1.3735 0.6513 0.8542 -0.0649 -0.3324 -0.0970 41  LEU A O   
297  C CB  . LEU A 43  ? 1.3686 0.6879 0.8318 -0.1226 -0.2575 -0.0806 41  LEU A CB  
298  C CG  . LEU A 43  ? 1.3938 0.6516 0.7972 -0.1537 -0.2651 -0.0639 41  LEU A CG  
299  C CD1 . LEU A 43  ? 1.3908 0.6656 0.7845 -0.1636 -0.2539 -0.0570 41  LEU A CD1 
300  C CD2 . LEU A 43  ? 1.3762 0.6097 0.7576 -0.1904 -0.2419 -0.0635 41  LEU A CD2 
301  N N   . VAL A 44  ? 1.3761 0.6800 0.8517 -0.0715 -0.3305 -0.0920 42  VAL A N   
302  C CA  . VAL A 44  ? 1.4191 0.6714 0.8781 -0.0528 -0.3824 -0.0945 42  VAL A CA  
303  C C   . VAL A 44  ? 1.5576 0.7285 0.9313 -0.0824 -0.3984 -0.0680 42  VAL A C   
304  O O   . VAL A 44  ? 1.5197 0.7005 0.8705 -0.1093 -0.3721 -0.0563 42  VAL A O   
305  C CB  . VAL A 44  ? 1.3508 0.6537 0.8676 -0.0236 -0.3995 -0.1207 42  VAL A CB  
306  C CG1 . VAL A 44  ? 1.4330 0.6795 0.9386 0.0021  -0.4645 -0.1281 42  VAL A CG1 
307  C CG2 . VAL A 44  ? 1.3208 0.6954 0.9105 -0.0043 -0.3739 -0.1512 42  VAL A CG2 
308  N N   . LEU A 45  ? 1.6498 0.7314 0.9679 -0.0800 -0.4402 -0.0597 43  LEU A N   
309  C CA  . LEU A 45  ? 1.7018 0.6791 0.9138 -0.1144 -0.4560 -0.0350 43  LEU A CA  
310  C C   . LEU A 45  ? 1.8367 0.7401 1.0078 -0.0884 -0.5259 -0.0352 43  LEU A C   
311  O O   . LEU A 45  ? 1.7937 0.6989 1.0077 -0.0451 -0.5689 -0.0542 43  LEU A O   
312  C CB  . LEU A 45  ? 1.7991 0.7066 0.9516 -0.1448 -0.4435 -0.0239 43  LEU A CB  
313  C CG  . LEU A 45  ? 1.7579 0.7177 0.9329 -0.1805 -0.3796 -0.0249 43  LEU A CG  
314  C CD1 . LEU A 45  ? 1.7511 0.6309 0.8587 -0.2186 -0.3688 -0.0189 43  LEU A CD1 
315  C CD2 . LEU A 45  ? 1.7038 0.6956 0.8724 -0.2098 -0.3440 -0.0188 43  LEU A CD2 
316  N N   . SER A 46  ? 1.9532 0.7884 1.0409 -0.1147 -0.5391 -0.0169 44  SER A N   
317  C CA  . SER A 46  ? 2.0331 0.7737 1.0565 -0.0947 -0.6134 -0.0137 44  SER A CA  
318  C C   . SER A 46  ? 2.1737 0.7843 1.0478 -0.1497 -0.6119 0.0172  44  SER A C   
319  O O   . SER A 46  ? 2.2092 0.8036 1.0413 -0.1972 -0.5561 0.0317  44  SER A O   
320  C CB  . SER A 46  ? 1.9345 0.7573 1.0381 -0.0599 -0.6350 -0.0356 44  SER A CB  
321  O OG  . SER A 46  ? 2.0141 0.7445 1.0569 -0.0389 -0.7137 -0.0354 44  SER A OG  
322  N N   . VAL A 47  ? 2.2290 0.7622 1.0356 -0.1407 -0.6644 0.0291  45  VAL A N   
323  C CA  . VAL A 47  ? 2.2945 0.7210 0.9632 -0.1937 -0.6480 0.0646  45  VAL A CA  
324  C C   . VAL A 47  ? 2.2362 0.7404 0.9261 -0.2434 -0.5664 0.0655  45  VAL A C   
325  O O   . VAL A 47  ? 2.3362 0.8057 0.9469 -0.2974 -0.5166 0.0826  45  VAL A O   
326  C CB  . VAL A 47  ? 2.4082 0.7402 1.0219 -0.1750 -0.7110 0.0738  45  VAL A CB  
327  C CG1 . VAL A 47  ? 2.5304 0.7837 1.0191 -0.2328 -0.6807 0.0941  45  VAL A CG1 
328  C CG2 . VAL A 47  ? 2.4482 0.7352 1.0912 -0.1152 -0.7888 0.0533  45  VAL A CG2 
329  N N   . ASN A 48  ? 2.1174 0.7418 0.9175 -0.2241 -0.5498 0.0415  46  ASN A N   
330  C CA  . ASN A 48  ? 2.0447 0.7567 0.8872 -0.2586 -0.4760 0.0396  46  ASN A CA  
331  C C   . ASN A 48  ? 1.9482 0.7917 0.9222 -0.2318 -0.4369 0.0203  46  ASN A C   
332  O O   . ASN A 48  ? 1.8644 0.7686 0.9216 -0.1809 -0.4661 0.0020  46  ASN A O   
333  C CB  . ASN A 48  ? 2.0438 0.7942 0.8994 -0.2548 -0.4819 0.0382  46  ASN A CB  
334  C CG  . ASN A 48  ? 2.0254 0.8014 0.9365 -0.1952 -0.5505 0.0205  46  ASN A CG  
335  O OD1 . ASN A 48  ? 1.9279 0.8005 0.9533 -0.1522 -0.5517 -0.0037 46  ASN A OD1 
336  N ND2 . ASN A 48  ? 1.9968 0.6945 0.8429 -0.1904 -0.5993 0.0319  46  ASN A ND2 
337  N N   . PRO A 49  ? 1.9412 0.8265 0.9355 -0.2648 -0.3736 0.0196  47  PRO A N   
338  C CA  . PRO A 49  ? 1.7870 0.7860 0.8935 -0.2393 -0.3412 0.0020  47  PRO A CA  
339  C C   . PRO A 49  ? 1.6265 0.7254 0.8144 -0.2103 -0.3326 -0.0107 47  PRO A C   
340  O O   . PRO A 49  ? 1.5915 0.7098 0.7693 -0.2305 -0.3094 -0.0063 47  PRO A O   
341  C CB  . PRO A 49  ? 1.7205 0.7326 0.8216 -0.2847 -0.2814 0.0014  47  PRO A CB  
342  C CG  . PRO A 49  ? 1.8511 0.7913 0.8604 -0.3349 -0.2678 0.0146  47  PRO A CG  
343  C CD  . PRO A 49  ? 1.9447 0.7726 0.8604 -0.3286 -0.3292 0.0299  47  PRO A CD  
344  N N   . TYR A 50  ? 1.5674 0.7257 0.8319 -0.1665 -0.3480 -0.0292 48  TYR A N   
345  C CA  . TYR A 50  ? 1.4757 0.7252 0.8131 -0.1454 -0.3314 -0.0465 48  TYR A CA  
346  C C   . TYR A 50  ? 1.4576 0.7618 0.8192 -0.1654 -0.2728 -0.0457 48  TYR A C   
347  O O   . TYR A 50  ? 1.3370 0.6719 0.7349 -0.1556 -0.2552 -0.0540 48  TYR A O   
348  C CB  . TYR A 50  ? 1.3629 0.6566 0.7719 -0.1018 -0.3539 -0.0727 48  TYR A CB  
349  C CG  . TYR A 50  ? 1.4847 0.7574 0.9039 -0.0721 -0.4127 -0.0876 48  TYR A CG  
350  C CD1 . TYR A 50  ? 1.5736 0.7549 0.9145 -0.0806 -0.4587 -0.0700 48  TYR A CD1 
351  C CD2 . TYR A 50  ? 1.4639 0.8023 0.9691 -0.0360 -0.4242 -0.1240 48  TYR A CD2 
352  C CE1 . TYR A 50  ? 1.5751 0.7313 0.9264 -0.0472 -0.5237 -0.0870 48  TYR A CE1 
353  C CE2 . TYR A 50  ? 1.4733 0.8009 1.0050 -0.0044 -0.4827 -0.1469 48  TYR A CE2 
354  C CZ  . TYR A 50  ? 1.5401 0.7763 0.9962 -0.0066 -0.5370 -0.1277 48  TYR A CZ  
355  O OH  . TYR A 50  ? 1.5929 0.8126 1.0758 0.0306  -0.6058 -0.1535 48  TYR A OH  
356  N N   . VAL A 51  ? 1.4264 0.7383 0.7661 -0.1919 -0.2463 -0.0373 49  VAL A N   
357  C CA  . VAL A 51  ? 1.3245 0.6819 0.6858 -0.2087 -0.1965 -0.0391 49  VAL A CA  
358  C C   . VAL A 51  ? 1.3728 0.7529 0.7268 -0.2220 -0.1782 -0.0368 49  VAL A C   
359  O O   . VAL A 51  ? 1.4352 0.7825 0.7527 -0.2290 -0.2017 -0.0299 49  VAL A O   
360  C CB  . VAL A 51  ? 1.3824 0.7032 0.7124 -0.2430 -0.1754 -0.0323 49  VAL A CB  
361  C CG1 . VAL A 51  ? 1.4992 0.7474 0.7506 -0.2824 -0.1793 -0.0174 49  VAL A CG1 
362  C CG2 . VAL A 51  ? 1.4048 0.7793 0.7752 -0.2508 -0.1327 -0.0426 49  VAL A CG2 
363  N N   . CYS A 52  ? 1.3165 0.7464 0.7005 -0.2244 -0.1397 -0.0435 50  CYS A N   
364  C CA  . CYS A 52  ? 1.2799 0.7290 0.6545 -0.2396 -0.1178 -0.0417 50  CYS A CA  
365  C C   . CYS A 52  ? 1.1937 0.5956 0.5138 -0.2802 -0.1077 -0.0279 50  CYS A C   
366  O O   . CYS A 52  ? 1.1972 0.5861 0.5116 -0.3024 -0.0854 -0.0286 50  CYS A O   
367  C CB  . CYS A 52  ? 1.1961 0.6926 0.6031 -0.2335 -0.0812 -0.0517 50  CYS A CB  
368  S SG  . CYS A 52  ? 1.1229 0.6471 0.5227 -0.2447 -0.0548 -0.0536 50  CYS A SG  
369  N N   . ASN A 53  ? 1.2461 0.6214 0.5261 -0.2926 -0.1229 -0.0198 51  ASN A N   
370  C CA  . ASN A 53  ? 1.3294 0.6439 0.5393 -0.3367 -0.1136 -0.0068 51  ASN A CA  
371  C C   . ASN A 53  ? 1.3206 0.6666 0.5375 -0.3631 -0.0644 -0.0105 51  ASN A C   
372  O O   . ASN A 53  ? 1.3215 0.6222 0.4830 -0.4056 -0.0465 -0.0043 51  ASN A O   
373  C CB  . ASN A 53  ? 1.3728 0.6294 0.5231 -0.3386 -0.1589 0.0038  51  ASN A CB  
374  C CG  . ASN A 53  ? 1.5326 0.6851 0.5815 -0.3824 -0.1665 0.0197  51  ASN A CG  
375  O OD1 . ASN A 53  ? 1.5237 0.6303 0.5469 -0.3935 -0.1689 0.0222  51  ASN A OD1 
376  N ND2 . ASN A 53  ? 1.5595 0.6668 0.5419 -0.4111 -0.1692 0.0292  51  ASN A ND2 
377  N N   . ALA A 54  ? 1.1913 0.6052 0.4674 -0.3407 -0.0423 -0.0219 52  ALA A N   
378  C CA  . ALA A 54  ? 1.1648 0.6060 0.4494 -0.3595 -0.0002 -0.0272 52  ALA A CA  
379  C C   . ALA A 54  ? 1.2552 0.6967 0.5569 -0.3800 0.0303  -0.0381 52  ALA A C   
380  O O   . ALA A 54  ? 1.1938 0.6467 0.5302 -0.3624 0.0234  -0.0466 52  ALA A O   
381  C CB  . ALA A 54  ? 1.2462 0.7427 0.5744 -0.3293 0.0106  -0.0370 52  ALA A CB  
382  N N   . PRO A 55  ? 1.1839 0.6165 0.4678 -0.4178 0.0646  -0.0430 53  PRO A N   
383  C CA  . PRO A 55  ? 1.2196 0.6598 0.5330 -0.4412 0.0965  -0.0640 53  PRO A CA  
384  C C   . PRO A 55  ? 1.2463 0.7424 0.6368 -0.4040 0.0998  -0.0835 53  PRO A C   
385  O O   . PRO A 55  ? 1.2330 0.7595 0.6441 -0.3774 0.1018  -0.0845 53  PRO A O   
386  C CB  . PRO A 55  ? 1.3623 0.8033 0.6555 -0.4754 0.1337  -0.0698 53  PRO A CB  
387  C CG  . PRO A 55  ? 1.3686 0.7722 0.5914 -0.4807 0.1112  -0.0462 53  PRO A CG  
388  C CD  . PRO A 55  ? 1.2103 0.6267 0.4496 -0.4438 0.0773  -0.0343 53  PRO A CD  
389  N N   . GLY A 56  ? 1.2857 0.7870 0.7111 -0.4036 0.0984  -0.1005 54  GLY A N   
390  C CA  . GLY A 56  ? 1.0783 0.6239 0.5739 -0.3700 0.0956  -0.1232 54  GLY A CA  
391  C C   . GLY A 56  ? 1.2392 0.7917 0.7435 -0.3226 0.0604  -0.1130 54  GLY A C   
392  O O   . GLY A 56  ? 1.2591 0.8354 0.8074 -0.2926 0.0516  -0.1300 54  GLY A O   
393  N N   . CYS A 57  ? 1.2517 0.7810 0.7151 -0.3147 0.0381  -0.0896 55  CYS A N   
394  C CA  . CYS A 57  ? 1.2055 0.7425 0.6767 -0.2744 0.0116  -0.0845 55  CYS A CA  
395  C C   . CYS A 57  ? 1.2213 0.7459 0.7041 -0.2666 -0.0102 -0.0872 55  CYS A C   
396  O O   . CYS A 57  ? 1.2943 0.7878 0.7517 -0.2906 -0.0155 -0.0802 55  CYS A O   
397  C CB  . CYS A 57  ? 1.1747 0.7044 0.6124 -0.2678 0.0006  -0.0680 55  CYS A CB  
398  S SG  . CYS A 57  ? 1.1335 0.6824 0.5804 -0.2293 -0.0061 -0.0734 55  CYS A SG  
399  N N   . ASP A 58  ? 1.2700 0.8094 0.7815 -0.2345 -0.0241 -0.0972 56  ASP A N   
400  C CA  . ASP A 58  ? 1.1929 0.7237 0.7187 -0.2242 -0.0448 -0.1018 56  ASP A CA  
401  C C   . ASP A 58  ? 1.1900 0.7116 0.7004 -0.1971 -0.0683 -0.0918 56  ASP A C   
402  O O   . ASP A 58  ? 1.2653 0.7818 0.7885 -0.1814 -0.0859 -0.0972 56  ASP A O   
403  C CB  . ASP A 58  ? 1.2211 0.7727 0.7931 -0.2088 -0.0473 -0.1257 56  ASP A CB  
404  C CG  . ASP A 58  ? 1.2371 0.7976 0.8108 -0.1810 -0.0488 -0.1313 56  ASP A CG  
405  O OD1 . ASP A 58  ? 1.3471 0.8934 0.8909 -0.1592 -0.0600 -0.1212 56  ASP A OD1 
406  O OD2 . ASP A 58  ? 1.2568 0.8330 0.8582 -0.1826 -0.0381 -0.1488 56  ASP A OD2 
407  N N   . VAL A 59  ? 1.1639 0.6866 0.6524 -0.1930 -0.0671 -0.0822 57  VAL A N   
408  C CA  . VAL A 59  ? 1.1633 0.6867 0.6496 -0.1692 -0.0831 -0.0833 57  VAL A CA  
409  C C   . VAL A 59  ? 1.2580 0.7600 0.7401 -0.1706 -0.1086 -0.0771 57  VAL A C   
410  O O   . VAL A 59  ? 1.1857 0.6702 0.6466 -0.1860 -0.1163 -0.0672 57  VAL A O   
411  C CB  . VAL A 59  ? 1.1821 0.7200 0.6562 -0.1673 -0.0702 -0.0845 57  VAL A CB  
412  C CG1 . VAL A 59  ? 1.1302 0.6746 0.6128 -0.1487 -0.0825 -0.0951 57  VAL A CG1 
413  C CG2 . VAL A 59  ? 1.2839 0.8266 0.7479 -0.1644 -0.0474 -0.0903 57  VAL A CG2 
414  N N   . THR A 60  ? 1.1837 0.6786 0.6790 -0.1539 -0.1250 -0.0831 58  THR A N   
415  C CA  . THR A 60  ? 1.1944 0.6616 0.6840 -0.1509 -0.1523 -0.0792 58  THR A CA  
416  C C   . THR A 60  ? 1.1966 0.6738 0.7049 -0.1230 -0.1685 -0.0911 58  THR A C   
417  O O   . THR A 60  ? 1.2379 0.6936 0.7459 -0.1147 -0.1961 -0.0911 58  THR A O   
418  C CB  . THR A 60  ? 1.1944 0.6409 0.6853 -0.1610 -0.1559 -0.0799 58  THR A CB  
419  O OG1 . THR A 60  ? 1.3029 0.7736 0.8200 -0.1470 -0.1469 -0.0927 58  THR A OG1 
420  C CG2 . THR A 60  ? 1.1596 0.5869 0.6294 -0.1978 -0.1396 -0.0741 58  THR A CG2 
421  N N   . ASP A 61  ? 1.2220 0.7244 0.7418 -0.1101 -0.1517 -0.1040 59  ASP A N   
422  C CA  . ASP A 61  ? 1.1850 0.6970 0.7221 -0.0904 -0.1574 -0.1225 59  ASP A CA  
423  C C   . ASP A 61  ? 1.2002 0.7323 0.7553 -0.0869 -0.1628 -0.1339 59  ASP A C   
424  O O   . ASP A 61  ? 1.2462 0.7984 0.7966 -0.0966 -0.1425 -0.1368 59  ASP A O   
425  C CB  . ASP A 61  ? 1.2047 0.7208 0.7281 -0.0862 -0.1335 -0.1337 59  ASP A CB  
426  C CG  . ASP A 61  ? 1.1865 0.7068 0.7192 -0.0743 -0.1295 -0.1577 59  ASP A CG  
427  O OD1 . ASP A 61  ? 1.1839 0.7143 0.7489 -0.0647 -0.1471 -0.1690 59  ASP A OD1 
428  O OD2 . ASP A 61  ? 1.3114 0.8184 0.8146 -0.0754 -0.1092 -0.1679 59  ASP A OD2 
429  N N   . VAL A 62  ? 1.1775 0.7041 0.7565 -0.0716 -0.1928 -0.1440 60  VAL A N   
430  C CA  . VAL A 62  ? 1.2041 0.7512 0.8116 -0.0633 -0.2095 -0.1609 60  VAL A CA  
431  C C   . VAL A 62  ? 1.2049 0.7988 0.8450 -0.0610 -0.1797 -0.1946 60  VAL A C   
432  O O   . VAL A 62  ? 1.2198 0.8443 0.8880 -0.0606 -0.1817 -0.2134 60  VAL A O   
433  C CB  . VAL A 62  ? 1.2376 0.7602 0.8646 -0.0419 -0.2564 -0.1680 60  VAL A CB  
434  C CG1 . VAL A 62  ? 1.2009 0.7319 0.8573 -0.0255 -0.2534 -0.1897 60  VAL A CG1 
435  C CG2 . VAL A 62  ? 1.2111 0.7521 0.8728 -0.0280 -0.2855 -0.1893 60  VAL A CG2 
436  N N   . THR A 63  ? 1.1931 0.7882 0.8246 -0.0628 -0.1511 -0.2055 61  THR A N   
437  C CA  . THR A 63  ? 1.1813 0.8054 0.8232 -0.0711 -0.1135 -0.2386 61  THR A CA  
438  C C   . THR A 63  ? 1.2216 0.8510 0.8303 -0.0918 -0.0839 -0.2287 61  THR A C   
439  O O   . THR A 63  ? 1.2225 0.8768 0.8388 -0.1042 -0.0526 -0.2573 61  THR A O   
440  C CB  . THR A 63  ? 1.2228 0.8245 0.8383 -0.0729 -0.0912 -0.2495 61  THR A CB  
441  O OG1 . THR A 63  ? 1.3218 0.8855 0.8782 -0.0803 -0.0837 -0.2187 61  THR A OG1 
442  C CG2 . THR A 63  ? 1.1866 0.7805 0.8326 -0.0533 -0.1197 -0.2573 61  THR A CG2 
443  N N   . GLN A 64  ? 1.2303 0.8365 0.8040 -0.0983 -0.0905 -0.1927 62  GLN A N   
444  C CA  . GLN A 64  ? 1.2076 0.8125 0.7471 -0.1164 -0.0643 -0.1805 62  GLN A CA  
445  C C   . GLN A 64  ? 1.2201 0.8382 0.7703 -0.1234 -0.0797 -0.1670 62  GLN A C   
446  O O   . GLN A 64  ? 1.2283 0.8431 0.7510 -0.1392 -0.0613 -0.1529 62  GLN A O   
447  C CB  . GLN A 64  ? 1.1733 0.7426 0.6698 -0.1187 -0.0589 -0.1568 62  GLN A CB  
448  C CG  . GLN A 64  ? 1.2093 0.7501 0.6773 -0.1120 -0.0492 -0.1672 62  GLN A CG  
449  C CD  . GLN A 64  ? 1.2967 0.8210 0.7193 -0.1256 -0.0126 -0.1835 62  GLN A CD  
450  O OE1 . GLN A 64  ? 1.3838 0.9048 0.8000 -0.1303 0.0054  -0.2105 62  GLN A OE1 
451  N NE2 . GLN A 64  ? 1.3438 0.8523 0.7301 -0.1351 0.0012  -0.1701 62  GLN A NE2 
452  N N   . LEU A 65  ? 1.2305 0.8558 0.8141 -0.1114 -0.1157 -0.1721 63  LEU A N   
453  C CA  . LEU A 65  ? 1.1746 0.7918 0.7515 -0.1176 -0.1406 -0.1567 63  LEU A CA  
454  C C   . LEU A 65  ? 1.2361 0.8916 0.8564 -0.1106 -0.1531 -0.1871 63  LEU A C   
455  O O   . LEU A 65  ? 1.2066 0.8964 0.8765 -0.0972 -0.1507 -0.2241 63  LEU A O   
456  C CB  . LEU A 65  ? 1.2222 0.7948 0.7841 -0.1103 -0.1816 -0.1365 63  LEU A CB  
457  C CG  . LEU A 65  ? 1.2147 0.7524 0.7353 -0.1268 -0.1690 -0.1080 63  LEU A CG  
458  C CD1 . LEU A 65  ? 1.2477 0.7347 0.7463 -0.1263 -0.2041 -0.0930 63  LEU A CD1 
459  C CD2 . LEU A 65  ? 1.2257 0.7625 0.7159 -0.1526 -0.1438 -0.0924 63  LEU A CD2 
460  N N   . TYR A 66  ? 1.1992 0.8493 0.8034 -0.1213 -0.1667 -0.1758 64  TYR A N   
461  C CA  . TYR A 66  ? 1.1913 0.8809 0.8382 -0.1159 -0.1808 -0.2066 64  TYR A CA  
462  C C   . TYR A 66  ? 1.2153 0.8659 0.8370 -0.1130 -0.2331 -0.1892 64  TYR A C   
463  O O   . TYR A 66  ? 1.2463 0.8421 0.8026 -0.1303 -0.2371 -0.1508 64  TYR A O   
464  C CB  . TYR A 66  ? 1.2049 0.9293 0.8458 -0.1399 -0.1312 -0.2162 64  TYR A CB  
465  C CG  . TYR A 66  ? 1.1919 0.9395 0.8397 -0.1473 -0.0799 -0.2380 64  TYR A CG  
466  C CD1 . TYR A 66  ? 1.1909 0.9044 0.7849 -0.1582 -0.0492 -0.2118 64  TYR A CD1 
467  C CD2 . TYR A 66  ? 1.2027 1.0002 0.9063 -0.1459 -0.0622 -0.2888 64  TYR A CD2 
468  C CE1 . TYR A 66  ? 1.2528 0.9661 0.8314 -0.1660 -0.0079 -0.2295 64  TYR A CE1 
469  C CE2 . TYR A 66  ? 1.2452 1.0458 0.9338 -0.1607 -0.0109 -0.3091 64  TYR A CE2 
470  C CZ  . TYR A 66  ? 1.2544 1.0052 0.8717 -0.1702 0.0135  -0.2763 64  TYR A CZ  
471  O OH  . TYR A 66  ? 1.3125 1.0458 0.8943 -0.1854 0.0586  -0.2944 64  TYR A OH  
472  N N   . LEU A 67  ? 1.2557 0.9312 0.9280 -0.0925 -0.2739 -0.2220 65  LEU A N   
473  C CA  . LEU A 67  ? 1.2568 0.8848 0.8973 -0.0865 -0.3337 -0.2100 65  LEU A CA  
474  C C   . LEU A 67  ? 1.2650 0.9181 0.8964 -0.1080 -0.3171 -0.2133 65  LEU A C   
475  O O   . LEU A 67  ? 1.2487 0.9706 0.9497 -0.1011 -0.3104 -0.2567 65  LEU A O   
476  C CB  . LEU A 67  ? 1.2549 0.8893 0.9569 -0.0459 -0.4000 -0.2472 65  LEU A CB  
477  C CG  . LEU A 67  ? 1.4007 0.9747 1.0635 -0.0345 -0.4741 -0.2398 65  LEU A CG  
478  C CD1 . LEU A 67  ? 1.4580 0.9189 0.9990 -0.0554 -0.4912 -0.1828 65  LEU A CD1 
479  C CD2 . LEU A 67  ? 1.4092 0.9929 1.1453 0.0134  -0.5467 -0.2847 65  LEU A CD2 
480  N N   . GLY A 68  ? 1.2957 0.8946 0.8436 -0.1372 -0.3072 -0.1717 66  GLY A N   
481  C CA  . GLY A 68  ? 1.3075 0.9217 0.8368 -0.1605 -0.2905 -0.1708 66  GLY A CA  
482  C C   . GLY A 68  ? 1.3588 0.8938 0.8139 -0.1683 -0.3442 -0.1469 66  GLY A C   
483  O O   . GLY A 68  ? 1.3593 0.8192 0.7296 -0.1922 -0.3397 -0.1076 66  GLY A O   
484  N N   . GLY A 69  ? 1.3865 0.9330 0.8698 -0.1502 -0.3958 -0.1741 67  GLY A N   
485  C CA  . GLY A 69  ? 1.4771 0.9305 0.8770 -0.1537 -0.4597 -0.1532 67  GLY A CA  
486  C C   . GLY A 69  ? 1.5905 0.9633 0.9544 -0.1301 -0.5170 -0.1408 67  GLY A C   
487  O O   . GLY A 69  ? 1.6028 1.0072 1.0429 -0.0881 -0.5570 -0.1747 67  GLY A O   
488  N N   . MET A 70  ? 1.6857 0.9527 0.9333 -0.1597 -0.5172 -0.0959 68  MET A N   
489  C CA  . MET A 70  ? 1.6521 0.8276 0.8463 -0.1460 -0.5635 -0.0803 68  MET A CA  
490  C C   . MET A 70  ? 1.6043 0.7808 0.7898 -0.1655 -0.5050 -0.0595 68  MET A C   
491  O O   . MET A 70  ? 1.7151 0.8401 0.8825 -0.1501 -0.5335 -0.0541 68  MET A O   
492  C CB  . MET A 70  ? 1.8409 0.8847 0.9129 -0.1635 -0.6018 -0.0444 68  MET A CB  
493  N N   . SER A 71  ? 1.5241 0.7563 0.7240 -0.1966 -0.4281 -0.0506 69  SER A N   
494  C CA  . SER A 71  ? 1.4931 0.7306 0.6898 -0.2151 -0.3746 -0.0352 69  SER A CA  
495  C C   . SER A 71  ? 1.4140 0.7558 0.7181 -0.1880 -0.3413 -0.0610 69  SER A C   
496  O O   . SER A 71  ? 1.3743 0.7823 0.7522 -0.1608 -0.3528 -0.0924 69  SER A O   
497  C CB  . SER A 71  ? 1.4952 0.7178 0.6365 -0.2652 -0.3169 -0.0133 69  SER A CB  
498  O OG  . SER A 71  ? 1.6679 0.7762 0.6941 -0.3004 -0.3359 0.0113  69  SER A OG  
499  N N   . TYR A 72  ? 1.3621 0.7147 0.6720 -0.1983 -0.2989 -0.0515 70  TYR A N   
500  C CA  . TYR A 72  ? 1.2828 0.7104 0.6708 -0.1764 -0.2696 -0.0721 70  TYR A CA  
501  C C   . TYR A 72  ? 1.2460 0.7089 0.6353 -0.2002 -0.2068 -0.0648 70  TYR A C   
502  O O   . TYR A 72  ? 1.2189 0.6456 0.5598 -0.2303 -0.1859 -0.0440 70  TYR A O   
503  C CB  . TYR A 72  ? 1.3299 0.7306 0.7244 -0.1586 -0.2889 -0.0711 70  TYR A CB  
504  C CG  . TYR A 72  ? 1.3880 0.7238 0.7552 -0.1397 -0.3564 -0.0712 70  TYR A CG  
505  C CD1 . TYR A 72  ? 1.4204 0.7879 0.8476 -0.1023 -0.3989 -0.1024 70  TYR A CD1 
506  C CD2 . TYR A 72  ? 1.4673 0.7041 0.7459 -0.1608 -0.3785 -0.0443 70  TYR A CD2 
507  C CE1 . TYR A 72  ? 1.4893 0.7904 0.8918 -0.0789 -0.4701 -0.1054 70  TYR A CE1 
508  C CE2 . TYR A 72  ? 1.5246 0.6819 0.7603 -0.1427 -0.4461 -0.0428 70  TYR A CE2 
509  C CZ  . TYR A 72  ? 1.5408 0.7299 0.8401 -0.0981 -0.4960 -0.0726 70  TYR A CZ  
510  O OH  . TYR A 72  ? 1.7346 0.8390 0.9929 -0.0739 -0.5722 -0.0741 70  TYR A OH  
511  N N   . TYR A 73  ? 1.1653 0.6934 0.6070 -0.1882 -0.1768 -0.0856 71  TYR A N   
512  C CA  . TYR A 73  ? 1.1187 0.6703 0.5551 -0.2057 -0.1248 -0.0807 71  TYR A CA  
513  C C   . TYR A 73  ? 1.1075 0.6967 0.5822 -0.1875 -0.1022 -0.1000 71  TYR A C   
514  O O   . TYR A 73  ? 1.0947 0.7054 0.6074 -0.1664 -0.1179 -0.1225 71  TYR A O   
515  C CB  . TYR A 73  ? 1.1035 0.6740 0.5283 -0.2242 -0.1053 -0.0826 71  TYR A CB  
516  C CG  . TYR A 73  ? 1.1426 0.6674 0.5173 -0.2458 -0.1277 -0.0646 71  TYR A CG  
517  C CD1 . TYR A 73  ? 1.1614 0.6478 0.4870 -0.2773 -0.1058 -0.0431 71  TYR A CD1 
518  C CD2 . TYR A 73  ? 1.2512 0.7671 0.6260 -0.2360 -0.1721 -0.0736 71  TYR A CD2 
519  C CE1 . TYR A 73  ? 1.2322 0.6638 0.4962 -0.3041 -0.1221 -0.0278 71  TYR A CE1 
520  C CE2 . TYR A 73  ? 1.2958 0.7528 0.6067 -0.2571 -0.1977 -0.0560 71  TYR A CE2 
521  C CZ  . TYR A 73  ? 1.2947 0.7052 0.5432 -0.2940 -0.1698 -0.0315 71  TYR A CZ  
522  O OH  . TYR A 73  ? 1.3533 0.6928 0.5232 -0.3218 -0.1910 -0.0150 71  TYR A OH  
523  N N   . CYS A 74  ? 1.0791 0.6701 0.5399 -0.1965 -0.0663 -0.0939 72  CYS A N   
524  C CA  . CYS A 74  ? 1.1427 0.7488 0.6144 -0.1842 -0.0441 -0.1094 72  CYS A CA  
525  C C   . CYS A 74  ? 1.1561 0.7872 0.6248 -0.1933 -0.0135 -0.1268 72  CYS A C   
526  O O   . CYS A 74  ? 1.1066 0.7525 0.5758 -0.2063 -0.0118 -0.1280 72  CYS A O   
527  C CB  . CYS A 74  ? 1.1184 0.7029 0.5712 -0.1851 -0.0303 -0.0975 72  CYS A CB  
528  S SG  . CYS A 74  ? 1.1182 0.6986 0.5440 -0.2061 0.0012  -0.0877 72  CYS A SG  
529  N N   . LYS A 75  ? 1.1286 0.7567 0.5856 -0.1897 0.0118  -0.1415 73  LYS A N   
530  C CA  . LYS A 75  ? 1.1925 0.8338 0.6353 -0.2042 0.0470  -0.1619 73  LYS A CA  
531  C C   . LYS A 75  ? 1.2449 0.8712 0.6488 -0.2217 0.0704  -0.1459 73  LYS A C   
532  O O   . LYS A 75  ? 1.3020 0.9411 0.6943 -0.2385 0.0975  -0.1599 73  LYS A O   
533  C CB  . LYS A 75  ? 1.2695 0.8900 0.6873 -0.2020 0.0701  -0.1816 73  LYS A CB  
534  N N   . SER A 76  ? 1.1929 0.7955 0.5817 -0.2194 0.0622  -0.1217 74  SER A N   
535  C CA  . SER A 76  ? 1.2259 0.8146 0.5852 -0.2336 0.0836  -0.1106 74  SER A CA  
536  C C   . SER A 76  ? 1.1856 0.7908 0.5562 -0.2511 0.0781  -0.0983 74  SER A C   
537  O O   . SER A 76  ? 1.3161 0.9148 0.6662 -0.2666 0.0990  -0.0919 74  SER A O   
538  C CB  . SER A 76  ? 1.3155 0.8728 0.6615 -0.2216 0.0788  -0.1009 74  SER A CB  
539  O OG  . SER A 76  ? 1.4099 0.9398 0.7363 -0.2039 0.0743  -0.1100 74  SER A OG  
540  N N   . HIS A 77  ? 1.1407 0.7582 0.5358 -0.2492 0.0489  -0.0957 75  HIS A N   
541  C CA  . HIS A 77  ? 1.1670 0.7796 0.5539 -0.2676 0.0370  -0.0821 75  HIS A CA  
542  C C   . HIS A 77  ? 1.1089 0.7389 0.5114 -0.2659 0.0109  -0.0924 75  HIS A C   
543  O O   . HIS A 77  ? 1.0871 0.7025 0.4698 -0.2817 -0.0043 -0.0818 75  HIS A O   
544  C CB  . HIS A 77  ? 1.0971 0.6812 0.4794 -0.2704 0.0180  -0.0660 75  HIS A CB  
545  C CG  . HIS A 77  ? 1.1367 0.7110 0.5161 -0.2761 0.0409  -0.0624 75  HIS A CG  
546  N ND1 . HIS A 77  ? 1.1770 0.7447 0.5746 -0.2600 0.0325  -0.0652 75  HIS A ND1 
547  C CD2 . HIS A 77  ? 1.1868 0.7593 0.5545 -0.2943 0.0689  -0.0611 75  HIS A CD2 
548  C CE1 . HIS A 77  ? 1.1056 0.6711 0.5085 -0.2659 0.0513  -0.0687 75  HIS A CE1 
549  N NE2 . HIS A 77  ? 1.1836 0.7518 0.5698 -0.2863 0.0744  -0.0667 75  HIS A NE2 
550  N N   . LYS A 78  ? 1.0128 0.6710 0.4500 -0.2479 0.0040  -0.1168 76  LYS A N   
551  C CA  . LYS A 78  ? 1.0531 0.7338 0.5231 -0.2392 -0.0297 -0.1353 76  LYS A CA  
552  C C   . LYS A 78  ? 1.1942 0.9022 0.6651 -0.2569 -0.0145 -0.1491 76  LYS A C   
553  O O   . LYS A 78  ? 1.1495 0.8703 0.6070 -0.2720 0.0302  -0.1561 76  LYS A O   
554  C CB  . LYS A 78  ? 1.0960 0.8070 0.6165 -0.2164 -0.0370 -0.1669 76  LYS A CB  
555  C CG  . LYS A 78  ? 1.0636 0.8061 0.5947 -0.2251 0.0102  -0.1967 76  LYS A CG  
556  C CD  . LYS A 78  ? 1.1267 0.8923 0.7033 -0.2079 0.0076  -0.2307 76  LYS A CD  
557  C CE  . LYS A 78  ? 1.1837 0.9858 0.7785 -0.2243 0.0523  -0.2748 76  LYS A CE  
558  N NZ  . LYS A 78  ? 1.1301 0.9879 0.7844 -0.2272 0.0401  -0.3109 76  LYS A NZ  
559  N N   . PRO A 79  ? 1.1458 0.8561 0.6267 -0.2550 -0.0544 -0.1543 77  PRO A N   
560  C CA  . PRO A 79  ? 1.1484 0.8890 0.6369 -0.2704 -0.0458 -0.1721 77  PRO A CA  
561  C C   . PRO A 79  ? 1.1434 0.9476 0.6957 -0.2636 -0.0266 -0.2207 77  PRO A C   
562  O O   . PRO A 79  ? 1.1797 1.0014 0.7723 -0.2445 -0.0298 -0.2418 77  PRO A O   
563  C CB  . PRO A 79  ? 1.1059 0.8187 0.5845 -0.2633 -0.1086 -0.1659 77  PRO A CB  
564  C CG  . PRO A 79  ? 1.1413 0.8408 0.6475 -0.2324 -0.1508 -0.1706 77  PRO A CG  
565  C CD  . PRO A 79  ? 1.1314 0.8076 0.6106 -0.2377 -0.1148 -0.1455 77  PRO A CD  
566  N N   . PRO A 80  ? 1.1682 1.0072 0.7298 -0.2831 -0.0013 -0.2430 78  PRO A N   
567  C CA  . PRO A 80  ? 1.1189 1.0214 0.7450 -0.2841 0.0227  -0.2990 78  PRO A CA  
568  C C   . PRO A 80  ? 1.1491 1.0906 0.8583 -0.2532 -0.0247 -0.3386 78  PRO A C   
569  O O   . PRO A 80  ? 1.2152 1.1892 0.9691 -0.2488 -0.0002 -0.3755 78  PRO A O   
570  C CB  . PRO A 80  ? 1.0796 1.0100 0.7052 -0.3088 0.0384  -0.3148 78  PRO A CB  
571  C CG  . PRO A 80  ? 1.1056 0.9868 0.6761 -0.3121 0.0020  -0.2693 78  PRO A CG  
572  C CD  . PRO A 80  ? 1.0932 0.9165 0.6084 -0.3092 0.0107  -0.2236 78  PRO A CD  
573  N N   . ILE A 81  ? 1.1400 1.0725 0.8666 -0.2323 -0.0931 -0.3349 79  ILE A N   
574  C CA  . ILE A 81  ? 1.1629 1.1277 0.9721 -0.1968 -0.1493 -0.3759 79  ILE A CA  
575  C C   . ILE A 81  ? 1.2093 1.1156 0.9881 -0.1734 -0.1830 -0.3404 79  ILE A C   
576  O O   . ILE A 81  ? 1.2931 1.1351 1.0182 -0.1652 -0.2328 -0.3022 79  ILE A O   
577  C CB  . ILE A 81  ? 1.1366 1.1127 0.9761 -0.1826 -0.2151 -0.3959 79  ILE A CB  
578  C CG1 . ILE A 81  ? 1.1201 1.1634 0.9999 -0.2074 -0.1790 -0.4381 79  ILE A CG1 
579  C CG2 . ILE A 81  ? 1.1385 1.1379 1.0634 -0.1384 -0.2843 -0.4385 79  ILE A CG2 
580  C CD1 . ILE A 81  ? 1.2133 1.2188 1.0031 -0.2440 -0.1434 -0.3941 79  ILE A CD1 
581  N N   . SER A 82  ? 1.1943 1.1161 0.9996 -0.1666 -0.1534 -0.3545 80  SER A N   
582  C CA  . SER A 82  ? 1.2065 1.0774 0.9857 -0.1471 -0.1782 -0.3240 80  SER A CA  
583  C C   . SER A 82  ? 1.2049 1.1174 1.0584 -0.1272 -0.1728 -0.3693 80  SER A C   
584  O O   . SER A 82  ? 1.2043 1.1620 1.0869 -0.1442 -0.1163 -0.4048 80  SER A O   
585  C CB  . SER A 82  ? 1.1955 1.0155 0.8905 -0.1692 -0.1353 -0.2721 80  SER A CB  
586  O OG  . SER A 82  ? 1.2173 1.0614 0.8976 -0.1963 -0.0697 -0.2808 80  SER A OG  
587  N N   . PHE A 83  ? 1.2038 1.0929 1.0803 -0.0942 -0.2300 -0.3694 81  PHE A N   
588  C CA  . PHE A 83  ? 1.1992 1.1237 1.1475 -0.0737 -0.2284 -0.4126 81  PHE A CA  
589  C C   . PHE A 83  ? 1.1751 1.0473 1.0692 -0.0733 -0.2134 -0.3738 81  PHE A C   
590  O O   . PHE A 83  ? 1.2051 1.0108 1.0315 -0.0710 -0.2409 -0.3218 81  PHE A O   
591  C CB  . PHE A 83  ? 1.1725 1.1086 1.1945 -0.0319 -0.3071 -0.4479 81  PHE A CB  
592  C CG  . PHE A 83  ? 1.2117 1.2299 1.3350 -0.0246 -0.3179 -0.5173 81  PHE A CG  
593  C CD1 . PHE A 83  ? 1.2417 1.3337 1.4123 -0.0541 -0.2455 -0.5643 81  PHE A CD1 
594  C CD2 . PHE A 83  ? 1.3181 1.3342 1.4858 0.0107  -0.4026 -0.5391 81  PHE A CD2 
595  C CE1 . PHE A 83  ? 1.2385 1.4136 1.5117 -0.0513 -0.2514 -0.6361 81  PHE A CE1 
596  C CE2 . PHE A 83  ? 1.2964 1.3957 1.5704 0.0201  -0.4176 -0.6103 81  PHE A CE2 
597  C CZ  . PHE A 83  ? 1.2377 1.4234 1.5712 -0.0123 -0.3389 -0.6611 81  PHE A CZ  
598  N N   . PRO A 84  ? 1.2166 1.1134 1.1348 -0.0787 -0.1689 -0.4003 82  PRO A N   
599  C CA  . PRO A 84  ? 1.2336 1.0812 1.1034 -0.0758 -0.1604 -0.3669 82  PRO A CA  
600  C C   . PRO A 84  ? 1.1410 0.9600 1.0333 -0.0413 -0.2241 -0.3621 82  PRO A C   
601  O O   . PRO A 84  ? 1.1502 1.0050 1.1226 -0.0157 -0.2580 -0.4088 82  PRO A O   
602  C CB  . PRO A 84  ? 1.1691 1.0482 1.0608 -0.0908 -0.1019 -0.4076 82  PRO A CB  
603  C CG  . PRO A 84  ? 1.1258 1.0793 1.1153 -0.0867 -0.1019 -0.4770 82  PRO A CG  
604  C CD  . PRO A 84  ? 1.2005 1.1668 1.1883 -0.0908 -0.1234 -0.4666 82  PRO A CD  
605  N N   . LEU A 85  ? 1.1548 0.9075 0.9776 -0.0413 -0.2407 -0.3093 83  LEU A N   
606  C CA  . LEU A 85  ? 1.3001 1.0093 1.1255 -0.0133 -0.2985 -0.3004 83  LEU A CA  
607  C C   . LEU A 85  ? 1.2266 0.9632 1.1132 0.0060  -0.2941 -0.3397 83  LEU A C   
608  O O   . LEU A 85  ? 1.2380 0.9792 1.1805 0.0374  -0.3433 -0.3694 83  LEU A O   
609  C CB  . LEU A 85  ? 1.2694 0.9052 1.0072 -0.0266 -0.3024 -0.2425 83  LEU A CB  
610  C CG  . LEU A 85  ? 1.3014 0.8941 0.9734 -0.0463 -0.3153 -0.2050 83  LEU A CG  
611  C CD1 . LEU A 85  ? 1.3139 0.8382 0.9117 -0.0627 -0.3146 -0.1602 83  LEU A CD1 
612  C CD2 . LEU A 85  ? 1.3601 0.9330 1.0427 -0.0269 -0.3791 -0.2172 83  LEU A CD2 
613  N N   . CYS A 86  ? 1.2354 0.9838 1.1078 -0.0120 -0.2379 -0.3421 84  CYS A N   
614  C CA  . CYS A 86  ? 1.2472 1.0188 1.1678 -0.0020 -0.2224 -0.3820 84  CYS A CA  
615  C C   . CYS A 86  ? 1.1979 1.0424 1.1911 -0.0110 -0.1870 -0.4461 84  CYS A C   
616  O O   . CYS A 86  ? 1.2591 1.1166 1.2265 -0.0415 -0.1253 -0.4574 84  CYS A O   
617  C CB  . CYS A 86  ? 1.1992 0.9354 1.0565 -0.0194 -0.1829 -0.3548 84  CYS A CB  
618  S SG  . CYS A 86  ? 1.1675 0.8309 0.9644 -0.0090 -0.2219 -0.2975 84  CYS A SG  
619  N N   . ALA A 87  ? 1.1526 1.0407 1.2357 0.0148  -0.2275 -0.4929 85  ALA A N   
620  C CA  . ALA A 87  ? 1.1887 1.1574 1.3592 0.0057  -0.1972 -0.5644 85  ALA A CA  
621  C C   . ALA A 87  ? 1.2177 1.2315 1.4991 0.0356  -0.2229 -0.6318 85  ALA A C   
622  O O   . ALA A 87  ? 1.2317 1.2187 1.5367 0.0753  -0.2928 -0.6244 85  ALA A O   
623  C CB  . ALA A 87  ? 1.1371 1.1334 1.3282 0.0068  -0.2225 -0.5685 85  ALA A CB  
624  N N   . ASN A 88  ? 1.1921 1.2691 1.5377 0.0139  -0.1643 -0.7007 86  ASN A N   
625  C CA  . ASN A 88  ? 1.1256 1.2627 1.5959 0.0362  -0.1754 -0.7820 86  ASN A CA  
626  C C   . ASN A 88  ? 1.1354 1.2222 1.5981 0.0704  -0.2214 -0.7599 86  ASN A C   
627  O O   . ASN A 88  ? 1.1893 1.2807 1.7213 0.1167  -0.2947 -0.7799 86  ASN A O   
628  C CB  . ASN A 88  ? 1.0841 1.2912 1.6732 0.0664  -0.2284 -0.8377 86  ASN A CB  
629  C CG  . ASN A 88  ? 1.0813 1.3267 1.6626 0.0354  -0.1949 -0.8429 86  ASN A CG  
630  O OD1 . ASN A 88  ? 1.1090 1.3932 1.6858 -0.0093 -0.1100 -0.8614 86  ASN A OD1 
631  N ND2 . ASN A 88  ? 1.0744 1.3015 1.6415 0.0573  -0.2595 -0.8130 86  ASN A ND2 
632  N N   . GLY A 89  ? 1.1491 1.1819 1.5224 0.0474  -0.1794 -0.7201 87  GLY A N   
633  C CA  . GLY A 89  ? 1.1534 1.1360 1.5089 0.0720  -0.2117 -0.6976 87  GLY A CA  
634  C C   . GLY A 89  ? 1.1832 1.1179 1.5292 0.1155  -0.3016 -0.6560 87  GLY A C   
635  O O   . GLY A 89  ? 1.1620 1.0763 1.5431 0.1491  -0.3473 -0.6680 87  GLY A O   
636  N N   . GLN A 90  ? 1.2185 1.1253 1.5069 0.1120  -0.3259 -0.6070 88  GLN A N   
637  C CA  . GLN A 90  ? 1.2366 1.0801 1.4909 0.1439  -0.4074 -0.5651 88  GLN A CA  
638  C C   . GLN A 90  ? 1.2509 1.0371 1.3887 0.1169  -0.3979 -0.4893 88  GLN A C   
639  O O   . GLN A 90  ? 1.2494 1.0611 1.3578 0.0827  -0.3416 -0.4795 88  GLN A O   
640  C CB  . GLN A 90  ? 1.2485 1.1303 1.5928 0.1784  -0.4697 -0.6138 88  GLN A CB  
641  C CG  . GLN A 90  ? 1.2622 1.1597 1.7069 0.2256  -0.5250 -0.6723 88  GLN A CG  
642  C CD  . GLN A 90  ? 1.3054 1.2409 1.8434 0.2638  -0.5948 -0.7250 88  GLN A CD  
643  O OE1 . GLN A 90  ? 1.3940 1.2683 1.9269 0.3079  -0.6852 -0.7180 88  GLN A OE1 
644  N NE2 . GLN A 90  ? 1.2158 1.2466 1.8347 0.2466  -0.5555 -0.7802 88  GLN A NE2 
645  N N   . VAL A 91  ? 1.2725 0.9760 1.3415 0.1306  -0.4522 -0.4391 89  VAL A N   
646  C CA  . VAL A 91  ? 1.3730 1.0174 1.3361 0.1046  -0.4479 -0.3730 89  VAL A CA  
647  C C   . VAL A 91  ? 1.4077 1.0081 1.3505 0.1225  -0.5178 -0.3628 89  VAL A C   
648  O O   . VAL A 91  ? 1.3976 0.9453 1.3419 0.1553  -0.5855 -0.3681 89  VAL A O   
649  C CB  . VAL A 91  ? 1.3731 0.9475 1.2562 0.0933  -0.4415 -0.3238 89  VAL A CB  
650  C CG1 . VAL A 91  ? 1.3735 0.8919 1.1594 0.0643  -0.4362 -0.2661 89  VAL A CG1 
651  C CG2 . VAL A 91  ? 1.3475 0.9573 1.2430 0.0774  -0.3795 -0.3344 89  VAL A CG2 
652  N N   . PHE A 92  ? 1.3846 0.9974 1.3005 0.1011  -0.5042 -0.3484 90  PHE A N   
653  C CA  . PHE A 92  ? 1.4175 0.9865 1.3067 0.1143  -0.5693 -0.3410 90  PHE A CA  
654  C C   . PHE A 92  ? 1.5125 0.9602 1.3065 0.1233  -0.6288 -0.2979 90  PHE A C   
655  O O   . PHE A 92  ? 1.5199 0.9085 1.2228 0.0927  -0.6015 -0.2477 90  PHE A O   
656  C CB  . PHE A 92  ? 1.4425 1.0233 1.2854 0.0787  -0.5340 -0.3157 90  PHE A CB  
657  C CG  . PHE A 92  ? 1.4914 0.9934 1.2598 0.0794  -0.5943 -0.2878 90  PHE A CG  
658  C CD1 . PHE A 92  ? 1.4298 0.9487 1.2489 0.1081  -0.6545 -0.3257 90  PHE A CD1 
659  C CD2 . PHE A 92  ? 1.5357 0.9446 1.1820 0.0486  -0.5901 -0.2280 90  PHE A CD2 
660  C CE1 . PHE A 92  ? 1.5660 0.9980 1.3012 0.1077  -0.7148 -0.2990 90  PHE A CE1 
661  C CE2 . PHE A 92  ? 1.6092 0.9315 1.1699 0.0422  -0.6416 -0.2030 90  PHE A CE2 
662  C CZ  . PHE A 92  ? 1.6303 0.9585 1.2285 0.0724  -0.7064 -0.2357 90  PHE A CZ  
663  N N   . GLY A 93  ? 1.5819 0.9897 1.3971 0.1645  -0.7113 -0.3221 91  GLY A N   
664  C CA  . GLY A 93  ? 1.6868 0.9606 1.3994 0.1748  -0.7775 -0.2861 91  GLY A CA  
665  C C   . GLY A 93  ? 1.8186 1.0619 1.5707 0.2270  -0.8758 -0.3251 91  GLY A C   
666  O O   . GLY A 93  ? 1.7150 1.0546 1.5874 0.2540  -0.8862 -0.3821 91  GLY A O   
667  N N   . LEU A 94  ? 1.9094 1.0187 1.5648 0.2411  -0.9334 -0.2899 92  LEU A N   
668  C CA  . LEU A 94  ? 1.9540 1.0155 1.6382 0.2936  -1.0125 -0.3134 92  LEU A CA  
669  C C   . LEU A 94  ? 1.9282 1.0623 1.7549 0.3475  -1.0395 -0.3795 92  LEU A C   
670  O O   . LEU A 94  ? 1.9214 1.1159 1.7985 0.3410  -1.0007 -0.3972 92  LEU A O   
671  C CB  . LEU A 94  ? 2.1326 1.0076 1.6608 0.2887  -1.0599 -0.2615 92  LEU A CB  
672  C CG  . LEU A 94  ? 2.1952 0.9830 1.5673 0.2227  -1.0143 -0.1934 92  LEU A CG  
673  C CD1 . LEU A 94  ? 2.3390 0.9373 1.5646 0.2142  -1.0566 -0.1570 92  LEU A CD1 
674  C CD2 . LEU A 94  ? 2.1218 0.9388 1.4673 0.1898  -0.9863 -0.1773 92  LEU A CD2 
675  N N   . TYR A 95  ? 1.9601 1.0823 1.8517 0.3997  -1.1050 -0.4211 93  TYR A N   
676  C CA  . TYR A 95  ? 1.9568 1.1347 1.9865 0.4556  -1.1385 -0.4916 93  TYR A CA  
677  C C   . TYR A 95  ? 1.8013 1.1580 1.9814 0.4469  -1.0714 -0.5475 93  TYR A C   
678  O O   . TYR A 95  ? 1.7750 1.1808 2.0503 0.4739  -1.0723 -0.5948 93  TYR A O   
679  C CB  . TYR A 95  ? 2.0495 1.1023 2.0043 0.4714  -1.1766 -0.4720 93  TYR A CB  
680  C CG  . TYR A 95  ? 2.2007 1.0664 1.9595 0.4430  -1.2052 -0.4015 93  TYR A CG  
681  C CD1 . TYR A 95  ? 2.3294 1.0876 2.0269 0.4584  -1.2681 -0.4034 93  TYR A CD1 
682  C CD2 . TYR A 95  ? 2.2143 1.0106 1.8479 0.3949  -1.1657 -0.3389 93  TYR A CD2 
683  C CE1 . TYR A 95  ? 2.4683 1.0518 1.9802 0.4227  -1.2883 -0.3458 93  TYR A CE1 
684  C CE2 . TYR A 95  ? 2.3590 0.9869 1.8153 0.3593  -1.1820 -0.2835 93  TYR A CE2 
685  C CZ  . TYR A 95  ? 2.4633 0.9844 1.8567 0.3707  -1.2419 -0.2880 93  TYR A CZ  
686  O OH  . TYR A 95  ? 2.6057 0.9593 1.8170 0.3264  -1.2534 -0.2396 93  TYR A OH  
687  N N   . LYS A 96  ? 1.7280 1.1737 1.9233 0.4042  -1.0083 -0.5461 94  LYS A N   
688  C CA  . LYS A 96  ? 1.5875 1.1821 1.9026 0.3822  -0.9310 -0.6014 94  LYS A CA  
689  C C   . LYS A 96  ? 1.5648 1.2659 2.0605 0.4295  -0.9480 -0.6939 94  LYS A C   
690  O O   . LYS A 96  ? 1.5448 1.3532 2.1412 0.4254  -0.9198 -0.7450 94  LYS A O   
691  C CB  . LYS A 96  ? 1.5497 1.2022 1.8443 0.3332  -0.8703 -0.5893 94  LYS A CB  
692  N N   . VAL A 105 ? 1.1246 1.0662 1.5202 -0.2638 -0.5572 -0.2612 103 VAL A N   
693  C CA  . VAL A 105 ? 1.1676 0.9810 1.4480 -0.2825 -0.5375 -0.2616 103 VAL A CA  
694  C C   . VAL A 105 ? 1.1382 0.8965 1.3936 -0.2860 -0.4794 -0.2440 103 VAL A C   
695  O O   . VAL A 105 ? 1.2049 0.8608 1.3514 -0.2693 -0.4570 -0.2390 103 VAL A O   
696  C CB  . VAL A 105 ? 1.2503 1.0610 1.5455 -0.3367 -0.5525 -0.2764 103 VAL A CB  
697  C CG1 . VAL A 105 ? 1.2277 1.0887 1.6168 -0.3892 -0.5175 -0.2683 103 VAL A CG1 
698  C CG2 . VAL A 105 ? 1.3366 1.0124 1.4974 -0.3374 -0.5456 -0.2836 103 VAL A CG2 
699  N N   . THR A 106 ? 1.0885 0.9214 1.4480 -0.3059 -0.4527 -0.2331 104 THR A N   
700  C CA  . THR A 106 ? 1.1228 0.9091 1.4610 -0.3037 -0.3973 -0.2127 104 THR A CA  
701  C C   . THR A 106 ? 1.0750 0.8225 1.3325 -0.2462 -0.3817 -0.2020 104 THR A C   
702  O O   . THR A 106 ? 1.1599 0.8193 1.3302 -0.2357 -0.3506 -0.1920 104 THR A O   
703  C CB  . THR A 106 ? 1.0479 0.9415 1.4998 -0.3185 -0.3557 -0.1940 104 THR A CB  
704  O OG1 . THR A 106 ? 1.0665 1.0673 1.5834 -0.2780 -0.3665 -0.1940 104 THR A OG1 
705  C CG2 . THR A 106 ? 1.0047 0.9406 1.5409 -0.3855 -0.3678 -0.2016 104 THR A CG2 
706  N N   . ASP A 107 ? 0.9904 0.8036 1.2768 -0.2084 -0.4031 -0.2036 105 ASP A N   
707  C CA  . ASP A 107 ? 1.0862 0.8558 1.2929 -0.1614 -0.3930 -0.1936 105 ASP A CA  
708  C C   . ASP A 107 ? 1.0541 0.7134 1.1406 -0.1570 -0.4152 -0.2027 105 ASP A C   
709  O O   . ASP A 107 ? 1.0879 0.6852 1.0957 -0.1398 -0.3838 -0.1895 105 ASP A O   
710  C CB  . ASP A 107 ? 1.0612 0.9030 1.3097 -0.1222 -0.4202 -0.1968 105 ASP A CB  
711  C CG  . ASP A 107 ? 1.0076 0.9594 1.3659 -0.1177 -0.3894 -0.1876 105 ASP A CG  
712  O OD1 . ASP A 107 ? 1.0088 0.9779 1.4064 -0.1487 -0.3458 -0.1758 105 ASP A OD1 
713  O OD2 . ASP A 107 ? 1.0359 1.0512 1.4339 -0.0802 -0.4073 -0.1916 105 ASP A OD2 
714  N N   . PHE A 108 ? 1.1131 0.7603 1.1815 -0.1675 -0.4578 -0.2196 106 PHE A N   
715  C CA  . PHE A 108 ? 1.2055 0.7621 1.1545 -0.1566 -0.4577 -0.2198 106 PHE A CA  
716  C C   . PHE A 108 ? 1.1987 0.6876 1.0976 -0.1724 -0.4108 -0.2134 106 PHE A C   
717  O O   . PHE A 108 ? 1.1823 0.6074 0.9905 -0.1517 -0.3877 -0.2052 106 PHE A O   
718  C CB  . PHE A 108 ? 1.1974 0.7577 1.1404 -0.1677 -0.5041 -0.2372 106 PHE A CB  
719  C CG  . PHE A 108 ? 1.2811 0.7479 1.1061 -0.1611 -0.5026 -0.2399 106 PHE A CG  
720  C CD1 . PHE A 108 ? 1.3106 0.7339 1.0499 -0.1264 -0.5130 -0.2320 106 PHE A CD1 
721  C CD2 . PHE A 108 ? 1.3394 0.7575 1.1359 -0.1894 -0.4891 -0.2497 106 PHE A CD2 
722  C CE1 . PHE A 108 ? 1.3920 0.7346 1.0254 -0.1205 -0.5094 -0.2337 106 PHE A CE1 
723  C CE2 . PHE A 108 ? 1.4225 0.7566 1.1108 -0.1788 -0.4878 -0.2544 106 PHE A CE2 
724  C CZ  . PHE A 108 ? 1.4464 0.7470 1.0553 -0.1445 -0.4973 -0.2461 106 PHE A CZ  
725  N N   . ASN A 109 ? 1.1847 0.6891 1.1438 -0.2080 -0.3948 -0.2156 107 ASN A N   
726  C CA  . ASN A 109 ? 1.2144 0.6462 1.1233 -0.2184 -0.3526 -0.2098 107 ASN A CA  
727  C C   . ASN A 109 ? 1.1258 0.5389 1.0086 -0.1923 -0.3099 -0.1894 107 ASN A C   
728  O O   . ASN A 109 ? 1.1954 0.5440 0.9992 -0.1744 -0.2818 -0.1840 107 ASN A O   
729  C CB  . ASN A 109 ? 1.2009 0.6490 1.1797 -0.2646 -0.3441 -0.2123 107 ASN A CB  
730  C CG  . ASN A 109 ? 1.2676 0.7118 1.2493 -0.2958 -0.3805 -0.2340 107 ASN A CG  
731  O OD1 . ASN A 109 ? 1.3182 0.7351 1.2385 -0.2793 -0.4107 -0.2470 107 ASN A OD1 
732  N ND2 . ASN A 109 ? 1.2894 0.7608 1.3412 -0.3436 -0.3775 -0.2366 107 ASN A ND2 
733  N N   . ALA A 110 ? 1.1469 0.6225 1.0992 -0.1880 -0.3046 -0.1784 108 ALA A N   
734  C CA  . ALA A 110 ? 1.0692 0.5517 1.0025 -0.1593 -0.2581 -0.1542 108 ALA A CA  
735  C C   . ALA A 110 ? 1.0984 0.5438 0.9480 -0.1295 -0.2645 -0.1534 108 ALA A C   
736  O O   . ALA A 110 ? 1.0744 0.4835 0.8685 -0.1137 -0.2307 -0.1411 108 ALA A O   
737  C CB  . ALA A 110 ? 0.9552 0.5325 0.9756 -0.1528 -0.2431 -0.1398 108 ALA A CB  
738  N N   . ILE A 111 ? 1.1532 0.6097 0.9932 -0.1214 -0.3076 -0.1649 109 ILE A N   
739  C CA  . ILE A 111 ? 1.1140 0.5342 0.8704 -0.0973 -0.3111 -0.1593 109 ILE A CA  
740  C C   . ILE A 111 ? 1.1519 0.5070 0.8222 -0.0951 -0.2962 -0.1614 109 ILE A C   
741  O O   . ILE A 111 ? 1.1455 0.4675 0.7471 -0.0800 -0.2750 -0.1511 109 ILE A O   
742  C CB  . ILE A 111 ? 1.0928 0.5361 0.8527 -0.0847 -0.3583 -0.1664 109 ILE A CB  
743  C CG1 . ILE A 111 ? 1.0057 0.5170 0.8449 -0.0748 -0.3666 -0.1636 109 ILE A CG1 
744  C CG2 . ILE A 111 ? 1.0842 0.4771 0.7458 -0.0651 -0.3603 -0.1563 109 ILE A CG2 
745  C CD1 . ILE A 111 ? 1.0988 0.6369 0.9585 -0.0590 -0.4219 -0.1769 109 ILE A CD1 
746  N N   . ALA A 112 ? 1.1425 0.4768 0.8135 -0.1114 -0.3067 -0.1759 110 ALA A N   
747  C CA  . ALA A 112 ? 1.2217 0.4876 0.8050 -0.1052 -0.2962 -0.1821 110 ALA A CA  
748  C C   . ALA A 112 ? 1.2254 0.4538 0.7851 -0.0991 -0.2489 -0.1754 110 ALA A C   
749  O O   . ALA A 112 ? 1.3228 0.4988 0.8004 -0.0808 -0.2290 -0.1757 110 ALA A O   
750  C CB  . ALA A 112 ? 1.3425 0.5918 0.9269 -0.1247 -0.3295 -0.2022 110 ALA A CB  
751  N N   . THR A 113 ? 1.2656 0.5163 0.8911 -0.1112 -0.2300 -0.1687 111 THR A N   
752  C CA  . THR A 113 ? 1.2375 0.4461 0.8406 -0.1015 -0.1882 -0.1607 111 THR A CA  
753  C C   . THR A 113 ? 1.2271 0.4618 0.8393 -0.0808 -0.1538 -0.1385 111 THR A C   
754  O O   . THR A 113 ? 1.2206 0.4350 0.8149 -0.0624 -0.1162 -0.1272 111 THR A O   
755  C CB  . THR A 113 ? 1.2113 0.4142 0.8689 -0.1291 -0.1857 -0.1630 111 THR A CB  
756  O OG1 . THR A 113 ? 1.2002 0.4704 0.9475 -0.1514 -0.1998 -0.1573 111 THR A OG1 
757  C CG2 . THR A 113 ? 1.2961 0.4624 0.9311 -0.1491 -0.2128 -0.1850 111 THR A CG2 
758  N N   . CYS A 114 ? 1.1178 0.4206 0.7676 -0.0781 -0.1616 -0.1272 112 CYS A N   
759  C CA  . CYS A 114 ? 1.0456 0.4056 0.7237 -0.0616 -0.1279 -0.1021 112 CYS A CA  
760  C C   . CYS A 114 ? 1.1093 0.4572 0.7219 -0.0397 -0.1051 -0.0940 112 CYS A C   
761  O O   . CYS A 114 ? 1.1617 0.4620 0.7052 -0.0368 -0.1165 -0.1065 112 CYS A O   
762  C CB  . CYS A 114 ? 0.9278 0.3536 0.6624 -0.0674 -0.1456 -0.0956 112 CYS A CB  
763  S SG  . CYS A 114 ? 1.0176 0.4378 0.7008 -0.0614 -0.1727 -0.0978 112 CYS A SG  
764  N N   . ASP A 115 ? 1.0896 0.4859 0.7244 -0.0251 -0.0722 -0.0723 113 ASP A N   
765  C CA  . ASP A 115 ? 1.0691 0.4792 0.6614 -0.0079 -0.0465 -0.0612 113 ASP A CA  
766  C C   . ASP A 115 ? 0.9852 0.4495 0.5922 -0.0178 -0.0512 -0.0466 113 ASP A C   
767  O O   . ASP A 115 ? 1.0601 0.5488 0.6414 -0.0125 -0.0298 -0.0345 113 ASP A O   
768  C CB  . ASP A 115 ? 1.0803 0.5086 0.6831 0.0184  -0.0075 -0.0476 113 ASP A CB  
769  C CG  . ASP A 115 ? 1.0132 0.4972 0.6838 0.0179  -0.0002 -0.0299 113 ASP A CG  
770  O OD1 . ASP A 115 ? 0.9914 0.4989 0.7010 -0.0025 -0.0216 -0.0300 113 ASP A OD1 
771  O OD2 . ASP A 115 ? 1.1365 0.6399 0.8165 0.0421  0.0270  -0.0160 113 ASP A OD2 
772  N N   . TRP A 116 ? 0.9482 0.4315 0.5951 -0.0324 -0.0775 -0.0477 114 TRP A N   
773  C CA  . TRP A 116 ? 0.9743 0.4861 0.6229 -0.0425 -0.0890 -0.0378 114 TRP A CA  
774  C C   . TRP A 116 ? 0.9383 0.5096 0.6154 -0.0403 -0.0633 -0.0174 114 TRP A C   
775  O O   . TRP A 116 ? 0.9173 0.5049 0.5787 -0.0529 -0.0665 -0.0074 114 TRP A O   
776  C CB  . TRP A 116 ? 0.9508 0.4219 0.5270 -0.0502 -0.1007 -0.0399 114 TRP A CB  
777  C CG  . TRP A 116 ? 1.0620 0.4744 0.6038 -0.0509 -0.1334 -0.0606 114 TRP A CG  
778  C CD1 . TRP A 116 ? 1.0644 0.4260 0.5508 -0.0453 -0.1314 -0.0734 114 TRP A CD1 
779  C CD2 . TRP A 116 ? 1.0971 0.4982 0.6572 -0.0548 -0.1760 -0.0727 114 TRP A CD2 
780  N NE1 . TRP A 116 ? 1.1646 0.4831 0.6325 -0.0502 -0.1742 -0.0928 114 TRP A NE1 
781  C CE2 . TRP A 116 ? 1.1320 0.4804 0.6502 -0.0548 -0.2022 -0.0919 114 TRP A CE2 
782  C CE3 . TRP A 116 ? 1.0328 0.4642 0.6383 -0.0545 -0.1951 -0.0704 114 TRP A CE3 
783  C CZ2 . TRP A 116 ? 1.1281 0.4653 0.6587 -0.0558 -0.2497 -0.1073 114 TRP A CZ2 
784  C CZ3 . TRP A 116 ? 1.0330 0.4524 0.6503 -0.0503 -0.2374 -0.0859 114 TRP A CZ3 
785  C CH2 . TRP A 116 ? 1.0883 0.4666 0.6732 -0.0516 -0.2656 -0.1034 114 TRP A CH2 
786  N N   . THR A 117 ? 0.8991 0.4985 0.6140 -0.0262 -0.0411 -0.0105 115 THR A N   
787  C CA  . THR A 117 ? 0.9144 0.5746 0.6583 -0.0209 -0.0223 0.0081  115 THR A CA  
788  C C   . THR A 117 ? 0.8407 0.5245 0.6269 -0.0238 -0.0324 0.0111  115 THR A C   
789  O O   . THR A 117 ? 0.8387 0.5686 0.6420 -0.0226 -0.0255 0.0245  115 THR A O   
790  C CB  . THR A 117 ? 0.9549 0.6299 0.7040 0.0050  0.0084  0.0166  115 THR A CB  
791  O OG1 . THR A 117 ? 0.9251 0.5618 0.6872 0.0145  0.0097  0.0101  115 THR A OG1 
792  C CG2 . THR A 117 ? 1.0413 0.6972 0.7440 0.0146  0.0243  0.0125  115 THR A CG2 
793  N N   . ASN A 118 ? 0.8376 0.4957 0.6408 -0.0274 -0.0484 -0.0017 116 ASN A N   
794  C CA  . ASN A 118 ? 0.8260 0.5084 0.6687 -0.0268 -0.0519 -0.0002 116 ASN A CA  
795  C C   . ASN A 118 ? 0.7882 0.4628 0.6282 -0.0343 -0.0808 -0.0120 116 ASN A C   
796  O O   . ASN A 118 ? 0.8125 0.4532 0.6289 -0.0397 -0.1022 -0.0241 116 ASN A O   
797  C CB  . ASN A 118 ? 0.8195 0.4900 0.6937 -0.0250 -0.0428 -0.0037 116 ASN A CB  
798  C CG  . ASN A 118 ? 0.8447 0.4921 0.7040 -0.0145 -0.0195 0.0039  116 ASN A CG  
799  O OD1 . ASN A 118 ? 0.7965 0.4599 0.6650 -0.0016 0.0017  0.0199  116 ASN A OD1 
800  N ND2 . ASN A 118 ? 0.8786 0.4810 0.7061 -0.0162 -0.0247 -0.0082 116 ASN A ND2 
801  N N   . ALA A 119 ? 0.7244 0.4249 0.5808 -0.0303 -0.0823 -0.0090 117 ALA A N   
802  C CA  . ALA A 119 ? 0.7986 0.4858 0.6469 -0.0286 -0.1087 -0.0210 117 ALA A CA  
803  C C   . ALA A 119 ? 0.7672 0.4545 0.6513 -0.0227 -0.1223 -0.0363 117 ALA A C   
804  O O   . ALA A 119 ? 0.7686 0.4339 0.6390 -0.0179 -0.1513 -0.0488 117 ALA A O   
805  C CB  . ALA A 119 ? 0.7274 0.4359 0.5772 -0.0212 -0.1051 -0.0172 117 ALA A CB  
806  N N   . GLY A 120 ? 0.7168 0.4287 0.6466 -0.0241 -0.1034 -0.0345 118 GLY A N   
807  C CA  . GLY A 120 ? 0.7273 0.4523 0.7026 -0.0268 -0.1165 -0.0483 118 GLY A CA  
808  C C   . GLY A 120 ? 0.7770 0.4643 0.7293 -0.0344 -0.1462 -0.0619 118 GLY A C   
809  O O   . GLY A 120 ? 0.7714 0.4712 0.7534 -0.0329 -0.1726 -0.0768 118 GLY A O   
810  N N   . ASP A 121 ? 0.7803 0.4256 0.6790 -0.0405 -0.1424 -0.0573 119 ASP A N   
811  C CA  . ASP A 121 ? 0.8169 0.4171 0.6749 -0.0455 -0.1700 -0.0700 119 ASP A CA  
812  C C   . ASP A 121 ? 0.8882 0.4719 0.7162 -0.0359 -0.2031 -0.0762 119 ASP A C   
813  O O   . ASP A 121 ? 0.9439 0.5124 0.7689 -0.0327 -0.2379 -0.0908 119 ASP A O   
814  C CB  . ASP A 121 ? 0.8519 0.4146 0.6525 -0.0491 -0.1514 -0.0624 119 ASP A CB  
815  C CG  . ASP A 121 ? 0.8897 0.4559 0.7091 -0.0500 -0.1195 -0.0557 119 ASP A CG  
816  O OD1 . ASP A 121 ? 0.8387 0.4260 0.7104 -0.0554 -0.1140 -0.0568 119 ASP A OD1 
817  O OD2 . ASP A 121 ? 0.8638 0.4115 0.6442 -0.0440 -0.0982 -0.0481 119 ASP A OD2 
818  N N   . TYR A 122 ? 0.9021 0.4838 0.7037 -0.0311 -0.1960 -0.0651 120 TYR A N   
819  C CA  . TYR A 122 ? 0.9205 0.4664 0.6783 -0.0221 -0.2267 -0.0689 120 TYR A CA  
820  C C   . TYR A 122 ? 0.9057 0.4806 0.7108 0.0002  -0.2473 -0.0815 120 TYR A C   
821  O O   . TYR A 122 ? 0.9114 0.4555 0.6900 0.0163  -0.2830 -0.0906 120 TYR A O   
822  C CB  . TYR A 122 ? 0.9278 0.4571 0.6415 -0.0307 -0.2131 -0.0538 120 TYR A CB  
823  C CG  . TYR A 122 ? 0.9738 0.4915 0.6492 -0.0506 -0.1909 -0.0405 120 TYR A CG  
824  C CD1 . TYR A 122 ? 0.8912 0.4529 0.5993 -0.0546 -0.1564 -0.0308 120 TYR A CD1 
825  C CD2 . TYR A 122 ? 0.9627 0.4267 0.5667 -0.0621 -0.2026 -0.0364 120 TYR A CD2 
826  C CE1 . TYR A 122 ? 0.8673 0.4300 0.5470 -0.0650 -0.1340 -0.0196 120 TYR A CE1 
827  C CE2 . TYR A 122 ? 0.9020 0.3673 0.4751 -0.0779 -0.1762 -0.0241 120 TYR A CE2 
828  C CZ  . TYR A 122 ? 0.8956 0.4154 0.5113 -0.0771 -0.1418 -0.0168 120 TYR A CZ  
829  O OH  . TYR A 122 ? 0.9054 0.4376 0.4965 -0.0855 -0.1137 -0.0053 120 TYR A OH  
830  N N   . ILE A 123 ? 0.8711 0.5056 0.7433 0.0047  -0.2240 -0.0812 121 ILE A N   
831  C CA  . ILE A 123 ? 0.8633 0.5422 0.7903 0.0283  -0.2355 -0.0931 121 ILE A CA  
832  C C   . ILE A 123 ? 0.8707 0.5700 0.8382 0.0299  -0.2654 -0.1081 121 ILE A C   
833  O O   . ILE A 123 ? 0.8613 0.5672 0.8376 0.0554  -0.2988 -0.1206 121 ILE A O   
834  C CB  . ILE A 123 ? 0.8323 0.5716 0.8167 0.0283  -0.1968 -0.0864 121 ILE A CB  
835  C CG1 . ILE A 123 ? 0.8569 0.5762 0.7956 0.0309  -0.1774 -0.0746 121 ILE A CG1 
836  C CG2 . ILE A 123 ? 0.8501 0.6521 0.9029 0.0515  -0.2011 -0.0987 121 ILE A CG2 
837  C CD1 . ILE A 123 ? 0.8032 0.5722 0.7804 0.0353  -0.1418 -0.0671 121 ILE A CD1 
838  N N   . LEU A 124 ? 0.8611 0.5677 0.8508 0.0038  -0.2569 -0.1081 122 LEU A N   
839  C CA  . LEU A 124 ? 0.8239 0.5452 0.8470 -0.0031 -0.2901 -0.1240 122 LEU A CA  
840  C C   . LEU A 124 ? 0.9453 0.6054 0.8973 0.0089  -0.3354 -0.1323 122 LEU A C   
841  O O   . LEU A 124 ? 0.9894 0.6702 0.9669 0.0234  -0.3769 -0.1470 122 LEU A O   
842  C CB  . LEU A 124 ? 0.8340 0.5477 0.8702 -0.0365 -0.2727 -0.1230 122 LEU A CB  
843  C CG  . LEU A 124 ? 0.9437 0.6911 1.0397 -0.0556 -0.2999 -0.1396 122 LEU A CG  
844  C CD1 . LEU A 124 ? 0.8936 0.7374 1.0960 -0.0577 -0.2853 -0.1397 122 LEU A CD1 
845  C CD2 . LEU A 124 ? 0.9729 0.6703 1.0415 -0.0877 -0.2891 -0.1407 122 LEU A CD2 
846  N N   . ALA A 125 ? 0.9197 0.5077 0.7821 0.0032  -0.3282 -0.1217 123 ALA A N   
847  C CA  . ALA A 125 ? 1.0074 0.5255 0.7865 0.0104  -0.3657 -0.1253 123 ALA A CA  
848  C C   . ALA A 125 ? 1.0607 0.5653 0.8225 0.0434  -0.3996 -0.1286 123 ALA A C   
849  O O   . ALA A 125 ? 1.0349 0.4760 0.7236 0.0539  -0.4363 -0.1305 123 ALA A O   
850  C CB  . ALA A 125 ? 0.9847 0.4396 0.6767 -0.0058 -0.3408 -0.1095 123 ALA A CB  
851  N N   . ASN A 126 ? 1.0557 0.6110 0.8742 0.0634  -0.3880 -0.1295 124 ASN A N   
852  C CA  . ASN A 126 ? 1.0866 0.6230 0.8851 0.1028  -0.4167 -0.1343 124 ASN A CA  
853  C C   . ASN A 126 ? 1.0263 0.6556 0.9262 0.1331  -0.4272 -0.1495 124 ASN A C   
854  O O   . ASN A 126 ? 1.1176 0.7389 1.0084 0.1764  -0.4554 -0.1573 124 ASN A O   
855  C CB  . ASN A 126 ? 1.0126 0.5057 0.7600 0.1047  -0.3915 -0.1218 124 ASN A CB  
856  C CG  . ASN A 126 ? 1.1419 0.5279 0.7727 0.0937  -0.4062 -0.1096 124 ASN A CG  
857  O OD1 . ASN A 126 ? 1.2169 0.5402 0.7891 0.1195  -0.4451 -0.1127 124 ASN A OD1 
858  N ND2 . ASN A 126 ? 1.1530 0.5190 0.7491 0.0560  -0.3745 -0.0943 124 ASN A ND2 
859  N N   . THR A 127 ? 1.0072 0.7229 1.0013 0.1125  -0.4043 -0.1532 125 THR A N   
860  C CA  . THR A 127 ? 0.9702 0.7925 1.0743 0.1322  -0.4087 -0.1658 125 THR A CA  
861  C C   . THR A 127 ? 0.9943 0.8627 1.1540 0.1162  -0.4453 -0.1791 125 THR A C   
862  O O   . THR A 127 ? 0.9730 0.9472 1.2408 0.1194  -0.4475 -0.1887 125 THR A O   
863  C CB  . THR A 127 ? 0.9771 0.8662 1.1481 0.1149  -0.3523 -0.1576 125 THR A CB  
864  O OG1 . THR A 127 ? 0.8989 0.7671 1.0608 0.0672  -0.3270 -0.1473 125 THR A OG1 
865  C CG2 . THR A 127 ? 0.9597 0.8132 1.0803 0.1372  -0.3245 -0.1492 125 THR A CG2 
866  N N   . CYS A 128 ? 0.9907 0.7840 1.0773 0.0971  -0.4739 -0.1801 126 CYS A N   
867  C CA  . CYS A 128 ? 1.0679 0.8850 1.1860 0.0759  -0.5126 -0.1945 126 CYS A CA  
868  C C   . CYS A 128 ? 1.0888 0.8871 1.1741 0.1145  -0.5790 -0.2065 126 CYS A C   
869  O O   . CYS A 128 ? 1.2066 0.9656 1.2416 0.1582  -0.5921 -0.2023 126 CYS A O   
870  C CB  . CYS A 128 ? 1.1132 0.8533 1.1615 0.0331  -0.4992 -0.1900 126 CYS A CB  
871  S SG  . CYS A 128 ? 1.1589 0.7629 1.0485 0.0420  -0.5028 -0.1774 126 CYS A SG  
872  N N   . THR A 129 ? 1.0786 0.8982 1.1865 0.0984  -0.6247 -0.2218 127 THR A N   
873  C CA  . THR A 129 ? 1.1454 0.9407 1.2121 0.1334  -0.6744 -0.2268 127 THR A CA  
874  C C   . THR A 129 ? 1.1984 0.8510 1.1113 0.1423  -0.6719 -0.2112 127 THR A C   
875  O O   . THR A 129 ? 1.2546 0.8385 1.0993 0.1138  -0.6360 -0.1987 127 THR A O   
876  C CB  . THR A 129 ? 1.1859 1.0302 1.3015 0.1060  -0.7020 -0.2397 127 THR A CB  
877  O OG1 . THR A 129 ? 1.2038 0.9496 1.2202 0.0726  -0.6937 -0.2344 127 THR A OG1 
878  C CG2 . THR A 129 ? 1.0847 1.0538 1.3430 0.0698  -0.6869 -0.2495 127 THR A CG2 
879  N N   . GLU A 130 ? 1.2804 0.8925 1.1422 0.1822  -0.7068 -0.2108 128 GLU A N   
880  C CA  . GLU A 130 ? 1.3598 0.8370 1.0798 0.1901  -0.7032 -0.1936 128 GLU A CA  
881  C C   . GLU A 130 ? 1.3859 0.8050 1.0390 0.1494  -0.6879 -0.1859 128 GLU A C   
882  O O   . GLU A 130 ? 1.5068 0.8518 1.0792 0.1310  -0.6515 -0.1675 128 GLU A O   
883  C CB  . GLU A 130 ? 1.4582 0.8999 1.1373 0.2370  -0.7462 -0.1973 128 GLU A CB  
884  C CG  . GLU A 130 ? 1.4764 0.8934 1.1378 0.2818  -0.7453 -0.1950 128 GLU A CG  
885  C CD  . GLU A 130 ? 1.4951 0.7957 1.0470 0.2681  -0.7112 -0.1744 128 GLU A CD  
886  O OE1 . GLU A 130 ? 1.5646 0.7637 1.0115 0.2502  -0.7073 -0.1596 128 GLU A OE1 
887  O OE2 . GLU A 130 ? 1.5364 0.8511 1.1089 0.2740  -0.6876 -0.1721 128 GLU A OE2 
888  N N   . ARG A 131 ? 1.4127 0.8680 1.0975 0.1356  -0.7144 -0.1996 129 ARG A N   
889  C CA  . ARG A 131 ? 1.4513 0.8472 1.0651 0.1029  -0.7002 -0.1947 129 ARG A CA  
890  C C   . ARG A 131 ? 1.3791 0.7786 1.0025 0.0666  -0.6461 -0.1881 129 ARG A C   
891  O O   . ARG A 131 ? 1.4783 0.8069 1.0148 0.0521  -0.6145 -0.1741 129 ARG A O   
892  C CB  . ARG A 131 ? 1.5255 0.9659 1.1803 0.0898  -0.7387 -0.2143 129 ARG A CB  
893  C CG  . ARG A 131 ? 1.5839 0.9363 1.1305 0.0764  -0.7418 -0.2108 129 ARG A CG  
894  C CD  . ARG A 131 ? 1.7515 1.1415 1.3299 0.0639  -0.7868 -0.2319 129 ARG A CD  
895  N NE  . ARG A 131 ? 1.8243 1.2751 1.4602 0.0950  -0.8394 -0.2425 129 ARG A NE  
896  C CZ  . ARG A 131 ? 1.7402 1.3069 1.4976 0.0838  -0.8668 -0.2608 129 ARG A CZ  
897  N NH1 . ARG A 131 ? 1.6894 1.3093 1.5140 0.0363  -0.8512 -0.2717 129 ARG A NH1 
898  N NH2 . ARG A 131 ? 1.6698 1.2997 1.4800 0.1199  -0.9103 -0.2678 129 ARG A NH2 
899  N N   . LEU A 132 ? 1.2888 0.7744 1.0193 0.0529  -0.6338 -0.1981 130 LEU A N   
900  C CA  . LEU A 132 ? 1.3316 0.8181 1.0731 0.0223  -0.5821 -0.1920 130 LEU A CA  
901  C C   . LEU A 132 ? 1.3556 0.7876 1.0300 0.0334  -0.5478 -0.1712 130 LEU A C   
902  O O   . LEU A 132 ? 1.3094 0.7062 0.9396 0.0130  -0.5046 -0.1597 130 LEU A O   
903  C CB  . LEU A 132 ? 1.2287 0.8151 1.0991 0.0064  -0.5779 -0.2054 130 LEU A CB  
904  C CG  . LEU A 132 ? 1.2346 0.8622 1.1649 -0.0315 -0.5846 -0.2203 130 LEU A CG  
905  C CD1 . LEU A 132 ? 1.1371 0.8576 1.1928 -0.0548 -0.5688 -0.2270 130 LEU A CD1 
906  C CD2 . LEU A 132 ? 1.2402 0.7868 1.0853 -0.0564 -0.5537 -0.2150 130 LEU A CD2 
907  N N   . LYS A 133 ? 1.3479 0.7737 1.0145 0.0660  -0.5663 -0.1668 131 LYS A N   
908  C CA  . LYS A 133 ? 1.3091 0.6761 0.9063 0.0707  -0.5369 -0.1465 131 LYS A CA  
909  C C   . LYS A 133 ? 1.3547 0.6350 0.8398 0.0595  -0.5214 -0.1274 131 LYS A C   
910  O O   . LYS A 133 ? 1.3888 0.6387 0.8280 0.0419  -0.4810 -0.1102 131 LYS A O   
911  C CB  . LYS A 133 ? 1.2784 0.6317 0.8678 0.1105  -0.5655 -0.1465 131 LYS A CB  
912  C CG  . LYS A 133 ? 1.2802 0.7221 0.9724 0.1312  -0.5776 -0.1636 131 LYS A CG  
913  C CD  . LYS A 133 ? 1.3490 0.7477 0.9986 0.1722  -0.5906 -0.1581 131 LYS A CD  
914  C CE  . LYS A 133 ? 1.2339 0.7247 0.9835 0.2164  -0.6107 -0.1739 131 LYS A CE  
915  N NZ  . LYS A 133 ? 1.2508 0.8449 1.1121 0.1990  -0.5609 -0.1762 131 LYS A NZ  
916  N N   . LEU A 134 ? 1.3627 0.6081 0.8050 0.0686  -0.5534 -0.1313 132 LEU A N   
917  C CA  . LEU A 134 ? 1.4467 0.6058 0.7763 0.0611  -0.5423 -0.1146 132 LEU A CA  
918  C C   . LEU A 134 ? 1.5072 0.6702 0.8227 0.0325  -0.5094 -0.1170 132 LEU A C   
919  O O   . LEU A 134 ? 1.6069 0.7145 0.8388 0.0205  -0.4797 -0.1021 132 LEU A O   
920  C CB  . LEU A 134 ? 1.5462 0.6583 0.8280 0.0853  -0.5908 -0.1195 132 LEU A CB  
921  C CG  . LEU A 134 ? 1.6736 0.6770 0.8306 0.0903  -0.5890 -0.0988 132 LEU A CG  
922  C CD1 . LEU A 134 ? 1.6593 0.6254 0.7968 0.1043  -0.5871 -0.0860 132 LEU A CD1 
923  C CD2 . LEU A 134 ? 1.7579 0.7183 0.8679 0.1107  -0.6353 -0.1077 132 LEU A CD2 
924  N N   . PHE A 135 ? 1.3865 0.6103 0.7796 0.0212  -0.5141 -0.1369 133 PHE A N   
925  C CA  . PHE A 135 ? 1.3800 0.5992 0.7602 -0.0026 -0.4812 -0.1419 133 PHE A CA  
926  C C   . PHE A 135 ? 1.3671 0.5994 0.7575 -0.0154 -0.4292 -0.1306 133 PHE A C   
927  O O   . PHE A 135 ? 1.3353 0.5290 0.6614 -0.0242 -0.3947 -0.1230 133 PHE A O   
928  C CB  . PHE A 135 ? 1.3671 0.6390 0.8282 -0.0166 -0.4998 -0.1653 133 PHE A CB  
929  C CG  . PHE A 135 ? 1.5126 0.7674 0.9579 -0.0386 -0.4672 -0.1724 133 PHE A CG  
930  C CD1 . PHE A 135 ? 1.4922 0.6768 0.8349 -0.0369 -0.4500 -0.1679 133 PHE A CD1 
931  C CD2 . PHE A 135 ? 1.4506 0.7520 0.9779 -0.0592 -0.4515 -0.1832 133 PHE A CD2 
932  C CE1 . PHE A 135 ? 1.5314 0.6924 0.8530 -0.0496 -0.4206 -0.1769 133 PHE A CE1 
933  C CE2 . PHE A 135 ? 1.4610 0.7318 0.9652 -0.0750 -0.4217 -0.1894 133 PHE A CE2 
934  C CZ  . PHE A 135 ? 1.4626 0.6633 0.8638 -0.0673 -0.4072 -0.1876 133 PHE A CZ  
935  N N   . ALA A 136 ? 1.3227 0.6106 0.7934 -0.0146 -0.4241 -0.1312 134 ALA A N   
936  C CA  . ALA A 136 ? 1.2407 0.5430 0.7248 -0.0249 -0.3794 -0.1204 134 ALA A CA  
937  C C   . ALA A 136 ? 1.2899 0.5400 0.6862 -0.0258 -0.3595 -0.0996 134 ALA A C   
938  O O   . ALA A 136 ? 1.3248 0.5636 0.6911 -0.0395 -0.3204 -0.0927 134 ALA A O   
939  C CB  . ALA A 136 ? 1.1621 0.5217 0.7329 -0.0192 -0.3850 -0.1244 134 ALA A CB  
940  N N   . ALA A 137 ? 1.2558 0.4695 0.6081 -0.0123 -0.3867 -0.0897 135 ALA A N   
941  C CA  . ALA A 137 ? 1.4078 0.5644 0.6742 -0.0212 -0.3689 -0.0679 135 ALA A CA  
942  C C   . ALA A 137 ? 1.3653 0.4765 0.5489 -0.0353 -0.3445 -0.0637 135 ALA A C   
943  O O   . ALA A 137 ? 1.4372 0.5371 0.5806 -0.0548 -0.3068 -0.0534 135 ALA A O   
944  C CB  . ALA A 137 ? 1.3729 0.4760 0.5939 -0.0027 -0.4062 -0.0587 135 ALA A CB  
945  N N   . GLU A 138 ? 1.4246 0.5092 0.5778 -0.0254 -0.3663 -0.0737 136 GLU A N   
946  C CA  . GLU A 138 ? 1.5845 0.6158 0.6452 -0.0331 -0.3444 -0.0715 136 GLU A CA  
947  C C   . GLU A 138 ? 1.5475 0.6074 0.6279 -0.0419 -0.3047 -0.0833 136 GLU A C   
948  O O   . GLU A 138 ? 1.6107 0.6428 0.6214 -0.0503 -0.2658 -0.0776 136 GLU A O   
949  C CB  . GLU A 138 ? 1.5844 0.5770 0.6079 -0.0181 -0.3830 -0.0813 136 GLU A CB  
950  C CG  . GLU A 138 ? 1.7475 0.6741 0.6634 -0.0207 -0.3657 -0.0802 136 GLU A CG  
951  C CD  . GLU A 138 ? 1.9218 0.8203 0.8161 -0.0066 -0.4082 -0.0954 136 GLU A CD  
952  O OE1 . GLU A 138 ? 1.8833 0.8164 0.8464 0.0036  -0.4520 -0.1052 136 GLU A OE1 
953  O OE2 . GLU A 138 ? 1.9479 0.7922 0.7559 -0.0056 -0.3978 -0.0991 136 GLU A OE2 
954  N N   . THR A 139 ? 1.4681 0.5811 0.6400 -0.0392 -0.3119 -0.0998 137 THR A N   
955  C CA  . THR A 139 ? 1.4735 0.6030 0.6675 -0.0442 -0.2748 -0.1100 137 THR A CA  
956  C C   . THR A 139 ? 1.4123 0.5572 0.6054 -0.0534 -0.2355 -0.0979 137 THR A C   
957  O O   . THR A 139 ? 1.3789 0.5289 0.5457 -0.0510 -0.1894 -0.0910 137 THR A O   
958  C CB  . THR A 139 ? 1.4357 0.6149 0.7312 -0.0456 -0.2902 -0.1253 137 THR A CB  
959  O OG1 . THR A 139 ? 1.4677 0.6435 0.7719 -0.0423 -0.3354 -0.1363 137 THR A OG1 
960  C CG2 . THR A 139 ? 1.3676 0.5350 0.6640 -0.0471 -0.2582 -0.1367 137 THR A CG2 
961  N N   . LEU A 140 ? 1.3343 0.5185 0.5840 -0.0584 -0.2449 -0.0861 138 LEU A N   
962  C CA  . LEU A 140 ? 1.2820 0.5180 0.5667 -0.0669 -0.2040 -0.0633 138 LEU A CA  
963  C C   . LEU A 140 ? 1.3465 0.5580 0.5487 -0.0785 -0.1747 -0.0446 138 LEU A C   
964  O O   . LEU A 140 ? 1.2975 0.5537 0.5141 -0.0816 -0.1280 -0.0322 138 LEU A O   
965  C CB  . LEU A 140 ? 1.2395 0.5005 0.5746 -0.0696 -0.2264 -0.0568 138 LEU A CB  
966  C CG  . LEU A 140 ? 1.1774 0.4794 0.5361 -0.0836 -0.1971 -0.0350 138 LEU A CG  
967  C CD1 . LEU A 140 ? 1.0462 0.4174 0.4713 -0.0812 -0.1562 -0.0307 138 LEU A CD1 
968  C CD2 . LEU A 140 ? 1.1323 0.4367 0.5220 -0.0808 -0.2259 -0.0348 138 LEU A CD2 
969  N N   . LYS A 141 ? 1.4166 0.5598 0.5314 -0.0842 -0.2012 -0.0406 139 LYS A N   
970  C CA  . LYS A 141 ? 1.4741 0.5903 0.5039 -0.1013 -0.1706 -0.0194 139 LYS A CA  
971  C C   . LYS A 141 ? 1.5439 0.6638 0.5363 -0.0911 -0.1298 -0.0251 139 LYS A C   
972  O O   . LYS A 141 ? 1.5233 0.6835 0.5079 -0.1009 -0.0796 -0.0072 139 LYS A O   
973  C CB  . LYS A 141 ? 1.5549 0.5785 0.4817 -0.1056 -0.2100 -0.0146 139 LYS A CB  
974  C CG  . LYS A 141 ? 1.6627 0.6509 0.4988 -0.1316 -0.1791 0.0133  139 LYS A CG  
975  C CD  . LYS A 141 ? 1.7200 0.6948 0.5632 -0.1557 -0.1909 0.0343  139 LYS A CD  
976  C CE  . LYS A 141 ? 1.7503 0.7078 0.5330 -0.1913 -0.1529 0.0616  139 LYS A CE  
977  N NZ  . LYS A 141 ? 1.8300 0.7599 0.6147 -0.2188 -0.1681 0.0769  139 LYS A NZ  
978  N N   . ALA A 142 ? 1.5080 0.5880 0.4776 -0.0707 -0.1515 -0.0513 140 ALA A N   
979  C CA  . ALA A 142 ? 1.5766 0.6439 0.4998 -0.0545 -0.1155 -0.0619 140 ALA A CA  
980  C C   . ALA A 142 ? 1.5312 0.6810 0.5404 -0.0450 -0.0677 -0.0567 140 ALA A C   
981  O O   . ALA A 142 ? 1.5922 0.7716 0.5784 -0.0374 -0.0162 -0.0461 140 ALA A O   
982  C CB  . ALA A 142 ? 1.5913 0.5932 0.4789 -0.0390 -0.1563 -0.0945 140 ALA A CB  
983  N N   . THR A 143 ? 1.4435 0.6343 0.5518 -0.0426 -0.0834 -0.0632 141 THR A N   
984  C CA  . THR A 143 ? 1.3285 0.5898 0.5127 -0.0299 -0.0437 -0.0569 141 THR A CA  
985  C C   . THR A 143 ? 1.3842 0.7199 0.5941 -0.0425 -0.0062 -0.0283 141 THR A C   
986  O O   . THR A 143 ? 1.4126 0.8042 0.6453 -0.0268 0.0385  -0.0200 141 THR A O   
987  C CB  . THR A 143 ? 1.2813 0.5698 0.5590 -0.0307 -0.0683 -0.0639 141 THR A CB  
988  O OG1 . THR A 143 ? 1.2457 0.4737 0.5072 -0.0295 -0.1090 -0.0892 141 THR A OG1 
989  C CG2 . THR A 143 ? 1.2518 0.5915 0.5889 -0.0119 -0.0310 -0.0589 141 THR A CG2 
990  N N   . GLU A 144 ? 1.3416 0.6778 0.5471 -0.0708 -0.0260 -0.0133 142 GLU A N   
991  C CA  . GLU A 144 ? 1.3494 0.7494 0.5744 -0.0942 0.0039  0.0137  142 GLU A CA  
992  C C   . GLU A 144 ? 1.4239 0.8304 0.5825 -0.0956 0.0488  0.0249  142 GLU A C   
993  O O   . GLU A 144 ? 1.3531 0.8455 0.5516 -0.1005 0.0913  0.0424  142 GLU A O   
994  C CB  . GLU A 144 ? 1.3221 0.6905 0.5317 -0.1256 -0.0309 0.0248  142 GLU A CB  
995  C CG  . GLU A 144 ? 1.2266 0.6278 0.5187 -0.1281 -0.0564 0.0227  142 GLU A CG  
996  C CD  . GLU A 144 ? 1.3128 0.6611 0.5720 -0.1502 -0.0938 0.0290  142 GLU A CD  
997  O OE1 . GLU A 144 ? 1.2786 0.5575 0.4490 -0.1632 -0.1038 0.0357  142 GLU A OE1 
998  O OE2 . GLU A 144 ? 1.1523 0.5208 0.4656 -0.1516 -0.1127 0.0273  142 GLU A OE2 
999  N N   . GLU A 145 ? 1.4849 0.8065 0.5415 -0.0904 0.0399  0.0152  143 GLU A N   
1000 C CA  . GLU A 145 ? 1.6014 0.9204 0.5787 -0.0920 0.0851  0.0265  143 GLU A CA  
1001 C C   . GLU A 145 ? 1.5713 0.9201 0.5520 -0.0498 0.1273  0.0123  143 GLU A C   
1002 O O   . GLU A 145 ? 1.5541 0.9797 0.5487 -0.0444 0.1820  0.0275  143 GLU A O   
1003 C CB  . GLU A 145 ? 1.6946 0.9006 0.5457 -0.0995 0.0576  0.0218  143 GLU A CB  
1004 C CG  . GLU A 145 ? 1.7756 0.9432 0.5933 -0.1396 0.0296  0.0437  143 GLU A CG  
1005 C CD  . GLU A 145 ? 1.9083 1.1356 0.7275 -0.1782 0.0770  0.0777  143 GLU A CD  
1006 O OE1 . GLU A 145 ? 1.9730 1.2226 0.7428 -0.1764 0.1289  0.0871  143 GLU A OE1 
1007 O OE2 . GLU A 145 ? 1.8926 1.1451 0.7610 -0.2115 0.0629  0.0943  143 GLU A OE2 
1008 N N   . THR A 146 ? 1.6014 0.8904 0.5702 -0.0193 0.1021  -0.0172 144 THR A N   
1009 C CA  . THR A 146 ? 1.6392 0.9299 0.5957 0.0247  0.1372  -0.0342 144 THR A CA  
1010 C C   . THR A 146 ? 1.6517 1.0544 0.7098 0.0427  0.1770  -0.0205 144 THR A C   
1011 O O   . THR A 146 ? 1.7125 1.1284 0.7606 0.0854  0.2148  -0.0296 144 THR A O   
1012 C CB  . THR A 146 ? 1.6370 0.8418 0.5779 0.0433  0.0952  -0.0670 144 THR A CB  
1013 O OG1 . THR A 146 ? 1.6632 0.9047 0.7099 0.0338  0.0669  -0.0659 144 THR A OG1 
1014 C CG2 . THR A 146 ? 1.6493 0.7528 0.4966 0.0270  0.0471  -0.0818 144 THR A CG2 
1015 N N   . PHE A 147 ? 1.5325 1.0112 0.6815 0.0149  0.1669  -0.0001 145 PHE A N   
1016 C CA  . PHE A 147 ? 1.4774 1.0653 0.7259 0.0295  0.1941  0.0137  145 PHE A CA  
1017 C C   . PHE A 147 ? 1.4956 1.1889 0.7757 0.0032  0.2296  0.0429  145 PHE A C   
1018 O O   . PHE A 147 ? 1.5160 1.3128 0.8610 0.0250  0.2653  0.0539  145 PHE A O   
1019 C CB  . PHE A 147 ? 1.4137 1.0114 0.7429 0.0179  0.1537  0.0130  145 PHE A CB  
1020 C CG  . PHE A 147 ? 1.4281 1.1364 0.8539 0.0268  0.1727  0.0303  145 PHE A CG  
1021 C CD1 . PHE A 147 ? 1.4301 1.1572 0.8892 0.0735  0.1897  0.0239  145 PHE A CD1 
1022 C CD2 . PHE A 147 ? 1.3852 1.1696 0.8615 -0.0117 0.1691  0.0525  145 PHE A CD2 
1023 C CE1 . PHE A 147 ? 1.2931 1.1205 0.8357 0.0861  0.2022  0.0406  145 PHE A CE1 
1024 C CE2 . PHE A 147 ? 1.3346 1.2223 0.8970 -0.0040 0.1801  0.0668  145 PHE A CE2 
1025 C CZ  . PHE A 147 ? 1.2898 1.2025 0.8862 0.0470  0.1961  0.0615  145 PHE A CZ  
1026 N N   . LYS A 148 ? 1.5389 1.2065 0.7726 -0.0439 0.2192  0.0566  146 LYS A N   
1027 C CA  . LYS A 148 ? 1.5206 1.2770 0.7737 -0.0817 0.2528  0.0859  146 LYS A CA  
1028 C C   . LYS A 148 ? 1.5731 1.3912 0.8021 -0.0548 0.3172  0.0916  146 LYS A C   
1029 O O   . LYS A 148 ? 1.5774 1.4941 0.8371 -0.0847 0.3542  0.1172  146 LYS A O   
1030 C CB  . LYS A 148 ? 1.5416 1.2227 0.7216 -0.1356 0.2278  0.0984  146 LYS A CB  
1031 C CG  . LYS A 148 ? 1.5296 1.1843 0.7495 -0.1680 0.1740  0.1008  146 LYS A CG  
1032 C CD  . LYS A 148 ? 1.5446 1.0971 0.6737 -0.2086 0.1440  0.1097  146 LYS A CD  
1033 C CE  . LYS A 148 ? 1.6266 1.2217 0.7426 -0.2656 0.1721  0.1423  146 LYS A CE  
1034 N NZ  . LYS A 148 ? 1.6453 1.1210 0.6545 -0.3026 0.1441  0.1535  146 LYS A NZ  
1035 N N   . LEU A 149 ? 1.5769 1.3387 0.7499 -0.0003 0.3319  0.0676  147 LEU A N   
1036 C CA  . LEU A 149 ? 1.5558 1.3659 0.6968 0.0400  0.3951  0.0672  147 LEU A CA  
1037 C C   . LEU A 149 ? 1.5113 1.4121 0.7387 0.0974  0.4205  0.0617  147 LEU A C   
1038 O O   . LEU A 149 ? 1.5981 1.5194 0.7941 0.1508  0.4684  0.0529  147 LEU A O   
1039 C CB  . LEU A 149 ? 1.7285 1.4043 0.7335 0.0688  0.3953  0.0414  147 LEU A CB  
1040 C CG  . LEU A 149 ? 1.7359 1.2865 0.7091 0.0897  0.3391  0.0091  147 LEU A CG  
1041 C CD1 . LEU A 149 ? 1.7933 1.3442 0.7879 0.1545  0.3567  -0.0126 147 LEU A CD1 
1042 C CD2 . LEU A 149 ? 1.7426 1.1569 0.5775 0.0820  0.3163  -0.0080 147 LEU A CD2 
1043 N N   . SER A 150 ? 1.5279 1.4782 0.8558 0.0920  0.3896  0.0669  148 SER A N   
1044 C CA  . SER A 150 ? 1.5544 1.5710 0.9543 0.1503  0.4046  0.0623  148 SER A CA  
1045 C C   . SER A 150 ? 1.5158 1.6974 1.0370 0.1354  0.4166  0.0894  148 SER A C   
1046 O O   . SER A 150 ? 1.4643 1.6984 1.0556 0.1751  0.4116  0.0893  148 SER A O   
1047 C CB  . SER A 150 ? 1.5708 1.4874 0.9718 0.1680  0.3563  0.0420  148 SER A CB  
1048 O OG  . SER A 150 ? 1.5489 1.3188 0.8469 0.1671  0.3339  0.0172  148 SER A OG  
1049 N N   . TYR A 151 ? 1.4357 1.6962 0.9792 0.0769  0.4297  0.1131  149 TYR A N   
1050 C CA  . TYR A 151 ? 1.3799 1.8087 1.0380 0.0569  0.4426  0.1382  149 TYR A CA  
1051 C C   . TYR A 151 ? 1.3045 1.8579 0.9782 0.0733  0.5103  0.1521  149 TYR A C   
1052 O O   . TYR A 151 ? 1.3620 1.8607 0.9451 0.0859  0.5468  0.1454  149 TYR A O   
1053 C CB  . TYR A 151 ? 1.2929 1.7255 0.9747 -0.0288 0.4043  0.1556  149 TYR A CB  
1054 C CG  . TYR A 151 ? 1.3672 1.7437 1.0796 -0.0337 0.3450  0.1463  149 TYR A CG  
1055 C CD1 . TYR A 151 ? 1.4093 1.6332 1.0498 -0.0392 0.3055  0.1278  149 TYR A CD1 
1056 C CD2 . TYR A 151 ? 1.3565 1.8380 1.1692 -0.0300 0.3290  0.1559  149 TYR A CD2 
1057 C CE1 . TYR A 151 ? 1.3226 1.5043 0.9930 -0.0419 0.2579  0.1199  149 TYR A CE1 
1058 C CE2 . TYR A 151 ? 1.2852 1.7126 1.1159 -0.0324 0.2797  0.1479  149 TYR A CE2 
1059 C CZ  . TYR A 151 ? 1.2813 1.5610 1.0421 -0.0384 0.2475  0.1302  149 TYR A CZ  
1060 O OH  . TYR A 151 ? 1.3215 1.5567 1.1026 -0.0395 0.2048  0.1230  149 TYR A OH  
1061 N N   . GLY A 152 ? 1.2982 2.0264 1.0882 0.0738  0.5272  0.1715  150 GLY A N   
1062 C CA  . GLY A 152 ? 1.2537 2.1178 1.0832 0.0925  0.5882  0.1823  150 GLY A CA  
1063 C C   . GLY A 152 ? 1.2810 2.1640 1.0895 0.0101  0.6089  0.2006  150 GLY A C   
1064 O O   . GLY A 152 ? 1.3331 2.1636 1.1102 -0.0658 0.5803  0.2148  150 GLY A O   
1065 N N   . ILE A 153 ? 1.3250 1.3609 1.6523 0.0417  0.2679  0.0504  151 ILE A N   
1066 C CA  . ILE A 153 ? 1.3736 1.3996 1.6758 0.0228  0.2766  0.0178  151 ILE A CA  
1067 C C   . ILE A 153 ? 1.3860 1.4490 1.7670 0.0405  0.2427  0.0453  151 ILE A C   
1068 O O   . ILE A 153 ? 1.3494 1.4377 1.8338 0.0605  0.2294  0.0888  151 ILE A O   
1069 C CB  . ILE A 153 ? 1.3404 1.3176 1.6652 -0.0102 0.3539  -0.0243 151 ILE A CB  
1070 C CG1 . ILE A 153 ? 1.3204 1.2622 1.5487 -0.0388 0.3788  -0.0472 151 ILE A CG1 
1071 C CG2 . ILE A 153 ? 1.3250 1.2953 1.6227 -0.0376 0.3610  -0.0545 151 ILE A CG2 
1072 C CD1 . ILE A 153 ? 1.2733 1.1635 1.4757 -0.0927 0.4499  -0.0952 151 ILE A CD1 
1073 N N   . ALA A 154 ? 1.4250 1.4928 1.7610 0.0288  0.2237  0.0260  152 ALA A N   
1074 C CA  . ALA A 154 ? 1.3958 1.4990 1.7863 0.0397  0.1853  0.0504  152 ALA A CA  
1075 C C   . ALA A 154 ? 1.3822 1.4728 1.8494 0.0257  0.2286  0.0296  152 ALA A C   
1076 O O   . ALA A 154 ? 1.4147 1.4722 1.8248 -0.0039 0.2648  -0.0145 152 ALA A O   
1077 C CB  . ALA A 154 ? 1.4383 1.5573 1.7242 0.0367  0.1288  0.0444  152 ALA A CB  
1078 N N   . THR A 155 ? 1.3415 1.4609 1.9408 0.0412  0.2238  0.0648  153 THR A N   
1079 C CA  . THR A 155 ? 1.3392 1.4556 2.0326 0.0307  0.2641  0.0491  153 THR A CA  
1080 C C   . THR A 155 ? 1.3141 1.4783 2.0502 0.0404  0.2028  0.0888  153 THR A C   
1081 O O   . THR A 155 ? 1.3195 1.5220 2.0962 0.0570  0.1485  0.1449  153 THR A O   
1082 C CB  . THR A 155 ? 1.2927 1.3947 2.1501 0.0383  0.3351  0.0530  153 THR A CB  
1083 O OG1 . THR A 155 ? 1.2747 1.3931 2.1911 0.0642  0.3105  0.1031  153 THR A OG1 
1084 C CG2 . THR A 155 ? 1.2540 1.2966 2.0643 0.0052  0.4212  -0.0131 153 THR A CG2 
1085 N N   . VAL A 156 ? 1.3085 1.4706 2.0279 0.0223  0.2091  0.0620  154 VAL A N   
1086 C CA  . VAL A 156 ? 1.3686 1.5715 2.1065 0.0247  0.1495  0.0938  154 VAL A CA  
1087 C C   . VAL A 156 ? 1.3252 1.5631 2.2564 0.0378  0.1604  0.1395  154 VAL A C   
1088 O O   . VAL A 156 ? 1.2691 1.4926 2.3069 0.0323  0.2302  0.1151  154 VAL A O   
1089 C CB  . VAL A 156 ? 1.4551 1.6424 2.1057 -0.0013 0.1493  0.0510  154 VAL A CB  
1090 C CG1 . VAL A 156 ? 1.4505 1.6780 2.1459 -0.0012 0.0996  0.0827  154 VAL A CG1 
1091 C CG2 . VAL A 156 ? 1.4516 1.6148 1.9369 -0.0111 0.1191  0.0240  154 VAL A CG2 
1092 N N   . ARG A 157 ? 1.2929 1.5778 2.2747 0.0493  0.0925  0.2075  155 ARG A N   
1093 C CA  . ARG A 157 ? 1.2047 1.5329 2.3858 0.0587  0.0861  0.2677  155 ARG A CA  
1094 C C   . ARG A 157 ? 1.2361 1.5836 2.4471 0.0453  0.0789  0.2611  155 ARG A C   
1095 O O   . ARG A 157 ? 1.2017 1.5455 2.5444 0.0463  0.1421  0.2436  155 ARG A O   
1096 C CB  . ARG A 157 ? 1.1518 1.5280 2.3632 0.0604  0.0035  0.3522  155 ARG A CB  
1097 N N   . GLU A 158 ? 1.2485 1.6148 2.3398 0.0295  0.0070  0.2715  156 GLU A N   
1098 C CA  . GLU A 158 ? 1.2514 1.6313 2.3425 0.0134  -0.0051 0.2607  156 GLU A CA  
1099 C C   . GLU A 158 ? 1.3479 1.7070 2.2365 -0.0048 -0.0489 0.2238  156 GLU A C   
1100 O O   . GLU A 158 ? 1.3763 1.7303 2.1525 -0.0064 -0.0902 0.2291  156 GLU A O   
1101 C CB  . GLU A 158 ? 1.1596 1.6023 2.3950 0.0104  -0.0595 0.3418  156 GLU A CB  
1102 C CG  . GLU A 158 ? 1.1926 1.6705 2.3787 -0.0016 -0.1488 0.4091  156 GLU A CG  
1103 C CD  . GLU A 158 ? 1.0714 1.6155 2.4340 -0.0104 -0.2015 0.5062  156 GLU A CD  
1104 O OE1 . GLU A 158 ? 0.9335 1.4959 2.5023 0.0109  -0.1663 0.5451  156 GLU A OE1 
1105 O OE2 . GLU A 158 ? 1.1276 1.7048 2.4299 -0.0421 -0.2779 0.5457  156 GLU A OE2 
1106 N N   . VAL A 159 ? 1.3825 1.7288 2.2344 -0.0207 -0.0359 0.1855  157 VAL A N   
1107 C CA  . VAL A 159 ? 1.4283 1.7527 2.1171 -0.0382 -0.0744 0.1518  157 VAL A CA  
1108 C C   . VAL A 159 ? 1.4067 1.7685 2.1059 -0.0537 -0.1380 0.1898  157 VAL A C   
1109 O O   . VAL A 159 ? 1.3329 1.7167 2.1252 -0.0614 -0.1284 0.2009  157 VAL A O   
1110 C CB  . VAL A 159 ? 1.4823 1.7655 2.1143 -0.0545 -0.0255 0.0896  157 VAL A CB  
1111 C CG1 . VAL A 159 ? 1.5299 1.7875 2.0115 -0.0694 -0.0682 0.0615  157 VAL A CG1 
1112 C CG2 . VAL A 159 ? 1.5353 1.7841 2.1692 -0.0503 0.0418  0.0571  157 VAL A CG2 
1113 N N   . LEU A 160 ? 1.4021 1.7700 2.0033 -0.0641 -0.1994 0.2071  158 LEU A N   
1114 C CA  . LEU A 160 ? 1.3589 1.7605 1.9553 -0.0893 -0.2632 0.2459  158 LEU A CA  
1115 C C   . LEU A 160 ? 1.3468 1.7189 1.8311 -0.1079 -0.2794 0.2002  158 LEU A C   
1116 O O   . LEU A 160 ? 1.2725 1.6628 1.7986 -0.1228 -0.2947 0.2117  158 LEU A O   
1117 C CB  . LEU A 160 ? 1.3679 1.7904 1.9099 -0.1062 -0.3189 0.2883  158 LEU A CB  
1118 C CG  . LEU A 160 ? 1.3559 1.7876 1.9517 -0.0875 -0.3018 0.3162  158 LEU A CG  
1119 C CD1 . LEU A 160 ? 1.3770 1.8198 1.8721 -0.1159 -0.3544 0.3430  158 LEU A CD1 
1120 C CD2 . LEU A 160 ? 1.2836 1.7597 2.0816 -0.0745 -0.2921 0.3794  158 LEU A CD2 
1121 N N   . SER A 161 ? 1.4198 1.7471 1.7750 -0.1073 -0.2760 0.1514  159 SER A N   
1122 C CA  . SER A 161 ? 1.3821 1.6763 1.6433 -0.1236 -0.2925 0.1104  159 SER A CA  
1123 C C   . SER A 161 ? 1.4885 1.7365 1.7043 -0.1104 -0.2507 0.0590  159 SER A C   
1124 O O   . SER A 161 ? 1.5270 1.7707 1.7859 -0.0951 -0.2056 0.0533  159 SER A O   
1125 C CB  . SER A 161 ? 1.3791 1.6654 1.5369 -0.1463 -0.3390 0.1082  159 SER A CB  
1126 O OG  . SER A 161 ? 1.4529 1.7206 1.5504 -0.1361 -0.3258 0.0907  159 SER A OG  
1127 N N   . ASP A 162 ? 1.5096 1.7215 1.6426 -0.1212 -0.2669 0.0240  160 ASP A N   
1128 C CA  . ASP A 162 ? 1.5102 1.6812 1.6028 -0.1154 -0.2415 -0.0131 160 ASP A CA  
1129 C C   . ASP A 162 ? 1.5604 1.7119 1.5994 -0.0999 -0.2369 -0.0289 160 ASP A C   
1130 O O   . ASP A 162 ? 1.6199 1.7431 1.6380 -0.0938 -0.2174 -0.0510 160 ASP A O   
1131 C CB  . ASP A 162 ? 1.4738 1.6161 1.5289 -0.1351 -0.2639 -0.0353 160 ASP A CB  
1132 C CG  . ASP A 162 ? 1.4237 1.5580 1.4318 -0.1458 -0.3048 -0.0406 160 ASP A CG  
1133 O OD1 . ASP A 162 ? 1.4494 1.6010 1.4394 -0.1451 -0.3164 -0.0281 160 ASP A OD1 
1134 O OD2 . ASP A 162 ? 1.3728 1.4814 1.3587 -0.1614 -0.3251 -0.0572 160 ASP A OD2 
1135 N N   . ARG A 163 ? 1.5539 1.7225 1.5702 -0.1001 -0.2557 -0.0150 161 ARG A N   
1136 C CA  . ARG A 163 ? 1.5962 1.7481 1.5551 -0.0925 -0.2491 -0.0341 161 ARG A CA  
1137 C C   . ARG A 163 ? 1.6064 1.7918 1.5779 -0.0892 -0.2485 -0.0010 161 ARG A C   
1138 O O   . ARG A 163 ? 1.5900 1.7695 1.5044 -0.0936 -0.2484 -0.0124 161 ARG A O   
1139 C CB  . ARG A 163 ? 1.5562 1.6845 1.4470 -0.1129 -0.2726 -0.0620 161 ARG A CB  
1140 C CG  . ARG A 163 ? 1.5328 1.6886 1.4129 -0.1435 -0.3102 -0.0348 161 ARG A CG  
1141 C CD  . ARG A 163 ? 1.5222 1.6461 1.3391 -0.1711 -0.3295 -0.0681 161 ARG A CD  
1142 N NE  . ARG A 163 ? 1.4867 1.5804 1.3287 -0.1624 -0.3279 -0.0899 161 ARG A NE  
1143 C CZ  . ARG A 163 ? 1.5197 1.5769 1.3290 -0.1800 -0.3403 -0.1214 161 ARG A CZ  
1144 N NH1 . ARG A 163 ? 1.5521 1.5870 1.2947 -0.2051 -0.3409 -0.1510 161 ARG A NH1 
1145 N NH2 . ARG A 163 ? 1.5147 1.5528 1.3579 -0.1767 -0.3481 -0.1266 161 ARG A NH2 
1146 N N   . GLU A 164 ? 1.6129 1.8333 1.6667 -0.0841 -0.2461 0.0406  162 GLU A N   
1147 C CA  . GLU A 164 ? 1.5556 1.8110 1.6442 -0.0833 -0.2533 0.0845  162 GLU A CA  
1148 C C   . GLU A 164 ? 1.5428 1.8182 1.7514 -0.0632 -0.2234 0.1132  162 GLU A C   
1149 O O   . GLU A 164 ? 1.5215 1.8032 1.7953 -0.0640 -0.2141 0.1160  162 GLU A O   
1150 C CB  . GLU A 164 ? 1.5297 1.8191 1.6038 -0.1183 -0.3061 0.1251  162 GLU A CB  
1151 C CG  . GLU A 164 ? 1.5404 1.8081 1.4882 -0.1499 -0.3269 0.0935  162 GLU A CG  
1152 C CD  . GLU A 164 ? 1.5143 1.7958 1.4323 -0.1926 -0.3732 0.1105  162 GLU A CD  
1153 O OE1 . GLU A 164 ? 1.4927 1.7668 1.4418 -0.1884 -0.3769 0.1013  162 GLU A OE1 
1154 O OE2 . GLU A 164 ? 1.5435 1.8436 1.4003 -0.2374 -0.4071 0.1346  162 GLU A OE2 
1155 N N   . LEU A 165 ? 1.5283 1.8114 1.7694 -0.0479 -0.2037 0.1314  163 LEU A N   
1156 C CA  . LEU A 165 ? 1.5048 1.7996 1.8695 -0.0292 -0.1649 0.1530  163 LEU A CA  
1157 C C   . LEU A 165 ? 1.4657 1.7939 1.8937 -0.0258 -0.1817 0.2099  163 LEU A C   
1158 O O   . LEU A 165 ? 1.4732 1.8119 1.8263 -0.0415 -0.2189 0.2262  163 LEU A O   
1159 C CB  . LEU A 165 ? 1.5304 1.7838 1.8759 -0.0149 -0.1062 0.1053  163 LEU A CB  
1160 C CG  . LEU A 165 ? 1.5820 1.8064 1.8274 -0.0087 -0.0977 0.0752  163 LEU A CG  
1161 C CD1 . LEU A 165 ? 1.5322 1.7749 1.7874 -0.0001 -0.1053 0.1075  163 LEU A CD1 
1162 C CD2 . LEU A 165 ? 1.6137 1.8014 1.8489 -0.0074 -0.0468 0.0368  163 LEU A CD2 
1163 N N   . HIS A 166 ? 1.4171 1.7612 1.9903 -0.0099 -0.1515 0.2403  164 HIS A N   
1164 C CA  . HIS A 166 ? 1.3799 1.7502 2.0432 -0.0022 -0.1590 0.2967  164 HIS A CA  
1165 C C   . HIS A 166 ? 1.3669 1.7002 2.0478 0.0218  -0.0921 0.2616  164 HIS A C   
1166 O O   . HIS A 166 ? 1.3671 1.6720 2.0855 0.0300  -0.0328 0.2194  164 HIS A O   
1167 C CB  . HIS A 166 ? 1.3015 1.7182 2.1483 -0.0022 -0.1748 0.3650  164 HIS A CB  
1168 C CG  . HIS A 166 ? 1.2666 1.7340 2.1111 -0.0347 -0.2596 0.4381  164 HIS A CG  
1169 N ND1 . HIS A 166 ? 1.2466 1.7619 2.2272 -0.0468 -0.2951 0.5021  164 HIS A ND1 
1170 C CD2 . HIS A 166 ? 1.2652 1.7434 1.9826 -0.0666 -0.3153 0.4574  164 HIS A CD2 
1171 C CE1 . HIS A 166 ? 1.2212 1.7751 2.1522 -0.0887 -0.3756 0.5632  164 HIS A CE1 
1172 N NE2 . HIS A 166 ? 1.2759 1.8062 2.0412 -0.1040 -0.3861 0.5336  164 HIS A NE2 
1173 N N   . LEU A 167 ? 1.3534 1.6858 1.9982 0.0253  -0.1007 0.2777  165 LEU A N   
1174 C CA  . LEU A 167 ? 1.3709 1.6652 2.0041 0.0425  -0.0430 0.2421  165 LEU A CA  
1175 C C   . LEU A 167 ? 1.2910 1.5999 2.0587 0.0560  -0.0304 0.2935  165 LEU A C   
1176 O O   . LEU A 167 ? 1.2371 1.5882 2.0591 0.0473  -0.0848 0.3630  165 LEU A O   
1177 C CB  . LEU A 167 ? 1.4300 1.7036 1.8983 0.0365  -0.0559 0.2071  165 LEU A CB  
1178 C CG  . LEU A 167 ? 1.4556 1.6819 1.8554 0.0435  -0.0031 0.1471  165 LEU A CG  
1179 C CD1 . LEU A 167 ? 1.4848 1.6876 1.8936 0.0366  0.0298  0.1068  165 LEU A CD1 
1180 C CD2 . LEU A 167 ? 1.4833 1.6998 1.7434 0.0371  -0.0263 0.1207  165 LEU A CD2 
1181 N N   . SER A 168 ? 1.3014 1.5731 2.1224 0.0709  0.0412  0.2605  166 SER A N   
1182 C CA  . SER A 168 ? 1.2777 1.5486 2.2273 0.0858  0.0680  0.2965  166 SER A CA  
1183 C C   . SER A 168 ? 1.2974 1.5239 2.1482 0.0883  0.1091  0.2512  166 SER A C   
1184 O O   . SER A 168 ? 1.3297 1.5153 2.0996 0.0806  0.1566  0.1857  166 SER A O   
1185 C CB  . SER A 168 ? 1.2004 1.4645 2.3450 0.0976  0.1299  0.2982  166 SER A CB  
1186 O OG  . SER A 168 ? 1.2338 1.4572 2.3311 0.0878  0.1950  0.2220  166 SER A OG  
1187 N N   . TRP A 169 ? 1.2800 1.5168 2.1362 0.0930  0.0868  0.2908  167 TRP A N   
1188 C CA  . TRP A 169 ? 1.3269 1.5289 2.0814 0.0932  0.1147  0.2560  167 TRP A CA  
1189 C C   . TRP A 169 ? 1.2833 1.4569 2.1590 0.1051  0.1731  0.2625  167 TRP A C   
1190 O O   . TRP A 169 ? 1.1901 1.3836 2.2362 0.1165  0.1699  0.3180  167 TRP A O   
1191 C CB  . TRP A 169 ? 1.3807 1.6105 2.0225 0.0835  0.0514  0.2849  167 TRP A CB  
1192 C CG  . TRP A 169 ? 1.3978 1.6376 1.8984 0.0691  0.0144  0.2556  167 TRP A CG  
1193 C CD1 . TRP A 169 ? 1.3764 1.6533 1.8614 0.0534  -0.0426 0.2846  167 TRP A CD1 
1194 C CD2 . TRP A 169 ? 1.4563 1.6661 1.8226 0.0660  0.0334  0.1931  167 TRP A CD2 
1195 N NE1 . TRP A 169 ? 1.4497 1.7162 1.7988 0.0430  -0.0536 0.2368  167 TRP A NE1 
1196 C CE2 . TRP A 169 ? 1.5047 1.7323 1.7899 0.0530  -0.0092 0.1836  167 TRP A CE2 
1197 C CE3 . TRP A 169 ? 1.4684 1.6387 1.7818 0.0686  0.0800  0.1487  167 TRP A CE3 
1198 C CZ2 . TRP A 169 ? 1.5211 1.7275 1.6946 0.0489  -0.0041 0.1321  167 TRP A CZ2 
1199 C CZ3 . TRP A 169 ? 1.4865 1.6419 1.6858 0.0611  0.0770  0.1054  167 TRP A CZ3 
1200 C CH2 . TRP A 169 ? 1.5141 1.6873 1.6544 0.0545  0.0365  0.0977  167 TRP A CH2 
1201 N N   . GLU A 170 ? 1.3084 1.4345 2.1000 0.0989  0.2256  0.2074  168 GLU A N   
1202 C CA  . GLU A 170 ? 1.2849 1.3707 2.1624 0.1026  0.2922  0.1972  168 GLU A CA  
1203 C C   . GLU A 170 ? 1.2736 1.3802 2.2036 0.1147  0.2564  0.2602  168 GLU A C   
1204 O O   . GLU A 170 ? 1.2698 1.4089 2.0982 0.1103  0.1916  0.2894  168 GLU A O   
1205 C CB  . GLU A 170 ? 1.3170 1.3506 2.0583 0.0805  0.3440  0.1271  168 GLU A CB  
1206 C CG  . GLU A 170 ? 1.3595 1.3525 2.1203 0.0768  0.3940  0.1181  168 GLU A CG  
1207 C CD  . GLU A 170 ? 1.3827 1.3221 2.0197 0.0415  0.4502  0.0494  168 GLU A CD  
1208 O OE1 . GLU A 170 ? 1.3145 1.2474 1.8740 0.0190  0.4551  0.0114  168 GLU A OE1 
1209 O OE2 . GLU A 170 ? 1.3684 1.2732 1.9833 0.0306  0.4851  0.0379  168 GLU A OE2 
1210 N N   . VAL A 171 ? 1.2582 1.3436 2.3535 0.1258  0.3034  0.2797  169 VAL A N   
1211 C CA  . VAL A 171 ? 1.2179 1.3177 2.3891 0.1349  0.2742  0.3444  169 VAL A CA  
1212 C C   . VAL A 171 ? 1.2893 1.3420 2.3590 0.1265  0.3159  0.3033  169 VAL A C   
1213 O O   . VAL A 171 ? 1.3232 1.3203 2.3575 0.1148  0.3932  0.2331  169 VAL A O   
1214 C CB  . VAL A 171 ? 1.0724 1.1734 2.5046 0.1530  0.3016  0.3941  169 VAL A CB  
1215 C CG1 . VAL A 171 ? 1.0553 1.1734 2.5748 0.1586  0.2615  0.4722  169 VAL A CG1 
1216 C CG2 . VAL A 171 ? 0.9930 1.1442 2.5337 0.1582  0.2597  0.4379  169 VAL A CG2 
1217 N N   . GLY A 172 ? 1.3093 1.3850 2.3255 0.1248  0.2639  0.3486  170 GLY A N   
1218 C CA  . GLY A 172 ? 1.3001 1.3391 2.2308 0.1168  0.2938  0.3226  170 GLY A CA  
1219 C C   . GLY A 172 ? 1.3959 1.4489 2.1139 0.1023  0.2586  0.2954  170 GLY A C   
1220 O O   . GLY A 172 ? 1.3869 1.4378 2.0394 0.0960  0.2483  0.3061  170 GLY A O   
1221 N N   . LYS A 173 ? 1.4334 1.5004 2.0543 0.0967  0.2421  0.2612  171 LYS A N   
1222 C CA  . LYS A 173 ? 1.4541 1.5308 1.8997 0.0850  0.2174  0.2311  171 LYS A CA  
1223 C C   . LYS A 173 ? 1.4530 1.5850 1.8461 0.0825  0.1459  0.2612  171 LYS A C   
1224 O O   . LYS A 173 ? 1.4263 1.5837 1.8939 0.0855  0.1189  0.2898  171 LYS A O   
1225 C CB  . LYS A 173 ? 1.3996 1.4416 1.7691 0.0730  0.2582  0.1640  171 LYS A CB  
1226 C CG  . LYS A 173 ? 1.3618 1.3444 1.7362 0.0562  0.3314  0.1235  171 LYS A CG  
1227 C CD  . LYS A 173 ? 1.3800 1.3479 1.6288 0.0387  0.3345  0.1039  171 LYS A CD  
1228 C CE  . LYS A 173 ? 1.3722 1.3632 1.6170 0.0500  0.3041  0.1463  171 LYS A CE  
1229 N NZ  . LYS A 173 ? 1.3784 1.3632 1.5025 0.0336  0.3034  0.1279  171 LYS A NZ  
1230 N N   . PRO A 174 ? 1.4523 1.6029 1.7196 0.0721  0.1179  0.2536  172 PRO A N   
1231 C CA  . PRO A 174 ? 1.4703 1.6645 1.6704 0.0599  0.0630  0.2663  172 PRO A CA  
1232 C C   . PRO A 174 ? 1.4596 1.6486 1.6299 0.0625  0.0649  0.2255  172 PRO A C   
1233 O O   . PRO A 174 ? 1.4239 1.5781 1.5906 0.0691  0.1051  0.1821  172 PRO A O   
1234 C CB  . PRO A 174 ? 1.4786 1.6819 1.5587 0.0478  0.0567  0.2499  172 PRO A CB  
1235 C CG  . PRO A 174 ? 1.4830 1.6444 1.5477 0.0573  0.1077  0.2124  172 PRO A CG  
1236 C CD  . PRO A 174 ? 1.4458 1.5781 1.6303 0.0668  0.1397  0.2310  172 PRO A CD  
1237 N N   . ARG A 175 ? 1.4724 1.6962 1.6144 0.0493  0.0183  0.2418  173 ARG A N   
1238 C CA  . ARG A 175 ? 1.4491 1.6693 1.5662 0.0500  0.0145  0.2076  173 ARG A CA  
1239 C C   . ARG A 175 ? 1.4809 1.7017 1.4757 0.0406  0.0090  0.1640  173 ARG A C   
1240 O O   . ARG A 175 ? 1.5084 1.7531 1.4391 0.0215  -0.0138 0.1740  173 ARG A O   
1241 C CB  . ARG A 175 ? 1.4230 1.6772 1.5949 0.0379  -0.0307 0.2516  173 ARG A CB  
1242 C CG  . ARG A 175 ? 1.4414 1.7022 1.7688 0.0483  -0.0287 0.3049  173 ARG A CG  
1243 C CD  . ARG A 175 ? 1.4428 1.7450 1.8295 0.0313  -0.0829 0.3580  173 ARG A CD  
1244 N NE  . ARG A 175 ? 1.3786 1.6893 1.9467 0.0451  -0.0780 0.4107  173 ARG A NE  
1245 C CZ  . ARG A 175 ? 1.3400 1.6883 2.0039 0.0337  -0.1220 0.4678  173 ARG A CZ  
1246 N NH1 . ARG A 175 ? 1.3724 1.7565 1.9534 -0.0014 -0.1839 0.4906  173 ARG A NH1 
1247 N NH2 . ARG A 175 ? 1.2397 1.5904 2.0944 0.0531  -0.1028 0.5065  173 ARG A NH2 
1248 N N   . PRO A 176 ? 1.4504 1.6457 1.4174 0.0489  0.0307  0.1168  174 PRO A N   
1249 C CA  . PRO A 176 ? 1.4585 1.6536 1.3407 0.0430  0.0272  0.0776  174 PRO A CA  
1250 C C   . PRO A 176 ? 1.5113 1.7260 1.3616 0.0265  -0.0055 0.0743  174 PRO A C   
1251 O O   . PRO A 176 ? 1.5121 1.7311 1.4046 0.0249  -0.0230 0.0884  174 PRO A O   
1252 C CB  . PRO A 176 ? 1.5095 1.6721 1.3976 0.0522  0.0523  0.0433  174 PRO A CB  
1253 C CG  . PRO A 176 ? 1.5558 1.7058 1.5143 0.0550  0.0630  0.0560  174 PRO A CG  
1254 C CD  . PRO A 176 ? 1.4854 1.6497 1.5038 0.0583  0.0623  0.0985  174 PRO A CD  
1255 N N   . PRO A 177 ? 1.5509 1.7765 1.3265 0.0091  -0.0101 0.0530  175 PRO A N   
1256 C CA  . PRO A 177 ? 1.5711 1.8071 1.3008 -0.0163 -0.0331 0.0386  175 PRO A CA  
1257 C C   . PRO A 177 ? 1.5784 1.7930 1.3299 -0.0044 -0.0334 0.0103  175 PRO A C   
1258 O O   . PRO A 177 ? 1.5951 1.7860 1.3806 0.0192  -0.0131 -0.0074 175 PRO A O   
1259 C CB  . PRO A 177 ? 1.5524 1.7899 1.2050 -0.0342 -0.0135 0.0000  175 PRO A CB  
1260 C CG  . PRO A 177 ? 1.5309 1.7575 1.2031 -0.0084 0.0180  -0.0082 175 PRO A CG  
1261 C CD  . PRO A 177 ? 1.5269 1.7545 1.2575 0.0070  0.0115  0.0377  175 PRO A CD  
1262 N N   . LEU A 178 ? 1.6037 1.8270 1.3306 -0.0281 -0.0596 0.0091  176 LEU A N   
1263 C CA  . LEU A 178 ? 1.6454 1.8504 1.3916 -0.0215 -0.0656 -0.0132 176 LEU A CA  
1264 C C   . LEU A 178 ? 1.6320 1.8184 1.3218 -0.0348 -0.0535 -0.0673 176 LEU A C   
1265 O O   . LEU A 178 ? 1.6503 1.8388 1.2974 -0.0651 -0.0708 -0.0784 176 LEU A O   
1266 C CB  . LEU A 178 ? 1.6552 1.8817 1.4296 -0.0385 -0.1035 0.0270  176 LEU A CB  
1267 C CG  . LEU A 178 ? 1.6255 1.8693 1.4894 -0.0235 -0.1098 0.0807  176 LEU A CG  
1268 C CD1 . LEU A 178 ? 1.6101 1.8760 1.5253 -0.0375 -0.1456 0.1186  176 LEU A CD1 
1269 C CD2 . LEU A 178 ? 1.6181 1.8342 1.5340 0.0097  -0.0717 0.0626  176 LEU A CD2 
1270 N N   . ASN A 179 ? 1.6056 1.7724 1.3037 -0.0150 -0.0218 -0.1005 177 ASN A N   
1271 C CA  . ASN A 179 ? 1.6033 1.7471 1.2871 -0.0190 -0.0015 -0.1532 177 ASN A CA  
1272 C C   . ASN A 179 ? 1.6232 1.7430 1.3750 0.0109  0.0058  -0.1624 177 ASN A C   
1273 O O   . ASN A 179 ? 1.6054 1.7265 1.3925 0.0274  0.0025  -0.1341 177 ASN A O   
1274 C CB  . ASN A 179 ? 1.5560 1.7043 1.1981 -0.0327 0.0319  -0.1829 177 ASN A CB  
1275 C CG  . ASN A 179 ? 1.5759 1.7378 1.2374 -0.0132 0.0454  -0.1593 177 ASN A CG  
1276 O OD1 . ASN A 179 ? 1.5721 1.7359 1.2742 0.0079  0.0328  -0.1236 177 ASN A OD1 
1277 N ND2 . ASN A 179 ? 1.5295 1.6989 1.1594 -0.0250 0.0758  -0.1828 177 ASN A ND2 
1278 N N   . ARG A 180 ? 1.6256 1.7213 1.3971 0.0112  0.0159  -0.2011 178 ARG A N   
1279 C CA  . ARG A 180 ? 1.5828 1.6587 1.4268 0.0318  0.0135  -0.1997 178 ARG A CA  
1280 C C   . ARG A 180 ? 1.5853 1.6663 1.4648 0.0473  0.0334  -0.1912 178 ARG A C   
1281 O O   . ARG A 180 ? 1.5867 1.6603 1.5162 0.0553  0.0221  -0.1692 178 ARG A O   
1282 C CB  . ARG A 180 ? 1.5710 1.6190 1.4488 0.0292  0.0189  -0.2384 178 ARG A CB  
1283 N N   . ASN A 181 ? 1.5786 1.6738 1.4280 0.0442  0.0607  -0.2055 179 ASN A N   
1284 C CA  . ASN A 181 ? 1.5474 1.6526 1.4265 0.0569  0.0785  -0.1932 179 ASN A CA  
1285 C C   . ASN A 181 ? 1.5326 1.6456 1.4050 0.0603  0.0606  -0.1479 179 ASN A C   
1286 O O   . ASN A 181 ? 1.5447 1.6574 1.4523 0.0658  0.0633  -0.1294 179 ASN A O   
1287 C CB  . ASN A 181 ? 1.5552 1.6776 1.3872 0.0460  0.1105  -0.2155 179 ASN A CB  
1288 C CG  . ASN A 181 ? 1.5932 1.7028 1.4141 0.0296  0.1398  -0.2712 179 ASN A CG  
1289 O OD1 . ASN A 181 ? 1.5936 1.6927 1.3738 0.0106  0.1274  -0.2861 179 ASN A OD1 
1290 N ND2 . ASN A 181 ? 1.4985 1.6077 1.3581 0.0328  0.1832  -0.3044 179 ASN A ND2 
1291 N N   . TYR A 182 ? 1.5237 1.6429 1.3575 0.0528  0.0445  -0.1294 180 TYR A N   
1292 C CA  . TYR A 182 ? 1.5438 1.6648 1.3793 0.0532  0.0388  -0.0947 180 TYR A CA  
1293 C C   . TYR A 182 ? 1.5321 1.6362 1.3926 0.0478  0.0211  -0.0880 180 TYR A C   
1294 O O   . TYR A 182 ? 1.5478 1.6553 1.4031 0.0435  0.0088  -0.0821 180 TYR A O   
1295 C CB  . TYR A 182 ? 1.4877 1.6284 1.2911 0.0482  0.0366  -0.0751 180 TYR A CB  
1296 C CG  . TYR A 182 ? 1.4704 1.6258 1.2527 0.0489  0.0534  -0.0647 180 TYR A CG  
1297 C CD1 . TYR A 182 ? 1.4678 1.6358 1.2170 0.0419  0.0664  -0.0871 180 TYR A CD1 
1298 C CD2 . TYR A 182 ? 1.4342 1.5887 1.2290 0.0521  0.0611  -0.0360 180 TYR A CD2 
1299 C CE1 . TYR A 182 ? 1.4250 1.6088 1.1516 0.0387  0.0814  -0.0769 180 TYR A CE1 
1300 C CE2 . TYR A 182 ? 1.4152 1.5823 1.1906 0.0513  0.0741  -0.0244 180 TYR A CE2 
1301 C CZ  . TYR A 182 ? 1.4164 1.6004 1.1560 0.0448  0.0815  -0.0426 180 TYR A CZ  
1302 O OH  . TYR A 182 ? 1.3406 1.5394 1.0578 0.0405  0.0941  -0.0304 180 TYR A OH  
1303 N N   . VAL A 183 ? 1.4924 1.5811 1.3829 0.0427  0.0173  -0.0846 181 VAL A N   
1304 C CA  . VAL A 183 ? 1.5550 1.6275 1.4611 0.0272  -0.0002 -0.0774 181 VAL A CA  
1305 C C   . VAL A 183 ? 1.5535 1.6202 1.4456 0.0105  0.0131  -0.0592 181 VAL A C   
1306 O O   . VAL A 183 ? 1.5285 1.5967 1.4083 0.0086  0.0325  -0.0492 181 VAL A O   
1307 C CB  . VAL A 183 ? 1.5450 1.6049 1.4924 0.0179  -0.0171 -0.0736 181 VAL A CB  
1308 C CG1 . VAL A 183 ? 1.5298 1.5744 1.4840 -0.0073 -0.0399 -0.0634 181 VAL A CG1 
1309 C CG2 . VAL A 183 ? 1.4967 1.5570 1.4788 0.0367  -0.0168 -0.0988 181 VAL A CG2 
1310 N N   . PHE A 184 ? 1.5720 1.6297 1.4684 -0.0049 0.0078  -0.0585 182 PHE A N   
1311 C CA  . PHE A 184 ? 1.5569 1.6043 1.4491 -0.0251 0.0330  -0.0517 182 PHE A CA  
1312 C C   . PHE A 184 ? 1.5539 1.5815 1.4379 -0.0655 0.0270  -0.0516 182 PHE A C   
1313 O O   . PHE A 184 ? 1.5724 1.5986 1.4655 -0.0708 -0.0022 -0.0535 182 PHE A O   
1314 C CB  . PHE A 184 ? 1.5560 1.6156 1.4736 -0.0111 0.0425  -0.0504 182 PHE A CB  
1315 C CG  . PHE A 184 ? 1.5391 1.6168 1.4653 0.0122  0.0520  -0.0382 182 PHE A CG  
1316 C CD1 . PHE A 184 ? 1.5206 1.5908 1.4610 0.0094  0.0850  -0.0292 182 PHE A CD1 
1317 C CD2 . PHE A 184 ? 1.5512 1.6515 1.4685 0.0295  0.0284  -0.0355 182 PHE A CD2 
1318 C CE1 . PHE A 184 ? 1.5155 1.6033 1.4706 0.0281  0.0878  -0.0109 182 PHE A CE1 
1319 C CE2 . PHE A 184 ? 1.5527 1.6725 1.4709 0.0400  0.0307  -0.0178 182 PHE A CE2 
1320 C CZ  . PHE A 184 ? 1.5302 1.6453 1.4723 0.0417  0.0573  -0.0019 182 PHE A CZ  
1321 N N   . THR A 185 ? 1.5341 1.5441 1.3963 -0.1007 0.0561  -0.0501 183 THR A N   
1322 C CA  . THR A 185 ? 1.5038 1.4936 1.3410 -0.1561 0.0578  -0.0516 183 THR A CA  
1323 C C   . THR A 185 ? 1.4793 1.4618 1.3330 -0.1655 0.0971  -0.0702 183 THR A C   
1324 O O   . THR A 185 ? 1.4549 1.4331 1.3283 -0.1548 0.1401  -0.0780 183 THR A O   
1325 C CB  . THR A 185 ? 1.4617 1.4332 1.2525 -0.2065 0.0683  -0.0407 183 THR A CB  
1326 O OG1 . THR A 185 ? 1.4165 1.4014 1.2166 -0.1882 0.0364  -0.0192 183 THR A OG1 
1327 C CG2 . THR A 185 ? 1.4400 1.3938 1.1913 -0.2784 0.0563  -0.0352 183 THR A CG2 
1328 N N   . GLY A 186 ? 1.5263 1.5078 1.3840 -0.1857 0.0838  -0.0758 184 GLY A N   
1329 C CA  . GLY A 186 ? 1.4847 1.4642 1.3753 -0.1934 0.1212  -0.0933 184 GLY A CA  
1330 C C   . GLY A 186 ? 1.4893 1.4400 1.3384 -0.2663 0.1623  -0.1120 184 GLY A C   
1331 O O   . GLY A 186 ? 1.5181 1.4564 1.3064 -0.3196 0.1374  -0.1037 184 GLY A O   
1332 N N   . TYR A 187 ? 1.4651 1.4051 1.3533 -0.2736 0.2266  -0.1359 185 TYR A N   
1333 C CA  . TYR A 187 ? 1.4323 1.3404 1.2817 -0.3500 0.2839  -0.1665 185 TYR A CA  
1334 C C   . TYR A 187 ? 1.3686 1.2807 1.2978 -0.3454 0.3340  -0.1910 185 TYR A C   
1335 O O   . TYR A 187 ? 1.3642 1.2899 1.3921 -0.2913 0.3595  -0.1890 185 TYR A O   
1336 C CB  . TYR A 187 ? 1.3667 1.2431 1.1823 -0.3812 0.3383  -0.1826 185 TYR A CB  
1337 C CG  . TYR A 187 ? 1.4683 1.3440 1.2169 -0.3871 0.2932  -0.1550 185 TYR A CG  
1338 C CD1 . TYR A 187 ? 1.4792 1.3391 1.1331 -0.4655 0.2693  -0.1447 185 TYR A CD1 
1339 C CD2 . TYR A 187 ? 1.4391 1.3322 1.2233 -0.3208 0.2740  -0.1350 185 TYR A CD2 
1340 C CE1 . TYR A 187 ? 1.4188 1.2828 1.0313 -0.4717 0.2261  -0.1123 185 TYR A CE1 
1341 C CE2 . TYR A 187 ? 1.4340 1.3292 1.1689 -0.3261 0.2379  -0.1107 185 TYR A CE2 
1342 C CZ  . TYR A 187 ? 1.3946 1.2763 1.0516 -0.3989 0.2140  -0.0981 185 TYR A CZ  
1343 O OH  . TYR A 187 ? 1.2569 1.1454 0.8838 -0.4049 0.1755  -0.0667 185 TYR A OH  
1344 N N   . GLN A 196 ? 1.3302 1.6677 0.9036 -0.7500 -0.2459 0.1883  194 GLN A N   
1345 C CA  . GLN A 196 ? 1.4979 1.5850 1.0461 -0.6901 -0.3042 0.2001  194 GLN A CA  
1346 C C   . GLN A 196 ? 1.6599 1.6546 1.1531 -0.7632 -0.3820 0.2124  194 GLN A C   
1347 O O   . GLN A 196 ? 1.7545 1.6148 1.1916 -0.8595 -0.4661 0.2658  194 GLN A O   
1348 C CB  . GLN A 196 ? 1.5074 1.4440 1.0331 -0.7122 -0.3475 0.2477  194 GLN A CB  
1349 C CG  . GLN A 196 ? 1.4795 1.5412 1.0511 -0.6875 -0.2808 0.2482  194 GLN A CG  
1350 C CD  . GLN A 196 ? 1.5061 1.4068 1.0507 -0.7080 -0.3316 0.2925  194 GLN A CD  
1351 O OE1 . GLN A 196 ? 1.6465 1.3288 1.1442 -0.7354 -0.4231 0.3197  194 GLN A OE1 
1352 N NE2 . GLN A 196 ? 1.3746 1.3833 0.9578 -0.6935 -0.2804 0.2946  194 GLN A NE2 
1353 N N   . ILE A 197 ? 1.5776 1.6393 1.0904 -0.7158 -0.3606 0.1632  195 ILE A N   
1354 C CA  . ILE A 197 ? 1.6484 1.6489 1.1242 -0.7804 -0.4296 0.1659  195 ILE A CA  
1355 C C   . ILE A 197 ? 1.7872 1.5662 1.2631 -0.7173 -0.4987 0.1579  195 ILE A C   
1356 O O   . ILE A 197 ? 1.8338 1.5518 1.2967 -0.7535 -0.5628 0.1523  195 ILE A O   
1357 C CB  . ILE A 197 ? 1.7076 1.8704 1.2080 -0.7562 -0.3867 0.1085  195 ILE A CB  
1358 C CG1 . ILE A 197 ? 1.6557 1.7870 1.1910 -0.5978 -0.3487 0.0526  195 ILE A CG1 
1359 C CG2 . ILE A 197 ? 1.5855 1.9856 1.1137 -0.8092 -0.3208 0.0935  195 ILE A CG2 
1360 C CD1 . ILE A 197 ? 1.5953 1.8817 1.1544 -0.5626 -0.3101 -0.0044 195 ILE A CD1 
1361 N N   . GLY A 198 ? 1.7621 1.4288 1.2649 -0.6239 -0.4885 0.1472  196 GLY A N   
1362 C CA  . GLY A 198 ? 1.8666 1.3332 1.3864 -0.5678 -0.5564 0.1238  196 GLY A CA  
1363 C C   . GLY A 198 ? 1.8493 1.3244 1.4058 -0.4251 -0.4979 0.0515  196 GLY A C   
1364 O O   . GLY A 198 ? 1.7939 1.4143 1.3527 -0.3751 -0.4206 0.0258  196 GLY A O   
1365 N N   . GLU A 199 ? 1.9311 1.2450 1.5176 -0.3646 -0.5427 0.0146  197 GLU A N   
1366 C CA  . GLU A 199 ? 1.9138 1.2271 1.5254 -0.2408 -0.4900 -0.0570 197 GLU A CA  
1367 C C   . GLU A 199 ? 1.9859 1.3623 1.5783 -0.2339 -0.5001 -0.0887 197 GLU A C   
1368 O O   . GLU A 199 ? 2.0144 1.3759 1.5965 -0.3156 -0.5748 -0.0699 197 GLU A O   
1369 C CB  . GLU A 199 ? 1.8796 1.0190 1.5395 -0.1895 -0.5410 -0.1055 197 GLU A CB  
1370 C CG  . GLU A 199 ? 1.8209 0.9081 1.5109 -0.1509 -0.5032 -0.1013 197 GLU A CG  
1371 C CD  . GLU A 199 ? 1.7918 0.7459 1.5466 -0.0777 -0.5287 -0.1748 197 GLU A CD  
1372 O OE1 . GLU A 199 ? 1.7259 0.6784 1.5115 -0.0549 -0.5598 -0.2203 197 GLU A OE1 
1373 O OE2 . GLU A 199 ? 1.8046 0.7780 1.6071 -0.0341 -0.4752 -0.1710 197 GLU A OE2 
1374 N N   . TYR A 200 ? 1.9563 1.3989 1.5420 -0.1369 -0.4273 -0.1362 198 TYR A N   
1375 C CA  . TYR A 200 ? 1.9942 1.5055 1.5544 -0.1196 -0.4302 -0.1688 198 TYR A CA  
1376 C C   . TYR A 200 ? 1.9878 1.4795 1.5413 -0.0103 -0.3880 -0.2344 198 TYR A C   
1377 O O   . TYR A 200 ? 1.9450 1.4292 1.5027 0.0542  -0.3211 -0.2448 198 TYR A O   
1378 C CB  . TYR A 200 ? 1.9606 1.6388 1.4942 -0.1412 -0.3763 -0.1441 198 TYR A CB  
1379 C CG  . TYR A 200 ? 1.9349 1.6700 1.4631 -0.2576 -0.4263 -0.1088 198 TYR A CG  
1380 C CD1 . TYR A 200 ? 1.8880 1.6440 1.4195 -0.3497 -0.4336 -0.0524 198 TYR A CD1 
1381 C CD2 . TYR A 200 ? 1.9722 1.7498 1.4897 -0.2785 -0.4617 -0.1350 198 TYR A CD2 
1382 C CE1 . TYR A 200 ? 1.8752 1.6942 1.3929 -0.4694 -0.4725 -0.0211 198 TYR A CE1 
1383 C CE2 . TYR A 200 ? 1.9624 1.7987 1.4784 -0.3909 -0.5012 -0.1079 198 TYR A CE2 
1384 C CZ  . TYR A 200 ? 1.9358 1.7948 1.4484 -0.4908 -0.5044 -0.0501 198 TYR A CZ  
1385 O OH  . TYR A 200 ? 1.9528 1.8792 1.4553 -0.6159 -0.5380 -0.0240 198 TYR A OH  
1386 N N   . THR A 201 ? 2.0351 1.5239 1.5781 0.0059  -0.4272 -0.2802 199 THR A N   
1387 C CA  . THR A 201 ? 2.0530 1.5476 1.5714 0.0972  -0.3882 -0.3446 199 THR A CA  
1388 C C   . THR A 201 ? 2.0505 1.6437 1.5187 0.1095  -0.3826 -0.3558 199 THR A C   
1389 O O   . THR A 201 ? 2.0319 1.6586 1.5089 0.0473  -0.4344 -0.3379 199 THR A O   
1390 C CB  . THR A 201 ? 2.0325 1.4194 1.6016 0.1157  -0.4520 -0.4142 199 THR A CB  
1391 O OG1 . THR A 201 ? 2.0144 1.3651 1.6227 0.0506  -0.5565 -0.4143 199 THR A OG1 
1392 C CG2 . THR A 201 ? 1.9938 1.2782 1.6173 0.1199  -0.4541 -0.4203 199 THR A CG2 
1393 N N   . PHE A 202 ? 2.0628 1.6984 1.4757 0.1868  -0.3224 -0.3865 200 PHE A N   
1394 C CA  . PHE A 202 ? 2.0580 1.7801 1.4146 0.2081  -0.3171 -0.3969 200 PHE A CA  
1395 C C   . PHE A 202 ? 2.0340 1.7410 1.3434 0.2742  -0.3144 -0.4628 200 PHE A C   
1396 O O   . PHE A 202 ? 2.0578 1.7234 1.3548 0.3178  -0.2742 -0.4923 200 PHE A O   
1397 C CB  . PHE A 202 ? 2.0374 1.8463 1.3589 0.2289  -0.2502 -0.3554 200 PHE A CB  
1398 C CG  . PHE A 202 ? 1.9691 1.8271 1.3419 0.1618  -0.2499 -0.3031 200 PHE A CG  
1399 C CD1 . PHE A 202 ? 1.9416 1.8776 1.3304 0.1009  -0.2871 -0.2955 200 PHE A CD1 
1400 C CD2 . PHE A 202 ? 1.9703 1.8042 1.3780 0.1569  -0.2111 -0.2689 200 PHE A CD2 
1401 C CE1 . PHE A 202 ? 1.9320 1.9325 1.3647 0.0291  -0.2821 -0.2554 200 PHE A CE1 
1402 C CE2 . PHE A 202 ? 1.9232 1.8159 1.3746 0.0921  -0.2101 -0.2251 200 PHE A CE2 
1403 C CZ  . PHE A 202 ? 1.9217 1.9033 1.3826 0.0243  -0.2441 -0.2187 200 PHE A CZ  
1404 N N   . GLU A 203 ? 2.0378 1.7866 1.3224 0.2787  -0.3557 -0.4917 201 GLU A N   
1405 C CA  . GLU A 203 ? 2.0567 1.8109 1.2875 0.3381  -0.3576 -0.5565 201 GLU A CA  
1406 C C   . GLU A 203 ? 2.0172 1.8443 1.1633 0.3703  -0.3439 -0.5507 201 GLU A C   
1407 O O   . GLU A 203 ? 1.9541 1.8248 1.1216 0.3392  -0.3841 -0.5401 201 GLU A O   
1408 C CB  . GLU A 203 ? 2.0563 1.7780 1.3566 0.3211  -0.4426 -0.6171 201 GLU A CB  
1409 C CG  . GLU A 203 ? 2.0897 1.7297 1.4709 0.3115  -0.4669 -0.6529 201 GLU A CG  
1410 C CD  . GLU A 203 ? 2.1201 1.7376 1.5813 0.3094  -0.5577 -0.7303 201 GLU A CD  
1411 O OE1 . GLU A 203 ? 2.1171 1.7283 1.6348 0.2608  -0.6340 -0.7149 201 GLU A OE1 
1412 O OE2 . GLU A 203 ? 2.0300 1.6438 1.5055 0.3536  -0.5539 -0.8117 201 GLU A OE2 
1413 N N   . LYS A 204 ? 2.0719 1.9087 1.1219 0.4284  -0.2915 -0.5607 202 LYS A N   
1414 C CA  . LYS A 204 ? 2.0569 1.9440 1.0189 0.4624  -0.2880 -0.5532 202 LYS A CA  
1415 C C   . LYS A 204 ? 2.0123 1.9238 0.9882 0.4657  -0.3495 -0.6000 202 LYS A C   
1416 O O   . LYS A 204 ? 2.0530 1.9518 1.0416 0.4799  -0.3634 -0.6495 202 LYS A O   
1417 C CB  . LYS A 204 ? 1.9801 1.8620 0.8729 0.4957  -0.2179 -0.5269 202 LYS A CB  
1418 N N   . ASP A 209 ? 1.5287 1.6564 1.4924 0.6616  -0.5431 0.0633  207 ASP A N   
1419 C CA  . ASP A 209 ? 1.4566 1.6103 1.5610 0.6187  -0.5240 0.0939  207 ASP A CA  
1420 C C   . ASP A 209 ? 1.4899 1.6144 1.5962 0.5955  -0.5262 0.0842  207 ASP A C   
1421 O O   . ASP A 209 ? 1.5031 1.6776 1.6095 0.5918  -0.4689 0.1019  207 ASP A O   
1422 C CB  . ASP A 209 ? 1.4278 1.5454 1.6419 0.5948  -0.5767 0.0988  207 ASP A CB  
1423 C CG  . ASP A 209 ? 1.4242 1.5758 1.8084 0.5544  -0.5492 0.1285  207 ASP A CG  
1424 O OD1 . ASP A 209 ? 1.4344 1.6326 1.8312 0.5297  -0.4676 0.1435  207 ASP A OD1 
1425 O OD2 . ASP A 209 ? 1.4005 1.5309 1.9031 0.5236  -0.5848 0.1381  207 ASP A OD2 
1426 N N   . ALA A 210 ? 1.5405 1.5796 1.6441 0.5775  -0.5959 0.0580  208 ALA A N   
1427 C CA  . ALA A 210 ? 1.5257 1.5242 1.6395 0.5464  -0.6113 0.0519  208 ALA A CA  
1428 C C   . ALA A 210 ? 1.5670 1.5737 1.5502 0.5745  -0.5815 0.0348  208 ALA A C   
1429 O O   . ALA A 210 ? 1.6025 1.6060 1.4797 0.6170  -0.5814 0.0105  208 ALA A O   
1430 C CB  . ALA A 210 ? 1.5693 1.4700 1.7065 0.5152  -0.6989 0.0316  208 ALA A CB  
1431 N N   . VAL A 211 ? 1.5931 1.6081 1.5904 0.5506  -0.5568 0.0477  209 VAL A N   
1432 C CA  . VAL A 211 ? 1.6041 1.6282 1.4967 0.5679  -0.5303 0.0378  209 VAL A CA  
1433 C C   . VAL A 211 ? 1.6421 1.5763 1.5195 0.5356  -0.5884 0.0177  209 VAL A C   
1434 O O   . VAL A 211 ? 1.6507 1.5536 1.6193 0.4566  -0.5814 0.0329  209 VAL A O   
1435 C CB  . VAL A 211 ? 1.5788 1.6857 1.4891 0.5409  -0.4312 0.0746  209 VAL A CB  
1436 C CG1 . VAL A 211 ? 1.6220 1.7364 1.4403 0.5598  -0.4213 0.0713  209 VAL A CG1 
1437 C CG2 . VAL A 211 ? 1.4826 1.6773 1.4013 0.5806  -0.3879 0.0993  209 VAL A CG2 
1438 N N   . VAL A 212 ? 1.7271 1.6235 1.5022 0.5621  -0.6063 -0.0162 210 VAL A N   
1439 C CA  . VAL A 212 ? 1.7525 1.5605 1.5025 0.5338  -0.6604 -0.0370 210 VAL A CA  
1440 C C   . VAL A 212 ? 1.7774 1.6130 1.5108 0.5118  -0.6216 -0.0143 210 VAL A C   
1441 O O   . VAL A 212 ? 1.7842 1.6910 1.4676 0.5437  -0.5618 -0.0058 210 VAL A O   
1442 C CB  . VAL A 212 ? 1.7672 1.5127 1.4172 0.5811  -0.6979 -0.0883 210 VAL A CB  
1443 C CG1 . VAL A 212 ? 1.8456 1.5044 1.4650 0.5565  -0.7447 -0.1085 210 VAL A CG1 
1444 C CG2 . VAL A 212 ? 1.7253 1.4159 1.3811 0.5962  -0.7524 -0.1123 210 VAL A CG2 
1445 N N   . TYR A 213 ? 1.8153 1.5957 1.5977 0.4387  -0.6412 -0.0007 211 TYR A N   
1446 C CA  . TYR A 213 ? 1.8400 1.6363 1.6117 0.3817  -0.5755 0.0201  211 TYR A CA  
1447 C C   . TYR A 213 ? 1.8629 1.5701 1.5742 0.3759  -0.6498 -0.0003 211 TYR A C   
1448 O O   . TYR A 213 ? 1.9143 1.5354 1.6298 0.3759  -0.7433 -0.0207 211 TYR A O   
1449 C CB  . TYR A 213 ? 1.9071 1.7216 1.7795 0.2791  -0.4933 0.0552  211 TYR A CB  
1450 C CG  . TYR A 213 ? 1.9760 1.7224 1.9220 0.2024  -0.5269 0.0628  211 TYR A CG  
1451 C CD1 . TYR A 213 ? 2.0237 1.7681 2.0643 0.1912  -0.5528 0.0687  211 TYR A CD1 
1452 C CD2 . TYR A 213 ? 2.0243 1.7162 1.9536 0.1362  -0.5292 0.0721  211 TYR A CD2 
1453 C CE1 . TYR A 213 ? 2.0793 1.7778 2.2031 0.1177  -0.5802 0.0875  211 TYR A CE1 
1454 C CE2 . TYR A 213 ? 2.0751 1.7167 2.0767 0.0623  -0.5553 0.0892  211 TYR A CE2 
1455 C CZ  . TYR A 213 ? 2.1077 1.7581 2.2111 0.0533  -0.5792 0.0992  211 TYR A CZ  
1456 O OH  . TYR A 213 ? 2.1614 1.7764 2.3509 -0.0223 -0.6041 0.1269  211 TYR A OH  
1457 N N   . ARG A 214 ? 1.8323 1.5569 1.4905 0.3691  -0.6143 0.0084  212 ARG A N   
1458 C CA  . ARG A 214 ? 1.9250 1.5710 1.5196 0.3707  -0.6823 -0.0096 212 ARG A CA  
1459 C C   . ARG A 214 ? 1.9145 1.5574 1.5196 0.2805  -0.6222 0.0216  212 ARG A C   
1460 O O   . ARG A 214 ? 1.8895 1.5924 1.4626 0.2908  -0.5655 0.0387  212 ARG A O   
1461 C CB  . ARG A 214 ? 1.8602 1.5417 1.3904 0.4491  -0.6633 -0.0419 212 ARG A CB  
1462 N N   . GLY A 215 ? 1.9456 1.5184 1.5947 0.1912  -0.6380 0.0332  213 GLY A N   
1463 C CA  . GLY A 215 ? 1.9672 1.5225 1.6166 0.1007  -0.5847 0.0624  213 GLY A CA  
1464 C C   . GLY A 215 ? 2.0126 1.4957 1.5917 0.0992  -0.6517 0.0523  213 GLY A C   
1465 O O   . GLY A 215 ? 2.0287 1.4279 1.6001 0.1005  -0.7465 0.0343  213 GLY A O   
1466 N N   . THR A 216 ? 1.9942 1.5045 1.5251 0.0955  -0.6110 0.0663  214 THR A N   
1467 C CA  . THR A 216 ? 2.0243 1.4689 1.4947 0.0876  -0.6693 0.0620  214 THR A CA  
1468 C C   . THR A 216 ? 2.1005 1.4473 1.5875 -0.0105 -0.7039 0.0750  214 THR A C   
1469 O O   . THR A 216 ? 2.0429 1.3136 1.4861 -0.0235 -0.7736 0.0700  214 THR A O   
1470 C CB  . THR A 216 ? 1.9427 1.4363 1.3791 0.0751  -0.6086 0.0884  214 THR A CB  
1471 O OG1 . THR A 216 ? 1.9679 1.4884 1.4376 -0.0043 -0.5140 0.1207  214 THR A OG1 
1472 C CG2 . THR A 216 ? 1.8086 1.3997 1.2248 0.1819  -0.5968 0.0814  214 THR A CG2 
1473 N N   . THR A 217 ? 2.1038 1.4573 1.6576 -0.0784 -0.6544 0.0956  215 THR A N   
1474 C CA  . THR A 217 ? 2.1397 1.4221 1.7251 -0.1729 -0.6747 0.1182  215 THR A CA  
1475 C C   . THR A 217 ? 2.1363 1.4267 1.8098 -0.1751 -0.6957 0.1187  215 THR A C   
1476 O O   . THR A 217 ? 2.1242 1.4770 1.8316 -0.1158 -0.6740 0.1039  215 THR A O   
1477 C CB  . THR A 217 ? 2.1183 1.4090 1.6999 -0.2664 -0.5756 0.1557  215 THR A CB  
1478 O OG1 . THR A 217 ? 2.1189 1.4664 1.7749 -0.2915 -0.4948 0.1710  215 THR A OG1 
1479 C CG2 . THR A 217 ? 2.0979 1.4210 1.6130 -0.2472 -0.5255 0.1574  215 THR A CG2 
1480 N N   . THR A 218 ? 2.1323 1.3609 1.8477 -0.2467 -0.7419 0.1414  216 THR A N   
1481 C CA  . THR A 218 ? 2.1457 1.3835 1.9627 -0.2620 -0.7675 0.1539  216 THR A CA  
1482 C C   . THR A 218 ? 2.1219 1.4268 2.0188 -0.3330 -0.6518 0.1949  216 THR A C   
1483 O O   . THR A 218 ? 2.0829 1.3827 2.0656 -0.3968 -0.6604 0.2312  216 THR A O   
1484 C CB  . THR A 218 ? 2.1577 1.2981 1.9919 -0.2996 -0.8902 0.1643  216 THR A CB  
1485 O OG1 . THR A 218 ? 2.1404 1.2036 1.8749 -0.2499 -0.9804 0.1298  216 THR A OG1 
1486 C CG2 . THR A 218 ? 2.0680 1.2016 1.9850 -0.2719 -0.9656 0.1598  216 THR A CG2 
1487 N N   . TYR A 219 ? 2.1497 1.5190 2.0212 -0.3203 -0.5439 0.1922  217 TYR A N   
1488 C CA  . TYR A 219 ? 2.1341 1.5638 2.0688 -0.3697 -0.4298 0.2221  217 TYR A CA  
1489 C C   . TYR A 219 ? 2.1519 1.6482 2.1847 -0.3242 -0.4200 0.2164  217 TYR A C   
1490 O O   . TYR A 219 ? 2.1616 1.6871 2.1739 -0.2448 -0.4367 0.1850  217 TYR A O   
1491 C CB  . TYR A 219 ? 2.0888 1.5396 1.9451 -0.3730 -0.3343 0.2191  217 TYR A CB  
1492 C CG  . TYR A 219 ? 2.0714 1.5857 1.9721 -0.3872 -0.2173 0.2327  217 TYR A CG  
1493 C CD1 . TYR A 219 ? 2.0578 1.6370 1.9878 -0.3226 -0.1861 0.2148  217 TYR A CD1 
1494 C CD2 . TYR A 219 ? 2.0222 1.5276 1.9259 -0.4612 -0.1381 0.2632  217 TYR A CD2 
1495 C CE1 . TYR A 219 ? 2.0256 1.6531 1.9944 -0.3325 -0.0859 0.2252  217 TYR A CE1 
1496 C CE2 . TYR A 219 ? 2.0256 1.5800 1.9604 -0.4647 -0.0323 0.2703  217 TYR A CE2 
1497 C CZ  . TYR A 219 ? 1.9923 1.6045 1.9625 -0.4006 -0.0097 0.2503  217 TYR A CZ  
1498 O OH  . TYR A 219 ? 1.8896 1.5414 1.8904 -0.4014 0.0888  0.2557  217 TYR A OH  
1499 N N   . LYS A 220 ? 2.1194 1.6444 2.2621 -0.3744 -0.3931 0.2513  218 LYS A N   
1500 C CA  . LYS A 220 ? 2.0968 1.6820 2.3472 -0.3376 -0.3930 0.2515  218 LYS A CA  
1501 C C   . LYS A 220 ? 2.1040 1.7613 2.3571 -0.3037 -0.2861 0.2414  218 LYS A C   
1502 O O   . LYS A 220 ? 2.0477 1.7471 2.3498 -0.3447 -0.1874 0.2670  218 LYS A O   
1503 C CB  . LYS A 220 ? 2.0344 1.6417 2.4179 -0.4042 -0.3912 0.3012  218 LYS A CB  
1504 N N   . LEU A 221 ? 2.1309 1.8005 2.3237 -0.2283 -0.3037 0.2061  219 LEU A N   
1505 C CA  . LEU A 221 ? 2.1310 1.8622 2.3190 -0.1990 -0.2120 0.2004  219 LEU A CA  
1506 C C   . LEU A 221 ? 2.0575 1.8476 2.3733 -0.2149 -0.1539 0.2227  219 LEU A C   
1507 O O   . LEU A 221 ? 2.0699 1.8796 2.4726 -0.1901 -0.2098 0.2243  219 LEU A O   
1508 C CB  . LEU A 221 ? 2.2242 1.9761 2.3613 -0.1104 -0.2566 0.1691  219 LEU A CB  
1509 N N   . ASN A 222 ? 1.9895 1.8033 2.3156 -0.2528 -0.0468 0.2396  220 ASN A N   
1510 C CA  . ASN A 222 ? 1.8860 1.7606 2.3331 -0.2623 0.0207  0.2607  220 ASN A CA  
1511 C C   . ASN A 222 ? 1.8030 1.7201 2.2456 -0.2113 0.0769  0.2441  220 ASN A C   
1512 O O   . ASN A 222 ? 1.8359 1.7405 2.1855 -0.1745 0.0634  0.2225  220 ASN A O   
1513 C CB  . ASN A 222 ? 1.8323 1.7030 2.2930 -0.3319 0.1044  0.2911  220 ASN A CB  
1514 C CG  . ASN A 222 ? 1.8923 1.6997 2.2090 -0.3639 0.1366  0.2830  220 ASN A CG  
1515 O OD1 . ASN A 222 ? 1.9421 1.6956 2.1841 -0.3746 0.0656  0.2755  220 ASN A OD1 
1516 N ND2 . ASN A 222 ? 1.8436 1.6496 2.1172 -0.3776 0.2384  0.2837  220 ASN A ND2 
1517 N N   . VAL A 223 ? 1.7196 1.6920 2.2726 -0.2078 0.1358  0.2587  221 VAL A N   
1518 C CA  . VAL A 223 ? 1.6614 1.6693 2.2206 -0.1631 0.1858  0.2466  221 VAL A CA  
1519 C C   . VAL A 223 ? 1.6508 1.6302 2.1310 -0.1903 0.2827  0.2451  221 VAL A C   
1520 O O   . VAL A 223 ? 1.6728 1.6189 2.1187 -0.2415 0.3220  0.2566  221 VAL A O   
1521 C CB  . VAL A 223 ? 1.5877 1.6609 2.3019 -0.1430 0.1978  0.2617  221 VAL A CB  
1522 C CG1 . VAL A 223 ? 1.4982 1.6021 2.2222 -0.1006 0.2504  0.2517  221 VAL A CG1 
1523 C CG2 . VAL A 223 ? 1.6462 1.7305 2.4275 -0.1191 0.0893  0.2634  221 VAL A CG2 
1524 N N   . GLY A 224 ? 1.5964 1.5810 2.0393 -0.1575 0.3169  0.2328  222 GLY A N   
1525 C CA  . GLY A 224 ? 1.5577 1.4950 1.9077 -0.1806 0.3918  0.2285  222 GLY A CA  
1526 C C   . GLY A 224 ? 1.6137 1.4943 1.8273 -0.1979 0.3573  0.2216  222 GLY A C   
1527 O O   . GLY A 224 ? 1.5972 1.4259 1.7161 -0.2178 0.4009  0.2188  222 GLY A O   
1528 N N   . ASP A 225 ? 1.6852 1.5691 1.8863 -0.1895 0.2754  0.2192  223 ASP A N   
1529 C CA  . ASP A 225 ? 1.7050 1.5468 1.7918 -0.1968 0.2344  0.2145  223 ASP A CA  
1530 C C   . ASP A 225 ? 1.6384 1.5130 1.6953 -0.1474 0.2200  0.2122  223 ASP A C   
1531 O O   . ASP A 225 ? 1.5671 1.4912 1.6891 -0.1096 0.2334  0.2130  223 ASP A O   
1532 C CB  . ASP A 225 ? 1.7514 1.5819 1.8389 -0.1979 0.1502  0.2110  223 ASP A CB  
1533 C CG  . ASP A 225 ? 1.8508 1.6523 1.9741 -0.2559 0.1603  0.2245  223 ASP A CG  
1534 O OD1 . ASP A 225 ? 1.8052 1.6087 1.9585 -0.2884 0.2408  0.2368  223 ASP A OD1 
1535 O OD2 . ASP A 225 ? 1.9454 1.7219 2.0646 -0.2675 0.0878  0.2252  223 ASP A OD2 
1536 N N   . TYR A 226 ? 1.6543 1.5049 1.6176 -0.1503 0.1940  0.2151  224 TYR A N   
1537 C CA  . TYR A 226 ? 1.6407 1.5319 1.5779 -0.1101 0.1845  0.2251  224 TYR A CA  
1538 C C   . TYR A 226 ? 1.6730 1.5728 1.5423 -0.0897 0.1252  0.2299  224 TYR A C   
1539 O O   . TYR A 226 ? 1.6839 1.5294 1.4838 -0.1294 0.1169  0.2333  224 TYR A O   
1540 C CB  . TYR A 226 ? 1.5894 1.4451 1.4926 -0.1411 0.2488  0.2370  224 TYR A CB  
1541 C CG  . TYR A 226 ? 1.5731 1.3640 1.3709 -0.1847 0.2531  0.2492  224 TYR A CG  
1542 C CD1 . TYR A 226 ? 1.5323 1.3503 1.2923 -0.1682 0.2231  0.2723  224 TYR A CD1 
1543 C CD2 . TYR A 226 ? 1.5969 1.3016 1.3343 -0.2432 0.2862  0.2425  224 TYR A CD2 
1544 C CE1 . TYR A 226 ? 1.5250 1.2823 1.1978 -0.2117 0.2190  0.2889  224 TYR A CE1 
1545 C CE2 . TYR A 226 ? 1.6252 1.2595 1.2591 -0.2851 0.2824  0.2542  224 TYR A CE2 
1546 C CZ  . TYR A 226 ? 1.5378 1.1971 1.1441 -0.2704 0.2452  0.2775  224 TYR A CZ  
1547 O OH  . TYR A 226 ? 1.5237 1.1125 1.0364 -0.3152 0.2332  0.2946  224 TYR A OH  
1548 N N   . VAL A 228 ? 1.6143 1.6047 1.3118 -0.0412 0.0446  0.3091  226 VAL A N   
1549 C CA  . VAL A 228 ? 1.5611 1.6263 1.2667 -0.0183 0.0513  0.3522  226 VAL A CA  
1550 C C   . VAL A 228 ? 1.5982 1.7351 1.2845 0.0350  0.0059  0.3695  226 VAL A C   
1551 O O   . VAL A 228 ? 1.6361 1.7311 1.2844 0.0294  -0.0282 0.3515  226 VAL A O   
1552 C CB  . VAL A 228 ? 1.5391 1.5397 1.2106 -0.0908 0.0810  0.3810  226 VAL A CB  
1553 C CG1 . VAL A 228 ? 1.4654 1.5059 1.1123 -0.0941 0.0533  0.4299  226 VAL A CG1 
1554 C CG2 . VAL A 228 ? 1.4143 1.4154 1.1237 -0.0988 0.1231  0.3894  226 VAL A CG2 
1555 N N   . LEU A 229 ? 1.5718 1.5164 1.3871 0.0262  0.1867  0.0629  227 LEU A N   
1556 C CA  . LEU A 229 ? 1.6061 1.5417 1.4115 -0.0001 0.1513  0.0608  227 LEU A CA  
1557 C C   . LEU A 229 ? 1.6703 1.5629 1.3867 0.0118  0.1511  0.0565  227 LEU A C   
1558 O O   . LEU A 229 ? 1.6809 1.5363 1.3299 0.0383  0.1492  0.0396  227 LEU A O   
1559 C CB  . LEU A 229 ? 1.5912 1.5210 1.4099 -0.0108 0.1071  0.0417  227 LEU A CB  
1560 C CG  . LEU A 229 ? 1.5677 1.5336 1.4633 -0.0385 0.0872  0.0491  227 LEU A CG  
1561 C CD1 . LEU A 229 ? 1.5276 1.4784 1.4200 -0.0467 0.0473  0.0328  227 LEU A CD1 
1562 C CD2 . LEU A 229 ? 1.5514 1.5323 1.4653 -0.0622 0.0869  0.0649  227 LEU A CD2 
1563 N N   . THR A 230 ? 1.6642 1.5587 1.3786 -0.0067 0.1488  0.0700  228 THR A N   
1564 C CA  . THR A 230 ? 1.6530 1.5069 1.2849 0.0042  0.1451  0.0673  228 THR A CA  
1565 C C   . THR A 230 ? 1.6600 1.4820 1.2480 0.0088  0.1010  0.0394  228 THR A C   
1566 O O   . THR A 230 ? 1.5956 1.4310 1.2265 -0.0075 0.0716  0.0284  228 THR A O   
1567 C CB  . THR A 230 ? 1.5590 1.4219 1.2070 -0.0199 0.1428  0.0850  228 THR A CB  
1568 N N   . SER A 231 ? 1.6618 1.4397 1.1649 0.0315  0.0954  0.0282  229 SER A N   
1569 C CA  . SER A 231 ? 1.6453 1.3927 1.1139 0.0338  0.0492  0.0010  229 SER A CA  
1570 C C   . SER A 231 ? 1.6731 1.3831 1.0663 0.0451  0.0366  -0.0024 229 SER A C   
1571 O O   . SER A 231 ? 1.6767 1.3900 1.0583 0.0414  0.0571  0.0185  229 SER A O   
1572 C CB  . SER A 231 ? 1.6977 1.4232 1.1434 0.0579  0.0438  -0.0214 229 SER A CB  
1573 O OG  . SER A 231 ? 1.6849 1.4446 1.1974 0.0516  0.0606  -0.0150 229 SER A OG  
1574 N N   . HIS A 232 ? 1.6899 1.3620 1.0325 0.0598  0.0009  -0.0291 230 HIS A N   
1575 C CA  . HIS A 232 ? 1.7250 1.3599 0.9974 0.0720  -0.0209 -0.0366 230 HIS A CA  
1576 C C   . HIS A 232 ? 1.7484 1.3465 0.9853 0.0858  -0.0666 -0.0707 230 HIS A C   
1577 O O   . HIS A 232 ? 1.7359 1.3404 1.0133 0.0787  -0.0836 -0.0863 230 HIS A O   
1578 C CB  . HIS A 232 ? 1.6918 1.3484 1.0042 0.0424  -0.0392 -0.0258 230 HIS A CB  
1579 C CG  . HIS A 232 ? 1.7698 1.3992 1.0188 0.0543  -0.0401 -0.0179 230 HIS A CG  
1580 N ND1 . HIS A 232 ? 1.8415 1.4208 0.9948 0.0892  -0.0463 -0.0298 230 HIS A ND1 
1581 C CD2 . HIS A 232 ? 1.7448 1.3874 1.0110 0.0368  -0.0384 0.0004  230 HIS A CD2 
1582 C CE1 . HIS A 232 ? 1.8126 1.3763 0.9268 0.0928  -0.0463 -0.0169 230 HIS A CE1 
1583 N NE2 . HIS A 232 ? 1.8055 1.4073 0.9891 0.0607  -0.0414 0.0014  230 HIS A NE2 
1584 N N   . THR A 233 ? 1.7923 1.3499 0.9555 0.1050  -0.0894 -0.0823 231 THR A N   
1585 C CA  . THR A 233 ? 1.7894 1.3092 0.9198 0.1182  -0.1391 -0.1165 231 THR A CA  
1586 C C   . THR A 233 ? 1.7528 1.2826 0.9171 0.0951  -0.1798 -0.1209 231 THR A C   
1587 O O   . THR A 233 ? 1.7831 1.3118 0.9229 0.0949  -0.1759 -0.1063 231 THR A O   
1588 C CB  . THR A 233 ? 1.8632 1.3240 0.8785 0.1632  -0.1406 -0.1313 231 THR A CB  
1589 O OG1 . THR A 233 ? 1.8446 1.2982 0.8306 0.1866  -0.0977 -0.1261 231 THR A OG1 
1590 C CG2 . THR A 233 ? 1.8978 1.3181 0.8855 0.1758  -0.1995 -0.1703 231 THR A CG2 
1591 N N   . VAL A 234 ? 1.7137 1.2526 0.9362 0.0764  -0.2172 -0.1397 232 VAL A N   
1592 C CA  . VAL A 234 ? 1.6102 1.1662 0.8819 0.0523  -0.2524 -0.1428 232 VAL A CA  
1593 C C   . VAL A 234 ? 1.6363 1.1489 0.8430 0.0755  -0.2935 -0.1650 232 VAL A C   
1594 O O   . VAL A 234 ? 1.5675 1.0515 0.7654 0.0857  -0.3327 -0.1946 232 VAL A O   
1595 C CB  . VAL A 234 ? 1.4953 1.0752 0.8538 0.0251  -0.2737 -0.1522 232 VAL A CB  
1596 C CG1 . VAL A 234 ? 1.3988 1.0002 0.8116 0.0013  -0.3031 -0.1519 232 VAL A CG1 
1597 C CG2 . VAL A 234 ? 1.5002 1.1176 0.9128 0.0071  -0.2358 -0.1311 232 VAL A CG2 
1598 N N   . MET A 235 ? 1.6184 1.1235 0.7802 0.0846  -0.2873 -0.1515 233 MET A N   
1599 C CA  . MET A 235 ? 1.6043 1.0711 0.7100 0.1056  -0.3309 -0.1714 233 MET A CA  
1600 C C   . MET A 235 ? 1.5463 1.0363 0.7328 0.0800  -0.3767 -0.1854 233 MET A C   
1601 O O   . MET A 235 ? 1.4480 0.9851 0.7189 0.0471  -0.3644 -0.1692 233 MET A O   
1602 C CB  . MET A 235 ? 1.6264 1.0806 0.6697 0.1202  -0.3119 -0.1500 233 MET A CB  
1603 C CG  . MET A 235 ? 1.6786 1.1137 0.6494 0.1435  -0.2591 -0.1298 233 MET A CG  
1604 S SD  . MET A 235 ? 1.8936 1.2644 0.7544 0.1918  -0.2661 -0.1565 233 MET A SD  
1605 C CE  . MET A 235 ? 1.8333 1.1546 0.6270 0.2173  -0.3313 -0.1843 233 MET A CE  
1606 N N   . PRO A 236 ? 1.6093 1.0667 0.7733 0.0954  -0.4297 -0.2155 234 PRO A N   
1607 C CA  . PRO A 236 ? 1.5806 1.0628 0.8317 0.0710  -0.4723 -0.2283 234 PRO A CA  
1608 C C   . PRO A 236 ? 1.5585 1.0678 0.8335 0.0593  -0.4718 -0.2098 234 PRO A C   
1609 O O   . PRO A 236 ? 1.5370 1.0372 0.7526 0.0728  -0.4466 -0.1905 234 PRO A O   
1610 C CB  . PRO A 236 ? 1.5620 1.0132 0.8013 0.0946  -0.5103 -0.2555 234 PRO A CB  
1611 C CG  . PRO A 236 ? 1.6374 1.0448 0.7622 0.1338  -0.4958 -0.2528 234 PRO A CG  
1612 C CD  . PRO A 236 ? 1.6781 1.0794 0.7494 0.1360  -0.4498 -0.2374 234 PRO A CD  
1613 N N   . LEU A 237 ? 1.4792 1.0235 0.8489 0.0344  -0.4960 -0.2138 235 LEU A N   
1614 C CA  . LEU A 237 ? 1.3770 0.9511 0.7829 0.0219  -0.4973 -0.1985 235 LEU A CA  
1615 C C   . LEU A 237 ? 1.3633 0.9426 0.8148 0.0289  -0.5347 -0.2140 235 LEU A C   
1616 O O   . LEU A 237 ? 1.3861 0.9605 0.8769 0.0294  -0.5594 -0.2340 235 LEU A O   
1617 C CB  . LEU A 237 ? 1.3510 0.9784 0.8502 -0.0148 -0.4711 -0.1785 235 LEU A CB  
1618 C CG  . LEU A 237 ? 1.3440 0.9888 0.8374 -0.0258 -0.4159 -0.1520 235 LEU A CG  
1619 C CD1 . LEU A 237 ? 1.1877 0.8818 0.7724 -0.0587 -0.3976 -0.1355 235 LEU A CD1 
1620 C CD2 . LEU A 237 ? 1.2818 0.9127 0.7037 -0.0102 -0.3882 -0.1324 235 LEU A CD2 
1621 N N   . SER A 238 ? 1.3598 0.9471 0.8070 0.0344  -0.5396 -0.2043 236 SER A N   
1622 C CA  . SER A 238 ? 1.4091 0.9992 0.8938 0.0440  -0.5757 -0.2182 236 SER A CA  
1623 C C   . SER A 238 ? 1.3400 0.9711 0.8910 0.0267  -0.5769 -0.2054 236 SER A C   
1624 O O   . SER A 238 ? 1.3521 1.0090 0.9854 0.0175  -0.6008 -0.2149 236 SER A O   
1625 C CB  . SER A 238 ? 1.4807 1.0225 0.8703 0.0823  -0.5885 -0.2252 236 SER A CB  
1626 O OG  . SER A 238 ? 1.4921 1.0209 0.8095 0.0926  -0.5608 -0.2033 236 SER A OG  
1627 N N   . ALA A 239 ? 1.3030 0.9393 0.8196 0.0233  -0.5507 -0.1836 237 ALA A N   
1628 C CA  . ALA A 239 ? 1.2894 0.9581 0.8567 0.0122  -0.5526 -0.1721 237 ALA A CA  
1629 C C   . ALA A 239 ? 1.2091 0.9250 0.8675 -0.0225 -0.5383 -0.1637 237 ALA A C   
1630 O O   . ALA A 239 ? 1.2188 0.9374 0.8770 -0.0382 -0.5176 -0.1585 237 ALA A O   
1631 C CB  . ALA A 239 ? 1.2760 0.9258 0.7680 0.0238  -0.5318 -0.1514 237 ALA A CB  
1632 N N   . PRO A 240 ? 1.1966 0.9490 0.9328 -0.0336 -0.5482 -0.1617 238 PRO A N   
1633 C CA  . PRO A 240 ? 1.0930 0.8889 0.9119 -0.0645 -0.5307 -0.1508 238 PRO A CA  
1634 C C   . PRO A 240 ? 1.1005 0.9041 0.8900 -0.0732 -0.4860 -0.1246 238 PRO A C   
1635 O O   . PRO A 240 ? 1.0663 0.8447 0.7818 -0.0578 -0.4747 -0.1149 238 PRO A O   
1636 C CB  . PRO A 240 ? 1.0591 0.8882 0.9584 -0.0661 -0.5497 -0.1546 238 PRO A CB  
1637 C CG  . PRO A 240 ? 1.0957 0.8985 0.9316 -0.0382 -0.5665 -0.1568 238 PRO A CG  
1638 C CD  . PRO A 240 ? 1.1618 0.9164 0.9119 -0.0169 -0.5743 -0.1679 238 PRO A CD  
1639 N N   . THR A 241 ? 0.9909 0.8292 0.8418 -0.0973 -0.4560 -0.1114 239 THR A N   
1640 C CA  . THR A 241 ? 1.0545 0.9033 0.8882 -0.1058 -0.4133 -0.0875 239 THR A CA  
1641 C C   . THR A 241 ? 1.0573 0.9149 0.8924 -0.0988 -0.4139 -0.0792 239 THR A C   
1642 O O   . THR A 241 ? 1.0084 0.8491 0.7887 -0.0915 -0.3959 -0.0660 239 THR A O   
1643 C CB  . THR A 241 ? 0.9746 0.8554 0.8702 -0.1298 -0.3861 -0.0768 239 THR A CB  
1644 O OG1 . THR A 241 ? 0.9556 0.8683 0.9340 -0.1391 -0.3984 -0.0806 239 THR A OG1 
1645 C CG2 . THR A 241 ? 0.9780 0.8461 0.8668 -0.1356 -0.3829 -0.0831 239 THR A CG2 
1646 N N   . LEU A 242 ? 1.0573 0.9418 0.9604 -0.1011 -0.4336 -0.0861 240 LEU A N   
1647 C CA  . LEU A 242 ? 1.0139 0.9091 0.9286 -0.0919 -0.4390 -0.0815 240 LEU A CA  
1648 C C   . LEU A 242 ? 1.0625 0.9524 0.9937 -0.0754 -0.4872 -0.1016 240 LEU A C   
1649 O O   . LEU A 242 ? 1.0729 0.9794 1.0666 -0.0824 -0.5105 -0.1163 240 LEU A O   
1650 C CB  . LEU A 242 ? 0.9478 0.8857 0.9376 -0.1079 -0.4150 -0.0701 240 LEU A CB  
1651 C CG  . LEU A 242 ? 0.9659 0.9079 0.9358 -0.1188 -0.3721 -0.0503 240 LEU A CG  
1652 C CD1 . LEU A 242 ? 0.8675 0.8482 0.9076 -0.1295 -0.3526 -0.0420 240 LEU A CD1 
1653 C CD2 . LEU A 242 ? 0.9974 0.9125 0.8996 -0.1058 -0.3655 -0.0417 240 LEU A CD2 
1654 N N   . VAL A 243 ? 1.1110 0.9758 0.9880 -0.0535 -0.5040 -0.1023 241 VAL A N   
1655 C CA  . VAL A 243 ? 1.0997 0.9600 0.9931 -0.0349 -0.5535 -0.1214 241 VAL A CA  
1656 C C   . VAL A 243 ? 1.0221 0.9331 1.0231 -0.0447 -0.5574 -0.1222 241 VAL A C   
1657 O O   . VAL A 243 ? 1.0596 0.9964 1.0895 -0.0564 -0.5205 -0.1048 241 VAL A O   
1658 C CB  . VAL A 243 ? 1.1338 0.9539 0.9418 -0.0072 -0.5680 -0.1186 241 VAL A CB  
1659 C CG1 . VAL A 243 ? 1.1914 0.9614 0.8981 0.0062  -0.5628 -0.1186 241 VAL A CG1 
1660 C CG2 . VAL A 243 ? 1.1285 0.9556 0.9274 -0.0099 -0.5329 -0.0961 241 VAL A CG2 
1661 N N   . PRO A 244 ? 1.0669 0.9939 1.1310 -0.0393 -0.5932 -0.1401 242 PRO A N   
1662 C CA  . PRO A 244 ? 1.0264 1.0045 1.1994 -0.0471 -0.5976 -0.1399 242 PRO A CA  
1663 C C   . PRO A 244 ? 1.0671 1.0513 1.2255 -0.0349 -0.5843 -0.1266 242 PRO A C   
1664 O O   . PRO A 244 ? 1.1118 1.0584 1.1887 -0.0137 -0.5965 -0.1257 242 PRO A O   
1665 C CB  . PRO A 244 ? 1.0435 1.0214 1.2562 -0.0333 -0.6322 -0.1594 242 PRO A CB  
1666 C CG  . PRO A 244 ? 1.1336 1.0731 1.2896 -0.0317 -0.6380 -0.1698 242 PRO A CG  
1667 C CD  . PRO A 244 ? 1.1139 1.0129 1.1548 -0.0234 -0.6203 -0.1588 242 PRO A CD  
1668 N N   . GLN A 245 ? 1.0700 1.0988 1.3051 -0.0465 -0.5552 -0.1150 243 GLN A N   
1669 C CA  . GLN A 245 ? 1.0725 1.1047 1.2912 -0.0347 -0.5352 -0.1019 243 GLN A CA  
1670 C C   . GLN A 245 ? 1.1200 1.1596 1.3700 -0.0112 -0.5766 -0.1142 243 GLN A C   
1671 O O   . GLN A 245 ? 1.1676 1.2350 1.4987 -0.0109 -0.6099 -0.1296 243 GLN A O   
1672 C CB  . GLN A 245 ? 0.9737 1.0471 1.2548 -0.0506 -0.4889 -0.0861 243 GLN A CB  
1673 C CG  . GLN A 245 ? 0.9736 1.0476 1.2352 -0.0374 -0.4666 -0.0741 243 GLN A CG  
1674 C CD  . GLN A 245 ? 1.0077 1.0334 1.1609 -0.0324 -0.4518 -0.0642 243 GLN A CD  
1675 O OE1 . GLN A 245 ? 1.0175 1.0050 1.1058 -0.0167 -0.4778 -0.0690 243 GLN A OE1 
1676 N NE2 . GLN A 245 ? 1.0279 1.0540 1.1621 -0.0452 -0.4100 -0.0498 243 GLN A NE2 
1677 N N   . GLU A 246 ? 1.1030 1.1162 1.2908 0.0086  -0.5759 -0.1073 244 GLU A N   
1678 C CA  . GLU A 246 ? 1.1573 1.1745 1.3675 0.0341  -0.6119 -0.1162 244 GLU A CA  
1679 C C   . GLU A 246 ? 1.1973 1.2213 1.4046 0.0421  -0.5806 -0.1009 244 GLU A C   
1680 O O   . GLU A 246 ? 1.1234 1.1128 1.2504 0.0416  -0.5528 -0.0867 244 GLU A O   
1681 C CB  . GLU A 246 ? 1.1401 1.1019 1.2570 0.0579  -0.6542 -0.1259 244 GLU A CB  
1682 C CG  . GLU A 246 ? 1.1822 1.1277 1.2867 0.0536  -0.6747 -0.1413 244 GLU A CG  
1683 C CD  . GLU A 246 ? 1.2430 1.1391 1.2731 0.0821  -0.7030 -0.1509 244 GLU A CD  
1684 O OE1 . GLU A 246 ? 1.3035 1.1523 1.2319 0.0972  -0.6961 -0.1399 244 GLU A OE1 
1685 O OE2 . GLU A 246 ? 1.3151 1.2175 1.3884 0.0893  -0.7315 -0.1686 244 GLU A OE2 
1686 N N   . HIS A 247 ? 1.1790 1.2474 1.4772 0.0498  -0.5849 -0.1042 245 HIS A N   
1687 C CA  . HIS A 247 ? 1.1533 1.2282 1.4535 0.0625  -0.5598 -0.0930 245 HIS A CA  
1688 C C   . HIS A 247 ? 1.1957 1.2603 1.4966 0.0939  -0.6025 -0.1025 245 HIS A C   
1689 O O   . HIS A 247 ? 1.0963 1.1949 1.4794 0.1023  -0.6380 -0.1170 245 HIS A O   
1690 C CB  . HIS A 247 ? 1.1192 1.2526 1.5192 0.0504  -0.5230 -0.0868 245 HIS A CB  
1691 C CG  . HIS A 247 ? 1.1203 1.2566 1.5049 0.0242  -0.4767 -0.0740 245 HIS A CG  
1692 N ND1 . HIS A 247 ? 1.1160 1.2319 1.4420 0.0222  -0.4369 -0.0600 245 HIS A ND1 
1693 C CD2 . HIS A 247 ? 1.1122 1.2668 1.5316 0.0000  -0.4665 -0.0739 245 HIS A CD2 
1694 C CE1 . HIS A 247 ? 1.1030 1.2257 1.4273 -0.0010 -0.4053 -0.0518 245 HIS A CE1 
1695 N NE2 . HIS A 247 ? 1.0768 1.2225 1.4564 -0.0147 -0.4210 -0.0590 245 HIS A NE2 
1696 N N   . TYR A 248 ? 1.2192 1.2364 1.4321 0.1110  -0.6001 -0.0940 246 TYR A N   
1697 C CA  . TYR A 248 ? 1.2130 1.2083 1.4064 0.1433  -0.6396 -0.1001 246 TYR A CA  
1698 C C   . TYR A 248 ? 1.2602 1.2803 1.5019 0.1576  -0.6205 -0.0947 246 TYR A C   
1699 O O   . TYR A 248 ? 1.2330 1.2747 1.4983 0.1441  -0.5740 -0.0848 246 TYR A O   
1700 C CB  . TYR A 248 ? 1.2429 1.1646 1.3060 0.1547  -0.6474 -0.0915 246 TYR A CB  
1701 C CG  . TYR A 248 ? 1.3125 1.2081 1.3181 0.1390  -0.6505 -0.0931 246 TYR A CG  
1702 C CD1 . TYR A 248 ? 1.3114 1.2280 1.3611 0.1347  -0.6844 -0.1111 246 TYR A CD1 
1703 C CD2 . TYR A 248 ? 1.2946 1.1464 1.2089 0.1278  -0.6185 -0.0771 246 TYR A CD2 
1704 C CE1 . TYR A 248 ? 1.3332 1.2238 1.3284 0.1226  -0.6867 -0.1140 246 TYR A CE1 
1705 C CE2 . TYR A 248 ? 1.2646 1.0948 1.1293 0.1154  -0.6182 -0.0783 246 TYR A CE2 
1706 C CZ  . TYR A 248 ? 1.2776 1.1259 1.1795 0.1139  -0.6520 -0.0972 246 TYR A CZ  
1707 O OH  . TYR A 248 ? 1.3554 1.1794 1.2049 0.1041  -0.6517 -0.1000 246 TYR A OH  
1708 N N   . VAL A 249 ? 1.3534 1.3675 1.6058 0.1881  -0.6582 -0.1022 247 VAL A N   
1709 C CA  . VAL A 249 ? 1.3342 1.3689 1.6309 0.2067  -0.6436 -0.0988 247 VAL A CA  
1710 C C   . VAL A 249 ? 1.3684 1.3428 1.5641 0.2188  -0.6258 -0.0849 247 VAL A C   
1711 O O   . VAL A 249 ? 1.3267 1.3100 1.5416 0.2275  -0.5984 -0.0795 247 VAL A O   
1712 C CB  . VAL A 249 ? 1.2795 1.3415 1.6491 0.2353  -0.6930 -0.1139 247 VAL A CB  
1713 C CG1 . VAL A 249 ? 1.1896 1.3200 1.6836 0.2210  -0.7057 -0.1269 247 VAL A CG1 
1714 C CG2 . VAL A 249 ? 1.3441 1.3477 1.6282 0.2582  -0.7462 -0.1196 247 VAL A CG2 
1715 N N   . ARG A 250 ? 1.4320 1.3436 1.5217 0.2200  -0.6395 -0.0787 248 ARG A N   
1716 C CA  . ARG A 250 ? 1.4355 1.2846 1.4307 0.2302  -0.6257 -0.0637 248 ARG A CA  
1717 C C   . ARG A 250 ? 1.4277 1.2266 1.3264 0.2137  -0.6181 -0.0534 248 ARG A C   
1718 O O   . ARG A 250 ? 1.3601 1.1687 1.2592 0.2012  -0.6309 -0.0602 248 ARG A O   
1719 C CB  . ARG A 250 ? 1.4332 1.2520 1.4073 0.2680  -0.6649 -0.0661 248 ARG A CB  
1720 N N   . ILE A 251 ? 1.4294 1.1742 1.2486 0.2137  -0.5960 -0.0367 249 ILE A N   
1721 C CA  . ILE A 251 ? 1.4527 1.1490 1.1826 0.1998  -0.5844 -0.0237 249 ILE A CA  
1722 C C   . ILE A 251 ? 1.5155 1.1843 1.1983 0.2185  -0.6272 -0.0290 249 ILE A C   
1723 O O   . ILE A 251 ? 1.4471 1.0846 1.0995 0.2492  -0.6599 -0.0291 249 ILE A O   
1724 C CB  . ILE A 251 ? 1.5280 1.1672 1.1879 0.2012  -0.5602 -0.0042 249 ILE A CB  
1725 C CG1 . ILE A 251 ? 1.4647 1.1279 1.1676 0.1848  -0.5224 -0.0028 249 ILE A CG1 
1726 C CG2 . ILE A 251 ? 1.5568 1.1482 1.1314 0.1876  -0.5458 0.0115  249 ILE A CG2 
1727 C CD1 . ILE A 251 ? 1.5026 1.1100 1.1443 0.1809  -0.4990 0.0143  249 ILE A CD1 
1728 N N   . THR A 252 ? 1.4938 1.1711 1.1666 0.2024  -0.6287 -0.0343 250 THR A N   
1729 C CA  . THR A 252 ? 1.4953 1.1488 1.1248 0.2205  -0.6713 -0.0438 250 THR A CA  
1730 C C   . THR A 252 ? 1.4949 1.0915 1.0176 0.2153  -0.6531 -0.0279 250 THR A C   
1731 O O   . THR A 252 ? 1.4433 1.0495 0.9643 0.1870  -0.6157 -0.0210 250 THR A O   
1732 C CB  . THR A 252 ? 1.4757 1.1845 1.1854 0.2094  -0.6933 -0.0664 250 THR A CB  
1733 O OG1 . THR A 252 ? 1.4761 1.2439 1.2964 0.2108  -0.7003 -0.0775 250 THR A OG1 
1734 C CG2 . THR A 252 ? 1.5044 1.1898 1.1823 0.2263  -0.7223 -0.0802 250 THR A CG2 
1735 N N   . GLY A 253 ? 1.5274 1.0697 0.9720 0.2398  -0.6649 -0.0220 251 GLY A N   
1736 C CA  . GLY A 253 ? 1.5981 1.0893 0.9471 0.2381  -0.6420 -0.0072 251 GLY A CA  
1737 C C   . GLY A 253 ? 1.6446 1.0888 0.9288 0.2330  -0.6082 0.0227  251 GLY A C   
1738 O O   . GLY A 253 ? 1.7255 1.1238 0.9298 0.2347  -0.5860 0.0389  251 GLY A O   
1739 N N   . LEU A 254 ? 1.6310 1.0877 0.9560 0.2252  -0.5963 0.0300  252 LEU A N   
1740 C CA  . LEU A 254 ? 1.6348 1.0556 0.9232 0.2117  -0.5544 0.0552  252 LEU A CA  
1741 C C   . LEU A 254 ? 1.6610 1.0545 0.9469 0.2320  -0.5642 0.0628  252 LEU A C   
1742 O O   . LEU A 254 ? 1.6547 1.0760 0.9931 0.2493  -0.5943 0.0464  252 LEU A O   
1743 C CB  . LEU A 254 ? 1.5815 1.0460 0.9308 0.1742  -0.5149 0.0545  252 LEU A CB  
1744 C CG  . LEU A 254 ? 1.5600 1.0198 0.8766 0.1522  -0.4869 0.0628  252 LEU A CG  
1745 C CD1 . LEU A 254 ? 1.7090 1.1001 0.9255 0.1662  -0.4779 0.0864  252 LEU A CD1 
1746 C CD2 . LEU A 254 ? 1.5594 1.0580 0.9030 0.1498  -0.5072 0.0416  252 LEU A CD2 
1747 N N   . TYR A 255 ? 1.7162 1.0546 0.9445 0.2299  -0.5379 0.0883  253 TYR A N   
1748 C CA  . TYR A 255 ? 1.7108 1.0087 0.9225 0.2503  -0.5459 0.0990  253 TYR A CA  
1749 C C   . TYR A 255 ? 1.7053 0.9992 0.9446 0.2255  -0.5083 0.1098  253 TYR A C   
1750 O O   . TYR A 255 ? 1.7045 0.9568 0.8987 0.2102  -0.4773 0.1329  253 TYR A O   
1751 C CB  . TYR A 255 ? 1.8339 1.0565 0.9428 0.2764  -0.5547 0.1210  253 TYR A CB  
1752 C CG  . TYR A 255 ? 1.8579 1.0972 0.9543 0.2929  -0.5776 0.1024  253 TYR A CG  
1753 C CD1 . TYR A 255 ? 1.8490 1.1046 0.9747 0.3194  -0.6166 0.0819  253 TYR A CD1 
1754 C CD2 . TYR A 255 ? 1.8987 1.1385 0.9593 0.2820  -0.5615 0.1035  253 TYR A CD2 
1755 C CE1 . TYR A 255 ? 1.8720 1.1392 0.9892 0.3336  -0.6407 0.0631  253 TYR A CE1 
1756 C CE2 . TYR A 255 ? 1.8791 1.1292 0.9275 0.2981  -0.5846 0.0843  253 TYR A CE2 
1757 C CZ  . TYR A 255 ? 1.9208 1.1830 0.9974 0.3232  -0.6252 0.0639  253 TYR A CZ  
1758 O OH  . TYR A 255 ? 2.0143 1.2822 1.0801 0.3387  -0.6511 0.0436  253 TYR A OH  
1759 N N   . PRO A 256 ? 1.6701 1.0055 0.9837 0.2216  -0.5098 0.0934  254 PRO A N   
1760 C CA  . PRO A 256 ? 1.6534 0.9860 0.9930 0.1989  -0.4777 0.0988  254 PRO A CA  
1761 C C   . PRO A 256 ? 1.7533 1.0149 1.0442 0.2091  -0.4720 0.1198  254 PRO A C   
1762 O O   . PRO A 256 ? 1.8028 1.0261 1.0580 0.2399  -0.4970 0.1256  254 PRO A O   
1763 C CB  . PRO A 256 ? 1.6152 1.0050 1.0363 0.2033  -0.4864 0.0747  254 PRO A CB  
1764 C CG  . PRO A 256 ? 1.6359 1.0380 1.0668 0.2362  -0.5269 0.0631  254 PRO A CG  
1765 C CD  . PRO A 256 ? 1.6553 1.0455 1.0368 0.2377  -0.5399 0.0681  254 PRO A CD  
1766 N N   . THR A 257 ? 1.7201 0.9629 1.0123 0.1828  -0.4404 0.1313  255 THR A N   
1767 C CA  . THR A 257 ? 1.8300 1.0085 1.0930 0.1877  -0.4337 0.1488  255 THR A CA  
1768 C C   . THR A 257 ? 1.8203 1.0129 1.1332 0.1973  -0.4428 0.1301  255 THR A C   
1769 O O   . THR A 257 ? 1.7679 1.0214 1.1383 0.1957  -0.4463 0.1066  255 THR A O   
1770 C CB  . THR A 257 ? 1.7959 0.9464 1.0455 0.1547  -0.3985 0.1685  255 THR A CB  
1771 O OG1 . THR A 257 ? 1.8495 0.9333 1.0750 0.1588  -0.3940 0.1863  255 THR A OG1 
1772 C CG2 . THR A 257 ? 1.7041 0.9061 1.0156 0.1255  -0.3816 0.1509  255 THR A CG2 
1773 N N   . LEU A 258 ? 1.9269 1.0596 1.2160 0.2085  -0.4448 0.1416  256 LEU A N   
1774 C CA  . LEU A 258 ? 1.9118 1.0460 1.2389 0.2200  -0.4517 0.1248  256 LEU A CA  
1775 C C   . LEU A 258 ? 1.9045 0.9918 1.2273 0.1992  -0.4317 0.1336  256 LEU A C   
1776 O O   . LEU A 258 ? 1.9416 1.0221 1.2898 0.2073  -0.4355 0.1187  256 LEU A O   
1777 C CB  . LEU A 258 ? 1.9430 1.0484 1.2531 0.2613  -0.4822 0.1241  256 LEU A CB  
1778 C CG  . LEU A 258 ? 1.9504 1.1009 1.2748 0.2874  -0.5111 0.1114  256 LEU A CG  
1779 C CD1 . LEU A 258 ? 1.8755 1.1123 1.2708 0.2747  -0.5058 0.0865  256 LEU A CD1 
1780 C CD2 . LEU A 258 ? 1.9643 1.0891 1.2268 0.2921  -0.5203 0.1301  256 LEU A CD2 
1781 N N   . ASN A 259 ? 1.9167 0.9712 1.2102 0.1734  -0.4108 0.1568  257 ASN A N   
1782 C CA  . ASN A 259 ? 1.9389 0.9532 1.2386 0.1474  -0.3920 0.1658  257 ASN A CA  
1783 C C   . ASN A 259 ? 1.9121 0.9627 1.2318 0.1107  -0.3674 0.1682  257 ASN A C   
1784 O O   . ASN A 259 ? 1.9558 0.9796 1.2503 0.0934  -0.3491 0.1936  257 ASN A O   
1785 C CB  . ASN A 259 ? 2.0121 0.9432 1.2631 0.1527  -0.3894 0.1968  257 ASN A CB  
1786 C CG  . ASN A 259 ? 2.0525 0.9382 1.3203 0.1271  -0.3750 0.2042  257 ASN A CG  
1787 O OD1 . ASN A 259 ? 2.0351 0.9491 1.3467 0.1089  -0.3715 0.1830  257 ASN A OD1 
1788 N ND2 . ASN A 259 ? 2.1093 0.9220 1.3420 0.1259  -0.3675 0.2347  257 ASN A ND2 
1789 N N   . ILE A 260 ? 1.8660 0.9771 1.2310 0.1003  -0.3654 0.1431  258 ILE A N   
1790 C CA  . ILE A 260 ? 1.8054 0.9517 1.1936 0.0670  -0.3447 0.1426  258 ILE A CA  
1791 C C   . ILE A 260 ? 1.7327 0.8562 1.1462 0.0463  -0.3379 0.1364  258 ILE A C   
1792 O O   . ILE A 260 ? 1.7299 0.8483 1.1587 0.0590  -0.3501 0.1164  258 ILE A O   
1793 C CB  . ILE A 260 ? 1.7042 0.9269 1.1237 0.0674  -0.3464 0.1210  258 ILE A CB  
1794 C CG1 . ILE A 260 ? 1.6249 0.8786 1.0578 0.0358  -0.3255 0.1258  258 ILE A CG1 
1795 C CG2 . ILE A 260 ? 1.6988 0.9479 1.1547 0.0773  -0.3540 0.0941  258 ILE A CG2 
1796 C CD1 . ILE A 260 ? 1.5910 0.9151 1.0548 0.0334  -0.3253 0.1071  258 ILE A CD1 
1797 N N   . SER A 261 ? 1.7662 0.8743 1.1847 0.0161  -0.3194 0.1531  259 SER A N   
1798 C CA  . SER A 261 ? 1.7264 0.8149 1.1750 -0.0069 -0.3164 0.1463  259 SER A CA  
1799 C C   . SER A 261 ? 1.6760 0.8070 1.1537 -0.0039 -0.3257 0.1132  259 SER A C   
1800 O O   . SER A 261 ? 1.6522 0.8424 1.1398 0.0005  -0.3233 0.1009  259 SER A O   
1801 C CB  . SER A 261 ? 1.6643 0.7577 1.1293 -0.0412 -0.2941 0.1649  259 SER A CB  
1802 O OG  . SER A 261 ? 1.6538 0.7425 1.1575 -0.0645 -0.2957 0.1528  259 SER A OG  
1803 N N   . ASP A 262 ? 1.6849 0.6413 1.0837 0.1807  -0.2768 0.0341  260 ASP A N   
1804 C CA  . ASP A 262 ? 1.5606 0.5758 1.0346 0.1943  -0.2652 0.0180  260 ASP A CA  
1805 C C   . ASP A 262 ? 1.5208 0.5794 1.0272 0.1669  -0.2429 0.0124  260 ASP A C   
1806 O O   . ASP A 262 ? 1.4679 0.5913 1.0441 0.1792  -0.2365 -0.0008 260 ASP A O   
1807 C CB  . ASP A 262 ? 1.5780 0.5596 1.0371 0.1954  -0.2518 0.0125  260 ASP A CB  
1808 C CG  . ASP A 262 ? 1.6625 0.6320 1.1283 0.2372  -0.2722 0.0097  260 ASP A CG  
1809 O OD1 . ASP A 262 ? 1.6933 0.7221 1.2258 0.2700  -0.2828 0.0011  260 ASP A OD1 
1810 O OD2 . ASP A 262 ? 1.7129 0.6154 1.1197 0.2367  -0.2769 0.0160  260 ASP A OD2 
1811 N N   . GLU A 263 ? 1.5488 0.5782 1.0077 0.1291  -0.2284 0.0221  261 GLU A N   
1812 C CA  . GLU A 263 ? 1.4289 0.5259 0.9274 0.0976  -0.2011 0.0156  261 GLU A CA  
1813 C C   . GLU A 263 ? 1.3659 0.5432 0.9237 0.1099  -0.2095 0.0097  261 GLU A C   
1814 O O   . GLU A 263 ? 1.3316 0.5777 0.9395 0.0942  -0.1900 0.0008  261 GLU A O   
1815 C CB  . GLU A 263 ? 1.4512 0.5094 0.8902 0.0568  -0.1825 0.0282  261 GLU A CB  
1816 C CG  . GLU A 263 ? 1.4808 0.5990 0.9561 0.0218  -0.1510 0.0215  261 GLU A CG  
1817 C CD  . GLU A 263 ? 1.5355 0.6159 0.9559 -0.0172 -0.1303 0.0346  261 GLU A CD  
1818 O OE1 . GLU A 263 ? 1.5046 0.5060 0.8527 -0.0185 -0.1391 0.0496  261 GLU A OE1 
1819 O OE2 . GLU A 263 ? 1.5856 0.7150 1.0353 -0.0460 -0.1047 0.0305  261 GLU A OE2 
1820 N N   . PHE A 264 ? 1.4413 0.6076 0.9925 0.1374  -0.2405 0.0147  262 PHE A N   
1821 C CA  . PHE A 264 ? 1.3867 0.6192 0.9875 0.1473  -0.2546 0.0102  262 PHE A CA  
1822 C C   . PHE A 264 ? 1.3477 0.6133 1.0074 0.1878  -0.2808 0.0034  262 PHE A C   
1823 O O   . PHE A 264 ? 1.2870 0.6050 0.9921 0.1982  -0.2987 0.0001  262 PHE A O   
1824 C CB  . PHE A 264 ? 1.3700 0.5624 0.9081 0.1394  -0.2710 0.0222  262 PHE A CB  
1825 C CG  . PHE A 264 ? 1.3952 0.5699 0.8857 0.1003  -0.2410 0.0283  262 PHE A CG  
1826 C CD1 . PHE A 264 ? 1.2455 0.4836 0.7717 0.0809  -0.2221 0.0212  262 PHE A CD1 
1827 C CD2 . PHE A 264 ? 1.4510 0.5454 0.8626 0.0831  -0.2306 0.0413  262 PHE A CD2 
1828 C CE1 . PHE A 264 ? 1.2582 0.4856 0.7465 0.0483  -0.1930 0.0261  262 PHE A CE1 
1829 C CE2 . PHE A 264 ? 1.4572 0.5426 0.8327 0.0466  -0.1997 0.0473  262 PHE A CE2 
1830 C CZ  . PHE A 264 ? 1.3381 0.4929 0.7544 0.0307  -0.1807 0.0392  262 PHE A CZ  
1831 N N   . SER A 265 ? 1.2810 0.5178 0.9426 0.2109  -0.2828 0.0006  263 SER A N   
1832 C CA  . SER A 265 ? 1.2542 0.5203 0.9717 0.2537  -0.3062 -0.0053 263 SER A CA  
1833 C C   . SER A 265 ? 1.1595 0.5269 0.9741 0.2573  -0.2921 -0.0185 263 SER A C   
1834 O O   . SER A 265 ? 1.1981 0.6137 1.0747 0.2856  -0.3124 -0.0223 263 SER A O   
1835 C CB  . SER A 265 ? 1.3661 0.5870 1.0613 0.2730  -0.3021 -0.0069 263 SER A CB  
1836 O OG  . SER A 265 ? 1.4433 0.6567 1.1362 0.2568  -0.2702 -0.0145 263 SER A OG  
1837 N N   . SER A 266 ? 1.1093 0.5101 0.9398 0.2290  -0.2581 -0.0251 264 SER A N   
1838 C CA  . SER A 266 ? 1.1231 0.6111 1.0370 0.2316  -0.2420 -0.0363 264 SER A CA  
1839 C C   . SER A 266 ? 1.1352 0.6817 1.0926 0.2251  -0.2568 -0.0354 264 SER A C   
1840 O O   . SER A 266 ? 1.1051 0.7234 1.1382 0.2328  -0.2518 -0.0426 264 SER A O   
1841 C CB  . SER A 266 ? 1.0864 0.5872 0.9970 0.2032  -0.2057 -0.0427 264 SER A CB  
1842 O OG  . SER A 266 ? 1.2096 0.6868 1.0720 0.1683  -0.1981 -0.0363 264 SER A OG  
1843 N N   . ASN A 267 ? 1.1240 0.6379 1.0318 0.2099  -0.2739 -0.0268 265 ASN A N   
1844 C CA  . ASN A 267 ? 1.0617 0.6191 0.9971 0.2004  -0.2890 -0.0269 265 ASN A CA  
1845 C C   . ASN A 267 ? 1.0493 0.6014 0.9941 0.2261  -0.3333 -0.0228 265 ASN A C   
1846 O O   . ASN A 267 ? 1.1291 0.7039 1.0848 0.2180  -0.3531 -0.0226 265 ASN A O   
1847 C CB  . ASN A 267 ? 1.0820 0.6091 0.9551 0.1678  -0.2781 -0.0219 265 ASN A CB  
1848 C CG  . ASN A 267 ? 1.1000 0.6505 0.9805 0.1415  -0.2384 -0.0273 265 ASN A CG  
1849 O OD1 . ASN A 267 ? 1.0099 0.6221 0.9525 0.1391  -0.2238 -0.0357 265 ASN A OD1 
1850 N ND2 . ASN A 267 ? 1.1250 0.6262 0.9423 0.1209  -0.2213 -0.0218 265 ASN A ND2 
1851 N N   . VAL A 268 ? 1.0720 0.5922 1.0115 0.2579  -0.3519 -0.0201 266 VAL A N   
1852 C CA  . VAL A 268 ? 1.1427 0.6511 1.0842 0.2839  -0.3992 -0.0152 266 VAL A CA  
1853 C C   . VAL A 268 ? 1.1010 0.7007 1.1443 0.2934  -0.4151 -0.0228 266 VAL A C   
1854 O O   . VAL A 268 ? 1.0924 0.7010 1.1409 0.2936  -0.4510 -0.0207 266 VAL A O   
1855 C CB  . VAL A 268 ? 1.2090 0.6672 1.1239 0.3159  -0.4122 -0.0113 266 VAL A CB  
1856 C CG1 . VAL A 268 ? 1.3461 0.7061 1.1529 0.3011  -0.4011 -0.0015 266 VAL A CG1 
1857 C CG2 . VAL A 268 ? 1.2324 0.7394 1.2177 0.3362  -0.3882 -0.0211 266 VAL A CG2 
1858 N N   . ALA A 269 ? 1.0451 0.7115 1.1689 0.3005  -0.3890 -0.0315 267 ALA A N   
1859 C CA  . ALA A 269 ? 0.9817 0.7378 1.2075 0.3066  -0.4003 -0.0375 267 ALA A CA  
1860 C C   . ALA A 269 ? 1.0118 0.7957 1.2421 0.2712  -0.4005 -0.0386 267 ALA A C   
1861 O O   . ALA A 269 ? 1.0431 0.8736 1.3281 0.2712  -0.4292 -0.0402 267 ALA A O   
1862 C CB  . ALA A 269 ? 0.8824 0.6994 1.1837 0.3179  -0.3641 -0.0457 267 ALA A CB  
1863 N N   . ASN A 270 ? 0.9890 0.7435 1.1624 0.2414  -0.3704 -0.0382 268 ASN A N   
1864 C CA  . ASN A 270 ? 1.0059 0.7737 1.1694 0.2106  -0.3705 -0.0394 268 ASN A CA  
1865 C C   . ASN A 270 ? 1.0487 0.7573 1.1394 0.2080  -0.4072 -0.0332 268 ASN A C   
1866 O O   . ASN A 270 ? 1.0156 0.7406 1.1152 0.1957  -0.4293 -0.0354 268 ASN A O   
1867 C CB  . ASN A 270 ? 0.9782 0.7375 1.1094 0.1837  -0.3262 -0.0415 268 ASN A CB  
1868 C CG  . ASN A 270 ? 0.9009 0.7230 1.1028 0.1812  -0.2929 -0.0483 268 ASN A CG  
1869 O OD1 . ASN A 270 ? 0.9122 0.7913 1.1922 0.1953  -0.2991 -0.0514 268 ASN A OD1 
1870 N ND2 . ASN A 270 ? 0.8617 0.6740 1.0362 0.1632  -0.2571 -0.0503 268 ASN A ND2 
1871 N N   . TYR A 271 ? 1.0669 0.7006 1.0789 0.2187  -0.4138 -0.0254 269 TYR A N   
1872 C CA  . TYR A 271 ? 1.1154 0.6831 1.0454 0.2173  -0.4463 -0.0181 269 TYR A CA  
1873 C C   . TYR A 271 ? 1.2276 0.8132 1.1941 0.2394  -0.5001 -0.0184 269 TYR A C   
1874 O O   . TYR A 271 ? 1.3349 0.8804 1.2461 0.2353  -0.5329 -0.0153 269 TYR A O   
1875 C CB  . TYR A 271 ? 1.1559 0.6373 0.9960 0.2249  -0.4413 -0.0079 269 TYR A CB  
1876 C CG  . TYR A 271 ? 1.1751 0.6257 0.9603 0.1965  -0.3959 -0.0056 269 TYR A CG  
1877 C CD1 . TYR A 271 ? 1.1382 0.6170 0.9255 0.1678  -0.3720 -0.0106 269 TYR A CD1 
1878 C CD2 . TYR A 271 ? 1.1867 0.5797 0.9200 0.1985  -0.3783 0.0013  269 TYR A CD2 
1879 C CE1 . TYR A 271 ? 1.1581 0.6160 0.9036 0.1434  -0.3320 -0.0088 269 TYR A CE1 
1880 C CE2 . TYR A 271 ? 1.1919 0.5625 0.8831 0.1702  -0.3387 0.0033  269 TYR A CE2 
1881 C CZ  . TYR A 271 ? 1.1881 0.5952 0.8890 0.1435  -0.3158 -0.0018 269 TYR A CZ  
1882 O OH  . TYR A 271 ? 1.2449 0.6372 0.9126 0.1168  -0.2777 -0.0001 269 TYR A OH  
1883 N N   . GLN A 272 ? 1.1610 0.8071 1.2204 0.2631  -0.5097 -0.0227 270 GLN A N   
1884 C CA  . GLN A 272 ? 1.1327 0.8153 1.2401 0.2745  -0.5456 -0.0261 270 GLN A CA  
1885 C C   . GLN A 272 ? 1.0807 0.8306 1.2563 0.2537  -0.5544 -0.0335 270 GLN A C   
1886 O O   . GLN A 272 ? 1.1121 0.8609 1.2834 0.2478  -0.5882 -0.0355 270 GLN A O   
1887 C CB  . GLN A 272 ? 1.1256 0.8507 1.3015 0.3025  -0.5382 -0.0283 270 GLN A CB  
1888 C CG  . GLN A 272 ? 1.1278 0.7804 1.2328 0.3245  -0.5400 -0.0216 270 GLN A CG  
1889 C CD  . GLN A 272 ? 1.1613 0.8538 1.3305 0.3534  -0.5257 -0.0246 270 GLN A CD  
1890 O OE1 . GLN A 272 ? 1.1494 0.9260 1.4165 0.3569  -0.5106 -0.0311 270 GLN A OE1 
1891 N NE2 . GLN A 272 ? 1.1738 0.8035 1.2845 0.3736  -0.5282 -0.0195 270 GLN A NE2 
1892 N N   . LYS A 273 ? 0.9934 0.7985 1.2302 0.2415  -0.5237 -0.0378 271 LYS A N   
1893 C CA  . LYS A 273 ? 0.9598 0.8256 1.2593 0.2178  -0.5274 -0.0443 271 LYS A CA  
1894 C C   . LYS A 273 ? 1.0138 0.8278 1.2359 0.1960  -0.5495 -0.0443 271 LYS A C   
1895 O O   . LYS A 273 ? 1.0513 0.8873 1.2975 0.1806  -0.5715 -0.0493 271 LYS A O   
1896 C CB  . LYS A 273 ? 0.8564 0.7740 1.2085 0.2028  -0.4779 -0.0483 271 LYS A CB  
1897 C CG  . LYS A 273 ? 0.9216 0.9177 1.3673 0.1847  -0.4786 -0.0537 271 LYS A CG  
1898 C CD  . LYS A 273 ? 0.8073 0.8460 1.2937 0.1727  -0.4234 -0.0562 271 LYS A CD  
1899 C CE  . LYS A 273 ? 0.8250 0.9504 1.4223 0.1632  -0.4204 -0.0592 271 LYS A CE  
1900 N NZ  . LYS A 273 ? 0.7211 0.8837 1.3540 0.1583  -0.3661 -0.0603 271 LYS A NZ  
1901 N N   . VAL A 274 ? 1.0405 0.7828 1.1611 0.1880  -0.5283 -0.0400 272 VAL A N   
1902 C CA  . VAL A 274 ? 1.0618 0.7476 1.0955 0.1690  -0.5401 -0.0403 272 VAL A CA  
1903 C C   . VAL A 274 ? 1.1682 0.8209 1.1717 0.1803  -0.5963 -0.0393 272 VAL A C   
1904 O O   . VAL A 274 ? 1.0957 0.7328 1.0709 0.1633  -0.6141 -0.0446 272 VAL A O   
1905 C CB  . VAL A 274 ? 1.0482 0.6646 0.9819 0.1621  -0.5048 -0.0341 272 VAL A CB  
1906 C CG1 . VAL A 274 ? 1.1230 0.6691 0.9542 0.1513  -0.5217 -0.0325 272 VAL A CG1 
1907 C CG2 . VAL A 274 ? 1.0490 0.6996 1.0083 0.1430  -0.4497 -0.0379 272 VAL A CG2 
1908 N N   . GLY A 275 ? 1.1526 0.7925 1.1578 0.2039  -0.6106 -0.0352 273 GLY A N   
1909 C CA  . GLY A 275 ? 1.1750 0.7809 1.1459 0.2111  -0.6502 -0.0358 273 GLY A CA  
1910 C C   . GLY A 275 ? 1.1602 0.8375 1.2295 0.2104  -0.6747 -0.0431 273 GLY A C   
1911 O O   . GLY A 275 ? 1.2675 0.9203 1.3125 0.2106  -0.7108 -0.0454 273 GLY A O   
1912 N N   . MET A 276 ? 1.0808 0.8444 1.2590 0.2086  -0.6542 -0.0465 274 MET A N   
1913 C CA  . MET A 276 ? 1.1128 0.9524 1.3930 0.2059  -0.6704 -0.0515 274 MET A CA  
1914 C C   . MET A 276 ? 1.1432 1.0194 1.4610 0.1740  -0.6643 -0.0575 274 MET A C   
1915 O O   . MET A 276 ? 1.1032 1.0539 1.5179 0.1660  -0.6642 -0.0604 274 MET A O   
1916 C CB  . MET A 276 ? 1.0489 0.9604 1.4245 0.2254  -0.6477 -0.0502 274 MET A CB  
1917 C CG  . MET A 276 ? 1.1278 1.0035 1.4703 0.2588  -0.6529 -0.0449 274 MET A CG  
1918 S SD  . MET A 276 ? 1.1950 1.1591 1.6564 0.2861  -0.6489 -0.0454 274 MET A SD  
1919 C CE  . MET A 276 ? 1.0006 1.0501 1.5557 0.2689  -0.5983 -0.0489 274 MET A CE  
1920 N N   . GLN A 277 ? 1.1217 0.9446 1.3612 0.1557  -0.6578 -0.0588 275 GLN A N   
1921 C CA  . GLN A 277 ? 1.0919 0.9364 1.3517 0.1260  -0.6493 -0.0647 275 GLN A CA  
1922 C C   . GLN A 277 ? 1.1690 0.9300 1.3147 0.1142  -0.6610 -0.0668 275 GLN A C   
1923 O O   . GLN A 277 ? 1.2232 0.9162 1.2761 0.1261  -0.6605 -0.0624 275 GLN A O   
1924 C CB  . GLN A 277 ? 1.0568 0.9480 1.3652 0.1163  -0.6056 -0.0649 275 GLN A CB  
1925 C CG  . GLN A 277 ? 1.0039 0.9836 1.4298 0.1225  -0.5864 -0.0640 275 GLN A CG  
1926 C CD  . GLN A 277 ? 0.9578 0.9775 1.4247 0.1100  -0.5427 -0.0649 275 GLN A CD  
1927 O OE1 . GLN A 277 ? 1.0159 1.0014 1.4292 0.0955  -0.5299 -0.0669 275 GLN A OE1 
1928 N NE2 . GLN A 277 ? 0.9404 1.0317 1.4999 0.1165  -0.5183 -0.0636 275 GLN A NE2 
1929 N N   . LYS A 278 ? 1.1511 0.9145 1.3006 0.0908  -0.6686 -0.0731 276 LYS A N   
1930 C CA  . LYS A 278 ? 1.1613 0.8458 1.2024 0.0807  -0.6755 -0.0764 276 LYS A CA  
1931 C C   . LYS A 278 ? 1.1292 0.7913 1.1193 0.0737  -0.6378 -0.0766 276 LYS A C   
1932 O O   . LYS A 278 ? 1.2167 0.8099 1.1053 0.0806  -0.6324 -0.0740 276 LYS A O   
1933 C CB  . LYS A 278 ? 1.2110 0.9029 1.2720 0.0593  -0.6937 -0.0833 276 LYS A CB  
1934 C CG  . LYS A 278 ? 1.2685 0.8782 1.2194 0.0508  -0.7014 -0.0879 276 LYS A CG  
1935 C CD  . LYS A 278 ? 1.3088 0.8435 1.1675 0.0685  -0.7293 -0.0852 276 LYS A CD  
1936 C CE  . LYS A 278 ? 1.4260 0.8876 1.1911 0.0594  -0.7410 -0.0908 276 LYS A CE  
1937 N NZ  . LYS A 278 ? 1.5502 0.9273 1.2071 0.0757  -0.7589 -0.0876 276 LYS A NZ  
1938 N N   . TYR A 279 ? 1.0025 0.7215 1.0605 0.0593  -0.6098 -0.0794 277 TYR A N   
1939 C CA  . TYR A 279 ? 0.9925 0.7007 1.0159 0.0530  -0.5744 -0.0808 277 TYR A CA  
1940 C C   . TYR A 279 ? 0.9541 0.7309 1.0651 0.0572  -0.5376 -0.0763 277 TYR A C   
1941 O O   . TYR A 279 ? 0.9838 0.8250 1.1921 0.0591  -0.5507 -0.0761 277 TYR A O   
1942 C CB  . TYR A 279 ? 0.9461 0.6410 0.9463 0.0295  -0.5605 -0.0895 277 TYR A CB  
1943 C CG  . TYR A 279 ? 0.9458 0.7043 1.0421 0.0111  -0.5551 -0.0923 277 TYR A CG  
1944 C CD1 . TYR A 279 ? 0.9143 0.7287 1.0789 0.0036  -0.5216 -0.0918 277 TYR A CD1 
1945 C CD2 . TYR A 279 ? 1.0639 0.8219 1.1769 -0.0001 -0.5809 -0.0946 277 TYR A CD2 
1946 C CE1 . TYR A 279 ? 0.9359 0.8031 1.1811 -0.0148 -0.5139 -0.0925 277 TYR A CE1 
1947 C CE2 . TYR A 279 ? 1.0065 0.8187 1.2018 -0.0196 -0.5740 -0.0955 277 TYR A CE2 
1948 C CZ  . TYR A 279 ? 0.9971 0.8628 1.2564 -0.0270 -0.5390 -0.0938 277 TYR A CZ  
1949 O OH  . TYR A 279 ? 0.9861 0.9008 1.3204 -0.0474 -0.5288 -0.0929 277 TYR A OH  
1950 N N   . SER A 280 ? 0.9320 0.6942 1.0069 0.0589  -0.4896 -0.0728 278 SER A N   
1951 C CA  . SER A 280 ? 0.9030 0.7170 1.0426 0.0640  -0.4514 -0.0691 278 SER A CA  
1952 C C   . SER A 280 ? 0.8119 0.6235 0.9287 0.0500  -0.4016 -0.0707 278 SER A C   
1953 O O   . SER A 280 ? 0.8731 0.6341 0.9101 0.0447  -0.3900 -0.0717 278 SER A O   
1954 C CB  . SER A 280 ? 0.8989 0.6947 1.0213 0.0884  -0.4528 -0.0616 278 SER A CB  
1955 O OG  . SER A 280 ? 1.0132 0.7335 1.0304 0.0916  -0.4541 -0.0579 278 SER A OG  
1956 N N   . THR A 281 ? 0.7527 0.6197 0.9395 0.0452  -0.3720 -0.0708 279 THR A N   
1957 C CA  . THR A 281 ? 0.8084 0.6793 0.9832 0.0333  -0.3283 -0.0723 279 THR A CA  
1958 C C   . THR A 281 ? 0.7756 0.6597 0.9610 0.0441  -0.2948 -0.0682 279 THR A C   
1959 O O   . THR A 281 ? 0.7219 0.6464 0.9692 0.0545  -0.2926 -0.0663 279 THR A O   
1960 C CB  . THR A 281 ? 0.6860 0.6007 0.9217 0.0163  -0.3213 -0.0758 279 THR A CB  
1961 O OG1 . THR A 281 ? 0.8185 0.7913 1.1412 0.0216  -0.3233 -0.0731 279 THR A OG1 
1962 C CG2 . THR A 281 ? 0.7669 0.6602 0.9851 0.0026  -0.3546 -0.0813 279 THR A CG2 
1963 N N   . LEU A 282 ? 0.7011 0.5525 0.8283 0.0413  -0.2682 -0.0674 280 LEU A N   
1964 C CA  . LEU A 282 ? 0.7325 0.5900 0.8628 0.0477  -0.2376 -0.0647 280 LEU A CA  
1965 C C   . LEU A 282 ? 0.6966 0.5665 0.8246 0.0347  -0.2024 -0.0677 280 LEU A C   
1966 O O   . LEU A 282 ? 0.6618 0.5047 0.7402 0.0260  -0.1930 -0.0691 280 LEU A O   
1967 C CB  . LEU A 282 ? 0.7538 0.5595 0.8191 0.0560  -0.2403 -0.0598 280 LEU A CB  
1968 C CG  . LEU A 282 ? 0.8050 0.6027 0.8575 0.0580  -0.2104 -0.0575 280 LEU A CG  
1969 C CD1 . LEU A 282 ? 0.8270 0.6579 0.9374 0.0726  -0.2069 -0.0579 280 LEU A CD1 
1970 C CD2 . LEU A 282 ? 0.8591 0.5985 0.8407 0.0605  -0.2136 -0.0513 280 LEU A CD2 
1971 N N   . GLN A 283 ? 0.6475 0.5575 0.8271 0.0348  -0.1827 -0.0685 281 GLN A N   
1972 C CA  . GLN A 283 ? 0.6348 0.5527 0.8081 0.0252  -0.1521 -0.0707 281 GLN A CA  
1973 C C   . GLN A 283 ? 0.5973 0.4972 0.7430 0.0306  -0.1342 -0.0694 281 GLN A C   
1974 O O   . GLN A 283 ? 0.6211 0.5292 0.7884 0.0422  -0.1307 -0.0683 281 GLN A O   
1975 C CB  . GLN A 283 ? 0.5840 0.5443 0.8128 0.0216  -0.1375 -0.0716 281 GLN A CB  
1976 C CG  . GLN A 283 ? 0.5264 0.4875 0.7390 0.0129  -0.1108 -0.0736 281 GLN A CG  
1977 C CD  . GLN A 283 ? 0.5685 0.5609 0.8224 0.0067  -0.0977 -0.0732 281 GLN A CD  
1978 O OE1 . GLN A 283 ? 0.4911 0.5096 0.7915 0.0063  -0.1054 -0.0711 281 GLN A OE1 
1979 N NE2 . GLN A 283 ? 0.5301 0.5202 0.7676 0.0013  -0.0779 -0.0744 281 GLN A NE2 
1980 N N   . GLY A 284 ? 0.6470 0.5223 0.7464 0.0223  -0.1227 -0.0699 282 GLY A N   
1981 C CA  . GLY A 284 ? 0.5912 0.4473 0.6634 0.0220  -0.1074 -0.0684 282 GLY A CA  
1982 C C   . GLY A 284 ? 0.5691 0.4385 0.6396 0.0117  -0.0838 -0.0718 282 GLY A C   
1983 O O   . GLY A 284 ? 0.5786 0.4385 0.6211 0.0028  -0.0766 -0.0726 282 GLY A O   
1984 N N   . PRO A 285 ? 0.5277 0.4193 0.6272 0.0141  -0.0714 -0.0742 283 PRO A N   
1985 C CA  . PRO A 285 ? 0.5338 0.4348 0.6288 0.0059  -0.0530 -0.0776 283 PRO A CA  
1986 C C   . PRO A 285 ? 0.5233 0.4019 0.5842 -0.0024 -0.0464 -0.0768 283 PRO A C   
1987 O O   . PRO A 285 ? 0.5535 0.4038 0.5911 -0.0012 -0.0532 -0.0729 283 PRO A O   
1988 C CB  . PRO A 285 ? 0.4878 0.4029 0.6077 0.0131  -0.0440 -0.0795 283 PRO A CB  
1989 C CG  . PRO A 285 ? 0.5142 0.4458 0.6679 0.0222  -0.0536 -0.0775 283 PRO A CG  
1990 C CD  . PRO A 285 ? 0.5571 0.4672 0.6948 0.0257  -0.0731 -0.0743 283 PRO A CD  
1991 N N   . PRO A 286 ? 0.5000 0.3903 0.5582 -0.0115 -0.0339 -0.0799 284 PRO A N   
1992 C CA  . PRO A 286 ? 0.5449 0.4215 0.5791 -0.0233 -0.0261 -0.0788 284 PRO A CA  
1993 C C   . PRO A 286 ? 0.5659 0.4162 0.5866 -0.0250 -0.0271 -0.0772 284 PRO A C   
1994 O O   . PRO A 286 ? 0.5334 0.3845 0.5661 -0.0183 -0.0273 -0.0804 284 PRO A O   
1995 C CB  . PRO A 286 ? 0.4971 0.4011 0.5461 -0.0294 -0.0158 -0.0838 284 PRO A CB  
1996 C CG  . PRO A 286 ? 0.4697 0.3922 0.5358 -0.0210 -0.0187 -0.0857 284 PRO A CG  
1997 C CD  . PRO A 286 ? 0.4724 0.3894 0.5507 -0.0117 -0.0270 -0.0839 284 PRO A CD  
1998 N N   . GLY A 287 ? 0.6109 0.4325 0.6012 -0.0337 -0.0268 -0.0719 285 GLY A N   
1999 C CA  . GLY A 287 ? 0.6181 0.4054 0.5877 -0.0384 -0.0277 -0.0696 285 GLY A CA  
2000 C C   . GLY A 287 ? 0.6451 0.4069 0.6099 -0.0208 -0.0408 -0.0680 285 GLY A C   
2001 O O   . GLY A 287 ? 0.6553 0.3872 0.6052 -0.0202 -0.0420 -0.0683 285 GLY A O   
2002 N N   . THR A 288 ? 0.6230 0.3955 0.6015 -0.0061 -0.0518 -0.0667 286 THR A N   
2003 C CA  . THR A 288 ? 0.6398 0.3994 0.6263 0.0136  -0.0654 -0.0657 286 THR A CA  
2004 C C   . THR A 288 ? 0.6990 0.4161 0.6495 0.0185  -0.0809 -0.0578 286 THR A C   
2005 O O   . THR A 288 ? 0.7450 0.4480 0.7006 0.0373  -0.0952 -0.0565 286 THR A O   
2006 C CB  . THR A 288 ? 0.6175 0.4174 0.6476 0.0257  -0.0708 -0.0686 286 THR A CB  
2007 O OG1 . THR A 288 ? 0.6044 0.4147 0.6315 0.0190  -0.0768 -0.0667 286 THR A OG1 
2008 C CG2 . THR A 288 ? 0.5656 0.3977 0.6245 0.0244  -0.0554 -0.0750 286 THR A CG2 
2009 N N   . GLY A 289 ? 0.7575 0.4539 0.6711 0.0036  -0.0779 -0.0523 287 GLY A N   
2010 C CA  . GLY A 289 ? 0.7829 0.4295 0.6494 0.0063  -0.0909 -0.0434 287 GLY A CA  
2011 C C   . GLY A 289 ? 0.8202 0.4668 0.6780 0.0147  -0.1086 -0.0408 287 GLY A C   
2012 O O   . GLY A 289 ? 0.8942 0.5145 0.7386 0.0306  -0.1315 -0.0365 287 GLY A O   
2013 N N   . LYS A 290 ? 0.7768 0.4496 0.6398 0.0052  -0.1004 -0.0440 288 LYS A N   
2014 C CA  . LYS A 290 ? 0.8369 0.5032 0.6844 0.0115  -0.1186 -0.0431 288 LYS A CA  
2015 C C   . LYS A 290 ? 0.8969 0.5062 0.6737 0.0075  -0.1227 -0.0341 288 LYS A C   
2016 O O   . LYS A 290 ? 0.9207 0.4983 0.6713 0.0201  -0.1489 -0.0297 288 LYS A O   
2017 C CB  . LYS A 290 ? 0.7625 0.4652 0.6294 0.0040  -0.1080 -0.0501 288 LYS A CB  
2018 C CG  . LYS A 290 ? 0.7128 0.4650 0.6424 0.0087  -0.1079 -0.0573 288 LYS A CG  
2019 C CD  . LYS A 290 ? 0.6701 0.4473 0.6094 0.0018  -0.0989 -0.0632 288 LYS A CD  
2020 C CE  . LYS A 290 ? 0.6611 0.4484 0.5929 -0.0101 -0.0719 -0.0648 288 LYS A CE  
2021 N NZ  . LYS A 290 ? 0.6208 0.4336 0.5884 -0.0120 -0.0605 -0.0671 288 LYS A NZ  
2022 N N   . SER A 291 ? 0.9345 0.5307 0.6796 -0.0104 -0.0969 -0.0307 289 SER A N   
2023 C CA  . SER A 291 ? 0.9738 0.5129 0.6466 -0.0169 -0.0944 -0.0204 289 SER A CA  
2024 C C   . SER A 291 ? 1.0927 0.5809 0.7358 -0.0079 -0.1128 -0.0115 289 SER A C   
2025 O O   . SER A 291 ? 1.1060 0.5415 0.6906 -0.0015 -0.1293 -0.0032 289 SER A O   
2026 C CB  . SER A 291 ? 1.0889 0.6314 0.7464 -0.0399 -0.0591 -0.0176 289 SER A CB  
2027 O OG  . SER A 291 ? 1.2032 0.7932 0.8898 -0.0439 -0.0431 -0.0263 289 SER A OG  
2028 N N   . HIS A 292 ? 1.0267 0.5253 0.7049 -0.0054 -0.1115 -0.0135 290 HIS A N   
2029 C CA  . HIS A 292 ? 0.9999 0.4483 0.6521 0.0069  -0.1292 -0.0065 290 HIS A CA  
2030 C C   . HIS A 292 ? 1.0515 0.4949 0.7106 0.0339  -0.1650 -0.0069 290 HIS A C   
2031 O O   . HIS A 292 ? 1.1815 0.5682 0.7908 0.0453  -0.1862 0.0022  290 HIS A O   
2032 C CB  . HIS A 292 ? 1.0518 0.5155 0.7430 0.0072  -0.1204 -0.0119 290 HIS A CB  
2033 C CG  . HIS A 292 ? 1.1021 0.5025 0.7541 0.0135  -0.1296 -0.0043 290 HIS A CG  
2034 N ND1 . HIS A 292 ? 1.1782 0.5290 0.7804 -0.0090 -0.1136 0.0044  290 HIS A ND1 
2035 C CD2 . HIS A 292 ? 1.1179 0.4953 0.7740 0.0404  -0.1530 -0.0043 290 HIS A CD2 
2036 C CE1 . HIS A 292 ? 1.2800 0.5728 0.8511 0.0031  -0.1279 0.0097  290 HIS A CE1 
2037 N NE2 . HIS A 292 ? 1.2726 0.5808 0.8757 0.0352  -0.1520 0.0041  290 HIS A NE2 
2038 N N   . PHE A 293 ? 1.0021 0.5042 0.7235 0.0436  -0.1734 -0.0168 291 PHE A N   
2039 C CA  . PHE A 293 ? 1.1070 0.6151 0.8465 0.0659  -0.2086 -0.0179 291 PHE A CA  
2040 C C   . PHE A 293 ? 1.0493 0.5176 0.7278 0.0644  -0.2265 -0.0124 291 PHE A C   
2041 O O   . PHE A 293 ? 1.0601 0.4974 0.7170 0.0822  -0.2606 -0.0080 291 PHE A O   
2042 C CB  . PHE A 293 ? 0.9669 0.5474 0.7856 0.0696  -0.2089 -0.0287 291 PHE A CB  
2043 C CG  . PHE A 293 ? 0.9650 0.5631 0.8154 0.0877  -0.2445 -0.0306 291 PHE A CG  
2044 C CD1 . PHE A 293 ? 0.9644 0.5547 0.7918 0.0837  -0.2640 -0.0312 291 PHE A CD1 
2045 C CD2 . PHE A 293 ? 0.9762 0.6011 0.8825 0.1088  -0.2582 -0.0327 291 PHE A CD2 
2046 C CE1 . PHE A 293 ? 1.0204 0.6289 0.8813 0.0977  -0.3007 -0.0335 291 PHE A CE1 
2047 C CE2 . PHE A 293 ? 1.0293 0.6794 0.9760 0.1241  -0.2917 -0.0344 291 PHE A CE2 
2048 C CZ  . PHE A 293 ? 0.9783 0.6205 0.9035 0.1171  -0.3148 -0.0347 291 PHE A CZ  
2049 N N   . ALA A 294 ? 1.0428 0.5099 0.6907 0.0451  -0.2047 -0.0131 292 ALA A N   
2050 C CA  . ALA A 294 ? 1.1300 0.5588 0.7154 0.0445  -0.2188 -0.0101 292 ALA A CA  
2051 C C   . ALA A 294 ? 1.1877 0.5373 0.6876 0.0465  -0.2261 0.0036  292 ALA A C   
2052 O O   . ALA A 294 ? 1.2219 0.5307 0.6813 0.0616  -0.2611 0.0079  292 ALA A O   
2053 C CB  . ALA A 294 ? 1.1155 0.5628 0.6895 0.0263  -0.1887 -0.0152 292 ALA A CB  
2054 N N   . ILE A 295 ? 1.1949 0.5193 0.6644 0.0301  -0.1947 0.0112  293 ILE A N   
2055 C CA  . ILE A 295 ? 1.3846 0.6276 0.7673 0.0281  -0.1973 0.0262  293 ILE A CA  
2056 C C   . ILE A 295 ? 1.3286 0.5387 0.7112 0.0515  -0.2318 0.0313  293 ILE A C   
2057 O O   . ILE A 295 ? 1.3850 0.5234 0.6941 0.0610  -0.2533 0.0428  293 ILE A O   
2058 C CB  . ILE A 295 ? 1.3899 0.6197 0.7508 0.0008  -0.1540 0.0331  293 ILE A CB  
2059 C CG1 . ILE A 295 ? 1.3554 0.6241 0.7226 -0.0180 -0.1206 0.0273  293 ILE A CG1 
2060 C CG2 . ILE A 295 ? 1.4378 0.5779 0.7055 -0.0047 -0.1539 0.0506  293 ILE A CG2 
2061 C CD1 . ILE A 295 ? 1.4134 0.6595 0.7277 -0.0108 -0.1316 0.0264  293 ILE A CD1 
2062 N N   . GLY A 296 ? 1.2654 0.5248 0.7271 0.0635  -0.2377 0.0228  294 GLY A N   
2063 C CA  . GLY A 296 ? 1.2676 0.5010 0.7360 0.0897  -0.2681 0.0261  294 GLY A CA  
2064 C C   . GLY A 296 ? 1.2643 0.4962 0.7353 0.1150  -0.3137 0.0251  294 GLY A C   
2065 O O   . GLY A 296 ? 1.3722 0.5612 0.8206 0.1387  -0.3453 0.0317  294 GLY A O   
2066 N N   . LEU A 297 ? 1.2957 0.5726 0.7946 0.1105  -0.3202 0.0166  295 LEU A N   
2067 C CA  . LEU A 297 ? 1.2450 0.5224 0.7486 0.1304  -0.3667 0.0146  295 LEU A CA  
2068 C C   . LEU A 297 ? 1.3860 0.5730 0.7828 0.1364  -0.3908 0.0272  295 LEU A C   
2069 O O   . LEU A 297 ? 1.3898 0.5543 0.7775 0.1604  -0.4372 0.0297  295 LEU A O   
2070 C CB  . LEU A 297 ? 1.2268 0.5595 0.7695 0.1185  -0.3654 0.0030  295 LEU A CB  
2071 C CG  . LEU A 297 ? 1.3302 0.6879 0.9067 0.1322  -0.4113 -0.0036 295 LEU A CG  
2072 C CD1 . LEU A 297 ? 1.1816 0.5961 0.8540 0.1531  -0.4318 -0.0079 295 LEU A CD1 
2073 C CD2 . LEU A 297 ? 1.2763 0.6735 0.8739 0.1136  -0.3994 -0.0143 295 LEU A CD2 
2074 N N   . ALA A 298 ? 1.4776 0.6123 0.7931 0.1150  -0.3596 0.0357  296 ALA A N   
2075 C CA  . ALA A 298 ? 1.5291 0.5697 0.7307 0.1180  -0.3756 0.0496  296 ALA A CA  
2076 C C   . ALA A 298 ? 1.6450 0.6240 0.8109 0.1331  -0.3889 0.0626  296 ALA A C   
2077 O O   . ALA A 298 ? 1.6606 0.5763 0.7601 0.1487  -0.4218 0.0704  296 ALA A O   
2078 C CB  . ALA A 298 ? 1.5389 0.5479 0.6692 0.0893  -0.3315 0.0550  296 ALA A CB  
2079 N N   . LEU A 299 ? 1.5814 0.5807 0.7914 0.1273  -0.3620 0.0623  297 LEU A N   
2080 C CA  . LEU A 299 ? 1.6150 0.5506 0.7898 0.1419  -0.3734 0.0735  297 LEU A CA  
2081 C C   . LEU A 299 ? 1.6278 0.5943 0.8603 0.1777  -0.4171 0.0651  297 LEU A C   
2082 O O   . LEU A 299 ? 1.7272 0.6537 0.9283 0.1921  -0.4330 0.0684  297 LEU A O   
2083 C CB  . LEU A 299 ? 1.6134 0.5659 0.8222 0.1240  -0.3326 0.0719  297 LEU A CB  
2084 C CG  . LEU A 299 ? 1.6872 0.6180 0.8472 0.0843  -0.2849 0.0789  297 LEU A CG  
2085 C CD1 . LEU A 299 ? 1.5750 0.5164 0.7681 0.0676  -0.2536 0.0771  297 LEU A CD1 
2086 C CD2 . LEU A 299 ? 1.6818 0.5105 0.7209 0.0774  -0.2883 0.0980  297 LEU A CD2 
2087 N N   . TYR A 300 ? 1.5813 0.6232 0.9020 0.1909  -0.4347 0.0537  298 TYR A N   
2088 C CA  . TYR A 300 ? 1.5773 0.6642 0.9661 0.2214  -0.4726 0.0444  298 TYR A CA  
2089 C C   . TYR A 300 ? 1.6276 0.6971 0.9806 0.2288  -0.5120 0.0430  298 TYR A C   
2090 O O   . TYR A 300 ? 1.6473 0.7234 1.0233 0.2524  -0.5444 0.0391  298 TYR A O   
2091 C CB  . TYR A 300 ? 1.3878 0.5680 0.8920 0.2288  -0.4710 0.0326  298 TYR A CB  
2092 C CG  . TYR A 300 ? 1.4057 0.6428 0.9961 0.2587  -0.4956 0.0235  298 TYR A CG  
2093 C CD1 . TYR A 300 ? 1.4283 0.6704 1.0495 0.2749  -0.4808 0.0219  298 TYR A CD1 
2094 C CD2 . TYR A 300 ? 1.4301 0.7171 1.0725 0.2692  -0.5313 0.0159  298 TYR A CD2 
2095 C CE1 . TYR A 300 ? 1.3901 0.6860 1.0898 0.3036  -0.4986 0.0141  298 TYR A CE1 
2096 C CE2 . TYR A 300 ? 1.4372 0.7815 1.1642 0.2947  -0.5496 0.0086  298 TYR A CE2 
2097 C CZ  . TYR A 300 ? 1.4103 0.7597 1.1653 0.3132  -0.5319 0.0081  298 TYR A CZ  
2098 O OH  . TYR A 300 ? 1.3678 0.7756 1.2061 0.3401  -0.5461 0.0014  298 TYR A OH  
2099 N N   . TYR A 301 ? 1.5765 0.6212 0.8713 0.2091  -0.5086 0.0453  299 TYR A N   
2100 C CA  . TYR A 301 ? 1.6894 0.7054 0.9352 0.2121  -0.5421 0.0423  299 TYR A CA  
2101 C C   . TYR A 301 ? 1.7540 0.6806 0.8742 0.1930  -0.5196 0.0537  299 TYR A C   
2102 O O   . TYR A 301 ? 1.7498 0.6643 0.8262 0.1746  -0.5047 0.0537  299 TYR A O   
2103 C CB  . TYR A 301 ? 1.5895 0.6645 0.8879 0.2065  -0.5583 0.0309  299 TYR A CB  
2104 C CG  . TYR A 301 ? 1.5350 0.7038 0.9629 0.2214  -0.5758 0.0201  299 TYR A CG  
2105 C CD1 . TYR A 301 ? 1.5218 0.7129 0.9993 0.2455  -0.6074 0.0158  299 TYR A CD1 
2106 C CD2 . TYR A 301 ? 1.5118 0.7477 1.0130 0.2115  -0.5579 0.0146  299 TYR A CD2 
2107 C CE1 . TYR A 301 ? 1.4460 0.7273 1.0447 0.2577  -0.6170 0.0065  299 TYR A CE1 
2108 C CE2 . TYR A 301 ? 1.3779 0.7012 0.9983 0.2229  -0.5684 0.0049  299 TYR A CE2 
2109 C CZ  . TYR A 301 ? 1.4138 0.7612 1.0835 0.2453  -0.5959 0.0011  299 TYR A CZ  
2110 O OH  . TYR A 301 ? 1.3619 0.7999 1.1518 0.2552  -0.6002 -0.0077 299 TYR A OH  
2111 N N   . PRO A 302 ? 1.8115 0.6744 0.8708 0.1968  -0.5148 0.0630  300 PRO A N   
2112 C CA  . PRO A 302 ? 1.9115 0.6946 0.8590 0.1743  -0.4827 0.0753  300 PRO A CA  
2113 C C   . PRO A 302 ? 1.9803 0.7101 0.8432 0.1718  -0.4989 0.0744  300 PRO A C   
2114 O O   . PRO A 302 ? 2.0449 0.7144 0.8173 0.1519  -0.4675 0.0836  300 PRO A O   
2115 C CB  . PRO A 302 ? 2.0013 0.7367 0.9204 0.1813  -0.4786 0.0840  300 PRO A CB  
2116 C CG  . PRO A 302 ? 1.8834 0.6817 0.9067 0.2080  -0.5023 0.0754  300 PRO A CG  
2117 C CD  . PRO A 302 ? 1.8379 0.6975 0.9255 0.2218  -0.5375 0.0627  300 PRO A CD  
2118 N N   . SER A 303 ? 1.9900 0.7400 0.8809 0.1903  -0.5448 0.0633  301 SER A N   
2119 C CA  . SER A 303 ? 2.0806 0.7763 0.8923 0.1894  -0.5635 0.0605  301 SER A CA  
2120 C C   . SER A 303 ? 2.0357 0.7689 0.8677 0.1797  -0.5652 0.0498  301 SER A C   
2121 O O   . SER A 303 ? 2.1100 0.7958 0.8717 0.1764  -0.5739 0.0467  301 SER A O   
2122 C CB  . SER A 303 ? 2.1451 0.8240 0.9624 0.2158  -0.6169 0.0555  301 SER A CB  
2123 O OG  . SER A 303 ? 2.0651 0.8287 0.9975 0.2314  -0.6499 0.0436  301 SER A OG  
2124 N N   . ALA A 304 ? 1.9221 0.7354 0.8457 0.1756  -0.5569 0.0438  302 ALA A N   
2125 C CA  . ALA A 304 ? 1.9196 0.7742 0.8731 0.1674  -0.5625 0.0321  302 ALA A CA  
2126 C C   . ALA A 304 ? 1.8987 0.7233 0.7800 0.1448  -0.5167 0.0359  302 ALA A C   
2127 O O   . ALA A 304 ? 1.8828 0.6898 0.7327 0.1316  -0.4733 0.0476  302 ALA A O   
2128 C CB  . ALA A 304 ? 1.7529 0.7048 0.8322 0.1709  -0.5692 0.0244  302 ALA A CB  
2129 N N   . ARG A 305 ? 1.9065 0.7269 0.7650 0.1401  -0.5250 0.0255  303 ARG A N   
2130 C CA  . ARG A 305 ? 1.9127 0.7166 0.7146 0.1218  -0.4818 0.0253  303 ARG A CA  
2131 C C   . ARG A 305 ? 1.8172 0.7028 0.7048 0.1140  -0.4704 0.0172  303 ARG A C   
2132 O O   . ARG A 305 ? 1.7976 0.7378 0.7650 0.1206  -0.5050 0.0051  303 ARG A O   
2133 C CB  . ARG A 305 ? 2.0075 0.7639 0.7432 0.1232  -0.4963 0.0167  303 ARG A CB  
2134 C CG  . ARG A 305 ? 2.0462 0.7702 0.7053 0.1083  -0.4473 0.0170  303 ARG A CG  
2135 C CD  . ARG A 305 ? 2.0796 0.7822 0.7100 0.1126  -0.4696 0.0037  303 ARG A CD  
2136 N NE  . ARG A 305 ? 2.1435 0.7996 0.6866 0.1044  -0.4268 0.0038  303 ARG A NE  
2137 C CZ  . ARG A 305 ? 2.0960 0.7823 0.6427 0.0920  -0.3769 0.0019  303 ARG A CZ  
2138 N NH1 . ARG A 305 ? 2.1305 0.8839 0.7501 0.0837  -0.3582 0.0023  303 ARG A NH1 
2139 N NH2 . ARG A 305 ? 2.1612 0.8083 0.6350 0.0889  -0.3431 -0.0005 303 ARG A NH2 
2140 N N   . ILE A 306 ? 1.8094 0.7053 0.6835 0.0986  -0.4215 0.0237  304 ILE A N   
2141 C CA  . ILE A 306 ? 1.7138 0.7011 0.6939 0.0882  -0.3973 0.0119  304 ILE A CA  
2142 C C   . ILE A 306 ? 1.6963 0.6860 0.6420 0.0716  -0.3491 0.0055  304 ILE A C   
2143 O O   . ILE A 306 ? 1.7131 0.6630 0.5909 0.0609  -0.3070 0.0157  304 ILE A O   
2144 C CB  . ILE A 306 ? 1.6033 0.6380 0.6614 0.0837  -0.3706 0.0182  304 ILE A CB  
2145 C CG1 . ILE A 306 ? 1.7158 0.7228 0.7764 0.1032  -0.4103 0.0283  304 ILE A CG1 
2146 C CG2 . ILE A 306 ? 1.5146 0.6470 0.6945 0.0782  -0.3593 0.0041  304 ILE A CG2 
2147 C CD1 . ILE A 306 ? 1.6942 0.7528 0.8406 0.1214  -0.4610 0.0184  304 ILE A CD1 
2148 N N   . VAL A 307 ? 1.5812 0.6166 0.5742 0.0697  -0.3549 -0.0110 305 VAL A N   
2149 C CA  . VAL A 307 ? 1.6247 0.6739 0.6030 0.0579  -0.3102 -0.0197 305 VAL A CA  
2150 C C   . VAL A 307 ? 1.4754 0.6156 0.5698 0.0482  -0.2804 -0.0257 305 VAL A C   
2151 O O   . VAL A 307 ? 1.4088 0.6032 0.5897 0.0515  -0.3062 -0.0340 305 VAL A O   
2152 C CB  . VAL A 307 ? 1.6579 0.6826 0.5958 0.0636  -0.3381 -0.0346 305 VAL A CB  
2153 C CG1 . VAL A 307 ? 1.5834 0.6293 0.5186 0.0553  -0.2913 -0.0454 305 VAL A CG1 
2154 C CG2 . VAL A 307 ? 1.7532 0.6890 0.5822 0.0731  -0.3619 -0.0282 305 VAL A CG2 
2155 N N   . TYR A 308 ? 1.4622 0.6189 0.5586 0.0356  -0.2266 -0.0208 306 TYR A N   
2156 C CA  . TYR A 308 ? 1.4174 0.6542 0.6124 0.0261  -0.1966 -0.0263 306 TYR A CA  
2157 C C   . TYR A 308 ? 1.3117 0.5677 0.5021 0.0225  -0.1677 -0.0385 306 TYR A C   
2158 O O   . TYR A 308 ? 1.3547 0.5790 0.4785 0.0185  -0.1334 -0.0358 306 TYR A O   
2159 C CB  . TYR A 308 ? 1.4066 0.6511 0.6125 0.0141  -0.1606 -0.0137 306 TYR A CB  
2160 C CG  . TYR A 308 ? 1.4559 0.6850 0.6764 0.0199  -0.1877 -0.0033 306 TYR A CG  
2161 C CD1 . TYR A 308 ? 1.3716 0.6568 0.6857 0.0250  -0.2043 -0.0080 306 TYR A CD1 
2162 C CD2 . TYR A 308 ? 1.4563 0.6105 0.5923 0.0220  -0.1956 0.0115  306 TYR A CD2 
2163 C CE1 . TYR A 308 ? 1.3110 0.5811 0.6377 0.0343  -0.2275 0.0002  306 TYR A CE1 
2164 C CE2 . TYR A 308 ? 1.5094 0.6444 0.6556 0.0308  -0.2216 0.0206  306 TYR A CE2 
2165 C CZ  . TYR A 308 ? 1.4545 0.6490 0.6979 0.0381  -0.2373 0.0142  306 TYR A CZ  
2166 O OH  . TYR A 308 ? 1.3935 0.5681 0.6467 0.0506  -0.2617 0.0221  306 TYR A OH  
2167 N N   . THR A 309 ? 1.2523 0.5579 0.5114 0.0247  -0.1803 -0.0516 307 THR A N   
2168 C CA  . THR A 309 ? 1.3448 0.6630 0.5985 0.0250  -0.1589 -0.0643 307 THR A CA  
2169 C C   . THR A 309 ? 1.2469 0.6411 0.6002 0.0203  -0.1440 -0.0714 307 THR A C   
2170 O O   . THR A 309 ? 1.1539 0.5880 0.5797 0.0185  -0.1622 -0.0699 307 THR A O   
2171 C CB  . THR A 309 ? 1.3741 0.6492 0.5797 0.0341  -0.1976 -0.0754 307 THR A CB  
2172 O OG1 . THR A 309 ? 1.4785 0.7472 0.6544 0.0370  -0.1724 -0.0874 307 THR A OG1 
2173 C CG2 . THR A 309 ? 1.3454 0.6581 0.6291 0.0344  -0.2404 -0.0815 307 THR A CG2 
2174 N N   . ALA A 310 ? 1.2497 0.6615 0.6022 0.0200  -0.1097 -0.0791 308 ALA A N   
2175 C CA  . ALA A 310 ? 1.1761 0.6510 0.6089 0.0180  -0.0951 -0.0865 308 ALA A CA  
2176 C C   . ALA A 310 ? 1.2284 0.6951 0.6292 0.0255  -0.0719 -0.0980 308 ALA A C   
2177 O O   . ALA A 310 ? 1.2107 0.6300 0.5320 0.0309  -0.0583 -0.0989 308 ALA A O   
2178 C CB  . ALA A 310 ? 1.0333 0.5575 0.5234 0.0083  -0.0662 -0.0783 308 ALA A CB  
2179 N N   . CYS A 311 ? 1.0123 0.5220 0.4716 0.0276  -0.0667 -0.1067 309 CYS A N   
2180 C CA  . CYS A 311 ? 1.1460 0.6452 0.5767 0.0388  -0.0482 -0.1189 309 CYS A CA  
2181 C C   . CYS A 311 ? 1.1388 0.6615 0.5655 0.0410  0.0014  -0.1168 309 CYS A C   
2182 O O   . CYS A 311 ? 1.1924 0.6886 0.5648 0.0527  0.0228  -0.1243 309 CYS A O   
2183 C CB  . CYS A 311 ? 1.1122 0.6429 0.6020 0.0412  -0.0605 -0.1280 309 CYS A CB  
2184 S SG  . CYS A 311 ? 1.2073 0.7163 0.7102 0.0356  -0.1158 -0.1315 309 CYS A SG  
2185 N N   . SER A 312 ? 1.0294 0.6009 0.5120 0.0300  0.0202  -0.1073 310 SER A N   
2186 C CA  . SER A 312 ? 1.1036 0.7097 0.6002 0.0284  0.0653  -0.1050 310 SER A CA  
2187 C C   . SER A 312 ? 1.1262 0.7086 0.5786 0.0165  0.0850  -0.0919 310 SER A C   
2188 O O   . SER A 312 ? 1.1105 0.6604 0.5395 0.0083  0.0620  -0.0826 310 SER A O   
2189 C CB  . SER A 312 ? 0.9904 0.6658 0.5783 0.0218  0.0724  -0.1039 310 SER A CB  
2190 O OG  . SER A 312 ? 1.0988 0.7822 0.7184 0.0082  0.0520  -0.0946 310 SER A OG  
2191 N N   . HIS A 313 ? 1.2047 0.8041 0.6475 0.0158  0.1289  -0.0906 311 HIS A N   
2192 C CA  . HIS A 313 ? 1.2064 0.7843 0.6081 0.0010  0.1541  -0.0766 311 HIS A CA  
2193 C C   . HIS A 313 ? 1.1868 0.8034 0.6507 -0.0201 0.1553  -0.0652 311 HIS A C   
2194 O O   . HIS A 313 ? 1.1931 0.7766 0.6225 -0.0347 0.1568  -0.0517 311 HIS A O   
2195 C CB  . HIS A 313 ? 1.1800 0.7694 0.5576 0.0053  0.2049  -0.0784 311 HIS A CB  
2196 C CG  . HIS A 313 ? 1.3120 0.8372 0.5932 0.0229  0.2098  -0.0853 311 HIS A CG  
2197 N ND1 . HIS A 313 ? 1.3321 0.7838 0.5185 0.0187  0.2064  -0.0760 311 HIS A ND1 
2198 C CD2 . HIS A 313 ? 1.3642 0.8816 0.6226 0.0460  0.2171  -0.1011 311 HIS A CD2 
2199 C CE1 . HIS A 313 ? 1.4849 0.8863 0.5926 0.0377  0.2110  -0.0863 311 HIS A CE1 
2200 N NE2 . HIS A 313 ? 1.4635 0.9029 0.6132 0.0546  0.2181  -0.1021 311 HIS A NE2 
2201 N N   . ALA A 314 ? 1.0864 0.7667 0.6359 -0.0213 0.1533  -0.0707 312 ALA A N   
2202 C CA  . ALA A 314 ? 1.1118 0.8265 0.7176 -0.0408 0.1538  -0.0621 312 ALA A CA  
2203 C C   . ALA A 314 ? 1.0949 0.7770 0.6942 -0.0445 0.1153  -0.0564 312 ALA A C   
2204 O O   . ALA A 314 ? 1.1021 0.7769 0.7063 -0.0608 0.1157  -0.0457 312 ALA A O   
2205 C CB  . ALA A 314 ? 1.0357 0.8215 0.7268 -0.0387 0.1583  -0.0705 312 ALA A CB  
2206 N N   . ALA A 315 ? 1.0909 0.7531 0.6810 -0.0295 0.0820  -0.0636 313 ALA A N   
2207 C CA  . ALA A 315 ? 1.0763 0.7138 0.6668 -0.0300 0.0457  -0.0588 313 ALA A CA  
2208 C C   . ALA A 315 ? 1.1166 0.6904 0.6328 -0.0341 0.0402  -0.0473 313 ALA A C   
2209 O O   . ALA A 315 ? 1.1342 0.6927 0.6525 -0.0420 0.0291  -0.0377 313 ALA A O   
2210 C CB  . ALA A 315 ? 0.9963 0.6314 0.5982 -0.0154 0.0129  -0.0688 313 ALA A CB  
2211 N N   . VAL A 316 ? 1.1705 0.7003 0.6139 -0.0269 0.0466  -0.0483 314 VAL A N   
2212 C CA  . VAL A 316 ? 1.2659 0.7268 0.6262 -0.0297 0.0413  -0.0365 314 VAL A CA  
2213 C C   . VAL A 316 ? 1.2774 0.7372 0.6326 -0.0498 0.0732  -0.0224 314 VAL A C   
2214 O O   . VAL A 316 ? 1.3327 0.7488 0.6540 -0.0563 0.0602  -0.0100 314 VAL A O   
2215 C CB  . VAL A 316 ? 1.2805 0.6931 0.5568 -0.0185 0.0480  -0.0412 314 VAL A CB  
2216 C CG1 . VAL A 316 ? 1.3508 0.6863 0.5314 -0.0216 0.0446  -0.0276 314 VAL A CG1 
2217 C CG2 . VAL A 316 ? 1.2372 0.6430 0.5158 -0.0017 0.0107  -0.0553 314 VAL A CG2 
2218 N N   . ASP A 317 ? 1.2883 0.7953 0.6783 -0.0601 0.1143  -0.0241 315 ASP A N   
2219 C CA  . ASP A 317 ? 1.3074 0.8201 0.7025 -0.0839 0.1456  -0.0110 315 ASP A CA  
2220 C C   . ASP A 317 ? 1.2726 0.7999 0.7200 -0.0947 0.1251  -0.0065 315 ASP A C   
2221 O O   . ASP A 317 ? 1.2953 0.7895 0.7177 -0.1119 0.1310  0.0071  315 ASP A O   
2222 C CB  . ASP A 317 ? 1.2560 0.8304 0.6959 -0.0917 0.1898  -0.0157 315 ASP A CB  
2223 C CG  . ASP A 317 ? 1.3555 0.9072 0.7317 -0.0827 0.2207  -0.0175 315 ASP A CG  
2224 O OD1 . ASP A 317 ? 1.3602 0.8421 0.6501 -0.0723 0.2063  -0.0148 315 ASP A OD1 
2225 O OD2 . ASP A 317 ? 1.4098 1.0127 0.8211 -0.0847 0.2586  -0.0221 315 ASP A OD2 
2226 N N   . ALA A 318 ? 1.2097 0.7816 0.7251 -0.0847 0.1018  -0.0176 316 ALA A N   
2227 C CA  . ALA A 318 ? 1.2270 0.8088 0.7864 -0.0912 0.0823  -0.0151 316 ALA A CA  
2228 C C   . ALA A 318 ? 1.2511 0.7685 0.7598 -0.0843 0.0515  -0.0065 316 ALA A C   
2229 O O   . ALA A 318 ? 1.2362 0.7307 0.7423 -0.0945 0.0469  0.0023  316 ALA A O   
2230 C CB  . ALA A 318 ? 1.1127 0.7494 0.7452 -0.0795 0.0651  -0.0284 316 ALA A CB  
2231 N N   . LEU A 319 ? 1.2444 0.7301 0.7122 -0.0660 0.0276  -0.0096 317 LEU A N   
2232 C CA  . LEU A 319 ? 1.2805 0.7077 0.7027 -0.0560 -0.0065 -0.0020 317 LEU A CA  
2233 C C   . LEU A 319 ? 1.4040 0.7637 0.7426 -0.0674 0.0082  0.0140  317 LEU A C   
2234 O O   . LEU A 319 ? 1.4007 0.7126 0.7094 -0.0660 -0.0116 0.0242  317 LEU A O   
2235 C CB  . LEU A 319 ? 1.2721 0.6869 0.6765 -0.0355 -0.0388 -0.0104 317 LEU A CB  
2236 C CG  . LEU A 319 ? 1.2663 0.6858 0.7072 -0.0200 -0.0825 -0.0136 317 LEU A CG  
2237 C CD1 . LEU A 319 ? 1.2173 0.6993 0.7476 -0.0227 -0.0781 -0.0197 317 LEU A CD1 
2238 C CD2 . LEU A 319 ? 1.2927 0.7098 0.7256 -0.0055 -0.1109 -0.0234 317 LEU A CD2 
2239 N N   . CYS A 320 ? 1.3626 0.7157 0.6610 -0.0778 0.0442  0.0167  318 CYS A N   
2240 C CA  . CYS A 320 ? 1.4558 0.7454 0.6729 -0.0924 0.0658  0.0335  318 CYS A CA  
2241 C C   . CYS A 320 ? 1.4530 0.7466 0.6976 -0.1161 0.0822  0.0441  318 CYS A C   
2242 O O   . CYS A 320 ? 1.4405 0.6691 0.6313 -0.1221 0.0727  0.0584  318 CYS A O   
2243 C CB  . CYS A 320 ? 1.4850 0.7781 0.6638 -0.0987 0.1081  0.0330  318 CYS A CB  
2244 S SG  . CYS A 320 ? 1.4532 0.7107 0.5634 -0.0724 0.0907  0.0227  318 CYS A SG  
2245 N N   . GLU A 321 ? 1.4117 0.7771 0.7371 -0.1299 0.1046  0.0369  319 GLU A N   
2246 C CA  . GLU A 321 ? 1.4414 0.8116 0.7949 -0.1555 0.1189  0.0451  319 GLU A CA  
2247 C C   . GLU A 321 ? 1.4275 0.7618 0.7823 -0.1471 0.0812  0.0478  319 GLU A C   
2248 O O   . GLU A 321 ? 1.4431 0.7336 0.7724 -0.1645 0.0849  0.0599  319 GLU A O   
2249 C CB  . GLU A 321 ? 1.3309 0.7884 0.7767 -0.1671 0.1393  0.0340  319 GLU A CB  
2250 C CG  . GLU A 321 ? 1.3350 0.8181 0.7861 -0.1942 0.1869  0.0405  319 GLU A CG  
2251 C CD  . GLU A 321 ? 1.4554 0.8923 0.8747 -0.2253 0.2016  0.0578  319 GLU A CD  
2252 O OE1 . GLU A 321 ? 1.5276 0.9579 0.9751 -0.2341 0.1823  0.0581  319 GLU A OE1 
2253 O OE2 . GLU A 321 ? 1.5393 0.9428 0.9019 -0.2412 0.2336  0.0711  319 GLU A OE2 
2254 N N   . LYS A 322 ? 1.3363 0.6868 0.7200 -0.1204 0.0458  0.0366  320 LYS A N   
2255 C CA  . LYS A 322 ? 1.4027 0.7250 0.7929 -0.1074 0.0112  0.0378  320 LYS A CA  
2256 C C   . LYS A 322 ? 1.4331 0.6681 0.7356 -0.0979 -0.0092 0.0516  320 LYS A C   
2257 O O   . LYS A 322 ? 1.5317 0.7207 0.8159 -0.0964 -0.0251 0.0594  320 LYS A O   
2258 C CB  . LYS A 322 ? 1.3079 0.6798 0.7600 -0.0828 -0.0166 0.0225  320 LYS A CB  
2259 C CG  . LYS A 322 ? 1.3688 0.7222 0.8373 -0.0646 -0.0505 0.0219  320 LYS A CG  
2260 C CD  . LYS A 322 ? 1.2725 0.6194 0.7615 -0.0782 -0.0418 0.0243  320 LYS A CD  
2261 C CE  . LYS A 322 ? 1.1737 0.5931 0.7440 -0.0815 -0.0329 0.0104  320 LYS A CE  
2262 N NZ  . LYS A 322 ? 1.3066 0.7126 0.8926 -0.0897 -0.0328 0.0103  320 LYS A NZ  
2263 N N   . ALA A 323 ? 1.4430 0.6491 0.6858 -0.0898 -0.0106 0.0544  321 ALA A N   
2264 C CA  . ALA A 323 ? 1.5846 0.7029 0.7353 -0.0792 -0.0331 0.0678  321 ALA A CA  
2265 C C   . ALA A 323 ? 1.5594 0.6147 0.6426 -0.1047 -0.0048 0.0867  321 ALA A C   
2266 O O   . ALA A 323 ? 1.5810 0.5588 0.6006 -0.0993 -0.0252 0.1001  321 ALA A O   
2267 C CB  . ALA A 323 ? 1.5281 0.6294 0.6273 -0.0645 -0.0430 0.0642  321 ALA A CB  
2268 N N   . LEU A 324 ? 1.5070 0.5946 0.6043 -0.1326 0.0419  0.0886  322 LEU A N   
2269 C CA  . LEU A 324 ? 1.5725 0.6103 0.6138 -0.1633 0.0764  0.1071  322 LEU A CA  
2270 C C   . LEU A 324 ? 1.6358 0.6391 0.6851 -0.1758 0.0658  0.1154  322 LEU A C   
2271 O O   . LEU A 324 ? 1.8182 0.7684 0.8178 -0.2032 0.0892  0.1324  322 LEU A O   
2272 C CB  . LEU A 324 ? 1.5647 0.6690 0.6500 -0.1896 0.1272  0.1038  322 LEU A CB  
2273 C CG  . LEU A 324 ? 1.7188 0.7937 0.7655 -0.2274 0.1730  0.1218  322 LEU A CG  
2274 C CD1 . LEU A 324 ? 1.7467 0.7436 0.6782 -0.2267 0.1886  0.1373  322 LEU A CD1 
2275 C CD2 . LEU A 324 ? 1.6613 0.8293 0.7904 -0.2495 0.2148  0.1136  322 LEU A CD2 
2276 N N   . LYS A 325 ? 1.5807 0.6093 0.6884 -0.1560 0.0316  0.1037  323 LYS A N   
2277 C CA  . LYS A 325 ? 1.5911 0.5895 0.7108 -0.1633 0.0201  0.1077  323 LYS A CA  
2278 C C   . LYS A 325 ? 1.6065 0.5389 0.6850 -0.1318 -0.0253 0.1116  323 LYS A C   
2279 O O   . LYS A 325 ? 1.6403 0.5101 0.6869 -0.1372 -0.0334 0.1212  323 LYS A O   
2280 C CB  . LYS A 325 ? 1.5028 0.5847 0.7263 -0.1665 0.0219  0.0902  323 LYS A CB  
2281 C CG  . LYS A 325 ? 1.5668 0.6198 0.8057 -0.1676 0.0051  0.0896  323 LYS A CG  
2282 C CD  . LYS A 325 ? 1.5883 0.5801 0.7798 -0.2044 0.0275  0.1058  323 LYS A CD  
2283 C CE  . LYS A 325 ? 1.6215 0.5720 0.8181 -0.2032 0.0077  0.1040  323 LYS A CE  
2284 N NZ  . LYS A 325 ? 1.6014 0.6286 0.8882 -0.1941 0.0002  0.0832  323 LYS A NZ  
2285 N N   . TYR A 326 ? 1.5919 0.5362 0.6714 -0.0988 -0.0562 0.1040  324 TYR A N   
2286 C CA  . TYR A 326 ? 1.6390 0.5375 0.6980 -0.0650 -0.1027 0.1053  324 TYR A CA  
2287 C C   . TYR A 326 ? 1.7145 0.5561 0.6931 -0.0454 -0.1278 0.1137  324 TYR A C   
2288 O O   . TYR A 326 ? 1.7139 0.5159 0.6729 -0.0154 -0.1703 0.1157  324 TYR A O   
2289 C CB  . TYR A 326 ? 1.4950 0.4703 0.6506 -0.0396 -0.1264 0.0858  324 TYR A CB  
2290 C CG  . TYR A 326 ? 1.4768 0.5020 0.7065 -0.0527 -0.1090 0.0760  324 TYR A CG  
2291 C CD1 . TYR A 326 ? 1.5105 0.4988 0.7421 -0.0444 -0.1227 0.0772  324 TYR A CD1 
2292 C CD2 . TYR A 326 ? 1.4638 0.5694 0.7580 -0.0707 -0.0811 0.0646  324 TYR A CD2 
2293 C CE1 . TYR A 326 ? 1.4901 0.5175 0.7813 -0.0557 -0.1088 0.0669  324 TYR A CE1 
2294 C CE2 . TYR A 326 ? 1.3807 0.5280 0.7369 -0.0818 -0.0690 0.0553  324 TYR A CE2 
2295 C CZ  . TYR A 326 ? 1.3772 0.4840 0.7297 -0.0750 -0.0829 0.0562  324 TYR A CZ  
2296 O OH  . TYR A 326 ? 1.4017 0.5429 0.8072 -0.0856 -0.0726 0.0459  324 TYR A OH  
2297 N N   . LEU A 327 ? 1.7099 0.5440 0.6393 -0.0597 -0.1039 0.1184  325 LEU A N   
2298 C CA  . LEU A 327 ? 1.8207 0.6002 0.6690 -0.0407 -0.1293 0.1241  325 LEU A CA  
2299 C C   . LEU A 327 ? 1.9032 0.6040 0.6425 -0.0623 -0.1000 0.1429  325 LEU A C   
2300 O O   . LEU A 327 ? 1.9028 0.6155 0.6422 -0.0955 -0.0510 0.1491  325 LEU A O   
2301 C CB  . LEU A 327 ? 1.7561 0.6026 0.6444 -0.0302 -0.1335 0.1071  325 LEU A CB  
2302 C CG  . LEU A 327 ? 1.6706 0.5882 0.6567 -0.0055 -0.1690 0.0892  325 LEU A CG  
2303 C CD1 . LEU A 327 ? 1.6209 0.5907 0.6334 0.0013  -0.1734 0.0743  325 LEU A CD1 
2304 C CD2 . LEU A 327 ? 1.7123 0.5840 0.6812 0.0248  -0.2215 0.0935  325 LEU A CD2 
2305 N N   . PRO A 328 ? 1.9918 0.6361 0.6607 -0.0443 -0.1271 0.1443  326 PRO A N   
2306 C CA  . PRO A 328 ? 2.1172 0.7053 0.6986 -0.0622 -0.0974 0.1538  326 PRO A CA  
2307 C C   . PRO A 328 ? 2.0969 0.7138 0.6643 -0.0802 -0.0533 0.1526  326 PRO A C   
2308 O O   . PRO A 328 ? 2.1065 0.7432 0.6709 -0.0635 -0.0675 0.1427  326 PRO A O   
2309 C CB  . PRO A 328 ? 2.1788 0.7095 0.6984 -0.0323 -0.1448 0.1510  326 PRO A CB  
2310 C CG  . PRO A 328 ? 2.1291 0.6794 0.7094 -0.0050 -0.1936 0.1443  326 PRO A CG  
2311 C CD  . PRO A 328 ? 2.0053 0.6353 0.6757 -0.0069 -0.1865 0.1366  326 PRO A CD  
2312 N N   . ILE A 329 ? 2.1034 0.7258 0.6661 -0.1143 0.0005  0.1615  327 ILE A N   
2313 C CA  . ILE A 329 ? 2.0882 0.7510 0.6525 -0.1325 0.0503  0.1596  327 ILE A CA  
2314 C C   . ILE A 329 ? 2.2467 0.8628 0.7251 -0.1208 0.0531  0.1583  327 ILE A C   
2315 O O   . ILE A 329 ? 2.1824 0.8263 0.6535 -0.1294 0.0927  0.1547  327 ILE A O   
2316 C CB  . ILE A 329 ? 2.0862 0.7739 0.6796 -0.1725 0.1053  0.1691  327 ILE A CB  
2317 C CG1 . ILE A 329 ? 2.0269 0.7895 0.6652 -0.1881 0.1535  0.1629  327 ILE A CG1 
2318 C CG2 . ILE A 329 ? 2.2072 0.8278 0.7239 -0.1863 0.1238  0.1817  327 ILE A CG2 
2319 C CD1 . ILE A 329 ? 2.0227 0.8230 0.7029 -0.2277 0.2068  0.1705  327 ILE A CD1 
2320 N N   . ASP A 330 ? 2.2617 0.8076 0.6769 -0.0996 0.0109  0.1598  328 ASP A N   
2321 C CA  . ASP A 330 ? 2.3904 0.8808 0.7180 -0.0885 0.0094  0.1586  328 ASP A CA  
2322 C C   . ASP A 330 ? 2.3525 0.8391 0.6719 -0.0549 -0.0428 0.1440  328 ASP A C   
2323 O O   . ASP A 330 ? 2.4280 0.8747 0.6810 -0.0445 -0.0456 0.1397  328 ASP A O   
2324 C CB  . ASP A 330 ? 2.4852 0.8900 0.7348 -0.0925 0.0039  0.1714  328 ASP A CB  
2325 C CG  . ASP A 330 ? 2.5204 0.8906 0.7720 -0.0699 -0.0554 0.1708  328 ASP A CG  
2326 O OD1 . ASP A 330 ? 2.4191 0.8257 0.7400 -0.0725 -0.0654 0.1711  328 ASP A OD1 
2327 O OD2 . ASP A 330 ? 2.6090 0.9152 0.7932 -0.0489 -0.0913 0.1695  328 ASP A OD2 
2328 N N   . LYS A 331 ? 2.2644 0.7920 0.6522 -0.0384 -0.0842 0.1361  329 LYS A N   
2329 C CA  . LYS A 331 ? 2.2386 0.7794 0.6398 -0.0101 -0.1337 0.1210  329 LYS A CA  
2330 C C   . LYS A 331 ? 2.1407 0.7583 0.6057 -0.0117 -0.1201 0.1096  329 LYS A C   
2331 O O   . LYS A 331 ? 2.0859 0.7323 0.5890 0.0084  -0.1629 0.0968  329 LYS A O   
2332 C CB  . LYS A 331 ? 2.2172 0.7553 0.6568 0.0126  -0.1934 0.1187  329 LYS A CB  
2333 C CG  . LYS A 331 ? 2.3277 0.7881 0.7004 0.0261  -0.2255 0.1237  329 LYS A CG  
2334 C CD  . LYS A 331 ? 2.3912 0.8083 0.7281 0.0061  -0.1939 0.1398  329 LYS A CD  
2335 C CE  . LYS A 331 ? 2.5223 0.8601 0.7911 0.0221  -0.2294 0.1442  329 LYS A CE  
2336 N NZ  . LYS A 331 ? 2.6215 0.9142 0.8556 0.0028  -0.2022 0.1595  329 LYS A NZ  
2337 N N   . CYS A 332 ? 2.1321 0.7862 0.6129 -0.0359 -0.0616 0.1131  330 CYS A N   
2338 C CA  . CYS A 332 ? 2.0649 0.7940 0.6072 -0.0392 -0.0428 0.1023  330 CYS A CA  
2339 C C   . CYS A 332 ? 2.0372 0.7746 0.5449 -0.0468 0.0052  0.0961  330 CYS A C   
2340 O O   . CYS A 332 ? 2.1055 0.8150 0.5699 -0.0633 0.0475  0.1063  330 CYS A O   
2341 C CB  . CYS A 332 ? 1.9573 0.7530 0.5949 -0.0597 -0.0153 0.1050  330 CYS A CB  
2342 S SG  . CYS A 332 ? 1.8542 0.6597 0.5618 -0.0488 -0.0640 0.1065  330 CYS A SG  
2343 N N   . SER A 333 ? 1.9908 0.7676 0.5209 -0.0337 -0.0015 0.0785  331 SER A N   
2344 C CA  . SER A 333 ? 2.0099 0.8044 0.5211 -0.0366 0.0446  0.0697  331 SER A CA  
2345 C C   . SER A 333 ? 1.9606 0.8372 0.5504 -0.0332 0.0545  0.0518  331 SER A C   
2346 O O   . SER A 333 ? 1.8363 0.7452 0.4854 -0.0184 0.0089  0.0379  331 SER A O   
2347 C CB  . SER A 333 ? 2.1039 0.8382 0.5391 -0.0174 0.0227  0.0625  331 SER A CB  
2348 O OG  . SER A 333 ? 2.1277 0.8771 0.5446 -0.0177 0.0689  0.0546  331 SER A OG  
2349 N N   . ARG A 334 ? 1.9831 0.9088 0.6026 -0.0466 0.1140  0.0497  332 ARG A N   
2350 C CA  . ARG A 334 ? 1.8338 0.8464 0.5446 -0.0408 0.1286  0.0298  332 ARG A CA  
2351 C C   . ARG A 334 ? 1.8986 0.8808 0.5355 -0.0238 0.1435  0.0174  332 ARG A C   
2352 O O   . ARG A 334 ? 1.9326 0.9042 0.5339 -0.0290 0.1898  0.0229  332 ARG A O   
2353 C CB  . ARG A 334 ? 1.7137 0.8032 0.5091 -0.0631 0.1809  0.0338  332 ARG A CB  
2354 C CG  . ARG A 334 ? 1.6138 0.7938 0.5058 -0.0557 0.1952  0.0144  332 ARG A CG  
2355 C CD  . ARG A 334 ? 1.5872 0.8063 0.5593 -0.0446 0.1438  0.0023  332 ARG A CD  
2356 N NE  . ARG A 334 ? 1.4704 0.7783 0.5450 -0.0431 0.1586  -0.0116 332 ARG A NE  
2357 C CZ  . ARG A 334 ? 1.4482 0.7799 0.5278 -0.0283 0.1743  -0.0268 332 ARG A CZ  
2358 N NH1 . ARG A 334 ? 1.5417 0.8148 0.5322 -0.0117 0.1706  -0.0332 332 ARG A NH1 
2359 N NH2 . ARG A 334 ? 1.4223 0.8337 0.5954 -0.0280 0.1896  -0.0366 332 ARG A NH2 
2360 N N   . ILE A 335 ? 1.8245 0.8073 0.4699 -0.0034 0.1011  -0.0005 333 ILE A N   
2361 C CA  . ILE A 335 ? 1.8745 0.8386 0.4796 0.0144  0.1072  -0.0147 333 ILE A CA  
2362 C C   . ILE A 335 ? 1.8080 0.8447 0.4752 0.0171  0.1493  -0.0291 333 ILE A C   
2363 O O   . ILE A 335 ? 1.8335 0.9376 0.5976 0.0158  0.1374  -0.0377 333 ILE A O   
2364 C CB  . ILE A 335 ? 1.8865 0.8159 0.4756 0.0322  0.0412  -0.0267 333 ILE A CB  
2365 C CG1 . ILE A 335 ? 1.9718 0.8254 0.4938 0.0342  0.0017  -0.0136 333 ILE A CG1 
2366 C CG2 . ILE A 335 ? 1.9203 0.8424 0.4881 0.0490  0.0478  -0.0431 333 ILE A CG2 
2367 C CD1 . ILE A 335 ? 1.9713 0.8245 0.5162 0.0235  -0.0218 0.0008  333 ILE A CD1 
2368 N N   . ILE A 336 ? 1.8777 0.9161 0.5201 0.0222  0.1952  -0.0308 334 ILE A N   
2369 C CA  . ILE A 336 ? 1.8055 0.9143 0.5091 0.0288  0.2368  -0.0442 334 ILE A CA  
2370 C C   . ILE A 336 ? 1.9096 0.9933 0.5759 0.0535  0.2309  -0.0601 334 ILE A C   
2371 O O   . ILE A 336 ? 1.9570 0.9733 0.5415 0.0601  0.2228  -0.0559 334 ILE A O   
2372 C CB  . ILE A 336 ? 1.8103 0.9634 0.5406 0.0120  0.3029  -0.0317 334 ILE A CB  
2373 C CG1 . ILE A 336 ? 1.9427 1.0445 0.5939 0.0141  0.3298  -0.0227 334 ILE A CG1 
2374 C CG2 . ILE A 336 ? 1.7992 0.9684 0.5624 -0.0158 0.3063  -0.0143 334 ILE A CG2 
2375 C CD1 . ILE A 336 ? 1.9519 1.0866 0.6116 0.0312  0.3722  -0.0346 334 ILE A CD1 
2376 N N   . PRO A 337 ? 1.9208 1.0517 0.6414 0.0679  0.2334  -0.0784 335 PRO A N   
2377 C CA  . PRO A 337 ? 1.8911 0.9967 0.5760 0.0911  0.2314  -0.0930 335 PRO A CA  
2378 C C   . PRO A 337 ? 1.9402 1.0561 0.6018 0.0963  0.2915  -0.0896 335 PRO A C   
2379 O O   . PRO A 337 ? 1.9149 1.0960 0.6330 0.0870  0.3396  -0.0841 335 PRO A O   
2380 C CB  . PRO A 337 ? 1.8445 1.0040 0.6054 0.1025  0.2199  -0.1113 335 PRO A CB  
2381 C CG  . PRO A 337 ? 1.7601 0.9932 0.6017 0.0874  0.2483  -0.1058 335 PRO A CG  
2382 C CD  . PRO A 337 ? 1.7698 0.9748 0.5847 0.0644  0.2370  -0.0867 335 PRO A CD  
2383 N N   . ALA A 338 ? 2.0205 1.0727 0.6005 0.1106  0.2879  -0.0928 336 ALA A N   
2384 C CA  . ALA A 338 ? 2.1439 1.2025 0.6966 0.1176  0.3448  -0.0908 336 ALA A CA  
2385 C C   . ALA A 338 ? 2.0780 1.2224 0.7134 0.1296  0.3844  -0.1032 336 ALA A C   
2386 O O   . ALA A 338 ? 2.0841 1.2708 0.7381 0.1285  0.4397  -0.0985 336 ALA A O   
2387 C CB  . ALA A 338 ? 2.2126 1.1871 0.6649 0.1355  0.3302  -0.0966 336 ALA A CB  
2388 N N   . ARG A 339 ? 2.0612 1.2332 0.7494 0.1412  0.3557  -0.1188 337 ARG A N   
2389 C CA  . ARG A 339 ? 1.9516 1.2068 0.7276 0.1535  0.3849  -0.1308 337 ARG A CA  
2390 C C   . ARG A 339 ? 1.8607 1.1854 0.7243 0.1328  0.3921  -0.1225 337 ARG A C   
2391 O O   . ARG A 339 ? 1.8920 1.2227 0.7906 0.1289  0.3534  -0.1273 337 ARG A O   
2392 C CB  . ARG A 339 ? 1.9093 1.1501 0.6924 0.1757  0.3485  -0.1507 337 ARG A CB  
2393 C CG  . ARG A 339 ? 2.0471 1.1964 0.7328 0.1885  0.3179  -0.1566 337 ARG A CG  
2394 C CD  . ARG A 339 ? 2.0458 1.1873 0.7430 0.2107  0.2941  -0.1761 337 ARG A CD  
2395 N NE  . ARG A 339 ? 2.0527 1.2562 0.8026 0.2299  0.3384  -0.1862 337 ARG A NE  
2396 C CZ  . ARG A 339 ? 2.0149 1.2252 0.7386 0.2426  0.3865  -0.1867 337 ARG A CZ  
2397 N NH1 . ARG A 339 ? 2.1209 1.2669 0.7534 0.2410  0.3950  -0.1796 337 ARG A NH1 
2398 N NH2 . ARG A 339 ? 1.9900 1.2713 0.7796 0.2589  0.4250  -0.1954 337 ARG A NH2 
2399 N N   . ALA A 340 ? 1.8884 1.2662 0.7894 0.1180  0.4415  -0.1100 338 ALA A N   
2400 C CA  . ALA A 340 ? 1.8275 1.2571 0.7962 0.0914  0.4496  -0.0975 338 ALA A CA  
2401 C C   . ALA A 340 ? 1.6944 1.2270 0.7756 0.0962  0.4800  -0.1048 338 ALA A C   
2402 O O   . ALA A 340 ? 1.7006 1.2849 0.8144 0.1004  0.5257  -0.1037 338 ALA A O   
2403 C CB  . ALA A 340 ? 1.7599 1.1720 0.6939 0.0653  0.4780  -0.0753 338 ALA A CB  
2404 N N   . ARG A 341 ? 1.5874 1.1507 0.7296 0.0962  0.4531  -0.1123 339 ARG A N   
2405 C CA  . ARG A 341 ? 1.5770 1.2332 0.8266 0.1045  0.4726  -0.1209 339 ARG A CA  
2406 C C   . ARG A 341 ? 1.5275 1.2454 0.8549 0.0728  0.4880  -0.1067 339 ARG A C   
2407 O O   . ARG A 341 ? 1.5372 1.3229 0.9234 0.0627  0.5301  -0.0997 339 ARG A O   
2408 C CB  . ARG A 341 ? 1.5406 1.1919 0.8122 0.1264  0.4325  -0.1390 339 ARG A CB  
2409 C CG  . ARG A 341 ? 1.4088 1.1556 0.8010 0.1321  0.4386  -0.1447 339 ARG A CG  
2410 C CD  . ARG A 341 ? 1.4405 1.1774 0.8532 0.1527  0.3932  -0.1598 339 ARG A CD  
2411 N NE  . ARG A 341 ? 1.3911 1.1446 0.8602 0.1320  0.3467  -0.1528 339 ARG A NE  
2412 C CZ  . ARG A 341 ? 1.3324 1.1619 0.8997 0.1176  0.3460  -0.1464 339 ARG A CZ  
2413 N NH1 . ARG A 341 ? 1.3720 1.2749 1.0028 0.1204  0.3852  -0.1461 339 ARG A NH1 
2414 N NH2 . ARG A 341 ? 1.2425 1.0753 0.8461 0.1010  0.3043  -0.1411 339 ARG A NH2 
2415 N N   . VAL A 342 ? 1.3815 1.0886 0.7324 0.0543  0.4390  -0.0999 340 VAL A N   
2416 C CA  . VAL A 342 ? 1.3599 1.1209 0.7894 0.0222  0.4380  -0.0854 340 VAL A CA  
2417 C C   . VAL A 342 ? 1.4463 1.1561 0.8102 -0.0053 0.4518  -0.0659 340 VAL A C   
2418 O O   . VAL A 342 ? 1.5652 1.1900 0.8238 0.0002  0.4429  -0.0631 340 VAL A O   
2419 C CB  . VAL A 342 ? 1.4072 1.1821 0.8944 0.0174  0.3824  -0.0879 340 VAL A CB  
2420 C CG1 . VAL A 342 ? 1.2384 1.0815 0.8109 0.0366  0.3770  -0.1024 340 VAL A CG1 
2421 C CG2 . VAL A 342 ? 1.3888 1.0819 0.8010 0.0259  0.3358  -0.0908 340 VAL A CG2 
2422 N N   . GLU A 343 ? 1.4453 1.2036 0.8692 -0.0357 0.4722  -0.0520 341 GLU A N   
2423 C CA  . GLU A 343 ? 1.4042 1.1124 0.7744 -0.0658 0.4791  -0.0316 341 GLU A CA  
2424 C C   . GLU A 343 ? 1.4614 1.1154 0.8073 -0.0712 0.4203  -0.0274 341 GLU A C   
2425 O O   . GLU A 343 ? 1.3547 1.0478 0.7753 -0.0730 0.3860  -0.0325 341 GLU A O   
2426 C CB  . GLU A 343 ? 1.2993 1.0748 0.7481 -0.0993 0.5125  -0.0190 341 GLU A CB  
2427 C CG  . GLU A 343 ? 1.4527 1.2936 0.9393 -0.0970 0.5740  -0.0213 341 GLU A CG  
2428 C CD  . GLU A 343 ? 1.5025 1.4113 1.0726 -0.1351 0.6019  -0.0080 341 GLU A CD  
2429 O OE1 . GLU A 343 ? 1.3614 1.3260 1.0232 -0.1465 0.5748  -0.0112 341 GLU A OE1 
2430 O OE2 . GLU A 343 ? 1.3640 1.2735 0.9184 -0.1503 0.6331  0.0063  341 GLU A OE2 
2431 N N   . CYS A 344 ? 1.4552 1.0191 0.6959 -0.0724 0.4088  -0.0181 342 CYS A N   
2432 C CA  . CYS A 344 ? 1.4967 1.0093 0.7137 -0.0760 0.3545  -0.0129 342 CYS A CA  
2433 C C   . CYS A 344 ? 1.5391 1.0303 0.7482 -0.1082 0.3610  0.0080  342 CYS A C   
2434 O O   . CYS A 344 ? 1.4812 1.0135 0.7284 -0.1319 0.4027  0.0172  342 CYS A O   
2435 C CB  . CYS A 344 ? 1.5099 0.9353 0.6192 -0.0541 0.3274  -0.0173 342 CYS A CB  
2436 S SG  . CYS A 344 ? 1.6355 1.0715 0.7405 -0.0182 0.3206  -0.0423 342 CYS A SG  
2437 N N   . PHE A 345 ? 1.5783 1.0040 0.7388 -0.1092 0.3189  0.0158  343 PHE A N   
2438 C CA  . PHE A 345 ? 1.5859 0.9801 0.7344 -0.1362 0.3165  0.0347  343 PHE A CA  
2439 C C   . PHE A 345 ? 1.6152 0.9401 0.6596 -0.1488 0.3527  0.0521  343 PHE A C   
2440 O O   . PHE A 345 ? 1.8090 1.0623 0.7543 -0.1311 0.3425  0.0523  343 PHE A O   
2441 C CB  . PHE A 345 ? 1.5386 0.8906 0.6764 -0.1259 0.2564  0.0347  343 PHE A CB  
2442 C CG  . PHE A 345 ? 1.5343 0.8554 0.6699 -0.1483 0.2459  0.0511  343 PHE A CG  
2443 C CD1 . PHE A 345 ? 1.4675 0.8462 0.6949 -0.1654 0.2453  0.0501  343 PHE A CD1 
2444 C CD2 . PHE A 345 ? 1.6240 0.8519 0.6611 -0.1498 0.2317  0.0666  343 PHE A CD2 
2445 C CE1 . PHE A 345 ? 1.4725 0.8154 0.6929 -0.1847 0.2339  0.0637  343 PHE A CE1 
2446 C CE2 . PHE A 345 ? 1.6869 0.8792 0.7181 -0.1679 0.2201  0.0814  343 PHE A CE2 
2447 C CZ  . PHE A 345 ? 1.6634 0.9126 0.7863 -0.1855 0.2218  0.0794  343 PHE A CZ  
2448 N N   . ASP A 346 ? 1.6440 0.9872 0.7079 -0.1809 0.3942  0.0669  344 ASP A N   
2449 C CA  . ASP A 346 ? 1.7121 0.9923 0.6796 -0.1973 0.4362  0.0857  344 ASP A CA  
2450 C C   . ASP A 346 ? 1.7612 0.9818 0.6961 -0.2231 0.4223  0.1064  344 ASP A C   
2451 O O   . ASP A 346 ? 1.8752 1.1143 0.8366 -0.2516 0.4546  0.1184  344 ASP A O   
2452 C CB  . ASP A 346 ? 1.7068 1.0662 0.7385 -0.2101 0.4937  0.0845  344 ASP A CB  
2453 C CG  . ASP A 346 ? 1.8313 1.1902 0.8223 -0.1819 0.5155  0.0739  344 ASP A CG  
2454 O OD1 . ASP A 346 ? 1.9512 1.2435 0.8606 -0.1551 0.4850  0.0672  344 ASP A OD1 
2455 O OD2 . ASP A 346 ? 1.8531 1.2778 0.8948 -0.1862 0.5608  0.0723  344 ASP A OD2 
2456 N N   . LYS A 347 ? 1.7723 0.9263 0.6592 -0.2104 0.3695  0.1090  345 LYS A N   
2457 C CA  . LYS A 347 ? 1.8468 0.9329 0.6933 -0.2284 0.3508  0.1276  345 LYS A CA  
2458 C C   . LYS A 347 ? 1.9117 0.9038 0.6626 -0.2024 0.3012  0.1304  345 LYS A C   
2459 O O   . LYS A 347 ? 1.9483 0.8791 0.6622 -0.2098 0.2792  0.1434  345 LYS A O   
2460 C CB  . LYS A 347 ? 1.7361 0.8669 0.6774 -0.2434 0.3286  0.1255  345 LYS A CB  
2461 C CG  . LYS A 347 ? 1.7326 0.9495 0.7692 -0.2750 0.3719  0.1251  345 LYS A CG  
2462 C CD  . LYS A 347 ? 1.7375 0.9987 0.8680 -0.2840 0.3416  0.1182  345 LYS A CD  
2463 C CE  . LYS A 347 ? 1.6535 0.9994 0.8789 -0.3164 0.3788  0.1170  345 LYS A CE  
2464 N NZ  . LYS A 347 ? 1.6122 1.0448 0.8947 -0.3041 0.4081  0.1024  345 LYS A NZ  
2465 N N   . PHE A 348 ? 1.8995 0.8800 0.6133 -0.1716 0.2808  0.1172  346 PHE A N   
2466 C CA  . PHE A 348 ? 1.9655 0.8661 0.5968 -0.1452 0.2309  0.1166  346 PHE A CA  
2467 C C   . PHE A 348 ? 2.0832 0.9539 0.6465 -0.1322 0.2505  0.1117  346 PHE A C   
2468 O O   . PHE A 348 ? 2.0440 0.9630 0.6308 -0.1381 0.2993  0.1066  346 PHE A O   
2469 C CB  . PHE A 348 ? 1.9256 0.8482 0.5933 -0.1182 0.1778  0.1001  346 PHE A CB  
2470 C CG  . PHE A 348 ? 1.8869 0.8448 0.6428 -0.1206 0.1432  0.0986  346 PHE A CG  
2471 C CD1 . PHE A 348 ? 1.8562 0.7759 0.5999 -0.1399 0.1438  0.1163  346 PHE A CD1 
2472 C CD2 . PHE A 348 ? 1.7319 0.7562 0.5781 -0.1028 0.1103  0.0792  346 PHE A CD2 
2473 C CE1 . PHE A 348 ? 1.8806 0.8287 0.7003 -0.1388 0.1125  0.1130  346 PHE A CE1 
2474 C CE2 . PHE A 348 ? 1.6191 0.6746 0.5418 -0.1029 0.0816  0.0771  346 PHE A CE2 
2475 C CZ  . PHE A 348 ? 1.6782 0.6957 0.5872 -0.1195 0.0827  0.0932  346 PHE A CZ  
2476 N N   . LYS A 349 ? 2.1330 0.9240 0.6142 -0.1131 0.2112  0.1129  347 LYS A N   
2477 C CA  . LYS A 349 ? 2.2180 0.9726 0.6292 -0.0979 0.2227  0.1069  347 LYS A CA  
2478 C C   . LYS A 349 ? 2.1575 0.9610 0.6005 -0.0776 0.2197  0.0858  347 LYS A C   
2479 O O   . LYS A 349 ? 2.0867 0.9098 0.5653 -0.0639 0.1771  0.0750  347 LYS A O   
2480 C CB  . LYS A 349 ? 2.3153 0.9752 0.6378 -0.0806 0.1734  0.1105  347 LYS A CB  
2481 N N   . VAL A 350 ? 2.2191 1.0429 0.6510 -0.0749 0.2645  0.0796  348 VAL A N   
2482 C CA  . VAL A 350 ? 2.1564 1.0272 0.6202 -0.0553 0.2674  0.0588  348 VAL A CA  
2483 C C   . VAL A 350 ? 2.2184 1.0221 0.6020 -0.0293 0.2334  0.0489  348 VAL A C   
2484 O O   . VAL A 350 ? 2.3290 1.0719 0.6337 -0.0279 0.2467  0.0563  348 VAL A O   
2485 C CB  . VAL A 350 ? 2.1191 1.0594 0.6293 -0.0640 0.3350  0.0560  348 VAL A CB  
2486 C CG1 . VAL A 350 ? 2.0643 1.0526 0.6116 -0.0410 0.3352  0.0332  348 VAL A CG1 
2487 C CG2 . VAL A 350 ? 2.0459 1.0520 0.6397 -0.0935 0.3663  0.0668  348 VAL A CG2 
2488 N N   . ASN A 351 ? 2.2396 1.0530 0.6440 -0.0100 0.1884  0.0320  349 ASN A N   
2489 C CA  . ASN A 351 ? 2.2519 1.0105 0.5950 0.0135  0.1520  0.0200  349 ASN A CA  
2490 C C   . ASN A 351 ? 2.3384 1.0065 0.5991 0.0166  0.1128  0.0311  349 ASN A C   
2491 O O   . ASN A 351 ? 2.4432 1.0492 0.6225 0.0254  0.1177  0.0317  349 ASN A O   
2492 C CB  . ASN A 351 ? 2.2858 1.0485 0.6001 0.0235  0.1970  0.0111  349 ASN A CB  
2493 C CG  . ASN A 351 ? 2.1904 1.0427 0.5890 0.0252  0.2320  -0.0021 349 ASN A CG  
2494 O OD1 . ASN A 351 ? 2.2007 1.0897 0.6545 0.0332  0.2017  -0.0157 349 ASN A OD1 
2495 N ND2 . ASN A 351 ? 2.2065 1.0960 0.6181 0.0184  0.2954  0.0015  349 ASN A ND2 
2496 N N   . SER A 352 ? 2.3363 0.9959 0.6180 0.0114  0.0724  0.0392  350 SER A N   
2497 C CA  . SER A 352 ? 2.3873 0.9668 0.6035 0.0178  0.0267  0.0478  350 SER A CA  
2498 C C   . SER A 352 ? 2.3300 0.9187 0.5886 0.0317  -0.0434 0.0384  350 SER A C   
2499 O O   . SER A 352 ? 2.2863 0.8949 0.5916 0.0267  -0.0671 0.0451  350 SER A O   
2500 C CB  . SER A 352 ? 2.4197 0.9752 0.6192 -0.0015 0.0467  0.0687  350 SER A CB  
2501 O OG  . SER A 352 ? 2.5028 0.9814 0.6417 0.0075  0.0001  0.0755  350 SER A OG  
2502 N N   . THR A 353 ? 2.3487 0.9237 0.5936 0.0490  -0.0764 0.0230  351 THR A N   
2503 C CA  . THR A 353 ? 2.2943 0.8868 0.5898 0.0606  -0.1417 0.0127  351 THR A CA  
2504 C C   . THR A 353 ? 2.3393 0.8847 0.6150 0.0663  -0.1927 0.0219  351 THR A C   
2505 O O   . THR A 353 ? 2.2818 0.8549 0.6177 0.0737  -0.2440 0.0164  351 THR A O   
2506 C CB  . THR A 353 ? 2.3251 0.9027 0.6018 0.0751  -0.1649 -0.0043 351 THR A CB  
2507 O OG1 . THR A 353 ? 2.2940 0.9107 0.5843 0.0730  -0.1150 -0.0135 351 THR A OG1 
2508 C CG2 . THR A 353 ? 2.3239 0.9351 0.6711 0.0827  -0.2271 -0.0156 351 THR A CG2 
2509 N N   . LEU A 354 ? 2.4426 0.9199 0.6388 0.0635  -0.1789 0.0353  352 LEU A N   
2510 C CA  . LEU A 354 ? 2.5066 0.9296 0.6727 0.0719  -0.2270 0.0425  352 LEU A CA  
2511 C C   . LEU A 354 ? 2.4403 0.8929 0.6623 0.0649  -0.2343 0.0535  352 LEU A C   
2512 O O   . LEU A 354 ? 2.5365 0.9574 0.7529 0.0753  -0.2797 0.0571  352 LEU A O   
2513 C CB  . LEU A 354 ? 2.6477 0.9812 0.7014 0.0714  -0.2078 0.0524  352 LEU A CB  
2514 C CG  . LEU A 354 ? 2.7320 1.0227 0.7164 0.0807  -0.2016 0.0425  352 LEU A CG  
2515 C CD1 . LEU A 354 ? 2.8811 1.0797 0.7508 0.0804  -0.1829 0.0534  352 LEU A CD1 
2516 C CD2 . LEU A 354 ? 2.7274 1.0154 0.7318 0.0983  -0.2667 0.0270  352 LEU A CD2 
2517 N N   . GLU A 355 ? 2.3534 0.8651 0.6297 0.0488  -0.1918 0.0582  353 GLU A N   
2518 C CA  . GLU A 355 ? 2.3181 0.8505 0.6403 0.0410  -0.1944 0.0698  353 GLU A CA  
2519 C C   . GLU A 355 ? 2.2166 0.7967 0.6231 0.0553  -0.2503 0.0614  353 GLU A C   
2520 O O   . GLU A 355 ? 2.1651 0.7848 0.6148 0.0642  -0.2746 0.0463  353 GLU A O   
2521 C CB  . GLU A 355 ? 2.2398 0.8214 0.5970 0.0176  -0.1321 0.0773  353 GLU A CB  
2522 C CG  . GLU A 355 ? 2.3241 0.8726 0.6149 0.0009  -0.0713 0.0865  353 GLU A CG  
2523 C CD  . GLU A 355 ? 2.4626 0.9382 0.6872 -0.0057 -0.0695 0.1028  353 GLU A CD  
2524 O OE1 . GLU A 355 ? 2.4302 0.8795 0.6588 0.0048  -0.1161 0.1062  353 GLU A OE1 
2525 O OE2 . GLU A 355 ? 2.5424 0.9888 0.7128 -0.0207 -0.0207 0.1117  353 GLU A OE2 
2526 N N   . GLN A 356 ? 2.2036 0.7808 0.6367 0.0573  -0.2696 0.0710  354 GLN A N   
2527 C CA  . GLN A 356 ? 2.1317 0.7580 0.6516 0.0724  -0.3193 0.0644  354 GLN A CA  
2528 C C   . GLN A 356 ? 2.0006 0.7091 0.6054 0.0643  -0.3020 0.0595  354 GLN A C   
2529 O O   . GLN A 356 ? 1.9286 0.6894 0.6094 0.0762  -0.3401 0.0489  354 GLN A O   
2530 C CB  . GLN A 356 ? 2.1469 0.7484 0.6726 0.0783  -0.3376 0.0757  354 GLN A CB  
2531 C CG  . GLN A 356 ? 2.0750 0.7273 0.6932 0.0975  -0.3875 0.0691  354 GLN A CG  
2532 C CD  . GLN A 356 ? 2.0960 0.7262 0.7213 0.1042  -0.3970 0.0796  354 GLN A CD  
2533 O OE1 . GLN A 356 ? 2.1661 0.7398 0.7246 0.0922  -0.3681 0.0922  354 GLN A OE1 
2534 N NE2 . GLN A 356 ? 2.0375 0.7143 0.7469 0.1232  -0.4358 0.0738  354 GLN A NE2 
2535 N N   . TYR A 357 ? 1.9786 0.7016 0.5746 0.0434  -0.2445 0.0665  355 TYR A N   
2536 C CA  . TYR A 357 ? 1.8688 0.6750 0.5539 0.0330  -0.2198 0.0599  355 TYR A CA  
2537 C C   . TYR A 357 ? 1.8573 0.6819 0.5214 0.0219  -0.1747 0.0506  355 TYR A C   
2538 O O   . TYR A 357 ? 2.0145 0.8095 0.6193 0.0063  -0.1256 0.0610  355 TYR A O   
2539 C CB  . TYR A 357 ? 1.8290 0.6573 0.5619 0.0171  -0.1886 0.0713  355 TYR A CB  
2540 C CG  . TYR A 357 ? 1.8617 0.6729 0.6190 0.0324  -0.2327 0.0781  355 TYR A CG  
2541 C CD1 . TYR A 357 ? 1.8645 0.7057 0.6773 0.0556  -0.2866 0.0669  355 TYR A CD1 
2542 C CD2 . TYR A 357 ? 1.9983 0.7596 0.7203 0.0245  -0.2211 0.0960  355 TYR A CD2 
2543 C CE1 . TYR A 357 ? 1.8797 0.7095 0.7189 0.0735  -0.3258 0.0723  355 TYR A CE1 
2544 C CE2 . TYR A 357 ? 1.9637 0.7050 0.7047 0.0429  -0.2618 0.1011  355 TYR A CE2 
2545 C CZ  . TYR A 357 ? 1.8878 0.6657 0.6887 0.0692  -0.3136 0.0891  355 TYR A CZ  
2546 O OH  . TYR A 357 ? 1.8634 0.6400 0.7023 0.0892  -0.3485 0.0888  355 TYR A OH  
2547 N N   . VAL A 358 ? 1.7997 0.6725 0.5134 0.0302  -0.1905 0.0314  356 VAL A N   
2548 C CA  . VAL A 358 ? 1.7976 0.6875 0.4947 0.0254  -0.1534 0.0196  356 VAL A CA  
2549 C C   . VAL A 358 ? 1.7116 0.7030 0.5337 0.0184  -0.1324 0.0067  356 VAL A C   
2550 O O   . VAL A 358 ? 1.5889 0.6278 0.4925 0.0256  -0.1676 -0.0030 356 VAL A O   
2551 C CB  . VAL A 358 ? 1.8614 0.7086 0.4989 0.0416  -0.1901 0.0071  356 VAL A CB  
2552 C CG1 . VAL A 358 ? 1.8603 0.7513 0.5262 0.0418  -0.1691 -0.0120 356 VAL A CG1 
2553 C CG2 . VAL A 358 ? 2.0325 0.8014 0.5737 0.0439  -0.1787 0.0163  356 VAL A CG2 
2554 N N   . PHE A 359 ? 1.6400 0.6644 0.4771 0.0044  -0.0749 0.0072  357 PHE A N   
2555 C CA  . PHE A 359 ? 1.5950 0.7105 0.5399 -0.0019 -0.0509 -0.0042 357 PHE A CA  
2556 C C   . PHE A 359 ? 1.6476 0.7691 0.5666 0.0044  -0.0266 -0.0182 357 PHE A C   
2557 O O   . PHE A 359 ? 1.6034 0.7003 0.4613 -0.0006 0.0171  -0.0137 357 PHE A O   
2558 C CB  . PHE A 359 ? 1.5308 0.6822 0.5195 -0.0221 -0.0080 0.0071  357 PHE A CB  
2559 C CG  . PHE A 359 ? 1.5594 0.6955 0.5655 -0.0268 -0.0310 0.0199  357 PHE A CG  
2560 C CD1 . PHE A 359 ? 1.6532 0.7086 0.5692 -0.0291 -0.0372 0.0369  357 PHE A CD1 
2561 C CD2 . PHE A 359 ? 1.4483 0.6449 0.5544 -0.0275 -0.0456 0.0151  357 PHE A CD2 
2562 C CE1 . PHE A 359 ? 1.6495 0.6845 0.5772 -0.0304 -0.0593 0.0482  357 PHE A CE1 
2563 C CE2 . PHE A 359 ? 1.4965 0.6749 0.6145 -0.0285 -0.0655 0.0255  357 PHE A CE2 
2564 C CZ  . PHE A 359 ? 1.5886 0.6861 0.6188 -0.0294 -0.0731 0.0418  357 PHE A CZ  
2565 N N   . CYS A 360 ? 1.5031 0.6543 0.4661 0.0155  -0.0537 -0.0349 358 CYS A N   
2566 C CA  . CYS A 360 ? 1.5313 0.6765 0.4613 0.0250  -0.0372 -0.0498 358 CYS A CA  
2567 C C   . CYS A 360 ? 1.4816 0.6920 0.5037 0.0293  -0.0479 -0.0657 358 CYS A C   
2568 O O   . CYS A 360 ? 1.3721 0.6048 0.4517 0.0300  -0.0892 -0.0685 358 CYS A O   
2569 C CB  . CYS A 360 ? 1.6523 0.7113 0.4730 0.0381  -0.0711 -0.0541 358 CYS A CB  
2570 S SG  . CYS A 360 ? 1.7689 0.7965 0.5173 0.0518  -0.0451 -0.0718 358 CYS A SG  
2571 N N   . THR A 361 ? 1.5125 0.7528 0.5477 0.0329  -0.0094 -0.0754 359 THR A N   
2572 C CA  . THR A 361 ? 1.3874 0.6742 0.4905 0.0395  -0.0192 -0.0909 359 THR A CA  
2573 C C   . THR A 361 ? 1.4320 0.6670 0.4861 0.0507  -0.0641 -0.1035 359 THR A C   
2574 O O   . THR A 361 ? 1.4912 0.6531 0.4462 0.0571  -0.0766 -0.1038 359 THR A O   
2575 C CB  . THR A 361 ? 1.3358 0.6591 0.4552 0.0448  0.0313  -0.0985 359 THR A CB  
2576 O OG1 . THR A 361 ? 1.4560 0.7205 0.4745 0.0560  0.0534  -0.1030 359 THR A OG1 
2577 C CG2 . THR A 361 ? 1.2725 0.6528 0.4499 0.0305  0.0713  -0.0866 359 THR A CG2 
2578 N N   . VAL A 362 ? 1.3667 0.6370 0.4886 0.0517  -0.0894 -0.1138 360 VAL A N   
2579 C CA  . VAL A 362 ? 1.4733 0.6998 0.5629 0.0572  -0.1376 -0.1253 360 VAL A CA  
2580 C C   . VAL A 362 ? 1.4694 0.6303 0.4580 0.0708  -0.1274 -0.1379 360 VAL A C   
2581 O O   . VAL A 362 ? 1.5405 0.6508 0.4778 0.0742  -0.1591 -0.1358 360 VAL A O   
2582 C CB  . VAL A 362 ? 1.3833 0.6613 0.5655 0.0529  -0.1580 -0.1333 360 VAL A CB  
2583 C CG1 . VAL A 362 ? 1.4301 0.6612 0.5785 0.0552  -0.2055 -0.1461 360 VAL A CG1 
2584 C CG2 . VAL A 362 ? 1.2651 0.5987 0.5362 0.0416  -0.1717 -0.1217 360 VAL A CG2 
2585 N N   . ASN A 363 ? 1.4641 0.6442 0.4522 0.0794  -0.0799 -0.1445 361 ASN A N   
2586 C CA  . ASN A 363 ? 1.5876 0.7277 0.5143 0.0941  -0.0659 -0.1515 361 ASN A CA  
2587 C C   . ASN A 363 ? 1.7015 0.7863 0.5391 0.0972  -0.0531 -0.1407 361 ASN A C   
2588 O O   . ASN A 363 ? 1.7195 0.7563 0.4988 0.1079  -0.0590 -0.1445 361 ASN A O   
2589 C CB  . ASN A 363 ? 1.6521 0.8312 0.6052 0.1057  -0.0165 -0.1609 361 ASN A CB  
2590 C CG  . ASN A 363 ? 1.5576 0.7706 0.5798 0.1080  -0.0338 -0.1731 361 ASN A CG  
2591 O OD1 . ASN A 363 ? 1.6811 0.8683 0.7004 0.1085  -0.0718 -0.1786 361 ASN A OD1 
2592 N ND2 . ASN A 363 ? 1.5460 0.8234 0.6413 0.1075  -0.0057 -0.1735 361 ASN A ND2 
2593 N N   . ALA A 364 ? 1.7077 0.7939 0.5309 0.0876  -0.0358 -0.1269 362 ALA A N   
2594 C CA  . ALA A 364 ? 1.7361 0.7683 0.4755 0.0884  -0.0206 -0.1141 362 ALA A CA  
2595 C C   . ALA A 364 ? 1.7737 0.7599 0.4821 0.0825  -0.0720 -0.1035 362 ALA A C   
2596 O O   . ALA A 364 ? 1.8493 0.7884 0.4911 0.0810  -0.0635 -0.0903 362 ALA A O   
2597 C CB  . ALA A 364 ? 1.7255 0.7858 0.4662 0.0800  0.0375  -0.1030 362 ALA A CB  
2598 N N   . LEU A 365 ? 1.7253 0.7257 0.4844 0.0795  -0.1247 -0.1087 363 LEU A N   
2599 C CA  . LEU A 365 ? 1.7532 0.7215 0.4988 0.0761  -0.1752 -0.0990 363 LEU A CA  
2600 C C   . LEU A 365 ? 1.9218 0.8148 0.5808 0.0855  -0.1934 -0.0966 363 LEU A C   
2601 O O   . LEU A 365 ? 1.9077 0.7810 0.5442 0.0938  -0.1950 -0.1076 363 LEU A O   
2602 C CB  . LEU A 365 ? 1.6806 0.6872 0.5084 0.0716  -0.2263 -0.1063 363 LEU A CB  
2603 C CG  . LEU A 365 ? 1.6785 0.7455 0.5875 0.0614  -0.2285 -0.1044 363 LEU A CG  
2604 C CD1 . LEU A 365 ? 1.5793 0.6812 0.5688 0.0574  -0.2797 -0.1107 363 LEU A CD1 
2605 C CD2 . LEU A 365 ? 1.6009 0.6493 0.4808 0.0577  -0.2259 -0.0879 363 LEU A CD2 
2606 N N   . PRO A 366 ? 1.9790 0.8246 0.5857 0.0851  -0.2082 -0.0829 364 PRO A N   
2607 C CA  . PRO A 366 ? 2.0489 0.8188 0.5748 0.0943  -0.2336 -0.0816 364 PRO A CA  
2608 C C   . PRO A 366 ? 2.0419 0.8088 0.6048 0.0955  -0.3024 -0.0860 364 PRO A C   
2609 O O   . PRO A 366 ? 2.0004 0.8220 0.6483 0.0889  -0.3283 -0.0869 364 PRO A O   
2610 C CB  . PRO A 366 ? 2.1196 0.8455 0.5832 0.0921  -0.2177 -0.0642 364 PRO A CB  
2611 C CG  . PRO A 366 ? 2.0235 0.7998 0.5576 0.0822  -0.2268 -0.0563 364 PRO A CG  
2612 C CD  . PRO A 366 ? 1.9604 0.8133 0.5735 0.0767  -0.2008 -0.0674 364 PRO A CD  
2613 N N   . GLU A 367 ? 2.1402 0.8438 0.6402 0.1037  -0.3306 -0.0892 365 GLU A N   
2614 C CA  . GLU A 367 ? 2.2116 0.9074 0.7417 0.1042  -0.3964 -0.0928 365 GLU A CA  
2615 C C   . GLU A 367 ? 2.1943 0.8576 0.6996 0.1067  -0.4229 -0.0797 365 GLU A C   
2616 O O   . GLU A 367 ? 2.3051 0.8945 0.7185 0.1141  -0.4236 -0.0743 365 GLU A O   
2617 C CB  . GLU A 367 ? 2.2415 0.8817 0.7140 0.1114  -0.4154 -0.1029 365 GLU A CB  
2618 C CG  . GLU A 367 ? 2.2319 0.8821 0.6922 0.1141  -0.3710 -0.1134 365 GLU A CG  
2619 C CD  . GLU A 367 ? 2.2865 0.9085 0.7332 0.1175  -0.4004 -0.1263 365 GLU A CD  
2620 O OE1 . GLU A 367 ? 2.3157 0.9144 0.7674 0.1155  -0.4562 -0.1273 365 GLU A OE1 
2621 O OE2 . GLU A 367 ? 2.3207 0.9440 0.7532 0.1224  -0.3679 -0.1358 365 GLU A OE2 
2622 N N   . THR A 368 ? 2.1118 0.8283 0.6979 0.1016  -0.4443 -0.0749 366 THR A N   
2623 C CA  . THR A 368 ? 2.1550 0.8456 0.7232 0.1056  -0.4647 -0.0622 366 THR A CA  
2624 C C   . THR A 368 ? 2.1076 0.8523 0.7756 0.1049  -0.5151 -0.0635 366 THR A C   
2625 O O   . THR A 368 ? 2.0179 0.8112 0.7601 0.1000  -0.5378 -0.0738 366 THR A O   
2626 C CB  . THR A 368 ? 2.2168 0.9108 0.7618 0.1010  -0.4133 -0.0497 366 THR A CB  
2627 O OG1 . THR A 368 ? 2.2272 0.8878 0.7486 0.1055  -0.4338 -0.0369 366 THR A OG1 
2628 C CG2 . THR A 368 ? 2.0308 0.8095 0.6683 0.0914  -0.3917 -0.0520 366 THR A CG2 
2629 N N   . THR A 369 ? 2.1116 0.8478 0.7818 0.1099  -0.5303 -0.0526 367 THR A N   
2630 C CA  . THR A 369 ? 2.0324 0.8172 0.7935 0.1132  -0.5754 -0.0522 367 THR A CA  
2631 C C   . THR A 369 ? 1.9966 0.8080 0.7844 0.1133  -0.5544 -0.0405 367 THR A C   
2632 O O   . THR A 369 ? 2.0137 0.7863 0.7321 0.1113  -0.5143 -0.0305 367 THR A O   
2633 C CB  . THR A 369 ? 2.1268 0.8618 0.8574 0.1246  -0.6280 -0.0522 367 THR A CB  
2634 O OG1 . THR A 369 ? 2.1362 0.9205 0.9541 0.1304  -0.6641 -0.0500 367 THR A OG1 
2635 C CG2 . THR A 369 ? 2.2434 0.8876 0.8535 0.1320  -0.6128 -0.0423 367 THR A CG2 
2636 N N   . ALA A 370 ? 1.8959 0.7745 0.7865 0.1150  -0.5798 -0.0414 368 ALA A N   
2637 C CA  . ALA A 370 ? 1.8520 0.7535 0.7708 0.1177  -0.5653 -0.0302 368 ALA A CA  
2638 C C   . ALA A 370 ? 1.7884 0.7536 0.8167 0.1260  -0.6061 -0.0325 368 ALA A C   
2639 O O   . ALA A 370 ? 1.7654 0.7691 0.8585 0.1252  -0.6387 -0.0428 368 ALA A O   
2640 C CB  . ALA A 370 ? 1.7959 0.7334 0.7278 0.1051  -0.5141 -0.0286 368 ALA A CB  
2641 N N   . ASP A 371 ? 1.7653 0.7416 0.8153 0.1337  -0.6011 -0.0221 369 ASP A N   
2642 C CA  . ASP A 371 ? 1.7079 0.7470 0.8633 0.1450  -0.6319 -0.0231 369 ASP A CA  
2643 C C   . ASP A 371 ? 1.6767 0.8021 0.9324 0.1371  -0.6142 -0.0271 369 ASP A C   
2644 O O   . ASP A 371 ? 1.5758 0.7696 0.9337 0.1386  -0.6381 -0.0349 369 ASP A O   
2645 C CB  . ASP A 371 ? 1.7475 0.7537 0.8774 0.1598  -0.6336 -0.0107 369 ASP A CB  
2646 C CG  . ASP A 371 ? 1.9088 0.8221 0.9288 0.1664  -0.6465 -0.0059 369 ASP A CG  
2647 O OD1 . ASP A 371 ? 1.9334 0.8329 0.9528 0.1742  -0.6878 -0.0131 369 ASP A OD1 
2648 O OD2 . ASP A 371 ? 1.9664 0.8198 0.9006 0.1626  -0.6146 0.0054  369 ASP A OD2 
2649 N N   . ILE A 372 ? 1.5580 0.6810 0.7856 0.1275  -0.5711 -0.0215 370 ILE A N   
2650 C CA  . ILE A 372 ? 1.5063 0.7050 0.8196 0.1183  -0.5475 -0.0259 370 ILE A CA  
2651 C C   . ILE A 372 ? 1.5002 0.6902 0.7712 0.0990  -0.4967 -0.0308 370 ILE A C   
2652 O O   . ILE A 372 ? 1.5745 0.7076 0.7564 0.0951  -0.4663 -0.0225 370 ILE A O   
2653 C CB  . ILE A 372 ? 1.4997 0.7290 0.8669 0.1245  -0.5217 -0.0166 370 ILE A CB  
2654 C CG1 . ILE A 372 ? 1.4727 0.6965 0.8646 0.1495  -0.5699 -0.0102 370 ILE A CG1 
2655 C CG2 . ILE A 372 ? 1.4024 0.7209 0.8791 0.1131  -0.4878 -0.0247 370 ILE A CG2 
2656 C CD1 . ILE A 372 ? 1.3904 0.6272 0.8172 0.1588  -0.5458 -0.0014 370 ILE A CD1 
2657 N N   . VAL A 373 ? 1.4222 0.6678 0.7568 0.0873  -0.4876 -0.0437 371 VAL A N   
2658 C CA  . VAL A 373 ? 1.3566 0.6090 0.6730 0.0722  -0.4382 -0.0497 371 VAL A CA  
2659 C C   . VAL A 373 ? 1.2200 0.5515 0.6383 0.0643  -0.4019 -0.0508 371 VAL A C   
2660 O O   . VAL A 373 ? 1.1581 0.5484 0.6686 0.0651  -0.4199 -0.0554 371 VAL A O   
2661 C CB  . VAL A 373 ? 1.3562 0.5970 0.6510 0.0664  -0.4565 -0.0642 371 VAL A CB  
2662 C CG1 . VAL A 373 ? 1.3447 0.6216 0.6664 0.0538  -0.4084 -0.0723 371 VAL A CG1 
2663 C CG2 . VAL A 373 ? 1.4772 0.6263 0.6440 0.0725  -0.4746 -0.0636 371 VAL A CG2 
2664 N N   . VAL A 374 ? 1.2790 0.6116 0.6800 0.0562  -0.3510 -0.0462 372 VAL A N   
2665 C CA  . VAL A 374 ? 1.1823 0.5816 0.6662 0.0482  -0.3152 -0.0475 372 VAL A CA  
2666 C C   . VAL A 374 ? 1.1507 0.5665 0.6305 0.0369  -0.2804 -0.0564 372 VAL A C   
2667 O O   . VAL A 374 ? 1.2189 0.5996 0.6314 0.0328  -0.2513 -0.0542 372 VAL A O   
2668 C CB  . VAL A 374 ? 1.2271 0.6182 0.7038 0.0475  -0.2886 -0.0355 372 VAL A CB  
2669 C CG1 . VAL A 374 ? 1.0948 0.5495 0.6482 0.0384  -0.2530 -0.0384 372 VAL A CG1 
2670 C CG2 . VAL A 374 ? 1.1848 0.5567 0.6661 0.0628  -0.3246 -0.0274 372 VAL A CG2 
2671 N N   . PHE A 375 ? 1.0451 0.5134 0.5964 0.0327  -0.2825 -0.0659 373 PHE A N   
2672 C CA  . PHE A 375 ? 1.0772 0.5653 0.6351 0.0250  -0.2520 -0.0747 373 PHE A CA  
2673 C C   . PHE A 375 ? 1.0273 0.5766 0.6619 0.0194  -0.2217 -0.0731 373 PHE A C   
2674 O O   . PHE A 375 ? 0.8950 0.4875 0.6021 0.0193  -0.2346 -0.0744 373 PHE A O   
2675 C CB  . PHE A 375 ? 1.0334 0.5232 0.6043 0.0237  -0.2803 -0.0863 373 PHE A CB  
2676 C CG  . PHE A 375 ? 1.0328 0.5152 0.5773 0.0206  -0.2559 -0.0963 373 PHE A CG  
2677 C CD1 . PHE A 375 ? 1.0545 0.5554 0.5992 0.0190  -0.2095 -0.0953 373 PHE A CD1 
2678 C CD2 . PHE A 375 ? 1.1488 0.6064 0.6720 0.0199  -0.2818 -0.1074 373 PHE A CD2 
2679 C CE1 . PHE A 375 ? 1.0592 0.5553 0.5834 0.0204  -0.1884 -0.1050 373 PHE A CE1 
2680 C CE2 . PHE A 375 ? 1.1806 0.6261 0.6768 0.0204  -0.2605 -0.1175 373 PHE A CE2 
2681 C CZ  . PHE A 375 ? 1.0950 0.5612 0.5927 0.0224  -0.2132 -0.1162 373 PHE A CZ  
2682 N N   . ASP A 376 ? 1.0666 0.6198 0.6850 0.0144  -0.1815 -0.0705 374 ASP A N   
2683 C CA  . ASP A 376 ? 1.0113 0.6158 0.6922 0.0087  -0.1543 -0.0693 374 ASP A CA  
2684 C C   . ASP A 376 ? 0.8897 0.5245 0.5938 0.0055  -0.1325 -0.0784 374 ASP A C   
2685 O O   . ASP A 376 ? 0.8911 0.5034 0.5569 0.0082  -0.1332 -0.0854 374 ASP A O   
2686 C CB  . ASP A 376 ? 1.0344 0.6249 0.6886 0.0033  -0.1283 -0.0597 374 ASP A CB  
2687 C CG  . ASP A 376 ? 1.0935 0.7276 0.8093 -0.0019 -0.1120 -0.0576 374 ASP A CG  
2688 O OD1 . ASP A 376 ? 1.0540 0.7280 0.8304 0.0007  -0.1200 -0.0627 374 ASP A OD1 
2689 O OD2 . ASP A 376 ? 1.1698 0.7946 0.8699 -0.0096 -0.0912 -0.0508 374 ASP A OD2 
2690 N N   . GLU A 377 ? 0.8182 0.5003 0.5813 0.0014  -0.1143 -0.0786 375 GLU A N   
2691 C CA  . GLU A 377 ? 0.8020 0.5139 0.5906 0.0003  -0.0953 -0.0861 375 GLU A CA  
2692 C C   . GLU A 377 ? 0.7645 0.4701 0.5578 0.0034  -0.1172 -0.0941 375 GLU A C   
2693 O O   . GLU A 377 ? 0.7667 0.4625 0.5379 0.0067  -0.1086 -0.1016 375 GLU A O   
2694 C CB  . GLU A 377 ? 0.8235 0.5279 0.5748 -0.0001 -0.0643 -0.0875 375 GLU A CB  
2695 C CG  . GLU A 377 ? 0.8746 0.6234 0.6688 -0.0007 -0.0401 -0.0921 375 GLU A CG  
2696 C CD  . GLU A 377 ? 1.0324 0.7837 0.8010 0.0001  -0.0085 -0.0936 375 GLU A CD  
2697 O OE1 . GLU A 377 ? 1.0813 0.8033 0.8019 0.0077  -0.0044 -0.0987 375 GLU A OE1 
2698 O OE2 . GLU A 377 ? 0.9557 0.7395 0.7538 -0.0069 0.0126  -0.0904 375 GLU A OE2 
2699 N N   . ILE A 378 ? 0.7545 0.4661 0.5791 0.0024  -0.1456 -0.0926 376 ILE A N   
2700 C CA  . ILE A 378 ? 0.8093 0.5120 0.6400 0.0010  -0.1713 -0.0991 376 ILE A CA  
2701 C C   . ILE A 378 ? 0.7202 0.4474 0.5848 -0.0022 -0.1590 -0.1045 376 ILE A C   
2702 O O   . ILE A 378 ? 0.7822 0.4904 0.6358 -0.0044 -0.1745 -0.1112 376 ILE A O   
2703 C CB  . ILE A 378 ? 0.8320 0.5462 0.7015 -0.0006 -0.2031 -0.0952 376 ILE A CB  
2704 C CG1 . ILE A 378 ? 0.8764 0.5573 0.7194 -0.0023 -0.2396 -0.1009 376 ILE A CG1 
2705 C CG2 . ILE A 378 ? 0.8027 0.5674 0.7484 -0.0055 -0.1968 -0.0935 376 ILE A CG2 
2706 C CD1 . ILE A 378 ? 0.9820 0.6047 0.7376 0.0038  -0.2452 -0.1033 376 ILE A CD1 
2707 N N   . SER A 379 ? 0.6308 0.3943 0.5320 -0.0028 -0.1338 -0.1017 377 SER A N   
2708 C CA  . SER A 379 ? 0.6788 0.4586 0.6032 -0.0039 -0.1231 -0.1060 377 SER A CA  
2709 C C   . SER A 379 ? 0.7520 0.5040 0.6289 0.0033  -0.1132 -0.1140 377 SER A C   
2710 O O   . SER A 379 ? 0.6560 0.3996 0.5338 0.0042  -0.1163 -0.1195 377 SER A O   
2711 C CB  . SER A 379 ? 0.6132 0.4322 0.5773 -0.0042 -0.1004 -0.1018 377 SER A CB  
2712 O OG  . SER A 379 ? 0.6215 0.4438 0.5653 -0.0002 -0.0782 -0.1016 377 SER A OG  
2713 N N   . MET A 380 ? 0.7616 0.4965 0.5948 0.0090  -0.1000 -0.1145 378 MET A N   
2714 C CA  . MET A 380 ? 0.8285 0.5406 0.6161 0.0189  -0.0843 -0.1222 378 MET A CA  
2715 C C   . MET A 380 ? 0.8539 0.5122 0.5832 0.0223  -0.1053 -0.1293 378 MET A C   
2716 O O   . MET A 380 ? 0.9906 0.6211 0.6706 0.0330  -0.0920 -0.1368 378 MET A O   
2717 C CB  . MET A 380 ? 0.8625 0.5836 0.6314 0.0215  -0.0559 -0.1186 378 MET A CB  
2718 C CG  . MET A 380 ? 0.8320 0.6027 0.6519 0.0184  -0.0346 -0.1142 378 MET A CG  
2719 S SD  . MET A 380 ? 0.8798 0.6732 0.7210 0.0301  -0.0192 -0.1225 378 MET A SD  
2720 C CE  . MET A 380 ? 0.7531 0.5259 0.5403 0.0428  0.0052  -0.1291 378 MET A CE  
2721 N N   . ALA A 381 ? 0.8615 0.5047 0.5960 0.0143  -0.1383 -0.1279 379 ALA A N   
2722 C CA  . ALA A 381 ? 0.9021 0.4913 0.5794 0.0156  -0.1651 -0.1347 379 ALA A CA  
2723 C C   . ALA A 381 ? 0.9405 0.5133 0.6248 0.0120  -0.1837 -0.1433 379 ALA A C   
2724 O O   . ALA A 381 ? 0.9136 0.5192 0.6577 0.0033  -0.1868 -0.1403 379 ALA A O   
2725 C CB  . ALA A 381 ? 0.8995 0.4801 0.5780 0.0091  -0.1961 -0.1284 379 ALA A CB  
2726 N N   . THR A 382 ? 1.0246 0.5414 0.6421 0.0183  -0.1949 -0.1541 380 THR A N   
2727 C CA  . THR A 382 ? 1.0748 0.5601 0.6851 0.0130  -0.2188 -0.1633 380 THR A CA  
2728 C C   . THR A 382 ? 1.1065 0.5585 0.6975 0.0018  -0.2639 -0.1655 380 THR A C   
2729 O O   . THR A 382 ? 1.0823 0.5213 0.6431 0.0044  -0.2746 -0.1621 380 THR A O   
2730 C CB  . THR A 382 ? 1.1443 0.5832 0.6895 0.0295  -0.2028 -0.1763 380 THR A CB  
2731 O OG1 . THR A 382 ? 1.2029 0.5970 0.6690 0.0407  -0.2003 -0.1813 380 THR A OG1 
2732 C CG2 . THR A 382 ? 1.0374 0.5154 0.6109 0.0421  -0.1619 -0.1745 380 THR A CG2 
2733 N N   . ASN A 383 ? 1.0901 0.5301 0.7015 -0.0115 -0.2911 -0.1694 381 ASN A N   
2734 C CA  . ASN A 383 ? 1.0711 0.4971 0.6800 -0.0217 -0.3295 -0.1658 381 ASN A CA  
2735 C C   . ASN A 383 ? 1.2124 0.5800 0.7311 -0.0082 -0.3354 -0.1703 381 ASN A C   
2736 O O   . ASN A 383 ? 1.2074 0.5590 0.7100 -0.0112 -0.3658 -0.1666 381 ASN A O   
2737 C CB  . ASN A 383 ? 1.0413 0.4747 0.6946 -0.0391 -0.3478 -0.1644 381 ASN A CB  
2738 C CG  . ASN A 383 ? 1.0641 0.5579 0.8117 -0.0571 -0.3561 -0.1556 381 ASN A CG  
2739 O OD1 . ASN A 383 ? 1.0112 0.5394 0.7904 -0.0552 -0.3538 -0.1510 381 ASN A OD1 
2740 N ND2 . ASN A 383 ? 1.0155 0.5210 0.8068 -0.0746 -0.3637 -0.1530 381 ASN A ND2 
2741 N N   . TYR A 384 ? 1.2091 0.5451 0.6695 0.0082  -0.3061 -0.1779 382 TYR A N   
2742 C CA  . TYR A 384 ? 1.2847 0.5660 0.6563 0.0228  -0.3043 -0.1815 382 TYR A CA  
2743 C C   . TYR A 384 ? 1.3188 0.5997 0.6629 0.0282  -0.2996 -0.1757 382 TYR A C   
2744 O O   . TYR A 384 ? 1.3397 0.5852 0.6372 0.0298  -0.3227 -0.1723 382 TYR A O   
2745 C CB  . TYR A 384 ? 1.2702 0.5284 0.5960 0.0414  -0.2676 -0.1905 382 TYR A CB  
2746 C CG  . TYR A 384 ? 1.4428 0.6401 0.6784 0.0561  -0.2660 -0.1952 382 TYR A CG  
2747 C CD1 . TYR A 384 ? 1.4268 0.6060 0.6036 0.0697  -0.2421 -0.1939 382 TYR A CD1 
2748 C CD2 . TYR A 384 ? 1.4618 0.6167 0.6683 0.0557  -0.2868 -0.2004 382 TYR A CD2 
2749 C CE1 . TYR A 384 ? 1.4987 0.6205 0.5912 0.0833  -0.2380 -0.1975 382 TYR A CE1 
2750 C CE2 . TYR A 384 ? 1.5253 0.6206 0.6465 0.0701  -0.2855 -0.2051 382 TYR A CE2 
2751 C CZ  . TYR A 384 ? 1.5925 0.6720 0.6572 0.0844  -0.2604 -0.2035 382 TYR A CZ  
2752 O OH  . TYR A 384 ? 1.6601 0.6782 0.6376 0.0989  -0.2568 -0.2076 382 TYR A OH  
2753 N N   . ASP A 385 ? 1.2145 0.5302 0.5833 0.0311  -0.2701 -0.1743 383 ASP A N   
2754 C CA  . ASP A 385 ? 1.3394 0.6537 0.6833 0.0340  -0.2638 -0.1678 383 ASP A CA  
2755 C C   . ASP A 385 ? 1.3436 0.6655 0.7162 0.0231  -0.3069 -0.1591 383 ASP A C   
2756 O O   . ASP A 385 ? 1.3122 0.6016 0.6327 0.0281  -0.3189 -0.1533 383 ASP A O   
2757 C CB  . ASP A 385 ? 1.1651 0.5425 0.5685 0.0349  -0.2217 -0.1587 383 ASP A CB  
2758 C CG  . ASP A 385 ? 1.3004 0.6801 0.6827 0.0483  -0.1773 -0.1650 383 ASP A CG  
2759 O OD1 . ASP A 385 ? 1.3437 0.6805 0.6477 0.0606  -0.1591 -0.1696 383 ASP A OD1 
2760 O OD2 . ASP A 385 ? 1.2495 0.6742 0.6933 0.0477  -0.1602 -0.1651 383 ASP A OD2 
2761 N N   . LEU A 386 ? 1.2445 0.6096 0.7008 0.0094  -0.3294 -0.1573 384 LEU A N   
2762 C CA  . LEU A 386 ? 1.2235 0.6073 0.7214 0.0013  -0.3683 -0.1493 384 LEU A CA  
2763 C C   . LEU A 386 ? 1.2677 0.6056 0.7173 0.0034  -0.4029 -0.1482 384 LEU A C   
2764 O O   . LEU A 386 ? 1.3169 0.6443 0.7555 0.0064  -0.4294 -0.1414 384 LEU A O   
2765 C CB  . LEU A 386 ? 1.0774 0.5200 0.6777 -0.0141 -0.3798 -0.1475 384 LEU A CB  
2766 C CG  . LEU A 386 ? 1.1116 0.6160 0.7803 -0.0147 -0.3429 -0.1400 384 LEU A CG  
2767 C CD1 . LEU A 386 ? 1.1561 0.7140 0.9200 -0.0299 -0.3553 -0.1366 384 LEU A CD1 
2768 C CD2 . LEU A 386 ? 1.1014 0.6217 0.7687 -0.0055 -0.3295 -0.1290 384 LEU A CD2 
2769 N N   . SER A 387 ? 1.3262 0.6331 0.7457 0.0028  -0.4047 -0.1550 385 SER A N   
2770 C CA  . SER A 387 ? 1.3402 0.5978 0.7104 0.0043  -0.4384 -0.1554 385 SER A CA  
2771 C C   . SER A 387 ? 1.4784 0.6784 0.7496 0.0206  -0.4293 -0.1538 385 SER A C   
2772 O O   . SER A 387 ? 1.4874 0.6577 0.7282 0.0236  -0.4603 -0.1486 385 SER A O   
2773 C CB  . SER A 387 ? 1.3728 0.6065 0.7304 -0.0003 -0.4404 -0.1637 385 SER A CB  
2774 O OG  . SER A 387 ? 1.4683 0.6440 0.7634 0.0031  -0.4696 -0.1657 385 SER A OG  
2775 N N   . VAL A 388 ? 1.4605 0.6437 0.6808 0.0318  -0.3853 -0.1578 386 VAL A N   
2776 C CA  . VAL A 388 ? 1.5617 0.6922 0.6874 0.0460  -0.3674 -0.1550 386 VAL A CA  
2777 C C   . VAL A 388 ? 1.5751 0.7064 0.6972 0.0461  -0.3828 -0.1436 386 VAL A C   
2778 O O   . VAL A 388 ? 1.6388 0.7168 0.6895 0.0538  -0.3953 -0.1383 386 VAL A O   
2779 C CB  . VAL A 388 ? 1.4853 0.6194 0.5821 0.0561  -0.3112 -0.1599 386 VAL A CB  
2780 C CG1 . VAL A 388 ? 1.5819 0.6726 0.5921 0.0674  -0.2861 -0.1540 386 VAL A CG1 
2781 C CG2 . VAL A 388 ? 1.5439 0.6628 0.6273 0.0618  -0.2987 -0.1711 386 VAL A CG2 
2782 N N   . VAL A 389 ? 1.4321 0.6196 0.6285 0.0385  -0.3825 -0.1395 387 VAL A N   
2783 C CA  . VAL A 389 ? 1.5155 0.7038 0.7100 0.0404  -0.3959 -0.1285 387 VAL A CA  
2784 C C   . VAL A 389 ? 1.5625 0.7405 0.7743 0.0395  -0.4499 -0.1239 387 VAL A C   
2785 O O   . VAL A 389 ? 1.5996 0.7322 0.7537 0.0480  -0.4667 -0.1165 387 VAL A O   
2786 C CB  . VAL A 389 ? 1.3872 0.6372 0.6576 0.0338  -0.3811 -0.1268 387 VAL A CB  
2787 C CG1 . VAL A 389 ? 1.4140 0.6670 0.6941 0.0366  -0.4049 -0.1154 387 VAL A CG1 
2788 C CG2 . VAL A 389 ? 1.3518 0.6107 0.6028 0.0364  -0.3237 -0.1278 387 VAL A CG2 
2789 N N   . ASN A 390 ? 1.5196 0.7398 0.8130 0.0288  -0.4766 -0.1279 388 ASN A N   
2790 C CA  . ASN A 390 ? 1.4406 0.6602 0.7636 0.0267  -0.5268 -0.1247 388 ASN A CA  
2791 C C   . ASN A 390 ? 1.6079 0.7532 0.8428 0.0336  -0.5475 -0.1267 388 ASN A C   
2792 O O   . ASN A 390 ? 1.6197 0.7525 0.8630 0.0343  -0.5904 -0.1242 388 ASN A O   
2793 C CB  . ASN A 390 ? 1.4165 0.6952 0.8411 0.0109  -0.5430 -0.1288 388 ASN A CB  
2794 C CG  . ASN A 390 ? 1.4787 0.8295 1.0028 0.0066  -0.5478 -0.1229 388 ASN A CG  
2795 O OD1 . ASN A 390 ? 1.4639 0.8170 0.9806 0.0168  -0.5463 -0.1160 388 ASN A OD1 
2796 N ND2 . ASN A 390 ? 1.4517 0.8595 1.0670 -0.0084 -0.5508 -0.1251 388 ASN A ND2 
2797 N N   . ALA A 391 ? 1.6019 0.6983 0.7538 0.0398  -0.5173 -0.1316 389 ALA A N   
2798 C CA  . ALA A 391 ? 1.7571 0.7770 0.8157 0.0481  -0.5314 -0.1340 389 ALA A CA  
2799 C C   . ALA A 391 ? 1.8311 0.8004 0.8032 0.0615  -0.5156 -0.1256 389 ALA A C   
2800 O O   . ALA A 391 ? 2.0183 0.9580 0.9678 0.0665  -0.5485 -0.1191 389 ALA A O   
2801 C CB  . ALA A 391 ? 1.7409 0.7357 0.7599 0.0489  -0.5063 -0.1444 389 ALA A CB  
2802 N N   . ARG A 392 ? 1.7939 0.7528 0.7184 0.0669  -0.4641 -0.1255 390 ARG A N   
2803 C CA  . ARG A 392 ? 1.9578 0.8645 0.7930 0.0771  -0.4407 -0.1168 390 ARG A CA  
2804 C C   . ARG A 392 ? 1.9258 0.8380 0.7754 0.0780  -0.4602 -0.1043 390 ARG A C   
2805 O O   . ARG A 392 ? 1.9156 0.7707 0.6863 0.0858  -0.4558 -0.0956 390 ARG A O   
2806 C CB  . ARG A 392 ? 1.8162 0.7354 0.6283 0.0791  -0.3778 -0.1181 390 ARG A CB  
2807 C CG  . ARG A 392 ? 1.8326 0.7429 0.6244 0.0830  -0.3534 -0.1306 390 ARG A CG  
2808 C CD  . ARG A 392 ? 1.8507 0.7785 0.6257 0.0873  -0.2899 -0.1319 390 ARG A CD  
2809 N NE  . ARG A 392 ? 1.9045 0.8302 0.6709 0.0941  -0.2675 -0.1448 390 ARG A NE  
2810 C CZ  . ARG A 392 ? 1.8885 0.8338 0.6490 0.1008  -0.2137 -0.1491 390 ARG A CZ  
2811 N NH1 . ARG A 392 ? 1.8141 0.7891 0.5842 0.0983  -0.1751 -0.1419 390 ARG A NH1 
2812 N NH2 . ARG A 392 ? 1.8225 0.7588 0.5707 0.1105  -0.1987 -0.1609 390 ARG A NH2 
2813 N N   . LEU A 393 ? 1.8105 0.7870 0.7574 0.0710  -0.4813 -0.1029 391 LEU A N   
2814 C CA  . LEU A 393 ? 1.8328 0.8198 0.7999 0.0742  -0.4964 -0.0914 391 LEU A CA  
2815 C C   . LEU A 393 ? 1.7862 0.8058 0.8319 0.0732  -0.5514 -0.0921 391 LEU A C   
2816 O O   . LEU A 393 ? 1.6740 0.7632 0.8187 0.0644  -0.5590 -0.0965 391 LEU A O   
2817 C CB  . LEU A 393 ? 1.6642 0.7037 0.6769 0.0689  -0.4606 -0.0879 391 LEU A CB  
2818 C CG  . LEU A 393 ? 1.7341 0.7444 0.6751 0.0702  -0.4095 -0.0804 391 LEU A CG  
2819 C CD1 . LEU A 393 ? 1.8655 0.8347 0.7311 0.0724  -0.3739 -0.0864 391 LEU A CD1 
2820 C CD2 . LEU A 393 ? 1.6201 0.6921 0.6243 0.0620  -0.3804 -0.0813 391 LEU A CD2 
2821 N N   . ARG A 394 ? 1.7962 0.7673 0.8007 0.0820  -0.5879 -0.0880 392 ARG A N   
2822 C CA  . ARG A 394 ? 1.8307 0.8335 0.9098 0.0830  -0.6394 -0.0884 392 ARG A CA  
2823 C C   . ARG A 394 ? 1.8228 0.8421 0.9263 0.0923  -0.6441 -0.0777 392 ARG A C   
2824 O O   . ARG A 394 ? 1.8300 0.7905 0.8509 0.1018  -0.6341 -0.0691 392 ARG A O   
2825 C CB  . ARG A 394 ? 1.8968 0.8366 0.9181 0.0883  -0.6793 -0.0918 392 ARG A CB  
2826 C CG  . ARG A 394 ? 1.9239 0.9025 1.0295 0.0852  -0.7324 -0.0959 392 ARG A CG  
2827 C CD  . ARG A 394 ? 1.8892 0.9456 1.0992 0.0686  -0.7294 -0.1030 392 ARG A CD  
2828 N NE  . ARG A 394 ? 1.9053 0.9413 1.0768 0.0595  -0.7041 -0.1107 392 ARG A NE  
2829 C CZ  . ARG A 394 ? 1.9721 0.9467 1.0738 0.0594  -0.7189 -0.1169 392 ARG A CZ  
2830 N NH1 . ARG A 394 ? 1.9798 0.9110 1.0501 0.0649  -0.7636 -0.1173 392 ARG A NH1 
2831 N NH2 . ARG A 394 ? 1.9301 0.8874 0.9961 0.0542  -0.6898 -0.1237 392 ARG A NH2 
2832 N N   . ALA A 395 ? 1.7406 0.8374 0.9558 0.0898  -0.6576 -0.0777 393 ALA A N   
2833 C CA  . ALA A 395 ? 1.6471 0.7632 0.8891 0.1004  -0.6568 -0.0678 393 ALA A CA  
2834 C C   . ALA A 395 ? 1.5922 0.7808 0.9531 0.1035  -0.6908 -0.0692 393 ALA A C   
2835 O O   . ALA A 395 ? 1.6107 0.8469 1.0449 0.0931  -0.7075 -0.0772 393 ALA A O   
2836 C CB  . ALA A 395 ? 1.6338 0.7730 0.8771 0.0956  -0.6093 -0.0634 393 ALA A CB  
2837 N N   . LYS A 396 ? 1.5884 0.7849 0.9675 0.1181  -0.6975 -0.0607 394 LYS A N   
2838 C CA  . LYS A 396 ? 1.5441 0.8095 1.0340 0.1259  -0.7254 -0.0612 394 LYS A CA  
2839 C C   . LYS A 396 ? 1.4574 0.8088 1.0501 0.1190  -0.7002 -0.0620 394 LYS A C   
2840 O O   . LYS A 396 ? 1.3908 0.8146 1.0904 0.1161  -0.7151 -0.0662 394 LYS A O   
2841 C CB  . LYS A 396 ? 1.5928 0.8293 1.0585 0.1475  -0.7402 -0.0522 394 LYS A CB  
2842 C CG  . LYS A 396 ? 1.7161 0.8544 1.0607 0.1557  -0.7558 -0.0486 394 LYS A CG  
2843 C CD  . LYS A 396 ? 1.7564 0.8689 1.0812 0.1763  -0.7646 -0.0390 394 LYS A CD  
2844 C CE  . LYS A 396 ? 1.8871 0.9035 1.0983 0.1853  -0.7855 -0.0357 394 LYS A CE  
2845 N NZ  . LYS A 396 ? 1.9442 0.9561 1.1689 0.1875  -0.8337 -0.0445 394 LYS A NZ  
2846 N N   . HIS A 397 ? 1.4336 0.7779 0.9947 0.1158  -0.6611 -0.0577 395 HIS A N   
2847 C CA  . HIS A 397 ? 1.2831 0.7003 0.9303 0.1111  -0.6357 -0.0579 395 HIS A CA  
2848 C C   . HIS A 397 ? 1.3721 0.7728 0.9686 0.0968  -0.5969 -0.0602 395 HIS A C   
2849 O O   . HIS A 397 ? 1.4405 0.7776 0.9378 0.0988  -0.5777 -0.0543 395 HIS A O   
2850 C CB  . HIS A 397 ? 1.2689 0.7013 0.9451 0.1306  -0.6315 -0.0478 395 HIS A CB  
2851 C CG  . HIS A 397 ? 1.2891 0.7435 1.0200 0.1473  -0.6658 -0.0473 395 HIS A CG  
2852 N ND1 . HIS A 397 ? 1.2276 0.7677 1.0808 0.1481  -0.6746 -0.0520 395 HIS A ND1 
2853 C CD2 . HIS A 397 ? 1.3739 0.7767 1.0533 0.1635  -0.6922 -0.0428 395 HIS A CD2 
2854 C CE1 . HIS A 397 ? 1.2719 0.8156 1.1488 0.1651  -0.7052 -0.0507 395 HIS A CE1 
2855 N NE2 . HIS A 397 ? 1.3609 0.8209 1.1333 0.1752  -0.7183 -0.0456 395 HIS A NE2 
2856 N N   . TYR A 398 ? 1.2705 0.7288 0.9361 0.0811  -0.5813 -0.0689 396 TYR A N   
2857 C CA  . TYR A 398 ? 1.2239 0.6842 0.8698 0.0666  -0.5267 -0.0720 396 TYR A CA  
2858 C C   . TYR A 398 ? 1.1191 0.6493 0.8551 0.0646  -0.4876 -0.0687 396 TYR A C   
2859 O O   . TYR A 398 ? 1.0977 0.6907 0.9298 0.0638  -0.4999 -0.0708 396 TYR A O   
2860 C CB  . TYR A 398 ? 1.2065 0.6676 0.8516 0.0503  -0.5341 -0.0849 396 TYR A CB  
2861 C CG  . TYR A 398 ? 1.3101 0.7031 0.8705 0.0516  -0.5612 -0.0884 396 TYR A CG  
2862 C CD1 . TYR A 398 ? 1.4496 0.7758 0.9015 0.0521  -0.5378 -0.0897 396 TYR A CD1 
2863 C CD2 . TYR A 398 ? 1.3801 0.7801 0.9763 0.0523  -0.6007 -0.0893 396 TYR A CD2 
2864 C CE1 . TYR A 398 ? 1.5022 0.7672 0.8805 0.0551  -0.5541 -0.0912 396 TYR A CE1 
2865 C CE2 . TYR A 398 ? 1.3942 0.7314 0.9162 0.0537  -0.6208 -0.0918 396 TYR A CE2 
2866 C CZ  . TYR A 398 ? 1.4563 0.7246 0.8681 0.0559  -0.5976 -0.0926 396 TYR A CZ  
2867 O OH  . TYR A 398 ? 1.5389 0.7424 0.8747 0.0588  -0.6162 -0.0951 396 TYR A OH  
2868 N N   . VAL A 399 ? 1.0797 0.5989 0.7848 0.0631  -0.4406 -0.0635 397 VAL A N   
2869 C CA  . VAL A 399 ? 0.9907 0.5661 0.7669 0.0611  -0.4032 -0.0610 397 VAL A CA  
2870 C C   . VAL A 399 ? 1.0059 0.5947 0.7779 0.0457  -0.3603 -0.0664 397 VAL A C   
2871 O O   . VAL A 399 ? 1.0225 0.5694 0.7216 0.0419  -0.3378 -0.0656 397 VAL A O   
2872 C CB  . VAL A 399 ? 1.0594 0.6130 0.8119 0.0728  -0.3889 -0.0504 397 VAL A CB  
2873 C CG1 . VAL A 399 ? 0.9345 0.5391 0.7512 0.0699  -0.3505 -0.0498 397 VAL A CG1 
2874 C CG2 . VAL A 399 ? 1.0675 0.6080 0.8277 0.0924  -0.4336 -0.0452 397 VAL A CG2 
2875 N N   . TYR A 400 ? 0.9121 0.5595 0.7626 0.0378  -0.3484 -0.0714 398 TYR A N   
2876 C CA  . TYR A 400 ? 0.8703 0.5351 0.7265 0.0256  -0.3123 -0.0766 398 TYR A CA  
2877 C C   . TYR A 400 ? 0.8507 0.5555 0.7532 0.0258  -0.2767 -0.0725 398 TYR A C   
2878 O O   . TYR A 400 ? 0.8175 0.5678 0.7911 0.0282  -0.2790 -0.0716 398 TYR A O   
2879 C CB  . TYR A 400 ? 0.8514 0.5417 0.7507 0.0150  -0.3270 -0.0847 398 TYR A CB  
2880 C CG  . TYR A 400 ? 0.9646 0.6108 0.8150 0.0128  -0.3647 -0.0909 398 TYR A CG  
2881 C CD1 . TYR A 400 ? 0.9905 0.5888 0.7650 0.0099  -0.3549 -0.0972 398 TYR A CD1 
2882 C CD2 . TYR A 400 ? 0.9180 0.5700 0.7977 0.0147  -0.4110 -0.0912 398 TYR A CD2 
2883 C CE1 . TYR A 400 ? 1.0487 0.5987 0.7690 0.0088  -0.3902 -0.1043 398 TYR A CE1 
2884 C CE2 . TYR A 400 ? 1.0289 0.6363 0.8598 0.0117  -0.4500 -0.0979 398 TYR A CE2 
2885 C CZ  . TYR A 400 ? 1.0693 0.6220 0.8161 0.0086  -0.4394 -0.1047 398 TYR A CZ  
2886 O OH  . TYR A 400 ? 1.1769 0.6778 0.8665 0.0065  -0.4790 -0.1127 398 TYR A OH  
2887 N N   . ILE A 401 ? 0.8433 0.5314 0.7055 0.0230  -0.2437 -0.0704 399 ILE A N   
2888 C CA  . ILE A 401 ? 0.8310 0.5480 0.7254 0.0219  -0.2124 -0.0673 399 ILE A CA  
2889 C C   . ILE A 401 ? 0.8651 0.6033 0.7679 0.0121  -0.1826 -0.0727 399 ILE A C   
2890 O O   . ILE A 401 ? 0.8600 0.5738 0.7153 0.0084  -0.1726 -0.0757 399 ILE A O   
2891 C CB  . ILE A 401 ? 0.8963 0.5773 0.7423 0.0249  -0.2014 -0.0594 399 ILE A CB  
2892 C CG1 . ILE A 401 ? 0.9002 0.5513 0.7290 0.0378  -0.2349 -0.0536 399 ILE A CG1 
2893 C CG2 . ILE A 401 ? 0.8156 0.5230 0.6947 0.0222  -0.1735 -0.0576 399 ILE A CG2 
2894 C CD1 . ILE A 401 ? 0.9307 0.5362 0.7053 0.0405  -0.2267 -0.0443 399 ILE A CD1 
2895 N N   . GLY A 402 ? 0.7406 0.5219 0.7008 0.0099  -0.1683 -0.0740 400 GLY A N   
2896 C CA  . GLY A 402 ? 0.7649 0.5648 0.7323 0.0030  -0.1418 -0.0781 400 GLY A CA  
2897 C C   . GLY A 402 ? 0.7015 0.5430 0.7269 0.0021  -0.1298 -0.0783 400 GLY A C   
2898 O O   . GLY A 402 ? 0.6758 0.5312 0.7306 0.0074  -0.1327 -0.0750 400 GLY A O   
2899 N N   . ASP A 403 ? 0.6660 0.5235 0.7027 -0.0029 -0.1158 -0.0824 401 ASP A N   
2900 C CA  . ASP A 403 ? 0.5672 0.4579 0.6484 -0.0044 -0.1027 -0.0822 401 ASP A CA  
2901 C C   . ASP A 403 ? 0.5396 0.4356 0.6266 -0.0094 -0.0996 -0.0860 401 ASP A C   
2902 O O   . ASP A 403 ? 0.4928 0.3796 0.5535 -0.0091 -0.0882 -0.0895 401 ASP A O   
2903 C CB  . ASP A 403 ? 0.5435 0.4414 0.6205 -0.0038 -0.0809 -0.0813 401 ASP A CB  
2904 C CG  . ASP A 403 ? 0.4937 0.4186 0.6076 -0.0031 -0.0692 -0.0810 401 ASP A CG  
2905 O OD1 . ASP A 403 ? 0.4644 0.4049 0.6100 -0.0034 -0.0746 -0.0801 401 ASP A OD1 
2906 O OD2 . ASP A 403 ? 0.5182 0.4473 0.6278 -0.0033 -0.0545 -0.0817 401 ASP A OD2 
2907 N N   . PRO A 404 ? 0.5527 0.4632 0.6750 -0.0138 -0.1086 -0.0850 402 PRO A N   
2908 C CA  . PRO A 404 ? 0.5460 0.4538 0.6696 -0.0199 -0.1059 -0.0875 402 PRO A CA  
2909 C C   . PRO A 404 ? 0.5046 0.4256 0.6331 -0.0184 -0.0830 -0.0868 402 PRO A C   
2910 O O   . PRO A 404 ? 0.4786 0.3916 0.6007 -0.0209 -0.0800 -0.0884 402 PRO A O   
2911 C CB  . PRO A 404 ? 0.6307 0.5532 0.7966 -0.0285 -0.1208 -0.0846 402 PRO A CB  
2912 C CG  . PRO A 404 ? 0.5572 0.5077 0.7583 -0.0231 -0.1155 -0.0800 402 PRO A CG  
2913 C CD  . PRO A 404 ? 0.5164 0.4479 0.6825 -0.0138 -0.1204 -0.0812 402 PRO A CD  
2914 N N   . ALA A 405 ? 0.4758 0.4117 0.6111 -0.0139 -0.0692 -0.0849 403 ALA A N   
2915 C CA  . ALA A 405 ? 0.4931 0.4390 0.6286 -0.0120 -0.0515 -0.0849 403 ALA A CA  
2916 C C   . ALA A 405 ? 0.4904 0.4292 0.5971 -0.0080 -0.0444 -0.0891 403 ALA A C   
2917 O O   . ALA A 405 ? 0.5151 0.4636 0.6220 -0.0056 -0.0334 -0.0900 403 ALA A O   
2918 C CB  . ALA A 405 ? 0.4219 0.3841 0.5768 -0.0094 -0.0415 -0.0821 403 ALA A CB  
2919 N N   . GLN A 406 ? 0.4974 0.4206 0.5799 -0.0071 -0.0505 -0.0916 404 GLN A N   
2920 C CA  . GLN A 406 ? 0.4603 0.3801 0.5187 -0.0037 -0.0408 -0.0953 404 GLN A CA  
2921 C C   . GLN A 406 ? 0.5051 0.4083 0.5431 0.0012  -0.0441 -0.1004 404 GLN A C   
2922 O O   . GLN A 406 ? 0.4906 0.3829 0.5331 -0.0004 -0.0546 -0.1006 404 GLN A O   
2923 C CB  . GLN A 406 ? 0.5265 0.4364 0.5664 -0.0060 -0.0405 -0.0934 404 GLN A CB  
2924 C CG  . GLN A 406 ? 0.5140 0.4345 0.5716 -0.0091 -0.0376 -0.0894 404 GLN A CG  
2925 C CD  . GLN A 406 ? 0.5307 0.4401 0.5676 -0.0132 -0.0320 -0.0870 404 GLN A CD  
2926 O OE1 . GLN A 406 ? 0.5302 0.4423 0.5532 -0.0162 -0.0199 -0.0884 404 GLN A OE1 
2927 N NE2 . GLN A 406 ? 0.5599 0.4572 0.5964 -0.0131 -0.0397 -0.0829 404 GLN A NE2 
2928 N N   . LEU A 407 ? 0.5132 0.4131 0.5285 0.0068  -0.0340 -0.1045 405 LEU A N   
2929 C CA  . LEU A 407 ? 0.5245 0.4089 0.5195 0.0160  -0.0334 -0.1109 405 LEU A CA  
2930 C C   . LEU A 407 ? 0.6261 0.4735 0.5859 0.0164  -0.0468 -0.1143 405 LEU A C   
2931 O O   . LEU A 407 ? 0.5966 0.4316 0.5381 0.0124  -0.0515 -0.1123 405 LEU A O   
2932 C CB  . LEU A 407 ? 0.5589 0.4598 0.5486 0.0247  -0.0147 -0.1148 405 LEU A CB  
2933 C CG  . LEU A 407 ? 0.5157 0.4497 0.5384 0.0266  -0.0077 -0.1137 405 LEU A CG  
2934 C CD1 . LEU A 407 ? 0.5386 0.4999 0.5688 0.0313  0.0093  -0.1167 405 LEU A CD1 
2935 C CD2 . LEU A 407 ? 0.5410 0.4663 0.5671 0.0350  -0.0151 -0.1156 405 LEU A CD2 
2936 N N   . PRO A 408 ? 0.6294 0.4535 0.5752 0.0211  -0.0553 -0.1195 406 PRO A N   
2937 C CA  . PRO A 408 ? 0.6790 0.4613 0.5846 0.0218  -0.0705 -0.1249 406 PRO A CA  
2938 C C   . PRO A 408 ? 0.6425 0.4056 0.5046 0.0367  -0.0563 -0.1332 406 PRO A C   
2939 O O   . PRO A 408 ? 0.6590 0.4466 0.5306 0.0467  -0.0350 -0.1347 406 PRO A O   
2940 C CB  . PRO A 408 ? 0.5864 0.3513 0.5010 0.0174  -0.0859 -0.1262 406 PRO A CB  
2941 C CG  . PRO A 408 ? 0.5714 0.3561 0.5040 0.0261  -0.0699 -0.1257 406 PRO A CG  
2942 C CD  . PRO A 408 ? 0.5467 0.3747 0.5090 0.0250  -0.0543 -0.1200 406 PRO A CD  
2943 N N   . ALA A 409 ? 0.7890 0.5081 0.6034 0.0388  -0.0689 -0.1392 407 ALA A N   
2944 C CA  . ALA A 409 ? 0.7924 0.4859 0.5578 0.0553  -0.0541 -0.1485 407 ALA A CA  
2945 C C   . ALA A 409 ? 0.8362 0.5194 0.6006 0.0691  -0.0508 -0.1562 407 ALA A C   
2946 O O   . ALA A 409 ? 0.9380 0.6016 0.7096 0.0628  -0.0708 -0.1567 407 ALA A O   
2947 C CB  . ALA A 409 ? 0.9007 0.5403 0.6049 0.0547  -0.0710 -0.1539 407 ALA A CB  
2948 N N   . PRO A 410 ? 0.8230 0.5189 0.5800 0.0880  -0.0259 -0.1617 408 PRO A N   
2949 C CA  . PRO A 410 ? 0.8380 0.5220 0.5927 0.1058  -0.0238 -0.1692 408 PRO A CA  
2950 C C   . PRO A 410 ? 0.8951 0.5111 0.5948 0.1106  -0.0431 -0.1791 408 PRO A C   
2951 O O   . PRO A 410 ? 0.9714 0.5497 0.6179 0.1142  -0.0444 -0.1859 408 PRO A O   
2952 C CB  . PRO A 410 ? 0.8775 0.5905 0.6328 0.1270  0.0077  -0.1742 408 PRO A CB  
2953 C CG  . PRO A 410 ? 0.8726 0.6310 0.6569 0.1122  0.0214  -0.1647 408 PRO A CG  
2954 C CD  . PRO A 410 ? 0.8256 0.5494 0.5794 0.0944  0.0025  -0.1609 408 PRO A CD  
2955 N N   . ARG A 411 ? 0.8940 0.4895 0.6021 0.1095  -0.0590 -0.1796 409 ARG A N   
2956 C CA  . ARG A 411 ? 0.9464 0.4727 0.6037 0.1129  -0.0788 -0.1895 409 ARG A CA  
2957 C C   . ARG A 411 ? 0.9466 0.4584 0.5884 0.1423  -0.0647 -0.1982 409 ARG A C   
2958 O O   . ARG A 411 ? 0.9523 0.4650 0.6170 0.1443  -0.0699 -0.1943 409 ARG A O   
2959 C CB  . ARG A 411 ? 0.9432 0.4528 0.6214 0.0872  -0.1072 -0.1825 409 ARG A CB  
2960 C CG  . ARG A 411 ? 0.9523 0.4961 0.6678 0.0616  -0.1179 -0.1719 409 ARG A CG  
2961 C CD  . ARG A 411 ? 1.0205 0.5335 0.6933 0.0565  -0.1324 -0.1775 409 ARG A CD  
2962 N NE  . ARG A 411 ? 1.0719 0.5964 0.7748 0.0313  -0.1568 -0.1696 409 ARG A NE  
2963 C CZ  . ARG A 411 ? 1.0004 0.5774 0.7527 0.0215  -0.1512 -0.1584 409 ARG A CZ  
2964 N NH1 . ARG A 411 ? 0.9358 0.5552 0.7081 0.0314  -0.1237 -0.1538 409 ARG A NH1 
2965 N NH2 . ARG A 411 ? 0.9931 0.5796 0.7755 0.0016  -0.1747 -0.1524 409 ARG A NH2 
2966 N N   . THR A 412 ? 0.9836 0.4804 0.5837 0.1667  -0.0460 -0.2097 410 THR A N   
2967 C CA  . THR A 412 ? 1.0288 0.5234 0.6209 0.2004  -0.0278 -0.2187 410 THR A CA  
2968 C C   . THR A 412 ? 1.0880 0.5250 0.6512 0.2070  -0.0466 -0.2223 410 THR A C   
2969 O O   . THR A 412 ? 1.1266 0.5706 0.6976 0.2319  -0.0358 -0.2244 410 THR A O   
2970 C CB  . THR A 412 ? 1.1535 0.6455 0.7064 0.2241  -0.0002 -0.2298 410 THR A CB  
2971 O OG1 . THR A 412 ? 1.2757 0.7129 0.7689 0.2135  -0.0137 -0.2328 410 THR A OG1 
2972 C CG2 . THR A 412 ? 1.1861 0.7503 0.7820 0.2155  0.0245  -0.2206 410 THR A CG2 
2973 N N   . LEU A 413 ? 1.0712 0.4614 0.6100 0.1826  -0.0744 -0.2193 411 LEU A N   
2974 C CA  . LEU A 413 ? 1.1180 0.4614 0.6376 0.1825  -0.0913 -0.2178 411 LEU A CA  
2975 C C   . LEU A 413 ? 1.0806 0.4292 0.6393 0.1655  -0.1053 -0.2073 411 LEU A C   
2976 O O   . LEU A 413 ? 1.1419 0.4587 0.6896 0.1709  -0.1128 -0.2046 411 LEU A O   
2977 C CB  . LEU A 413 ? 1.1805 0.4688 0.6528 0.1651  -0.1143 -0.2200 411 LEU A CB  
2978 C CG  . LEU A 413 ? 1.2498 0.5157 0.6680 0.1816  -0.1039 -0.2299 411 LEU A CG  
2979 C CD1 . LEU A 413 ? 1.3102 0.5146 0.6800 0.1659  -0.1322 -0.2316 411 LEU A CD1 
2980 C CD2 . LEU A 413 ? 1.2688 0.5392 0.6729 0.2195  -0.0765 -0.2376 411 LEU A CD2 
2981 N N   . LEU A 414 ? 1.0174 0.4025 0.6179 0.1458  -0.1080 -0.2008 412 LEU A N   
2982 C CA  . LEU A 414 ? 0.9850 0.3749 0.6214 0.1269  -0.1193 -0.1896 412 LEU A CA  
2983 C C   . LEU A 414 ? 0.9591 0.3804 0.6210 0.1498  -0.1033 -0.1850 412 LEU A C   
2984 O O   . LEU A 414 ? 0.9053 0.3910 0.6041 0.1596  -0.0846 -0.1822 412 LEU A O   
2985 C CB  . LEU A 414 ? 0.9277 0.3710 0.6136 0.0965  -0.1217 -0.1775 412 LEU A CB  
2986 C CG  . LEU A 414 ? 0.8929 0.3598 0.6248 0.0754  -0.1253 -0.1619 412 LEU A CG  
2987 C CD1 . LEU A 414 ? 0.9450 0.3480 0.6530 0.0603  -0.1454 -0.1605 412 LEU A CD1 
2988 C CD2 . LEU A 414 ? 0.8545 0.3717 0.6320 0.0498  -0.1265 -0.1526 412 LEU A CD2 
2989 N N   . THR A 415 ? 1.0518 0.4294 0.6954 0.1562  -0.1124 -0.1825 413 THR A N   
2990 C CA  . THR A 415 ? 1.0286 0.4214 0.6869 0.1807  -0.1041 -0.1790 413 THR A CA  
2991 C C   . THR A 415 ? 1.0954 0.4733 0.7668 0.1611  -0.1149 -0.1637 413 THR A C   
2992 O O   . THR A 415 ? 1.1001 0.5079 0.7942 0.1740  -0.1084 -0.1563 413 THR A O   
2993 C CB  . THR A 415 ? 1.0624 0.4288 0.6873 0.2124  -0.0997 -0.1854 413 THR A CB  
2994 O OG1 . THR A 415 ? 1.1645 0.4655 0.7477 0.1983  -0.1165 -0.1835 413 THR A OG1 
2995 C CG2 . THR A 415 ? 1.0551 0.4480 0.6730 0.2348  -0.0814 -0.1983 413 THR A CG2 
2996 N N   . LYS A 416 ? 1.0288 0.3638 0.6874 0.1292  -0.1306 -0.1579 414 LYS A N   
2997 C CA  . LYS A 416 ? 1.0354 0.3489 0.7010 0.1074  -0.1376 -0.1424 414 LYS A CA  
2998 C C   . LYS A 416 ? 1.0663 0.4229 0.7774 0.0685  -0.1373 -0.1314 414 LYS A C   
2999 O O   . LYS A 416 ? 1.0980 0.4400 0.8074 0.0458  -0.1492 -0.1350 414 LYS A O   
3000 C CB  . LYS A 416 ? 1.0941 0.3416 0.7189 0.0992  -0.1505 -0.1392 414 LYS A CB  
3001 C CG  . LYS A 416 ? 1.1449 0.3659 0.7335 0.1368  -0.1482 -0.1448 414 LYS A CG  
3002 C CD  . LYS A 416 ? 1.2243 0.3826 0.7679 0.1299  -0.1614 -0.1470 414 LYS A CD  
3003 C CE  . LYS A 416 ? 1.2337 0.3924 0.7655 0.1243  -0.1655 -0.1595 414 LYS A CE  
3004 N NZ  . LYS A 416 ? 1.3113 0.4079 0.8021 0.1097  -0.1826 -0.1607 414 LYS A NZ  
3005 N N   . GLY A 417 ? 0.9398 0.3482 0.6901 0.0626  -0.1249 -0.1189 415 GLY A N   
3006 C CA  . GLY A 417 ? 0.9100 0.3618 0.7054 0.0305  -0.1213 -0.1083 415 GLY A CA  
3007 C C   . GLY A 417 ? 0.9620 0.4832 0.7932 0.0359  -0.1105 -0.1121 415 GLY A C   
3008 O O   . GLY A 417 ? 1.0557 0.5914 0.8774 0.0598  -0.1056 -0.1230 415 GLY A O   
3009 N N   . THR A 418 ? 0.9075 0.4706 0.7804 0.0127  -0.1054 -0.1025 416 THR A N   
3010 C CA  . THR A 418 ? 0.8609 0.4844 0.7672 0.0143  -0.0961 -0.1041 416 THR A CA  
3011 C C   . THR A 418 ? 0.7981 0.4331 0.7269 -0.0094 -0.1057 -0.1037 416 THR A C   
3012 O O   . THR A 418 ? 0.8484 0.4759 0.7957 -0.0336 -0.1116 -0.0956 416 THR A O   
3013 C CB  . THR A 418 ? 0.9785 0.6432 0.9128 0.0141  -0.0813 -0.0939 416 THR A CB  
3014 O OG1 . THR A 418 ? 0.9722 0.6194 0.9118 -0.0053 -0.0799 -0.0814 416 THR A OG1 
3015 C CG2 . THR A 418 ? 0.9279 0.5962 0.8462 0.0420  -0.0752 -0.0972 416 THR A CG2 
3016 N N   . LEU A 419 ? 0.8096 0.4621 0.7368 -0.0025 -0.1078 -0.1122 417 LEU A N   
3017 C CA  . LEU A 419 ? 0.8151 0.4794 0.7615 -0.0208 -0.1203 -0.1123 417 LEU A CA  
3018 C C   . LEU A 419 ? 0.7052 0.4252 0.6996 -0.0291 -0.1095 -0.1033 417 LEU A C   
3019 O O   . LEU A 419 ? 0.7062 0.4571 0.7060 -0.0160 -0.0961 -0.1041 417 LEU A O   
3020 C CB  . LEU A 419 ? 0.7994 0.4503 0.7133 -0.0084 -0.1270 -0.1242 417 LEU A CB  
3021 C CG  . LEU A 419 ? 0.8550 0.4951 0.7706 -0.0255 -0.1497 -0.1266 417 LEU A CG  
3022 C CD1 . LEU A 419 ? 0.9216 0.5242 0.8369 -0.0459 -0.1695 -0.1254 417 LEU A CD1 
3023 C CD2 . LEU A 419 ? 0.9141 0.5277 0.7812 -0.0113 -0.1555 -0.1385 417 LEU A CD2 
3024 N N   . GLU A 420 ? 0.6905 0.4230 0.7207 -0.0509 -0.1148 -0.0951 418 GLU A N   
3025 C CA  . GLU A 420 ? 0.7349 0.5174 0.8097 -0.0562 -0.1038 -0.0875 418 GLU A CA  
3026 C C   . GLU A 420 ? 0.6745 0.4763 0.7616 -0.0563 -0.1154 -0.0917 418 GLU A C   
3027 O O   . GLU A 420 ? 0.6346 0.4108 0.7019 -0.0592 -0.1357 -0.0984 418 GLU A O   
3028 C CB  . GLU A 420 ? 0.6663 0.4591 0.7781 -0.0773 -0.1002 -0.0767 418 GLU A CB  
3029 C CG  . GLU A 420 ? 0.7699 0.5415 0.8637 -0.0765 -0.0856 -0.0699 418 GLU A CG  
3030 C CD  . GLU A 420 ? 0.9316 0.7179 1.0102 -0.0553 -0.0685 -0.0703 418 GLU A CD  
3031 O OE1 . GLU A 420 ? 0.8403 0.6644 0.9445 -0.0540 -0.0557 -0.0665 418 GLU A OE1 
3032 O OE2 . GLU A 420 ? 1.0419 0.8016 1.0836 -0.0393 -0.0693 -0.0751 418 GLU A OE2 
3033 N N   . PRO A 421 ? 0.6545 0.4956 0.7683 -0.0520 -0.1042 -0.0879 419 PRO A N   
3034 C CA  . PRO A 421 ? 0.6394 0.4934 0.7589 -0.0493 -0.1154 -0.0907 419 PRO A CA  
3035 C C   . PRO A 421 ? 0.6324 0.4831 0.7724 -0.0633 -0.1409 -0.0909 419 PRO A C   
3036 O O   . PRO A 421 ? 0.6308 0.4680 0.7506 -0.0594 -0.1587 -0.0962 419 PRO A O   
3037 C CB  . PRO A 421 ? 0.5665 0.4597 0.7171 -0.0449 -0.0983 -0.0849 419 PRO A CB  
3038 C CG  . PRO A 421 ? 0.5792 0.4716 0.7164 -0.0382 -0.0780 -0.0834 419 PRO A CG  
3039 C CD  . PRO A 421 ? 0.5740 0.4428 0.7069 -0.0481 -0.0820 -0.0812 419 PRO A CD  
3040 N N   . GLU A 422 ? 0.5916 0.4536 0.7707 -0.0805 -0.1441 -0.0850 420 GLU A N   
3041 C CA  . GLU A 422 ? 0.6388 0.5051 0.8477 -0.0958 -0.1712 -0.0854 420 GLU A CA  
3042 C C   . GLU A 422 ? 0.7099 0.5253 0.8738 -0.1006 -0.1976 -0.0945 420 GLU A C   
3043 O O   . GLU A 422 ? 0.7687 0.5808 0.9487 -0.1130 -0.2266 -0.0969 420 GLU A O   
3044 C CB  . GLU A 422 ? 0.7040 0.5988 0.9711 -0.1159 -0.1649 -0.0761 420 GLU A CB  
3045 C CG  . GLU A 422 ? 0.7537 0.6151 1.0030 -0.1300 -0.1597 -0.0737 420 GLU A CG  
3046 C CD  . GLU A 422 ? 0.8556 0.7448 1.1634 -0.1541 -0.1521 -0.0630 420 GLU A CD  
3047 O OE1 . GLU A 422 ? 0.8142 0.7258 1.1694 -0.1706 -0.1729 -0.0623 420 GLU A OE1 
3048 O OE2 . GLU A 422 ? 0.9910 0.8805 1.2979 -0.1567 -0.1253 -0.0547 420 GLU A OE2 
3049 N N   . TYR A 423 ? 0.7048 0.4801 0.8126 -0.0898 -0.1894 -0.1005 421 TYR A N   
3050 C CA  . TYR A 423 ? 0.7698 0.4888 0.8260 -0.0911 -0.2108 -0.1106 421 TYR A CA  
3051 C C   . TYR A 423 ? 0.7838 0.4790 0.7819 -0.0690 -0.2083 -0.1197 421 TYR A C   
3052 O O   . TYR A 423 ? 0.8556 0.4999 0.7993 -0.0640 -0.2203 -0.1298 421 TYR A O   
3053 C CB  . TYR A 423 ? 0.7882 0.4726 0.8250 -0.0963 -0.2034 -0.1105 421 TYR A CB  
3054 C CG  . TYR A 423 ? 0.7693 0.4743 0.8588 -0.1201 -0.1997 -0.0992 421 TYR A CG  
3055 C CD1 . TYR A 423 ? 0.8642 0.5753 0.9922 -0.1456 -0.2240 -0.0973 421 TYR A CD1 
3056 C CD2 . TYR A 423 ? 0.7491 0.4675 0.8497 -0.1177 -0.1719 -0.0902 421 TYR A CD2 
3057 C CE1 . TYR A 423 ? 0.8758 0.6097 1.0562 -0.1696 -0.2164 -0.0859 421 TYR A CE1 
3058 C CE2 . TYR A 423 ? 0.7145 0.4486 0.8577 -0.1401 -0.1643 -0.0787 421 TYR A CE2 
3059 C CZ  . TYR A 423 ? 0.8185 0.5622 1.0036 -0.1666 -0.1844 -0.0762 421 TYR A CZ  
3060 O OH  . TYR A 423 ? 0.8332 0.5965 1.0648 -0.1910 -0.1727 -0.0637 421 TYR A OH  
3061 N N   . PHE A 424 ? 0.7515 0.4798 0.7583 -0.0564 -0.1919 -0.1164 422 PHE A N   
3062 C CA  . PHE A 424 ? 0.7749 0.4847 0.7302 -0.0382 -0.1845 -0.1229 422 PHE A CA  
3063 C C   . PHE A 424 ? 0.7987 0.4722 0.7152 -0.0396 -0.2130 -0.1298 422 PHE A C   
3064 O O   . PHE A 424 ? 0.8356 0.4648 0.6903 -0.0290 -0.2144 -0.1391 422 PHE A O   
3065 C CB  . PHE A 424 ? 0.6491 0.4005 0.6266 -0.0301 -0.1642 -0.1164 422 PHE A CB  
3066 C CG  . PHE A 424 ? 0.6908 0.4675 0.6852 -0.0236 -0.1359 -0.1127 422 PHE A CG  
3067 C CD1 . PHE A 424 ? 0.6944 0.4583 0.6861 -0.0237 -0.1299 -0.1138 422 PHE A CD1 
3068 C CD2 . PHE A 424 ? 0.6754 0.4848 0.6863 -0.0177 -0.1182 -0.1081 422 PHE A CD2 
3069 C CE1 . PHE A 424 ? 0.5919 0.3769 0.5961 -0.0163 -0.1081 -0.1103 422 PHE A CE1 
3070 C CE2 . PHE A 424 ? 0.5883 0.4193 0.6132 -0.0124 -0.0967 -0.1056 422 PHE A CE2 
3071 C CZ  . PHE A 424 ? 0.6050 0.4249 0.6266 -0.0110 -0.0924 -0.1067 422 PHE A CZ  
3072 N N   . ASN A 425 ? 0.8169 0.5078 0.7676 -0.0509 -0.2365 -0.1256 423 ASN A N   
3073 C CA  . ASN A 425 ? 0.8400 0.4979 0.7580 -0.0532 -0.2706 -0.1312 423 ASN A CA  
3074 C C   . ASN A 425 ? 0.8339 0.5276 0.8180 -0.0685 -0.2962 -0.1249 423 ASN A C   
3075 O O   . ASN A 425 ? 0.7939 0.5348 0.8440 -0.0767 -0.2830 -0.1169 423 ASN A O   
3076 C CB  . ASN A 425 ? 0.8610 0.5018 0.7263 -0.0365 -0.2639 -0.1325 423 ASN A CB  
3077 C CG  . ASN A 425 ? 0.7804 0.4672 0.6838 -0.0312 -0.2463 -0.1223 423 ASN A CG  
3078 O OD1 . ASN A 425 ? 0.7916 0.5089 0.7446 -0.0371 -0.2619 -0.1162 423 ASN A OD1 
3079 N ND2 . ASN A 425 ? 0.7517 0.4433 0.6331 -0.0197 -0.2142 -0.1209 423 ASN A ND2 
3080 N N   . SER A 426 ? 0.8803 0.5517 0.8457 -0.0709 -0.3330 -0.1288 424 SER A N   
3081 C CA  . SER A 426 ? 0.8550 0.5628 0.8881 -0.0844 -0.3626 -0.1242 424 SER A CA  
3082 C C   . SER A 426 ? 0.7915 0.5540 0.8768 -0.0745 -0.3483 -0.1141 424 SER A C   
3083 O O   . SER A 426 ? 0.6896 0.5036 0.8535 -0.0837 -0.3517 -0.1078 424 SER A O   
3084 C CB  . SER A 426 ? 0.8966 0.5682 0.8917 -0.0844 -0.4032 -0.1283 424 SER A CB  
3085 O OG  . SER A 426 ? 1.0237 0.6414 0.9556 -0.0861 -0.4056 -0.1349 424 SER A OG  
3086 N N   . VAL A 427 ? 0.7780 0.5286 0.8199 -0.0561 -0.3314 -0.1126 425 VAL A N   
3087 C CA  . VAL A 427 ? 0.7962 0.5882 0.8779 -0.0456 -0.3183 -0.1039 425 VAL A CA  
3088 C C   . VAL A 427 ? 0.7770 0.6133 0.9093 -0.0481 -0.2811 -0.0984 425 VAL A C   
3089 O O   . VAL A 427 ? 0.7154 0.5986 0.9123 -0.0480 -0.2767 -0.0922 425 VAL A O   
3090 C CB  . VAL A 427 ? 0.7909 0.5504 0.8067 -0.0288 -0.3094 -0.1030 425 VAL A CB  
3091 C CG1 . VAL A 427 ? 0.7567 0.5508 0.8085 -0.0183 -0.2958 -0.0945 425 VAL A CG1 
3092 C CG2 . VAL A 427 ? 0.8292 0.5395 0.7877 -0.0254 -0.3474 -0.1074 425 VAL A CG2 
3093 N N   . CYS A 428 ? 0.7682 0.5890 0.8699 -0.0483 -0.2541 -0.1009 426 CYS A N   
3094 C CA  . CYS A 428 ? 0.6835 0.5390 0.8231 -0.0498 -0.2215 -0.0959 426 CYS A CA  
3095 C C   . CYS A 428 ? 0.6524 0.5367 0.8531 -0.0666 -0.2261 -0.0924 426 CYS A C   
3096 O O   . CYS A 428 ? 0.6794 0.6029 0.9272 -0.0676 -0.2047 -0.0859 426 CYS A O   
3097 C CB  . CYS A 428 ? 0.6183 0.4499 0.7121 -0.0450 -0.1971 -0.0997 426 CYS A CB  
3098 S SG  . CYS A 428 ? 0.8833 0.6967 0.9210 -0.0282 -0.1798 -0.1013 426 CYS A SG  
3099 N N   . ARG A 429 ? 0.6321 0.4945 0.8298 -0.0810 -0.2526 -0.0967 427 ARG A N   
3100 C CA  . ARG A 429 ? 0.6740 0.5648 0.9346 -0.1015 -0.2586 -0.0922 427 ARG A CA  
3101 C C   . ARG A 429 ? 0.7040 0.6497 1.0368 -0.1012 -0.2667 -0.0862 427 ARG A C   
3102 O O   . ARG A 429 ? 0.6873 0.6774 1.0813 -0.1088 -0.2475 -0.0789 427 ARG A O   
3103 C CB  . ARG A 429 ? 0.6157 0.4674 0.8566 -0.1188 -0.2912 -0.0990 427 ARG A CB  
3104 C CG  . ARG A 429 ? 0.6476 0.5250 0.9533 -0.1455 -0.2975 -0.0938 427 ARG A CG  
3105 C CD  . ARG A 429 ? 0.8239 0.6477 1.0908 -0.1625 -0.3172 -0.1000 427 ARG A CD  
3106 N NE  . ARG A 429 ? 0.8988 0.7478 1.2204 -0.1878 -0.3149 -0.0914 427 ARG A NE  
3107 C CZ  . ARG A 429 ? 0.8253 0.6985 1.1873 -0.2000 -0.2862 -0.0826 427 ARG A CZ  
3108 N NH1 . ARG A 429 ? 0.8301 0.6959 1.1654 -0.1855 -0.2541 -0.0807 427 ARG A NH1 
3109 N NH2 . ARG A 429 ? 0.8844 0.7878 1.3017 -0.2240 -0.2837 -0.0738 427 ARG A NH2 
3110 N N   . LEU A 430 ? 0.6958 0.6371 1.0202 -0.0909 -0.2947 -0.0891 428 LEU A N   
3111 C CA  . LEU A 430 ? 0.7236 0.7158 1.1149 -0.0845 -0.3042 -0.0840 428 LEU A CA  
3112 C C   . LEU A 430 ? 0.6556 0.6803 1.0676 -0.0693 -0.2657 -0.0780 428 LEU A C   
3113 O O   . LEU A 430 ? 0.5841 0.6604 1.0663 -0.0710 -0.2524 -0.0724 428 LEU A O   
3114 C CB  . LEU A 430 ? 0.6947 0.6644 1.0566 -0.0715 -0.3417 -0.0879 428 LEU A CB  
3115 C CG  . LEU A 430 ? 0.7324 0.6808 1.0914 -0.0859 -0.3897 -0.0938 428 LEU A CG  
3116 C CD1 . LEU A 430 ? 0.7832 0.7160 1.1203 -0.0694 -0.4271 -0.0955 428 LEU A CD1 
3117 C CD2 . LEU A 430 ? 0.6879 0.6862 1.1317 -0.1063 -0.3941 -0.0891 428 LEU A CD2 
3118 N N   . MET A 431 ? 0.5876 0.5820 0.9387 -0.0547 -0.2467 -0.0795 429 MET A N   
3119 C CA  . MET A 431 ? 0.6127 0.6294 0.9747 -0.0408 -0.2142 -0.0753 429 MET A CA  
3120 C C   . MET A 431 ? 0.6030 0.6479 1.0004 -0.0501 -0.1825 -0.0711 429 MET A C   
3121 O O   . MET A 431 ? 0.5438 0.6180 0.9700 -0.0406 -0.1592 -0.0673 429 MET A O   
3122 C CB  . MET A 431 ? 0.6502 0.6281 0.9412 -0.0294 -0.2003 -0.0778 429 MET A CB  
3123 C CG  . MET A 431 ? 0.7081 0.6561 0.9576 -0.0172 -0.2224 -0.0792 429 MET A CG  
3124 S SD  . MET A 431 ? 0.7762 0.6880 0.9539 -0.0085 -0.1972 -0.0801 429 MET A SD  
3125 C CE  . MET A 431 ? 0.7212 0.5945 0.8511 0.0027  -0.2243 -0.0791 429 MET A CE  
3126 N N   . LYS A 432 ? 0.6382 0.6692 1.0284 -0.0678 -0.1812 -0.0715 430 LYS A N   
3127 C CA  . LYS A 432 ? 0.6014 0.6473 1.0110 -0.0772 -0.1513 -0.0663 430 LYS A CA  
3128 C C   . LYS A 432 ? 0.6022 0.6861 1.0824 -0.0959 -0.1540 -0.0605 430 LYS A C   
3129 O O   . LYS A 432 ? 0.6049 0.7078 1.1088 -0.1033 -0.1254 -0.0539 430 LYS A O   
3130 C CB  . LYS A 432 ? 0.6227 0.6244 0.9762 -0.0838 -0.1459 -0.0692 430 LYS A CB  
3131 C CG  . LYS A 432 ? 0.6052 0.5796 0.8988 -0.0667 -0.1346 -0.0738 430 LYS A CG  
3132 C CD  . LYS A 432 ? 0.5630 0.5578 0.8620 -0.0554 -0.1053 -0.0703 430 LYS A CD  
3133 C CE  . LYS A 432 ? 0.5716 0.5715 0.8794 -0.0633 -0.0821 -0.0649 430 LYS A CE  
3134 N NZ  . LYS A 432 ? 0.5362 0.5481 0.8382 -0.0512 -0.0566 -0.0630 430 LYS A NZ  
3135 N N   . THR A 433 ? 0.6832 0.7784 1.1967 -0.1045 -0.1878 -0.0625 431 THR A N   
3136 C CA  . THR A 433 ? 0.5772 0.7137 1.1667 -0.1258 -0.1943 -0.0573 431 THR A CA  
3137 C C   . THR A 433 ? 0.6181 0.8136 1.2794 -0.1135 -0.1982 -0.0548 431 THR A C   
3138 O O   . THR A 433 ? 0.6664 0.9074 1.3802 -0.1123 -0.1676 -0.0482 431 THR A O   
3139 C CB  . THR A 433 ? 0.6606 0.7689 1.2423 -0.1471 -0.2337 -0.0621 431 THR A CB  
3140 O OG1 . THR A 433 ? 0.7079 0.7954 1.2600 -0.1333 -0.2699 -0.0699 431 THR A OG1 
3141 C CG2 . THR A 433 ? 0.6943 0.7443 1.2097 -0.1580 -0.2263 -0.0644 431 THR A CG2 
3142 N N   . ILE A 434 ? 0.6382 0.8310 1.2993 -0.1022 -0.2351 -0.0601 432 ILE A N   
3143 C CA  . ILE A 434 ? 0.4942 0.7420 1.2260 -0.0876 -0.2446 -0.0582 432 ILE A CA  
3144 C C   . ILE A 434 ? 0.6113 0.8563 1.3168 -0.0563 -0.2232 -0.0584 432 ILE A C   
3145 O O   . ILE A 434 ? 0.6381 0.9305 1.4021 -0.0402 -0.2148 -0.0560 432 ILE A O   
3146 C CB  . ILE A 434 ? 0.4605 0.7042 1.2025 -0.0879 -0.2978 -0.0628 432 ILE A CB  
3147 C CG1 . ILE A 434 ? 0.5765 0.7577 1.2291 -0.0704 -0.3194 -0.0693 432 ILE A CG1 
3148 C CG2 . ILE A 434 ? 0.5622 0.7911 1.3006 -0.1168 -0.3134 -0.0621 432 ILE A CG2 
3149 C CD1 . ILE A 434 ? 0.6297 0.7955 1.2739 -0.0667 -0.3703 -0.0730 432 ILE A CD1 
3150 N N   . GLY A 435 ? 0.5397 0.7306 1.1608 -0.0475 -0.2143 -0.0617 433 GLY A N   
3151 C CA  . GLY A 435 ? 0.5233 0.7024 1.1117 -0.0222 -0.1970 -0.0623 433 GLY A CA  
3152 C C   . GLY A 435 ? 0.5274 0.6634 1.0598 -0.0091 -0.2275 -0.0663 433 GLY A C   
3153 O O   . GLY A 435 ? 0.5342 0.6605 1.0673 -0.0143 -0.2657 -0.0685 433 GLY A O   
3154 N N   . PRO A 436 ? 0.5043 0.6103 0.9839 0.0067  -0.2119 -0.0669 434 PRO A N   
3155 C CA  . PRO A 436 ? 0.5977 0.6613 1.0229 0.0196  -0.2367 -0.0685 434 PRO A CA  
3156 C C   . PRO A 436 ? 0.6316 0.7163 1.0961 0.0406  -0.2568 -0.0666 434 PRO A C   
3157 O O   . PRO A 436 ? 0.6183 0.7502 1.1474 0.0499  -0.2428 -0.0648 434 PRO A O   
3158 C CB  . PRO A 436 ? 0.6450 0.6750 1.0095 0.0250  -0.2076 -0.0688 434 PRO A CB  
3159 C CG  . PRO A 436 ? 0.5741 0.6397 0.9792 0.0281  -0.1737 -0.0673 434 PRO A CG  
3160 C CD  . PRO A 436 ? 0.5595 0.6648 1.0224 0.0117  -0.1716 -0.0660 434 PRO A CD  
3161 N N   . ASP A 437 ? 0.6856 0.7320 1.1069 0.0498  -0.2897 -0.0669 435 ASP A N   
3162 C CA  . ASP A 437 ? 0.6637 0.7214 1.1136 0.0733  -0.3138 -0.0647 435 ASP A CA  
3163 C C   . ASP A 437 ? 0.7218 0.7637 1.1489 0.0939  -0.2887 -0.0627 435 ASP A C   
3164 O O   . ASP A 437 ? 0.6781 0.7483 1.1527 0.1154  -0.2901 -0.0617 435 ASP A O   
3165 C CB  . ASP A 437 ? 0.6716 0.6844 1.0723 0.0773  -0.3593 -0.0648 435 ASP A CB  
3166 C CG  . ASP A 437 ? 0.8245 0.8499 1.2490 0.0584  -0.3916 -0.0683 435 ASP A CG  
3167 O OD1 . ASP A 437 ? 0.7486 0.8338 1.2614 0.0545  -0.4023 -0.0685 435 ASP A OD1 
3168 O OD2 . ASP A 437 ? 0.7985 0.7730 1.1531 0.0469  -0.4058 -0.0711 435 ASP A OD2 
3169 N N   . MET A 438 ? 0.6808 0.6778 1.0371 0.0876  -0.2660 -0.0627 436 MET A N   
3170 C CA  . MET A 438 ? 0.6445 0.6173 0.9699 0.1019  -0.2436 -0.0614 436 MET A CA  
3171 C C   . MET A 438 ? 0.6688 0.6368 0.9692 0.0861  -0.2058 -0.0634 436 MET A C   
3172 O O   . MET A 438 ? 0.6781 0.6371 0.9537 0.0672  -0.2022 -0.0648 436 MET A O   
3173 C CB  . MET A 438 ? 0.7078 0.6181 0.9614 0.1114  -0.2647 -0.0577 436 MET A CB  
3174 C CG  . MET A 438 ? 0.7251 0.6326 0.9928 0.1264  -0.3096 -0.0555 436 MET A CG  
3175 S SD  . MET A 438 ? 0.9976 0.8228 1.1636 0.1279  -0.3395 -0.0503 436 MET A SD  
3176 C CE  . MET A 438 ? 0.8678 0.6860 1.0040 0.0998  -0.3424 -0.0545 436 MET A CE  
3177 N N   . PHE A 439 ? 0.6527 0.6244 0.9580 0.0957  -0.1794 -0.0644 437 PHE A N   
3178 C CA  . PHE A 439 ? 0.6299 0.5980 0.9137 0.0830  -0.1466 -0.0667 437 PHE A CA  
3179 C C   . PHE A 439 ? 0.6232 0.5550 0.8659 0.0927  -0.1334 -0.0672 437 PHE A C   
3180 O O   . PHE A 439 ? 0.6183 0.5562 0.8822 0.1116  -0.1279 -0.0685 437 PHE A O   
3181 C CB  . PHE A 439 ? 0.5511 0.5685 0.8915 0.0803  -0.1246 -0.0685 437 PHE A CB  
3182 C CG  . PHE A 439 ? 0.5535 0.5647 0.8698 0.0708  -0.0939 -0.0709 437 PHE A CG  
3183 C CD1 . PHE A 439 ? 0.5784 0.5803 0.8674 0.0517  -0.0892 -0.0713 437 PHE A CD1 
3184 C CD2 . PHE A 439 ? 0.5066 0.5192 0.8253 0.0828  -0.0716 -0.0734 437 PHE A CD2 
3185 C CE1 . PHE A 439 ? 0.5439 0.5414 0.8127 0.0449  -0.0654 -0.0735 437 PHE A CE1 
3186 C CE2 . PHE A 439 ? 0.5290 0.5330 0.8219 0.0743  -0.0480 -0.0761 437 PHE A CE2 
3187 C CZ  . PHE A 439 ? 0.5292 0.5275 0.7993 0.0553  -0.0461 -0.0758 437 PHE A CZ  
3188 N N   . LEU A 440 ? 0.6035 0.4971 0.7885 0.0796  -0.1281 -0.0665 438 LEU A N   
3189 C CA  . LEU A 440 ? 0.6670 0.5248 0.8122 0.0817  -0.1147 -0.0671 438 LEU A CA  
3190 C C   . LEU A 440 ? 0.5798 0.4574 0.7381 0.0764  -0.0875 -0.0723 438 LEU A C   
3191 O O   . LEU A 440 ? 0.5800 0.4685 0.7319 0.0597  -0.0764 -0.0737 438 LEU A O   
3192 C CB  . LEU A 440 ? 0.6381 0.4539 0.7238 0.0667  -0.1177 -0.0635 438 LEU A CB  
3193 C CG  . LEU A 440 ? 0.6812 0.4708 0.7413 0.0703  -0.1443 -0.0579 438 LEU A CG  
3194 C CD1 . LEU A 440 ? 0.7304 0.4773 0.7272 0.0546  -0.1397 -0.0537 438 LEU A CD1 
3195 C CD2 . LEU A 440 ? 0.7208 0.4923 0.7861 0.0936  -0.1639 -0.0550 438 LEU A CD2 
3196 N N   . GLY A 441 ? 0.5732 0.4519 0.7453 0.0925  -0.0774 -0.0756 439 GLY A N   
3197 C CA  . GLY A 441 ? 0.6176 0.5130 0.7995 0.0908  -0.0529 -0.0808 439 GLY A CA  
3198 C C   . GLY A 441 ? 0.6438 0.5029 0.7819 0.0865  -0.0409 -0.0853 439 GLY A C   
3199 O O   . GLY A 441 ? 0.6162 0.4843 0.7571 0.0876  -0.0230 -0.0904 439 GLY A O   
3200 N N   . THR A 442 ? 0.5887 0.4048 0.6842 0.0800  -0.0504 -0.0834 440 THR A N   
3201 C CA  . THR A 442 ? 0.6032 0.3828 0.6598 0.0730  -0.0419 -0.0878 440 THR A CA  
3202 C C   . THR A 442 ? 0.6038 0.3716 0.6322 0.0469  -0.0430 -0.0851 440 THR A C   
3203 O O   . THR A 442 ? 0.6411 0.3853 0.6472 0.0403  -0.0534 -0.0787 440 THR A O   
3204 C CB  . THR A 442 ? 0.6793 0.4116 0.7102 0.0895  -0.0496 -0.0883 440 THR A CB  
3205 O OG1 . THR A 442 ? 0.7740 0.5224 0.8354 0.1169  -0.0446 -0.0925 440 THR A OG1 
3206 C CG2 . THR A 442 ? 0.6986 0.3867 0.6851 0.0772  -0.0436 -0.0932 440 THR A CG2 
3207 N N   . CYS A 443 ? 0.6048 0.3888 0.6336 0.0330  -0.0318 -0.0896 441 CYS A N   
3208 C CA  . CYS A 443 ? 0.6100 0.3905 0.6206 0.0096  -0.0306 -0.0881 441 CYS A CA  
3209 C C   . CYS A 443 ? 0.6093 0.3459 0.5849 -0.0006 -0.0315 -0.0898 441 CYS A C   
3210 O O   . CYS A 443 ? 0.6336 0.3545 0.5999 0.0040  -0.0284 -0.0970 441 CYS A O   
3211 C CB  . CYS A 443 ? 0.5448 0.3610 0.5729 0.0013  -0.0219 -0.0924 441 CYS A CB  
3212 S SG  . CYS A 443 ? 0.5498 0.3763 0.5699 -0.0238 -0.0195 -0.0917 441 CYS A SG  
3213 N N   . ARG A 444 ? 0.6425 0.3241 0.4977 -0.0129 -0.1517 0.0144  442 ARG A N   
3214 C CA  . ARG A 444 ? 0.6543 0.3131 0.5304 -0.0187 -0.1642 0.0299  442 ARG A CA  
3215 C C   . ARG A 444 ? 0.6497 0.3113 0.5106 -0.0329 -0.1361 0.0587  442 ARG A C   
3216 O O   . ARG A 444 ? 0.6640 0.3111 0.5556 -0.0402 -0.1442 0.0728  442 ARG A O   
3217 C CB  . ARG A 444 ? 0.7446 0.3533 0.6062 -0.0142 -0.1963 0.0493  442 ARG A CB  
3218 C CG  . ARG A 444 ? 0.7620 0.3666 0.6563 0.0007  -0.2313 0.0173  442 ARG A CG  
3219 C CD  . ARG A 444 ? 0.9903 0.5416 0.8822 0.0054  -0.2707 0.0354  442 ARG A CD  
3220 N NE  . ARG A 444 ? 1.0775 0.6253 1.0073 0.0209  -0.3066 0.0022  442 ARG A NE  
3221 C CZ  . ARG A 444 ? 1.0847 0.6400 1.0036 0.0312  -0.3134 -0.0159 442 ARG A CZ  
3222 N NH1 . ARG A 444 ? 1.0119 0.5650 0.8716 0.0300  -0.2953 -0.0011 442 ARG A NH1 
3223 N NH2 . ARG A 444 ? 0.9992 0.5614 0.9727 0.0446  -0.3429 -0.0504 442 ARG A NH2 
3224 N N   . ARG A 445 ? 0.6411 0.3224 0.4657 -0.0366 -0.1052 0.0656  443 ARG A N   
3225 C CA  . ARG A 445 ? 0.6817 0.3691 0.4944 -0.0486 -0.0765 0.0916  443 ARG A CA  
3226 C C   . ARG A 445 ? 0.6373 0.3620 0.4840 -0.0534 -0.0612 0.0737  443 ARG A C   
3227 O O   . ARG A 445 ? 0.6871 0.4123 0.5607 -0.0628 -0.0551 0.0870  443 ARG A O   
3228 C CB  . ARG A 445 ? 0.6453 0.3313 0.3968 -0.0465 -0.0538 0.1071  443 ARG A CB  
3229 C CG  . ARG A 445 ? 0.7372 0.4426 0.4821 -0.0561 -0.0194 0.1239  443 ARG A CG  
3230 C CD  . ARG A 445 ? 0.7618 0.4782 0.4592 -0.0493 -0.0011 0.1197  443 ARG A CD  
3231 N NE  . ARG A 445 ? 0.8356 0.5217 0.4739 -0.0379 -0.0086 0.1328  443 ARG A NE  
3232 C CZ  . ARG A 445 ? 0.7873 0.4742 0.3811 -0.0265 -0.0039 0.1237  443 ARG A CZ  
3233 N NH1 . ARG A 445 ? 0.6538 0.3692 0.2630 -0.0270 0.0064  0.1026  443 ARG A NH1 
3234 N NH2 . ARG A 445 ? 0.7599 0.4159 0.2924 -0.0126 -0.0137 0.1352  443 ARG A NH2 
3235 N N   . CYS A 446 ? 0.5691 0.3239 0.4184 -0.0467 -0.0566 0.0455  444 CYS A N   
3236 C CA  . CYS A 446 ? 0.6133 0.4016 0.4765 -0.0496 -0.0388 0.0343  444 CYS A CA  
3237 C C   . CYS A 446 ? 0.6510 0.4566 0.5549 -0.0420 -0.0549 0.0054  444 CYS A C   
3238 O O   . CYS A 446 ? 0.6465 0.4526 0.5668 -0.0315 -0.0737 -0.0157 444 CYS A O   
3239 C CB  . CYS A 446 ? 0.5383 0.3510 0.3771 -0.0471 -0.0199 0.0266  444 CYS A CB  
3240 S SG  . CYS A 446 ? 0.6177 0.4116 0.4063 -0.0495 -0.0054 0.0504  444 CYS A SG  
3241 N N   . PRO A 447 ? 0.6411 0.4611 0.5618 -0.0449 -0.0495 0.0019  445 PRO A N   
3242 C CA  . PRO A 447 ? 0.5539 0.3935 0.5018 -0.0324 -0.0648 -0.0307 445 PRO A CA  
3243 C C   . PRO A 447 ? 0.5968 0.4694 0.5279 -0.0202 -0.0537 -0.0526 445 PRO A C   
3244 O O   . PRO A 447 ? 0.5377 0.4229 0.4426 -0.0248 -0.0315 -0.0413 445 PRO A O   
3245 C CB  . PRO A 447 ? 0.5514 0.4006 0.5080 -0.0374 -0.0579 -0.0270 445 PRO A CB  
3246 C CG  . PRO A 447 ? 0.6587 0.4828 0.6199 -0.0546 -0.0491 0.0093  445 PRO A CG  
3247 C CD  . PRO A 447 ? 0.6416 0.4606 0.5598 -0.0571 -0.0317 0.0250  445 PRO A CD  
3248 N N   . ALA A 448 ? 0.5249 0.4129 0.4762 -0.0035 -0.0692 -0.0843 446 ALA A N   
3249 C CA  . ALA A 448 ? 0.5178 0.4412 0.4618 0.0091  -0.0556 -0.1031 446 ALA A CA  
3250 C C   . ALA A 448 ? 0.5026 0.4568 0.4170 0.0068  -0.0253 -0.0941 446 ALA A C   
3251 O O   . ALA A 448 ? 0.5145 0.4900 0.4228 0.0065  -0.0061 -0.0894 446 ALA A O   
3252 C CB  . ALA A 448 ? 0.4929 0.4333 0.4605 0.0314  -0.0739 -0.1414 446 ALA A CB  
3253 N N   . GLU A 449 ? 0.5000 0.4558 0.4022 0.0052  -0.0234 -0.0907 447 GLU A N   
3254 C CA  . GLU A 449 ? 0.4783 0.4584 0.3520 0.0029  0.0016  -0.0792 447 GLU A CA  
3255 C C   . GLU A 449 ? 0.4508 0.4253 0.3147 -0.0131 0.0207  -0.0521 447 GLU A C   
3256 O O   . GLU A 449 ? 0.4511 0.4496 0.3052 -0.0130 0.0406  -0.0453 447 GLU A O   
3257 C CB  . GLU A 449 ? 0.4978 0.4717 0.3653 0.0019  -0.0056 -0.0778 447 GLU A CB  
3258 C CG  . GLU A 449 ? 0.5821 0.5541 0.4652 0.0191  -0.0336 -0.1082 447 GLU A CG  
3259 C CD  . GLU A 449 ? 0.6367 0.5730 0.5598 0.0094  -0.0593 -0.1047 447 GLU A CD  
3260 O OE1 . GLU A 449 ? 0.5689 0.4840 0.5088 -0.0008 -0.0623 -0.0919 447 GLU A OE1 
3261 O OE2 . GLU A 449 ? 0.6677 0.5964 0.6081 0.0126  -0.0782 -0.1135 447 GLU A OE2 
3262 N N   . ILE A 450 ? 0.4869 0.4298 0.3540 -0.0255 0.0143  -0.0358 448 ILE A N   
3263 C CA  . ILE A 450 ? 0.4350 0.3697 0.2887 -0.0358 0.0274  -0.0162 448 ILE A CA  
3264 C C   . ILE A 450 ? 0.5201 0.4605 0.3844 -0.0312 0.0252  -0.0235 448 ILE A C   
3265 O O   . ILE A 450 ? 0.4787 0.4342 0.3438 -0.0335 0.0383  -0.0176 448 ILE A O   
3266 C CB  . ILE A 450 ? 0.4783 0.3801 0.3246 -0.0456 0.0230  0.0021  448 ILE A CB  
3267 C CG1 . ILE A 450 ? 0.4889 0.3909 0.3390 -0.0513 0.0278  0.0101  448 ILE A CG1 
3268 C CG2 . ILE A 450 ? 0.4730 0.3649 0.2988 -0.0500 0.0323  0.0156  448 ILE A CG2 
3269 C CD1 . ILE A 450 ? 0.4917 0.3679 0.3446 -0.0606 0.0282  0.0305  448 ILE A CD1 
3270 N N   . VAL A 451 ? 0.4963 0.4240 0.3772 -0.0246 0.0057  -0.0366 449 VAL A N   
3271 C CA  . VAL A 451 ? 0.5146 0.4456 0.4143 -0.0194 -0.0012 -0.0456 449 VAL A CA  
3272 C C   . VAL A 451 ? 0.5042 0.4793 0.4222 -0.0133 0.0179  -0.0550 449 VAL A C   
3273 O O   . VAL A 451 ? 0.5115 0.4969 0.4444 -0.0167 0.0259  -0.0490 449 VAL A O   
3274 C CB  . VAL A 451 ? 0.5312 0.4432 0.4515 -0.0110 -0.0282 -0.0611 449 VAL A CB  
3275 C CG1 . VAL A 451 ? 0.5334 0.4531 0.4825 -0.0036 -0.0373 -0.0746 449 VAL A CG1 
3276 C CG2 . VAL A 451 ? 0.5684 0.4354 0.4704 -0.0187 -0.0441 -0.0427 449 VAL A CG2 
3277 N N   . ASP A 452 ? 0.4862 0.4883 0.4045 -0.0032 0.0251  -0.0691 450 ASP A N   
3278 C CA  . ASP A 452 ? 0.4616 0.5097 0.3904 0.0047  0.0489  -0.0736 450 ASP A CA  
3279 C C   . ASP A 452 ? 0.4550 0.5133 0.3744 -0.0077 0.0711  -0.0475 450 ASP A C   
3280 O O   . ASP A 452 ? 0.4462 0.5304 0.3928 -0.0090 0.0871  -0.0407 450 ASP A O   
3281 C CB  . ASP A 452 ? 0.4432 0.5150 0.3558 0.0214  0.0523  -0.0925 450 ASP A CB  
3282 C CG  . ASP A 452 ? 0.5859 0.6550 0.5212 0.0379  0.0294  -0.1245 450 ASP A CG  
3283 O OD1 . ASP A 452 ? 0.6611 0.7135 0.6268 0.0357  0.0136  -0.1295 450 ASP A OD1 
3284 O OD2 . ASP A 452 ? 0.6050 0.6862 0.5282 0.0548  0.0230  -0.1466 450 ASP A OD2 
3285 N N   . THR A 453 ? 0.3912 0.4299 0.2812 -0.0170 0.0713  -0.0323 451 THR A N   
3286 C CA  . THR A 453 ? 0.4360 0.4827 0.3207 -0.0273 0.0886  -0.0094 451 THR A CA  
3287 C C   . THR A 453 ? 0.4570 0.4903 0.3671 -0.0363 0.0842  -0.0008 451 THR A C   
3288 O O   . THR A 453 ? 0.4568 0.5109 0.3934 -0.0404 0.0976  0.0106  451 THR A O   
3289 C CB  . THR A 453 ? 0.4759 0.5034 0.3308 -0.0337 0.0864  0.0012  451 THR A CB  
3290 O OG1 . THR A 453 ? 0.5532 0.5906 0.3893 -0.0235 0.0841  -0.0099 451 THR A OG1 
3291 C CG2 . THR A 453 ? 0.4463 0.4811 0.3002 -0.0426 0.1008  0.0229  451 THR A CG2 
3292 N N   . VAL A 454 ? 0.4140 0.4116 0.3176 -0.0384 0.0638  -0.0053 452 VAL A N   
3293 C CA  . VAL A 454 ? 0.4312 0.4110 0.3504 -0.0425 0.0531  -0.0018 452 VAL A CA  
3294 C C   . VAL A 454 ? 0.4989 0.4957 0.4659 -0.0377 0.0478  -0.0128 452 VAL A C   
3295 O O   . VAL A 454 ? 0.5121 0.5127 0.5135 -0.0415 0.0456  -0.0084 452 VAL A O   
3296 C CB  . VAL A 454 ? 0.4954 0.4328 0.3829 -0.0419 0.0338  -0.0025 452 VAL A CB  
3297 C CG1 . VAL A 454 ? 0.4147 0.3417 0.2672 -0.0473 0.0437  0.0100  452 VAL A CG1 
3298 C CG2 . VAL A 454 ? 0.5026 0.4258 0.3899 -0.0350 0.0167  -0.0147 452 VAL A CG2 
3299 N N   . SER A 455 ? 0.5299 0.5370 0.5078 -0.0285 0.0431  -0.0292 453 SER A N   
3300 C CA  . SER A 455 ? 0.5710 0.5963 0.6023 -0.0225 0.0374  -0.0424 453 SER A CA  
3301 C C   . SER A 455 ? 0.5096 0.5782 0.5836 -0.0268 0.0641  -0.0305 453 SER A C   
3302 O O   . SER A 455 ? 0.5131 0.5888 0.6418 -0.0293 0.0584  -0.0307 453 SER A O   
3303 C CB  . SER A 455 ? 0.5697 0.6059 0.6084 -0.0095 0.0314  -0.0642 453 SER A CB  
3304 O OG  . SER A 455 ? 0.5879 0.6309 0.6793 -0.0025 0.0170  -0.0803 453 SER A OG  
3305 N N   . ALA A 456 ? 0.4464 0.5430 0.4985 -0.0275 0.0919  -0.0181 454 ALA A N   
3306 C CA  . ALA A 456 ? 0.5076 0.6453 0.5953 -0.0323 0.1211  0.0015  454 ALA A CA  
3307 C C   . ALA A 456 ? 0.4412 0.5607 0.5399 -0.0472 0.1178  0.0237  454 ALA A C   
3308 O O   . ALA A 456 ? 0.4637 0.6038 0.6207 -0.0544 0.1276  0.0385  454 ALA A O   
3309 C CB  . ALA A 456 ? 0.3835 0.5544 0.4333 -0.0245 0.1496  0.0084  454 ALA A CB  
3310 N N   . LEU A 457 ? 0.4320 0.5141 0.4830 -0.0511 0.1033  0.0257  455 LEU A N   
3311 C CA  . LEU A 457 ? 0.4873 0.5540 0.5452 -0.0620 0.1004  0.0435  455 LEU A CA  
3312 C C   . LEU A 457 ? 0.4858 0.5313 0.5901 -0.0644 0.0752  0.0360  455 LEU A C   
3313 O O   . LEU A 457 ? 0.3988 0.4514 0.5524 -0.0726 0.0762  0.0502  455 LEU A O   
3314 C CB  . LEU A 457 ? 0.4421 0.4790 0.4402 -0.0627 0.0935  0.0440  455 LEU A CB  
3315 C CG  . LEU A 457 ? 0.5063 0.5271 0.5063 -0.0707 0.0896  0.0581  455 LEU A CG  
3316 C CD1 . LEU A 457 ? 0.5286 0.5732 0.5248 -0.0759 0.1119  0.0813  455 LEU A CD1 
3317 C CD2 . LEU A 457 ? 0.4809 0.4659 0.4344 -0.0676 0.0749  0.0485  455 LEU A CD2 
3318 N N   . VAL A 458 ? 0.4659 0.4838 0.5586 -0.0564 0.0493  0.0143  456 VAL A N   
3319 C CA  . VAL A 458 ? 0.4996 0.4897 0.6229 -0.0546 0.0183  0.0038  456 VAL A CA  
3320 C C   . VAL A 458 ? 0.5095 0.4962 0.6673 -0.0460 -0.0032 -0.0164 456 VAL A C   
3321 O O   . VAL A 458 ? 0.4994 0.4672 0.6959 -0.0427 -0.0324 -0.0275 456 VAL A O   
3322 C CB  . VAL A 458 ? 0.5186 0.4645 0.5797 -0.0497 -0.0010 -0.0022 456 VAL A CB  
3323 C CG1 . VAL A 458 ? 0.5107 0.4580 0.5635 -0.0572 0.0113  0.0135  456 VAL A CG1 
3324 C CG2 . VAL A 458 ? 0.5366 0.4675 0.5331 -0.0441 0.0012  -0.0069 456 VAL A CG2 
3325 N N   . TYR A 459 ? 0.5284 0.5309 0.6759 -0.0405 0.0062  -0.0242 457 TYR A N   
3326 C CA  . TYR A 459 ? 0.5351 0.5296 0.7114 -0.0305 -0.0182 -0.0455 457 TYR A CA  
3327 C C   . TYR A 459 ? 0.5180 0.5628 0.7671 -0.0292 0.0009  -0.0494 457 TYR A C   
3328 O O   . TYR A 459 ? 0.5241 0.5694 0.7998 -0.0193 -0.0156 -0.0694 457 TYR A O   
3329 C CB  . TYR A 459 ? 0.5557 0.5210 0.6682 -0.0223 -0.0310 -0.0551 457 TYR A CB  
3330 C CG  . TYR A 459 ? 0.5456 0.4640 0.5894 -0.0217 -0.0471 -0.0493 457 TYR A CG  
3331 C CD1 . TYR A 459 ? 0.5307 0.4133 0.5694 -0.0153 -0.0790 -0.0569 457 TYR A CD1 
3332 C CD2 . TYR A 459 ? 0.5555 0.4674 0.5413 -0.0255 -0.0301 -0.0374 457 TYR A CD2 
3333 C CE1 . TYR A 459 ? 0.5977 0.4419 0.5666 -0.0109 -0.0891 -0.0519 457 TYR A CE1 
3334 C CE2 . TYR A 459 ? 0.5464 0.4221 0.4745 -0.0242 -0.0386 -0.0303 457 TYR A CE2 
3335 C CZ  . TYR A 459 ? 0.5933 0.4366 0.5089 -0.0161 -0.0656 -0.0371 457 TYR A CZ  
3336 O OH  . TYR A 459 ? 0.5768 0.3884 0.4281 -0.0112 -0.0696 -0.0302 457 TYR A OH  
3337 N N   . ASP A 460 ? 0.4734 0.5614 0.7555 -0.0379 0.0361  -0.0296 458 ASP A N   
3338 C CA  . ASP A 460 ? 0.5184 0.6621 0.8718 -0.0361 0.0629  -0.0281 458 ASP A CA  
3339 C C   . ASP A 460 ? 0.5695 0.7298 0.9058 -0.0208 0.0675  -0.0505 458 ASP A C   
3340 O O   . ASP A 460 ? 0.4679 0.6579 0.8687 -0.0129 0.0691  -0.0656 458 ASP A O   
3341 C CB  . ASP A 460 ? 0.5201 0.6686 0.9722 -0.0393 0.0435  -0.0330 458 ASP A CB  
3342 C CG  . ASP A 460 ? 0.5961 0.8103 1.1363 -0.0428 0.0817  -0.0191 458 ASP A CG  
3343 O OD1 . ASP A 460 ? 0.5846 0.8298 1.1240 -0.0524 0.1196  0.0118  458 ASP A OD1 
3344 O OD2 . ASP A 460 ? 0.6134 0.8489 1.2261 -0.0355 0.0743  -0.0372 458 ASP A OD2 
3345 N N   . ASN A 461 ? 0.4944 0.6361 0.7508 -0.0160 0.0678  -0.0544 459 ASN A N   
3346 C CA  . ASN A 461 ? 0.5017 0.6566 0.7377 -0.0005 0.0702  -0.0763 459 ASN A CA  
3347 C C   . ASN A 461 ? 0.5158 0.6448 0.7779 0.0094  0.0326  -0.1035 459 ASN A C   
3348 O O   . ASN A 461 ? 0.5409 0.6896 0.8183 0.0241  0.0324  -0.1263 459 ASN A O   
3349 C CB  . ASN A 461 ? 0.4912 0.7122 0.7578 0.0083  0.1115  -0.0758 459 ASN A CB  
3350 C CG  . ASN A 461 ? 0.6011 0.8440 0.8238 0.0027  0.1465  -0.0485 459 ASN A CG  
3351 O OD1 . ASN A 461 ? 0.5767 0.8061 0.7308 0.0076  0.1462  -0.0510 459 ASN A OD1 
3352 N ND2 . ASN A 461 ? 0.5394 0.8146 0.8066 -0.0078 0.1741  -0.0211 459 ASN A ND2 
3353 N N   . LYS A 462 ? 0.5681 0.6509 0.8321 0.0041  -0.0021 -0.1031 460 LYS A N   
3354 C CA  . LYS A 462 ? 0.5554 0.6066 0.8390 0.0141  -0.0430 -0.1254 460 LYS A CA  
3355 C C   . LYS A 462 ? 0.6054 0.6024 0.8151 0.0165  -0.0692 -0.1258 460 LYS A C   
3356 O O   . LYS A 462 ? 0.6300 0.5951 0.8453 0.0254  -0.1048 -0.1403 460 LYS A O   
3357 C CB  . LYS A 462 ? 0.5270 0.5595 0.8595 0.0110  -0.0704 -0.1264 460 LYS A CB  
3358 C CG  . LYS A 462 ? 0.6836 0.7616 1.1222 0.0146  -0.0647 -0.1386 460 LYS A CG  
3359 C CD  . LYS A 462 ? 0.6619 0.8084 1.1304 0.0119  -0.0102 -0.1277 460 LYS A CD  
3360 C CE  . LYS A 462 ? 0.6916 0.8901 1.2737 0.0151  0.0022  -0.1357 460 LYS A CE  
3361 N NZ  . LYS A 462 ? 0.6392 0.9082 1.2415 0.0153  0.0610  -0.1213 460 LYS A NZ  
3362 N N   . LEU A 463 ? 0.5562 0.5428 0.7024 0.0087  -0.0526 -0.1081 461 LEU A N   
3363 C CA  . LEU A 463 ? 0.5573 0.4986 0.6423 0.0088  -0.0707 -0.1030 461 LEU A CA  
3364 C C   . LEU A 463 ? 0.5792 0.5362 0.6601 0.0158  -0.0636 -0.1149 461 LEU A C   
3365 O O   . LEU A 463 ? 0.5524 0.5480 0.6318 0.0162  -0.0340 -0.1150 461 LEU A O   
3366 C CB  . LEU A 463 ? 0.5710 0.4937 0.5997 -0.0027 -0.0578 -0.0792 461 LEU A CB  
3367 C CG  . LEU A 463 ? 0.6257 0.5043 0.5958 -0.0044 -0.0709 -0.0673 461 LEU A CG  
3368 C CD1 . LEU A 463 ? 0.6002 0.4338 0.5593 0.0028  -0.1075 -0.0697 461 LEU A CD1 
3369 C CD2 . LEU A 463 ? 0.5430 0.4144 0.4679 -0.0143 -0.0518 -0.0463 461 LEU A CD2 
3370 N N   . LYS A 464 ? 0.5191 0.4437 0.5973 0.0230  -0.0939 -0.1249 462 LYS A N   
3371 C CA  . LYS A 464 ? 0.5678 0.5020 0.6532 0.0323  -0.0970 -0.1419 462 LYS A CA  
3372 C C   . LYS A 464 ? 0.5949 0.4896 0.6342 0.0246  -0.1066 -0.1245 462 LYS A C   
3373 O O   . LYS A 464 ? 0.6119 0.4661 0.6174 0.0156  -0.1174 -0.1017 462 LYS A O   
3374 C CB  . LYS A 464 ? 0.5795 0.5088 0.7145 0.0473  -0.1275 -0.1689 462 LYS A CB  
3375 C CG  . LYS A 464 ? 0.6826 0.6566 0.8786 0.0558  -0.1168 -0.1876 462 LYS A CG  
3376 C CD  . LYS A 464 ? 0.7403 0.7759 0.9428 0.0576  -0.0710 -0.1894 462 LYS A CD  
3377 C CE  . LYS A 464 ? 0.7509 0.8339 1.0202 0.0620  -0.0533 -0.1981 462 LYS A CE  
3378 N NZ  . LYS A 464 ? 0.8399 0.9848 1.1117 0.0650  -0.0049 -0.1943 462 LYS A NZ  
3379 N N   . ALA A 465 ? 0.5260 0.4339 0.5667 0.0300  -0.1028 -0.1362 463 ALA A N   
3380 C CA  . ALA A 465 ? 0.6281 0.5043 0.6431 0.0222  -0.1118 -0.1209 463 ALA A CA  
3381 C C   . ALA A 465 ? 0.6426 0.4890 0.6872 0.0305  -0.1489 -0.1344 463 ALA A C   
3382 O O   . ALA A 465 ? 0.6860 0.5534 0.7686 0.0473  -0.1606 -0.1677 463 ALA A O   
3383 C CB  . ALA A 465 ? 0.5484 0.4540 0.5496 0.0228  -0.0894 -0.1251 463 ALA A CB  
3384 N N   . HIS A 466 ? 0.6648 0.4632 0.6936 0.0196  -0.1666 -0.1077 464 HIS A N   
3385 C CA  . HIS A 466 ? 0.6832 0.4473 0.7438 0.0242  -0.2035 -0.1126 464 HIS A CA  
3386 C C   . HIS A 466 ? 0.6845 0.4470 0.7584 0.0209  -0.2058 -0.1130 464 HIS A C   
3387 O O   . HIS A 466 ? 0.6893 0.4454 0.8068 0.0322  -0.2346 -0.1376 464 HIS A O   
3388 C CB  . HIS A 466 ? 0.7211 0.4320 0.7600 0.0148  -0.2227 -0.0780 464 HIS A CB  
3389 C CG  . HIS A 466 ? 0.7151 0.3857 0.7892 0.0164  -0.2609 -0.0741 464 HIS A CG  
3390 N ND1 . HIS A 466 ? 0.7900 0.4533 0.9110 0.0321  -0.2966 -0.1038 464 HIS A ND1 
3391 C CD2 . HIS A 466 ? 0.8080 0.4447 0.8867 0.0041  -0.2699 -0.0436 464 HIS A CD2 
3392 C CE1 . HIS A 466 ? 0.8801 0.5024 1.0306 0.0294  -0.3291 -0.0915 464 HIS A CE1 
3393 N NE2 . HIS A 466 ? 0.9118 0.5176 1.0391 0.0115  -0.3127 -0.0531 464 HIS A NE2 
3394 N N   . LYS A 467 ? 0.6622 0.4299 0.7051 0.0070  -0.1792 -0.0889 465 LYS A N   
3395 C CA  . LYS A 467 ? 0.6635 0.4298 0.7249 0.0030  -0.1827 -0.0885 465 LYS A CA  
3396 C C   . LYS A 467 ? 0.5909 0.4013 0.6582 0.0193  -0.1748 -0.1269 465 LYS A C   
3397 O O   . LYS A 467 ? 0.5689 0.4158 0.6166 0.0282  -0.1534 -0.1421 465 LYS A O   
3398 C CB  . LYS A 467 ? 0.6675 0.4257 0.6988 -0.0166 -0.1566 -0.0493 465 LYS A CB  
3399 C CG  . LYS A 467 ? 0.7393 0.4546 0.7618 -0.0311 -0.1612 -0.0068 465 LYS A CG  
3400 C CD  . LYS A 467 ? 0.6850 0.4021 0.6878 -0.0474 -0.1318 0.0264  465 LYS A CD  
3401 C CE  . LYS A 467 ? 0.7320 0.4106 0.7277 -0.0605 -0.1313 0.0726  465 LYS A CE  
3402 N NZ  . LYS A 467 ? 0.7266 0.4141 0.7093 -0.0745 -0.0981 0.1030  465 LYS A NZ  
3403 N N   . ASP A 468 ? 0.6176 0.4238 0.7137 0.0239  -0.1935 -0.1412 466 ASP A N   
3404 C CA  . ASP A 468 ? 0.6485 0.4917 0.7400 0.0422  -0.1897 -0.1767 466 ASP A CA  
3405 C C   . ASP A 468 ? 0.5921 0.4521 0.6457 0.0305  -0.1584 -0.1556 466 ASP A C   
3406 O O   . ASP A 468 ? 0.5573 0.4002 0.5972 0.0091  -0.1419 -0.1173 466 ASP A O   
3407 C CB  . ASP A 468 ? 0.6234 0.4498 0.7645 0.0548  -0.2314 -0.2051 466 ASP A CB  
3408 C CG  . ASP A 468 ? 0.7096 0.5734 0.8403 0.0838  -0.2356 -0.2531 466 ASP A CG  
3409 O OD1 . ASP A 468 ? 0.8424 0.7473 0.9285 0.0938  -0.2031 -0.2612 466 ASP A OD1 
3410 O OD2 . ASP A 468 ? 0.8571 0.7084 1.0248 0.0977  -0.2725 -0.2819 466 ASP A OD2 
3411 N N   . LYS A 469 ? 0.5894 0.4837 0.6231 0.0471  -0.1500 -0.1814 467 LYS A N   
3412 C CA  . LYS A 469 ? 0.5897 0.4955 0.5939 0.0383  -0.1288 -0.1643 467 LYS A CA  
3413 C C   . LYS A 469 ? 0.6108 0.4859 0.6519 0.0263  -0.1509 -0.1524 467 LYS A C   
3414 O O   . LYS A 469 ? 0.6112 0.4701 0.6959 0.0365  -0.1876 -0.1759 467 LYS A O   
3415 C CB  . LYS A 469 ? 0.6422 0.5870 0.6142 0.0620  -0.1210 -0.1942 467 LYS A CB  
3416 C CG  . LYS A 469 ? 0.6905 0.6729 0.6336 0.0730  -0.0924 -0.2009 467 LYS A CG  
3417 C CD  . LYS A 469 ? 0.7033 0.7252 0.6061 0.0967  -0.0794 -0.2224 467 LYS A CD  
3418 C CE  . LYS A 469 ? 0.7899 0.8539 0.6723 0.1049  -0.0442 -0.2212 467 LYS A CE  
3419 N NZ  . LYS A 469 ? 0.9584 1.0609 0.7901 0.1226  -0.0210 -0.2254 467 LYS A NZ  
3420 N N   . SER A 470 ? 0.5634 0.4312 0.5948 0.0050  -0.1296 -0.1164 468 SER A N   
3421 C CA  . SER A 470 ? 0.5914 0.4342 0.6683 -0.0092 -0.1446 -0.0992 468 SER A CA  
3422 C C   . SER A 470 ? 0.5890 0.4431 0.6788 0.0019  -0.1611 -0.1223 468 SER A C   
3423 O O   . SER A 470 ? 0.5388 0.3728 0.6871 -0.0019 -0.1894 -0.1245 468 SER A O   
3424 C CB  . SER A 470 ? 0.5508 0.3856 0.6149 -0.0333 -0.1131 -0.0537 468 SER A CB  
3425 O OG  . SER A 470 ? 0.5373 0.3976 0.5613 -0.0336 -0.0864 -0.0501 468 SER A OG  
3426 N N   . ALA A 471 ? 0.5392 0.4234 0.5785 0.0156  -0.1458 -0.1375 469 ALA A N   
3427 C CA  . ALA A 471 ? 0.5317 0.4255 0.5691 0.0274  -0.1603 -0.1557 469 ALA A CA  
3428 C C   . ALA A 471 ? 0.5164 0.4002 0.5803 0.0053  -0.1506 -0.1246 469 ALA A C   
3429 O O   . ALA A 471 ? 0.5499 0.4314 0.6395 0.0109  -0.1729 -0.1373 469 ALA A O   
3430 C CB  . ALA A 471 ? 0.6374 0.5197 0.7152 0.0492  -0.2090 -0.1976 469 ALA A CB  
3431 N N   . GLN A 472 ? 0.5264 0.4046 0.5865 -0.0175 -0.1193 -0.0860 470 GLN A N   
3432 C CA  . GLN A 472 ? 0.5668 0.4417 0.6475 -0.0373 -0.1011 -0.0548 470 GLN A CA  
3433 C C   . GLN A 472 ? 0.5525 0.4437 0.5781 -0.0442 -0.0620 -0.0339 470 GLN A C   
3434 O O   . GLN A 472 ? 0.5284 0.4155 0.5613 -0.0607 -0.0390 -0.0044 470 GLN A O   
3435 C CB  . GLN A 472 ? 0.5193 0.3696 0.6563 -0.0567 -0.1019 -0.0263 470 GLN A CB  
3436 C CG  . GLN A 472 ? 0.5724 0.4024 0.7794 -0.0523 -0.1447 -0.0439 470 GLN A CG  
3437 C CD  . GLN A 472 ? 0.5631 0.3704 0.8374 -0.0749 -0.1426 -0.0064 470 GLN A CD  
3438 O OE1 . GLN A 472 ? 0.6132 0.4256 0.9202 -0.0900 -0.1247 0.0194  470 GLN A OE1 
3439 N NE2 . GLN A 472 ? 0.5851 0.3684 0.8834 -0.0768 -0.1600 -0.0014 470 GLN A NE2 
3440 N N   . CYS A 473 ? 0.5606 0.4710 0.5341 -0.0306 -0.0541 -0.0488 471 CYS A N   
3441 C CA  . CYS A 473 ? 0.5584 0.4836 0.4878 -0.0357 -0.0227 -0.0318 471 CYS A CA  
3442 C C   . CYS A 473 ? 0.5492 0.4934 0.4529 -0.0250 -0.0228 -0.0411 471 CYS A C   
3443 O O   . CYS A 473 ? 0.5326 0.4918 0.4086 -0.0067 -0.0308 -0.0622 471 CYS A O   
3444 C CB  . CYS A 473 ? 0.5349 0.4664 0.4357 -0.0311 -0.0122 -0.0349 471 CYS A CB  
3445 S SG  . CYS A 473 ? 0.5487 0.4533 0.4676 -0.0420 -0.0141 -0.0205 471 CYS A SG  
3446 N N   . PHE A 474 ? 0.5573 0.5018 0.4682 -0.0344 -0.0136 -0.0251 472 PHE A N   
3447 C CA  . PHE A 474 ? 0.5524 0.5091 0.4435 -0.0245 -0.0197 -0.0316 472 PHE A CA  
3448 C C   . PHE A 474 ? 0.5395 0.5056 0.4038 -0.0323 0.0064  -0.0098 472 PHE A C   
3449 O O   . PHE A 474 ? 0.4657 0.4264 0.3385 -0.0462 0.0256  0.0081  472 PHE A O   
3450 C CB  . PHE A 474 ? 0.5890 0.5357 0.5267 -0.0257 -0.0427 -0.0374 472 PHE A CB  
3451 C CG  . PHE A 474 ? 0.5799 0.5130 0.5614 -0.0204 -0.0730 -0.0574 472 PHE A CG  
3452 C CD1 . PHE A 474 ? 0.5683 0.5034 0.5346 0.0030  -0.1037 -0.0902 472 PHE A CD1 
3453 C CD2 . PHE A 474 ? 0.5609 0.4787 0.5992 -0.0372 -0.0715 -0.0428 472 PHE A CD2 
3454 C CE1 . PHE A 474 ? 0.5552 0.4750 0.5695 0.0096  -0.1376 -0.1126 472 PHE A CE1 
3455 C CE2 . PHE A 474 ? 0.5488 0.4512 0.6382 -0.0340 -0.1026 -0.0584 472 PHE A CE2 
3456 C CZ  . PHE A 474 ? 0.5598 0.4620 0.6409 -0.0105 -0.1382 -0.0956 472 PHE A CZ  
3457 N N   . LYS A 475 ? 0.4769 0.4557 0.3077 -0.0213 0.0045  -0.0117 473 LYS A N   
3458 C CA  . LYS A 475 ? 0.4281 0.4137 0.2403 -0.0279 0.0238  0.0095  473 LYS A CA  
3459 C C   . LYS A 475 ? 0.4841 0.4710 0.2871 -0.0198 0.0090  0.0097  473 LYS A C   
3460 O O   . LYS A 475 ? 0.5166 0.5042 0.3059 -0.0033 -0.0141 -0.0083 473 LYS A O   
3461 C CB  . LYS A 475 ? 0.4425 0.4440 0.2206 -0.0246 0.0425  0.0170  473 LYS A CB  
3462 C CG  . LYS A 475 ? 0.4664 0.4859 0.2043 -0.0043 0.0374  0.0061  473 LYS A CG  
3463 C CD  . LYS A 475 ? 0.4682 0.5086 0.1859 -0.0039 0.0627  0.0192  473 LYS A CD  
3464 C CE  . LYS A 475 ? 0.5858 0.6501 0.2568 0.0175  0.0663  0.0155  473 LYS A CE  
3465 N NZ  . LYS A 475 ? 0.5148 0.6034 0.1803 0.0155  0.0957  0.0329  473 LYS A NZ  
3466 N N   . MET A 476 ? 0.5074 0.4924 0.3174 -0.0290 0.0189  0.0281  474 MET A N   
3467 C CA  . MET A 476 ? 0.4704 0.4536 0.2737 -0.0220 0.0033  0.0316  474 MET A CA  
3468 C C   . MET A 476 ? 0.4563 0.4412 0.2530 -0.0302 0.0193  0.0555  474 MET A C   
3469 O O   . MET A 476 ? 0.4785 0.4599 0.3013 -0.0432 0.0347  0.0631  474 MET A O   
3470 C CB  . MET A 476 ? 0.5481 0.5208 0.4027 -0.0249 -0.0158 0.0214  474 MET A CB  
3471 C CG  . MET A 476 ? 0.6496 0.6177 0.4971 -0.0114 -0.0445 0.0155  474 MET A CG  
3472 S SD  . MET A 476 ? 0.7199 0.6796 0.6468 -0.0184 -0.0624 0.0085  474 MET A SD  
3473 C CE  . MET A 476 ? 0.6757 0.6337 0.6531 -0.0255 -0.0632 -0.0059 474 MET A CE  
3474 N N   . PHE A 477 ? 0.4924 0.4812 0.2530 -0.0209 0.0140  0.0675  475 PHE A N   
3475 C CA  . PHE A 477 ? 0.5028 0.4902 0.2633 -0.0282 0.0235  0.0930  475 PHE A CA  
3476 C C   . PHE A 477 ? 0.5110 0.4854 0.2943 -0.0265 0.0016  0.0936  475 PHE A C   
3477 O O   . PHE A 477 ? 0.5292 0.4996 0.2881 -0.0125 -0.0211 0.0905  475 PHE A O   
3478 C CB  . PHE A 477 ? 0.5410 0.5416 0.2529 -0.0204 0.0339  0.1127  475 PHE A CB  
3479 C CG  . PHE A 477 ? 0.6534 0.6520 0.3737 -0.0300 0.0436  0.1441  475 PHE A CG  
3480 C CD1 . PHE A 477 ? 0.5389 0.5418 0.2859 -0.0437 0.0637  0.1549  475 PHE A CD1 
3481 C CD2 . PHE A 477 ? 0.6740 0.6643 0.3768 -0.0239 0.0290  0.1632  475 PHE A CD2 
3482 C CE1 . PHE A 477 ? 0.6364 0.6338 0.4036 -0.0520 0.0677  0.1808  475 PHE A CE1 
3483 C CE2 . PHE A 477 ? 0.6542 0.6401 0.3721 -0.0335 0.0352  0.1949  475 PHE A CE2 
3484 C CZ  . PHE A 477 ? 0.6919 0.6817 0.4460 -0.0481 0.0545  0.2032  475 PHE A CZ  
3485 N N   . TYR A 478 ? 0.4639 0.4318 0.2928 -0.0381 0.0068  0.0955  476 TYR A N   
3486 C CA  . TYR A 478 ? 0.4972 0.4554 0.3611 -0.0366 -0.0124 0.0930  476 TYR A CA  
3487 C C   . TYR A 478 ? 0.4815 0.4360 0.3777 -0.0465 -0.0009 0.1027  476 TYR A C   
3488 O O   . TYR A 478 ? 0.4349 0.3925 0.3606 -0.0530 0.0144  0.0922  476 TYR A O   
3489 C CB  . TYR A 478 ? 0.5517 0.5105 0.4566 -0.0358 -0.0220 0.0701  476 TYR A CB  
3490 C CG  . TYR A 478 ? 0.6123 0.5650 0.5629 -0.0320 -0.0451 0.0629  476 TYR A CG  
3491 C CD1 . TYR A 478 ? 0.5943 0.5497 0.5985 -0.0393 -0.0349 0.0613  476 TYR A CD1 
3492 C CD2 . TYR A 478 ? 0.6701 0.6152 0.6116 -0.0183 -0.0788 0.0545  476 TYR A CD2 
3493 C CE1 . TYR A 478 ? 0.6222 0.5755 0.6778 -0.0349 -0.0554 0.0528  476 TYR A CE1 
3494 C CE2 . TYR A 478 ? 0.6939 0.6327 0.6852 -0.0141 -0.1041 0.0461  476 TYR A CE2 
3495 C CZ  . TYR A 478 ? 0.6688 0.6131 0.7213 -0.0234 -0.0911 0.0457  476 TYR A CZ  
3496 O OH  . TYR A 478 ? 0.7304 0.6718 0.8413 -0.0184 -0.1156 0.0356  476 TYR A OH  
3497 N N   . LYS A 479 ? 0.4689 0.4155 0.3586 -0.0456 -0.0099 0.1225  477 LYS A N   
3498 C CA  . LYS A 479 ? 0.5252 0.4656 0.4490 -0.0529 -0.0044 0.1292  477 LYS A CA  
3499 C C   . LYS A 479 ? 0.5052 0.4436 0.4817 -0.0513 -0.0108 0.1097  477 LYS A C   
3500 O O   . LYS A 479 ? 0.4513 0.3911 0.4542 -0.0543 0.0020  0.1006  477 LYS A O   
3501 C CB  . LYS A 479 ? 0.5911 0.5210 0.5056 -0.0531 -0.0163 0.1581  477 LYS A CB  
3502 C CG  . LYS A 479 ? 0.5712 0.5087 0.4504 -0.0578 0.0006  0.1824  477 LYS A CG  
3503 C CD  . LYS A 479 ? 0.7254 0.6548 0.5871 -0.0563 -0.0104 0.2183  477 LYS A CD  
3504 C CE  . LYS A 479 ? 0.7012 0.6442 0.5374 -0.0616 0.0124  0.2468  477 LYS A CE  
3505 N NZ  . LYS A 479 ? 0.8050 0.7448 0.6917 -0.0754 0.0209  0.2569  477 LYS A NZ  
3506 N N   . GLY A 480 ? 0.5396 0.4761 0.5333 -0.0445 -0.0311 0.1014  478 GLY A N   
3507 C CA  . GLY A 480 ? 0.5429 0.4836 0.5964 -0.0424 -0.0342 0.0826  478 GLY A CA  
3508 C C   . GLY A 480 ? 0.5402 0.4718 0.6282 -0.0403 -0.0445 0.0853  478 GLY A C   
3509 O O   . GLY A 480 ? 0.5462 0.4623 0.6209 -0.0390 -0.0642 0.1044  478 GLY A O   
3510 N N   . VAL A 481 ? 0.5287 0.4702 0.6624 -0.0386 -0.0312 0.0665  479 VAL A N   
3511 C CA  . VAL A 481 ? 0.5309 0.4659 0.7061 -0.0330 -0.0417 0.0601  479 VAL A CA  
3512 C C   . VAL A 481 ? 0.5219 0.4668 0.7033 -0.0311 -0.0150 0.0443  479 VAL A C   
3513 O O   . VAL A 481 ? 0.5205 0.4840 0.7056 -0.0303 0.0107  0.0314  479 VAL A O   
3514 C CB  . VAL A 481 ? 0.5439 0.4838 0.7797 -0.0246 -0.0601 0.0450  479 VAL A CB  
3515 C CG1 . VAL A 481 ? 0.5393 0.4755 0.8238 -0.0161 -0.0688 0.0319  479 VAL A CG1 
3516 C CG2 . VAL A 481 ? 0.5664 0.4906 0.7900 -0.0226 -0.0946 0.0592  479 VAL A CG2 
3517 N N   . ILE A 482 ? 0.5204 0.4520 0.7034 -0.0293 -0.0225 0.0461  480 ILE A N   
3518 C CA  . ILE A 482 ? 0.5322 0.4686 0.7112 -0.0236 -0.0037 0.0284  480 ILE A CA  
3519 C C   . ILE A 482 ? 0.5936 0.5323 0.8240 -0.0083 -0.0119 0.0031  480 ILE A C   
3520 O O   . ILE A 482 ? 0.5539 0.4753 0.8172 -0.0053 -0.0413 0.0055  480 ILE A O   
3521 C CB  . ILE A 482 ? 0.5158 0.4358 0.6665 -0.0299 -0.0085 0.0420  480 ILE A CB  
3522 C CG1 . ILE A 482 ? 0.5105 0.4326 0.6136 -0.0426 0.0015  0.0649  480 ILE A CG1 
3523 C CG2 . ILE A 482 ? 0.5445 0.4661 0.6892 -0.0199 0.0041  0.0184  480 ILE A CG2 
3524 C CD1 . ILE A 482 ? 0.4863 0.3979 0.5818 -0.0499 -0.0174 0.0939  480 ILE A CD1 
3525 N N   . THR A 483 ? 0.5760 0.5370 0.8139 0.0023  0.0147  -0.0201 481 THR A N   
3526 C CA  . THR A 483 ? 0.5741 0.5453 0.8541 0.0217  0.0157  -0.0502 481 THR A CA  
3527 C C   . THR A 483 ? 0.5848 0.5576 0.8269 0.0336  0.0340  -0.0680 481 THR A C   
3528 O O   . THR A 483 ? 0.5972 0.5682 0.7870 0.0257  0.0506  -0.0563 481 THR A O   
3529 C CB  . THR A 483 ? 0.5577 0.5595 0.8798 0.0275  0.0359  -0.0617 481 THR A CB  
3530 O OG1 . THR A 483 ? 0.5504 0.5459 0.9100 0.0191  0.0097  -0.0489 481 THR A OG1 
3531 C CG2 . THR A 483 ? 0.5985 0.6175 0.9629 0.0510  0.0430  -0.0956 481 THR A CG2 
3532 N N   . HIS A 484 ? 0.5770 0.5515 0.8441 0.0554  0.0276  -0.0989 482 HIS A N   
3533 C CA  . HIS A 484 ? 0.5951 0.5663 0.8213 0.0719  0.0368  -0.1204 482 HIS A CA  
3534 C C   . HIS A 484 ? 0.6441 0.6418 0.8816 0.1007  0.0590  -0.1565 482 HIS A C   
3535 O O   . HIS A 484 ? 0.6416 0.6463 0.9371 0.1139  0.0452  -0.1771 482 HIS A O   
3536 C CB  . HIS A 484 ? 0.5888 0.5261 0.8249 0.0738  -0.0038 -0.1256 482 HIS A CB  
3537 C CG  . HIS A 484 ? 0.5868 0.5025 0.8157 0.0472  -0.0214 -0.0877 482 HIS A CG  
3538 N ND1 . HIS A 484 ? 0.5984 0.5059 0.7798 0.0368  -0.0139 -0.0734 482 HIS A ND1 
3539 C CD2 . HIS A 484 ? 0.5653 0.4675 0.8268 0.0309  -0.0449 -0.0607 482 HIS A CD2 
3540 C CE1 . HIS A 484 ? 0.5779 0.4720 0.7659 0.0154  -0.0282 -0.0401 482 HIS A CE1 
3541 N NE2 . HIS A 484 ? 0.5670 0.4570 0.7984 0.0118  -0.0464 -0.0302 482 HIS A NE2 
3542 N N   . ASP A 485 ? 0.7248 0.7386 0.9058 0.1115  0.0945  -0.1628 483 ASP A N   
3543 C CA  . ASP A 485 ? 0.7690 0.8097 0.9410 0.1436  0.1214  -0.1965 483 ASP A CA  
3544 C C   . ASP A 485 ? 0.7940 0.8086 0.9280 0.1662  0.0951  -0.2260 483 ASP A C   
3545 O O   . ASP A 485 ? 0.8681 0.8724 0.9338 0.1694  0.1034  -0.2229 483 ASP A O   
3546 C CB  . ASP A 485 ? 0.7494 0.8212 0.8788 0.1429  0.1754  -0.1805 483 ASP A CB  
3547 C CG  . ASP A 485 ? 1.0046 1.1150 1.1357 0.1752  0.2127  -0.2085 483 ASP A CG  
3548 O OD1 . ASP A 485 ? 0.9957 1.1006 1.0998 0.2071  0.2022  -0.2458 483 ASP A OD1 
3549 O OD2 . ASP A 485 ? 1.0741 1.2216 1.2368 0.1699  0.2524  -0.1940 483 ASP A OD2 
3550 N N   . VAL A 486 ? 0.8309 0.8316 1.0157 0.1820  0.0574  -0.2557 484 VAL A N   
3551 C CA  . VAL A 486 ? 0.8707 0.8404 1.0418 0.2021  0.0187  -0.2862 484 VAL A CA  
3552 C C   . VAL A 486 ? 0.8617 0.7955 1.0340 0.1713  -0.0124 -0.2534 484 VAL A C   
3553 O O   . VAL A 486 ? 0.9388 0.8520 1.1713 0.1550  -0.0473 -0.2396 484 VAL A O   
3554 C CB  . VAL A 486 ? 0.8874 0.8659 0.9782 0.2345  0.0411  -0.3150 484 VAL A CB  
3555 C CG1 . VAL A 486 ? 0.8531 0.7961 0.9403 0.2583  -0.0088 -0.3531 484 VAL A CG1 
3556 C CG2 . VAL A 486 ? 0.8719 0.8943 0.9585 0.2646  0.0828  -0.3410 484 VAL A CG2 
3557 N N   . SER A 487 ? 0.8960 0.8236 1.0028 0.1637  0.0020  -0.2382 485 SER A N   
3558 C CA  . SER A 487 ? 0.8441 0.7456 0.9498 0.1350  -0.0187 -0.2060 485 SER A CA  
3559 C C   . SER A 487 ? 0.8570 0.7710 0.9132 0.1123  0.0163  -0.1701 485 SER A C   
3560 O O   . SER A 487 ? 0.8792 0.7799 0.9420 0.0860  0.0058  -0.1392 485 SER A O   
3561 C CB  . SER A 487 ? 0.7935 0.6651 0.8847 0.1499  -0.0534 -0.2297 485 SER A CB  
3562 O OG  . SER A 487 ? 0.9575 0.8156 1.0962 0.1751  -0.0899 -0.2691 485 SER A OG  
3563 N N   . SER A 488 ? 0.8366 0.7763 0.8468 0.1224  0.0577  -0.1724 486 SER A N   
3564 C CA  . SER A 488 ? 0.7797 0.7302 0.7540 0.1007  0.0883  -0.1382 486 SER A CA  
3565 C C   . SER A 488 ? 0.6872 0.6477 0.7109 0.0746  0.0907  -0.1101 486 SER A C   
3566 O O   . SER A 488 ? 0.6826 0.6597 0.7527 0.0795  0.0944  -0.1180 486 SER A O   
3567 C CB  . SER A 488 ? 0.8191 0.7951 0.7439 0.1177  0.1323  -0.1433 486 SER A CB  
3568 O OG  . SER A 488 ? 0.7806 0.7562 0.6614 0.1007  0.1530  -0.1138 486 SER A OG  
3569 N N   . ALA A 489 ? 0.6223 0.5732 0.6359 0.0496  0.0868  -0.0801 487 ALA A N   
3570 C CA  . ALA A 489 ? 0.6289 0.5842 0.6801 0.0285  0.0816  -0.0560 487 ALA A CA  
3571 C C   . ALA A 489 ? 0.5693 0.5485 0.6183 0.0204  0.1126  -0.0423 487 ALA A C   
3572 O O   . ALA A 489 ? 0.5286 0.5168 0.5392 0.0224  0.1395  -0.0388 487 ALA A O   
3573 C CB  . ALA A 489 ? 0.6216 0.5580 0.6640 0.0088  0.0624  -0.0319 487 ALA A CB  
3574 N N   . ILE A 490 ? 0.5714 0.5584 0.6663 0.0112  0.1051  -0.0334 488 ILE A N   
3575 C CA  . ILE A 490 ? 0.5249 0.5323 0.6383 0.0020  0.1249  -0.0213 488 ILE A CA  
3576 C C   . ILE A 490 ? 0.5341 0.5314 0.6678 -0.0134 0.0992  -0.0041 488 ILE A C   
3577 O O   . ILE A 490 ? 0.5772 0.5610 0.7328 -0.0124 0.0712  -0.0045 488 ILE A O   
3578 C CB  . ILE A 490 ? 0.5079 0.5428 0.6695 0.0155  0.1442  -0.0377 488 ILE A CB  
3579 C CG1 . ILE A 490 ? 0.5077 0.5559 0.6367 0.0355  0.1742  -0.0545 488 ILE A CG1 
3580 C CG2 . ILE A 490 ? 0.4629 0.5177 0.6626 0.0035  0.1589  -0.0235 488 ILE A CG2 
3581 C CD1 . ILE A 490 ? 0.4905 0.5695 0.6669 0.0540  0.1948  -0.0750 488 ILE A CD1 
3582 N N   . ASN A 491 ? 0.4764 0.4785 0.6011 -0.0258 0.1066  0.0111  489 ASN A N   
3583 C CA  . ASN A 491 ? 0.4669 0.4616 0.6043 -0.0354 0.0821  0.0234  489 ASN A CA  
3584 C C   . ASN A 491 ? 0.4559 0.4680 0.6315 -0.0394 0.0913  0.0238  489 ASN A C   
3585 O O   . ASN A 491 ? 0.3980 0.4113 0.5561 -0.0475 0.0998  0.0327  489 ASN A O   
3586 C CB  . ASN A 491 ? 0.4367 0.4158 0.5227 -0.0444 0.0732  0.0389  489 ASN A CB  
3587 C CG  . ASN A 491 ? 0.4495 0.4191 0.5349 -0.0483 0.0459  0.0507  489 ASN A CG  
3588 O OD1 . ASN A 491 ? 0.4640 0.4387 0.5766 -0.0477 0.0351  0.0483  489 ASN A OD1 
3589 N ND2 . ASN A 491 ? 0.4457 0.4017 0.5006 -0.0510 0.0341  0.0643  489 ASN A ND2 
3590 N N   . ARG A 492 ? 0.4538 0.4793 0.6904 -0.0332 0.0874  0.0132  490 ARG A N   
3591 C CA  . ARG A 492 ? 0.4204 0.4641 0.7126 -0.0374 0.0933  0.0131  490 ARG A CA  
3592 C C   . ARG A 492 ? 0.4202 0.4500 0.7047 -0.0455 0.0653  0.0214  490 ARG A C   
3593 O O   . ARG A 492 ? 0.3878 0.4251 0.6875 -0.0529 0.0745  0.0261  490 ARG A O   
3594 C CB  . ARG A 492 ? 0.4279 0.4880 0.7949 -0.0280 0.0881  -0.0020 490 ARG A CB  
3595 C CG  . ARG A 492 ? 0.4888 0.5648 0.8611 -0.0146 0.1150  -0.0161 490 ARG A CG  
3596 C CD  . ARG A 492 ? 0.5017 0.6049 0.9600 -0.0043 0.1207  -0.0328 490 ARG A CD  
3597 N NE  . ARG A 492 ? 0.4725 0.6051 0.9371 0.0090  0.1643  -0.0440 490 ARG A NE  
3598 C CZ  . ARG A 492 ? 0.6157 0.7781 1.0968 0.0065  0.2076  -0.0346 490 ARG A CZ  
3599 N NH1 . ARG A 492 ? 0.4788 0.6478 0.9964 -0.0098 0.2102  -0.0168 490 ARG A NH1 
3600 N NH2 . ARG A 492 ? 0.6181 0.8049 1.0835 0.0225  0.2482  -0.0436 490 ARG A NH2 
3601 N N   . PRO A 493 ? 0.4588 0.4685 0.7218 -0.0430 0.0301  0.0236  491 PRO A N   
3602 C CA  . PRO A 493 ? 0.4754 0.4730 0.7187 -0.0454 0.0039  0.0281  491 PRO A CA  
3603 C C   . PRO A 493 ? 0.4586 0.4541 0.6542 -0.0524 0.0188  0.0353  491 PRO A C   
3604 O O   . PRO A 493 ? 0.4666 0.4602 0.6704 -0.0537 0.0047  0.0323  491 PRO A O   
3605 C CB  . PRO A 493 ? 0.5246 0.5015 0.7297 -0.0395 -0.0261 0.0354  491 PRO A CB  
3606 C CG  . PRO A 493 ? 0.5230 0.5025 0.7721 -0.0340 -0.0283 0.0290  491 PRO A CG  
3607 C CD  . PRO A 493 ? 0.4934 0.4898 0.7495 -0.0361 0.0111  0.0230  491 PRO A CD  
3608 N N   . GLN A 494 ? 0.4346 0.4284 0.5848 -0.0554 0.0424  0.0421  492 GLN A N   
3609 C CA  . GLN A 494 ? 0.4073 0.3985 0.5181 -0.0612 0.0543  0.0476  492 GLN A CA  
3610 C C   . GLN A 494 ? 0.3906 0.3946 0.5406 -0.0670 0.0748  0.0474  492 GLN A C   
3611 O O   . GLN A 494 ? 0.3687 0.3688 0.5133 -0.0716 0.0709  0.0494  492 GLN A O   
3612 C CB  . GLN A 494 ? 0.3757 0.3606 0.4350 -0.0620 0.0700  0.0538  492 GLN A CB  
3613 C CG  . GLN A 494 ? 0.4782 0.4511 0.4961 -0.0604 0.0525  0.0618  492 GLN A CG  
3614 C CD  . GLN A 494 ? 0.5577 0.5256 0.5399 -0.0625 0.0659  0.0674  492 GLN A CD  
3615 O OE1 . GLN A 494 ? 0.3630 0.3329 0.3440 -0.0627 0.0844  0.0624  492 GLN A OE1 
3616 N NE2 . GLN A 494 ? 0.3762 0.3381 0.3303 -0.0631 0.0562  0.0787  492 GLN A NE2 
3617 N N   . ILE A 495 ? 0.3580 0.3780 0.5502 -0.0660 0.0973  0.0459  493 ILE A N   
3618 C CA  . ILE A 495 ? 0.4210 0.4572 0.6609 -0.0723 0.1204  0.0521  493 ILE A CA  
3619 C C   . ILE A 495 ? 0.3887 0.4272 0.6937 -0.0760 0.0949  0.0477  493 ILE A C   
3620 O O   . ILE A 495 ? 0.4018 0.4419 0.7366 -0.0841 0.0977  0.0545  493 ILE A O   
3621 C CB  . ILE A 495 ? 0.3647 0.4235 0.6355 -0.0670 0.1538  0.0514  493 ILE A CB  
3622 C CG1 . ILE A 495 ? 0.4174 0.4699 0.6225 -0.0583 0.1694  0.0486  493 ILE A CG1 
3623 C CG2 . ILE A 495 ? 0.3725 0.4512 0.6896 -0.0744 0.1856  0.0659  493 ILE A CG2 
3624 C CD1 . ILE A 495 ? 0.5295 0.5747 0.6802 -0.0616 0.1901  0.0609  493 ILE A CD1 
3625 N N   . GLY A 496 ? 0.3705 0.4063 0.7014 -0.0692 0.0653  0.0357  494 GLY A N   
3626 C CA  . GLY A 496 ? 0.3649 0.4001 0.7592 -0.0693 0.0336  0.0270  494 GLY A CA  
3627 C C   . GLY A 496 ? 0.3775 0.3940 0.7372 -0.0697 0.0074  0.0243  494 GLY A C   
3628 O O   . GLY A 496 ? 0.4152 0.4325 0.8302 -0.0738 -0.0065 0.0205  494 GLY A O   
3629 N N   . VAL A 497 ? 0.4221 0.4230 0.6958 -0.0645 -0.0002 0.0252  495 VAL A N   
3630 C CA  . VAL A 497 ? 0.4596 0.4465 0.6927 -0.0613 -0.0211 0.0198  495 VAL A CA  
3631 C C   . VAL A 497 ? 0.4306 0.4204 0.6820 -0.0719 -0.0012 0.0267  495 VAL A C   
3632 O O   . VAL A 497 ? 0.4262 0.4081 0.6982 -0.0708 -0.0242 0.0176  495 VAL A O   
3633 C CB  . VAL A 497 ? 0.5132 0.4903 0.6559 -0.0548 -0.0214 0.0241  495 VAL A CB  
3634 C CG1 . VAL A 497 ? 0.5494 0.5190 0.6490 -0.0512 -0.0303 0.0187  495 VAL A CG1 
3635 C CG2 . VAL A 497 ? 0.5721 0.5417 0.6959 -0.0433 -0.0488 0.0213  495 VAL A CG2 
3636 N N   . VAL A 498 ? 0.3691 0.3681 0.6130 -0.0804 0.0386  0.0422  496 VAL A N   
3637 C CA  . VAL A 498 ? 0.4099 0.4090 0.6672 -0.0903 0.0582  0.0543  496 VAL A CA  
3638 C C   . VAL A 498 ? 0.4251 0.4337 0.7800 -0.0982 0.0547  0.0577  496 VAL A C   
3639 O O   . VAL A 498 ? 0.4071 0.4077 0.7926 -0.1041 0.0437  0.0604  496 VAL A O   
3640 C CB  . VAL A 498 ? 0.3879 0.3933 0.6075 -0.0938 0.0997  0.0703  496 VAL A CB  
3641 C CG1 . VAL A 498 ? 0.3746 0.3785 0.6077 -0.1035 0.1199  0.0881  496 VAL A CG1 
3642 C CG2 . VAL A 498 ? 0.4126 0.4068 0.5498 -0.0872 0.0976  0.0661  496 VAL A CG2 
3643 N N   . ARG A 499 ? 0.4088 0.4353 0.8229 -0.0982 0.0625  0.0574  497 ARG A N   
3644 C CA  . ARG A 499 ? 0.4101 0.4498 0.9333 -0.1062 0.0591  0.0611  497 ARG A CA  
3645 C C   . ARG A 499 ? 0.4620 0.4839 1.0205 -0.1025 0.0062  0.0419  497 ARG A C   
3646 O O   . ARG A 499 ? 0.5231 0.5429 1.1499 -0.1116 -0.0021 0.0474  497 ARG A O   
3647 C CB  . ARG A 499 ? 0.3671 0.4298 0.9474 -0.1029 0.0695  0.0572  497 ARG A CB  
3648 C CG  . ARG A 499 ? 0.4241 0.5086 1.1323 -0.1119 0.0739  0.0635  497 ARG A CG  
3649 C CD  . ARG A 499 ? 0.4551 0.5637 1.2121 -0.1053 0.0841  0.0553  497 ARG A CD  
3650 N NE  . ARG A 499 ? 0.6726 0.7622 1.3778 -0.0908 0.0442  0.0320  497 ARG A NE  
3651 C CZ  . ARG A 499 ? 0.7393 0.8394 1.4606 -0.0814 0.0427  0.0211  497 ARG A CZ  
3652 N NH1 . ARG A 499 ? 0.6821 0.8147 1.4579 -0.0822 0.0833  0.0272  497 ARG A NH1 
3653 N NH2 . ARG A 499 ? 0.6198 0.6975 1.2963 -0.0694 0.0010  0.0048  497 ARG A NH2 
3654 N N   . GLU A 500 ? 0.4619 0.4696 0.9739 -0.0875 -0.0319 0.0194  498 GLU A N   
3655 C CA  . GLU A 500 ? 0.5855 0.5749 1.1158 -0.0774 -0.0859 -0.0042 498 GLU A CA  
3656 C C   . GLU A 500 ? 0.5133 0.4876 1.0113 -0.0786 -0.0927 -0.0056 498 GLU A C   
3657 O O   . GLU A 500 ? 0.5883 0.5502 1.1346 -0.0744 -0.1318 -0.0226 498 GLU A O   
3658 C CB  . GLU A 500 ? 0.5617 0.5387 1.0257 -0.0580 -0.1200 -0.0235 498 GLU A CB  
3659 C CG  . GLU A 500 ? 0.6016 0.5887 1.0951 -0.0548 -0.1204 -0.0236 498 GLU A CG  
3660 C CD  . GLU A 500 ? 0.7560 0.7584 1.3783 -0.0623 -0.1259 -0.0261 498 GLU A CD  
3661 O OE1 . GLU A 500 ? 0.7644 0.7574 1.4495 -0.0579 -0.1684 -0.0435 498 GLU A OE1 
3662 O OE2 . GLU A 500 ? 0.8136 0.8390 1.4785 -0.0709 -0.0887 -0.0124 498 GLU A OE2 
3663 N N   . PHE A 501 ? 0.4220 0.3958 0.8440 -0.0827 -0.0592 0.0093  499 PHE A N   
3664 C CA  . PHE A 501 ? 0.4672 0.4269 0.8570 -0.0827 -0.0651 0.0073  499 PHE A CA  
3665 C C   . PHE A 501 ? 0.4888 0.4493 0.9578 -0.1000 -0.0510 0.0268  499 PHE A C   
3666 O O   . PHE A 501 ? 0.4593 0.4047 0.9600 -0.0994 -0.0793 0.0173  499 PHE A O   
3667 C CB  . PHE A 501 ? 0.4226 0.3817 0.7127 -0.0810 -0.0364 0.0166  499 PHE A CB  
3668 C CG  . PHE A 501 ? 0.4422 0.3891 0.7037 -0.0821 -0.0369 0.0170  499 PHE A CG  
3669 C CD1 . PHE A 501 ? 0.4874 0.4240 0.7063 -0.0663 -0.0680 -0.0075 499 PHE A CD1 
3670 C CD2 . PHE A 501 ? 0.4301 0.3764 0.7035 -0.0965 -0.0061 0.0416  499 PHE A CD2 
3671 C CE1 . PHE A 501 ? 0.4849 0.4116 0.6839 -0.0656 -0.0700 -0.0103 499 PHE A CE1 
3672 C CE2 . PHE A 501 ? 0.4647 0.3968 0.7148 -0.0968 -0.0107 0.0419  499 PHE A CE2 
3673 C CZ  . PHE A 501 ? 0.4943 0.4171 0.7118 -0.0817 -0.0433 0.0145  499 PHE A CZ  
3674 N N   . LEU A 502 ? 0.4589 0.4371 0.9601 -0.1141 -0.0071 0.0549  500 LEU A N   
3675 C CA  . LEU A 502 ? 0.5338 0.5153 1.1058 -0.1313 0.0144  0.0827  500 LEU A CA  
3676 C C   . LEU A 502 ? 0.4312 0.4120 1.1136 -0.1327 -0.0199 0.0744  500 LEU A C   
3677 O O   . LEU A 502 ? 0.4738 0.4460 1.1896 -0.1344 -0.0280 0.0841  500 LEU A O   
3678 C CB  . LEU A 502 ? 0.4307 0.4367 0.9993 -0.1379 0.0699  0.1111  500 LEU A CB  
3679 C CG  . LEU A 502 ? 0.5465 0.5494 1.0140 -0.1364 0.1039  0.1231  500 LEU A CG  
3680 C CD1 . LEU A 502 ? 0.4633 0.4895 0.9090 -0.1323 0.1484  0.1395  500 LEU A CD1 
3681 C CD2 . LEU A 502 ? 0.5084 0.4893 0.9417 -0.1403 0.0996  0.1339  500 LEU A CD2 
3682 N N   . THR A 503 ? 0.4311 0.4199 1.1597 -0.1254 -0.0446 0.0542  501 THR A N   
3683 C CA  . THR A 503 ? 0.4431 0.4307 1.2639 -0.1173 -0.0808 0.0424  501 THR A CA  
3684 C C   . THR A 503 ? 0.4661 0.4262 1.2906 -0.1075 -0.1345 0.0171  501 THR A C   
3685 O O   . THR A 503 ? 0.5434 0.4994 1.4442 -0.1010 -0.1594 0.0149  501 THR A O   
3686 C CB  . THR A 503 ? 0.5165 0.5127 1.3745 -0.1072 -0.1039 0.0212  501 THR A CB  
3687 O OG1 . THR A 503 ? 0.6826 0.6627 1.4755 -0.0990 -0.1398 -0.0087 501 THR A OG1 
3688 C CG2 . THR A 503 ? 0.5005 0.5258 1.3675 -0.1135 -0.0524 0.0427  501 THR A CG2 
3689 N N   . ARG A 504 ? 0.4565 0.3976 1.2016 -0.1039 -0.1534 -0.0036 502 ARG A N   
3690 C CA  . ARG A 504 ? 0.5056 0.4216 1.2383 -0.0878 -0.2066 -0.0365 502 ARG A CA  
3691 C C   . ARG A 504 ? 0.5419 0.4448 1.2326 -0.0939 -0.1931 -0.0259 502 ARG A C   
3692 O O   . ARG A 504 ? 0.6381 0.5217 1.3258 -0.0795 -0.2348 -0.0529 502 ARG A O   
3693 C CB  . ARG A 504 ? 0.5477 0.4572 1.1895 -0.0613 -0.2387 -0.0727 502 ARG A CB  
3694 C CG  . ARG A 504 ? 0.5275 0.4471 1.2027 -0.0562 -0.2514 -0.0800 502 ARG A CG  
3695 C CD  . ARG A 504 ? 0.5704 0.4831 1.1451 -0.0293 -0.2782 -0.1067 502 ARG A CD  
3696 N NE  . ARG A 504 ? 0.8270 0.7483 1.4331 -0.0272 -0.2852 -0.1069 502 ARG A NE  
3697 C CZ  . ARG A 504 ? 0.9486 0.8635 1.4840 -0.0060 -0.3093 -0.1231 502 ARG A CZ  
3698 N NH1 . ARG A 504 ? 0.9395 0.8407 1.3736 0.0178  -0.3332 -0.1435 502 ARG A NH1 
3699 N NH2 . ARG A 504 ? 0.9400 0.8627 1.5109 -0.0071 -0.3111 -0.1186 502 ARG A NH2 
3700 N N   . ASN A 505 ? 0.4631 0.3766 1.1157 -0.1097 -0.1374 0.0109  503 ASN A N   
3701 C CA  . ASN A 505 ? 0.5265 0.4268 1.1379 -0.1149 -0.1231 0.0251  503 ASN A CA  
3702 C C   . ASN A 505 ? 0.5374 0.4489 1.1887 -0.1332 -0.0784 0.0715  503 ASN A C   
3703 O O   . ASN A 505 ? 0.5721 0.4929 1.1677 -0.1415 -0.0313 0.0979  503 ASN A O   
3704 C CB  . ASN A 505 ? 0.4894 0.3929 0.9727 -0.1037 -0.1009 0.0197  503 ASN A CB  
3705 C CG  . ASN A 505 ? 0.5296 0.4299 0.9527 -0.0785 -0.1372 -0.0215 503 ASN A CG  
3706 O OD1 . ASN A 505 ? 0.5007 0.4086 0.9263 -0.0694 -0.1518 -0.0359 503 ASN A OD1 
3707 N ND2 . ASN A 505 ? 0.5208 0.4105 0.8899 -0.0656 -0.1521 -0.0400 503 ASN A ND2 
3708 N N   . PRO A 506 ? 0.5686 0.4821 1.3000 -0.1324 -0.0921 0.0808  504 PRO A N   
3709 C CA  . PRO A 506 ? 0.5330 0.4624 1.2905 -0.1438 -0.0483 0.1242  504 PRO A CA  
3710 C C   . PRO A 506 ? 0.6129 0.5319 1.3006 -0.1515 -0.0187 0.1498  504 PRO A C   
3711 O O   . PRO A 506 ? 0.6463 0.5798 1.3061 -0.1580 0.0276  0.1813  504 PRO A O   
3712 C CB  . PRO A 506 ? 0.5417 0.4691 1.4052 -0.1402 -0.0811 0.1249  504 PRO A CB  
3713 C CG  . PRO A 506 ? 0.5794 0.4829 1.4470 -0.1255 -0.1414 0.0831  504 PRO A CG  
3714 C CD  . PRO A 506 ? 0.5988 0.5002 1.3990 -0.1183 -0.1496 0.0517  504 PRO A CD  
3715 N N   . ALA A 507 ? 0.6309 0.5239 1.2869 -0.1480 -0.0469 0.1343  505 ALA A N   
3716 C CA  . ALA A 507 ? 0.5559 0.4349 1.1519 -0.1534 -0.0254 0.1576  505 ALA A CA  
3717 C C   . ALA A 507 ? 0.6489 0.5360 1.1514 -0.1553 0.0184  0.1699  505 ALA A C   
3718 O O   . ALA A 507 ? 0.6334 0.5097 1.0770 -0.1572 0.0381  0.1894  505 ALA A O   
3719 C CB  . ALA A 507 ? 0.6519 0.5016 1.2359 -0.1462 -0.0684 0.1317  505 ALA A CB  
3720 N N   . TRP A 508 ? 0.6645 0.5694 1.1533 -0.1527 0.0302  0.1575  506 TRP A N   
3721 C CA  . TRP A 508 ? 0.5632 0.4776 0.9680 -0.1504 0.0659  0.1633  506 TRP A CA  
3722 C C   . TRP A 508 ? 0.4911 0.4324 0.8917 -0.1507 0.1068  0.1835  506 TRP A C   
3723 O O   . TRP A 508 ? 0.6332 0.5844 0.9659 -0.1452 0.1337  0.1844  506 TRP A O   
3724 C CB  . TRP A 508 ? 0.5271 0.4455 0.9046 -0.1410 0.0480  0.1304  506 TRP A CB  
3725 C CG  . TRP A 508 ? 0.6106 0.5116 0.9419 -0.1276 0.0116  0.0993  506 TRP A CG  
3726 C CD1 . TRP A 508 ? 0.5753 0.4621 0.9507 -0.1217 -0.0333 0.0752  506 TRP A CD1 
3727 C CD2 . TRP A 508 ? 0.4935 0.3930 0.7309 -0.1161 0.0169  0.0862  506 TRP A CD2 
3728 N NE1 . TRP A 508 ? 0.4988 0.3780 0.8076 -0.1058 -0.0522 0.0481  506 TRP A NE1 
3729 C CE2 . TRP A 508 ? 0.5055 0.3934 0.7334 -0.1037 -0.0206 0.0564  506 TRP A CE2 
3730 C CE3 . TRP A 508 ? 0.5131 0.4205 0.6797 -0.1141 0.0481  0.0954  506 TRP A CE3 
3731 C CZ2 . TRP A 508 ? 0.5215 0.4099 0.6753 -0.0911 -0.0220 0.0395  506 TRP A CZ2 
3732 C CZ3 . TRP A 508 ? 0.5112 0.4151 0.6103 -0.1032 0.0417  0.0786  506 TRP A CZ3 
3733 C CH2 . TRP A 508 ? 0.4556 0.3522 0.5503 -0.0927 0.0096  0.0527  506 TRP A CH2 
3734 N N   . ARG A 509 ? 0.6065 0.5599 1.0810 -0.1551 0.1097  0.1977  507 ARG A N   
3735 C CA  . ARG A 509 ? 0.6995 0.6798 1.1780 -0.1547 0.1484  0.2158  507 ARG A CA  
3736 C C   . ARG A 509 ? 0.6019 0.5798 0.9970 -0.1533 0.1809  0.2371  507 ARG A C   
3737 O O   . ARG A 509 ? 0.7304 0.7297 1.1001 -0.1489 0.2137  0.2455  507 ARG A O   
3738 C CB  . ARG A 509 ? 0.5572 0.5495 1.1399 -0.1601 0.1446  0.2300  507 ARG A CB  
3739 C CG  . ARG A 509 ? 0.6681 0.6884 1.3050 -0.1567 0.1562  0.2231  507 ARG A CG  
3740 C CD  . ARG A 509 ? 0.6612 0.6967 1.3981 -0.1613 0.1627  0.2437  507 ARG A CD  
3741 N NE  . ARG A 509 ? 0.6746 0.7368 1.4608 -0.1569 0.1766  0.2368  507 ARG A NE  
3742 C CZ  . ARG A 509 ? 0.6881 0.7682 1.5682 -0.1591 0.1855  0.2516  507 ARG A CZ  
3743 N NH1 . ARG A 509 ? 0.7149 0.7902 1.6551 -0.1662 0.1817  0.2762  507 ARG A NH1 
3744 N NH2 . ARG A 509 ? 0.7680 0.8710 1.6887 -0.1539 0.1976  0.2420  507 ARG A NH2 
3745 N N   . LYS A 510 ? 0.5782 0.5293 0.9315 -0.1553 0.1688  0.2430  508 LYS A N   
3746 C CA  . LYS A 510 ? 0.6145 0.5552 0.8860 -0.1530 0.1891  0.2603  508 LYS A CA  
3747 C C   . LYS A 510 ? 0.7285 0.6609 0.9100 -0.1433 0.1879  0.2412  508 LYS A C   
3748 O O   . LYS A 510 ? 0.7760 0.6964 0.8872 -0.1391 0.1963  0.2502  508 LYS A O   
3749 C CB  . LYS A 510 ? 0.7948 0.7072 1.0808 -0.1600 0.1714  0.2779  508 LYS A CB  
3750 C CG  . LYS A 510 ? 0.7242 0.6139 1.0320 -0.1599 0.1305  0.2552  508 LYS A CG  
3751 C CD  . LYS A 510 ? 0.8745 0.7339 1.1928 -0.1638 0.1082  0.2679  508 LYS A CD  
3752 C CE  . LYS A 510 ? 0.9003 0.7399 1.1260 -0.1600 0.1230  0.2823  508 LYS A CE  
3753 N NZ  . LYS A 510 ? 0.9058 0.7120 1.1431 -0.1618 0.0943  0.2893  508 LYS A NZ  
3754 N N   . ALA A 511 ? 0.5460 0.4841 0.7315 -0.1391 0.1756  0.2160  509 ALA A N   
3755 C CA  . ALA A 511 ? 0.6788 0.6099 0.7900 -0.1299 0.1722  0.1987  509 ALA A CA  
3756 C C   . ALA A 511 ? 0.7344 0.6839 0.7893 -0.1195 0.1962  0.1977  509 ALA A C   
3757 O O   . ALA A 511 ? 0.5538 0.5265 0.6338 -0.1185 0.2173  0.2041  509 ALA A O   
3758 C CB  . ALA A 511 ? 0.4802 0.4136 0.6154 -0.1287 0.1555  0.1757  509 ALA A CB  
3759 N N   . VAL A 512 ? 0.5638 0.5040 0.5491 -0.1102 0.1909  0.1888  510 VAL A N   
3760 C CA  . VAL A 512 ? 0.5501 0.5061 0.4871 -0.0968 0.2049  0.1809  510 VAL A CA  
3761 C C   . VAL A 512 ? 0.5902 0.5544 0.5272 -0.0899 0.1974  0.1568  510 VAL A C   
3762 O O   . VAL A 512 ? 0.4809 0.4317 0.4097 -0.0902 0.1786  0.1453  510 VAL A O   
3763 C CB  . VAL A 512 ? 0.6739 0.6149 0.5451 -0.0882 0.1992  0.1842  510 VAL A CB  
3764 C CG1 . VAL A 512 ? 0.6683 0.6221 0.4943 -0.0711 0.2090  0.1703  510 VAL A CG1 
3765 C CG2 . VAL A 512 ? 0.6304 0.5600 0.4969 -0.0955 0.2079  0.2119  510 VAL A CG2 
3766 N N   . PHE A 513 ? 0.5080 0.4930 0.4559 -0.0835 0.2139  0.1503  511 PHE A N   
3767 C CA  . PHE A 513 ? 0.6118 0.6010 0.5574 -0.0768 0.2081  0.1299  511 PHE A CA  
3768 C C   . PHE A 513 ? 0.5792 0.5611 0.4643 -0.0624 0.2036  0.1175  511 PHE A C   
3769 O O   . PHE A 513 ? 0.5220 0.5090 0.3758 -0.0525 0.2174  0.1199  511 PHE A O   
3770 C CB  . PHE A 513 ? 0.4754 0.4871 0.4649 -0.0750 0.2271  0.1276  511 PHE A CB  
3771 C CG  . PHE A 513 ? 0.5039 0.5161 0.4984 -0.0703 0.2214  0.1095  511 PHE A CG  
3772 C CD1 . PHE A 513 ? 0.4566 0.4689 0.4124 -0.0563 0.2275  0.0962  511 PHE A CD1 
3773 C CD2 . PHE A 513 ? 0.4181 0.4281 0.4581 -0.0799 0.2096  0.1061  511 PHE A CD2 
3774 C CE1 . PHE A 513 ? 0.5664 0.5752 0.5307 -0.0539 0.2235  0.0823  511 PHE A CE1 
3775 C CE2 . PHE A 513 ? 0.4894 0.4986 0.5323 -0.0762 0.2001  0.0913  511 PHE A CE2 
3776 C CZ  . PHE A 513 ? 0.5467 0.5553 0.5537 -0.0641 0.2059  0.0803  511 PHE A CZ  
3777 N N   . ILE A 514 ? 0.4603 0.4294 0.3301 -0.0609 0.1848  0.1040  512 ILE A N   
3778 C CA  . ILE A 514 ? 0.4689 0.4269 0.2926 -0.0485 0.1776  0.0911  512 ILE A CA  
3779 C C   . ILE A 514 ? 0.6443 0.5995 0.4745 -0.0476 0.1718  0.0767  512 ILE A C   
3780 O O   . ILE A 514 ? 0.4580 0.4133 0.3127 -0.0573 0.1620  0.0766  512 ILE A O   
3781 C CB  . ILE A 514 ? 0.4710 0.4108 0.2682 -0.0488 0.1601  0.0925  512 ILE A CB  
3782 C CG1 . ILE A 514 ? 0.7860 0.7235 0.5783 -0.0522 0.1657  0.1111  512 ILE A CG1 
3783 C CG2 . ILE A 514 ? 0.4876 0.4118 0.2410 -0.0362 0.1530  0.0787  512 ILE A CG2 
3784 C CD1 . ILE A 514 ? 0.7396 0.6546 0.4999 -0.0493 0.1510  0.1127  512 ILE A CD1 
3785 N N   . SER A 515 ? 0.6561 0.6064 0.4611 -0.0355 0.1790  0.0648  513 SER A N   
3786 C CA  . SER A 515 ? 0.6572 0.6011 0.4693 -0.0351 0.1735  0.0526  513 SER A CA  
3787 C C   . SER A 515 ? 0.6321 0.5615 0.4103 -0.0197 0.1625  0.0360  513 SER A C   
3788 O O   . SER A 515 ? 0.6680 0.5898 0.4029 -0.0064 0.1722  0.0333  513 SER A O   
3789 C CB  . SER A 515 ? 0.6655 0.6288 0.5202 -0.0333 0.1834  0.0487  513 SER A CB  
3790 O OG  . SER A 515 ? 0.5744 0.5417 0.4145 -0.0151 0.1941  0.0342  513 SER A OG  
3791 N N   . PRO A 516 ? 0.4591 0.3832 0.2571 -0.0198 0.1402  0.0253  514 PRO A N   
3792 C CA  . PRO A 516 ? 0.4837 0.3923 0.2640 -0.0045 0.1233  0.0062  514 PRO A CA  
3793 C C   . PRO A 516 ? 0.6193 0.5334 0.4011 0.0145  0.1289  -0.0129 514 PRO A C   
3794 O O   . PRO A 516 ? 0.6329 0.5328 0.4023 0.0312  0.1106  -0.0344 514 PRO A O   
3795 C CB  . PRO A 516 ? 0.4633 0.3667 0.2805 -0.0155 0.0988  0.0081  514 PRO A CB  
3796 C CG  . PRO A 516 ? 0.4233 0.3395 0.2583 -0.0338 0.1060  0.0283  514 PRO A CG  
3797 C CD  . PRO A 516 ? 0.5301 0.4599 0.3676 -0.0332 0.1269  0.0320  514 PRO A CD  
3798 N N   . TYR A 517 ? 0.5630 0.4980 0.3659 0.0140  0.1510  -0.0085 515 TYR A N   
3799 C CA  . TYR A 517 ? 0.6231 0.5689 0.4379 0.0330  0.1574  -0.0290 515 TYR A CA  
3800 C C   . TYR A 517 ? 0.6489 0.6173 0.4469 0.0427  0.1964  -0.0240 515 TYR A C   
3801 O O   . TYR A 517 ? 0.6103 0.5946 0.4330 0.0270  0.2163  -0.0023 515 TYR A O   
3802 C CB  . TYR A 517 ? 0.4986 0.4509 0.3761 0.0246  0.1422  -0.0310 515 TYR A CB  
3803 C CG  . TYR A 517 ? 0.5979 0.5292 0.4940 0.0183  0.1068  -0.0333 515 TYR A CG  
3804 C CD1 . TYR A 517 ? 0.6014 0.5184 0.5059 0.0350  0.0835  -0.0577 515 TYR A CD1 
3805 C CD2 . TYR A 517 ? 0.5232 0.4502 0.4316 -0.0031 0.0971  -0.0110 515 TYR A CD2 
3806 C CE1 . TYR A 517 ? 0.6583 0.5568 0.5928 0.0271  0.0518  -0.0553 515 TYR A CE1 
3807 C CE2 . TYR A 517 ? 0.5808 0.4932 0.5110 -0.0096 0.0707  -0.0073 515 TYR A CE2 
3808 C CZ  . TYR A 517 ? 0.6216 0.5195 0.5695 0.0037  0.0484  -0.0272 515 TYR A CZ  
3809 O OH  . TYR A 517 ? 0.6765 0.5604 0.6586 -0.0049 0.0226  -0.0192 515 TYR A OH  
3810 N N   . ASN A 518 ? 0.6831 0.6540 0.4424 0.0701  0.2068  -0.0445 516 ASN A N   
3811 C CA  . ASN A 518 ? 0.6875 0.6848 0.4277 0.0830  0.2502  -0.0381 516 ASN A CA  
3812 C C   . ASN A 518 ? 0.6494 0.6784 0.4619 0.0753  0.2692  -0.0342 516 ASN A C   
3813 O O   . ASN A 518 ? 0.7869 0.8391 0.6174 0.0661  0.3035  -0.0107 516 ASN A O   
3814 C CB  . ASN A 518 ? 0.8730 0.8691 0.5550 0.1199  0.2552  -0.0671 516 ASN A CB  
3815 C CG  . ASN A 518 ? 1.0166 0.9980 0.6332 0.1226  0.2455  -0.0590 516 ASN A CG  
3816 O OD1 . ASN A 518 ? 1.0146 1.0109 0.6269 0.1072  0.2616  -0.0302 516 ASN A OD1 
3817 N ND2 . ASN A 518 ? 1.1112 1.0615 0.6849 0.1425  0.2136  -0.0856 516 ASN A ND2 
3818 N N   . SER A 519 ? 0.5995 0.6285 0.4607 0.0789  0.2450  -0.0562 517 SER A N   
3819 C CA  . SER A 519 ? 0.5814 0.6383 0.5155 0.0746  0.2568  -0.0568 517 SER A CA  
3820 C C   . SER A 519 ? 0.6198 0.6808 0.5969 0.0446  0.2576  -0.0271 517 SER A C   
3821 O O   . SER A 519 ? 0.5947 0.6837 0.6181 0.0392  0.2838  -0.0158 517 SER A O   
3822 C CB  . SER A 519 ? 0.6164 0.6644 0.5931 0.0833  0.2218  -0.0842 517 SER A CB  
3823 O OG  . SER A 519 ? 0.7865 0.8035 0.7659 0.0662  0.1827  -0.0767 517 SER A OG  
3824 N N   . GLN A 520 ? 0.5020 0.5371 0.4697 0.0264  0.2280  -0.0159 518 GLN A N   
3825 C CA  . GLN A 520 ? 0.5450 0.5823 0.5448 0.0027  0.2254  0.0074  518 GLN A CA  
3826 C C   . GLN A 520 ? 0.5651 0.6162 0.5541 -0.0027 0.2597  0.0286  518 GLN A C   
3827 O O   . GLN A 520 ? 0.5366 0.6047 0.5788 -0.0148 0.2708  0.0424  518 GLN A O   
3828 C CB  . GLN A 520 ? 0.5998 0.6104 0.5780 -0.0112 0.1940  0.0150  518 GLN A CB  
3829 C CG  . GLN A 520 ? 0.5921 0.6034 0.5933 -0.0308 0.1879  0.0337  518 GLN A CG  
3830 C CD  . GLN A 520 ? 0.3953 0.4094 0.4468 -0.0362 0.1650  0.0312  518 GLN A CD  
3831 O OE1 . GLN A 520 ? 0.4817 0.5088 0.5755 -0.0285 0.1663  0.0204  518 GLN A OE1 
3832 N NE2 . GLN A 520 ? 0.4643 0.4663 0.5092 -0.0471 0.1430  0.0402  518 GLN A NE2 
3833 N N   . ASN A 521 ? 0.5813 0.6226 0.5048 0.0062  0.2737  0.0327  519 ASN A N   
3834 C CA  . ASN A 521 ? 0.6361 0.6881 0.5513 -0.0009 0.2880  0.0557  519 ASN A CA  
3835 C C   . ASN A 521 ? 0.5583 0.6459 0.5155 0.0045  0.3166  0.0595  519 ASN A C   
3836 O O   . ASN A 521 ? 0.5577 0.6585 0.5539 -0.0099 0.3238  0.0801  519 ASN A O   
3837 C CB  . ASN A 521 ? 0.6738 0.7105 0.5150 0.0094  0.2811  0.0554  519 ASN A CB  
3838 C CG  . ASN A 521 ? 0.7022 0.7075 0.5141 0.0010  0.2521  0.0558  519 ASN A CG  
3839 O OD1 . ASN A 521 ? 0.7100 0.7081 0.5533 -0.0157 0.2382  0.0621  519 ASN A OD1 
3840 N ND2 . ASN A 521 ? 0.7600 0.7477 0.5131 0.0139  0.2420  0.0476  519 ASN A ND2 
3841 N N   . ALA A 522 ? 0.5806 0.6844 0.5365 0.0262  0.3324  0.0375  520 ALA A N   
3842 C CA  . ALA A 522 ? 0.6056 0.7484 0.6046 0.0332  0.3608  0.0385  520 ALA A CA  
3843 C C   . ALA A 522 ? 0.5638 0.7219 0.6584 0.0165  0.3614  0.0461  520 ALA A C   
3844 O O   . ALA A 522 ? 0.5761 0.7581 0.7167 0.0078  0.3774  0.0633  520 ALA A O   
3845 C CB  . ALA A 522 ? 0.6379 0.7954 0.6195 0.0636  0.3724  0.0060  520 ALA A CB  
3846 N N   . VAL A 523 ? 0.5187 0.6631 0.6488 0.0119  0.3431  0.0327  521 VAL A N   
3847 C CA  . VAL A 523 ? 0.4819 0.6381 0.7037 -0.0033 0.3308  0.0359  521 VAL A CA  
3848 C C   . VAL A 523 ? 0.5541 0.7006 0.7922 -0.0266 0.3224  0.0628  521 VAL A C   
3849 O O   . VAL A 523 ? 0.5766 0.7394 0.8904 -0.0370 0.3217  0.0711  521 VAL A O   
3850 C CB  . VAL A 523 ? 0.4797 0.6134 0.7120 -0.0029 0.2822  0.0144  521 VAL A CB  
3851 C CG1 . VAL A 523 ? 0.4228 0.5590 0.7319 -0.0179 0.2577  0.0186  521 VAL A CG1 
3852 C CG2 . VAL A 523 ? 0.5080 0.6518 0.7461 0.0204  0.2825  -0.0145 521 VAL A CG2 
3853 N N   . ALA A 524 ? 0.4993 0.6173 0.6696 -0.0331 0.3087  0.0730  522 ALA A N   
3854 C CA  . ALA A 524 ? 0.5606 0.6662 0.7450 -0.0517 0.2928  0.0922  522 ALA A CA  
3855 C C   . ALA A 524 ? 0.5328 0.6540 0.7292 -0.0547 0.3119  0.1120  522 ALA A C   
3856 O O   . ALA A 524 ? 0.7003 0.8239 0.9546 -0.0685 0.3057  0.1254  522 ALA A O   
3857 C CB  . ALA A 524 ? 0.4902 0.5635 0.6040 -0.0555 0.2716  0.0938  522 ALA A CB  
3858 N N   . SER A 525 ? 0.5369 0.6678 0.6806 -0.0416 0.3342  0.1142  523 SER A N   
3859 C CA  . SER A 525 ? 0.5817 0.7307 0.7357 -0.0445 0.3580  0.1357  523 SER A CA  
3860 C C   . SER A 525 ? 0.5805 0.7587 0.8299 -0.0495 0.3731  0.1405  523 SER A C   
3861 O O   . SER A 525 ? 0.5925 0.7747 0.8911 -0.0630 0.3766  0.1617  523 SER A O   
3862 C CB  . SER A 525 ? 0.6352 0.7952 0.7185 -0.0259 0.3811  0.1320  523 SER A CB  
3863 O OG  . SER A 525 ? 0.7093 0.8889 0.7997 -0.0289 0.4089  0.1553  523 SER A OG  
3864 N N   . LYS A 526 ? 0.6179 0.8159 0.9020 -0.0381 0.3799  0.1196  524 LYS A N   
3865 C CA  . LYS A 526 ? 0.5692 0.7977 0.9491 -0.0403 0.3930  0.1204  524 LYS A CA  
3866 C C   . LYS A 526 ? 0.5278 0.7440 0.9903 -0.0577 0.3631  0.1228  524 LYS A C   
3867 O O   . LYS A 526 ? 0.5410 0.7703 1.0773 -0.0669 0.3679  0.1368  524 LYS A O   
3868 C CB  . LYS A 526 ? 0.5672 0.8192 0.9632 -0.0209 0.4039  0.0927  524 LYS A CB  
3869 C CG  . LYS A 526 ? 0.6133 0.8767 0.9250 0.0011  0.4283  0.0833  524 LYS A CG  
3870 C CD  . LYS A 526 ? 0.8024 1.0795 1.1217 0.0239  0.4293  0.0483  524 LYS A CD  
3871 C CE  . LYS A 526 ? 0.8452 1.1245 1.0699 0.0486  0.4432  0.0330  524 LYS A CE  
3872 N NZ  . LYS A 526 ? 0.9269 1.2130 1.1571 0.0746  0.4382  -0.0064 524 LYS A NZ  
3873 N N   . ILE A 527 ? 0.4834 0.6748 0.9366 -0.0618 0.3308  0.1091  525 ILE A N   
3874 C CA  . ILE A 527 ? 0.4501 0.6328 0.9821 -0.0748 0.2976  0.1058  525 ILE A CA  
3875 C C   . ILE A 527 ? 0.5466 0.7087 1.0767 -0.0892 0.2824  0.1246  525 ILE A C   
3876 O O   . ILE A 527 ? 0.4553 0.6194 1.0653 -0.0977 0.2675  0.1297  525 ILE A O   
3877 C CB  . ILE A 527 ? 0.5154 0.6838 1.0422 -0.0738 0.2680  0.0844  525 ILE A CB  
3878 C CG1 . ILE A 527 ? 0.5518 0.7411 1.0970 -0.0585 0.2790  0.0633  525 ILE A CG1 
3879 C CG2 . ILE A 527 ? 0.4604 0.6181 1.0583 -0.0857 0.2258  0.0791  525 ILE A CG2 
3880 C CD1 . ILE A 527 ? 0.5069 0.6672 1.0136 -0.0527 0.2328  0.0419  525 ILE A CD1 
3881 N N   . LEU A 528 ? 0.4619 0.6030 0.9064 -0.0903 0.2835  0.1334  526 LEU A N   
3882 C CA  . LEU A 528 ? 0.5175 0.6365 0.9594 -0.1025 0.2646  0.1469  526 LEU A CA  
3883 C C   . LEU A 528 ? 0.5347 0.6589 0.9673 -0.1058 0.2883  0.1727  526 LEU A C   
3884 O O   . LEU A 528 ? 0.5174 0.6336 0.9981 -0.1165 0.2764  0.1865  526 LEU A O   
3885 C CB  . LEU A 528 ? 0.4646 0.5555 0.8265 -0.1026 0.2464  0.1399  526 LEU A CB  
3886 C CG  . LEU A 528 ? 0.4574 0.5404 0.8135 -0.1003 0.2260  0.1190  526 LEU A CG  
3887 C CD1 . LEU A 528 ? 0.4550 0.5121 0.7237 -0.0988 0.2164  0.1160  526 LEU A CD1 
3888 C CD2 . LEU A 528 ? 0.3850 0.4658 0.8244 -0.1094 0.1926  0.1102  526 LEU A CD2 
3889 N N   . GLY A 529 ? 0.6316 0.7683 1.0047 -0.0961 0.3193  0.1792  527 GLY A N   
3890 C CA  . GLY A 529 ? 0.5950 0.7383 0.9547 -0.0990 0.3437  0.2056  527 GLY A CA  
3891 C C   . GLY A 529 ? 0.6097 0.7253 0.8922 -0.1019 0.3342  0.2155  527 GLY A C   
3892 O O   . GLY A 529 ? 0.6719 0.7884 0.9400 -0.1055 0.3517  0.2399  527 GLY A O   
3893 N N   . LEU A 530 ? 0.6512 0.7427 0.8871 -0.1004 0.3075  0.1985  528 LEU A N   
3894 C CA  . LEU A 530 ? 0.6393 0.7037 0.8114 -0.1031 0.2943  0.2054  528 LEU A CA  
3895 C C   . LEU A 530 ? 0.6550 0.7205 0.7402 -0.0894 0.3098  0.2034  528 LEU A C   
3896 O O   . LEU A 530 ? 0.6178 0.6995 0.6837 -0.0758 0.3221  0.1877  528 LEU A O   
3897 C CB  . LEU A 530 ? 0.5375 0.5782 0.6970 -0.1058 0.2609  0.1875  528 LEU A CB  
3898 C CG  . LEU A 530 ? 0.6156 0.6539 0.8554 -0.1158 0.2392  0.1817  528 LEU A CG  
3899 C CD1 . LEU A 530 ? 0.4646 0.4845 0.6776 -0.1148 0.2132  0.1618  528 LEU A CD1 
3900 C CD2 . LEU A 530 ? 0.5229 0.5508 0.8116 -0.1277 0.2303  0.2006  528 LEU A CD2 
3901 N N   . PRO A 531 ? 0.6518 0.6991 0.6869 -0.0912 0.3074  0.2179  529 PRO A N   
3902 C CA  . PRO A 531 ? 0.7074 0.7506 0.6584 -0.0763 0.3131  0.2114  529 PRO A CA  
3903 C C   . PRO A 531 ? 0.6378 0.6701 0.5575 -0.0670 0.2898  0.1828  529 PRO A C   
3904 O O   . PRO A 531 ? 0.5920 0.6103 0.5335 -0.0750 0.2658  0.1746  529 PRO A O   
3905 C CB  . PRO A 531 ? 0.7197 0.7384 0.6357 -0.0831 0.3059  0.2329  529 PRO A CB  
3906 C CG  . PRO A 531 ? 0.6860 0.6886 0.6604 -0.1003 0.2851  0.2398  529 PRO A CG  
3907 C CD  . PRO A 531 ? 0.6663 0.6931 0.7217 -0.1057 0.2966  0.2396  529 PRO A CD  
3908 N N   . THR A 532 ? 0.6569 0.6951 0.5262 -0.0491 0.2976  0.1675  530 THR A N   
3909 C CA  . THR A 532 ? 0.6208 0.6494 0.4682 -0.0392 0.2787  0.1411  530 THR A CA  
3910 C C   . THR A 532 ? 0.6509 0.6618 0.4251 -0.0246 0.2689  0.1325  530 THR A C   
3911 O O   . THR A 532 ? 0.7077 0.7199 0.4411 -0.0165 0.2828  0.1421  530 THR A O   
3912 C CB  . THR A 532 ? 0.6110 0.6606 0.4819 -0.0284 0.2937  0.1238  530 THR A CB  
3913 O OG1 . THR A 532 ? 0.8413 0.9070 0.6766 -0.0112 0.3182  0.1205  530 THR A OG1 
3914 C CG2 . THR A 532 ? 0.5857 0.6534 0.5363 -0.0413 0.3029  0.1319  530 THR A CG2 
3915 N N   . GLN A 533 ? 0.6176 0.6106 0.3764 -0.0208 0.2449  0.1145  531 GLN A N   
3916 C CA  . GLN A 533 ? 0.6423 0.6142 0.3405 -0.0063 0.2306  0.1028  531 GLN A CA  
3917 C C   . GLN A 533 ? 0.7376 0.6957 0.4339 -0.0008 0.2126  0.0796  531 GLN A C   
3918 O O   . GLN A 533 ? 0.5599 0.5165 0.2941 -0.0141 0.2019  0.0797  531 GLN A O   
3919 C CB  . GLN A 533 ? 0.6486 0.6012 0.3312 -0.0146 0.2146  0.1182  531 GLN A CB  
3920 C CG  . GLN A 533 ? 0.7238 0.6528 0.3438 0.0015  0.2007  0.1092  531 GLN A CG  
3921 C CD  . GLN A 533 ? 0.7515 0.6776 0.3334 0.0056  0.2120  0.1292  531 GLN A CD  
3922 O OE1 . GLN A 533 ? 0.8242 0.7470 0.4223 -0.0090 0.2127  0.1535  531 GLN A OE1 
3923 N NE2 . GLN A 533 ? 0.8096 0.7350 0.3389 0.0263  0.2207  0.1195  531 GLN A NE2 
3924 N N   . THR A 534 ? 0.6396 0.5848 0.2892 0.0194  0.2082  0.0597  532 THR A N   
3925 C CA  . THR A 534 ? 0.7601 0.6831 0.4023 0.0238  0.1887  0.0399  532 THR A CA  
3926 C C   . THR A 534 ? 0.7798 0.6789 0.4057 0.0172  0.1653  0.0442  532 THR A C   
3927 O O   . THR A 534 ? 0.6898 0.5836 0.2916 0.0190  0.1623  0.0552  532 THR A O   
3928 C CB  . THR A 534 ? 0.8059 0.7168 0.4049 0.0509  0.1856  0.0121  532 THR A CB  
3929 O OG1 . THR A 534 ? 0.9134 0.8166 0.4602 0.0670  0.1809  0.0098  532 THR A OG1 
3930 C CG2 . THR A 534 ? 0.8003 0.7352 0.4217 0.0604  0.2085  0.0020  532 THR A CG2 
3931 N N   . VAL A 535 ? 0.6962 0.5799 0.3348 0.0094  0.1503  0.0362  533 VAL A N   
3932 C CA  . VAL A 535 ? 0.7446 0.6066 0.3706 0.0040  0.1295  0.0375  533 VAL A CA  
3933 C C   . VAL A 535 ? 0.7747 0.6109 0.3423 0.0247  0.1148  0.0258  533 VAL A C   
3934 O O   . VAL A 535 ? 0.6451 0.4720 0.1954 0.0248  0.1067  0.0356  533 VAL A O   
3935 C CB  . VAL A 535 ? 0.7392 0.6003 0.4033 -0.0067 0.1118  0.0283  533 VAL A CB  
3936 C CG1 . VAL A 535 ? 0.8055 0.6535 0.4712 -0.0119 0.0909  0.0280  533 VAL A CG1 
3937 C CG2 . VAL A 535 ? 0.6996 0.5829 0.4095 -0.0233 0.1241  0.0393  533 VAL A CG2 
3938 N N   . ASP A 536 ? 0.6644 0.4903 0.2081 0.0448  0.1056  0.0018  534 ASP A N   
3939 C CA  . ASP A 536 ? 0.7547 0.5535 0.2425 0.0694  0.0826  -0.0164 534 ASP A CA  
3940 C C   . ASP A 536 ? 0.7897 0.5988 0.2477 0.0764  0.0954  -0.0002 534 ASP A C   
3941 O O   . ASP A 536 ? 0.8360 0.6226 0.2575 0.0868  0.0754  -0.0019 534 ASP A O   
3942 C CB  . ASP A 536 ? 0.9079 0.7040 0.3981 0.0908  0.0656  -0.0490 534 ASP A CB  
3943 C CG  . ASP A 536 ? 1.0259 0.8303 0.5962 0.0746  0.0469  -0.0579 534 ASP A CG  
3944 O OD1 . ASP A 536 ? 0.8365 0.6636 0.4512 0.0542  0.0664  -0.0414 534 ASP A OD1 
3945 O OD2 . ASP A 536 ? 1.0871 0.8742 0.6777 0.0830  0.0110  -0.0801 534 ASP A OD2 
3946 N N   . SER A 537 ? 0.7553 0.5965 0.2312 0.0693  0.1269  0.0168  535 SER A N   
3947 C CA  . SER A 537 ? 0.8229 0.6733 0.2719 0.0724  0.1415  0.0363  535 SER A CA  
3948 C C   . SER A 537 ? 0.8261 0.6775 0.2990 0.0507  0.1437  0.0653  535 SER A C   
3949 O O   . SER A 537 ? 0.8250 0.6737 0.2701 0.0527  0.1494  0.0839  535 SER A O   
3950 C CB  . SER A 537 ? 0.8210 0.7041 0.2784 0.0753  0.1740  0.0411  535 SER A CB  
3951 O OG  . SER A 537 ? 0.8436 0.7517 0.3638 0.0529  0.1914  0.0554  535 SER A OG  
3952 N N   . SER A 538 ? 0.7160 0.5693 0.2373 0.0316  0.1379  0.0690  536 SER A N   
3953 C CA  . SER A 538 ? 0.6961 0.5486 0.2429 0.0140  0.1361  0.0914  536 SER A CA  
3954 C C   . SER A 538 ? 0.7162 0.5336 0.2302 0.0197  0.1101  0.0883  536 SER A C   
3955 O O   . SER A 538 ? 0.7150 0.5240 0.2389 0.0095  0.1059  0.1061  536 SER A O   
3956 C CB  . SER A 538 ? 0.6291 0.4970 0.2375 -0.0051 0.1379  0.0928  536 SER A CB  
3957 O OG  . SER A 538 ? 0.6018 0.4533 0.2117 -0.0056 0.1199  0.0751  536 SER A OG  
3958 N N   . GLN A 539 ? 0.7388 0.5323 0.2157 0.0367  0.0895  0.0647  537 GLN A N   
3959 C CA  . GLN A 539 ? 0.8335 0.5907 0.2849 0.0424  0.0586  0.0569  537 GLN A CA  
3960 C C   . GLN A 539 ? 0.8609 0.6028 0.2753 0.0496  0.0538  0.0747  537 GLN A C   
3961 O O   . GLN A 539 ? 0.8657 0.6124 0.2428 0.0638  0.0632  0.0792  537 GLN A O   
3962 C CB  . GLN A 539 ? 0.9018 0.6364 0.3246 0.0621  0.0315  0.0254  537 GLN A CB  
3963 C CG  . GLN A 539 ? 0.9339 0.6326 0.3447 0.0668  -0.0080 0.0119  537 GLN A CG  
3964 C CD  . GLN A 539 ? 0.9340 0.6300 0.3770 0.0754  -0.0378 -0.0211 537 GLN A CD  
3965 O OE1 . GLN A 539 ? 0.8115 0.5321 0.3191 0.0601  -0.0315 -0.0261 537 GLN A OE1 
3966 N NE2 . GLN A 539 ? 1.0120 0.6776 0.4142 0.1008  -0.0727 -0.0427 537 GLN A NE2 
3967 N N   . GLY A 540 ? 0.9168 0.6389 0.3396 0.0401  0.0393  0.0856  538 GLY A N   
3968 C CA  . GLY A 540 ? 0.9351 0.6376 0.3272 0.0448  0.0315  0.1059  538 GLY A CA  
3969 C C   . GLY A 540 ? 0.9535 0.6781 0.3731 0.0283  0.0584  0.1401  538 GLY A C   
3970 O O   . GLY A 540 ? 0.9020 0.6104 0.3009 0.0294  0.0532  0.1635  538 GLY A O   
3971 N N   . SER A 541 ? 0.8058 0.5655 0.2742 0.0136  0.0836  0.1443  539 SER A N   
3972 C CA  . SER A 541 ? 0.8008 0.5823 0.3071 -0.0033 0.1052  0.1744  539 SER A CA  
3973 C C   . SER A 541 ? 0.8061 0.5858 0.3689 -0.0210 0.0996  0.1755  539 SER A C   
3974 O O   . SER A 541 ? 0.6999 0.4769 0.2768 -0.0226 0.0900  0.1516  539 SER A O   
3975 C CB  . SER A 541 ? 0.7981 0.6172 0.3184 -0.0056 0.1341  0.1761  539 SER A CB  
3976 O OG  . SER A 541 ? 0.8708 0.6913 0.3414 0.0055  0.1466  0.1892  539 SER A OG  
3977 N N   . GLU A 542 ? 0.7521 0.5311 0.3467 -0.0349 0.1045  0.2038  540 GLU A N   
3978 C CA  . GLU A 542 ? 0.8681 0.6376 0.5136 -0.0498 0.0964  0.2042  540 GLU A CA  
3979 C C   . GLU A 542 ? 0.7756 0.5685 0.4768 -0.0673 0.1138  0.2265  540 GLU A C   
3980 O O   . GLU A 542 ? 0.7454 0.5470 0.4402 -0.0730 0.1270  0.2509  540 GLU A O   
3981 C CB  . GLU A 542 ? 0.8038 0.5272 0.4365 -0.0499 0.0694  0.2115  540 GLU A CB  
3982 C CG  . GLU A 542 ? 0.9188 0.6306 0.5587 -0.0535 0.0698  0.2500  540 GLU A CG  
3983 C CD  . GLU A 542 ? 1.0077 0.6701 0.6455 -0.0537 0.0362  0.2524  540 GLU A CD  
3984 O OE1 . GLU A 542 ? 0.8957 0.5362 0.5257 -0.0533 0.0102  0.2228  540 GLU A OE1 
3985 O OE2 . GLU A 542 ? 0.9780 0.6251 0.6259 -0.0548 0.0331  0.2845  540 GLU A OE2 
3986 N N   . TYR A 543 ? 0.6563 0.4531 0.4065 -0.0782 0.1119  0.2155  541 TYR A N   
3987 C CA  . TYR A 543 ? 0.6493 0.4609 0.4539 -0.0961 0.1231  0.2283  541 TYR A CA  
3988 C C   . TYR A 543 ? 0.6834 0.4741 0.5389 -0.1062 0.1080  0.2214  541 TYR A C   
3989 O O   . TYR A 543 ? 0.6341 0.4160 0.4804 -0.1003 0.0927  0.1949  541 TYR A O   
3990 C CB  . TYR A 543 ? 0.6230 0.4718 0.4379 -0.0945 0.1426  0.2138  541 TYR A CB  
3991 C CG  . TYR A 543 ? 0.6443 0.5108 0.4096 -0.0797 0.1556  0.2085  541 TYR A CG  
3992 C CD1 . TYR A 543 ? 0.6978 0.5708 0.4436 -0.0805 0.1744  0.2282  541 TYR A CD1 
3993 C CD2 . TYR A 543 ? 0.6192 0.4909 0.3568 -0.0647 0.1499  0.1819  541 TYR A CD2 
3994 C CE1 . TYR A 543 ? 0.7260 0.6115 0.4233 -0.0643 0.1866  0.2204  541 TYR A CE1 
3995 C CE2 . TYR A 543 ? 0.6799 0.5604 0.3747 -0.0502 0.1587  0.1735  541 TYR A CE2 
3996 C CZ  . TYR A 543 ? 0.6990 0.5867 0.3719 -0.0487 0.1770  0.1918  541 TYR A CZ  
3997 O OH  . TYR A 543 ? 0.7765 0.6699 0.4017 -0.0312 0.1863  0.1808  541 TYR A OH  
3998 N N   . ASP A 544 ? 0.6354 0.4206 0.5467 -0.1189 0.1092  0.2345  542 ASP A N   
3999 C CA  . ASP A 544 ? 0.6437 0.4219 0.6288 -0.1256 0.0838  0.2268  542 ASP A CA  
4000 C C   . ASP A 544 ? 0.5995 0.4047 0.6022 -0.1223 0.0798  0.1933  542 ASP A C   
4001 O O   . ASP A 544 ? 0.5449 0.3516 0.5432 -0.1139 0.0539  0.1593  542 ASP A O   
4002 C CB  . ASP A 544 ? 0.6310 0.4076 0.6829 -0.1363 0.0812  0.2435  542 ASP A CB  
4003 C CG  . ASP A 544 ? 0.7688 0.5139 0.8190 -0.1373 0.0668  0.2638  542 ASP A CG  
4004 O OD1 . ASP A 544 ? 0.8446 0.5666 0.8507 -0.1294 0.0511  0.2604  542 ASP A OD1 
4005 O OD2 . ASP A 544 ? 0.8013 0.5454 0.8972 -0.1456 0.0696  0.2844  542 ASP A OD2 
4006 N N   . TYR A 545 ? 0.5451 0.3737 0.5648 -0.1267 0.1057  0.2011  543 TYR A N   
4007 C CA  . TYR A 545 ? 0.5682 0.4205 0.6045 -0.1231 0.1008  0.1724  543 TYR A CA  
4008 C C   . TYR A 545 ? 0.5106 0.3801 0.4962 -0.1166 0.1294  0.1715  543 TYR A C   
4009 O O   . TYR A 545 ? 0.5372 0.4202 0.5043 -0.1152 0.1456  0.1834  543 TYR A O   
4010 C CB  . TYR A 545 ? 0.5885 0.4514 0.7105 -0.1333 0.0960  0.1771  543 TYR A CB  
4011 C CG  . TYR A 545 ? 0.5844 0.4308 0.7648 -0.1357 0.0565  0.1650  543 TYR A CG  
4012 C CD1 . TYR A 545 ? 0.4822 0.3315 0.6644 -0.1242 0.0230  0.1247  543 TYR A CD1 
4013 C CD2 . TYR A 545 ? 0.5422 0.3710 0.7742 -0.1467 0.0517  0.1925  543 TYR A CD2 
4014 C CE1 . TYR A 545 ? 0.4919 0.3260 0.7258 -0.1216 -0.0165 0.1072  543 TYR A CE1 
4015 C CE2 . TYR A 545 ? 0.6553 0.4656 0.9511 -0.1483 0.0104  0.1793  543 TYR A CE2 
4016 C CZ  . TYR A 545 ? 0.6140 0.4274 0.9087 -0.1339 -0.0251 0.1327  543 TYR A CZ  
4017 O OH  . TYR A 545 ? 0.6653 0.4609 1.0191 -0.1301 -0.0696 0.1120  543 TYR A OH  
4018 N N   . VAL A 546 ? 0.5220 0.4014 0.4810 -0.1080 0.1191  0.1430  544 VAL A N   
4019 C CA  . VAL A 546 ? 0.6035 0.4964 0.5226 -0.1008 0.1376  0.1371  544 VAL A CA  
4020 C C   . VAL A 546 ? 0.5099 0.4214 0.4554 -0.0998 0.1292  0.1179  544 VAL A C   
4021 O O   . VAL A 546 ? 0.5762 0.4878 0.5344 -0.0978 0.1046  0.1001  544 VAL A O   
4022 C CB  . VAL A 546 ? 0.6482 0.5327 0.5094 -0.0900 0.1287  0.1247  544 VAL A CB  
4023 C CG1 . VAL A 546 ? 0.5987 0.5036 0.4440 -0.0799 0.1307  0.1089  544 VAL A CG1 
4024 C CG2 . VAL A 546 ? 0.4950 0.3703 0.3290 -0.0842 0.1298  0.1397  544 VAL A CG2 
4025 N N   . ILE A 547 ? 0.4343 0.3615 0.3860 -0.0987 0.1484  0.1208  545 ILE A N   
4026 C CA  . ILE A 547 ? 0.5089 0.4508 0.4804 -0.0962 0.1390  0.1046  545 ILE A CA  
4027 C C   . ILE A 547 ? 0.5469 0.4928 0.4767 -0.0881 0.1486  0.0978  545 ILE A C   
4028 O O   . ILE A 547 ? 0.4117 0.3677 0.3318 -0.0810 0.1604  0.1015  545 ILE A O   
4029 C CB  . ILE A 547 ? 0.5094 0.4661 0.5455 -0.1020 0.1462  0.1111  545 ILE A CB  
4030 C CG1 . ILE A 547 ? 0.4058 0.3560 0.4965 -0.1098 0.1274  0.1139  545 ILE A CG1 
4031 C CG2 . ILE A 547 ? 0.4722 0.4410 0.5210 -0.0969 0.1355  0.0950  545 ILE A CG2 
4032 C CD1 . ILE A 547 ? 0.5223 0.4870 0.6933 -0.1168 0.1310  0.1208  545 ILE A CD1 
4033 N N   . PHE A 548 ? 0.3838 0.3300 0.2962 -0.0841 0.1317  0.0838  546 PHE A N   
4034 C CA  . PHE A 548 ? 0.3817 0.3282 0.2642 -0.0778 0.1351  0.0784  546 PHE A CA  
4035 C C   . PHE A 548 ? 0.5376 0.4937 0.4374 -0.0763 0.1249  0.0717  546 PHE A C   
4036 O O   . PHE A 548 ? 0.3816 0.3404 0.2875 -0.0769 0.1086  0.0679  546 PHE A O   
4037 C CB  . PHE A 548 ? 0.3798 0.3190 0.2319 -0.0731 0.1223  0.0730  546 PHE A CB  
4038 C CG  . PHE A 548 ? 0.4860 0.4260 0.3246 -0.0672 0.1181  0.0668  546 PHE A CG  
4039 C CD1 . PHE A 548 ? 0.3917 0.3244 0.2119 -0.0601 0.1234  0.0640  546 PHE A CD1 
4040 C CD2 . PHE A 548 ? 0.3783 0.3226 0.2185 -0.0698 0.1102  0.0655  546 PHE A CD2 
4041 C CE1 . PHE A 548 ? 0.5170 0.4399 0.3229 -0.0581 0.1213  0.0581  546 PHE A CE1 
4042 C CE2 . PHE A 548 ? 0.3938 0.3345 0.2285 -0.0687 0.1082  0.0648  546 PHE A CE2 
4043 C CZ  . PHE A 548 ? 0.4701 0.3999 0.2940 -0.0628 0.1106  0.0592  546 PHE A CZ  
4044 N N   . THR A 549 ? 0.5551 0.5155 0.4604 -0.0721 0.1328  0.0697  547 THR A N   
4045 C CA  . THR A 549 ? 0.3858 0.3510 0.3074 -0.0700 0.1209  0.0657  547 THR A CA  
4046 C C   . THR A 549 ? 0.4384 0.3965 0.3399 -0.0652 0.1185  0.0626  547 THR A C   
4047 O O   . THR A 549 ? 0.3784 0.3337 0.2719 -0.0586 0.1287  0.0568  547 THR A O   
4048 C CB  . THR A 549 ? 0.4481 0.4245 0.4119 -0.0682 0.1270  0.0632  547 THR A CB  
4049 O OG1 . THR A 549 ? 0.4230 0.4037 0.3836 -0.0627 0.1498  0.0618  547 THR A OG1 
4050 C CG2 . THR A 549 ? 0.4199 0.4027 0.4195 -0.0738 0.1230  0.0657  547 THR A CG2 
4051 N N   . GLN A 550 ? 0.3616 0.3174 0.2562 -0.0673 0.1045  0.0667  548 GLN A N   
4052 C CA  . GLN A 550 ? 0.3657 0.3140 0.2556 -0.0650 0.0992  0.0661  548 GLN A CA  
4053 C C   . GLN A 550 ? 0.3722 0.3183 0.2865 -0.0591 0.0950  0.0596  548 GLN A C   
4054 O O   . GLN A 550 ? 0.4722 0.4093 0.3876 -0.0534 0.0900  0.0519  548 GLN A O   
4055 C CB  . GLN A 550 ? 0.3633 0.3141 0.2499 -0.0699 0.0897  0.0782  548 GLN A CB  
4056 C CG  . GLN A 550 ? 0.3662 0.3107 0.2543 -0.0707 0.0861  0.0798  548 GLN A CG  
4057 C CD  . GLN A 550 ? 0.5063 0.4597 0.3971 -0.0763 0.0842  0.0967  548 GLN A CD  
4058 O OE1 . GLN A 550 ? 0.3714 0.3344 0.2523 -0.0769 0.0848  0.1065  548 GLN A OE1 
4059 N NE2 . GLN A 550 ? 0.3688 0.3204 0.2738 -0.0788 0.0818  0.1002  548 GLN A NE2 
4060 N N   . THR A 551 ? 0.3701 0.3235 0.3088 -0.0586 0.0933  0.0595  549 THR A N   
4061 C CA  . THR A 551 ? 0.3769 0.3311 0.3466 -0.0511 0.0893  0.0500  549 THR A CA  
4062 C C   . THR A 551 ? 0.4122 0.3558 0.3991 -0.0515 0.0681  0.0559  549 THR A C   
4063 O O   . THR A 551 ? 0.4649 0.4084 0.4810 -0.0499 0.0554  0.0576  549 THR A O   
4064 C CB  . THR A 551 ? 0.4599 0.4147 0.4209 -0.0400 0.1042  0.0340  549 THR A CB  
4065 O OG1 . THR A 551 ? 0.3920 0.3541 0.3320 -0.0417 0.1253  0.0370  549 THR A OG1 
4066 C CG2 . THR A 551 ? 0.4465 0.4099 0.4437 -0.0293 0.1056  0.0201  549 THR A CG2 
4067 N N   . THR A 552 ? 0.4178 0.3516 0.3941 -0.0538 0.0621  0.0608  550 THR A N   
4068 C CA  . THR A 552 ? 0.4925 0.4154 0.4956 -0.0561 0.0424  0.0712  550 THR A CA  
4069 C C   . THR A 552 ? 0.4651 0.3869 0.4567 -0.0657 0.0421  0.0902  550 THR A C   
4070 O O   . THR A 552 ? 0.4661 0.3944 0.4296 -0.0681 0.0549  0.0892  550 THR A O   
4071 C CB  . THR A 552 ? 0.5661 0.4773 0.5958 -0.0452 0.0305  0.0512  550 THR A CB  
4072 O OG1 . THR A 552 ? 0.5807 0.4883 0.5863 -0.0391 0.0373  0.0359  550 THR A OG1 
4073 C CG2 . THR A 552 ? 0.5428 0.4601 0.5910 -0.0334 0.0327  0.0320  550 THR A CG2 
4074 N N   . GLU A 553 ? 0.5636 0.4781 0.5833 -0.0712 0.0277  0.1093  551 GLU A N   
4075 C CA  . GLU A 553 ? 0.6540 0.5706 0.6799 -0.0807 0.0291  0.1310  551 GLU A CA  
4076 C C   . GLU A 553 ? 0.5839 0.4847 0.6563 -0.0798 0.0111  0.1241  551 GLU A C   
4077 O O   . GLU A 553 ? 0.7127 0.6040 0.8277 -0.0851 -0.0047 0.1428  551 GLU A O   
4078 C CB  . GLU A 553 ? 0.6220 0.5448 0.6457 -0.0883 0.0293  0.1662  551 GLU A CB  
4079 C CG  . GLU A 553 ? 0.6644 0.5909 0.6602 -0.0834 0.0283  0.1672  551 GLU A CG  
4080 C CD  . GLU A 553 ? 0.8258 0.7555 0.8072 -0.0868 0.0260  0.2024  551 GLU A CD  
4081 O OE1 . GLU A 553 ? 0.7985 0.7352 0.7847 -0.0942 0.0351  0.2286  551 GLU A OE1 
4082 O OE2 . GLU A 553 ? 0.8816 0.8077 0.8477 -0.0810 0.0152  0.2048  551 GLU A OE2 
4083 N N   . THR A 554 ? 0.5596 0.4550 0.6244 -0.0714 0.0102  0.0967  552 THR A N   
4084 C CA  . THR A 554 ? 0.5472 0.4249 0.6524 -0.0656 -0.0127 0.0810  552 THR A CA  
4085 C C   . THR A 554 ? 0.5373 0.4161 0.6387 -0.0676 -0.0110 0.0768  552 THR A C   
4086 O O   . THR A 554 ? 0.5093 0.4020 0.5725 -0.0713 0.0090  0.0817  552 THR A O   
4087 C CB  . THR A 554 ? 0.5305 0.3973 0.6272 -0.0460 -0.0222 0.0439  552 THR A CB  
4088 O OG1 . THR A 554 ? 0.5177 0.3922 0.5582 -0.0377 -0.0023 0.0269  552 THR A OG1 
4089 C CG2 . THR A 554 ? 0.5359 0.4040 0.6462 -0.0426 -0.0248 0.0442  552 THR A CG2 
4090 N N   . ALA A 555 ? 0.4795 0.3414 0.6261 -0.0633 -0.0367 0.0642  553 ALA A N   
4091 C CA  . ALA A 555 ? 0.5331 0.3930 0.6841 -0.0627 -0.0419 0.0554  553 ALA A CA  
4092 C C   . ALA A 555 ? 0.4986 0.3558 0.5820 -0.0476 -0.0330 0.0276  553 ALA A C   
4093 O O   . ALA A 555 ? 0.4842 0.3473 0.5470 -0.0500 -0.0248 0.0285  553 ALA A O   
4094 C CB  . ALA A 555 ? 0.5619 0.4003 0.7810 -0.0580 -0.0787 0.0417  553 ALA A CB  
4095 N N   . HIS A 556 ? 0.5297 0.3793 0.5803 -0.0314 -0.0336 0.0045  554 HIS A N   
4096 C CA  . HIS A 556 ? 0.5997 0.4489 0.5832 -0.0176 -0.0194 -0.0141 554 HIS A CA  
4097 C C   . HIS A 556 ? 0.5487 0.4176 0.4968 -0.0301 0.0115  0.0072  554 HIS A C   
4098 O O   . HIS A 556 ? 0.5610 0.4298 0.4727 -0.0287 0.0199  0.0052  554 HIS A O   
4099 C CB  . HIS A 556 ? 0.6116 0.4551 0.5747 0.0029  -0.0209 -0.0395 554 HIS A CB  
4100 C CG  . HIS A 556 ? 0.6237 0.4711 0.5180 0.0165  0.0012  -0.0508 554 HIS A CG  
4101 N ND1 . HIS A 556 ? 0.6315 0.4630 0.4829 0.0371  -0.0092 -0.0742 554 HIS A ND1 
4102 C CD2 . HIS A 556 ? 0.6879 0.5528 0.5523 0.0132  0.0323  -0.0398 554 HIS A CD2 
4103 C CE1 . HIS A 556 ? 0.6596 0.4993 0.4528 0.0450  0.0183  -0.0726 554 HIS A CE1 
4104 N NE2 . HIS A 556 ? 0.6410 0.5019 0.4475 0.0295  0.0441  -0.0517 554 HIS A NE2 
4105 N N   . SER A 557 ? 0.4986 0.3818 0.4593 -0.0412 0.0242  0.0265  555 SER A N   
4106 C CA  . SER A 557 ? 0.5685 0.4681 0.4997 -0.0499 0.0474  0.0414  555 SER A CA  
4107 C C   . SER A 557 ? 0.4709 0.3807 0.4053 -0.0619 0.0522  0.0588  555 SER A C   
4108 O O   . SER A 557 ? 0.4181 0.3378 0.3242 -0.0649 0.0666  0.0631  555 SER A O   
4109 C CB  . SER A 557 ? 0.4391 0.3485 0.3822 -0.0542 0.0534  0.0522  555 SER A CB  
4110 O OG  . SER A 557 ? 0.6509 0.5632 0.6261 -0.0645 0.0450  0.0737  555 SER A OG  
4111 N N   . CYS A 558 ? 0.5441 0.4537 0.5188 -0.0684 0.0410  0.0693  556 CYS A N   
4112 C CA  . CYS A 558 ? 0.5528 0.4787 0.5373 -0.0785 0.0502  0.0871  556 CYS A CA  
4113 C C   . CYS A 558 ? 0.5196 0.4398 0.5193 -0.0760 0.0401  0.0755  556 CYS A C   
4114 O O   . CYS A 558 ? 0.3896 0.3265 0.4060 -0.0830 0.0486  0.0877  556 CYS A O   
4115 C CB  . CYS A 558 ? 0.4969 0.4334 0.5225 -0.0894 0.0511  0.1159  556 CYS A CB  
4116 S SG  . CYS A 558 ? 0.5270 0.4696 0.5348 -0.0918 0.0584  0.1347  556 CYS A SG  
4117 N N   . ASN A 559 ? 0.4466 0.3445 0.4399 -0.0640 0.0214  0.0509  557 ASN A N   
4118 C CA  . ASN A 559 ? 0.4605 0.3484 0.4643 -0.0586 0.0055  0.0365  557 ASN A CA  
4119 C C   . ASN A 559 ? 0.4373 0.3367 0.4103 -0.0607 0.0204  0.0390  557 ASN A C   
4120 O O   . ASN A 559 ? 0.4820 0.3815 0.4054 -0.0577 0.0341  0.0373  557 ASN A O   
4121 C CB  . ASN A 559 ? 0.5322 0.3922 0.5084 -0.0394 -0.0161 0.0068  557 ASN A CB  
4122 C CG  . ASN A 559 ? 0.5796 0.4232 0.5688 -0.0305 -0.0423 -0.0113 557 ASN A CG  
4123 O OD1 . ASN A 559 ? 0.5611 0.3967 0.5051 -0.0225 -0.0421 -0.0204 557 ASN A OD1 
4124 N ND2 . ASN A 559 ? 0.5170 0.3531 0.5732 -0.0315 -0.0685 -0.0163 557 ASN A ND2 
4125 N N   . VAL A 560 ? 0.4342 0.3439 0.4450 -0.0658 0.0167  0.0428  558 VAL A N   
4126 C CA  . VAL A 560 ? 0.4135 0.3371 0.4031 -0.0669 0.0302  0.0439  558 VAL A CA  
4127 C C   . VAL A 560 ? 0.4657 0.3649 0.4097 -0.0545 0.0169  0.0236  558 VAL A C   
4128 O O   . VAL A 560 ? 0.4414 0.3438 0.3507 -0.0538 0.0278  0.0244  558 VAL A O   
4129 C CB  . VAL A 560 ? 0.4024 0.3491 0.4503 -0.0740 0.0330  0.0526  558 VAL A CB  
4130 C CG1 . VAL A 560 ? 0.3699 0.3457 0.4489 -0.0860 0.0553  0.0812  558 VAL A CG1 
4131 C CG2 . VAL A 560 ? 0.4343 0.3641 0.5329 -0.0699 0.0032  0.0383  558 VAL A CG2 
4132 N N   . ASN A 561 ? 0.5206 0.3934 0.4631 -0.0429 -0.0091 0.0056  559 ASN A N   
4133 C CA  . ASN A 561 ? 0.5543 0.4015 0.4415 -0.0286 -0.0213 -0.0097 559 ASN A CA  
4134 C C   . ASN A 561 ? 0.5429 0.3863 0.3703 -0.0255 -0.0014 -0.0040 559 ASN A C   
4135 O O   . ASN A 561 ? 0.5763 0.4146 0.3652 -0.0240 0.0067  0.0002  559 ASN A O   
4136 C CB  . ASN A 561 ? 0.5675 0.3860 0.4574 -0.0121 -0.0561 -0.0327 559 ASN A CB  
4137 C CG  . ASN A 561 ? 0.5960 0.4162 0.5545 -0.0145 -0.0804 -0.0401 559 ASN A CG  
4138 O OD1 . ASN A 561 ? 0.6618 0.5088 0.6858 -0.0302 -0.0693 -0.0253 559 ASN A OD1 
4139 N ND2 . ASN A 561 ? 0.5753 0.3675 0.5202 0.0020  -0.1136 -0.0618 559 ASN A ND2 
4140 N N   . ARG A 562 ? 0.5396 0.3864 0.3676 -0.0253 0.0063  -0.0024 560 ARG A N   
4141 C CA  . ARG A 562 ? 0.4751 0.3238 0.2611 -0.0232 0.0275  0.0034  560 ARG A CA  
4142 C C   . ARG A 562 ? 0.4963 0.3648 0.2837 -0.0371 0.0494  0.0212  560 ARG A C   
4143 O O   . ARG A 562 ? 0.4504 0.3158 0.2052 -0.0360 0.0617  0.0267  560 ARG A O   
4144 C CB  . ARG A 562 ? 0.5031 0.3546 0.3040 -0.0198 0.0283  -0.0011 560 ARG A CB  
4145 C CG  . ARG A 562 ? 0.5999 0.4589 0.3726 -0.0176 0.0513  0.0039  560 ARG A CG  
4146 C CD  . ARG A 562 ? 0.6786 0.5351 0.4626 -0.0068 0.0456  -0.0097 560 ARG A CD  
4147 N NE  . ARG A 562 ? 0.6961 0.5311 0.4506 0.0156  0.0270  -0.0338 560 ARG A NE  
4148 C CZ  . ARG A 562 ? 0.6013 0.4220 0.3856 0.0241  -0.0033 -0.0523 560 ARG A CZ  
4149 N NH1 . ARG A 562 ? 0.6031 0.4294 0.4522 0.0089  -0.0159 -0.0437 560 ARG A NH1 
4150 N NH2 . ARG A 562 ? 0.6729 0.4726 0.4218 0.0495  -0.0228 -0.0791 560 ARG A NH2 
4151 N N   . PHE A 563 ? 0.4126 0.3015 0.2386 -0.0490 0.0539  0.0309  561 PHE A N   
4152 C CA  . PHE A 563 ? 0.3937 0.2998 0.2166 -0.0572 0.0692  0.0418  561 PHE A CA  
4153 C C   . PHE A 563 ? 0.3997 0.2999 0.2077 -0.0552 0.0654  0.0379  561 PHE A C   
4154 O O   . PHE A 563 ? 0.3973 0.2998 0.1915 -0.0574 0.0732  0.0420  561 PHE A O   
4155 C CB  . PHE A 563 ? 0.3744 0.3039 0.2306 -0.0657 0.0749  0.0528  561 PHE A CB  
4156 C CG  . PHE A 563 ? 0.4256 0.3714 0.2713 -0.0693 0.0874  0.0602  561 PHE A CG  
4157 C CD1 . PHE A 563 ? 0.5497 0.4921 0.3810 -0.0693 0.0926  0.0618  561 PHE A CD1 
4158 C CD2 . PHE A 563 ? 0.5399 0.5056 0.3932 -0.0703 0.0927  0.0631  561 PHE A CD2 
4159 C CE1 . PHE A 563 ? 0.7180 0.6729 0.5456 -0.0702 0.0967  0.0647  561 PHE A CE1 
4160 C CE2 . PHE A 563 ? 0.3579 0.3362 0.1968 -0.0689 0.0988  0.0646  561 PHE A CE2 
4161 C CZ  . PHE A 563 ? 0.3579 0.3287 0.1849 -0.0691 0.0981  0.0649  561 PHE A CZ  
4162 N N   . ASN A 564 ? 0.4088 0.3007 0.2279 -0.0508 0.0498  0.0291  562 ASN A N   
4163 C CA  . ASN A 564 ? 0.4179 0.3014 0.2278 -0.0474 0.0413  0.0238  562 ASN A CA  
4164 C C   . ASN A 564 ? 0.4785 0.3374 0.2420 -0.0416 0.0405  0.0264  562 ASN A C   
4165 O O   . ASN A 564 ? 0.4467 0.3039 0.2018 -0.0443 0.0444  0.0321  562 ASN A O   
4166 C CB  . ASN A 564 ? 0.4489 0.3261 0.2861 -0.0424 0.0206  0.0123  562 ASN A CB  
4167 C CG  . ASN A 564 ? 0.5179 0.3790 0.3442 -0.0358 0.0047  0.0043  562 ASN A CG  
4168 O OD1 . ASN A 564 ? 0.5087 0.3786 0.3364 -0.0385 0.0106  0.0062  562 ASN A OD1 
4169 N ND2 . ASN A 564 ? 0.5369 0.3723 0.3551 -0.0252 -0.0203 -0.0070 562 ASN A ND2 
4170 N N   . VAL A 565 ? 0.4739 0.3138 0.2083 -0.0322 0.0352  0.0229  563 VAL A N   
4171 C CA  . VAL A 565 ? 0.5153 0.3350 0.1996 -0.0249 0.0406  0.0304  563 VAL A CA  
4172 C C   . VAL A 565 ? 0.5223 0.3560 0.2084 -0.0347 0.0650  0.0463  563 VAL A C   
4173 O O   . VAL A 565 ? 0.5104 0.3369 0.1876 -0.0381 0.0690  0.0583  563 VAL A O   
4174 C CB  . VAL A 565 ? 0.5831 0.3867 0.2317 -0.0090 0.0349  0.0211  563 VAL A CB  
4175 C CG1 . VAL A 565 ? 0.5909 0.3826 0.1844 -0.0008 0.0518  0.0343  563 VAL A CG1 
4176 C CG2 . VAL A 565 ? 0.6099 0.3926 0.2562 0.0035  0.0027  0.0030  563 VAL A CG2 
4177 N N   . ALA A 566 ? 0.6703 0.5232 0.3768 -0.0397 0.0780  0.0466  564 ALA A N   
4178 C CA  . ALA A 566 ? 0.6928 0.5604 0.4117 -0.0475 0.0967  0.0583  564 ALA A CA  
4179 C C   . ALA A 566 ? 0.6824 0.5548 0.4213 -0.0561 0.0946  0.0646  564 ALA A C   
4180 O O   . ALA A 566 ? 0.4541 0.3260 0.1990 -0.0577 0.0999  0.0756  564 ALA A O   
4181 C CB  . ALA A 566 ? 0.5165 0.4027 0.2622 -0.0515 0.1020  0.0548  564 ALA A CB  
4182 N N   . ILE A 567 ? 0.4232 0.3049 0.1815 -0.0595 0.0850  0.0564  565 ILE A N   
4183 C CA  . ILE A 567 ? 0.4954 0.3834 0.2726 -0.0637 0.0803  0.0556  565 ILE A CA  
4184 C C   . ILE A 567 ? 0.4444 0.3130 0.2148 -0.0611 0.0674  0.0557  565 ILE A C   
4185 O O   . ILE A 567 ? 0.4758 0.3419 0.2632 -0.0640 0.0615  0.0569  565 ILE A O   
4186 C CB  . ILE A 567 ? 0.3909 0.3018 0.1872 -0.0635 0.0774  0.0456  565 ILE A CB  
4187 C CG1 . ILE A 567 ? 0.4249 0.3382 0.2257 -0.0593 0.0695  0.0373  565 ILE A CG1 
4188 C CG2 . ILE A 567 ? 0.4622 0.3880 0.2640 -0.0662 0.0872  0.0501  565 ILE A CG2 
4189 C CD1 . ILE A 567 ? 0.3750 0.3170 0.1948 -0.0585 0.0742  0.0328  565 ILE A CD1 
4190 N N   . THR A 568 ? 0.5288 0.3809 0.2785 -0.0546 0.0582  0.0531  566 THR A N   
4191 C CA  . THR A 568 ? 0.5144 0.3440 0.2560 -0.0507 0.0414  0.0538  566 THR A CA  
4192 C C   . THR A 568 ? 0.5974 0.4034 0.3098 -0.0509 0.0475  0.0750  566 THR A C   
4193 O O   . THR A 568 ? 0.5495 0.3297 0.2421 -0.0458 0.0331  0.0812  566 THR A O   
4194 C CB  . THR A 568 ? 0.4885 0.3081 0.2222 -0.0417 0.0242  0.0413  566 THR A CB  
4195 O OG1 . THR A 568 ? 0.5073 0.3191 0.2123 -0.0360 0.0284  0.0422  566 THR A OG1 
4196 C CG2 . THR A 568 ? 0.5439 0.3903 0.3179 -0.0426 0.0208  0.0249  566 THR A CG2 
4197 N N   . ARG A 569 ? 0.6166 0.4319 0.3280 -0.0562 0.0693  0.0883  567 ARG A N   
4198 C CA  . ARG A 569 ? 0.5622 0.3627 0.2525 -0.0574 0.0833  0.1137  567 ARG A CA  
4199 C C   . ARG A 569 ? 0.5503 0.3492 0.2819 -0.0689 0.0820  0.1278  567 ARG A C   
4200 O O   . ARG A 569 ? 0.5878 0.3707 0.3125 -0.0717 0.0892  0.1542  567 ARG A O   
4201 C CB  . ARG A 569 ? 0.6738 0.5065 0.3755 -0.0525 0.1026  0.1145  567 ARG A CB  
4202 C CG  . ARG A 569 ? 0.7069 0.5424 0.3784 -0.0394 0.1014  0.0988  567 ARG A CG  
4203 C CD  . ARG A 569 ? 0.6837 0.4896 0.3013 -0.0262 0.0887  0.0986  567 ARG A CD  
4204 N NE  . ARG A 569 ? 0.6224 0.4020 0.2243 -0.0261 0.0663  0.0846  567 ARG A NE  
4205 C CZ  . ARG A 569 ? 0.7330 0.4865 0.3048 -0.0148 0.0430  0.0797  567 ARG A CZ  
4206 N NH1 . ARG A 569 ? 0.6881 0.4210 0.2133 -0.0043 0.0432  0.0950  567 ARG A NH1 
4207 N NH2 . ARG A 569 ? 0.6107 0.3641 0.2098 -0.0134 0.0185  0.0593  567 ARG A NH2 
4208 N N   . ALA A 570 ? 0.5129 0.3279 0.2883 -0.0739 0.0714  0.1112  568 ALA A N   
4209 C CA  . ALA A 570 ? 0.5214 0.3362 0.3453 -0.0827 0.0649  0.1177  568 ALA A CA  
4210 C C   . ALA A 570 ? 0.5460 0.3397 0.3848 -0.0809 0.0377  0.1136  568 ALA A C   
4211 O O   . ALA A 570 ? 0.5791 0.3731 0.4095 -0.0725 0.0209  0.0917  568 ALA A O   
4212 C CB  . ALA A 570 ? 0.5236 0.3639 0.3808 -0.0839 0.0617  0.0973  568 ALA A CB  
4213 N N   . LYS A 571 ? 0.5521 0.3288 0.4223 -0.0890 0.0329  0.1351  569 LYS A N   
4214 C CA  . LYS A 571 ? 0.6272 0.3799 0.5225 -0.0880 0.0031  0.1332  569 LYS A CA  
4215 C C   . LYS A 571 ? 0.5509 0.3113 0.5099 -0.0895 -0.0189 0.1129  569 LYS A C   
4216 O O   . LYS A 571 ? 0.6042 0.3541 0.5844 -0.0823 -0.0485 0.0926  569 LYS A O   
4217 C CB  . LYS A 571 ? 0.6204 0.3429 0.5120 -0.0955 0.0072  0.1748  569 LYS A CB  
4218 C CG  . LYS A 571 ? 0.7114 0.4187 0.5292 -0.0881 0.0212  0.1931  569 LYS A CG  
4219 C CD  . LYS A 571 ? 0.8150 0.4891 0.6233 -0.0930 0.0216  0.2368  569 LYS A CD  
4220 C CE  . LYS A 571 ? 0.8087 0.4982 0.6440 -0.1015 0.0571  0.2667  569 LYS A CE  
4221 N NZ  . LYS A 571 ? 0.8430 0.5063 0.6931 -0.1053 0.0547  0.2949  569 LYS A NZ  
4222 N N   . VAL A 572 ? 0.5655 0.3433 0.5568 -0.0964 -0.0081 0.1147  570 VAL A N   
4223 C CA  . VAL A 572 ? 0.5534 0.3356 0.6060 -0.0954 -0.0338 0.0936  570 VAL A CA  
4224 C C   . VAL A 572 ? 0.5566 0.3691 0.6004 -0.0874 -0.0301 0.0651  570 VAL A C   
4225 O O   . VAL A 572 ? 0.5578 0.3797 0.6038 -0.0738 -0.0516 0.0309  570 VAL A O   
4226 C CB  . VAL A 572 ? 0.5455 0.3158 0.6624 -0.1108 -0.0334 0.1234  570 VAL A CB  
4227 C CG1 . VAL A 572 ? 0.5704 0.3431 0.7565 -0.1074 -0.0672 0.0959  570 VAL A CG1 
4228 C CG2 . VAL A 572 ? 0.5867 0.3245 0.7112 -0.1188 -0.0375 0.1578  570 VAL A CG2 
4229 N N   . GLY A 573 ? 0.5167 0.3452 0.5490 -0.0938 -0.0031 0.0790  571 GLY A N   
4230 C CA  . GLY A 573 ? 0.4633 0.3163 0.4903 -0.0871 -0.0024 0.0571  571 GLY A CA  
4231 C C   . GLY A 573 ? 0.4439 0.3122 0.4307 -0.0896 0.0287  0.0689  571 GLY A C   
4232 O O   . GLY A 573 ? 0.5497 0.4123 0.5228 -0.0970 0.0518  0.0944  571 GLY A O   
4233 N N   . ILE A 574 ? 0.4827 0.3702 0.4498 -0.0814 0.0280  0.0498  572 ILE A N   
4234 C CA  . ILE A 574 ? 0.4967 0.3978 0.4351 -0.0827 0.0511  0.0575  572 ILE A CA  
4235 C C   . ILE A 574 ? 0.4928 0.4106 0.4394 -0.0771 0.0427  0.0427  572 ILE A C   
4236 O O   . ILE A 574 ? 0.5298 0.4521 0.4762 -0.0668 0.0217  0.0219  572 ILE A O   
4237 C CB  . ILE A 574 ? 0.5702 0.4723 0.4603 -0.0779 0.0605  0.0556  572 ILE A CB  
4238 C CG1 . ILE A 574 ? 0.6076 0.5192 0.4776 -0.0792 0.0803  0.0636  572 ILE A CG1 
4239 C CG2 . ILE A 574 ? 0.4967 0.4099 0.3745 -0.0672 0.0464  0.0336  572 ILE A CG2 
4240 C CD1 . ILE A 574 ? 0.5795 0.4853 0.4135 -0.0760 0.0878  0.0655  572 ILE A CD1 
4241 N N   . LEU A 575 ? 0.4432 0.3695 0.3954 -0.0815 0.0577  0.0527  573 LEU A N   
4242 C CA  . LEU A 575 ? 0.4291 0.3683 0.3834 -0.0760 0.0500  0.0428  573 LEU A CA  
4243 C C   . LEU A 575 ? 0.5236 0.4704 0.4451 -0.0759 0.0684  0.0504  573 LEU A C   
4244 O O   . LEU A 575 ? 0.3732 0.3184 0.2968 -0.0814 0.0875  0.0629  573 LEU A O   
4245 C CB  . LEU A 575 ? 0.4000 0.3411 0.4103 -0.0810 0.0440  0.0456  573 LEU A CB  
4246 C CG  . LEU A 575 ? 0.4879 0.4395 0.5017 -0.0755 0.0363  0.0386  573 LEU A CG  
4247 C CD1 . LEU A 575 ? 0.5128 0.4657 0.4992 -0.0609 0.0095  0.0185  573 LEU A CD1 
4248 C CD2 . LEU A 575 ? 0.4150 0.3701 0.4960 -0.0816 0.0330  0.0423  573 LEU A CD2 
4249 N N   . CYS A 576 ? 0.3920 0.3469 0.2835 -0.0685 0.0630  0.0434  574 CYS A N   
4250 C CA  . CYS A 576 ? 0.3878 0.3475 0.2581 -0.0693 0.0761  0.0518  574 CYS A CA  
4251 C C   . CYS A 576 ? 0.5036 0.4708 0.3771 -0.0654 0.0678  0.0522  574 CYS A C   
4252 O O   . CYS A 576 ? 0.3839 0.3573 0.2390 -0.0571 0.0555  0.0467  574 CYS A O   
4253 C CB  . CYS A 576 ? 0.4809 0.4439 0.3221 -0.0663 0.0797  0.0511  574 CYS A CB  
4254 S SG  . CYS A 576 ? 0.5473 0.4967 0.3824 -0.0697 0.0863  0.0520  574 CYS A SG  
4255 N N   . ILE A 577 ? 0.4201 0.3866 0.3146 -0.0692 0.0740  0.0581  575 ILE A N   
4256 C CA  . ILE A 577 ? 0.4955 0.4656 0.3957 -0.0656 0.0640  0.0602  575 ILE A CA  
4257 C C   . ILE A 577 ? 0.5018 0.4720 0.3809 -0.0664 0.0719  0.0703  575 ILE A C   
4258 O O   . ILE A 577 ? 0.5024 0.4688 0.3897 -0.0696 0.0831  0.0724  575 ILE A O   
4259 C CB  . ILE A 577 ? 0.4253 0.3964 0.3698 -0.0681 0.0648  0.0590  575 ILE A CB  
4260 C CG1 . ILE A 577 ? 0.4445 0.4161 0.4255 -0.0709 0.0609  0.0531  575 ILE A CG1 
4261 C CG2 . ILE A 577 ? 0.3829 0.3544 0.3362 -0.0627 0.0474  0.0595  575 ILE A CG2 
4262 C CD1 . ILE A 577 ? 0.4580 0.4272 0.4404 -0.0637 0.0330  0.0413  575 ILE A CD1 
4263 N N   . MET A 578 ? 0.4685 0.4434 0.3222 -0.0622 0.0657  0.0767  576 MET A N   
4264 C CA  . MET A 578 ? 0.5373 0.5141 0.3803 -0.0649 0.0734  0.0904  576 MET A CA  
4265 C C   . MET A 578 ? 0.4652 0.4385 0.3180 -0.0649 0.0653  0.1041  576 MET A C   
4266 O O   . MET A 578 ? 0.5199 0.4922 0.3694 -0.0594 0.0512  0.1058  576 MET A O   
4267 C CB  . MET A 578 ? 0.4358 0.4246 0.2500 -0.0610 0.0782  0.0946  576 MET A CB  
4268 C CG  . MET A 578 ? 0.5171 0.5067 0.3287 -0.0614 0.0844  0.0814  576 MET A CG  
4269 S SD  . MET A 578 ? 0.4849 0.4647 0.3132 -0.0695 0.0940  0.0832  576 MET A SD  
4270 C CE  . MET A 578 ? 0.5138 0.4799 0.3516 -0.0709 0.0944  0.0719  576 MET A CE  
4271 N N   . SER A 579 ? 0.4103 0.3789 0.2785 -0.0701 0.0699  0.1127  577 SER A N   
4272 C CA  . SER A 579 ? 0.6400 0.6022 0.5247 -0.0713 0.0601  0.1285  577 SER A CA  
4273 C C   . SER A 579 ? 0.4480 0.4152 0.3293 -0.0759 0.0654  0.1524  577 SER A C   
4274 O O   . SER A 579 ? 0.7051 0.6673 0.5967 -0.0775 0.0568  0.1735  577 SER A O   
4275 C CB  . SER A 579 ? 0.4024 0.3536 0.3225 -0.0720 0.0564  0.1175  577 SER A CB  
4276 O OG  . SER A 579 ? 0.5000 0.4497 0.4362 -0.0674 0.0495  0.1058  577 SER A OG  
4277 N N   . ASP A 580 ? 0.5611 0.5386 0.4331 -0.0782 0.0791  0.1516  578 ASP A N   
4278 C CA  . ASP A 580 ? 0.5119 0.4955 0.3955 -0.0807 0.0869  0.1672  578 ASP A CA  
4279 C C   . ASP A 580 ? 0.4420 0.4392 0.2917 -0.0719 0.0978  0.1649  578 ASP A C   
4280 O O   . ASP A 580 ? 0.4312 0.4346 0.2641 -0.0665 0.1030  0.1466  578 ASP A O   
4281 C CB  . ASP A 580 ? 0.6224 0.6038 0.5347 -0.0873 0.0898  0.1599  578 ASP A CB  
4282 C CG  . ASP A 580 ? 0.4720 0.4612 0.4125 -0.0919 0.0954  0.1740  578 ASP A CG  
4283 O OD1 . ASP A 580 ? 0.4866 0.4695 0.4612 -0.0977 0.0876  0.1929  578 ASP A OD1 
4284 O OD2 . ASP A 580 ? 0.4322 0.4346 0.3676 -0.0905 0.1064  0.1671  578 ASP A OD2 
4285 N N   . ARG A 581 ? 0.4826 0.4846 0.3236 -0.0703 0.1012  0.1846  579 ARG A N   
4286 C CA  . ARG A 581 ? 0.5061 0.5226 0.3082 -0.0609 0.1118  0.1830  579 ARG A CA  
4287 C C   . ARG A 581 ? 0.4942 0.5259 0.3081 -0.0625 0.1265  0.1715  579 ARG A C   
4288 O O   . ARG A 581 ? 0.5005 0.5437 0.2862 -0.0532 0.1316  0.1561  579 ARG A O   
4289 C CB  . ARG A 581 ? 0.5548 0.5739 0.3433 -0.0594 0.1152  0.2103  579 ARG A CB  
4290 C CG  . ARG A 581 ? 0.7166 0.7538 0.4608 -0.0486 0.1284  0.2100  579 ARG A CG  
4291 C CD  . ARG A 581 ? 0.8743 0.9130 0.5695 -0.0332 0.1182  0.1882  579 ARG A CD  
4292 N NE  . ARG A 581 ? 0.9522 0.9794 0.6102 -0.0238 0.1004  0.1981  579 ARG A NE  
4293 C CZ  . ARG A 581 ? 0.9159 0.9453 0.5300 -0.0078 0.0850  0.1816  579 ARG A CZ  
4294 N NH1 . ARG A 581 ? 0.8708 0.9145 0.4714 0.0014  0.0872  0.1547  579 ARG A NH1 
4295 N NH2 . ARG A 581 ? 0.9296 0.9467 0.5141 0.0014  0.0633  0.1915  579 ARG A NH2 
4296 N N   . ASP A 582 ? 0.5479 0.5822 0.4071 -0.0735 0.1310  0.1796  580 ASP A N   
4297 C CA  . ASP A 582 ? 0.4696 0.5224 0.3476 -0.0754 0.1437  0.1727  580 ASP A CA  
4298 C C   . ASP A 582 ? 0.5887 0.6381 0.4554 -0.0709 0.1397  0.1466  580 ASP A C   
4299 O O   . ASP A 582 ? 0.4871 0.5520 0.3359 -0.0629 0.1478  0.1344  580 ASP A O   
4300 C CB  . ASP A 582 ? 0.5688 0.6237 0.5066 -0.0879 0.1434  0.1879  580 ASP A CB  
4301 C CG  . ASP A 582 ? 0.7510 0.8292 0.7194 -0.0900 0.1560  0.1849  580 ASP A CG  
4302 O OD1 . ASP A 582 ? 0.8983 0.9961 0.8406 -0.0816 0.1696  0.1757  580 ASP A OD1 
4303 O OD2 . ASP A 582 ? 0.8091 0.8864 0.8333 -0.0992 0.1506  0.1916  580 ASP A OD2 
4304 N N   . LEU A 583 ? 0.4591 0.4896 0.3372 -0.0749 0.1277  0.1392  581 LEU A N   
4305 C CA  . LEU A 583 ? 0.4091 0.4356 0.2766 -0.0703 0.1247  0.1195  581 LEU A CA  
4306 C C   . LEU A 583 ? 0.4005 0.4292 0.2310 -0.0578 0.1222  0.1071  581 LEU A C   
4307 O O   . LEU A 583 ? 0.3950 0.4334 0.2159 -0.0524 0.1225  0.0930  581 LEU A O   
4308 C CB  . LEU A 583 ? 0.4024 0.4113 0.2829 -0.0765 0.1130  0.1161  581 LEU A CB  
4309 C CG  . LEU A 583 ? 0.3721 0.3758 0.2908 -0.0856 0.1085  0.1202  581 LEU A CG  
4310 C CD1 . LEU A 583 ? 0.5469 0.5234 0.4695 -0.0845 0.0930  0.1068  581 LEU A CD1 
4311 C CD2 . LEU A 583 ? 0.3638 0.3755 0.2928 -0.0834 0.1105  0.1086  581 LEU A CD2 
4312 N N   . TYR A 584 ? 0.6296 0.6535 0.4401 -0.0546 0.1171  0.1131  582 TYR A N   
4313 C CA  . TYR A 584 ? 0.5946 0.6249 0.3703 -0.0442 0.1105  0.1022  582 TYR A CA  
4314 C C   . TYR A 584 ? 0.4696 0.5195 0.2222 -0.0341 0.1189  0.0945  582 TYR A C   
4315 O O   . TYR A 584 ? 0.4586 0.5181 0.1949 -0.0251 0.1140  0.0756  582 TYR A O   
4316 C CB  . TYR A 584 ? 0.4507 0.4764 0.2086 -0.0425 0.1007  0.1136  582 TYR A CB  
4317 C CG  . TYR A 584 ? 0.5897 0.6267 0.3070 -0.0295 0.0892  0.1026  582 TYR A CG  
4318 C CD1 . TYR A 584 ? 0.4601 0.4832 0.1898 -0.0290 0.0715  0.0813  582 TYR A CD1 
4319 C CD2 . TYR A 584 ? 0.5176 0.5645 0.1982 -0.0149 0.0907  0.1035  582 TYR A CD2 
4320 C CE1 . TYR A 584 ? 0.4851 0.5077 0.1943 -0.0136 0.0522  0.0623  582 TYR A CE1 
4321 C CE2 . TYR A 584 ? 0.5470 0.6020 0.1871 0.0045  0.0745  0.0870  582 TYR A CE2 
4322 C CZ  . TYR A 584 ? 0.5296 0.5676 0.1903 0.0048  0.0514  0.0629  582 TYR A CZ  
4323 O OH  . TYR A 584 ? 0.5626 0.5979 0.1993 0.0246  0.0265  0.0388  582 TYR A OH  
4324 N N   . ASP A 585 ? 0.6818 0.7426 0.4352 -0.0351 0.1315  0.1087  583 ASP A N   
4325 C CA  . ASP A 585 ? 0.5306 0.6162 0.2631 -0.0230 0.1428  0.1016  583 ASP A CA  
4326 C C   . ASP A 585 ? 0.6733 0.7728 0.4271 -0.0216 0.1499  0.0859  583 ASP A C   
4327 O O   . ASP A 585 ? 0.7276 0.8453 0.4618 -0.0063 0.1517  0.0675  583 ASP A O   
4328 C CB  . ASP A 585 ? 0.6524 0.7517 0.3877 -0.0260 0.1594  0.1249  583 ASP A CB  
4329 C CG  . ASP A 585 ? 0.7317 0.8230 0.4307 -0.0207 0.1525  0.1396  583 ASP A CG  
4330 O OD1 . ASP A 585 ? 0.7431 0.8331 0.4006 -0.0059 0.1393  0.1255  583 ASP A OD1 
4331 O OD2 . ASP A 585 ? 0.7705 0.8577 0.4836 -0.0301 0.1580  0.1655  583 ASP A OD2 
4332 N N   . LYS A 586 ? 0.5579 0.6503 0.3510 -0.0350 0.1516  0.0915  584 LYS A N   
4333 C CA  . LYS A 586 ? 0.6137 0.7222 0.4287 -0.0339 0.1570  0.0800  584 LYS A CA  
4334 C C   . LYS A 586 ? 0.5533 0.6549 0.3508 -0.0283 0.1413  0.0566  584 LYS A C   
4335 O O   . LYS A 586 ? 0.6592 0.7650 0.4708 -0.0226 0.1377  0.0374  584 LYS A O   
4336 C CB  . LYS A 586 ? 0.5715 0.6758 0.4321 -0.0497 0.1587  0.0938  584 LYS A CB  
4337 C CG  . LYS A 586 ? 0.4228 0.5485 0.3197 -0.0557 0.1755  0.1134  584 LYS A CG  
4338 C CD  . LYS A 586 ? 0.4428 0.5593 0.3914 -0.0708 0.1699  0.1284  584 LYS A CD  
4339 C CE  . LYS A 586 ? 0.6361 0.7788 0.6404 -0.0770 0.1850  0.1462  584 LYS A CE  
4340 N NZ  . LYS A 586 ? 0.5891 0.7441 0.5754 -0.0750 0.1983  0.1611  584 LYS A NZ  
4341 N N   . LEU A 587 ? 0.4259 0.5041 0.2054 -0.0300 0.1258  0.0534  585 LEU A N   
4342 C CA  . LEU A 587 ? 0.6062 0.6631 0.3855 -0.0272 0.1060  0.0308  585 LEU A CA  
4343 C C   . LEU A 587 ? 0.5185 0.5903 0.2780 -0.0080 0.0990  0.0080  585 LEU A C   
4344 O O   . LEU A 587 ? 0.4927 0.5726 0.2227 0.0035  0.0954  0.0058  585 LEU A O   
4345 C CB  . LEU A 587 ? 0.4032 0.4365 0.1807 -0.0347 0.0945  0.0357  585 LEU A CB  
4346 C CG  . LEU A 587 ? 0.5570 0.5705 0.3531 -0.0493 0.0964  0.0481  585 LEU A CG  
4347 C CD1 . LEU A 587 ? 0.4682 0.4675 0.2655 -0.0531 0.0890  0.0514  585 LEU A CD1 
4348 C CD2 . LEU A 587 ? 0.5996 0.5972 0.4083 -0.0525 0.0913  0.0391  585 LEU A CD2 
4349 N N   . GLN A 588 ? 0.5100 0.5833 0.2851 -0.0020 0.0931  -0.0115 586 GLN A N   
4350 C CA  . GLN A 588 ? 0.4596 0.5456 0.2226 0.0192  0.0821  -0.0401 586 GLN A CA  
4351 C C   . GLN A 588 ? 0.5524 0.6096 0.3213 0.0206  0.0525  -0.0565 586 GLN A C   
4352 O O   . GLN A 588 ? 0.4855 0.5295 0.2765 0.0251  0.0333  -0.0767 586 GLN A O   
4353 C CB  . GLN A 588 ? 0.4572 0.5561 0.2448 0.0252  0.0854  -0.0553 586 GLN A CB  
4354 C CG  . GLN A 588 ? 0.5020 0.6290 0.3029 0.0199  0.1142  -0.0361 586 GLN A CG  
4355 C CD  . GLN A 588 ? 0.5623 0.7096 0.3942 0.0294  0.1182  -0.0540 586 GLN A CD  
4356 O OE1 . GLN A 588 ? 0.5873 0.7296 0.4251 0.0430  0.0994  -0.0834 586 GLN A OE1 
4357 N NE2 . GLN A 588 ? 0.4486 0.6185 0.3095 0.0221  0.1404  -0.0370 586 GLN A NE2 
4358 N N   . PHE A 589 ? 0.4751 0.5223 0.2319 0.0162  0.0472  -0.0460 587 PHE A N   
4359 C CA  . PHE A 589 ? 0.4665 0.4888 0.2416 0.0149  0.0207  -0.0568 587 PHE A CA  
4360 C C   . PHE A 589 ? 0.6001 0.6303 0.3478 0.0343  0.0045  -0.0726 587 PHE A C   
4361 O O   . PHE A 589 ? 0.5676 0.6202 0.2734 0.0462  0.0181  -0.0670 587 PHE A O   
4362 C CB  . PHE A 589 ? 0.5221 0.5241 0.3176 -0.0066 0.0250  -0.0331 587 PHE A CB  
4363 C CG  . PHE A 589 ? 0.5152 0.5054 0.3276 -0.0228 0.0380  -0.0178 587 PHE A CG  
4364 C CD1 . PHE A 589 ? 0.5174 0.5073 0.3368 -0.0202 0.0374  -0.0264 587 PHE A CD1 
4365 C CD2 . PHE A 589 ? 0.5075 0.4855 0.3279 -0.0379 0.0481  0.0027  587 PHE A CD2 
4366 C CE1 . PHE A 589 ? 0.5060 0.4811 0.3349 -0.0322 0.0444  -0.0133 587 PHE A CE1 
4367 C CE2 . PHE A 589 ? 0.5279 0.4934 0.3541 -0.0481 0.0574  0.0140  587 PHE A CE2 
4368 C CZ  . PHE A 589 ? 0.6291 0.5915 0.4572 -0.0452 0.0541  0.0066  587 PHE A CZ  
4369 N N   . THR A 590 ? 0.6097 0.6203 0.3834 0.0384  -0.0264 -0.0910 588 THR A N   
4370 C CA  . THR A 590 ? 0.5749 0.5864 0.3278 0.0580  -0.0508 -0.1094 588 THR A CA  
4371 C C   . THR A 590 ? 0.5562 0.5618 0.3061 0.0458  -0.0455 -0.0849 588 THR A C   
4372 O O   . THR A 590 ? 0.5133 0.5039 0.3045 0.0236  -0.0404 -0.0670 588 THR A O   
4373 C CB  . THR A 590 ? 0.5753 0.5654 0.3735 0.0653  -0.0910 -0.1387 588 THR A CB  
4374 O OG1 . THR A 590 ? 0.7384 0.7352 0.5343 0.0831  -0.1012 -0.1675 588 THR A OG1 
4375 C CG2 . THR A 590 ? 0.6026 0.5869 0.3911 0.0834  -0.1236 -0.1579 588 THR A CG2 
4376 N N   . SER A 591 ? 0.5736 0.5919 0.2732 0.0620  -0.0460 -0.0835 589 SER A N   
4377 C CA  . SER A 591 ? 0.5717 0.5829 0.2680 0.0534  -0.0460 -0.0619 589 SER A CA  
4378 C C   . SER A 591 ? 0.6275 0.6185 0.3586 0.0583  -0.0847 -0.0801 589 SER A C   
4379 O O   . SER A 591 ? 0.6775 0.6646 0.3994 0.0814  -0.1172 -0.1119 589 SER A O   
4380 C CB  . SER A 591 ? 0.6782 0.7078 0.3070 0.0688  -0.0332 -0.0479 589 SER A CB  
4381 O OG  . SER A 591 ? 0.8793 0.9170 0.4595 0.1011  -0.0542 -0.0757 589 SER A OG  
4382 N N   . LEU A 592 ? 0.5901 0.5692 0.3662 0.0382  -0.0828 -0.0625 590 LEU A N   
4383 C CA  . LEU A 592 ? 0.6205 0.5837 0.4429 0.0403  -0.1170 -0.0760 590 LEU A CA  
4384 C C   . LEU A 592 ? 0.8108 0.7734 0.6046 0.0473  -0.1249 -0.0649 590 LEU A C   
4385 O O   . LEU A 592 ? 0.8414 0.8127 0.5996 0.0410  -0.0984 -0.0387 590 LEU A O   
4386 C CB  . LEU A 592 ? 0.6440 0.5980 0.5456 0.0146  -0.1079 -0.0640 590 LEU A CB  
4387 C CG  . LEU A 592 ? 0.6323 0.5802 0.5720 0.0068  -0.1071 -0.0714 590 LEU A CG  
4388 C CD1 . LEU A 592 ? 0.6680 0.6084 0.6816 -0.0169 -0.0958 -0.0534 590 LEU A CD1 
4389 C CD2 . LEU A 592 ? 0.6231 0.5626 0.5734 0.0280  -0.1490 -0.1072 590 LEU A CD2 
4390 N N   . GLU A 593 ? 0.8194 0.7692 0.6343 0.0608  -0.1658 -0.0851 591 GLU A N   
4391 C CA  . GLU A 593 ? 0.8586 0.8033 0.6462 0.0709  -0.1821 -0.0773 591 GLU A CA  
4392 C C   . GLU A 593 ? 0.9949 0.9269 0.8669 0.0602  -0.2053 -0.0814 591 GLU A C   
4393 O O   . GLU A 593 ? 0.9736 0.8980 0.9130 0.0584  -0.2284 -0.1023 591 GLU A O   
4394 C CB  . GLU A 593 ? 0.8773 0.8195 0.5910 0.1067  -0.2154 -0.1004 591 GLU A CB  
4395 C CG  . GLU A 593 ? 1.1680 1.1066 0.8218 0.1194  -0.2228 -0.0818 591 GLU A CG  
4396 C CD  . GLU A 593 ? 1.1119 1.0674 0.7094 0.1101  -0.1758 -0.0430 591 GLU A CD  
4397 O OE1 . GLU A 593 ? 1.1357 1.1068 0.7382 0.0964  -0.1397 -0.0349 591 GLU A OE1 
4398 O OE2 . GLU A 593 ? 1.1141 1.0659 0.6678 0.1165  -0.1777 -0.0195 591 GLU A OE2 
4399 N N   . ILE A 594 ? 0.9988 0.9293 0.8746 0.0531  -0.1994 -0.0606 592 ILE A N   
4400 C CA  . ILE A 594 ? 1.0116 0.9344 0.9696 0.0450  -0.2195 -0.0642 592 ILE A CA  
4401 C C   . ILE A 594 ? 1.0122 0.9342 0.9564 0.0406  -0.2102 -0.0403 592 ILE A C   
4402 O O   . ILE A 594 ? 1.0696 0.9959 0.9470 0.0409  -0.1872 -0.0184 592 ILE A O   
4403 C CB  . ILE A 594 ? 0.9220 0.8519 0.9702 0.0205  -0.1970 -0.0610 592 ILE A CB  
4404 C CG1 . ILE A 594 ? 0.9359 0.8599 1.0823 0.0196  -0.2305 -0.0775 592 ILE A CG1 
4405 C CG2 . ILE A 594 ? 0.8961 0.8374 0.9501 -0.0003 -0.1508 -0.0322 592 ILE A CG2 
4406 C CD1 . ILE A 594 ? 0.8747 0.7835 1.0264 0.0425  -0.2856 -0.1117 592 ILE A CD1 
4407 N N   . VAL B 4   ? 1.2002 0.8383 1.2606 0.1125  0.4931  0.3908  2   VAL B N   
4408 C CA  . VAL B 4   ? 1.1584 0.8238 1.3405 0.0552  0.5112  0.3544  2   VAL B CA  
4409 C C   . VAL B 4   ? 1.1485 0.7614 1.3911 0.0258  0.5069  0.3391  2   VAL B C   
4410 O O   . VAL B 4   ? 1.1703 0.7188 1.3656 0.0453  0.5196  0.3694  2   VAL B O   
4411 C CB  . VAL B 4   ? 1.1163 0.8101 1.3172 0.0402  0.5667  0.3657  2   VAL B CB  
4412 C CG1 . VAL B 4   ? 1.0588 0.7963 1.3952 -0.0183 0.5771  0.3222  2   VAL B CG1 
4413 C CG2 . VAL B 4   ? 1.1377 0.8874 1.2700 0.0754  0.5708  0.3721  2   VAL B CG2 
4414 N N   . GLY B 5   ? 1.0132 0.6559 1.3558 -0.0179 0.4881  0.2895  3   GLY B N   
4415 C CA  . GLY B 5   ? 1.0102 0.6078 1.4026 -0.0447 0.4802  0.2654  3   GLY B CA  
4416 C C   . GLY B 5   ? 0.9327 0.5828 1.4287 -0.0905 0.4543  0.2043  3   GLY B C   
4417 O O   . GLY B 5   ? 0.9205 0.6431 1.4694 -0.1089 0.4562  0.1843  3   GLY B O   
4418 N N   . ALA B 6   ? 0.9293 0.5485 1.4501 -0.1043 0.4275  0.1720  4   ALA B N   
4419 C CA  . ALA B 6   ? 0.8790 0.5439 1.4865 -0.1446 0.3978  0.1100  4   ALA B CA  
4420 C C   . ALA B 6   ? 0.8799 0.5591 1.4699 -0.1301 0.3427  0.0790  4   ALA B C   
4421 O O   . ALA B 6   ? 0.9441 0.5749 1.4718 -0.0994 0.3313  0.0960  4   ALA B O   
4422 C CB  . ALA B 6   ? 0.9669 0.5846 1.6192 -0.1789 0.4151  0.0900  4   ALA B CB  
4423 N N   . CYS B 7   ? 0.7996 0.5500 1.4456 -0.1503 0.3080  0.0328  5   CYS B N   
4424 C CA  . CYS B 7   ? 0.8111 0.5774 1.4373 -0.1381 0.2562  0.0031  5   CYS B CA  
4425 C C   . CYS B 7   ? 0.7125 0.4374 1.3362 -0.1466 0.2397  -0.0298 5   CYS B C   
4426 O O   . CYS B 7   ? 0.7578 0.4801 1.4323 -0.1778 0.2476  -0.0589 5   CYS B O   
4427 C CB  . CYS B 7   ? 0.7710 0.6275 1.4507 -0.1516 0.2210  -0.0361 5   CYS B CB  
4428 S SG  . CYS B 7   ? 0.6470 0.5351 1.2835 -0.1334 0.1489  -0.0793 5   CYS B SG  
4429 N N   . VAL B 8   ? 0.8122 0.5071 1.3778 -0.1185 0.2180  -0.0273 6   VAL B N   
4430 C CA  . VAL B 8   ? 0.8502 0.5038 1.4057 -0.1199 0.2076  -0.0573 6   VAL B CA  
4431 C C   . VAL B 8   ? 0.8717 0.5690 1.4583 -0.1424 0.1671  -0.1203 6   VAL B C   
4432 O O   . VAL B 8   ? 0.8400 0.5053 1.4153 -0.1445 0.1579  -0.1523 6   VAL B O   
4433 C CB  . VAL B 8   ? 0.8163 0.4337 1.3043 -0.0778 0.2016  -0.0348 6   VAL B CB  
4434 C CG1 . VAL B 8   ? 0.8670 0.4490 1.3152 -0.0479 0.2333  0.0267  6   VAL B CG1 
4435 C CG2 . VAL B 8   ? 0.7643 0.4291 1.2304 -0.0644 0.1647  -0.0470 6   VAL B CG2 
4436 N N   . LEU B 9   ? 0.8045 0.5745 1.4260 -0.1555 0.1414  -0.1406 7   LEU B N   
4437 C CA  . LEU B 9   ? 0.7468 0.5667 1.3847 -0.1680 0.0949  -0.1985 7   LEU B CA  
4438 C C   . LEU B 9   ? 0.7753 0.6526 1.4916 -0.2008 0.0887  -0.2319 7   LEU B C   
4439 O O   . LEU B 9   ? 0.8092 0.7132 1.5395 -0.2139 0.0560  -0.2830 7   LEU B O   
4440 C CB  . LEU B 9   ? 0.6782 0.5467 1.2756 -0.1441 0.0557  -0.1974 7   LEU B CB  
4441 C CG  . LEU B 9   ? 0.7135 0.5515 1.2207 -0.1114 0.0451  -0.1833 7   LEU B CG  
4442 C CD1 . LEU B 9   ? 0.6360 0.5241 1.0866 -0.0874 0.0099  -0.1723 7   LEU B CD1 
4443 C CD2 . LEU B 9   ? 0.6799 0.4868 1.1771 -0.1183 0.0350  -0.2304 7   LEU B CD2 
4444 N N   . CYS B 10  ? 0.7232 0.6232 1.4883 -0.2125 0.1204  -0.2048 8   CYS B N   
4445 C CA  . CYS B 10  ? 0.6713 0.6374 1.5204 -0.2426 0.1191  -0.2339 8   CYS B CA  
4446 C C   . CYS B 10  ? 0.7277 0.6620 1.6152 -0.2641 0.1791  -0.2003 8   CYS B C   
4447 O O   . CYS B 10  ? 0.7697 0.7548 1.7335 -0.2940 0.1876  -0.2210 8   CYS B O   
4448 C CB  . CYS B 10  ? 0.6017 0.6666 1.4811 -0.2295 0.0857  -0.2448 8   CYS B CB  
4449 S SG  . CYS B 10  ? 0.7487 0.8261 1.6225 -0.2079 0.1215  -0.1868 8   CYS B SG  
4450 N N   . ASN B 11  ? 0.7987 0.6532 1.6319 -0.2474 0.2199  -0.1479 9   ASN B N   
4451 C CA  . ASN B 11  ? 0.8255 0.6335 1.6702 -0.2598 0.2792  -0.1066 9   ASN B CA  
4452 C C   . ASN B 11  ? 0.8423 0.7093 1.7180 -0.2598 0.3062  -0.0794 9   ASN B C   
4453 O O   . ASN B 11  ? 0.8711 0.6999 1.7360 -0.2614 0.3590  -0.0351 9   ASN B O   
4454 C CB  . ASN B 11  ? 0.9194 0.7026 1.8214 -0.3022 0.2941  -0.1367 9   ASN B CB  
4455 C CG  . ASN B 11  ? 1.0212 0.7097 1.8994 -0.3060 0.3521  -0.0892 9   ASN B CG  
4456 O OD1 . ASN B 11  ? 1.1205 0.7357 1.9224 -0.2721 0.3630  -0.0519 9   ASN B OD1 
4457 N ND2 . ASN B 11  ? 1.0980 0.7907 2.0399 -0.3447 0.3892  -0.0878 9   ASN B ND2 
4458 N N   . SER B 12  ? 0.7778 0.7383 1.6893 -0.2552 0.2717  -0.1060 10  SER B N   
4459 C CA  . SER B 12  ? 0.7618 0.7857 1.7008 -0.2481 0.2969  -0.0832 10  SER B CA  
4460 C C   . SER B 12  ? 0.7218 0.6879 1.5809 -0.2170 0.3376  -0.0192 10  SER B C   
4461 O O   . SER B 12  ? 0.7992 0.7122 1.5850 -0.1901 0.3225  0.0000  10  SER B O   
4462 C CB  . SER B 12  ? 0.6562 0.7789 1.6243 -0.2306 0.2461  -0.1166 10  SER B CB  
4463 O OG  . SER B 12  ? 0.6658 0.8380 1.6848 -0.2490 0.1977  -0.1749 10  SER B OG  
4464 N N   . GLN B 13  ? 0.7463 0.7269 1.6154 -0.2191 0.3887  0.0133  11  GLN B N   
4465 C CA  . GLN B 13  ? 0.7792 0.7053 1.5604 -0.1867 0.4300  0.0753  11  GLN B CA  
4466 C C   . GLN B 13  ? 0.7880 0.7498 1.5223 -0.1478 0.4075  0.0847  11  GLN B C   
4467 O O   . GLN B 13  ? 0.7554 0.8006 1.5391 -0.1449 0.3740  0.0481  11  GLN B O   
4468 C CB  . GLN B 13  ? 0.8578 0.7996 1.6573 -0.1981 0.4901  0.1035  11  GLN B CB  
4469 C CG  . GLN B 13  ? 0.9419 0.8090 1.6392 -0.1673 0.5370  0.1693  11  GLN B CG  
4470 C CD  . GLN B 13  ? 1.0714 0.9295 1.7904 -0.1905 0.5985  0.1951  11  GLN B CD  
4471 O OE1 . GLN B 13  ? 1.0638 0.9765 1.8828 -0.2335 0.6079  0.1631  11  GLN B OE1 
4472 N NE2 . GLN B 13  ? 1.1807 0.9732 1.8046 -0.1614 0.6393  0.2534  11  GLN B NE2 
4473 N N   . THR B 14  ? 0.8752 0.7748 1.5095 -0.1132 0.4222  0.1329  12  THR B N   
4474 C CA  . THR B 14  ? 0.6990 0.6221 1.2461 -0.0654 0.3752  0.1302  12  THR B CA  
4475 C C   . THR B 14  ? 0.8001 0.6737 1.2348 -0.0255 0.3999  0.1832  12  THR B C   
4476 O O   . THR B 14  ? 0.9101 0.7155 1.3187 -0.0271 0.4424  0.2262  12  THR B O   
4477 C CB  . THR B 14  ? 0.7108 0.6207 1.2368 -0.0592 0.3094  0.0993  12  THR B CB  
4478 O OG1 . THR B 14  ? 0.6037 0.5255 1.0455 -0.0192 0.2706  0.1010  12  THR B OG1 
4479 C CG2 . THR B 14  ? 0.7548 0.5814 1.2561 -0.0636 0.3182  0.1191  12  THR B CG2 
4480 N N   . SER B 15  ? 0.7331 0.6382 1.0975 0.0126  0.3702  0.1781  13  SER B N   
4481 C CA  . SER B 15  ? 0.8393 0.7121 1.0876 0.0555  0.3746  0.2152  13  SER B CA  
4482 C C   . SER B 15  ? 0.7903 0.6575 0.9798 0.0786  0.3085  0.1974  13  SER B C   
4483 O O   . SER B 15  ? 0.8633 0.7292 0.9644 0.1138  0.2935  0.2088  13  SER B O   
4484 C CB  . SER B 15  ? 0.8409 0.7549 1.0511 0.0793  0.4032  0.2208  13  SER B CB  
4485 O OG  . SER B 15  ? 0.8452 0.8100 1.0634 0.0904  0.3584  0.1751  13  SER B OG  
4486 N N   . LEU B 16  ? 0.7767 0.6452 1.0146 0.0577  0.2698  0.1669  14  LEU B N   
4487 C CA  . LEU B 16  ? 0.7531 0.6252 0.9517 0.0707  0.2132  0.1473  14  LEU B CA  
4488 C C   . LEU B 16  ? 0.7626 0.5985 0.9704 0.0644  0.2022  0.1529  14  LEU B C   
4489 O O   . LEU B 16  ? 0.7445 0.5570 1.0107 0.0397  0.2224  0.1493  14  LEU B O   
4490 C CB  . LEU B 16  ? 0.6972 0.6080 0.9321 0.0583  0.1764  0.1043  14  LEU B CB  
4491 C CG  . LEU B 16  ? 0.7652 0.7130 0.9998 0.0708  0.1836  0.0913  14  LEU B CG  
4492 C CD1 . LEU B 16  ? 0.6710 0.6468 0.9437 0.0645  0.1454  0.0535  14  LEU B CD1 
4493 C CD2 . LEU B 16  ? 0.8227 0.7617 0.9663 0.1035  0.1772  0.1010  14  LEU B CD2 
4494 N N   . ARG B 17  ? 0.7360 0.5709 0.8902 0.0871  0.1706  0.1575  15  ARG B N   
4495 C CA  . ARG B 17  ? 0.7576 0.5730 0.9204 0.0888  0.1562  0.1574  15  ARG B CA  
4496 C C   . ARG B 17  ? 0.6745 0.5260 0.8178 0.0911  0.1091  0.1334  15  ARG B C   
4497 O O   . ARG B 17  ? 0.6512 0.5278 0.7562 0.0997  0.0890  0.1273  15  ARG B O   
4498 C CB  . ARG B 17  ? 0.7802 0.5589 0.9026 0.1217  0.1763  0.1997  15  ARG B CB  
4499 C CG  . ARG B 17  ? 0.8508 0.5731 0.9850 0.1185  0.2313  0.2335  15  ARG B CG  
4500 C CD  . ARG B 17  ? 0.9238 0.6136 0.9848 0.1652  0.2461  0.2843  15  ARG B CD  
4501 N NE  . ARG B 17  ? 0.9916 0.7287 0.9823 0.1922  0.2234  0.2885  15  ARG B NE  
4502 C CZ  . ARG B 17  ? 0.9915 0.7260 0.9032 0.2397  0.2176  0.3231  15  ARG B CZ  
4503 N NH1 . ARG B 17  ? 1.0486 0.7407 0.9416 0.2727  0.2254  0.3584  15  ARG B NH1 
4504 N NH2 . ARG B 17  ? 1.1221 0.8992 0.9691 0.2591  0.1982  0.3179  15  ARG B NH2 
4505 N N   . CYS B 18  ? 0.7238 0.5745 0.8933 0.0816  0.0952  0.1179  16  CYS B N   
4506 C CA  . CYS B 18  ? 0.6054 0.4901 0.7624 0.0786  0.0598  0.0996  16  CYS B CA  
4507 C C   . CYS B 18  ? 0.6491 0.5544 0.7777 0.1076  0.0496  0.1181  16  CYS B C   
4508 O O   . CYS B 18  ? 0.7020 0.5947 0.8407 0.1274  0.0617  0.1332  16  CYS B O   
4509 C CB  . CYS B 18  ? 0.6416 0.5241 0.8315 0.0600  0.0545  0.0765  16  CYS B CB  
4510 S SG  . CYS B 18  ? 0.6215 0.5431 0.7978 0.0482  0.0233  0.0587  16  CYS B SG  
4511 N N   . GLY B 19  ? 0.6646 0.6023 0.7590 0.1128  0.0249  0.1138  17  GLY B N   
4512 C CA  . GLY B 19  ? 0.6949 0.6711 0.7687 0.1393  0.0053  0.1235  17  GLY B CA  
4513 C C   . GLY B 19  ? 0.6577 0.6770 0.7688 0.1307  -0.0122 0.1082  17  GLY B C   
4514 O O   . GLY B 19  ? 0.7740 0.8406 0.8858 0.1554  -0.0291 0.1141  17  GLY B O   
4515 N N   . ALA B 20  ? 0.5845 0.5949 0.7256 0.0997  -0.0076 0.0890  18  ALA B N   
4516 C CA  . ALA B 20  ? 0.6599 0.7125 0.8333 0.0877  -0.0153 0.0748  18  ALA B CA  
4517 C C   . ALA B 20  ? 0.6501 0.6893 0.8511 0.1035  0.0079  0.0782  18  ALA B C   
4518 O O   . ALA B 20  ? 0.6233 0.7089 0.8521 0.1118  0.0072  0.0724  18  ALA B O   
4519 C CB  . ALA B 20  ? 0.5944 0.6410 0.7671 0.0466  -0.0225 0.0543  18  ALA B CB  
4520 N N   . CYS B 21  ? 0.6890 0.6676 0.8877 0.1067  0.0299  0.0836  19  CYS B N   
4521 C CA  . CYS B 21  ? 0.5949 0.5438 0.8157 0.1233  0.0527  0.0825  19  CYS B CA  
4522 C C   . CYS B 21  ? 0.6439 0.5912 0.8616 0.1705  0.0591  0.1106  19  CYS B C   
4523 O O   . CYS B 21  ? 0.6872 0.6259 0.8756 0.1881  0.0561  0.1363  19  CYS B O   
4524 C CB  . CYS B 21  ? 0.6463 0.5296 0.8727 0.1059  0.0723  0.0753  19  CYS B CB  
4525 S SG  . CYS B 21  ? 0.6236 0.5069 0.8573 0.0669  0.0641  0.0367  19  CYS B SG  
4526 N N   . ILE B 22  ? 0.6020 0.5571 0.8438 0.1972  0.0688  0.1067  20  ILE B N   
4527 C CA  . ILE B 22  ? 0.5967 0.5562 0.8343 0.2527  0.0699  0.1357  20  ILE B CA  
4528 C C   . ILE B 22  ? 0.6669 0.5287 0.8785 0.2719  0.0973  0.1667  20  ILE B C   
4529 O O   . ILE B 22  ? 0.7264 0.5771 0.9088 0.3171  0.0969  0.2039  20  ILE B O   
4530 C CB  . ILE B 22  ? 0.7267 0.7210 1.0018 0.2840  0.0761  0.1223  20  ILE B CB  
4531 C CG1 . ILE B 22  ? 0.6396 0.5565 0.9252 0.2763  0.1072  0.1012  20  ILE B CG1 
4532 C CG2 . ILE B 22  ? 0.6944 0.7940 1.0004 0.2607  0.0563  0.0969  20  ILE B CG2 
4533 C CD1 . ILE B 22  ? 0.6914 0.6336 1.0078 0.3147  0.1194  0.0850  20  ILE B CD1 
4534 N N   . ARG B 23  ? 0.6720 0.4631 0.8934 0.2379  0.1217  0.1529  21  ARG B N   
4535 C CA  . ARG B 23  ? 0.7883 0.4823 0.9983 0.2443  0.1556  0.1800  21  ARG B CA  
4536 C C   . ARG B 23  ? 0.7378 0.4218 0.9268 0.2159  0.1621  0.1960  21  ARG B C   
4537 O O   . ARG B 23  ? 0.7993 0.4184 0.9808 0.2060  0.1933  0.2146  21  ARG B O   
4538 C CB  . ARG B 23  ? 0.7745 0.4028 1.0172 0.2189  0.1785  0.1475  21  ARG B CB  
4539 C CG  . ARG B 23  ? 0.8082 0.4354 1.0618 0.2519  0.1789  0.1297  21  ARG B CG  
4540 C CD  . ARG B 23  ? 0.8817 0.5044 1.1047 0.3050  0.1771  0.1667  21  ARG B CD  
4541 N NE  . ARG B 23  ? 0.9742 0.5121 1.1682 0.3001  0.2011  0.1949  21  ARG B NE  
4542 C CZ  . ARG B 23  ? 1.0594 0.5752 1.2153 0.3425  0.2038  0.2343  21  ARG B CZ  
4543 N NH1 . ARG B 23  ? 1.0532 0.6391 1.1929 0.3905  0.1762  0.2513  21  ARG B NH1 
4544 N NH2 . ARG B 23  ? 1.1588 0.5860 1.2936 0.3349  0.2340  0.2573  21  ARG B NH2 
4545 N N   . ARG B 24  ? 0.7288 0.4839 0.9054 0.1976  0.1333  0.1836  22  ARG B N   
4546 C CA  . ARG B 24  ? 0.8141 0.5716 0.9703 0.1760  0.1375  0.1917  22  ARG B CA  
4547 C C   . ARG B 24  ? 0.7793 0.4800 0.9699 0.1404  0.1717  0.1854  22  ARG B C   
4548 O O   . ARG B 24  ? 0.7310 0.3920 0.9077 0.1424  0.2042  0.2164  22  ARG B O   
4549 C CB  . ARG B 24  ? 0.8293 0.5866 0.9264 0.2160  0.1404  0.2348  22  ARG B CB  
4550 C CG  . ARG B 24  ? 0.7984 0.6329 0.8682 0.2434  0.0969  0.2306  22  ARG B CG  
4551 C CD  . ARG B 24  ? 0.9932 0.8299 0.9931 0.2884  0.0945  0.2700  22  ARG B CD  
4552 N NE  . ARG B 24  ? 1.0567 0.9781 1.0386 0.3125  0.0462  0.2580  22  ARG B NE  
4553 C CZ  . ARG B 24  ? 1.1203 1.0672 1.0365 0.3548  0.0278  0.2809  22  ARG B CZ  
4554 N NH1 . ARG B 24  ? 1.1477 1.0381 0.9972 0.3792  0.0582  0.3220  22  ARG B NH1 
4555 N NH2 . ARG B 24  ? 1.1041 1.1398 1.0208 0.3714  -0.0217 0.2603  22  ARG B NH2 
4556 N N   . PRO B 25  ? 0.6920 0.3931 0.9281 0.1071  0.1661  0.1447  23  PRO B N   
4557 C CA  . PRO B 25  ? 0.6785 0.3405 0.9610 0.0695  0.1918  0.1291  23  PRO B CA  
4558 C C   . PRO B 25  ? 0.7429 0.4380 1.0322 0.0482  0.1959  0.1311  23  PRO B C   
4559 O O   . PRO B 25  ? 0.7438 0.4947 1.0125 0.0496  0.1665  0.1202  23  PRO B O   
4560 C CB  . PRO B 25  ? 0.6895 0.3677 1.0039 0.0463  0.1693  0.0783  23  PRO B CB  
4561 C CG  . PRO B 25  ? 0.5599 0.3011 0.8410 0.0606  0.1332  0.0716  23  PRO B CG  
4562 C CD  . PRO B 25  ? 0.6846 0.4278 0.9304 0.1015  0.1361  0.1096  23  PRO B CD  
4563 N N   . PHE B 26  ? 0.7721 0.4300 1.0942 0.0281  0.2364  0.1443  24  PHE B N   
4564 C CA  . PHE B 26  ? 0.7701 0.4701 1.1153 0.0070  0.2461  0.1401  24  PHE B CA  
4565 C C   . PHE B 26  ? 0.7259 0.4773 1.1236 -0.0230 0.2133  0.0870  24  PHE B C   
4566 O O   . PHE B 26  ? 0.7770 0.5124 1.2144 -0.0441 0.2047  0.0545  24  PHE B O   
4567 C CB  . PHE B 26  ? 0.7320 0.3882 1.1154 -0.0149 0.3043  0.1650  24  PHE B CB  
4568 C CG  . PHE B 26  ? 0.8349 0.4532 1.1486 0.0193  0.3388  0.2231  24  PHE B CG  
4569 C CD1 . PHE B 26  ? 0.9394 0.5913 1.2110 0.0364  0.3521  0.2487  24  PHE B CD1 
4570 C CD2 . PHE B 26  ? 0.9668 0.5274 1.2487 0.0376  0.3531  0.2445  24  PHE B CD2 
4571 C CE1 . PHE B 26  ? 1.0119 0.6291 1.2067 0.0716  0.3833  0.3022  24  PHE B CE1 
4572 C CE2 . PHE B 26  ? 1.0095 0.5406 1.2199 0.0731  0.3792  0.2957  24  PHE B CE2 
4573 C CZ  . PHE B 26  ? 0.9826 0.5442 1.1466 0.0904  0.3927  0.3236  24  PHE B CZ  
4574 N N   . LEU B 27  ? 0.5474 0.3573 0.9384 -0.0198 0.1933  0.0771  25  LEU B N   
4575 C CA  . LEU B 27  ? 0.6645 0.5243 1.0939 -0.0371 0.1585  0.0333  25  LEU B CA  
4576 C C   . LEU B 27  ? 0.5610 0.4719 1.0182 -0.0382 0.1670  0.0308  25  LEU B C   
4577 O O   . LEU B 27  ? 0.5772 0.4943 0.9854 -0.0135 0.1743  0.0541  25  LEU B O   
4578 C CB  . LEU B 27  ? 0.5469 0.4197 0.9225 -0.0197 0.1130  0.0214  25  LEU B CB  
4579 C CG  . LEU B 27  ? 0.6101 0.4557 0.9685 -0.0188 0.0998  0.0112  25  LEU B CG  
4580 C CD1 . LEU B 27  ? 0.5564 0.4213 0.8610 -0.0040 0.0666  0.0099  25  LEU B CD1 
4581 C CD2 . LEU B 27  ? 0.6078 0.4526 1.0145 -0.0441 0.0919  -0.0290 25  LEU B CD2 
4582 N N   . CYS B 28  ? 0.5247 0.4782 1.0621 -0.0640 0.1649  -0.0016 26  CYS B N   
4583 C CA  . CYS B 28  ? 0.5836 0.6003 1.1595 -0.0596 0.1722  -0.0082 26  CYS B CA  
4584 C C   . CYS B 28  ? 0.5831 0.6282 1.1129 -0.0288 0.1249  -0.0222 26  CYS B C   
4585 O O   . CYS B 28  ? 0.5406 0.5604 1.0174 -0.0195 0.0879  -0.0279 26  CYS B O   
4586 C CB  . CYS B 28  ? 0.5915 0.6642 1.2809 -0.0949 0.1780  -0.0439 26  CYS B CB  
4587 S SG  . CYS B 28  ? 0.5659 0.6601 1.2817 -0.1085 0.1167  -0.0976 26  CYS B SG  
4588 N N   . CYS B 29  ? 0.5589 0.6528 1.1089 -0.0120 0.1317  -0.0261 27  CYS B N   
4589 C CA  . CYS B 29  ? 0.5704 0.6755 1.0739 0.0216  0.0926  -0.0367 27  CYS B CA  
4590 C C   . CYS B 29  ? 0.5354 0.6465 1.0394 0.0207  0.0402  -0.0633 27  CYS B C   
4591 O O   . CYS B 29  ? 0.5782 0.6542 1.0108 0.0394  0.0088  -0.0594 27  CYS B O   
4592 C CB  . CYS B 29  ? 0.6393 0.8060 1.1880 0.0417  0.1087  -0.0464 27  CYS B CB  
4593 S SG  . CYS B 29  ? 0.6844 0.8564 1.2363 0.0413  0.1820  -0.0154 27  CYS B SG  
4594 N N   . LYS B 30  ? 0.4913 0.6452 1.0724 -0.0028 0.0312  -0.0912 28  LYS B N   
4595 C CA  . LYS B 30  ? 0.5345 0.7026 1.1074 0.0025  -0.0210 -0.1186 28  LYS B CA  
4596 C C   . LYS B 30  ? 0.5869 0.6920 1.0923 -0.0080 -0.0326 -0.1118 28  LYS B C   
4597 O O   . LYS B 30  ? 0.5632 0.6436 0.9993 0.0104  -0.0645 -0.1086 28  LYS B O   
4598 C CB  . LYS B 30  ? 0.4625 0.7063 1.1400 -0.0195 -0.0324 -0.1589 28  LYS B CB  
4599 N N   . CYS B 31  ? 0.5206 0.5956 1.0445 -0.0357 -0.0023 -0.1073 29  CYS B N   
4600 C CA  . CYS B 31  ? 0.5043 0.5291 0.9739 -0.0408 -0.0105 -0.1056 29  CYS B CA  
4601 C C   . CYS B 31  ? 0.5443 0.5265 0.9354 -0.0218 -0.0042 -0.0701 29  CYS B C   
4602 O O   . CYS B 31  ? 0.5441 0.5039 0.8806 -0.0165 -0.0221 -0.0687 29  CYS B O   
4603 C CB  . CYS B 31  ? 0.5111 0.5081 1.0257 -0.0700 0.0199  -0.1137 29  CYS B CB  
4604 S SG  . CYS B 31  ? 0.5606 0.6061 1.1818 -0.1066 0.0116  -0.1675 29  CYS B SG  
4605 N N   . CYS B 32  ? 0.5255 0.5025 0.9106 -0.0122 0.0210  -0.0441 30  CYS B N   
4606 C CA  . CYS B 32  ? 0.5614 0.5086 0.8774 0.0042  0.0200  -0.0185 30  CYS B CA  
4607 C C   . CYS B 32  ? 0.5766 0.5218 0.8465 0.0176  -0.0146 -0.0245 30  CYS B C   
4608 O O   . CYS B 32  ? 0.4909 0.4113 0.7110 0.0177  -0.0255 -0.0153 30  CYS B O   
4609 C CB  . CYS B 32  ? 0.5771 0.5233 0.8871 0.0157  0.0502  0.0046  30  CYS B CB  
4610 S SG  . CYS B 32  ? 0.6324 0.5531 0.8623 0.0348  0.0435  0.0273  30  CYS B SG  
4611 N N   . TYR B 33  ? 0.5736 0.5445 0.8636 0.0294  -0.0303 -0.0391 31  TYR B N   
4612 C CA  . TYR B 33  ? 0.6783 0.6314 0.9197 0.0469  -0.0622 -0.0410 31  TYR B CA  
4613 C C   . TYR B 33  ? 0.6560 0.5950 0.8663 0.0384  -0.0844 -0.0462 31  TYR B C   
4614 O O   . TYR B 33  ? 0.6790 0.5796 0.8294 0.0385  -0.0934 -0.0327 31  TYR B O   
4615 C CB  . TYR B 33  ? 0.6346 0.6228 0.9096 0.0708  -0.0759 -0.0559 31  TYR B CB  
4616 C CG  . TYR B 33  ? 0.6494 0.6081 0.8715 0.0963  -0.1103 -0.0550 31  TYR B CG  
4617 C CD1 . TYR B 33  ? 0.7001 0.6671 0.9098 0.1019  -0.1415 -0.0641 31  TYR B CD1 
4618 C CD2 . TYR B 33  ? 0.7616 0.6760 0.9382 0.1170  -0.1112 -0.0452 31  TYR B CD2 
4619 C CE1 . TYR B 33  ? 0.7333 0.6612 0.8826 0.1301  -0.1701 -0.0548 31  TYR B CE1 
4620 C CE2 . TYR B 33  ? 0.7695 0.6377 0.8936 0.1412  -0.1387 -0.0400 31  TYR B CE2 
4621 C CZ  . TYR B 33  ? 0.7665 0.6397 0.8751 0.1490  -0.1667 -0.0406 31  TYR B CZ  
4622 O OH  . TYR B 33  ? 0.8406 0.6566 0.8854 0.1778  -0.1913 -0.0273 31  TYR B OH  
4623 N N   . ASP B 34  ? 0.5922 0.5625 0.8420 0.0288  -0.0913 -0.0681 32  ASP B N   
4624 C CA  . ASP B 34  ? 0.6647 0.6251 0.8739 0.0259  -0.1121 -0.0775 32  ASP B CA  
4625 C C   . ASP B 34  ? 0.6507 0.5782 0.8224 0.0111  -0.0923 -0.0625 32  ASP B C   
4626 O O   . ASP B 34  ? 0.7061 0.6159 0.8228 0.0116  -0.1014 -0.0587 32  ASP B O   
4627 C CB  . ASP B 34  ? 0.6586 0.6615 0.9197 0.0165  -0.1249 -0.1136 32  ASP B CB  
4628 C CG  . ASP B 34  ? 0.7539 0.8101 1.0592 0.0340  -0.1528 -0.1335 32  ASP B CG  
4629 O OD1 . ASP B 34  ? 0.8120 0.8626 1.0684 0.0636  -0.1823 -0.1253 32  ASP B OD1 
4630 O OD2 . ASP B 34  ? 0.7894 0.8938 1.1820 0.0189  -0.1439 -0.1565 32  ASP B OD2 
4631 N N   . HIS B 35  ? 0.5511 0.4742 0.7509 0.0015  -0.0636 -0.0522 33  HIS B N   
4632 C CA  . HIS B 35  ? 0.6520 0.5577 0.8271 -0.0053 -0.0471 -0.0388 33  HIS B CA  
4633 C C   . HIS B 35  ? 0.6491 0.5388 0.7789 -0.0039 -0.0513 -0.0172 33  HIS B C   
4634 O O   . HIS B 35  ? 0.6326 0.5154 0.7286 -0.0113 -0.0510 -0.0115 33  HIS B O   
4635 C CB  . HIS B 35  ? 0.6271 0.5311 0.8421 -0.0075 -0.0191 -0.0314 33  HIS B CB  
4636 C CG  . HIS B 35  ? 0.6255 0.5224 0.8252 -0.0050 -0.0047 -0.0187 33  HIS B CG  
4637 N ND1 . HIS B 35  ? 0.6163 0.5156 0.7940 -0.0075 -0.0065 -0.0279 33  HIS B ND1 
4638 C CD2 . HIS B 35  ? 0.6348 0.5304 0.8389 0.0048  0.0113  0.0021  33  HIS B CD2 
4639 C CE1 . HIS B 35  ? 0.5852 0.4911 0.7658 0.0000  0.0089  -0.0152 33  HIS B CE1 
4640 N NE2 . HIS B 35  ? 0.5632 0.4671 0.7588 0.0091  0.0162  0.0033  33  HIS B NE2 
4641 N N   . VAL B 36  ? 0.6593 0.5432 0.7894 0.0032  -0.0527 -0.0079 34  VAL B N   
4642 C CA  . VAL B 36  ? 0.6596 0.5234 0.7527 -0.0008 -0.0576 0.0048  34  VAL B CA  
4643 C C   . VAL B 36  ? 0.6674 0.4984 0.7153 -0.0038 -0.0743 0.0080  34  VAL B C   
4644 O O   . VAL B 36  ? 0.6708 0.4821 0.6908 -0.0200 -0.0724 0.0181  34  VAL B O   
4645 C CB  . VAL B 36  ? 0.6613 0.5216 0.7564 0.0110  -0.0557 0.0068  34  VAL B CB  
4646 C CG1 . VAL B 36  ? 0.5865 0.4707 0.7094 0.0163  -0.0347 0.0134  34  VAL B CG1 
4647 C CG2 . VAL B 36  ? 0.7142 0.5692 0.8155 0.0288  -0.0649 -0.0025 34  VAL B CG2 
4648 N N   . ILE B 37  ? 0.7419 0.5672 0.7827 0.0120  -0.0904 0.0008  35  ILE B N   
4649 C CA  . ILE B 37  ? 0.7809 0.5621 0.7657 0.0188  -0.1068 0.0113  35  ILE B CA  
4650 C C   . ILE B 37  ? 0.7985 0.5759 0.7448 0.0096  -0.1051 0.0174  35  ILE B C   
4651 O O   . ILE B 37  ? 0.8317 0.5651 0.7182 0.0151  -0.1134 0.0339  35  ILE B O   
4652 C CB  . ILE B 37  ? 0.8995 0.6794 0.8866 0.0513  -0.1301 0.0031  35  ILE B CB  
4653 C CG1 . ILE B 37  ? 0.8674 0.6994 0.8862 0.0603  -0.1431 -0.0170 35  ILE B CG1 
4654 C CG2 . ILE B 37  ? 0.8113 0.5989 0.8335 0.0641  -0.1251 -0.0045 35  ILE B CG2 
4655 C CD1 . ILE B 37  ? 0.8460 0.6625 0.8052 0.0743  -0.1660 -0.0128 35  ILE B CD1 
4656 N N   . SER B 38  ? 0.7928 0.6085 0.7646 -0.0009 -0.0916 0.0059  36  SER B N   
4657 C CA  . SER B 38  ? 0.8202 0.6383 0.7519 -0.0051 -0.0863 0.0056  36  SER B CA  
4658 C C   . SER B 38  ? 0.8203 0.6565 0.7637 -0.0261 -0.0566 0.0106  36  SER B C   
4659 O O   . SER B 38  ? 0.9108 0.7543 0.8217 -0.0290 -0.0440 0.0092  36  SER B O   
4660 C CB  . SER B 38  ? 0.8622 0.7122 0.8104 0.0084  -0.1012 -0.0243 36  SER B CB  
4661 O OG  . SER B 38  ? 0.8422 0.7207 0.8611 0.0015  -0.0895 -0.0425 36  SER B OG  
4662 N N   . THR B 39  ? 0.7350 0.5852 0.7220 -0.0363 -0.0459 0.0148  37  THR B N   
4663 C CA  . THR B 39  ? 0.7647 0.6480 0.7768 -0.0493 -0.0227 0.0175  37  THR B CA  
4664 C C   . THR B 39  ? 0.7147 0.5980 0.7406 -0.0661 -0.0231 0.0297  37  THR B C   
4665 O O   . THR B 39  ? 0.6688 0.5141 0.6754 -0.0683 -0.0381 0.0347  37  THR B O   
4666 C CB  . THR B 39  ? 0.6944 0.6073 0.7551 -0.0354 -0.0140 0.0024  37  THR B CB  
4667 O OG1 . THR B 39  ? 0.6843 0.5957 0.7755 -0.0283 -0.0212 0.0056  37  THR B OG1 
4668 C CG2 . THR B 39  ? 0.7315 0.6377 0.7861 -0.0241 -0.0184 -0.0197 37  THR B CG2 
4669 N N   . SER B 40  ? 0.6842 0.6136 0.7461 -0.0751 -0.0089 0.0299  38  SER B N   
4670 C CA  . SER B 40  ? 0.6457 0.5933 0.7307 -0.0921 -0.0146 0.0326  38  SER B CA  
4671 C C   . SER B 40  ? 0.6134 0.5758 0.7225 -0.0710 -0.0282 0.0270  38  SER B C   
4672 O O   . SER B 40  ? 0.6163 0.5938 0.7353 -0.0798 -0.0403 0.0237  38  SER B O   
4673 C CB  . SER B 40  ? 0.6577 0.6669 0.7787 -0.1100 0.0042  0.0334  38  SER B CB  
4674 O OG  . SER B 40  ? 0.6593 0.7139 0.8116 -0.0834 0.0160  0.0273  38  SER B OG  
4675 N N   . HIS B 41  ? 0.6129 0.5700 0.7288 -0.0451 -0.0250 0.0250  39  HIS B N   
4676 C CA  . HIS B 41  ? 0.6202 0.5845 0.7503 -0.0235 -0.0287 0.0274  39  HIS B CA  
4677 C C   . HIS B 41  ? 0.6505 0.5798 0.7557 -0.0221 -0.0421 0.0252  39  HIS B C   
4678 O O   . HIS B 41  ? 0.6347 0.5348 0.7305 -0.0182 -0.0432 0.0217  39  HIS B O   
4679 C CB  . HIS B 41  ? 0.6309 0.5893 0.7800 -0.0034 -0.0131 0.0278  39  HIS B CB  
4680 C CG  . HIS B 41  ? 0.5960 0.5828 0.7688 0.0062  0.0017  0.0276  39  HIS B CG  
4681 N ND1 . HIS B 41  ? 0.5865 0.5628 0.7791 0.0295  0.0171  0.0309  39  HIS B ND1 
4682 C CD2 . HIS B 41  ? 0.6422 0.6658 0.8241 -0.0024 0.0075  0.0242  39  HIS B CD2 
4683 C CE1 . HIS B 41  ? 0.6185 0.6214 0.8288 0.0408  0.0285  0.0274  39  HIS B CE1 
4684 N NE2 . HIS B 41  ? 0.6208 0.6609 0.8280 0.0217  0.0240  0.0226  39  HIS B NE2 
4685 N N   . LYS B 42  ? 0.6163 0.5541 0.7117 -0.0222 -0.0541 0.0231  40  LYS B N   
4686 C CA  . LYS B 42  ? 0.7075 0.6105 0.7741 -0.0166 -0.0646 0.0159  40  LYS B CA  
4687 C C   . LYS B 42  ? 0.6792 0.5984 0.7348 0.0071  -0.0647 0.0172  40  LYS B C   
4688 O O   . LYS B 42  ? 0.7386 0.6330 0.7683 0.0184  -0.0673 0.0095  40  LYS B O   
4689 C CB  . LYS B 42  ? 0.7432 0.6194 0.7884 -0.0424 -0.0805 0.0045  40  LYS B CB  
4690 C CG  . LYS B 42  ? 0.6952 0.5504 0.7386 -0.0680 -0.0752 0.0107  40  LYS B CG  
4691 C CD  . LYS B 42  ? 0.7106 0.5255 0.7338 -0.0541 -0.0728 0.0168  40  LYS B CD  
4692 C CE  . LYS B 42  ? 0.7164 0.5056 0.7181 -0.0750 -0.0670 0.0278  40  LYS B CE  
4693 N NZ  . LYS B 42  ? 0.7833 0.5416 0.7577 -0.0550 -0.0719 0.0330  40  LYS B NZ  
4694 N N   . LEU B 43  ? 0.6760 0.6346 0.7444 0.0206  -0.0607 0.0281  41  LEU B N   
4695 C CA  . LEU B 43  ? 0.7043 0.6752 0.7469 0.0495  -0.0595 0.0365  41  LEU B CA  
4696 C C   . LEU B 43  ? 0.6782 0.6274 0.7260 0.0687  -0.0291 0.0558  41  LEU B C   
4697 O O   . LEU B 43  ? 0.7149 0.6634 0.7929 0.0716  -0.0120 0.0694  41  LEU B O   
4698 C CB  . LEU B 43  ? 0.7169 0.7395 0.7670 0.0630  -0.0715 0.0434  41  LEU B CB  
4699 C CG  . LEU B 43  ? 0.7795 0.8142 0.7873 0.1015  -0.0724 0.0584  41  LEU B CG  
4700 C CD1 . LEU B 43  ? 0.8058 0.8305 0.7627 0.1020  -0.0895 0.0369  41  LEU B CD1 
4701 C CD2 . LEU B 43  ? 0.7904 0.8837 0.8090 0.1235  -0.0902 0.0666  41  LEU B CD2 
4702 N N   . VAL B 44  ? 0.6929 0.6241 0.7152 0.0803  -0.0193 0.0546  42  VAL B N   
4703 C CA  . VAL B 44  ? 0.7902 0.7077 0.8272 0.0914  0.0153  0.0717  42  VAL B CA  
4704 C C   . VAL B 44  ? 0.7859 0.7069 0.7755 0.1215  0.0315  0.0931  42  VAL B C   
4705 O O   . VAL B 44  ? 0.8718 0.8008 0.8102 0.1348  0.0155  0.0813  42  VAL B O   
4706 C CB  . VAL B 44  ? 0.7588 0.6652 0.8131 0.0836  0.0206  0.0547  42  VAL B CB  
4707 C CG1 . VAL B 44  ? 0.7272 0.6356 0.8119 0.0892  0.0596  0.0692  42  VAL B CG1 
4708 C CG2 . VAL B 44  ? 0.6817 0.5818 0.7675 0.0610  0.0019  0.0386  42  VAL B CG2 
4709 N N   . LEU B 45  ? 0.7407 0.6486 0.7403 0.1330  0.0640  0.1242  43  LEU B N   
4710 C CA  . LEU B 45  ? 0.7892 0.6913 0.7323 0.1664  0.0846  0.1559  43  LEU B CA  
4711 C C   . LEU B 45  ? 0.8809 0.7617 0.8328 0.1659  0.1356  0.1752  43  LEU B C   
4712 O O   . LEU B 45  ? 0.7960 0.6615 0.8136 0.1413  0.1602  0.1766  43  LEU B O   
4713 C CB  . LEU B 45  ? 0.8253 0.7194 0.7631 0.1874  0.0859  0.1862  43  LEU B CB  
4714 C CG  . LEU B 45  ? 0.8618 0.7965 0.7974 0.1949  0.0399  0.1713  43  LEU B CG  
4715 C CD1 . LEU B 45  ? 0.9503 0.8805 0.8754 0.2314  0.0450  0.2060  43  LEU B CD1 
4716 C CD2 . LEU B 45  ? 0.8790 0.8513 0.7629 0.2027  0.0034  0.1475  43  LEU B CD2 
4717 N N   . SER B 46  ? 0.9868 0.8718 0.8736 0.1917  0.1522  0.1868  44  SER B N   
4718 C CA  . SER B 46  ? 1.0233 0.8963 0.9116 0.1941  0.2100  0.2107  44  SER B CA  
4719 C C   . SER B 46  ? 1.1500 1.0062 0.9429 0.2354  0.2326  0.2542  44  SER B C   
4720 O O   . SER B 46  ? 1.1756 1.0265 0.9229 0.2603  0.2046  0.2700  44  SER B O   
4721 C CB  . SER B 46  ? 0.9972 0.8986 0.8991 0.1884  0.2136  0.1765  44  SER B CB  
4722 O OG  . SER B 46  ? 1.0215 0.9286 0.9655 0.1789  0.2722  0.1928  44  SER B OG  
4723 N N   . VAL B 47  ? 1.1292 0.9815 0.8906 0.2464  0.2857  0.2759  45  VAL B N   
4724 C CA  . VAL B 47  ? 1.1989 1.0345 0.8480 0.2913  0.3114  0.3192  45  VAL B CA  
4725 C C   . VAL B 47  ? 1.2179 1.0792 0.7838 0.3254  0.2459  0.2965  45  VAL B C   
4726 O O   . VAL B 47  ? 1.3108 1.1619 0.7960 0.3654  0.2361  0.3305  45  VAL B O   
4727 C CB  . VAL B 47  ? 1.2347 1.0830 0.8514 0.2998  0.3696  0.3271  45  VAL B CB  
4728 C CG1 . VAL B 47  ? 1.2856 1.1166 0.7632 0.3523  0.3937  0.3717  45  VAL B CG1 
4729 C CG2 . VAL B 47  ? 1.1842 1.0207 0.9015 0.2594  0.4357  0.3474  45  VAL B CG2 
4730 N N   . ASN B 48  ? 1.2454 1.1397 0.8333 0.3097  0.1996  0.2383  46  ASN B N   
4731 C CA  . ASN B 48  ? 1.2790 1.2016 0.8217 0.3228  0.1321  0.2022  46  ASN B CA  
4732 C C   . ASN B 48  ? 1.1893 1.1216 0.8253 0.2805  0.0920  0.1644  46  ASN B C   
4733 O O   . ASN B 48  ? 1.1197 1.0411 0.8310 0.2490  0.1108  0.1533  46  ASN B O   
4734 C CB  . ASN B 48  ? 1.2756 1.2141 0.7391 0.3431  0.1207  0.1640  46  ASN B CB  
4735 C CG  . ASN B 48  ? 1.4189 1.3496 0.7795 0.3868  0.1691  0.2006  46  ASN B CG  
4736 O OD1 . ASN B 48  ? 1.4527 1.3795 0.7385 0.4226  0.1690  0.2414  46  ASN B OD1 
4737 N ND2 . ASN B 48  ? 1.4306 1.3607 0.7839 0.3883  0.2131  0.1883  46  ASN B ND2 
4738 N N   . PRO B 49  ? 1.1855 1.1438 0.8195 0.2796  0.0377  0.1449  47  PRO B N   
4739 C CA  . PRO B 49  ? 1.0924 1.0588 0.8054 0.2378  0.0057  0.1107  47  PRO B CA  
4740 C C   . PRO B 49  ? 1.1282 1.0840 0.8408 0.2186  -0.0070 0.0649  47  PRO B C   
4741 O O   . PRO B 49  ? 1.1258 1.0836 0.7694 0.2379  -0.0180 0.0414  47  PRO B O   
4742 C CB  . PRO B 49  ? 1.0164 1.0258 0.7214 0.2449  -0.0442 0.1007  47  PRO B CB  
4743 C CG  . PRO B 49  ? 1.1572 1.1857 0.7621 0.2887  -0.0571 0.1038  47  PRO B CG  
4744 C CD  . PRO B 49  ? 1.2256 1.2155 0.7886 0.3168  0.0025  0.1525  47  PRO B CD  
4745 N N   . TYR B 50  ? 1.0289 0.9685 0.8122 0.1849  -0.0058 0.0516  48  TYR B N   
4746 C CA  . TYR B 50  ? 1.0396 0.9575 0.8242 0.1705  -0.0209 0.0118  48  TYR B CA  
4747 C C   . TYR B 50  ? 1.0463 0.9695 0.8185 0.1514  -0.0699 -0.0211 48  TYR B C   
4748 O O   . TYR B 50  ? 0.9994 0.9241 0.8220 0.1196  -0.0872 -0.0252 48  TYR B O   
4749 C CB  . TYR B 50  ? 0.9666 0.8668 0.8221 0.1475  -0.0073 0.0128  48  TYR B CB  
4750 C CG  . TYR B 50  ? 0.9747 0.8791 0.8561 0.1600  0.0383  0.0319  48  TYR B CG  
4751 C CD1 . TYR B 50  ? 1.0373 0.9507 0.8718 0.1893  0.0711  0.0453  48  TYR B CD1 
4752 C CD2 . TYR B 50  ? 0.8901 0.7955 0.8437 0.1413  0.0492  0.0345  48  TYR B CD2 
4753 C CE1 . TYR B 50  ? 1.0072 0.9321 0.8779 0.1940  0.1197  0.0631  48  TYR B CE1 
4754 C CE2 . TYR B 50  ? 0.8668 0.7890 0.8611 0.1461  0.0894  0.0460  48  TYR B CE2 
4755 C CZ  . TYR B 50  ? 0.9381 0.8710 0.8966 0.1696  0.1276  0.0613  48  TYR B CZ  
4756 O OH  . TYR B 50  ? 0.9027 0.8598 0.9136 0.1680  0.1743  0.0730  48  TYR B OH  
4757 N N   . VAL B 51  ? 1.1041 1.0328 0.8080 0.1691  -0.0904 -0.0474 49  VAL B N   
4758 C CA  . VAL B 51  ? 1.1221 1.0598 0.8161 0.1466  -0.1385 -0.0879 49  VAL B CA  
4759 C C   . VAL B 51  ? 1.1540 1.0567 0.7799 0.1598  -0.1493 -0.1327 49  VAL B C   
4760 O O   . VAL B 51  ? 1.2404 1.1398 0.8055 0.1992  -0.1247 -0.1279 49  VAL B O   
4761 C CB  . VAL B 51  ? 1.1642 1.1680 0.8471 0.1581  -0.1664 -0.0793 49  VAL B CB  
4762 C CG1 . VAL B 51  ? 1.1183 1.1394 0.7220 0.2116  -0.1498 -0.0541 49  VAL B CG1 
4763 C CG2 . VAL B 51  ? 1.1638 1.1919 0.8448 0.1311  -0.2188 -0.1306 49  VAL B CG2 
4764 N N   . CYS B 52  ? 1.1587 1.0294 0.7937 0.1258  -0.1817 -0.1772 50  CYS B N   
4765 C CA  . CYS B 52  ? 1.2724 1.0989 0.8402 0.1373  -0.1959 -0.2289 50  CYS B CA  
4766 C C   . CYS B 52  ? 1.3376 1.2140 0.8267 0.1681  -0.2193 -0.2487 50  CYS B C   
4767 O O   . CYS B 52  ? 1.2738 1.1994 0.7711 0.1489  -0.2624 -0.2684 50  CYS B O   
4768 C CB  . CYS B 52  ? 1.2033 0.9746 0.7978 0.0884  -0.2265 -0.2729 50  CYS B CB  
4769 S SG  . CYS B 52  ? 1.3994 1.0906 0.9120 0.1024  -0.2419 -0.3440 50  CYS B SG  
4770 N N   . ASN B 53  ? 1.3775 1.2491 0.7899 0.2179  -0.1909 -0.2438 51  ASN B N   
4771 C CA  . ASN B 53  ? 1.3941 1.3101 0.7101 0.2568  -0.2093 -0.2570 51  ASN B CA  
4772 C C   . ASN B 53  ? 1.5106 1.3969 0.7613 0.2534  -0.2501 -0.3360 51  ASN B C   
4773 O O   . ASN B 53  ? 1.6529 1.5320 0.8016 0.2979  -0.2412 -0.3592 51  ASN B O   
4774 C CB  . ASN B 53  ? 1.4020 1.3235 0.6550 0.3110  -0.1530 -0.2140 51  ASN B CB  
4775 C CG  . ASN B 53  ? 1.4381 1.3672 0.7674 0.3056  -0.1055 -0.1451 51  ASN B CG  
4776 O OD1 . ASN B 53  ? 1.4408 1.3447 0.7941 0.3131  -0.0566 -0.1280 51  ASN B OD1 
4777 N ND2 . ASN B 53  ? 1.3413 1.3090 0.7143 0.2933  -0.1209 -0.1101 51  ASN B ND2 
4778 N N   . ALA B 54  ? 1.5225 1.3883 0.8295 0.1989  -0.2920 -0.3792 52  ALA B N   
4779 C CA  . ALA B 54  ? 1.5582 1.3863 0.8281 0.1798  -0.3280 -0.4541 52  ALA B CA  
4780 C C   . ALA B 54  ? 1.5495 1.4530 0.8555 0.1418  -0.3794 -0.4754 52  ALA B C   
4781 O O   . ALA B 54  ? 1.4924 1.4472 0.8760 0.1112  -0.3972 -0.4538 52  ALA B O   
4782 C CB  . ALA B 54  ? 1.5644 1.2899 0.8849 0.1380  -0.3208 -0.4816 52  ALA B CB  
4783 N N   . PRO B 55  ? 1.6636 1.5811 0.9183 0.1438  -0.4035 -0.5191 53  PRO B N   
4784 C CA  . PRO B 55  ? 1.6630 1.6623 0.9520 0.1112  -0.4543 -0.5413 53  PRO B CA  
4785 C C   . PRO B 55  ? 1.6151 1.6100 1.0164 0.0322  -0.4744 -0.5598 53  PRO B C   
4786 O O   . PRO B 55  ? 1.6669 1.5790 1.0863 -0.0144 -0.4711 -0.5999 53  PRO B O   
4787 C CB  . PRO B 55  ? 1.8174 1.7989 1.0259 0.1204  -0.4726 -0.5976 53  PRO B CB  
4788 C CG  . PRO B 55  ? 1.8559 1.7281 1.0186 0.1364  -0.4315 -0.6148 53  PRO B CG  
4789 C CD  . PRO B 55  ? 1.7468 1.6088 0.9117 0.1767  -0.3858 -0.5530 53  PRO B CD  
4790 N N   . GLY B 56  ? 1.5534 1.6343 1.0304 0.0179  -0.4896 -0.5270 54  GLY B N   
4791 C CA  . GLY B 56  ? 1.4871 1.5842 1.0753 -0.0571 -0.5043 -0.5391 54  GLY B CA  
4792 C C   . GLY B 56  ? 1.4100 1.4441 1.0619 -0.0871 -0.4701 -0.5110 54  GLY B C   
4793 O O   . GLY B 56  ? 1.4647 1.4932 1.2017 -0.1546 -0.4717 -0.5193 54  GLY B O   
4794 N N   . CYS B 57  ? 1.3593 1.3442 0.9707 -0.0402 -0.4376 -0.4761 55  CYS B N   
4795 C CA  . CYS B 57  ? 1.3714 1.2967 1.0396 -0.0632 -0.4073 -0.4439 55  CYS B CA  
4796 C C   . CYS B 57  ? 1.2874 1.3003 1.0217 -0.0553 -0.3913 -0.3809 55  CYS B C   
4797 O O   . CYS B 57  ? 1.2821 1.3748 0.9899 -0.0078 -0.3994 -0.3571 55  CYS B O   
4798 C CB  . CYS B 57  ? 1.4010 1.2283 1.0108 -0.0224 -0.3618 -0.4202 55  CYS B CB  
4799 S SG  . CYS B 57  ? 1.3295 1.0669 1.0072 -0.0575 -0.3192 -0.3785 55  CYS B SG  
4800 N N   . ASP B 58  ? 1.2908 1.2794 1.1038 -0.0986 -0.3661 -0.3527 56  ASP B N   
4801 C CA  . ASP B 58  ? 1.1537 1.2170 1.0348 -0.0967 -0.3489 -0.3010 56  ASP B CA  
4802 C C   . ASP B 58  ? 1.1319 1.1294 1.0263 -0.0915 -0.2988 -0.2494 56  ASP B C   
4803 O O   . ASP B 58  ? 1.1571 1.1920 1.1144 -0.1067 -0.2813 -0.2160 56  ASP B O   
4804 C CB  . ASP B 58  ? 1.1592 1.2921 1.1353 -0.1579 -0.3706 -0.3220 56  ASP B CB  
4805 C CG  . ASP B 58  ? 1.2082 1.2517 1.2136 -0.2269 -0.3617 -0.3480 56  ASP B CG  
4806 O OD1 . ASP B 58  ? 1.3223 1.2849 1.2750 -0.2364 -0.3766 -0.3923 56  ASP B OD1 
4807 O OD2 . ASP B 58  ? 1.2095 1.2560 1.2842 -0.2690 -0.3364 -0.3228 56  ASP B OD2 
4808 N N   . VAL B 59  ? 1.1296 1.0379 0.9680 -0.0675 -0.2768 -0.2455 57  VAL B N   
4809 C CA  . VAL B 59  ? 1.1448 0.9953 0.9989 -0.0641 -0.2378 -0.2053 57  VAL B CA  
4810 C C   . VAL B 59  ? 1.0647 0.9563 0.9132 -0.0164 -0.2124 -0.1611 57  VAL B C   
4811 O O   . VAL B 59  ? 0.9987 0.8974 0.7938 0.0267  -0.2077 -0.1606 57  VAL B O   
4812 C CB  . VAL B 59  ? 1.1394 0.8816 0.9480 -0.0577 -0.2282 -0.2236 57  VAL B CB  
4813 C CG1 . VAL B 59  ? 1.1812 0.8820 1.0061 -0.0446 -0.1949 -0.1823 57  VAL B CG1 
4814 C CG2 . VAL B 59  ? 1.1757 0.8544 0.9906 -0.1098 -0.2484 -0.2644 57  VAL B CG2 
4815 N N   . THR B 60  ? 1.0380 0.9508 0.9390 -0.0258 -0.1923 -0.1248 58  THR B N   
4816 C CA  . THR B 60  ? 1.0085 0.9483 0.9159 0.0098  -0.1659 -0.0850 58  THR B CA  
4817 C C   . THR B 60  ? 0.9610 0.8614 0.8965 0.0034  -0.1381 -0.0609 58  THR B C   
4818 O O   . THR B 60  ? 0.9389 0.8510 0.8843 0.0273  -0.1146 -0.0342 58  THR B O   
4819 C CB  . THR B 60  ? 0.9801 1.0004 0.9230 0.0154  -0.1735 -0.0684 58  THR B CB  
4820 O OG1 . THR B 60  ? 0.9715 1.0153 0.9732 -0.0269 -0.1797 -0.0740 58  THR B OG1 
4821 C CG2 . THR B 60  ? 0.9912 1.0636 0.8974 0.0373  -0.2051 -0.0877 58  THR B CG2 
4822 N N   . ASP B 61  ? 0.8636 0.7153 0.8093 -0.0280 -0.1406 -0.0698 59  ASP B N   
4823 C CA  . ASP B 61  ? 0.8901 0.7058 0.8493 -0.0275 -0.1213 -0.0495 59  ASP B CA  
4824 C C   . ASP B 61  ? 0.8659 0.6489 0.8001 0.0073  -0.1103 -0.0504 59  ASP B C   
4825 O O   . ASP B 61  ? 0.9533 0.6974 0.8508 0.0182  -0.1186 -0.0731 59  ASP B O   
4826 C CB  . ASP B 61  ? 0.8726 0.6356 0.8323 -0.0644 -0.1264 -0.0539 59  ASP B CB  
4827 C CG  . ASP B 61  ? 0.8959 0.6256 0.8571 -0.0594 -0.1121 -0.0317 59  ASP B CG  
4828 O OD1 . ASP B 61  ? 0.9226 0.6689 0.8911 -0.0294 -0.1024 -0.0216 59  ASP B OD1 
4829 O OD2 . ASP B 61  ? 0.9715 0.6599 0.9259 -0.0868 -0.1104 -0.0244 59  ASP B OD2 
4830 N N   . VAL B 62  ? 0.8249 0.6272 0.7845 0.0242  -0.0907 -0.0298 60  VAL B N   
4831 C CA  . VAL B 62  ? 0.8598 0.6531 0.8153 0.0549  -0.0764 -0.0313 60  VAL B CA  
4832 C C   . VAL B 62  ? 0.9424 0.6815 0.8869 0.0603  -0.0858 -0.0419 60  VAL B C   
4833 O O   . VAL B 62  ? 0.9589 0.6840 0.8919 0.0895  -0.0802 -0.0539 60  VAL B O   
4834 C CB  . VAL B 62  ? 0.7898 0.6226 0.7888 0.0628  -0.0532 -0.0108 60  VAL B CB  
4835 C CG1 . VAL B 62  ? 0.7213 0.5512 0.7502 0.0444  -0.0585 -0.0039 60  VAL B CG1 
4836 C CG2 . VAL B 62  ? 0.8628 0.7044 0.8732 0.0894  -0.0335 -0.0138 60  VAL B CG2 
4837 N N   . THR B 63  ? 0.8714 0.5784 0.8158 0.0372  -0.0974 -0.0355 61  THR B N   
4838 C CA  . THR B 63  ? 0.9320 0.5768 0.8556 0.0488  -0.1070 -0.0376 61  THR B CA  
4839 C C   . THR B 63  ? 0.9943 0.5716 0.8747 0.0543  -0.1169 -0.0605 61  THR B C   
4840 O O   . THR B 63  ? 1.0521 0.5741 0.9122 0.0815  -0.1219 -0.0657 61  THR B O   
4841 C CB  . THR B 63  ? 0.9604 0.5794 0.8787 0.0231  -0.1121 -0.0190 61  THR B CB  
4842 O OG1 . THR B 63  ? 1.0475 0.6511 0.9563 -0.0171 -0.1137 -0.0210 61  THR B OG1 
4843 C CG2 . THR B 63  ? 0.8492 0.5302 0.8040 0.0212  -0.1036 -0.0051 61  THR B CG2 
4844 N N   . GLN B 64  ? 0.9845 0.5655 0.8505 0.0323  -0.1225 -0.0778 62  GLN B N   
4845 C CA  . GLN B 64  ? 1.0952 0.6084 0.9193 0.0296  -0.1351 -0.1092 62  GLN B CA  
4846 C C   . GLN B 64  ? 1.0958 0.6406 0.8965 0.0579  -0.1332 -0.1354 62  GLN B C   
4847 O O   . GLN B 64  ? 1.1555 0.6716 0.9216 0.0472  -0.1483 -0.1690 62  GLN B O   
4848 C CB  . GLN B 64  ? 1.0235 0.5157 0.8488 -0.0247 -0.1480 -0.1175 62  GLN B CB  
4849 C CG  . GLN B 64  ? 1.0390 0.5335 0.8912 -0.0582 -0.1404 -0.0853 62  GLN B CG  
4850 C CD  . GLN B 64  ? 1.1686 0.5700 0.9924 -0.0510 -0.1365 -0.0671 62  GLN B CD  
4851 O OE1 . GLN B 64  ? 1.0973 0.4021 0.8874 -0.0615 -0.1418 -0.0802 62  GLN B OE1 
4852 N NE2 . GLN B 64  ? 1.1257 0.5508 0.9585 -0.0311 -0.1288 -0.0376 62  GLN B NE2 
4853 N N   . LEU B 65  ? 1.0171 0.6198 0.8335 0.0925  -0.1132 -0.1223 63  LEU B N   
4854 C CA  . LEU B 65  ? 1.0557 0.6948 0.8425 0.1206  -0.1024 -0.1378 63  LEU B CA  
4855 C C   . LEU B 65  ? 1.0271 0.6706 0.8168 0.1669  -0.0778 -0.1401 63  LEU B C   
4856 O O   . LEU B 65  ? 0.9425 0.5965 0.7777 0.1763  -0.0689 -0.1222 63  LEU B O   
4857 C CB  . LEU B 65  ? 1.0063 0.7234 0.8107 0.1142  -0.0923 -0.1131 63  LEU B CB  
4858 C CG  . LEU B 65  ? 1.0337 0.7712 0.8298 0.0829  -0.1179 -0.1201 63  LEU B CG  
4859 C CD1 . LEU B 65  ? 1.0284 0.8363 0.8444 0.0882  -0.1065 -0.0890 63  LEU B CD1 
4860 C CD2 . LEU B 65  ? 1.0852 0.8024 0.8212 0.0880  -0.1399 -0.1628 63  LEU B CD2 
4861 N N   . TYR B 66  ? 1.1248 0.7700 0.8665 0.1973  -0.0671 -0.1650 64  TYR B N   
4862 C CA  . TYR B 66  ? 1.1181 0.7737 0.8611 0.2448  -0.0389 -0.1740 64  TYR B CA  
4863 C C   . TYR B 66  ? 1.0996 0.8095 0.8057 0.2688  -0.0087 -0.1738 64  TYR B C   
4864 O O   . TYR B 66  ? 1.2096 0.9203 0.8579 0.2609  -0.0218 -0.1844 64  TYR B O   
4865 C CB  . TYR B 66  ? 1.1486 0.7191 0.8504 0.2696  -0.0529 -0.2143 64  TYR B CB  
4866 C CG  . TYR B 66  ? 1.2060 0.6996 0.9231 0.2485  -0.0804 -0.2107 64  TYR B CG  
4867 C CD1 . TYR B 66  ? 1.1946 0.6377 0.8921 0.1996  -0.1079 -0.2158 64  TYR B CD1 
4868 C CD2 . TYR B 66  ? 1.1851 0.6579 0.9341 0.2797  -0.0779 -0.2017 64  TYR B CD2 
4869 C CE1 . TYR B 66  ? 1.2994 0.6647 1.0031 0.1782  -0.1245 -0.2062 64  TYR B CE1 
4870 C CE2 . TYR B 66  ? 1.1880 0.5805 0.9340 0.2662  -0.1011 -0.1915 64  TYR B CE2 
4871 C CZ  . TYR B 66  ? 1.2739 0.6074 0.9936 0.2137  -0.1206 -0.1914 64  TYR B CZ  
4872 O OH  . TYR B 66  ? 1.3368 0.5839 1.0470 0.1977  -0.1352 -0.1748 64  TYR B OH  
4873 N N   . LEU B 67  ? 1.1318 0.8920 0.8718 0.2989  0.0323  -0.1610 65  LEU B N   
4874 C CA  . LEU B 67  ? 1.1831 0.9912 0.8842 0.3251  0.0735  -0.1546 65  LEU B CA  
4875 C C   . LEU B 67  ? 1.2735 1.0556 0.9126 0.3719  0.0857  -0.1980 65  LEU B C   
4876 O O   . LEU B 67  ? 1.2812 1.0577 0.9581 0.4000  0.0963  -0.2147 65  LEU B O   
4877 C CB  . LEU B 67  ? 1.1643 1.0445 0.9430 0.3255  0.1210  -0.1172 65  LEU B CB  
4878 C CG  . LEU B 67  ? 1.2573 1.1820 0.9959 0.3549  0.1771  -0.1058 65  LEU B CG  
4879 C CD1 . LEU B 67  ? 1.2718 1.1982 0.9462 0.3427  0.1801  -0.0752 65  LEU B CD1 
4880 C CD2 . LEU B 67  ? 1.1585 1.1530 0.9920 0.3578  0.2305  -0.0839 65  LEU B CD2 
4881 N N   . GLY B 68  ? 1.3624 1.1312 0.9041 0.3851  0.0818  -0.2191 66  GLY B N   
4882 C CA  . GLY B 68  ? 1.4028 1.1471 0.8696 0.4327  0.0964  -0.2655 66  GLY B CA  
4883 C C   . GLY B 68  ? 1.5038 1.3029 0.9002 0.4620  0.1416  -0.2513 66  GLY B C   
4884 O O   . GLY B 68  ? 1.5020 1.3078 0.8307 0.4513  0.1244  -0.2418 66  GLY B O   
4885 N N   . GLY B 69  ? 1.5308 1.3738 0.9412 0.5015  0.2008  -0.2479 67  GLY B N   
4886 C CA  . GLY B 69  ? 1.4399 1.3362 0.7858 0.5267  0.2565  -0.2221 67  GLY B CA  
4887 C C   . GLY B 69  ? 1.4948 1.4368 0.8980 0.4899  0.2787  -0.1530 67  GLY B C   
4888 O O   . GLY B 69  ? 1.4636 1.4450 0.9822 0.4705  0.3062  -0.1247 67  GLY B O   
4889 N N   . MET B 70  ? 1.5155 1.4516 0.8393 0.4824  0.2640  -0.1286 68  MET B N   
4890 C CA  . MET B 70  ? 1.4392 1.3976 0.8064 0.4504  0.2769  -0.0648 68  MET B CA  
4891 C C   . MET B 70  ? 1.4735 1.4022 0.8282 0.4212  0.2066  -0.0667 68  MET B C   
4892 O O   . MET B 70  ? 1.4476 1.3868 0.8242 0.4013  0.2085  -0.0186 68  MET B O   
4893 C CB  . MET B 70  ? 1.5079 1.4929 0.7934 0.4775  0.3383  -0.0176 68  MET B CB  
4894 C CG  . MET B 70  ? 1.5317 1.5529 0.8129 0.5073  0.4099  -0.0196 68  MET B CG  
4895 S SD  . MET B 70  ? 1.7173 1.7953 1.1712 0.4780  0.4746  0.0096  68  MET B SD  
4896 C CE  . MET B 70  ? 1.4691 1.5377 0.9596 0.4351  0.4920  0.0855  68  MET B CE  
4897 N N   . SER B 71  ? 1.4733 1.3645 0.7978 0.4179  0.1479  -0.1226 69  SER B N   
4898 C CA  . SER B 71  ? 1.4527 1.3251 0.7752 0.3867  0.0813  -0.1351 69  SER B CA  
4899 C C   . SER B 71  ? 1.3958 1.2391 0.8214 0.3455  0.0521  -0.1477 69  SER B C   
4900 O O   . SER B 71  ? 1.3618 1.1937 0.8451 0.3488  0.0733  -0.1548 69  SER B O   
4901 C CB  . SER B 71  ? 1.4769 1.3280 0.6912 0.4052  0.0371  -0.1926 69  SER B CB  
4902 O OG  . SER B 71  ? 1.5860 1.4091 0.7548 0.4383  0.0575  -0.2386 69  SER B OG  
4903 N N   . TYR B 72  ? 1.3523 1.1886 0.7989 0.3099  0.0034  -0.1496 70  TYR B N   
4904 C CA  . TYR B 72  ? 1.3176 1.1266 0.8501 0.2691  -0.0211 -0.1528 70  TYR B CA  
4905 C C   . TYR B 72  ? 1.3199 1.0876 0.8279 0.2440  -0.0753 -0.2012 70  TYR B C   
4906 O O   . TYR B 72  ? 1.3024 1.0909 0.7590 0.2419  -0.1061 -0.2190 70  TYR B O   
4907 C CB  . TYR B 72  ? 1.3164 1.1594 0.9164 0.2414  -0.0184 -0.1045 70  TYR B CB  
4908 C CG  . TYR B 72  ? 1.2531 1.1313 0.8741 0.2582  0.0343  -0.0565 70  TYR B CG  
4909 C CD1 . TYR B 72  ? 1.2082 1.0919 0.8969 0.2573  0.0700  -0.0452 70  TYR B CD1 
4910 C CD2 . TYR B 72  ? 1.1999 1.1054 0.7763 0.2743  0.0476  -0.0220 70  TYR B CD2 
4911 C CE1 . TYR B 72  ? 1.2106 1.1262 0.9303 0.2628  0.1210  -0.0049 70  TYR B CE1 
4912 C CE2 . TYR B 72  ? 1.2227 1.1446 0.8179 0.2843  0.1018  0.0254  70  TYR B CE2 
4913 C CZ  . TYR B 72  ? 1.1898 1.1168 0.8613 0.2736  0.1400  0.0319  70  TYR B CZ  
4914 O OH  . TYR B 72  ? 1.1589 1.1021 0.8611 0.2739  0.1966  0.0755  70  TYR B OH  
4915 N N   . TYR B 73  ? 1.2971 1.0063 0.8431 0.2248  -0.0874 -0.2221 71  TYR B N   
4916 C CA  . TYR B 73  ? 1.3281 0.9801 0.8557 0.1947  -0.1307 -0.2687 71  TYR B CA  
4917 C C   . TYR B 73  ? 1.2725 0.8759 0.8676 0.1580  -0.1386 -0.2560 71  TYR B C   
4918 O O   . TYR B 73  ? 1.1977 0.8038 0.8398 0.1681  -0.1144 -0.2233 71  TYR B O   
4919 C CB  . TYR B 73  ? 1.4013 0.9925 0.8566 0.2250  -0.1334 -0.3250 71  TYR B CB  
4920 C CG  . TYR B 73  ? 1.4556 1.0888 0.8256 0.2704  -0.1191 -0.3401 71  TYR B CG  
4921 C CD1 . TYR B 73  ? 1.4725 1.1278 0.7763 0.2654  -0.1558 -0.3741 71  TYR B CD1 
4922 C CD2 . TYR B 73  ? 1.4440 1.0997 0.7983 0.3193  -0.0682 -0.3218 71  TYR B CD2 
4923 C CE1 . TYR B 73  ? 1.5569 1.2483 0.7649 0.3128  -0.1431 -0.3857 71  TYR B CE1 
4924 C CE2 . TYR B 73  ? 1.4979 1.1889 0.7634 0.3622  -0.0472 -0.3309 71  TYR B CE2 
4925 C CZ  . TYR B 73  ? 1.5922 1.2966 0.7763 0.3613  -0.0854 -0.3614 71  TYR B CZ  
4926 O OH  . TYR B 73  ? 1.5893 1.3270 0.6677 0.4095  -0.0653 -0.3684 71  TYR B OH  
4927 N N   . CYS B 74  ? 1.3112 0.8726 0.9095 0.1141  -0.1727 -0.2832 72  CYS B N   
4928 C CA  . CYS B 74  ? 1.3149 0.8139 0.9586 0.0776  -0.1778 -0.2718 72  CYS B CA  
4929 C C   . CYS B 74  ? 1.3794 0.7686 0.9888 0.0971  -0.1759 -0.3020 72  CYS B C   
4930 O O   . CYS B 74  ? 1.3536 0.7251 0.9122 0.1408  -0.1682 -0.3332 72  CYS B O   
4931 C CB  . CYS B 74  ? 1.2540 0.7598 0.9243 0.0166  -0.2068 -0.2840 72  CYS B CB  
4932 S SG  . CYS B 74  ? 1.4174 0.8774 1.0362 -0.0062 -0.2445 -0.3601 72  CYS B SG  
4933 N N   . LYS B 75  ? 1.3681 0.6772 0.9992 0.0690  -0.1803 -0.2916 73  LYS B N   
4934 C CA  . LYS B 75  ? 1.4841 0.6793 1.0830 0.0918  -0.1772 -0.3128 73  LYS B CA  
4935 C C   . LYS B 75  ? 1.5212 0.6793 1.0872 0.0719  -0.1889 -0.3645 73  LYS B C   
4936 O O   . LYS B 75  ? 1.5875 0.6976 1.1235 0.1068  -0.1776 -0.3881 73  LYS B O   
4937 C CB  . LYS B 75  ? 1.4255 0.5646 1.0584 0.0650  -0.1700 -0.2723 73  LYS B CB  
4938 C CG  . LYS B 75  ? 1.4982 0.5397 1.1179 0.0514  -0.1648 -0.2869 73  LYS B CG  
4939 C CD  . LYS B 75  ? 1.6068 0.6217 1.2495 -0.0242 -0.1713 -0.2932 73  LYS B CD  
4940 C CE  . LYS B 75  ? 1.6404 0.5473 1.2743 -0.0386 -0.1609 -0.3091 73  LYS B CE  
4941 N NZ  . LYS B 75  ? 1.7374 0.6134 1.3372 -0.0225 -0.1672 -0.3694 73  LYS B NZ  
4942 N N   . SER B 76  ? 1.5411 0.7295 1.1184 0.0165  -0.2118 -0.3853 74  SER B N   
4943 C CA  . SER B 76  ? 1.5611 0.7215 1.1194 -0.0134 -0.2255 -0.4387 74  SER B CA  
4944 C C   . SER B 76  ? 1.6014 0.8105 1.0993 0.0255  -0.2362 -0.4823 74  SER B C   
4945 O O   . SER B 76  ? 1.7120 0.8889 1.1812 0.0133  -0.2446 -0.5320 74  SER B O   
4946 C CB  . SER B 76  ? 1.5779 0.7736 1.1864 -0.0898 -0.2449 -0.4458 74  SER B CB  
4947 O OG  . SER B 76  ? 1.6233 0.7646 1.2803 -0.1285 -0.2266 -0.4085 74  SER B OG  
4948 N N   . HIS B 77  ? 1.5275 0.8111 1.0011 0.0723  -0.2321 -0.4648 75  HIS B N   
4949 C CA  . HIS B 77  ? 1.6256 0.9658 1.0325 0.1124  -0.2360 -0.4963 75  HIS B CA  
4950 C C   . HIS B 77  ? 1.6440 1.0003 1.0181 0.1847  -0.1987 -0.4753 75  HIS B C   
4951 O O   . HIS B 77  ? 1.6920 1.1182 1.0152 0.2226  -0.1898 -0.4762 75  HIS B O   
4952 C CB  . HIS B 77  ? 1.5654 1.0090 0.9702 0.0951  -0.2653 -0.4946 75  HIS B CB  
4953 C CG  . HIS B 77  ? 1.5717 1.0293 1.0232 0.0239  -0.3000 -0.5180 75  HIS B CG  
4954 N ND1 . HIS B 77  ? 1.5350 1.0318 1.0591 -0.0218 -0.3127 -0.4889 75  HIS B ND1 
4955 C CD2 . HIS B 77  ? 1.6495 1.0936 1.0904 -0.0116 -0.3210 -0.5695 75  HIS B CD2 
4956 C CE1 . HIS B 77  ? 1.5021 1.0167 1.0642 -0.0823 -0.3365 -0.5194 75  HIS B CE1 
4957 N NE2 . HIS B 77  ? 1.6217 1.1022 1.1332 -0.0792 -0.3433 -0.5697 75  HIS B NE2 
4958 N N   . LYS B 78  ? 1.6106 0.9113 1.0166 0.2053  -0.1729 -0.4529 76  LYS B N   
4959 C CA  . LYS B 78  ? 1.6170 0.9583 1.0166 0.2683  -0.1344 -0.4303 76  LYS B CA  
4960 C C   . LYS B 78  ? 1.6004 0.9174 0.9615 0.3129  -0.1118 -0.4614 76  LYS B C   
4961 O O   . LYS B 78  ? 1.6927 0.9313 1.0476 0.2995  -0.1225 -0.4914 76  LYS B O   
4962 C CB  . LYS B 78  ? 1.5064 0.8388 0.9777 0.2714  -0.1193 -0.3826 76  LYS B CB  
4963 C CG  . LYS B 78  ? 1.5045 0.7588 1.0014 0.2821  -0.1139 -0.3806 76  LYS B CG  
4964 C CD  . LYS B 78  ? 1.3725 0.6377 0.9342 0.2849  -0.1074 -0.3305 76  LYS B CD  
4965 C CE  . LYS B 78  ? 1.4296 0.6541 1.0153 0.3188  -0.0963 -0.3204 76  LYS B CE  
4966 N NZ  . LYS B 78  ? 1.6084 0.8873 1.1975 0.3803  -0.0667 -0.3332 76  LYS B NZ  
4967 N N   . PRO B 79  ? 1.5950 0.9790 0.9310 0.3649  -0.0757 -0.4541 77  PRO B N   
4968 C CA  . PRO B 79  ? 1.6867 1.0586 0.9980 0.4115  -0.0470 -0.4787 77  PRO B CA  
4969 C C   . PRO B 79  ? 1.6717 1.0081 1.0494 0.4325  -0.0317 -0.4612 77  PRO B C   
4970 O O   . PRO B 79  ? 1.6738 1.0159 1.1146 0.4185  -0.0363 -0.4225 77  PRO B O   
4971 C CB  . PRO B 79  ? 1.6664 1.1371 0.9480 0.4524  -0.0051 -0.4603 77  PRO B CB  
4972 C CG  . PRO B 79  ? 1.5984 1.1211 0.9275 0.4376  0.0004  -0.4115 77  PRO B CG  
4973 C CD  . PRO B 79  ? 1.5427 1.0188 0.8708 0.3821  -0.0533 -0.4206 77  PRO B CD  
4974 N N   . PRO B 80  ? 1.7707 1.0728 1.1351 0.4687  -0.0153 -0.4888 78  PRO B N   
4975 C CA  . PRO B 80  ? 1.7677 1.0407 1.1950 0.4938  -0.0059 -0.4708 78  PRO B CA  
4976 C C   . PRO B 80  ? 1.7069 1.0807 1.2042 0.5256  0.0259  -0.4303 78  PRO B C   
4977 O O   . PRO B 80  ? 1.6860 1.0573 1.2492 0.5257  0.0178  -0.3994 78  PRO B O   
4978 C CB  . PRO B 80  ? 1.9127 1.1347 1.3006 0.5306  0.0069  -0.5163 78  PRO B CB  
4979 C CG  . PRO B 80  ? 1.9967 1.1892 1.3020 0.5039  -0.0104 -0.5620 78  PRO B CG  
4980 C CD  . PRO B 80  ? 1.9009 1.1870 1.1918 0.4903  -0.0072 -0.5388 78  PRO B CD  
4981 N N   . ILE B 81  ? 1.6456 1.1117 1.1322 0.5498  0.0634  -0.4284 79  ILE B N   
4982 C CA  . ILE B 81  ? 1.5652 1.1387 1.1306 0.5689  0.0998  -0.3908 79  ILE B CA  
4983 C C   . ILE B 81  ? 1.5183 1.1276 1.0986 0.5316  0.0916  -0.3563 79  ILE B C   
4984 O O   . ILE B 81  ? 1.5447 1.1881 1.0724 0.5237  0.1057  -0.3529 79  ILE B O   
4985 C CB  . ILE B 81  ? 1.5936 1.2487 1.1476 0.6070  0.1541  -0.3994 79  ILE B CB  
4986 C CG1 . ILE B 81  ? 1.7143 1.3296 1.2535 0.6477  0.1621  -0.4379 79  ILE B CG1 
4987 C CG2 . ILE B 81  ? 1.4946 1.2666 1.1473 0.6141  0.1956  -0.3601 79  ILE B CG2 
4988 C CD1 . ILE B 81  ? 1.7651 1.4661 1.3054 0.6870  0.2204  -0.4460 79  ILE B CD1 
4989 N N   . SER B 82  ? 1.3847 0.9853 1.0319 0.5117  0.0687  -0.3290 80  SER B N   
4990 C CA  . SER B 82  ? 1.3887 1.0120 1.0536 0.4768  0.0580  -0.2992 80  SER B CA  
4991 C C   . SER B 82  ? 1.2261 0.8736 0.9856 0.4697  0.0464  -0.2678 80  SER B C   
4992 O O   . SER B 82  ? 1.2935 0.9093 1.0810 0.4849  0.0310  -0.2706 80  SER B O   
4993 C CB  . SER B 82  ? 1.3867 0.9320 0.9891 0.4296  0.0147  -0.3104 80  SER B CB  
4994 O OG  . SER B 82  ? 1.4957 0.9398 1.0825 0.4215  -0.0174 -0.3320 80  SER B OG  
4995 N N   . PHE B 83  ? 1.1089 0.8264 0.9238 0.4284  0.0521  -0.2274 81  PHE B N   
4996 C CA  . PHE B 83  ? 1.0541 0.8012 0.9526 0.4153  0.0364  -0.2011 81  PHE B CA  
4997 C C   . PHE B 83  ? 1.0882 0.8291 0.9912 0.3548  0.0145  -0.1710 81  PHE B C   
4998 O O   . PHE B 83  ? 1.0256 0.7929 0.9075 0.3276  0.0284  -0.1584 81  PHE B O   
4999 C CB  . PHE B 83  ? 1.0168 0.8800 1.0105 0.4361  0.0736  -0.1902 81  PHE B CB  
5000 C CG  . PHE B 83  ? 0.9688 0.9091 0.9931 0.4007  0.1108  -0.1623 81  PHE B CG  
5001 C CD1 . PHE B 83  ? 1.0316 0.9940 1.1019 0.3522  0.0987  -0.1325 81  PHE B CD1 
5002 C CD2 . PHE B 83  ? 1.0431 1.0290 1.0474 0.4200  0.1626  -0.1650 81  PHE B CD2 
5003 C CE1 . PHE B 83  ? 1.0096 1.0260 1.1064 0.3229  0.1356  -0.1057 81  PHE B CE1 
5004 C CE2 . PHE B 83  ? 1.0495 1.0914 1.0753 0.3896  0.2020  -0.1322 81  PHE B CE2 
5005 C CZ  . PHE B 83  ? 0.9818 1.0341 1.0560 0.3409  0.1879  -0.1024 81  PHE B CZ  
5006 N N   . PRO B 84  ? 1.0155 0.7208 0.9396 0.3386  -0.0185 -0.1584 82  PRO B N   
5007 C CA  . PRO B 84  ? 0.9910 0.6878 0.9154 0.2846  -0.0368 -0.1336 82  PRO B CA  
5008 C C   . PRO B 84  ? 0.9160 0.7023 0.8976 0.2613  -0.0130 -0.1093 82  PRO B C   
5009 O O   . PRO B 84  ? 0.8663 0.7224 0.9141 0.2768  0.0080  -0.1057 82  PRO B O   
5010 C CB  . PRO B 84  ? 0.9724 0.6245 0.9089 0.2855  -0.0675 -0.1235 82  PRO B CB  
5011 C CG  . PRO B 84  ? 0.9386 0.6285 0.9195 0.3392  -0.0619 -0.1335 82  PRO B CG  
5012 C CD  . PRO B 84  ? 0.9803 0.6589 0.9284 0.3747  -0.0384 -0.1627 82  PRO B CD  
5013 N N   . LEU B 85  ? 0.8718 0.6554 0.8320 0.2236  -0.0157 -0.0945 83  LEU B N   
5014 C CA  . LEU B 85  ? 0.9016 0.7482 0.9076 0.2021  0.0071  -0.0694 83  LEU B CA  
5015 C C   . LEU B 85  ? 0.8400 0.7057 0.9053 0.1812  -0.0070 -0.0570 83  LEU B C   
5016 O O   . LEU B 85  ? 0.8650 0.7861 0.9908 0.1711  0.0139  -0.0461 83  LEU B O   
5017 C CB  . LEU B 85  ? 0.8527 0.6900 0.8142 0.1790  0.0055  -0.0576 83  LEU B CB  
5018 C CG  . LEU B 85  ? 0.9733 0.8080 0.8689 0.2004  0.0194  -0.0680 83  LEU B CG  
5019 C CD1 . LEU B 85  ? 0.9989 0.8330 0.8551 0.1809  0.0048  -0.0576 83  LEU B CD1 
5020 C CD2 . LEU B 85  ? 1.0138 0.8992 0.9281 0.2240  0.0678  -0.0557 83  LEU B CD2 
5021 N N   . CYS B 86  ? 0.8299 0.6467 0.8746 0.1734  -0.0403 -0.0594 84  CYS B N   
5022 C CA  . CYS B 86  ? 0.8769 0.7055 0.9555 0.1561  -0.0571 -0.0489 84  CYS B CA  
5023 C C   . CYS B 86  ? 0.8908 0.6973 0.9691 0.1861  -0.0814 -0.0572 84  CYS B C   
5024 O O   . CYS B 86  ? 1.0350 0.7674 1.0589 0.1884  -0.1021 -0.0548 84  CYS B O   
5025 C CB  . CYS B 86  ? 0.8131 0.6063 0.8573 0.1208  -0.0698 -0.0365 84  CYS B CB  
5026 S SG  . CYS B 86  ? 0.8407 0.6476 0.9086 0.0992  -0.0838 -0.0250 84  CYS B SG  
5027 N N   . ALA B 87  ? 0.8164 0.6872 0.9577 0.2093  -0.0789 -0.0658 85  ALA B N   
5028 C CA  . ALA B 87  ? 0.7134 0.5769 0.8586 0.2482  -0.1072 -0.0728 85  ALA B CA  
5029 C C   . ALA B 87  ? 0.7568 0.7236 0.9947 0.2598  -0.1086 -0.0852 85  ALA B C   
5030 O O   . ALA B 87  ? 0.7547 0.7899 1.0563 0.2394  -0.0781 -0.0901 85  ALA B O   
5031 C CB  . ALA B 87  ? 0.7990 0.6122 0.9072 0.2921  -0.1060 -0.0853 85  ALA B CB  
5032 N N   . ASN B 88  ? 0.7078 0.6843 0.9527 0.2929  -0.1448 -0.0897 86  ASN B N   
5033 C CA  . ASN B 88  ? 0.7153 0.8010 1.0539 0.3067  -0.1590 -0.1088 86  ASN B CA  
5034 C C   . ASN B 88  ? 0.6487 0.7814 1.0295 0.2556  -0.1582 -0.1124 86  ASN B C   
5035 O O   . ASN B 88  ? 0.6681 0.8987 1.1469 0.2446  -0.1532 -0.1339 86  ASN B O   
5036 C CB  . ASN B 88  ? 0.6768 0.8468 1.1000 0.3284  -0.1274 -0.1282 86  ASN B CB  
5037 C CG  . ASN B 88  ? 0.6535 0.8406 1.0886 0.3986  -0.1492 -0.1412 86  ASN B CG  
5038 O OD1 . ASN B 88  ? 0.7469 0.8730 1.1159 0.4249  -0.1864 -0.1293 86  ASN B OD1 
5039 N ND2 . ASN B 88  ? 0.6529 0.9164 1.1568 0.4176  -0.1156 -0.1570 86  ASN B ND2 
5040 N N   . GLY B 89  ? 0.6872 0.7517 0.9998 0.2232  -0.1617 -0.0947 87  GLY B N   
5041 C CA  . GLY B 89  ? 0.6460 0.7421 0.9896 0.1800  -0.1593 -0.1012 87  GLY B CA  
5042 C C   . GLY B 89  ? 0.6077 0.7286 1.0037 0.1431  -0.1132 -0.1009 87  GLY B C   
5043 O O   . GLY B 89  ? 0.5581 0.7160 1.0071 0.1105  -0.1062 -0.1133 87  GLY B O   
5044 N N   . GLN B 90  ? 0.6189 0.7127 0.9936 0.1492  -0.0815 -0.0873 88  GLN B N   
5045 C CA  . GLN B 90  ? 0.5976 0.7098 1.0075 0.1237  -0.0346 -0.0795 88  GLN B CA  
5046 C C   . GLN B 90  ? 0.6874 0.7359 1.0187 0.1286  -0.0168 -0.0591 88  GLN B C   
5047 O O   . GLN B 90  ? 0.7101 0.7209 0.9891 0.1568  -0.0306 -0.0609 88  GLN B O   
5048 C CB  . GLN B 90  ? 0.5566 0.7502 1.0556 0.1342  -0.0072 -0.0936 88  GLN B CB  
5049 C CG  . GLN B 90  ? 0.5241 0.8032 1.1264 0.1205  -0.0219 -0.1210 88  GLN B CG  
5050 C CD  . GLN B 90  ? 0.5465 0.9141 1.2547 0.1144  0.0205  -0.1320 88  GLN B CD  
5051 O OE1 . GLN B 90  ? 0.5358 0.9328 1.2520 0.1505  0.0363  -0.1334 88  GLN B OE1 
5052 N NE2 . GLN B 90  ? 0.5676 0.9758 1.3595 0.0675  0.0428  -0.1414 88  GLN B NE2 
5053 N N   . VAL B 91  ? 0.5639 0.5983 0.8863 0.1032  0.0114  -0.0421 89  VAL B N   
5054 C CA  . VAL B 91  ? 0.6346 0.6276 0.8895 0.1093  0.0270  -0.0257 89  VAL B CA  
5055 C C   . VAL B 91  ? 0.7362 0.7640 1.0147 0.1200  0.0721  -0.0196 89  VAL B C   
5056 O O   . VAL B 91  ? 0.6151 0.6849 0.9635 0.1029  0.1017  -0.0159 89  VAL B O   
5057 C CB  . VAL B 91  ? 0.6765 0.6383 0.9015 0.0849  0.0276  -0.0077 89  VAL B CB  
5058 C CG1 . VAL B 91  ? 0.7220 0.6599 0.8847 0.0951  0.0401  0.0068  89  VAL B CG1 
5059 C CG2 . VAL B 91  ? 0.7014 0.6347 0.9009 0.0743  -0.0088 -0.0130 89  VAL B CG2 
5060 N N   . PHE B 92  ? 0.7666 0.7753 0.9862 0.1463  0.0804  -0.0202 90  PHE B N   
5061 C CA  . PHE B 92  ? 0.7414 0.7857 0.9720 0.1624  0.1281  -0.0144 90  PHE B CA  
5062 C C   . PHE B 92  ? 0.7664 0.8078 0.9918 0.1423  0.1672  0.0180  90  PHE B C   
5063 O O   . PHE B 92  ? 0.7496 0.7496 0.9122 0.1387  0.1564  0.0345  90  PHE B O   
5064 C CB  . PHE B 92  ? 0.7953 0.8136 0.9479 0.1986  0.1277  -0.0270 90  PHE B CB  
5065 C CG  . PHE B 92  ? 0.8726 0.9292 1.0226 0.2199  0.1822  -0.0208 90  PHE B CG  
5066 C CD1 . PHE B 92  ? 0.8236 0.9510 1.0658 0.2215  0.2177  -0.0244 90  PHE B CD1 
5067 C CD2 . PHE B 92  ? 0.9438 0.9738 1.0008 0.2375  0.1993  -0.0116 90  PHE B CD2 
5068 C CE1 . PHE B 92  ? 0.8833 1.0515 1.1265 0.2384  0.2774  -0.0157 90  PHE B CE1 
5069 C CE2 . PHE B 92  ? 1.0080 1.0724 1.0500 0.2596  0.2555  -0.0023 90  PHE B CE2 
5070 C CZ  . PHE B 92  ? 0.9638 1.0959 1.0998 0.2589  0.2989  -0.0023 90  PHE B CZ  
5071 N N   . GLY B 93  ? 0.7585 0.8449 1.0534 0.1305  0.2139  0.0278  91  GLY B N   
5072 C CA  . GLY B 93  ? 0.7258 0.7977 1.0155 0.1136  0.2616  0.0647  91  GLY B CA  
5073 C C   . GLY B 93  ? 0.7816 0.9106 1.1649 0.0962  0.3169  0.0684  91  GLY B C   
5074 O O   . GLY B 93  ? 0.7655 0.9582 1.2238 0.0996  0.3125  0.0385  91  GLY B O   
5075 N N   . LEU B 94  ? 0.7353 0.8421 1.1176 0.0780  0.3707  0.1067  92  LEU B N   
5076 C CA  . LEU B 94  ? 0.8045 0.9633 1.2777 0.0544  0.4351  0.1147  92  LEU B CA  
5077 C C   . LEU B 94  ? 0.7707 0.9685 1.3763 0.0080  0.4208  0.0857  92  LEU B C   
5078 O O   . LEU B 94  ? 0.6174 0.7911 1.2287 -0.0030 0.3655  0.0650  92  LEU B O   
5079 C CB  . LEU B 94  ? 0.9195 1.0277 1.3463 0.0463  0.5024  0.1706  92  LEU B CB  
5080 C CG  . LEU B 94  ? 0.9408 1.0395 1.2516 0.0921  0.5368  0.1985  92  LEU B CG  
5081 C CD1 . LEU B 94  ? 0.9628 1.0085 1.2283 0.0845  0.6080  0.2612  92  LEU B CD1 
5082 C CD2 . LEU B 94  ? 0.9172 1.1008 1.2693 0.1108  0.5624  0.1706  92  LEU B CD2 
5083 N N   . TYR B 95  ? 0.7193 0.9848 1.4337 -0.0200 0.4729  0.0814  93  TYR B N   
5084 C CA  . TYR B 95  ? 0.6844 0.9971 1.5296 -0.0689 0.4582  0.0470  93  TYR B CA  
5085 C C   . TYR B 95  ? 0.6991 1.0605 1.5813 -0.0540 0.3809  -0.0036 93  TYR B C   
5086 O O   . TYR B 95  ? 0.6780 1.0495 1.6262 -0.0868 0.3461  -0.0331 93  TYR B O   
5087 C CB  . TYR B 95  ? 0.7572 0.9820 1.5959 -0.1118 0.4657  0.0654  93  TYR B CB  
5088 C CG  . TYR B 95  ? 0.8316 0.9805 1.5944 -0.1115 0.5271  0.1223  93  TYR B CG  
5089 C CD1 . TYR B 95  ? 0.8576 1.0214 1.6630 -0.1404 0.5763  0.1335  93  TYR B CD1 
5090 C CD2 . TYR B 95  ? 0.9009 0.9668 1.5469 -0.0797 0.5336  0.1657  93  TYR B CD2 
5091 C CE1 . TYR B 95  ? 0.9645 1.0556 1.6944 -0.1359 0.6307  0.1876  93  TYR B CE1 
5092 C CE2 . TYR B 95  ? 0.9856 0.9831 1.5515 -0.0700 0.5815  0.2183  93  TYR B CE2 
5093 C CZ  . TYR B 95  ? 0.9868 0.9937 1.5934 -0.0974 0.6305  0.2297  93  TYR B CZ  
5094 O OH  . TYR B 95  ? 1.1610 1.0980 1.6844 -0.0848 0.6780  0.2838  93  TYR B OH  
5095 N N   . LYS B 96  ? 0.6654 1.0471 1.4900 -0.0013 0.3504  -0.0146 94  LYS B N   
5096 C CA  . LYS B 96  ? 0.6543 1.0622 1.4845 0.0230  0.2759  -0.0533 94  LYS B CA  
5097 C C   . LYS B 96  ? 0.6516 1.1740 1.6243 0.0092  0.2616  -0.0954 94  LYS B C   
5098 O O   . LYS B 96  ? 0.6549 1.2078 1.6346 0.0359  0.1991  -0.1260 94  LYS B O   
5099 C CB  . LYS B 96  ? 0.6428 1.0333 1.3810 0.0824  0.2564  -0.0534 94  LYS B CB  
5100 N N   . ASN B 97  ? 0.5862 1.1594 1.6444 -0.0309 0.3098  -0.0941 95  ASN B N   
5101 C CA  . ASN B 97  ? 0.5517 1.2251 1.7121 -0.0472 0.2886  -0.1308 95  ASN B CA  
5102 C C   . ASN B 97  ? 0.5992 1.2600 1.8156 -0.1087 0.2759  -0.1486 95  ASN B C   
5103 O O   . ASN B 97  ? 0.5930 1.3270 1.8803 -0.1180 0.2323  -0.1891 95  ASN B O   
5104 C CB  . ASN B 97  ? 0.6069 1.3504 1.8087 -0.0445 0.3476  -0.1192 95  ASN B CB  
5105 C CG  . ASN B 97  ? 0.6996 1.3720 1.8434 -0.0643 0.4237  -0.0702 95  ASN B CG  
5106 O OD1 . ASN B 97  ? 0.6541 1.2541 1.6965 -0.0335 0.4395  -0.0409 95  ASN B OD1 
5107 N ND2 . ASN B 97  ? 0.7229 1.4131 1.9249 -0.1136 0.4699  -0.0599 95  ASN B ND2 
5108 N N   . THR B 98  ? 0.5587 1.1234 1.7372 -0.1455 0.3119  -0.1200 96  THR B N   
5109 C CA  . THR B 98  ? 0.5981 1.1291 1.8171 -0.2001 0.3065  -0.1372 96  THR B CA  
5110 C C   . THR B 98  ? 0.6394 1.0838 1.7973 -0.2017 0.2670  -0.1428 96  THR B C   
5111 O O   . THR B 98  ? 0.6333 1.0064 1.7855 -0.2377 0.2786  -0.1420 96  THR B O   
5112 C CB  . THR B 98  ? 0.6959 1.1759 1.9190 -0.2379 0.3805  -0.1004 96  THR B CB  
5113 O OG1 . THR B 98  ? 0.7802 1.2015 2.0263 -0.2847 0.3755  -0.1160 96  THR B OG1 
5114 C CG2 . THR B 98  ? 0.7048 1.0943 1.8204 -0.2115 0.4249  -0.0424 96  THR B CG2 
5115 N N   . CYS B 99  ? 0.6408 1.0899 1.7520 -0.1604 0.2210  -0.1493 97  CYS B N   
5116 C CA  . CYS B 99  ? 0.5672 0.9492 1.6233 -0.1599 0.1806  -0.1569 97  CYS B CA  
5117 C C   . CYS B 99  ? 0.5893 1.0267 1.6793 -0.1619 0.1120  -0.2114 97  CYS B C   
5118 O O   . CYS B 99  ? 0.5888 1.1055 1.6981 -0.1281 0.0720  -0.2319 97  CYS B O   
5119 C CB  . CYS B 99  ? 0.5948 0.9268 1.5380 -0.1108 0.1651  -0.1260 97  CYS B CB  
5120 S SG  . CYS B 99  ? 0.8662 1.2468 1.7668 -0.0540 0.0932  -0.1491 97  CYS B SG  
5121 N N   . VAL B 100 ? 0.5555 0.9473 1.6429 -0.1950 0.0988  -0.2339 98  VAL B N   
5122 C CA  . VAL B 100 ? 0.5141 0.9564 1.6228 -0.1973 0.0371  -0.2869 98  VAL B CA  
5123 C C   . VAL B 100 ? 0.5746 0.9972 1.6046 -0.1617 -0.0194 -0.2947 98  VAL B C   
5124 O O   . VAL B 100 ? 0.4997 0.9870 1.5245 -0.1290 -0.0739 -0.3178 98  VAL B O   
5125 C CB  . VAL B 100 ? 0.5848 0.9863 1.7193 -0.2445 0.0485  -0.3123 98  VAL B CB  
5126 C CG1 . VAL B 100 ? 0.6136 1.0791 1.7727 -0.2465 -0.0138 -0.3705 98  VAL B CG1 
5127 C CG2 . VAL B 100 ? 0.6386 1.0429 1.8430 -0.2822 0.1107  -0.2960 98  VAL B CG2 
5128 N N   . GLY B 101 ? 0.6026 0.9335 1.5648 -0.1647 -0.0069 -0.2726 99  GLY B N   
5129 C CA  . GLY B 101 ? 0.5757 0.8716 1.4408 -0.1329 -0.0522 -0.2720 99  GLY B CA  
5130 C C   . GLY B 101 ? 0.6317 0.8964 1.4780 -0.1539 -0.0776 -0.3110 99  GLY B C   
5131 O O   . GLY B 101 ? 0.5774 0.8191 1.4568 -0.1869 -0.0533 -0.3272 99  GLY B O   
5132 N N   . SER B 102 ? 0.5939 0.8426 1.3472 -0.1224 -0.1216 -0.3152 100 SER B N   
5133 C CA  . SER B 102 ? 0.6976 0.9173 1.4141 -0.1339 -0.1465 -0.3540 100 SER B CA  
5134 C C   . SER B 102 ? 0.7877 1.0206 1.4039 -0.0905 -0.1991 -0.3555 100 SER B C   
5135 O O   . SER B 102 ? 0.8439 1.0490 1.3844 -0.0572 -0.1962 -0.3088 100 SER B O   
5136 C CB  . SER B 102 ? 0.7860 0.9052 1.4565 -0.1461 -0.1025 -0.3309 100 SER B CB  
5137 O OG  . SER B 102 ? 0.9462 1.0355 1.5684 -0.1485 -0.1227 -0.3683 100 SER B OG  
5138 N N   . ASP B 103 ? 0.8460 1.1005 1.4822 0.4322  -0.1873 -0.2063 101 ASP B N   
5139 C CA  . ASP B 103 ? 0.8476 0.9990 1.4813 0.4529  -0.2300 -0.1550 101 ASP B CA  
5140 C C   . ASP B 103 ? 0.9143 0.9479 1.4819 0.4188  -0.2367 -0.1027 101 ASP B C   
5141 O O   . ASP B 103 ? 1.0590 0.9965 1.6083 0.4224  -0.2682 -0.0597 101 ASP B O   
5142 C CB  . ASP B 103 ? 0.8140 1.0307 1.4731 0.4673  -0.2595 -0.1232 101 ASP B CB  
5143 N N   . ASN B 104 ? 0.8681 0.9107 1.3975 0.3828  -0.2081 -0.1062 102 ASN B N   
5144 C CA  . ASN B 104 ? 0.9413 0.8843 1.4058 0.3452  -0.2102 -0.0604 102 ASN B CA  
5145 C C   . ASN B 104 ? 0.9659 0.8874 1.4002 0.3208  -0.1700 -0.0935 102 ASN B C   
5146 O O   . ASN B 104 ? 0.9506 0.9368 1.3535 0.2864  -0.1327 -0.1088 102 ASN B O   
5147 C CB  . ASN B 104 ? 0.8161 0.7949 1.2211 0.2958  -0.2018 -0.0148 102 ASN B CB  
5148 N N   . VAL B 105 ? 0.9558 0.7888 1.3802 0.3240  -0.1736 -0.0973 103 VAL B N   
5149 C CA  . VAL B 105 ? 0.8490 0.6544 1.2436 0.2999  -0.1420 -0.1225 103 VAL B CA  
5150 C C   . VAL B 105 ? 0.7938 0.5050 1.1253 0.2620  -0.1466 -0.0766 103 VAL B C   
5151 O O   . VAL B 105 ? 0.8048 0.4937 1.1048 0.2368  -0.1219 -0.0900 103 VAL B O   
5152 C CB  . VAL B 105 ? 0.7860 0.5848 1.2097 0.3209  -0.1348 -0.1684 103 VAL B CB  
5153 C CG1 . VAL B 105 ? 0.7843 0.5760 1.1780 0.2926  -0.1012 -0.1962 103 VAL B CG1 
5154 C CG2 . VAL B 105 ? 0.7738 0.6751 1.2606 0.3555  -0.1323 -0.2147 103 VAL B CG2 
5155 N N   . THR B 106 ? 0.8275 0.4953 1.1367 0.2523  -0.1771 -0.0226 104 THR B N   
5156 C CA  . THR B 106 ? 0.8480 0.4416 1.0940 0.2091  -0.1819 0.0210  104 THR B CA  
5157 C C   . THR B 106 ? 0.8957 0.5134 1.0964 0.1696  -0.1488 0.0209  104 THR B C   
5158 O O   . THR B 106 ? 0.9245 0.4963 1.0879 0.1412  -0.1380 0.0251  104 THR B O   
5159 C CB  . THR B 106 ? 0.8801 0.4530 1.1078 0.1978  -0.2175 0.0773  104 THR B CB  
5160 O OG1 . THR B 106 ? 1.1117 0.7589 1.3563 0.2049  -0.2208 0.0857  104 THR B OG1 
5161 C CG2 . THR B 106 ? 0.9294 0.4651 1.1866 0.2281  -0.2490 0.0818  104 THR B CG2 
5162 N N   . ASP B 107 ? 0.8346 0.5352 1.0297 0.1610  -0.1283 0.0155  105 ASP B N   
5163 C CA  . ASP B 107 ? 0.7942 0.5197 0.9390 0.1216  -0.0967 0.0171  105 ASP B CA  
5164 C C   . ASP B 107 ? 0.7312 0.4669 0.8775 0.1210  -0.0684 -0.0228 105 ASP B C   
5165 O O   . ASP B 107 ? 0.7146 0.4324 0.8231 0.0940  -0.0525 -0.0196 105 ASP B O   
5166 C CB  . ASP B 107 ? 0.7773 0.5736 0.9113 0.1096  -0.0873 0.0237  105 ASP B CB  
5167 C CG  . ASP B 107 ? 0.8896 0.6825 1.0075 0.0967  -0.1113 0.0661  105 ASP B CG  
5168 O OD1 . ASP B 107 ? 1.0033 0.7382 1.1161 0.0952  -0.1375 0.0945  105 ASP B OD1 
5169 O OD2 . ASP B 107 ? 0.8726 0.7200 0.9781 0.0826  -0.1051 0.0723  105 ASP B OD2 
5170 N N   . PHE B 108 ? 0.7140 0.4898 0.9043 0.1484  -0.0617 -0.0625 106 PHE B N   
5171 C CA  . PHE B 108 ? 0.6705 0.4598 0.8598 0.1424  -0.0367 -0.1000 106 PHE B CA  
5172 C C   . PHE B 108 ? 0.6690 0.3816 0.8479 0.1379  -0.0415 -0.1001 106 PHE B C   
5173 O O   . PHE B 108 ? 0.6761 0.3847 0.8236 0.1128  -0.0226 -0.1058 106 PHE B O   
5174 C CB  . PHE B 108 ? 0.6150 0.4684 0.8568 0.1702  -0.0298 -0.1486 106 PHE B CB  
5175 C CG  . PHE B 108 ? 0.5919 0.4633 0.8337 0.1609  -0.0060 -0.1899 106 PHE B CG  
5176 C CD1 . PHE B 108 ? 0.5483 0.4780 0.7580 0.1287  0.0184  -0.1972 106 PHE B CD1 
5177 C CD2 . PHE B 108 ? 0.6408 0.4674 0.9110 0.1808  -0.0107 -0.2200 106 PHE B CD2 
5178 C CE1 . PHE B 108 ? 0.5336 0.4866 0.7389 0.1146  0.0379  -0.2311 106 PHE B CE1 
5179 C CE2 . PHE B 108 ? 0.6219 0.4753 0.8847 0.1647  0.0124  -0.2557 106 PHE B CE2 
5180 C CZ  . PHE B 108 ? 0.5852 0.5049 0.8199 0.1331  0.0369  -0.2644 106 PHE B CZ  
5181 N N   . ASN B 109 ? 0.7473 0.3963 0.9504 0.1600  -0.0701 -0.0916 107 ASN B N   
5182 C CA  . ASN B 109 ? 0.7776 0.3583 0.9564 0.1449  -0.0733 -0.0867 107 ASN B CA  
5183 C C   . ASN B 109 ? 0.7960 0.3460 0.9213 0.1030  -0.0693 -0.0542 107 ASN B C   
5184 O O   . ASN B 109 ? 0.8261 0.3605 0.9271 0.0806  -0.0543 -0.0651 107 ASN B O   
5185 C CB  . ASN B 109 ? 0.7880 0.3155 0.9813 0.1636  -0.1039 -0.0686 107 ASN B CB  
5186 C CG  . ASN B 109 ? 0.8213 0.3726 1.0686 0.2044  -0.1061 -0.1111 107 ASN B CG  
5187 O OD1 . ASN B 109 ? 0.8162 0.4239 1.0836 0.2112  -0.0813 -0.1564 107 ASN B OD1 
5188 N ND2 . ASN B 109 ? 0.8960 0.4092 1.1668 0.2295  -0.1369 -0.0975 107 ASN B ND2 
5189 N N   . ALA B 110 ? 0.7713 0.3295 0.8736 0.0881  -0.0795 -0.0155 108 ALA B N   
5190 C CA  . ALA B 110 ? 0.8358 0.3882 0.8860 0.0459  -0.0723 0.0112  108 ALA B CA  
5191 C C   . ALA B 110 ? 0.8072 0.4125 0.8410 0.0328  -0.0399 -0.0114 108 ALA B C   
5192 O O   . ALA B 110 ? 0.8195 0.4166 0.8274 0.0085  -0.0296 -0.0138 108 ALA B O   
5193 C CB  . ALA B 110 ? 0.7849 0.3533 0.8150 0.0313  -0.0862 0.0499  108 ALA B CB  
5194 N N   . ILE B 111 ? 0.6857 0.3464 0.7333 0.0468  -0.0265 -0.0268 109 ILE B N   
5195 C CA  . ILE B 111 ? 0.6795 0.3810 0.7099 0.0349  -0.0033 -0.0426 109 ILE B CA  
5196 C C   . ILE B 111 ? 0.6851 0.3800 0.7216 0.0338  0.0079  -0.0707 109 ILE B C   
5197 O O   . ILE B 111 ? 0.6439 0.3536 0.6583 0.0166  0.0202  -0.0750 109 ILE B O   
5198 C CB  . ILE B 111 ? 0.6612 0.4142 0.7008 0.0439  0.0039  -0.0510 109 ILE B CB  
5199 C CG1 . ILE B 111 ? 0.6523 0.4151 0.6801 0.0388  -0.0054 -0.0248 109 ILE B CG1 
5200 C CG2 . ILE B 111 ? 0.5683 0.3502 0.5875 0.0302  0.0207  -0.0634 109 ILE B CG2 
5201 C CD1 . ILE B 111 ? 0.6021 0.4124 0.6417 0.0454  -0.0029 -0.0316 109 ILE B CD1 
5202 N N   . ALA B 112 ? 0.7232 0.3988 0.7921 0.0532  0.0025  -0.0930 110 ALA B N   
5203 C CA  . ALA B 112 ? 0.7348 0.4117 0.8114 0.0504  0.0152  -0.1273 110 ALA B CA  
5204 C C   . ALA B 112 ? 0.8099 0.4312 0.8662 0.0304  0.0106  -0.1215 110 ALA B C   
5205 O O   . ALA B 112 ? 0.7752 0.4058 0.8250 0.0170  0.0242  -0.1453 110 ALA B O   
5206 C CB  . ALA B 112 ? 0.7184 0.4034 0.8428 0.0804  0.0129  -0.1645 110 ALA B CB  
5207 N N   . THR B 113 ? 0.7882 0.3573 0.8297 0.0216  -0.0089 -0.0893 111 THR B N   
5208 C CA  . THR B 113 ? 0.8193 0.3326 0.8367 -0.0054 -0.0163 -0.0818 111 THR B CA  
5209 C C   . THR B 113 ? 0.8320 0.3637 0.8068 -0.0421 -0.0129 -0.0533 111 THR B C   
5210 O O   . THR B 113 ? 0.8815 0.3850 0.8303 -0.0738 -0.0153 -0.0488 111 THR B O   
5211 C CB  . THR B 113 ? 0.8261 0.2749 0.8504 0.0043  -0.0401 -0.0646 111 THR B CB  
5212 O OG1 . THR B 113 ? 0.9472 0.3958 0.9728 0.0114  -0.0591 -0.0297 111 THR B OG1 
5213 C CG2 . THR B 113 ? 0.8048 0.2516 0.8646 0.0404  -0.0388 -0.0990 111 THR B CG2 
5214 N N   . CYS B 114 ? 0.7813 0.3626 0.7484 -0.0407 -0.0073 -0.0383 112 CYS B N   
5215 C CA  . CYS B 114 ? 0.7662 0.3746 0.7002 -0.0719 -0.0041 -0.0197 112 CYS B CA  
5216 C C   . CYS B 114 ? 0.7713 0.4282 0.6966 -0.0832 0.0155  -0.0410 112 CYS B C   
5217 O O   . CYS B 114 ? 0.8258 0.5033 0.7668 -0.0665 0.0265  -0.0635 112 CYS B O   
5218 C CB  . CYS B 114 ? 0.7491 0.3924 0.6807 -0.0651 -0.0054 -0.0033 112 CYS B CB  
5219 S SG  . CYS B 114 ? 0.7308 0.4282 0.6784 -0.0384 0.0114  -0.0234 112 CYS B SG  
5220 N N   . ASP B 115 ? 0.7477 0.4318 0.6477 -0.1141 0.0183  -0.0339 113 ASP B N   
5221 C CA  . ASP B 115 ? 0.5959 0.3364 0.4917 -0.1233 0.0329  -0.0534 113 ASP B CA  
5222 C C   . ASP B 115 ? 0.6087 0.4106 0.5095 -0.1094 0.0392  -0.0577 113 ASP B C   
5223 O O   . ASP B 115 ? 0.6095 0.4631 0.5129 -0.1100 0.0465  -0.0737 113 ASP B O   
5224 C CB  . ASP B 115 ? 0.7149 0.4593 0.5840 -0.1675 0.0327  -0.0512 113 ASP B CB  
5225 C CG  . ASP B 115 ? 0.6660 0.4159 0.5099 -0.1988 0.0241  -0.0279 113 ASP B CG  
5226 O OD1 . ASP B 115 ? 0.7378 0.4902 0.5868 -0.1837 0.0191  -0.0150 113 ASP B OD1 
5227 O OD2 . ASP B 115 ? 0.9308 0.6870 0.7458 -0.2445 0.0224  -0.0225 113 ASP B OD2 
5228 N N   . TRP B 116 ? 0.6247 0.4213 0.5282 -0.0968 0.0341  -0.0453 114 TRP B N   
5229 C CA  . TRP B 116 ? 0.5457 0.3863 0.4543 -0.0817 0.0379  -0.0530 114 TRP B CA  
5230 C C   . TRP B 116 ? 0.6551 0.5562 0.5552 -0.1019 0.0434  -0.0646 114 TRP B C   
5231 O O   . TRP B 116 ? 0.5426 0.4874 0.4555 -0.0836 0.0467  -0.0835 114 TRP B O   
5232 C CB  . TRP B 116 ? 0.6021 0.4508 0.5260 -0.0535 0.0400  -0.0663 114 TRP B CB  
5233 C CG  . TRP B 116 ? 0.5759 0.3858 0.5076 -0.0398 0.0375  -0.0604 114 TRP B CG  
5234 C CD1 . TRP B 116 ? 0.6093 0.4031 0.5475 -0.0399 0.0401  -0.0681 114 TRP B CD1 
5235 C CD2 . TRP B 116 ? 0.6170 0.4108 0.5525 -0.0268 0.0331  -0.0508 114 TRP B CD2 
5236 N NE1 . TRP B 116 ? 0.6816 0.4578 0.6312 -0.0256 0.0384  -0.0673 114 TRP B NE1 
5237 C CE2 . TRP B 116 ? 0.6354 0.4121 0.5828 -0.0182 0.0335  -0.0548 114 TRP B CE2 
5238 C CE3 . TRP B 116 ? 0.5936 0.3933 0.5238 -0.0242 0.0298  -0.0432 114 TRP B CE3 
5239 C CZ2 . TRP B 116 ? 0.6135 0.3860 0.5692 -0.0070 0.0304  -0.0502 114 TRP B CZ2 
5240 C CZ3 . TRP B 116 ? 0.6222 0.4091 0.5564 -0.0152 0.0261  -0.0353 114 TRP B CZ3 
5241 C CH2 . TRP B 116 ? 0.6744 0.4512 0.6220 -0.0066 0.0262  -0.0383 114 TRP B CH2 
5242 N N   . THR B 117 ? 0.5992 0.5050 0.4781 -0.1409 0.0426  -0.0551 115 THR B N   
5243 C CA  . THR B 117 ? 0.6581 0.6390 0.5269 -0.1692 0.0498  -0.0695 115 THR B CA  
5244 C C   . THR B 117 ? 0.6726 0.6753 0.5254 -0.1903 0.0481  -0.0603 115 THR B C   
5245 O O   . THR B 117 ? 0.7018 0.7845 0.5517 -0.2096 0.0570  -0.0814 115 THR B O   
5246 C CB  . THR B 117 ? 0.6048 0.5932 0.4510 -0.2135 0.0508  -0.0659 115 THR B CB  
5247 O OG1 . THR B 117 ? 0.7216 0.6406 0.5391 -0.2452 0.0373  -0.0327 115 THR B OG1 
5248 C CG2 . THR B 117 ? 0.6337 0.6088 0.4936 -0.1980 0.0539  -0.0782 115 THR B CG2 
5249 N N   . ASN B 118 ? 0.6564 0.5999 0.5004 -0.1886 0.0367  -0.0321 116 ASN B N   
5250 C CA  . ASN B 118 ? 0.6344 0.5966 0.4597 -0.2123 0.0321  -0.0179 116 ASN B CA  
5251 C C   . ASN B 118 ? 0.6862 0.6440 0.5304 -0.1753 0.0335  -0.0255 116 ASN B C   
5252 O O   . ASN B 118 ? 0.6607 0.5751 0.5250 -0.1378 0.0312  -0.0256 116 ASN B O   
5253 C CB  . ASN B 118 ? 0.7861 0.6847 0.5840 -0.2430 0.0115  0.0258  116 ASN B CB  
5254 C CG  . ASN B 118 ? 0.8502 0.7337 0.6212 -0.2865 0.0057  0.0377  116 ASN B CG  
5255 O OD1 . ASN B 118 ? 0.9398 0.8904 0.6874 -0.3310 0.0137  0.0289  116 ASN B OD1 
5256 N ND2 . ASN B 118 ? 0.9794 0.7781 0.7535 -0.2763 -0.0080 0.0540  116 ASN B ND2 
5257 N N   . ALA B 119 ? 0.6326 0.6404 0.4666 -0.1923 0.0377  -0.0335 117 ALA B N   
5258 C CA  . ALA B 119 ? 0.6087 0.6138 0.4560 -0.1637 0.0396  -0.0446 117 ALA B CA  
5259 C C   . ALA B 119 ? 0.6410 0.5865 0.4840 -0.1571 0.0249  -0.0093 117 ALA B C   
5260 O O   . ALA B 119 ? 0.6055 0.5317 0.4622 -0.1284 0.0250  -0.0148 117 ALA B O   
5261 C CB  . ALA B 119 ? 0.6387 0.7181 0.4761 -0.1869 0.0493  -0.0690 117 ALA B CB  
5262 N N   . GLY B 120 ? 0.5981 0.5140 0.4229 -0.1837 0.0094  0.0270  118 GLY B N   
5263 C CA  . GLY B 120 ? 0.5884 0.4532 0.4187 -0.1701 -0.0086 0.0578  118 GLY B CA  
5264 C C   . GLY B 120 ? 0.6576 0.4791 0.5186 -0.1259 -0.0078 0.0494  118 GLY B C   
5265 O O   . GLY B 120 ? 0.6711 0.4753 0.5461 -0.1058 -0.0160 0.0592  118 GLY B O   
5266 N N   . ASP B 121 ? 0.6107 0.4258 0.4820 -0.1139 0.0023  0.0294  119 ASP B N   
5267 C CA  . ASP B 121 ? 0.6564 0.4425 0.5524 -0.0795 0.0045  0.0189  119 ASP B CA  
5268 C C   . ASP B 121 ? 0.6512 0.4560 0.5552 -0.0590 0.0123  0.0035  119 ASP B C   
5269 O O   . ASP B 121 ? 0.5795 0.3694 0.4972 -0.0402 0.0097  0.0047  119 ASP B O   
5270 C CB  . ASP B 121 ? 0.6286 0.4119 0.5286 -0.0786 0.0128  0.0021  119 ASP B CB  
5271 C CG  . ASP B 121 ? 0.6813 0.4350 0.5684 -0.1042 0.0038  0.0169  119 ASP B CG  
5272 O OD1 . ASP B 121 ? 0.7754 0.4965 0.6540 -0.1163 -0.0137 0.0438  119 ASP B OD1 
5273 O OD2 . ASP B 121 ? 0.7423 0.5030 0.6257 -0.1144 0.0113  0.0034  119 ASP B OD2 
5274 N N   . TYR B 122 ? 0.6121 0.4510 0.5076 -0.0642 0.0207  -0.0138 120 TYR B N   
5275 C CA  . TYR B 122 ? 0.5718 0.4143 0.4699 -0.0477 0.0240  -0.0289 120 TYR B CA  
5276 C C   . TYR B 122 ? 0.6178 0.4630 0.5072 -0.0561 0.0194  -0.0169 120 TYR B C   
5277 O O   . TYR B 122 ? 0.6000 0.4328 0.4901 -0.0458 0.0181  -0.0190 120 TYR B O   
5278 C CB  . TYR B 122 ? 0.5284 0.4023 0.4267 -0.0451 0.0309  -0.0572 120 TYR B CB  
5279 C CG  . TYR B 122 ? 0.5475 0.4282 0.4571 -0.0352 0.0333  -0.0687 120 TYR B CG  
5280 C CD1 . TYR B 122 ? 0.5309 0.4389 0.4372 -0.0558 0.0375  -0.0685 120 TYR B CD1 
5281 C CD2 . TYR B 122 ? 0.5607 0.4225 0.4798 -0.0114 0.0291  -0.0767 120 TYR B CD2 
5282 C CE1 . TYR B 122 ? 0.5192 0.4411 0.4347 -0.0508 0.0401  -0.0798 120 TYR B CE1 
5283 C CE2 . TYR B 122 ? 0.5413 0.4169 0.4702 -0.0047 0.0294  -0.0853 120 TYR B CE2 
5284 C CZ  . TYR B 122 ? 0.5804 0.4888 0.5091 -0.0233 0.0362  -0.0887 120 TYR B CZ  
5285 O OH  . TYR B 122 ? 0.5682 0.4979 0.5056 -0.0203 0.0369  -0.0984 120 TYR B OH  
5286 N N   . ILE B 123 ? 0.5767 0.4418 0.4538 -0.0806 0.0155  -0.0022 121 ILE B N   
5287 C CA  . ILE B 123 ? 0.5828 0.4582 0.4508 -0.0924 0.0086  0.0131  121 ILE B CA  
5288 C C   . ILE B 123 ? 0.6007 0.4517 0.4851 -0.0754 -0.0023 0.0324  121 ILE B C   
5289 O O   . ILE B 123 ? 0.6279 0.4877 0.5129 -0.0724 -0.0037 0.0328  121 ILE B O   
5290 C CB  . ILE B 123 ? 0.5801 0.4842 0.4280 -0.1278 0.0022  0.0315  121 ILE B CB  
5291 C CG1 . ILE B 123 ? 0.5952 0.5463 0.4300 -0.1476 0.0167  0.0023  121 ILE B CG1 
5292 C CG2 . ILE B 123 ? 0.6079 0.5272 0.4465 -0.1413 -0.0086 0.0521  121 ILE B CG2 
5293 C CD1 . ILE B 123 ? 0.6129 0.6055 0.4207 -0.1942 0.0119  0.0193  121 ILE B CD1 
5294 N N   . LEU B 124 ? 0.5646 0.3892 0.4639 -0.0653 -0.0104 0.0445  122 LEU B N   
5295 C CA  . LEU B 124 ? 0.5931 0.4040 0.5176 -0.0435 -0.0207 0.0530  122 LEU B CA  
5296 C C   . LEU B 124 ? 0.6278 0.4441 0.5627 -0.0263 -0.0088 0.0308  122 LEU B C   
5297 O O   . LEU B 124 ? 0.6219 0.4554 0.5699 -0.0178 -0.0120 0.0308  122 LEU B O   
5298 C CB  . LEU B 124 ? 0.5812 0.3552 0.5210 -0.0347 -0.0326 0.0630  122 LEU B CB  
5299 C CG  . LEU B 124 ? 0.7113 0.4732 0.6881 -0.0040 -0.0419 0.0583  122 LEU B CG  
5300 C CD1 . LEU B 124 ? 0.6730 0.4565 0.6644 0.0035  -0.0596 0.0762  122 LEU B CD1 
5301 C CD2 . LEU B 124 ? 0.6571 0.3694 0.6461 0.0035  -0.0535 0.0612  122 LEU B CD2 
5302 N N   . ALA B 125 ? 0.5921 0.3998 0.5197 -0.0247 0.0029  0.0129  123 ALA B N   
5303 C CA  . ALA B 125 ? 0.6586 0.4669 0.5882 -0.0157 0.0096  -0.0021 123 ALA B CA  
5304 C C   . ALA B 125 ? 0.5707 0.3884 0.4823 -0.0256 0.0102  -0.0039 123 ALA B C   
5305 O O   . ALA B 125 ? 0.6216 0.4379 0.5269 -0.0268 0.0118  -0.0103 123 ALA B O   
5306 C CB  . ALA B 125 ? 0.6813 0.4775 0.6062 -0.0125 0.0161  -0.0155 123 ALA B CB  
5307 N N   . ASN B 126 ? 0.6277 0.4550 0.5264 -0.0383 0.0082  0.0015  124 ASN B N   
5308 C CA  . ASN B 126 ? 0.6948 0.5263 0.5735 -0.0518 0.0086  -0.0034 124 ASN B CA  
5309 C C   . ASN B 126 ? 0.6479 0.5107 0.5266 -0.0644 0.0030  0.0112  124 ASN B C   
5310 O O   . ASN B 126 ? 0.6896 0.5606 0.5485 -0.0818 0.0037  0.0071  124 ASN B O   
5311 C CB  . ASN B 126 ? 0.6460 0.4674 0.5088 -0.0567 0.0126  -0.0205 124 ASN B CB  
5312 C CG  . ASN B 126 ? 0.6920 0.4789 0.5482 -0.0457 0.0111  -0.0361 124 ASN B CG  
5313 O OD1 . ASN B 126 ? 0.6914 0.4553 0.5302 -0.0532 0.0060  -0.0376 124 ASN B OD1 
5314 N ND2 . ASN B 126 ? 0.7610 0.5432 0.6289 -0.0307 0.0125  -0.0451 124 ASN B ND2 
5315 N N   . THR B 127 ? 0.6210 0.4990 0.5218 -0.0561 -0.0055 0.0281  125 THR B N   
5316 C CA  . THR B 127 ? 0.6434 0.5554 0.5499 -0.0638 -0.0168 0.0460  125 THR B CA  
5317 C C   . THR B 127 ? 0.6410 0.5733 0.5830 -0.0421 -0.0258 0.0501  125 THR B C   
5318 O O   . THR B 127 ? 0.7111 0.6805 0.6656 -0.0427 -0.0383 0.0632  125 THR B O   
5319 C CB  . THR B 127 ? 0.6752 0.5901 0.5754 -0.0757 -0.0276 0.0669  125 THR B CB  
5320 O OG1 . THR B 127 ? 0.6050 0.4885 0.5198 -0.0616 -0.0334 0.0739  125 THR B OG1 
5321 C CG2 . THR B 127 ? 0.6920 0.6130 0.5601 -0.1015 -0.0166 0.0546  125 THR B CG2 
5322 N N   . CYS B 128 ? 0.6914 0.6083 0.6522 -0.0228 -0.0204 0.0357  126 CYS B N   
5323 C CA  . CYS B 128 ? 0.7013 0.6453 0.7023 0.0008  -0.0262 0.0277  126 CYS B CA  
5324 C C   . CYS B 128 ? 0.7584 0.7516 0.7561 -0.0109 -0.0171 0.0123  126 CYS B C   
5325 O O   . CYS B 128 ? 0.7141 0.7103 0.6763 -0.0384 -0.0112 0.0145  126 CYS B O   
5326 C CB  . CYS B 128 ? 0.6532 0.5655 0.6724 0.0201  -0.0219 0.0133  126 CYS B CB  
5327 S SG  . CYS B 128 ? 0.6215 0.5116 0.6091 0.0048  -0.0020 -0.0036 126 CYS B SG  
5328 N N   . THR B 129 ? 0.7663 0.8003 0.7999 0.0067  -0.0163 -0.0066 127 THR B N   
5329 C CA  . THR B 129 ? 0.7352 0.8296 0.7639 -0.0121 -0.0066 -0.0234 127 THR B CA  
5330 C C   . THR B 129 ? 0.6815 0.7491 0.6718 -0.0365 0.0076  -0.0321 127 THR B C   
5331 O O   . THR B 129 ? 0.6969 0.7137 0.6805 -0.0283 0.0109  -0.0328 127 THR B O   
5332 C CB  . THR B 129 ? 0.7013 0.8643 0.7857 0.0144  -0.0088 -0.0489 127 THR B CB  
5333 O OG1 . THR B 129 ? 0.6791 0.8136 0.7868 0.0379  -0.0044 -0.0677 127 THR B OG1 
5334 C CG2 . THR B 129 ? 0.6965 0.8862 0.8225 0.0424  -0.0304 -0.0373 127 THR B CG2 
5335 N N   . GLU B 130 ? 0.6375 0.7410 0.5998 -0.0704 0.0130  -0.0362 128 GLU B N   
5336 C CA  . GLU B 130 ? 0.6842 0.7526 0.6013 -0.0996 0.0185  -0.0356 128 GLU B CA  
5337 C C   . GLU B 130 ? 0.6170 0.6898 0.5505 -0.0881 0.0256  -0.0522 128 GLU B C   
5338 O O   . GLU B 130 ? 0.5785 0.5965 0.4875 -0.0920 0.0251  -0.0457 128 GLU B O   
5339 C CB  . GLU B 130 ? 0.6912 0.8014 0.5733 -0.1450 0.0196  -0.0355 128 GLU B CB  
5340 C CG  . GLU B 130 ? 0.7906 0.8416 0.6131 -0.1821 0.0155  -0.0235 128 GLU B CG  
5341 C CD  . GLU B 130 ? 0.7550 0.7142 0.5519 -0.1748 0.0066  -0.0085 128 GLU B CD  
5342 O OE1 . GLU B 130 ? 0.7429 0.6982 0.5373 -0.1757 0.0045  -0.0043 128 GLU B OE1 
5343 O OE2 . GLU B 130 ? 0.7189 0.6177 0.4997 -0.1690 0.0012  -0.0039 128 GLU B OE2 
5344 N N   . ARG B 131 ? 0.5911 0.7336 0.5690 -0.0724 0.0314  -0.0773 129 ARG B N   
5345 C CA  . ARG B 131 ? 0.5978 0.7536 0.5888 -0.0676 0.0407  -0.0998 129 ARG B CA  
5346 C C   . ARG B 131 ? 0.5746 0.6633 0.5826 -0.0348 0.0379  -0.0964 129 ARG B C   
5347 O O   . ARG B 131 ? 0.5496 0.6185 0.5469 -0.0396 0.0436  -0.1033 129 ARG B O   
5348 C CB  . ARG B 131 ? 0.5458 0.7998 0.5864 -0.0564 0.0490  -0.1383 129 ARG B CB  
5349 C CG  . ARG B 131 ? 0.6402 0.9200 0.6913 -0.0589 0.0617  -0.1691 129 ARG B CG  
5350 C CD  . ARG B 131 ? 0.7639 1.0467 0.7516 -0.1144 0.0661  -0.1562 129 ARG B CD  
5351 N NE  . ARG B 131 ? 0.7766 1.0638 0.7589 -0.1233 0.0748  -0.1730 129 ARG B NE  
5352 C CZ  . ARG B 131 ? 0.7324 0.9469 0.7098 -0.1061 0.0716  -0.1625 129 ARG B CZ  
5353 N NH1 . ARG B 131 ? 0.6898 0.8287 0.6785 -0.0723 0.0624  -0.1432 129 ARG B NH1 
5354 N NH2 . ARG B 131 ? 0.8754 1.1050 0.8368 -0.1267 0.0783  -0.1740 129 ARG B NH2 
5355 N N   . LEU B 132 ? 0.6033 0.6611 0.6341 -0.0069 0.0279  -0.0842 130 LEU B N   
5356 C CA  . LEU B 132 ? 0.5860 0.5791 0.6229 0.0136  0.0238  -0.0765 130 LEU B CA  
5357 C C   . LEU B 132 ? 0.5662 0.5055 0.5578 -0.0046 0.0237  -0.0552 130 LEU B C   
5358 O O   . LEU B 132 ? 0.6019 0.5027 0.5900 0.0017  0.0249  -0.0546 130 LEU B O   
5359 C CB  . LEU B 132 ? 0.5989 0.5760 0.6672 0.0407  0.0088  -0.0651 130 LEU B CB  
5360 C CG  . LEU B 132 ? 0.6328 0.6399 0.7585 0.0741  0.0028  -0.0910 130 LEU B CG  
5361 C CD1 . LEU B 132 ? 0.5845 0.5534 0.7355 0.1004  -0.0210 -0.0705 130 LEU B CD1 
5362 C CD2 . LEU B 132 ? 0.5252 0.5212 0.6632 0.0808  0.0139  -0.1204 130 LEU B CD2 
5363 N N   . LYS B 133 ? 0.5809 0.5189 0.5398 -0.0267 0.0214  -0.0415 131 LYS B N   
5364 C CA  . LYS B 133 ? 0.5841 0.4723 0.5064 -0.0384 0.0191  -0.0298 131 LYS B CA  
5365 C C   . LYS B 133 ? 0.5775 0.4580 0.4828 -0.0493 0.0213  -0.0357 131 LYS B C   
5366 O O   . LYS B 133 ? 0.6379 0.4829 0.5348 -0.0428 0.0189  -0.0329 131 LYS B O   
5367 C CB  . LYS B 133 ? 0.6074 0.4878 0.4983 -0.0600 0.0139  -0.0190 131 LYS B CB  
5368 C CG  . LYS B 133 ? 0.6243 0.5106 0.5220 -0.0562 0.0105  -0.0106 131 LYS B CG  
5369 C CD  . LYS B 133 ? 0.6775 0.5513 0.5388 -0.0823 0.0071  -0.0058 131 LYS B CD  
5370 C CE  . LYS B 133 ? 0.7113 0.5989 0.5742 -0.0852 0.0047  0.0010  131 LYS B CE  
5371 N NZ  . LYS B 133 ? 0.7329 0.6055 0.5586 -0.1133 0.0027  -0.0004 131 LYS B NZ  
5372 N N   . LEU B 134 ? 0.5499 0.4734 0.4498 -0.0690 0.0251  -0.0442 132 LEU B N   
5373 C CA  . LEU B 134 ? 0.5785 0.5043 0.4592 -0.0860 0.0255  -0.0472 132 LEU B CA  
5374 C C   . LEU B 134 ? 0.5795 0.5088 0.4893 -0.0646 0.0333  -0.0634 132 LEU B C   
5375 O O   . LEU B 134 ? 0.5669 0.4709 0.4624 -0.0666 0.0298  -0.0586 132 LEU B O   
5376 C CB  . LEU B 134 ? 0.5474 0.5356 0.4146 -0.1199 0.0298  -0.0559 132 LEU B CB  
5377 C CG  . LEU B 134 ? 0.6369 0.6279 0.4701 -0.1510 0.0224  -0.0409 132 LEU B CG  
5378 C CD1 . LEU B 134 ? 0.6517 0.7143 0.4639 -0.1959 0.0269  -0.0493 132 LEU B CD1 
5379 C CD2 . LEU B 134 ? 0.5972 0.5035 0.3873 -0.1602 0.0047  -0.0147 132 LEU B CD2 
5380 N N   . PHE B 135 ? 0.5157 0.4736 0.4674 -0.0433 0.0412  -0.0831 133 PHE B N   
5381 C CA  . PHE B 135 ? 0.5046 0.4563 0.4821 -0.0259 0.0474  -0.1013 133 PHE B CA  
5382 C C   . PHE B 135 ? 0.5418 0.4356 0.5101 -0.0153 0.0417  -0.0848 133 PHE B C   
5383 O O   . PHE B 135 ? 0.5768 0.4609 0.5395 -0.0185 0.0445  -0.0901 133 PHE B O   
5384 C CB  . PHE B 135 ? 0.4990 0.4743 0.5254 0.0004  0.0500  -0.1245 133 PHE B CB  
5385 C CG  . PHE B 135 ? 0.4443 0.3957 0.4957 0.0181  0.0532  -0.1443 133 PHE B CG  
5386 C CD1 . PHE B 135 ? 0.4284 0.4126 0.4836 0.0073  0.0653  -0.1739 133 PHE B CD1 
5387 C CD2 . PHE B 135 ? 0.5481 0.4445 0.6140 0.0389  0.0429  -0.1327 133 PHE B CD2 
5388 C CE1 . PHE B 135 ? 0.5241 0.4827 0.5996 0.0197  0.0686  -0.1955 133 PHE B CE1 
5389 C CE2 . PHE B 135 ? 0.5036 0.3682 0.5862 0.0488  0.0435  -0.1497 133 PHE B CE2 
5390 C CZ  . PHE B 135 ? 0.5829 0.4766 0.6716 0.0408  0.0570  -0.1830 133 PHE B CZ  
5391 N N   . ALA B 136 ? 0.4568 0.3228 0.4236 -0.0064 0.0345  -0.0671 134 ALA B N   
5392 C CA  . ALA B 136 ? 0.6057 0.4341 0.5642 -0.0016 0.0309  -0.0561 134 ALA B CA  
5393 C C   . ALA B 136 ? 0.6145 0.4329 0.5467 -0.0109 0.0282  -0.0513 134 ALA B C   
5394 O O   . ALA B 136 ? 0.6161 0.4269 0.5485 -0.0084 0.0291  -0.0547 134 ALA B O   
5395 C CB  . ALA B 136 ? 0.4357 0.2508 0.3925 0.0018  0.0243  -0.0402 134 ALA B CB  
5396 N N   . ALA B 137 ? 0.5850 0.4020 0.4945 -0.0224 0.0218  -0.0430 135 ALA B N   
5397 C CA  . ALA B 137 ? 0.6619 0.4578 0.5485 -0.0266 0.0111  -0.0358 135 ALA B CA  
5398 C C   . ALA B 137 ? 0.6101 0.4231 0.4944 -0.0341 0.0116  -0.0407 135 ALA B C   
5399 O O   . ALA B 137 ? 0.5846 0.3887 0.4662 -0.0275 0.0043  -0.0389 135 ALA B O   
5400 C CB  . ALA B 137 ? 0.5369 0.3143 0.3944 -0.0424 -0.0007 -0.0234 135 ALA B CB  
5401 N N   . GLU B 138 ? 0.6413 0.4890 0.5284 -0.0489 0.0202  -0.0501 136 GLU B N   
5402 C CA  . GLU B 138 ? 0.6208 0.4953 0.5048 -0.0616 0.0235  -0.0592 136 GLU B CA  
5403 C C   . GLU B 138 ? 0.6611 0.5339 0.5685 -0.0463 0.0323  -0.0736 136 GLU B C   
5404 O O   . GLU B 138 ? 0.6164 0.4951 0.5169 -0.0508 0.0287  -0.0732 136 GLU B O   
5405 C CB  . GLU B 138 ? 0.6089 0.5352 0.4971 -0.0812 0.0353  -0.0773 136 GLU B CB  
5406 C CG  . GLU B 138 ? 0.6691 0.6171 0.5208 -0.1164 0.0267  -0.0641 136 GLU B CG  
5407 C CD  . GLU B 138 ? 0.7414 0.7648 0.6028 -0.1385 0.0430  -0.0921 136 GLU B CD  
5408 O OE1 . GLU B 138 ? 0.6983 0.7564 0.5739 -0.1416 0.0546  -0.1165 136 GLU B OE1 
5409 O OE2 . GLU B 138 ? 0.6944 0.7496 0.5508 -0.1542 0.0453  -0.0943 136 GLU B OE2 
5410 N N   . THR B 139 ? 0.6273 0.4914 0.5602 -0.0311 0.0409  -0.0839 137 THR B N   
5411 C CA  . THR B 139 ? 0.6782 0.5315 0.6270 -0.0243 0.0470  -0.0956 137 THR B CA  
5412 C C   . THR B 139 ? 0.6304 0.4691 0.5692 -0.0216 0.0406  -0.0834 137 THR B C   
5413 O O   . THR B 139 ? 0.6688 0.5177 0.6068 -0.0281 0.0432  -0.0910 137 THR B O   
5414 C CB  . THR B 139 ? 0.6254 0.4591 0.5989 -0.0100 0.0491  -0.1014 137 THR B CB  
5415 O OG1 . THR B 139 ? 0.5881 0.4490 0.5815 -0.0068 0.0550  -0.1222 137 THR B OG1 
5416 C CG2 . THR B 139 ? 0.5670 0.3740 0.5484 -0.0099 0.0505  -0.1079 137 THR B CG2 
5417 N N   . LEU B 140 ? 0.5801 0.4037 0.5126 -0.0133 0.0330  -0.0692 138 LEU B N   
5418 C CA  . LEU B 140 ? 0.6634 0.4878 0.5930 -0.0082 0.0282  -0.0665 138 LEU B CA  
5419 C C   . LEU B 140 ? 0.5961 0.4364 0.5178 -0.0074 0.0186  -0.0663 138 LEU B C   
5420 O O   . LEU B 140 ? 0.6230 0.4851 0.5504 -0.0067 0.0184  -0.0734 138 LEU B O   
5421 C CB  . LEU B 140 ? 0.6032 0.4142 0.5291 0.0000  0.0229  -0.0590 138 LEU B CB  
5422 C CG  . LEU B 140 ? 0.6989 0.5223 0.6264 0.0095  0.0172  -0.0656 138 LEU B CG  
5423 C CD1 . LEU B 140 ? 0.5137 0.3633 0.4488 0.0007  0.0258  -0.0743 138 LEU B CD1 
5424 C CD2 . LEU B 140 ? 0.5707 0.3813 0.4938 0.0161  0.0128  -0.0652 138 LEU B CD2 
5425 N N   . LYS B 141 ? 0.5548 0.3871 0.4616 -0.0108 0.0078  -0.0561 139 LYS B N   
5426 C CA  . LYS B 141 ? 0.5770 0.4155 0.4733 -0.0099 -0.0099 -0.0482 139 LYS B CA  
5427 C C   . LYS B 141 ? 0.6641 0.5389 0.5614 -0.0246 -0.0038 -0.0558 139 LYS B C   
5428 O O   . LYS B 141 ? 0.6284 0.5243 0.5294 -0.0193 -0.0140 -0.0557 139 LYS B O   
5429 C CB  . LYS B 141 ? 0.6549 0.4682 0.5252 -0.0203 -0.0269 -0.0294 139 LYS B CB  
5430 C CG  . LYS B 141 ? 0.6908 0.4854 0.5492 -0.0117 -0.0568 -0.0136 139 LYS B CG  
5431 C CD  . LYS B 141 ? 0.7860 0.5471 0.6077 -0.0341 -0.0772 0.0110  139 LYS B CD  
5432 C CE  . LYS B 141 ? 0.8364 0.5472 0.6482 -0.0163 -0.1148 0.0287  139 LYS B CE  
5433 N NZ  . LYS B 141 ? 0.9671 0.7033 0.7978 0.0036  -0.1301 0.0275  139 LYS B NZ  
5434 N N   . ALA B 142 ? 0.6149 0.5030 0.5121 -0.0422 0.0124  -0.0666 140 ALA B N   
5435 C CA  . ALA B 142 ? 0.6188 0.5419 0.5165 -0.0595 0.0211  -0.0808 140 ALA B CA  
5436 C C   . ALA B 142 ? 0.5946 0.5239 0.5074 -0.0543 0.0292  -0.0932 140 ALA B C   
5437 O O   . ALA B 142 ? 0.5647 0.5264 0.4752 -0.0648 0.0276  -0.0984 140 ALA B O   
5438 C CB  . ALA B 142 ? 0.6299 0.5670 0.5315 -0.0750 0.0382  -0.1003 140 ALA B CB  
5439 N N   . THR B 143 ? 0.5979 0.5011 0.5226 -0.0440 0.0364  -0.0963 141 THR B N   
5440 C CA  . THR B 143 ? 0.6047 0.5147 0.5356 -0.0488 0.0424  -0.1045 141 THR B CA  
5441 C C   . THR B 143 ? 0.6464 0.5902 0.5795 -0.0398 0.0312  -0.1007 141 THR B C   
5442 O O   . THR B 143 ? 0.7123 0.6930 0.6472 -0.0514 0.0336  -0.1103 141 THR B O   
5443 C CB  . THR B 143 ? 0.6452 0.5203 0.5815 -0.0455 0.0471  -0.1014 141 THR B CB  
5444 O OG1 . THR B 143 ? 0.6368 0.4830 0.5796 -0.0450 0.0524  -0.1068 141 THR B OG1 
5445 C CG2 . THR B 143 ? 0.4612 0.3417 0.3945 -0.0632 0.0520  -0.1070 141 THR B CG2 
5446 N N   . GLU B 144 ? 0.5759 0.5101 0.5113 -0.0184 0.0179  -0.0904 142 GLU B N   
5447 C CA  . GLU B 144 ? 0.5723 0.5381 0.5190 -0.0001 0.0033  -0.0932 142 GLU B CA  
5448 C C   . GLU B 144 ? 0.5949 0.5946 0.5399 -0.0033 -0.0097 -0.0901 142 GLU B C   
5449 O O   . GLU B 144 ? 0.6046 0.6549 0.5639 0.0014  -0.0145 -0.1005 142 GLU B O   
5450 C CB  . GLU B 144 ? 0.5957 0.5294 0.5439 0.0246  -0.0125 -0.0853 142 GLU B CB  
5451 C CG  . GLU B 144 ? 0.6087 0.5302 0.5626 0.0301  -0.0028 -0.0929 142 GLU B CG  
5452 C CD  . GLU B 144 ? 0.7034 0.5811 0.6511 0.0460  -0.0156 -0.0851 142 GLU B CD  
5453 O OE1 . GLU B 144 ? 0.7026 0.5508 0.6365 0.0473  -0.0317 -0.0694 142 GLU B OE1 
5454 O OE2 . GLU B 144 ? 0.6254 0.4996 0.5779 0.0517  -0.0106 -0.0944 142 GLU B OE2 
5455 N N   . GLU B 145 ? 0.6488 0.6314 0.5757 -0.0150 -0.0162 -0.0762 143 GLU B N   
5456 C CA  . GLU B 145 ? 0.6614 0.6784 0.5803 -0.0244 -0.0321 -0.0678 143 GLU B CA  
5457 C C   . GLU B 145 ? 0.6964 0.7619 0.6173 -0.0490 -0.0147 -0.0857 143 GLU B C   
5458 O O   . GLU B 145 ? 0.7030 0.8187 0.6288 -0.0507 -0.0265 -0.0859 143 GLU B O   
5459 C CB  . GLU B 145 ? 0.7254 0.7207 0.6169 -0.0432 -0.0409 -0.0490 143 GLU B CB  
5460 C CG  . GLU B 145 ? 0.8492 0.7939 0.7302 -0.0264 -0.0653 -0.0265 143 GLU B CG  
5461 C CD  . GLU B 145 ? 0.9798 0.9229 0.8623 -0.0065 -0.1036 -0.0075 143 GLU B CD  
5462 O OE1 . GLU B 145 ? 0.9876 0.9810 0.8799 -0.0069 -0.1112 -0.0101 143 GLU B OE1 
5463 O OE2 . GLU B 145 ? 1.0632 0.9526 0.9378 0.0101  -0.1288 0.0095  143 GLU B OE2 
5464 N N   . THR B 146 ? 0.7160 0.7652 0.6337 -0.0679 0.0108  -0.1014 144 THR B N   
5465 C CA  . THR B 146 ? 0.7733 0.8538 0.6885 -0.0953 0.0267  -0.1208 144 THR B CA  
5466 C C   . THR B 146 ? 0.7371 0.8502 0.6643 -0.0942 0.0287  -0.1297 144 THR B C   
5467 O O   . THR B 146 ? 0.7470 0.9122 0.6726 -0.1137 0.0304  -0.1398 144 THR B O   
5468 C CB  . THR B 146 ? 0.7906 0.8307 0.7025 -0.1106 0.0480  -0.1372 144 THR B CB  
5469 O OG1 . THR B 146 ? 0.8471 0.8926 0.7495 -0.1227 0.0506  -0.1416 144 THR B OG1 
5470 C CG2 . THR B 146 ? 0.7222 0.7710 0.6317 -0.1367 0.0624  -0.1583 144 THR B CG2 
5471 N N   . PHE B 147 ? 0.6816 0.7750 0.6192 -0.0765 0.0292  -0.1279 145 PHE B N   
5472 C CA  . PHE B 147 ? 0.6921 0.8308 0.6393 -0.0819 0.0330  -0.1398 145 PHE B CA  
5473 C C   . PHE B 147 ? 0.6967 0.9091 0.6622 -0.0653 0.0158  -0.1438 145 PHE B C   
5474 O O   . PHE B 147 ? 0.5997 0.8784 0.5733 -0.0790 0.0202  -0.1595 145 PHE B O   
5475 C CB  . PHE B 147 ? 0.6637 0.7774 0.6170 -0.0681 0.0355  -0.1381 145 PHE B CB  
5476 C CG  . PHE B 147 ? 0.7239 0.8966 0.6842 -0.0804 0.0412  -0.1532 145 PHE B CG  
5477 C CD1 . PHE B 147 ? 0.7420 0.9095 0.6825 -0.1216 0.0556  -0.1564 145 PHE B CD1 
5478 C CD2 . PHE B 147 ? 0.6571 0.8919 0.6439 -0.0527 0.0304  -0.1663 145 PHE B CD2 
5479 C CE1 . PHE B 147 ? 0.7495 0.9816 0.6897 -0.1437 0.0614  -0.1696 145 PHE B CE1 
5480 C CE2 . PHE B 147 ? 0.7964 1.1053 0.7921 -0.0674 0.0383  -0.1872 145 PHE B CE2 
5481 C CZ  . PHE B 147 ? 0.7582 1.0704 0.7274 -0.1174 0.0550  -0.1875 145 PHE B CZ  
5482 N N   . LYS B 148 ? 0.7092 0.9124 0.6811 -0.0372 -0.0069 -0.1290 146 LYS B N   
5483 C CA  . LYS B 148 ? 0.6837 0.9487 0.6770 -0.0145 -0.0318 -0.1291 146 LYS B CA  
5484 C C   . LYS B 148 ? 0.6342 0.9586 0.6188 -0.0445 -0.0307 -0.1318 146 LYS B C   
5485 O O   . LYS B 148 ? 0.6606 1.0628 0.6669 -0.0349 -0.0443 -0.1404 146 LYS B O   
5486 C CB  . LYS B 148 ? 0.6490 0.8689 0.6436 0.0180  -0.0625 -0.1059 146 LYS B CB  
5487 C CG  . LYS B 148 ? 0.7448 0.9250 0.7562 0.0532  -0.0686 -0.1111 146 LYS B CG  
5488 C CD  . LYS B 148 ? 0.8477 0.9818 0.8620 0.0870  -0.1060 -0.0906 146 LYS B CD  
5489 C CE  . LYS B 148 ? 0.8744 0.9532 0.8489 0.0609  -0.1131 -0.0585 146 LYS B CE  
5490 N NZ  . LYS B 148 ? 0.9779 1.0055 0.9456 0.0840  -0.1555 -0.0316 146 LYS B NZ  
5491 N N   . LEU B 149 ? 0.6422 0.9386 0.5981 -0.0806 -0.0147 -0.1290 147 LEU B N   
5492 C CA  . LEU B 149 ? 0.5779 0.9300 0.5212 -0.1159 -0.0101 -0.1363 147 LEU B CA  
5493 C C   . LEU B 149 ? 0.7147 1.1076 0.6579 -0.1459 0.0117  -0.1611 147 LEU B C   
5494 O O   . LEU B 149 ? 0.8036 1.2624 0.7415 -0.1737 0.0129  -0.1707 147 LEU B O   
5495 C CB  . LEU B 149 ? 0.6581 0.9714 0.5728 -0.1457 0.0021  -0.1346 147 LEU B CB  
5496 C CG  . LEU B 149 ? 0.7948 1.0690 0.6984 -0.1323 -0.0153 -0.1101 147 LEU B CG  
5497 C CD1 . LEU B 149 ? 0.7217 0.9769 0.6016 -0.1664 0.0043  -0.1209 147 LEU B CD1 
5498 C CD2 . LEU B 149 ? 0.7736 1.0919 0.6779 -0.1210 -0.0515 -0.0849 147 LEU B CD2 
5499 N N   . SER B 150 ? 0.6058 0.9624 0.5501 -0.1468 0.0272  -0.1695 148 SER B N   
5500 C CA  . SER B 150 ? 0.6737 1.0640 0.6100 -0.1832 0.0444  -0.1880 148 SER B CA  
5501 C C   . SER B 150 ? 0.6262 1.1274 0.5865 -0.1774 0.0348  -0.2002 148 SER B C   
5502 O O   . SER B 150 ? 0.6853 1.2410 0.6350 -0.2182 0.0473  -0.2165 148 SER B O   
5503 C CB  . SER B 150 ? 0.6541 0.9818 0.5828 -0.1872 0.0566  -0.1870 148 SER B CB  
5504 O OG  . SER B 150 ? 0.7532 1.1123 0.7059 -0.1551 0.0482  -0.1873 148 SER B OG  
5505 N N   . TYR B 151 ? 0.6076 1.1440 0.6009 -0.1280 0.0110  -0.1947 149 TYR B N   
5506 C CA  . TYR B 151 ? 0.5436 1.1929 0.5722 -0.1107 -0.0013 -0.2127 149 TYR B CA  
5507 C C   . TYR B 151 ? 0.5094 1.2367 0.5406 -0.1243 -0.0144 -0.2121 149 TYR B C   
5508 O O   . TYR B 151 ? 0.5565 1.2487 0.5696 -0.1296 -0.0242 -0.1921 149 TYR B O   
5509 C CB  . TYR B 151 ? 0.5060 1.1537 0.5745 -0.0457 -0.0269 -0.2112 149 TYR B CB  
5510 C CG  . TYR B 151 ? 0.6651 1.2779 0.7397 -0.0330 -0.0141 -0.2225 149 TYR B CG  
5511 C CD1 . TYR B 151 ? 0.5869 1.2569 0.6591 -0.0651 0.0087  -0.2467 149 TYR B CD1 
5512 C CD2 . TYR B 151 ? 0.6712 1.1967 0.7482 0.0035  -0.0252 -0.2077 149 TYR B CD2 
5513 C CE1 . TYR B 151 ? 0.6465 1.2923 0.7199 -0.0599 0.0195  -0.2555 149 TYR B CE1 
5514 C CE2 . TYR B 151 ? 0.7228 1.2221 0.8033 0.0113  -0.0133 -0.2186 149 TYR B CE2 
5515 C CZ  . TYR B 151 ? 0.7255 1.2869 0.8045 -0.0201 0.0089  -0.2423 149 TYR B CZ  
5516 O OH  . TYR B 151 ? 0.8227 1.3658 0.9011 -0.0184 0.0198  -0.2517 149 TYR B OH  
5517 N N   . GLY B 152 ? 0.4484 1.2940 0.5020 -0.1335 -0.0146 -0.2354 150 GLY B N   
5518 C CA  . GLY B 152 ? 0.5430 1.4788 0.6002 -0.1506 -0.0269 -0.2365 150 GLY B CA  
5519 C C   . GLY B 152 ? 0.5363 1.5154 0.6352 -0.0911 -0.0697 -0.2230 150 GLY B C   
5520 O O   . GLY B 152 ? 0.5915 1.5557 0.7278 -0.0325 -0.0902 -0.2241 150 GLY B O   
5521 N N   . ILE B 153 ? 0.7824 0.8047 0.7834 -0.1531 0.0493  -0.0637 151 ILE B N   
5522 C CA  . ILE B 153 ? 0.8001 0.7603 0.7273 -0.1510 0.0641  -0.0628 151 ILE B CA  
5523 C C   . ILE B 153 ? 0.8349 0.7692 0.7290 -0.1203 0.0583  -0.0495 151 ILE B C   
5524 O O   . ILE B 153 ? 0.8241 0.7961 0.7594 -0.0991 0.0479  -0.0393 151 ILE B O   
5525 C CB  . ILE B 153 ? 0.7823 0.7422 0.7014 -0.1499 0.0748  -0.0679 151 ILE B CB  
5526 C CG1 . ILE B 153 ? 0.8439 0.8450 0.8102 -0.1743 0.0879  -0.0843 151 ILE B CG1 
5527 C CG2 . ILE B 153 ? 0.8830 0.7741 0.7190 -0.1497 0.0882  -0.0579 151 ILE B CG2 
5528 C CD1 . ILE B 153 ? 0.8128 0.8217 0.7637 -0.1686 0.1019  -0.0957 151 ILE B CD1 
5529 N N   . ALA B 154 ? 0.8952 0.7656 0.7252 -0.1178 0.0665  -0.0490 152 ALA B N   
5530 C CA  . ALA B 154 ? 0.9818 0.8243 0.7836 -0.0838 0.0659  -0.0396 152 ALA B CA  
5531 C C   . ALA B 154 ? 1.0108 0.8046 0.7735 -0.0714 0.0675  -0.0304 152 ALA B C   
5532 O O   . ALA B 154 ? 1.0643 0.8070 0.7837 -0.0919 0.0769  -0.0303 152 ALA B O   
5533 C CB  . ALA B 154 ? 1.0107 0.8114 0.7689 -0.0823 0.0708  -0.0505 152 ALA B CB  
5534 N N   . THR B 155 ? 1.0087 0.8196 0.7901 -0.0390 0.0566  -0.0189 153 THR B N   
5535 C CA  . THR B 155 ? 1.1053 0.8784 0.8507 -0.0229 0.0478  -0.0073 153 THR B CA  
5536 C C   . THR B 155 ? 1.1544 0.9051 0.9002 0.0172  0.0416  0.0040  153 THR B C   
5537 O O   . THR B 155 ? 1.1135 0.9131 0.9144 0.0377  0.0410  0.0053  153 THR B O   
5538 C CB  . THR B 155 ? 1.0580 0.8800 0.8348 -0.0210 0.0298  -0.0094 153 THR B CB  
5539 O OG1 . THR B 155 ? 0.9999 0.8475 0.7860 -0.0529 0.0404  -0.0244 153 THR B OG1 
5540 C CG2 . THR B 155 ? 1.1441 0.9254 0.8644 -0.0048 0.0150  0.0028  153 THR B CG2 
5541 N N   . VAL B 156 ? 1.2416 0.9196 0.9312 0.0293  0.0394  0.0155  154 VAL B N   
5542 C CA  . VAL B 156 ? 1.2862 0.9376 0.9826 0.0725  0.0332  0.0252  154 VAL B CA  
5543 C C   . VAL B 156 ? 1.2218 0.9361 0.9788 0.1007  0.0074  0.0357  154 VAL B C   
5544 O O   . VAL B 156 ? 1.1963 0.9141 0.9377 0.0991  -0.0174 0.0439  154 VAL B O   
5545 C CB  . VAL B 156 ? 1.3517 0.9038 0.9801 0.0799  0.0309  0.0404  154 VAL B CB  
5546 C CG1 . VAL B 156 ? 1.3681 0.8970 1.0178 0.1321  0.0200  0.0504  154 VAL B CG1 
5547 C CG2 . VAL B 156 ? 1.3855 0.8728 0.9717 0.0485  0.0536  0.0272  154 VAL B CG2 
5548 N N   . ARG B 157 ? 1.1480 0.9143 0.9746 0.1261  0.0131  0.0347  155 ARG B N   
5549 C CA  . ARG B 157 ? 1.1314 0.9635 1.0401 0.1514  -0.0112 0.0455  155 ARG B CA  
5550 C C   . ARG B 157 ? 1.2350 1.0443 1.1613 0.1984  -0.0217 0.0588  155 ARG B C   
5551 O O   . ARG B 157 ? 1.1827 1.0252 1.1595 0.2194  -0.0570 0.0704  155 ARG B O   
5552 C CB  . ARG B 157 ? 1.0918 1.0067 1.0841 0.1462  0.0060  0.0441  155 ARG B CB  
5553 C CG  . ARG B 157 ? 0.9933 0.9849 1.0984 0.1717  -0.0067 0.0585  155 ARG B CG  
5554 C CD  . ARG B 157 ? 0.9844 1.0384 1.1456 0.1628  0.0269  0.0651  155 ARG B CD  
5555 N NE  . ARG B 157 ? 0.9176 1.0573 1.2044 0.1685  0.0184  0.0835  155 ARG B NE  
5556 C CZ  . ARG B 157 ? 0.8978 1.0799 1.2674 0.2018  0.0178  0.0977  155 ARG B CZ  
5557 N NH1 . ARG B 157 ? 0.9449 1.0969 1.2861 0.2395  0.0359  0.0959  155 ARG B NH1 
5558 N NH2 . ARG B 157 ? 0.8149 1.0747 1.3115 0.1973  0.0017  0.1142  155 ARG B NH2 
5559 N N   . GLU B 158 ? 1.2551 1.0059 1.1436 0.2164  0.0043  0.0540  156 GLU B N   
5560 C CA  . GLU B 158 ? 1.2383 0.9624 1.1513 0.2671  -0.0008 0.0632  156 GLU B CA  
5561 C C   . GLU B 158 ? 1.3314 0.9583 1.1729 0.2744  0.0249  0.0495  156 GLU B C   
5562 O O   . GLU B 158 ? 1.4075 1.0328 1.2273 0.2598  0.0582  0.0261  156 GLU B O   
5563 C CB  . GLU B 158 ? 1.1856 1.0018 1.2086 0.2985  0.0147  0.0644  156 GLU B CB  
5564 C CG  . GLU B 158 ? 1.1938 1.0021 1.2679 0.3566  0.0134  0.0714  156 GLU B CG  
5565 C CD  . GLU B 158 ? 1.1745 1.0970 1.3817 0.3813  0.0225  0.0806  156 GLU B CD  
5566 O OE1 . GLU B 158 ? 1.0797 1.0768 1.3326 0.3494  0.0265  0.0846  156 GLU B OE1 
5567 O OE2 . GLU B 158 ? 1.1695 1.1080 1.4448 0.4322  0.0268  0.0857  156 GLU B OE2 
5568 N N   . VAL B 159 ? 1.3947 0.9367 1.1982 0.2965  0.0056  0.0639  157 VAL B N   
5569 C CA  . VAL B 159 ? 1.4882 0.9266 1.2408 0.3095  0.0252  0.0499  157 VAL B CA  
5570 C C   . VAL B 159 ? 1.4791 0.9351 1.3011 0.3726  0.0377  0.0409  157 VAL B C   
5571 O O   . VAL B 159 ? 1.4527 0.8804 1.3054 0.4159  0.0130  0.0614  157 VAL B O   
5572 C CB  . VAL B 159 ? 1.5969 0.9265 1.2780 0.2996  0.0015  0.0759  157 VAL B CB  
5573 C CG1 . VAL B 159 ? 1.6511 0.8666 1.2841 0.2980  0.0226  0.0565  157 VAL B CG1 
5574 C CG2 . VAL B 159 ? 1.5496 0.8911 1.1778 0.2444  -0.0086 0.0905  157 VAL B CG2 
5575 N N   . LEU B 160 ? 1.4514 0.9586 1.2985 0.3804  0.0777  0.0113  158 LEU B N   
5576 C CA  . LEU B 160 ? 1.3561 0.8935 1.2711 0.4418  0.1025  -0.0012 158 LEU B CA  
5577 C C   . LEU B 160 ? 1.5336 0.9552 1.4255 0.4841  0.0966  -0.0095 158 LEU B C   
5578 O O   . LEU B 160 ? 1.5300 0.9531 1.4877 0.5340  0.0764  0.0104  158 LEU B O   
5579 C CB  . LEU B 160 ? 1.3812 0.9674 1.2860 0.4394  0.1535  -0.0347 158 LEU B CB  
5580 C CG  . LEU B 160 ? 1.3223 1.0422 1.2931 0.4236  0.1694  -0.0190 158 LEU B CG  
5581 C CD1 . LEU B 160 ? 1.2382 1.0414 1.3328 0.4558  0.1515  0.0126  158 LEU B CD1 
5582 C CD2 . LEU B 160 ? 1.3035 1.0365 1.2328 0.3584  0.1490  -0.0091 158 LEU B CD2 
5583 N N   . SER B 161 ? 1.6450 0.9635 1.4515 0.4646  0.1100  -0.0391 159 SER B N   
5584 C CA  . SER B 161 ? 1.5908 0.7778 1.3707 0.4964  0.1030  -0.0497 159 SER B CA  
5585 C C   . SER B 161 ? 1.6870 0.7714 1.3715 0.4405  0.1022  -0.0688 159 SER B C   
5586 O O   . SER B 161 ? 1.7666 0.8941 1.4140 0.3879  0.1119  -0.0810 159 SER B O   
5587 C CB  . SER B 161 ? 1.6277 0.8146 1.4499 0.5635  0.1395  -0.0908 159 SER B CB  
5588 O OG  . SER B 161 ? 1.5872 0.8714 1.5181 0.6161  0.1395  -0.0682 159 SER B OG  
5589 N N   . ASP B 162 ? 1.8308 0.7790 1.4864 0.4510  0.0878  -0.0680 160 ASP B N   
5590 C CA  . ASP B 162 ? 1.8996 0.7474 1.4820 0.3929  0.0840  -0.0809 160 ASP B CA  
5591 C C   . ASP B 162 ? 1.8683 0.7383 1.4176 0.3737  0.1130  -0.1442 160 ASP B C   
5592 O O   . ASP B 162 ? 1.8925 0.7826 1.4555 0.4221  0.1391  -0.1880 160 ASP B O   
5593 C CB  . ASP B 162 ? 1.9481 0.6509 1.5254 0.4096  0.0672  -0.0744 160 ASP B CB  
5594 C CG  . ASP B 162 ? 2.0122 0.6214 1.5358 0.3393  0.0568  -0.0658 160 ASP B CG  
5595 O OD1 . ASP B 162 ? 2.0327 0.6787 1.5172 0.2834  0.0638  -0.0683 160 ASP B OD1 
5596 O OD2 . ASP B 162 ? 2.1033 0.6204 1.6424 0.3361  0.0418  -0.0536 160 ASP B OD2 
5597 N N   . ARG B 163 ? 1.8400 0.7124 1.3449 0.3048  0.1086  -0.1485 161 ARG B N   
5598 C CA  . ARG B 163 ? 1.8501 0.7460 1.3156 0.2757  0.1234  -0.2018 161 ARG B CA  
5599 C C   . ARG B 163 ? 1.8209 0.8664 1.3055 0.2822  0.1426  -0.2010 161 ARG B C   
5600 O O   . ARG B 163 ? 1.8068 0.8916 1.2561 0.2515  0.1493  -0.2303 161 ARG B O   
5601 C CB  . ARG B 163 ? 1.8725 0.6778 1.3073 0.3104  0.1354  -0.2686 161 ARG B CB  
5602 N N   . GLU B 164 ? 1.7674 0.8960 1.3117 0.3194  0.1480  -0.1659 162 GLU B N   
5603 C CA  . GLU B 164 ? 1.6051 0.8724 1.1852 0.3228  0.1655  -0.1552 162 GLU B CA  
5604 C C   . GLU B 164 ? 1.6089 0.9387 1.2260 0.2895  0.1412  -0.1043 162 GLU B C   
5605 O O   . GLU B 164 ? 1.6209 0.9068 1.2487 0.2914  0.1164  -0.0725 162 GLU B O   
5606 C CB  . GLU B 164 ? 1.5998 0.9221 1.2383 0.3924  0.1931  -0.1591 162 GLU B CB  
5607 C CG  . GLU B 164 ? 1.7649 1.0108 1.3691 0.4392  0.2186  -0.2135 162 GLU B CG  
5608 C CD  . GLU B 164 ? 1.7425 1.0425 1.4205 0.5139  0.2494  -0.2146 162 GLU B CD  
5609 O OE1 . GLU B 164 ? 1.6897 1.0914 1.4527 0.5251  0.2478  -0.1706 162 GLU B OE1 
5610 O OE2 . GLU B 164 ? 1.7081 0.9550 1.3698 0.5582  0.2729  -0.2612 162 GLU B OE2 
5611 N N   . LEU B 165 ? 1.5274 0.9563 1.1595 0.2609  0.1470  -0.0971 163 LEU B N   
5612 C CA  . LEU B 165 ? 1.4308 0.9115 1.0925 0.2271  0.1235  -0.0602 163 LEU B CA  
5613 C C   . LEU B 165 ? 1.3549 0.9554 1.0657 0.2191  0.1341  -0.0509 163 LEU B C   
5614 O O   . LEU B 165 ? 1.3610 0.9918 1.0507 0.2133  0.1556  -0.0706 163 LEU B O   
5615 C CB  . LEU B 165 ? 1.5242 0.9479 1.1320 0.1698  0.1089  -0.0622 163 LEU B CB  
5616 C CG  . LEU B 165 ? 1.5163 0.9457 1.1289 0.1418  0.0863  -0.0278 163 LEU B CG  
5617 C CD1 . LEU B 165 ? 1.5216 0.8951 1.1346 0.1764  0.0692  -0.0011 163 LEU B CD1 
5618 C CD2 . LEU B 165 ? 1.5444 0.9259 1.1114 0.0858  0.0853  -0.0338 163 LEU B CD2 
5619 N N   . HIS B 166 ? 1.2919 0.9561 1.0661 0.2190  0.1159  -0.0200 164 HIS B N   
5620 C CA  . HIS B 166 ? 1.2403 1.0090 1.0741 0.2049  0.1199  -0.0061 164 HIS B CA  
5621 C C   . HIS B 166 ? 1.2444 1.0215 1.0673 0.1555  0.0966  0.0003  164 HIS B C   
5622 O O   . HIS B 166 ? 1.2458 0.9897 1.0558 0.1464  0.0721  0.0096  164 HIS B O   
5623 C CB  . HIS B 166 ? 1.2011 1.0419 1.1333 0.2389  0.1142  0.0178  164 HIS B CB  
5624 C CG  . HIS B 166 ? 1.1467 1.0871 1.1469 0.2385  0.1376  0.0303  164 HIS B CG  
5625 N ND1 . HIS B 166 ? 1.1486 1.1499 1.1982 0.2051  0.1218  0.0473  164 HIS B ND1 
5626 C CD2 . HIS B 166 ? 1.1195 1.1059 1.1438 0.2672  0.1790  0.0307  164 HIS B CD2 
5627 C CE1 . HIS B 166 ? 1.1191 1.1963 1.2248 0.2104  0.1501  0.0637  164 HIS B CE1 
5628 N NE2 . HIS B 166 ? 1.1892 1.2633 1.2768 0.2477  0.1879  0.0556  164 HIS B NE2 
5629 N N   . LEU B 167 ? 1.1600 0.9828 0.9864 0.1269  0.1051  -0.0036 165 LEU B N   
5630 C CA  . LEU B 167 ? 1.1574 0.9882 0.9780 0.0827  0.0882  -0.0040 165 LEU B CA  
5631 C C   . LEU B 167 ? 1.0883 1.0058 0.9867 0.0724  0.0804  0.0125  165 LEU B C   
5632 O O   . LEU B 167 ? 1.0196 0.9914 0.9563 0.0831  0.0960  0.0241  165 LEU B O   
5633 C CB  . LEU B 167 ? 1.1093 0.9068 0.8711 0.0533  0.0962  -0.0255 165 LEU B CB  
5634 C CG  . LEU B 167 ? 1.2338 0.9340 0.9252 0.0496  0.0986  -0.0456 165 LEU B CG  
5635 C CD1 . LEU B 167 ? 1.2557 0.9371 0.9089 0.0133  0.0974  -0.0691 165 LEU B CD1 
5636 C CD2 . LEU B 167 ? 1.2847 0.9374 0.9647 0.0401  0.0853  -0.0324 165 LEU B CD2 
5637 N N   . SER B 168 ? 1.0616 0.9884 0.9810 0.0519  0.0578  0.0137  166 SER B N   
5638 C CA  . SER B 168 ? 0.9822 0.9754 0.9762 0.0371  0.0450  0.0217  166 SER B CA  
5639 C C   . SER B 168 ? 0.9358 0.9257 0.9099 0.0015  0.0441  0.0086  166 SER B C   
5640 O O   . SER B 168 ? 0.9555 0.9012 0.8777 -0.0154 0.0432  -0.0058 166 SER B O   
5641 C CB  . SER B 168 ? 0.9734 0.9811 1.0100 0.0443  0.0165  0.0228  166 SER B CB  
5642 O OG  . SER B 168 ? 0.9723 0.9924 1.0453 0.0778  0.0109  0.0360  166 SER B OG  
5643 N N   . TRP B 169 ? 0.8559 0.8948 0.8773 -0.0095 0.0451  0.0177  167 TRP B N   
5644 C CA  . TRP B 169 ? 0.8210 0.8642 0.8363 -0.0388 0.0416  0.0072  167 TRP B CA  
5645 C C   . TRP B 169 ? 0.7093 0.7920 0.8004 -0.0508 0.0241  0.0054  167 TRP B C   
5646 O O   . TRP B 169 ? 0.6688 0.7830 0.8269 -0.0392 0.0127  0.0168  167 TRP B O   
5647 C CB  . TRP B 169 ? 0.8148 0.8777 0.8175 -0.0410 0.0496  0.0184  167 TRP B CB  
5648 C CG  . TRP B 169 ? 0.9108 0.9274 0.8290 -0.0310 0.0652  0.0063  167 TRP B CG  
5649 C CD1 . TRP B 169 ? 0.9554 0.9654 0.8505 -0.0001 0.0841  0.0130  167 TRP B CD1 
5650 C CD2 . TRP B 169 ? 0.9636 0.9330 0.8179 -0.0513 0.0629  -0.0188 167 TRP B CD2 
5651 N NE1 . TRP B 169 ? 0.9787 0.9333 0.7918 0.0032  0.0931  -0.0109 167 TRP B NE1 
5652 C CE2 . TRP B 169 ? 1.0377 0.9643 0.8258 -0.0305 0.0775  -0.0304 167 TRP B CE2 
5653 C CE3 . TRP B 169 ? 0.9649 0.9268 0.8221 -0.0852 0.0503  -0.0344 167 TRP B CE3 
5654 C CZ2 . TRP B 169 ? 1.1272 0.9948 0.8491 -0.0450 0.0744  -0.0596 167 TRP B CZ2 
5655 C CZ3 . TRP B 169 ? 1.0037 0.9160 0.8039 -0.1025 0.0485  -0.0581 167 TRP B CZ3 
5656 C CH2 . TRP B 169 ? 1.0459 0.9071 0.7776 -0.0836 0.0578  -0.0717 167 TRP B CH2 
5657 N N   . GLU B 170 ? 0.6545 0.7356 0.7432 -0.0740 0.0217  -0.0117 168 GLU B N   
5658 C CA  . GLU B 170 ? 0.6404 0.7540 0.7996 -0.0823 0.0082  -0.0224 168 GLU B CA  
5659 C C   . GLU B 170 ? 0.6114 0.7701 0.8514 -0.0809 -0.0041 0.0007  168 GLU B C   
5660 O O   . GLU B 170 ? 0.5642 0.7335 0.7918 -0.0851 -0.0015 0.0192  168 GLU B O   
5661 C CB  . GLU B 170 ? 0.6836 0.7904 0.8261 -0.1050 0.0162  -0.0461 168 GLU B CB  
5662 C CG  . GLU B 170 ? 0.5949 0.7343 0.8077 -0.1095 0.0087  -0.0659 168 GLU B CG  
5663 C CD  . GLU B 170 ? 0.7338 0.8750 0.9344 -0.1305 0.0263  -0.0882 168 GLU B CD  
5664 O OE1 . GLU B 170 ? 0.7508 0.8648 0.8928 -0.1459 0.0406  -0.0850 168 GLU B OE1 
5665 O OE2 . GLU B 170 ? 0.7555 0.9256 1.0126 -0.1316 0.0273  -0.1103 168 GLU B OE2 
5666 N N   . VAL B 171 ? 0.6098 0.7911 0.9305 -0.0754 -0.0205 -0.0001 169 VAL B N   
5667 C CA  . VAL B 171 ? 0.5711 0.7880 0.9821 -0.0751 -0.0336 0.0286  169 VAL B CA  
5668 C C   . VAL B 171 ? 0.5897 0.8217 1.0434 -0.0873 -0.0435 0.0199  169 VAL B C   
5669 O O   . VAL B 171 ? 0.6122 0.8381 1.0681 -0.0930 -0.0433 -0.0175 169 VAL B O   
5670 C CB  . VAL B 171 ? 0.6541 0.8825 1.1494 -0.0668 -0.0519 0.0289  169 VAL B CB  
5671 C CG1 . VAL B 171 ? 0.6865 0.8954 1.1715 -0.0657 -0.0635 -0.0201 169 VAL B CG1 
5672 C CG2 . VAL B 171 ? 0.6087 0.8641 1.2137 -0.0714 -0.0680 0.0563  169 VAL B CG2 
5673 N N   . GLY B 172 ? 0.5646 0.8197 1.0520 -0.0893 -0.0511 0.0566  170 GLY B N   
5674 C CA  . GLY B 172 ? 0.4772 0.7515 1.0232 -0.0963 -0.0680 0.0560  170 GLY B CA  
5675 C C   . GLY B 172 ? 0.5141 0.7912 1.0019 -0.1082 -0.0659 0.0474  170 GLY B C   
5676 O O   . GLY B 172 ? 0.6258 0.9266 1.1688 -0.1128 -0.0840 0.0493  170 GLY B O   
5677 N N   . LYS B 173 ? 0.5466 0.7991 0.9343 -0.1129 -0.0481 0.0366  171 LYS B N   
5678 C CA  . LYS B 173 ? 0.6258 0.8740 0.9620 -0.1289 -0.0491 0.0216  171 LYS B CA  
5679 C C   . LYS B 173 ? 0.6407 0.8734 0.8868 -0.1259 -0.0465 0.0402  171 LYS B C   
5680 O O   . LYS B 173 ? 0.5639 0.7764 0.7635 -0.1117 -0.0283 0.0494  171 LYS B O   
5681 C CB  . LYS B 173 ? 0.5886 0.8101 0.8891 -0.1412 -0.0287 -0.0181 171 LYS B CB  
5682 C CG  . LYS B 173 ? 0.6253 0.8710 1.0024 -0.1466 -0.0269 -0.0443 171 LYS B CG  
5683 C CD  . LYS B 173 ? 0.6367 0.8625 0.9697 -0.1631 -0.0005 -0.0749 171 LYS B CD  
5684 C CE  . LYS B 173 ? 0.5599 0.8260 0.9713 -0.1725 0.0063  -0.0995 171 LYS B CE  
5685 N NZ  . LYS B 173 ? 0.6505 0.9074 1.0255 -0.1976 0.0346  -0.1174 171 LYS B NZ  
5686 N N   . PRO B 174 ? 0.6902 0.9343 0.9118 -0.1365 -0.0661 0.0431  172 PRO B N   
5687 C CA  . PRO B 174 ? 0.7472 0.9716 0.8667 -0.1320 -0.0647 0.0495  172 PRO B CA  
5688 C C   . PRO B 174 ? 0.7936 0.9646 0.8349 -0.1352 -0.0417 0.0161  172 PRO B C   
5689 O O   . PRO B 174 ? 0.7477 0.8978 0.8041 -0.1504 -0.0334 -0.0111 172 PRO B O   
5690 C CB  . PRO B 174 ? 0.7103 0.9573 0.8291 -0.1472 -0.1012 0.0473  172 PRO B CB  
5691 C CG  . PRO B 174 ? 0.7194 0.9857 0.9316 -0.1655 -0.1092 0.0238  172 PRO B CG  
5692 C CD  . PRO B 174 ? 0.6637 0.9416 0.9517 -0.1510 -0.0938 0.0367  172 PRO B CD  
5693 N N   . ARG B 175 ? 0.9131 1.0603 0.8687 -0.1184 -0.0284 0.0205  173 ARG B N   
5694 C CA  . ARG B 175 ? 0.9542 1.0420 0.8371 -0.1160 -0.0091 -0.0101 173 ARG B CA  
5695 C C   . ARG B 175 ? 0.9843 1.0419 0.7989 -0.1328 -0.0280 -0.0406 173 ARG B C   
5696 O O   . ARG B 175 ? 1.0342 1.1125 0.8078 -0.1283 -0.0468 -0.0333 173 ARG B O   
5697 C CB  . ARG B 175 ? 0.9896 1.0675 0.8312 -0.0831 0.0193  0.0045  173 ARG B CB  
5698 C CG  . ARG B 175 ? 0.9305 1.0342 0.8471 -0.0689 0.0332  0.0294  173 ARG B CG  
5699 C CD  . ARG B 175 ? 0.9922 1.0952 0.8839 -0.0368 0.0620  0.0437  173 ARG B CD  
5700 N NE  . ARG B 175 ? 0.9456 1.0866 0.9255 -0.0260 0.0679  0.0721  173 ARG B NE  
5701 C CZ  . ARG B 175 ? 0.9022 1.0600 0.8978 0.0001  0.0918  0.0901  173 ARG B CZ  
5702 N NH1 . ARG B 175 ? 0.9098 1.0481 0.8347 0.0234  0.1176  0.0808  173 ARG B NH1 
5703 N NH2 . ARG B 175 ? 0.8768 1.0727 0.9693 0.0035  0.0890  0.1146  173 ARG B NH2 
5704 N N   . PRO B 176 ? 1.0181 1.0256 0.8184 -0.1535 -0.0261 -0.0733 174 PRO B N   
5705 C CA  . PRO B 176 ? 1.0428 1.0154 0.7906 -0.1743 -0.0491 -0.1073 174 PRO B CA  
5706 C C   . PRO B 176 ? 1.0913 1.0249 0.7341 -0.1482 -0.0430 -0.1229 174 PRO B C   
5707 O O   . PRO B 176 ? 1.0707 0.9888 0.6851 -0.1157 -0.0108 -0.1124 174 PRO B O   
5708 C CB  . PRO B 176 ? 1.0300 0.9502 0.7961 -0.2007 -0.0375 -0.1292 174 PRO B CB  
5709 C CG  . PRO B 176 ? 1.0079 0.9144 0.7814 -0.1770 -0.0036 -0.1096 174 PRO B CG  
5710 C CD  . PRO B 176 ? 0.9787 0.9592 0.8129 -0.1626 -0.0060 -0.0787 174 PRO B CD  
5711 N N   . PRO B 177 ? 1.1371 1.0569 0.7217 -0.1595 -0.0745 -0.1517 175 PRO B N   
5712 C CA  . PRO B 177 ? 1.2133 1.0862 0.6843 -0.1334 -0.0673 -0.1804 175 PRO B CA  
5713 C C   . PRO B 177 ? 1.3182 1.1002 0.7635 -0.1346 -0.0497 -0.2175 175 PRO B C   
5714 O O   . PRO B 177 ? 1.3982 1.1419 0.8824 -0.1713 -0.0653 -0.2373 175 PRO B O   
5715 C CB  . PRO B 177 ? 1.2512 1.1352 0.6733 -0.1514 -0.1178 -0.2061 175 PRO B CB  
5716 C CG  . PRO B 177 ? 1.2742 1.2326 0.7947 -0.1761 -0.1473 -0.1725 175 PRO B CG  
5717 C CD  . PRO B 177 ? 1.1290 1.0830 0.7502 -0.1930 -0.1218 -0.1611 175 PRO B CD  
5718 N N   . LEU B 178 ? 1.2873 1.0361 0.6753 -0.0935 -0.0153 -0.2231 176 LEU B N   
5719 C CA  . LEU B 178 ? 1.3437 1.0020 0.7138 -0.0852 0.0029  -0.2512 176 LEU B CA  
5720 C C   . LEU B 178 ? 1.5111 1.0925 0.7944 -0.0864 -0.0171 -0.3132 176 LEU B C   
5721 O O   . LEU B 178 ? 1.5190 1.0605 0.7290 -0.0458 0.0042  -0.3407 176 LEU B O   
5722 C CB  . LEU B 178 ? 1.3445 1.0084 0.7155 -0.0370 0.0468  -0.2279 176 LEU B CB  
5723 C CG  . LEU B 178 ? 1.2693 1.0083 0.7251 -0.0337 0.0612  -0.1726 176 LEU B CG  
5724 C CD1 . LEU B 178 ? 1.1777 0.9164 0.6469 0.0110  0.0975  -0.1551 176 LEU B CD1 
5725 C CD2 . LEU B 178 ? 1.2741 1.0089 0.8004 -0.0737 0.0455  -0.1603 176 LEU B CD2 
5726 N N   . ASN B 179 ? 1.5420 1.1041 0.8413 -0.1336 -0.0597 -0.3392 177 ASN B N   
5727 C CA  . ASN B 179 ? 1.5079 0.9912 0.7391 -0.1448 -0.0907 -0.4047 177 ASN B CA  
5728 C C   . ASN B 179 ? 1.5756 0.9945 0.8770 -0.1971 -0.1101 -0.4188 177 ASN B C   
5729 O O   . ASN B 179 ? 1.6494 1.0877 1.0360 -0.2187 -0.0927 -0.3765 177 ASN B O   
5730 C CB  . ASN B 179 ? 1.5680 1.0992 0.7375 -0.1511 -0.1346 -0.4279 177 ASN B CB  
5731 C CG  . ASN B 179 ? 1.6003 1.2020 0.8560 -0.1988 -0.1758 -0.4033 177 ASN B CG  
5732 O OD1 . ASN B 179 ? 1.6185 1.1913 0.9416 -0.2464 -0.2030 -0.4215 177 ASN B OD1 
5733 N ND2 . ASN B 179 ? 1.5808 1.2767 0.8431 -0.1856 -0.1793 -0.3599 177 ASN B ND2 
5734 N N   . ARG B 180 ? 1.6353 0.9913 0.9170 -0.2137 -0.1437 -0.4734 178 ARG B N   
5735 C CA  . ARG B 180 ? 1.6938 0.9944 1.0631 -0.2579 -0.1553 -0.4782 178 ARG B CA  
5736 C C   . ARG B 180 ? 1.7131 1.0792 1.1781 -0.3142 -0.1897 -0.4645 178 ARG B C   
5737 O O   . ARG B 180 ? 1.7380 1.0746 1.2906 -0.3536 -0.1922 -0.4582 178 ARG B O   
5738 C CB  . ARG B 180 ? 1.7883 1.0119 1.1377 -0.2483 -0.1740 -0.5371 178 ARG B CB  
5739 N N   . ASN B 181 ? 1.6751 1.1328 1.1340 -0.3169 -0.2148 -0.4556 179 ASN B N   
5740 C CA  . ASN B 181 ? 1.5597 1.0938 1.1288 -0.3629 -0.2420 -0.4352 179 ASN B CA  
5741 C C   . ASN B 181 ? 1.4676 1.0470 1.1003 -0.3774 -0.2019 -0.3804 179 ASN B C   
5742 O O   . ASN B 181 ? 1.3864 1.0382 1.1248 -0.4092 -0.2126 -0.3593 179 ASN B O   
5743 C CB  . ASN B 181 ? 1.4902 1.1053 1.0358 -0.3569 -0.2920 -0.4462 179 ASN B CB  
5744 C CG  . ASN B 181 ? 1.6225 1.2130 1.1303 -0.3538 -0.3380 -0.5068 179 ASN B CG  
5745 O OD1 . ASN B 181 ? 1.6990 1.2162 1.2224 -0.3646 -0.3356 -0.5434 179 ASN B OD1 
5746 N ND2 . ASN B 181 ? 1.6583 1.3132 1.1170 -0.3408 -0.3797 -0.5172 179 ASN B ND2 
5747 N N   . TYR B 182 ? 1.4671 1.0246 1.0598 -0.3385 -0.1530 -0.3527 180 TYR B N   
5748 C CA  . TYR B 182 ? 1.3999 1.0089 1.0553 -0.3325 -0.1124 -0.2994 180 TYR B CA  
5749 C C   . TYR B 182 ? 1.3989 0.9231 1.0446 -0.3291 -0.0733 -0.2872 180 TYR B C   
5750 O O   . TYR B 182 ? 1.4501 0.9271 1.0296 -0.2856 -0.0526 -0.2870 180 TYR B O   
5751 C CB  . TYR B 182 ? 1.3074 0.9846 0.9328 -0.2848 -0.0997 -0.2712 180 TYR B CB  
5752 C CG  . TYR B 182 ? 1.3004 1.0593 0.9406 -0.2898 -0.1399 -0.2711 180 TYR B CG  
5753 C CD1 . TYR B 182 ? 1.2235 1.0648 0.9642 -0.3110 -0.1490 -0.2443 180 TYR B CD1 
5754 C CD2 . TYR B 182 ? 1.3210 1.0719 0.8717 -0.2721 -0.1708 -0.2994 180 TYR B CD2 
5755 C CE1 . TYR B 182 ? 1.1790 1.0917 0.9402 -0.3130 -0.1915 -0.2400 180 TYR B CE1 
5756 C CE2 . TYR B 182 ? 1.3256 1.1485 0.8807 -0.2757 -0.2134 -0.2934 180 TYR B CE2 
5757 C CZ  . TYR B 182 ? 1.2777 1.1803 0.9433 -0.2961 -0.2260 -0.2612 180 TYR B CZ  
5758 O OH  . TYR B 182 ? 1.2286 1.2004 0.9052 -0.2962 -0.2733 -0.2502 180 TYR B OH  
5759 N N   . VAL B 183 ? 1.3601 0.8687 1.0752 -0.3740 -0.0624 -0.2735 181 VAL B N   
5760 C CA  . VAL B 183 ? 1.3487 0.7735 1.0551 -0.3777 -0.0286 -0.2531 181 VAL B CA  
5761 C C   . VAL B 183 ? 1.2514 0.7325 0.9910 -0.3695 0.0092  -0.2037 181 VAL B C   
5762 O O   . VAL B 183 ? 1.2110 0.7761 1.0212 -0.3938 0.0126  -0.1906 181 VAL B O   
5763 C CB  . VAL B 183 ? 1.3542 0.7233 1.1143 -0.4302 -0.0388 -0.2634 181 VAL B CB  
5764 C CG1 . VAL B 183 ? 1.3950 0.6663 1.1358 -0.4290 -0.0066 -0.2353 181 VAL B CG1 
5765 C CG2 . VAL B 183 ? 1.4183 0.7596 1.1660 -0.4296 -0.0871 -0.3158 181 VAL B CG2 
5766 N N   . PHE B 184 ? 1.3081 0.7428 0.9988 -0.3336 0.0351  -0.1799 182 PHE B N   
5767 C CA  . PHE B 184 ? 1.2921 0.7745 0.9940 -0.3168 0.0636  -0.1399 182 PHE B CA  
5768 C C   . PHE B 184 ? 1.3520 0.7681 1.0455 -0.3370 0.0912  -0.1085 182 PHE B C   
5769 O O   . PHE B 184 ? 1.4824 0.7975 1.1476 -0.3453 0.0896  -0.1109 182 PHE B O   
5770 C CB  . PHE B 184 ? 1.2881 0.7800 0.9440 -0.2575 0.0666  -0.1319 182 PHE B CB  
5771 C CG  . PHE B 184 ? 1.2306 0.8005 0.8956 -0.2356 0.0496  -0.1459 182 PHE B CG  
5772 C CD1 . PHE B 184 ? 1.3023 0.8507 0.9264 -0.2216 0.0308  -0.1774 182 PHE B CD1 
5773 C CD2 . PHE B 184 ? 1.0508 0.7107 0.7602 -0.2274 0.0531  -0.1269 182 PHE B CD2 
5774 C CE1 . PHE B 184 ? 1.1975 0.8169 0.8189 -0.2014 0.0184  -0.1813 182 PHE B CE1 
5775 C CE2 . PHE B 184 ? 1.0793 0.8044 0.8002 -0.2087 0.0378  -0.1305 182 PHE B CE2 
5776 C CZ  . PHE B 184 ? 1.1687 0.8755 0.8423 -0.1962 0.0219  -0.1533 182 PHE B CZ  
5777 N N   . THR B 185 ? 1.3054 0.7752 1.0196 -0.3431 0.1167  -0.0783 183 THR B N   
5778 C CA  . THR B 185 ? 1.2964 0.7144 0.9845 -0.3567 0.1473  -0.0394 183 THR B CA  
5779 C C   . THR B 185 ? 1.2348 0.6645 0.8711 -0.3091 0.1547  -0.0151 183 THR B C   
5780 O O   . THR B 185 ? 1.2482 0.7640 0.9050 -0.2928 0.1553  -0.0193 183 THR B O   
5781 C CB  . THR B 185 ? 1.3056 0.7767 1.0534 -0.4071 0.1759  -0.0259 183 THR B CB  
5782 O OG1 . THR B 185 ? 1.2782 0.7473 1.0920 -0.4534 0.1614  -0.0505 183 THR B OG1 
5783 C CG2 . THR B 185 ? 1.3246 0.7372 1.0302 -0.4226 0.2131  0.0212  183 THR B CG2 
5784 N N   . GLY B 186 ? 1.3166 0.6575 0.8923 -0.2867 0.1555  0.0094  184 GLY B N   
5785 C CA  . GLY B 186 ? 1.3699 0.7189 0.8990 -0.2423 0.1541  0.0332  184 GLY B CA  
5786 C C   . GLY B 186 ? 1.3859 0.7585 0.8890 -0.2586 0.1809  0.0662  184 GLY B C   
5787 O O   . GLY B 186 ? 1.4571 0.8203 0.9713 -0.3042 0.2093  0.0815  184 GLY B O   
5788 N N   . TYR B 187 ? 1.3594 0.7651 0.8274 -0.2207 0.1721  0.0761  185 TYR B N   
5789 C CA  . TYR B 187 ? 1.4065 0.8403 0.8315 -0.2273 0.1943  0.0992  185 TYR B CA  
5790 C C   . TYR B 187 ? 1.4243 0.8444 0.7866 -0.1784 0.1683  0.1166  185 TYR B C   
5791 O O   . TYR B 187 ? 1.3201 0.7616 0.7094 -0.1411 0.1362  0.0980  185 TYR B O   
5792 C CB  . TYR B 187 ? 1.2172 0.7579 0.6980 -0.2415 0.2080  0.0683  185 TYR B CB  
5793 C CG  . TYR B 187 ? 1.2318 0.8020 0.7801 -0.2919 0.2356  0.0567  185 TYR B CG  
5794 C CD1 . TYR B 187 ? 1.2908 0.8593 0.8266 -0.3298 0.2802  0.0811  185 TYR B CD1 
5795 C CD2 . TYR B 187 ? 1.1586 0.7646 0.7857 -0.3014 0.2167  0.0235  185 TYR B CD2 
5796 C CE1 . TYR B 187 ? 1.2522 0.8582 0.8704 -0.3773 0.3044  0.0706  185 TYR B CE1 
5797 C CE2 . TYR B 187 ? 1.1848 0.8238 0.8834 -0.3468 0.2328  0.0117  185 TYR B CE2 
5798 C CZ  . TYR B 187 ? 1.2205 0.8619 0.9235 -0.3853 0.2763  0.0342  185 TYR B CZ  
5799 O OH  . TYR B 187 ? 1.2930 0.9770 1.0869 -0.4318 0.2915  0.0228  185 TYR B OH  
5800 N N   . ARG B 188 ? 1.4872 0.8755 0.7673 -0.1792 0.1818  0.1543  186 ARG B N   
5801 C CA  . ARG B 188 ? 1.5556 0.9341 0.7678 -0.1347 0.1506  0.1721  186 ARG B CA  
5802 C C   . ARG B 188 ? 1.5560 0.9987 0.7207 -0.1360 0.1633  0.1642  186 ARG B C   
5803 O O   . ARG B 188 ? 1.5645 1.0169 0.7001 -0.1707 0.2089  0.1757  186 ARG B O   
5804 C CB  . ARG B 188 ? 1.6057 0.8765 0.7402 -0.1245 0.1445  0.2281  186 ARG B CB  
5805 N N   . VAL B 189 ? 1.5315 1.0184 0.6920 -0.0978 0.1238  0.1423  187 VAL B N   
5806 C CA  . VAL B 189 ? 1.5915 1.1395 0.7109 -0.0933 0.1274  0.1194  187 VAL B CA  
5807 C C   . VAL B 189 ? 1.6706 1.1705 0.6501 -0.0854 0.1320  0.1621  187 VAL B C   
5808 O O   . VAL B 189 ? 1.7547 1.1990 0.6793 -0.0553 0.0925  0.1959  187 VAL B O   
5809 C CB  . VAL B 189 ? 1.5083 1.1149 0.6827 -0.0585 0.0769  0.0783  187 VAL B CB  
5810 C CG1 . VAL B 189 ? 1.4376 1.0901 0.5550 -0.0488 0.0713  0.0499  187 VAL B CG1 
5811 C CG2 . VAL B 189 ? 1.4060 1.0656 0.7091 -0.0695 0.0800  0.0426  187 VAL B CG2 
5812 N N   . THR B 190 ? 1.6732 1.1976 0.5945 -0.1101 0.1810  0.1628  188 THR B N   
5813 C CA  . THR B 190 ? 1.8071 1.2993 0.5793 -0.1033 0.1933  0.2017  188 THR B CA  
5814 C C   . THR B 190 ? 1.8641 1.4328 0.5966 -0.0844 0.1878  0.1513  188 THR B C   
5815 O O   . THR B 190 ? 1.7900 1.4216 0.6042 -0.0817 0.1805  0.0906  188 THR B O   
5816 C CB  . THR B 190 ? 1.8358 1.3173 0.6130 -0.1424 0.2558  0.2448  188 THR B CB  
5817 O OG1 . THR B 190 ? 1.7983 1.3620 0.6179 -0.1668 0.3093  0.2083  188 THR B OG1 
5818 C CG2 . THR B 190 ? 1.8018 1.2166 0.6518 -0.1703 0.2646  0.2724  188 THR B CG2 
5819 N N   . LYS B 191 ? 1.9088 1.4834 0.5422 -0.0678 0.1848  0.1743  189 LYS B N   
5820 C CA  . LYS B 191 ? 1.9936 1.6347 0.5741 -0.0454 0.1737  0.1239  189 LYS B CA  
5821 C C   . LYS B 191 ? 1.9706 1.6834 0.6230 -0.0627 0.2214  0.0626  189 LYS B C   
5822 O O   . LYS B 191 ? 1.9731 1.7241 0.6549 -0.0447 0.1913  -0.0029 189 LYS B O   
5823 C CB  . LYS B 191 ? 2.1173 1.7647 0.5815 -0.0391 0.1901  0.1645  189 LYS B CB  
5824 N N   . ASN B 192 ? 1.9299 1.6625 0.6244 -0.0972 0.2930  0.0828  190 ASN B N   
5825 C CA  . ASN B 192 ? 1.8021 1.6091 0.5764 -0.1106 0.3409  0.0293  190 ASN B CA  
5826 C C   . ASN B 192 ? 1.7492 1.5601 0.6505 -0.1536 0.3797  0.0385  190 ASN B C   
5827 O O   . ASN B 192 ? 1.6969 1.5742 0.6816 -0.1677 0.4222  0.0027  190 ASN B O   
5828 C CB  . ASN B 192 ? 1.9212 1.7811 0.6318 -0.1044 0.3939  0.0315  190 ASN B CB  
5829 C CG  . ASN B 192 ? 1.9843 1.8882 0.6270 -0.0623 0.3665  -0.0314 190 ASN B CG  
5830 O OD1 . ASN B 192 ? 1.9926 1.8903 0.6542 -0.0418 0.3071  -0.0808 190 ASN B OD1 
5831 N ND2 . ASN B 192 ? 2.0983 2.0486 0.6647 -0.0495 0.4088  -0.0319 190 ASN B ND2 
5832 N N   . SER B 193 ? 1.6726 1.4170 0.5972 -0.1724 0.3631  0.0819  191 SER B N   
5833 C CA  . SER B 193 ? 1.5614 1.3132 0.6081 -0.2130 0.3906  0.0821  191 SER B CA  
5834 C C   . SER B 193 ? 1.5535 1.2299 0.6231 -0.2151 0.3472  0.1094  191 SER B C   
5835 O O   . SER B 193 ? 1.5509 1.1917 0.5780 -0.1787 0.2906  0.1124  191 SER B O   
5836 C CB  . SER B 193 ? 1.6234 1.3960 0.7013 -0.2472 0.4528  0.1171  191 SER B CB  
5837 O OG  . SER B 193 ? 1.6211 1.4154 0.8312 -0.2862 0.4721  0.1074  191 SER B OG  
5838 N N   . LYS B 194 ? 1.5816 1.2425 0.7372 -0.2531 0.3681  0.1248  192 LYS B N   
5839 C CA  . LYS B 194 ? 1.5346 1.1329 0.7367 -0.2540 0.3299  0.1395  192 LYS B CA  
5840 C C   . LYS B 194 ? 1.6529 1.1756 0.8366 -0.2943 0.3636  0.1939  192 LYS B C   
5841 O O   . LYS B 194 ? 1.5785 1.1365 0.7867 -0.3221 0.4087  0.2084  192 LYS B O   
5842 C CB  . LYS B 194 ? 1.3896 1.0427 0.7261 -0.2615 0.3122  0.0928  192 LYS B CB  
5843 C CG  . LYS B 194 ? 1.3862 1.1032 0.8061 -0.3040 0.3605  0.0774  192 LYS B CG  
5844 C CD  . LYS B 194 ? 1.3242 1.0894 0.8701 -0.3114 0.3356  0.0386  192 LYS B CD  
5845 C CE  . LYS B 194 ? 1.3418 1.1759 0.9824 -0.3520 0.3777  0.0253  192 LYS B CE  
5846 N NZ  . LYS B 194 ? 1.1756 1.0555 0.9328 -0.3577 0.3455  -0.0082 192 LYS B NZ  
5847 N N   . VAL B 195 ? 1.6789 1.1145 0.8564 -0.2856 0.3291  0.2177  193 VAL B N   
5848 C CA  . VAL B 195 ? 1.7272 1.0880 0.9226 -0.3192 0.3457  0.2590  193 VAL B CA  
5849 C C   . VAL B 195 ? 1.6055 0.9222 0.8771 -0.3285 0.3173  0.2344  193 VAL B C   
5850 O O   . VAL B 195 ? 1.6172 0.9199 0.8892 -0.2857 0.2707  0.2135  193 VAL B O   
5851 C CB  . VAL B 195 ? 1.7901 1.0718 0.8924 -0.2951 0.3317  0.3176  193 VAL B CB  
5852 C CG1 . VAL B 195 ? 1.8778 1.1180 0.9127 -0.2417 0.2788  0.3154  193 VAL B CG1 
5853 C CG2 . VAL B 195 ? 1.8443 1.0431 0.9900 -0.3229 0.3352  0.3529  193 VAL B CG2 
5854 N N   . GLN B 196 ? 1.6160 0.9324 0.9720 -0.3756 0.3370  0.2292  194 GLN B N   
5855 C CA  . GLN B 196 ? 1.6107 0.8766 1.0284 -0.3871 0.3081  0.2025  194 GLN B CA  
5856 C C   . GLN B 196 ? 1.6626 0.8076 1.0239 -0.3582 0.2784  0.2289  194 GLN B C   
5857 O O   . GLN B 196 ? 1.7340 0.8261 1.0521 -0.3545 0.2859  0.2784  194 GLN B O   
5858 C CB  . GLN B 196 ? 1.5479 0.8355 1.0678 -0.4382 0.3238  0.1951  194 GLN B CB  
5859 C CG  . GLN B 196 ? 1.4923 0.9013 1.0993 -0.4618 0.3412  0.1588  194 GLN B CG  
5860 C CD  . GLN B 196 ? 1.5673 0.9924 1.2885 -0.5009 0.3277  0.1343  194 GLN B CD  
5861 O OE1 . GLN B 196 ? 1.5461 0.8882 1.2783 -0.5123 0.3052  0.1385  194 GLN B OE1 
5862 N NE2 . GLN B 196 ? 1.5003 1.0330 1.3110 -0.5180 0.3365  0.1069  194 GLN B NE2 
5863 N N   . ILE B 197 ? 1.6424 0.7741 1.0290 -0.3242 0.2372  0.1896  195 ILE B N   
5864 C CA  . ILE B 197 ? 1.7034 0.7296 1.0501 -0.2868 0.2086  0.2053  195 ILE B CA  
5865 C C   . ILE B 197 ? 1.8534 0.8231 1.2548 -0.2976 0.1902  0.1657  195 ILE B C   
5866 O O   . ILE B 197 ? 1.9462 0.8380 1.3311 -0.2597 0.1652  0.1597  195 ILE B O   
5867 C CB  . ILE B 197 ? 1.7333 0.7968 1.0466 -0.2211 0.1775  0.1966  195 ILE B CB  
5868 C CG1 . ILE B 197 ? 1.8769 0.8355 1.1371 -0.1802 0.1549  0.2346  195 ILE B CG1 
5869 C CG2 . ILE B 197 ? 1.5852 0.7132 0.9591 -0.1996 0.1558  0.1379  195 ILE B CG2 
5870 C CD1 . ILE B 197 ? 1.9018 0.7913 1.0887 -0.1979 0.1736  0.3039  195 ILE B CD1 
5871 N N   . GLY B 198 ? 1.7871 0.7971 1.2552 -0.3469 0.2001  0.1348  196 GLY B N   
5872 C CA  . GLY B 198 ? 1.7396 0.6906 1.2510 -0.3636 0.1787  0.0937  196 GLY B CA  
5873 C C   . GLY B 198 ? 1.6310 0.6730 1.1916 -0.3637 0.1594  0.0334  196 GLY B C   
5874 O O   . GLY B 198 ? 1.5886 0.7301 1.1493 -0.3369 0.1580  0.0235  196 GLY B O   
5875 N N   . GLU B 199 ? 1.6218 0.6273 1.2235 -0.3942 0.1407  -0.0064 197 GLU B N   
5876 C CA  . GLU B 199 ? 1.5690 0.6481 1.2011 -0.3899 0.1147  -0.0623 197 GLU B CA  
5877 C C   . GLU B 199 ? 1.5930 0.6310 1.1747 -0.3319 0.0910  -0.0964 197 GLU B C   
5878 O O   . GLU B 199 ? 1.6659 0.5978 1.2112 -0.3077 0.0886  -0.0908 197 GLU B O   
5879 C CB  . GLU B 199 ? 1.5995 0.6932 1.3087 -0.4394 0.0960  -0.0905 197 GLU B CB  
5880 C CG  . GLU B 199 ? 1.5581 0.7554 1.3463 -0.4823 0.1161  -0.0685 197 GLU B CG  
5881 C CD  . GLU B 199 ? 1.5805 0.8117 1.4645 -0.5220 0.0883  -0.0958 197 GLU B CD  
5882 O OE1 . GLU B 199 ? 1.5799 0.7368 1.4932 -0.5419 0.0767  -0.0943 197 GLU B OE1 
5883 O OE2 . GLU B 199 ? 1.5320 0.8635 1.4693 -0.5321 0.0742  -0.1171 197 GLU B OE2 
5884 N N   . TYR B 200 ? 1.5660 0.6896 1.1491 -0.3080 0.0760  -0.1294 198 TYR B N   
5885 C CA  . TYR B 200 ? 1.5912 0.7001 1.1273 -0.2487 0.0652  -0.1555 198 TYR B CA  
5886 C C   . TYR B 200 ? 1.5707 0.7432 1.1077 -0.2470 0.0433  -0.2020 198 TYR B C   
5887 O O   . TYR B 200 ? 1.5466 0.8011 1.1259 -0.2799 0.0347  -0.2043 198 TYR B O   
5888 C CB  . TYR B 200 ? 1.6095 0.7728 1.1300 -0.1992 0.0800  -0.1217 198 TYR B CB  
5889 C CG  . TYR B 200 ? 1.6320 0.7259 1.1287 -0.1809 0.0923  -0.0782 198 TYR B CG  
5890 C CD1 . TYR B 200 ? 1.6660 0.7622 1.1686 -0.2140 0.1083  -0.0345 198 TYR B CD1 
5891 C CD2 . TYR B 200 ? 1.6876 0.7195 1.1545 -0.1268 0.0884  -0.0788 198 TYR B CD2 
5892 C CE1 . TYR B 200 ? 1.7024 0.7351 1.1690 -0.1958 0.1156  0.0109  198 TYR B CE1 
5893 C CE2 . TYR B 200 ? 1.8002 0.7696 1.2464 -0.1069 0.0920  -0.0344 198 TYR B CE2 
5894 C CZ  . TYR B 200 ? 1.7926 0.7605 1.2322 -0.1423 0.1033  0.0123  198 TYR B CZ  
5895 O OH  . TYR B 200 ? 1.8960 0.8005 1.3009 -0.1216 0.1032  0.0619  198 TYR B OH  
5896 N N   . THR B 201 ? 1.6269 0.7608 1.1142 -0.2047 0.0352  -0.2381 199 THR B N   
5897 C CA  . THR B 201 ? 1.6081 0.7945 1.0685 -0.1915 0.0172  -0.2798 199 THR B CA  
5898 C C   . THR B 201 ? 1.6211 0.8253 1.0388 -0.1240 0.0360  -0.2800 199 THR B C   
5899 O O   . THR B 201 ? 1.7255 0.8545 1.1232 -0.0888 0.0494  -0.2805 199 THR B O   
5900 C CB  . THR B 201 ? 1.6098 0.7188 1.0449 -0.2165 -0.0130 -0.3387 199 THR B CB  
5901 O OG1 . THR B 201 ? 1.6509 0.8006 1.1401 -0.2782 -0.0379 -0.3430 199 THR B OG1 
5902 C CG2 . THR B 201 ? 1.7183 0.8403 1.0802 -0.1742 -0.0229 -0.3870 199 THR B CG2 
5903 N N   . PHE B 202 ? 1.4973 0.8018 0.9102 -0.1057 0.0380  -0.2757 200 PHE B N   
5904 C CA  . PHE B 202 ? 1.5220 0.8641 0.9153 -0.0467 0.0626  -0.2651 200 PHE B CA  
5905 C C   . PHE B 202 ? 1.5414 0.9130 0.8736 -0.0231 0.0610  -0.3018 200 PHE B C   
5906 O O   . PHE B 202 ? 1.5726 0.9586 0.8806 -0.0536 0.0337  -0.3276 200 PHE B O   
5907 C CB  . PHE B 202 ? 1.4558 0.8983 0.9052 -0.0417 0.0740  -0.2136 200 PHE B CB  
5908 C CG  . PHE B 202 ? 1.3960 0.8217 0.8891 -0.0576 0.0774  -0.1774 200 PHE B CG  
5909 C CD1 . PHE B 202 ? 1.3832 0.8195 0.9086 -0.1089 0.0669  -0.1666 200 PHE B CD1 
5910 C CD2 . PHE B 202 ? 1.4677 0.8744 0.9691 -0.0194 0.0913  -0.1533 200 PHE B CD2 
5911 C CE1 . PHE B 202 ? 1.4484 0.8726 0.9976 -0.1216 0.0755  -0.1331 200 PHE B CE1 
5912 C CE2 . PHE B 202 ? 1.5048 0.8964 1.0285 -0.0322 0.0905  -0.1190 200 PHE B CE2 
5913 C CZ  . PHE B 202 ? 1.4626 0.8617 1.0023 -0.0832 0.0853  -0.1091 200 PHE B CZ  
5914 N N   . GLU B 203 ? 1.5574 0.9425 0.8650 0.0331  0.0908  -0.3025 201 GLU B N   
5915 C CA  . GLU B 203 ? 1.5834 1.0133 0.8265 0.0630  0.1025  -0.3262 201 GLU B CA  
5916 C C   . GLU B 203 ? 1.5412 1.0315 0.8075 0.1169  0.1455  -0.2952 201 GLU B C   
5917 O O   . GLU B 203 ? 1.5497 1.0180 0.8665 0.1403  0.1606  -0.2758 201 GLU B O   
5918 C CB  . GLU B 203 ? 1.6040 0.9442 0.7589 0.0752  0.0932  -0.3976 201 GLU B CB  
5919 C CG  . GLU B 203 ? 1.6672 1.0597 0.7334 0.0951  0.0972  -0.4238 201 GLU B CG  
5920 C CD  . GLU B 203 ? 1.7973 1.1408 0.8118 0.0837  0.0653  -0.4897 201 GLU B CD  
5921 O OE1 . GLU B 203 ? 1.8470 1.1017 0.8921 0.0631  0.0435  -0.5194 201 GLU B OE1 
5922 O OE2 . GLU B 203 ? 1.8537 1.2540 0.8052 0.0929  0.0615  -0.5077 201 GLU B OE2 
5923 N N   . LYS B 204 ? 1.5221 1.0913 0.7537 0.1355  0.1636  -0.2876 202 LYS B N   
5924 C CA  . LYS B 204 ? 1.4786 1.1225 0.7464 0.1805  0.2082  -0.2523 202 LYS B CA  
5925 C C   . LYS B 204 ? 1.5743 1.1654 0.8256 0.2366  0.2424  -0.2850 202 LYS B C   
5926 O O   . LYS B 204 ? 1.6597 1.1614 0.8396 0.2479  0.2368  -0.3442 202 LYS B O   
5927 C CB  . LYS B 204 ? 1.4874 1.2163 0.7062 0.1870  0.2244  -0.2368 202 LYS B CB  
5928 C CG  . LYS B 204 ? 1.4218 1.2452 0.6968 0.2215  0.2722  -0.1869 202 LYS B CG  
5929 C CD  . LYS B 204 ? 1.4693 1.3614 0.6714 0.2289  0.2928  -0.1718 202 LYS B CD  
5930 C CE  . LYS B 204 ? 1.3864 1.3784 0.6575 0.2559  0.3443  -0.1128 202 LYS B CE  
5931 N NZ  . LYS B 204 ? 1.5268 1.5830 0.7216 0.2603  0.3673  -0.0882 202 LYS B NZ  
5932 N N   . GLY B 205 ? 1.5185 1.1660 0.8461 0.2729  0.2757  -0.2483 203 GLY B N   
5933 C CA  . GLY B 205 ? 1.5331 1.1475 0.8687 0.3329  0.3109  -0.2733 203 GLY B CA  
5934 C C   . GLY B 205 ? 1.4362 1.1553 0.8504 0.3746  0.3577  -0.2325 203 GLY B C   
5935 O O   . GLY B 205 ? 1.5770 1.2924 1.0028 0.4314  0.3970  -0.2536 203 GLY B O   
5936 N N   . ALA B 210 ? 1.1136 1.1784 0.9743 0.3012  0.0324  0.0365  208 ALA B N   
5937 C CA  . ALA B 210 ? 1.1106 1.1798 0.9653 0.3337  0.0409  0.0134  208 ALA B CA  
5938 C C   . ALA B 210 ? 1.2187 1.2043 1.0385 0.3114  0.0455  -0.0206 208 ALA B C   
5939 O O   . ALA B 210 ? 1.2146 1.2219 1.0370 0.3182  0.0510  -0.0468 208 ALA B O   
5940 C CB  . ALA B 210 ? 1.0216 1.1957 0.9199 0.3319  0.0480  0.0151  208 ALA B CB  
5941 N N   . VAL B 211 ? 1.2399 1.1335 1.0260 0.2833  0.0445  -0.0217 209 VAL B N   
5942 C CA  . VAL B 211 ? 1.2963 1.1144 1.0550 0.2491  0.0508  -0.0574 209 VAL B CA  
5943 C C   . VAL B 211 ? 1.3657 1.0539 1.0658 0.2617  0.0555  -0.0589 209 VAL B C   
5944 O O   . VAL B 211 ? 1.3870 1.0383 1.0629 0.2891  0.0520  -0.0265 209 VAL B O   
5945 C CB  . VAL B 211 ? 1.2183 1.0506 0.9933 0.1848  0.0513  -0.0627 209 VAL B CB  
5946 C CG1 . VAL B 211 ? 1.1055 1.0492 0.9274 0.1780  0.0464  -0.0593 209 VAL B CG1 
5947 C CG2 . VAL B 211 ? 1.2373 1.0238 0.9939 0.1636  0.0508  -0.0310 209 VAL B CG2 
5948 N N   . VAL B 212 ? 1.3944 1.0107 1.0680 0.2425  0.0632  -0.0990 210 VAL B N   
5949 C CA  . VAL B 212 ? 1.5180 0.9880 1.1282 0.2432  0.0720  -0.1071 210 VAL B CA  
5950 C C   . VAL B 212 ? 1.5813 0.9933 1.1803 0.1653  0.0838  -0.1223 210 VAL B C   
5951 O O   . VAL B 212 ? 1.5313 0.9931 1.1618 0.1226  0.0855  -0.1609 210 VAL B O   
5952 C CB  . VAL B 212 ? 1.5663 0.9924 1.1528 0.2788  0.0738  -0.1480 210 VAL B CB  
5953 C CG1 . VAL B 212 ? 1.6875 0.9500 1.2097 0.2540  0.0866  -0.1704 210 VAL B CG1 
5954 C CG2 . VAL B 212 ? 1.5280 0.9900 1.1114 0.3618  0.0660  -0.1292 210 VAL B CG2 
5955 N N   . TYR B 213 ? 1.7236 1.0362 1.2759 0.1482  0.0928  -0.0928 211 TYR B N   
5956 C CA  . TYR B 213 ? 1.7392 1.0034 1.2804 0.0703  0.1088  -0.1019 211 TYR B CA  
5957 C C   . TYR B 213 ? 1.8180 0.9194 1.2934 0.0463  0.1286  -0.1246 211 TYR B C   
5958 O O   . TYR B 213 ? 1.8692 0.8572 1.2823 0.0944  0.1308  -0.1053 211 TYR B O   
5959 C CB  . TYR B 213 ? 1.7183 0.9883 1.2499 0.0562  0.1096  -0.0524 211 TYR B CB  
5960 C CG  . TYR B 213 ? 1.7971 0.9768 1.2655 0.1089  0.1079  -0.0048 211 TYR B CG  
5961 C CD1 . TYR B 213 ? 1.7377 0.9934 1.2249 0.1771  0.0875  0.0248  211 TYR B CD1 
5962 C CD2 . TYR B 213 ? 1.9040 0.9252 1.2916 0.0898  0.1278  0.0107  211 TYR B CD2 
5963 C CE1 . TYR B 213 ? 1.7870 0.9745 1.2168 0.2322  0.0824  0.0648  211 TYR B CE1 
5964 C CE2 . TYR B 213 ? 1.9829 0.9178 1.3022 0.1469  0.1245  0.0561  211 TYR B CE2 
5965 C CZ  . TYR B 213 ? 1.9322 0.9568 1.2744 0.2215  0.0996  0.0814  211 TYR B CZ  
5966 O OH  . TYR B 213 ? 1.9381 0.8903 1.2127 0.2856  0.0929  0.1228  211 TYR B OH  
5967 N N   . ARG B 214 ? 1.8323 0.9232 1.3209 -0.0280 0.1434  -0.1679 212 ARG B N   
5968 C CA  . ARG B 214 ? 1.9623 0.9010 1.3952 -0.0725 0.1670  -0.1975 212 ARG B CA  
5969 C C   . ARG B 214 ? 1.9484 0.8550 1.3731 -0.1596 0.1916  -0.1921 212 ARG B C   
5970 O O   . ARG B 214 ? 1.8811 0.8542 1.3519 -0.2267 0.1994  -0.2388 212 ARG B O   
5971 C CB  . ARG B 214 ? 1.8892 0.8546 1.3502 -0.0854 0.1635  -0.2683 212 ARG B CB  
5972 N N   . GLY B 215 ? 1.9993 0.8101 1.3632 -0.1557 0.2043  -0.1364 213 GLY B N   
5973 C CA  . GLY B 215 ? 1.9991 0.7814 1.3478 -0.2334 0.2306  -0.1230 213 GLY B CA  
5974 C C   . GLY B 215 ? 2.1936 0.7940 1.4702 -0.2941 0.2674  -0.1385 213 GLY B C   
5975 O O   . GLY B 215 ? 2.2808 0.7308 1.4865 -0.2569 0.2726  -0.1315 213 GLY B O   
5976 N N   . THR B 216 ? 2.1589 0.7888 1.4594 -0.3862 0.2925  -0.1601 214 THR B N   
5977 C CA  . THR B 216 ? 2.2566 0.7968 1.5242 -0.4373 0.3202  -0.1671 214 THR B CA  
5978 C C   . THR B 216 ? 2.4220 0.8082 1.5882 -0.4045 0.3348  -0.0998 214 THR B C   
5979 O O   . THR B 216 ? 2.5501 0.8030 1.6565 -0.3838 0.3422  -0.0963 214 THR B O   
5980 C CB  . THR B 216 ? 2.1629 0.8137 1.4889 -0.5261 0.3399  -0.1945 214 THR B CB  
5981 N N   . THR B 217 ? 2.4027 0.8111 1.5474 -0.3954 0.3371  -0.0474 215 THR B N   
5982 C CA  . THR B 217 ? 2.4522 0.7384 1.5020 -0.3512 0.3447  0.0175  215 THR B CA  
5983 C C   . THR B 217 ? 2.5201 0.7926 1.5422 -0.2464 0.3122  0.0537  215 THR B C   
5984 O O   . THR B 217 ? 2.4115 0.7628 1.4861 -0.2154 0.2884  0.0307  215 THR B O   
5985 C CB  . THR B 217 ? 2.4542 0.7829 1.4951 -0.3932 0.3629  0.0520  215 THR B CB  
5986 O OG1 . THR B 217 ? 2.5865 0.8064 1.5338 -0.3399 0.3657  0.1139  215 THR B OG1 
5987 C CG2 . THR B 217 ? 2.3015 0.7857 1.4093 -0.3916 0.3433  0.0545  215 THR B CG2 
5988 N N   . THR B 218 ? 2.5446 0.7260 1.4849 -0.1869 0.3102  0.1087  216 THR B N   
5989 C CA  . THR B 218 ? 2.5505 0.7429 1.4686 -0.0810 0.2772  0.1441  216 THR B CA  
5990 C C   . THR B 218 ? 2.5114 0.7454 1.4028 -0.0553 0.2705  0.2004  216 THR B C   
5991 O O   . THR B 218 ? 2.6043 0.7656 1.4346 -0.0720 0.2902  0.2290  216 THR B O   
5992 C CB  . THR B 218 ? 2.6356 0.7038 1.4855 -0.0121 0.2714  0.1497  216 THR B CB  
5993 O OG1 . THR B 218 ? 2.6855 0.7818 1.5093 0.0912  0.2411  0.1907  216 THR B OG1 
5994 C CG2 . THR B 218 ? 2.8331 0.7623 1.6054 -0.0514 0.3035  0.1636  216 THR B CG2 
5995 N N   . TYR B 219 ? 2.4186 0.7724 1.3557 -0.0138 0.2423  0.2146  217 TYR B N   
5996 C CA  . TYR B 219 ? 2.3603 0.7813 1.2842 0.0191  0.2278  0.2620  217 TYR B CA  
5997 C C   . TYR B 219 ? 2.2810 0.7956 1.2343 0.1117  0.1871  0.2761  217 TYR B C   
5998 O O   . TYR B 219 ? 2.2756 0.8919 1.3115 0.1220  0.1690  0.2389  217 TYR B O   
5999 C CB  . TYR B 219 ? 2.2773 0.7955 1.2479 -0.0597 0.2407  0.2588  217 TYR B CB  
6000 C CG  . TYR B 219 ? 2.3791 0.8365 1.3156 -0.1336 0.2771  0.2601  217 TYR B CG  
6001 C CD1 . TYR B 219 ? 2.4529 0.8855 1.3321 -0.1152 0.2814  0.3038  217 TYR B CD1 
6002 C CD2 . TYR B 219 ? 2.3860 0.8216 1.3514 -0.2199 0.3065  0.2146  217 TYR B CD2 
6003 C CE1 . TYR B 219 ? 2.4654 0.8414 1.3107 -0.1803 0.3169  0.3071  217 TYR B CE1 
6004 C CE2 . TYR B 219 ? 2.3998 0.7924 1.3386 -0.2862 0.3405  0.2147  217 TYR B CE2 
6005 C CZ  . TYR B 219 ? 2.4852 0.8422 1.3612 -0.2662 0.3471  0.2632  217 TYR B CZ  
6006 O OH  . TYR B 219 ? 2.5947 0.9057 1.4408 -0.3311 0.3833  0.2654  217 TYR B OH  
6007 N N   . LYS B 220 ? 2.2652 0.8091 1.1874 0.1754  0.1672  0.3146  218 LYS B N   
6008 C CA  . LYS B 220 ? 2.1249 0.7899 1.0872 0.2603  0.1271  0.3247  218 LYS B CA  
6009 C C   . LYS B 220 ? 2.0471 0.8858 1.1018 0.2271  0.1116  0.3155  218 LYS B C   
6010 O O   . LYS B 220 ? 2.0531 0.9648 1.1077 0.2364  0.0985  0.3412  218 LYS B O   
6011 C CB  . LYS B 220 ? 2.1939 0.8563 1.1062 0.3282  0.1107  0.3573  218 LYS B CB  
6012 N N   . LEU B 221 ? 2.0147 0.9408 1.1621 0.1851  0.1112  0.2690  219 LEU B N   
6013 C CA  . LEU B 221 ? 1.8744 0.9757 1.1229 0.1485  0.0967  0.2494  219 LEU B CA  
6014 C C   . LEU B 221 ? 1.7842 1.0094 1.0674 0.2118  0.0623  0.2685  219 LEU B C   
6015 O O   . LEU B 221 ? 1.8051 1.0303 1.0752 0.2866  0.0447  0.2779  219 LEU B O   
6016 C CB  . LEU B 221 ? 1.7362 0.9071 1.0675 0.1183  0.0968  0.1996  219 LEU B CB  
6017 C CG  . LEU B 221 ? 1.7953 0.9302 1.1376 0.0326  0.1244  0.1658  219 LEU B CG  
6018 C CD1 . LEU B 221 ? 1.9577 0.9091 1.2130 0.0164  0.1533  0.1672  219 LEU B CD1 
6019 C CD2 . LEU B 221 ? 1.7560 0.9941 1.1849 0.0178  0.1156  0.1180  219 LEU B CD2 
6020 N N   . ASN B 222 ? 1.6875 1.0245 1.0174 0.1809  0.0526  0.2701  220 ASN B N   
6021 C CA  . ASN B 222 ? 1.5663 1.0277 0.9339 0.2276  0.0209  0.2827  220 ASN B CA  
6022 C C   . ASN B 222 ? 1.4606 1.0670 0.9263 0.1826  0.0109  0.2553  220 ASN B C   
6023 O O   . ASN B 222 ? 1.4649 1.0738 0.9573 0.1196  0.0274  0.2323  220 ASN B O   
6024 C CB  . ASN B 222 ? 1.6640 1.0881 0.9552 0.2521  0.0159  0.3228  220 ASN B CB  
6025 C CG  . ASN B 222 ? 1.8057 1.1513 1.0460 0.1852  0.0450  0.3329  220 ASN B CG  
6026 O OD1 . ASN B 222 ? 1.8392 1.0591 1.0321 0.1501  0.0757  0.3308  220 ASN B OD1 
6027 N ND2 . ASN B 222 ? 1.8169 1.2395 1.0671 0.1652  0.0368  0.3411  220 ASN B ND2 
6028 N N   . VAL B 223 ? 1.3856 1.1139 0.9040 0.2174  -0.0164 0.2558  221 VAL B N   
6029 C CA  . VAL B 223 ? 1.1724 1.0271 0.7767 0.1798  -0.0264 0.2322  221 VAL B CA  
6030 C C   . VAL B 223 ? 1.2936 1.1456 0.8867 0.1223  -0.0171 0.2308  221 VAL B C   
6031 O O   . VAL B 223 ? 1.3466 1.1591 0.8798 0.1265  -0.0163 0.2553  221 VAL B O   
6032 C CB  . VAL B 223 ? 1.1628 1.1383 0.8137 0.2204  -0.0551 0.2354  221 VAL B CB  
6033 C CG1 . VAL B 223 ? 1.0778 1.1638 0.8081 0.1767  -0.0624 0.2121  221 VAL B CG1 
6034 C CG2 . VAL B 223 ? 1.1645 1.1581 0.8321 0.2774  -0.0616 0.2332  221 VAL B CG2 
6035 N N   . GLY B 224 ? 1.1582 1.0545 0.8045 0.0728  -0.0098 0.2019  222 GLY B N   
6036 C CA  . GLY B 224 ? 1.2009 1.1132 0.8470 0.0207  -0.0017 0.1931  222 GLY B CA  
6037 C C   . GLY B 224 ? 1.2242 1.0666 0.8499 -0.0270 0.0266  0.1768  222 GLY B C   
6038 O O   . GLY B 224 ? 1.1642 1.0456 0.8114 -0.0722 0.0336  0.1568  222 GLY B O   
6039 N N   . ASP B 225 ? 1.3143 1.0577 0.8995 -0.0180 0.0428  0.1813  223 ASP B N   
6040 C CA  . ASP B 225 ? 1.3233 1.0053 0.8957 -0.0690 0.0702  0.1586  223 ASP B CA  
6041 C C   . ASP B 225 ? 1.1867 0.9456 0.8316 -0.0881 0.0659  0.1167  223 ASP B C   
6042 O O   . ASP B 225 ? 1.1516 0.9541 0.8347 -0.0527 0.0503  0.1100  223 ASP B O   
6043 C CB  . ASP B 225 ? 1.4472 0.9970 0.9581 -0.0528 0.0870  0.1693  223 ASP B CB  
6044 C CG  . ASP B 225 ? 1.5369 0.9893 0.9586 -0.0305 0.0946  0.2139  223 ASP B CG  
6045 O OD1 . ASP B 225 ? 1.6109 1.0517 0.9999 -0.0670 0.1086  0.2274  223 ASP B OD1 
6046 O OD2 . ASP B 225 ? 1.5994 0.9871 0.9787 0.0277  0.0869  0.2356  223 ASP B OD2 
6047 N N   . TYR B 226 ? 1.1509 0.9314 0.8119 -0.1419 0.0804  0.0884  224 TYR B N   
6048 C CA  . TYR B 226 ? 1.0844 0.9451 0.8069 -0.1549 0.0739  0.0484  224 TYR B CA  
6049 C C   . TYR B 226 ? 1.1103 0.9347 0.8302 -0.1972 0.0957  0.0123  224 TYR B C   
6050 O O   . TYR B 226 ? 1.1427 0.8919 0.8195 -0.2339 0.1198  0.0160  224 TYR B O   
6051 C CB  . TYR B 226 ? 0.9741 0.9323 0.7322 -0.1687 0.0618  0.0399  224 TYR B CB  
6052 C CG  . TYR B 226 ? 0.9183 0.8857 0.6598 -0.2165 0.0778  0.0322  224 TYR B CG  
6053 C CD1 . TYR B 226 ? 0.9872 0.9318 0.6865 -0.2187 0.0811  0.0647  224 TYR B CD1 
6054 C CD2 . TYR B 226 ? 0.9081 0.9212 0.6772 -0.2554 0.0885  -0.0094 224 TYR B CD2 
6055 C CE1 . TYR B 226 ? 0.9870 0.9468 0.6690 -0.2619 0.0986  0.0584  224 TYR B CE1 
6056 C CE2 . TYR B 226 ? 0.9200 0.9573 0.6788 -0.2992 0.1051  -0.0191 224 TYR B CE2 
6057 C CZ  . TYR B 226 ? 0.9559 0.9644 0.6703 -0.3037 0.1116  0.0161  224 TYR B CZ  
6058 O OH  . TYR B 226 ? 0.9759 1.0131 0.6773 -0.3471 0.1311  0.0072  224 TYR B OH  
6059 N N   . PHE B 227 ? 1.0443 0.9229 0.8087 -0.1921 0.0879  -0.0238 225 PHE B N   
6060 C CA  . PHE B 227 ? 1.0705 0.9316 0.8411 -0.2251 0.1028  -0.0669 225 PHE B CA  
6061 C C   . PHE B 227 ? 0.9242 0.8948 0.7457 -0.2406 0.0945  -0.1089 225 PHE B C   
6062 O O   . PHE B 227 ? 0.8802 0.9176 0.7310 -0.2049 0.0740  -0.1081 225 PHE B O   
6063 C CB  . PHE B 227 ? 1.1501 0.9616 0.9137 -0.1893 0.0992  -0.0740 225 PHE B CB  
6064 C CG  . PHE B 227 ? 1.3228 1.0253 1.0321 -0.1620 0.1049  -0.0357 225 PHE B CG  
6065 C CD1 . PHE B 227 ? 1.4033 0.9898 1.0605 -0.1921 0.1288  -0.0369 225 PHE B CD1 
6066 C CD2 . PHE B 227 ? 1.3460 1.0620 1.0542 -0.1056 0.0870  0.0003  225 PHE B CD2 
6067 C CE1 . PHE B 227 ? 1.5240 0.9995 1.1202 -0.1576 0.1330  -0.0001 225 PHE B CE1 
6068 C CE2 . PHE B 227 ? 1.4407 1.0659 1.0971 -0.0707 0.0893  0.0332  225 PHE B CE2 
6069 C CZ  . PHE B 227 ? 1.5380 1.0377 1.1339 -0.0925 0.1114  0.0346  225 PHE B CZ  
6070 N N   . VAL B 228 ? 0.9867 0.9748 0.8157 -0.2931 0.1113  -0.1462 226 VAL B N   
6071 C CA  . VAL B 228 ? 0.9589 1.0579 0.8333 -0.3050 0.1031  -0.1920 226 VAL B CA  
6072 C C   . VAL B 228 ? 1.0081 1.1104 0.8947 -0.3465 0.1181  -0.2458 226 VAL B C   
6073 O O   . VAL B 228 ? 1.0080 1.0368 0.8686 -0.3948 0.1443  -0.2478 226 VAL B O   
6074 C CB  . VAL B 228 ? 0.9058 1.0657 0.7876 -0.3294 0.1059  -0.1879 226 VAL B CB  
6075 C CG1 . VAL B 228 ? 0.8832 1.1569 0.8076 -0.3418 0.0998  -0.2423 226 VAL B CG1 
6076 C CG2 . VAL B 228 ? 0.7551 0.9242 0.6310 -0.2875 0.0866  -0.1449 226 VAL B CG2 
6077 N N   . LEU B 229 ? 0.6539 1.1003 1.5397 -0.2620 -0.3147 -0.1863 227 LEU B N   
6078 C CA  . LEU B 229 ? 0.6005 1.0386 1.4484 -0.2470 -0.2804 -0.1735 227 LEU B CA  
6079 C C   . LEU B 229 ? 0.6593 1.0330 1.3926 -0.2405 -0.3138 -0.1581 227 LEU B C   
6080 O O   . LEU B 229 ? 0.7100 1.0392 1.3739 -0.2625 -0.3125 -0.1572 227 LEU B O   
6081 C CB  . LEU B 229 ? 0.5681 1.0140 1.4191 -0.2696 -0.2078 -0.1760 227 LEU B CB  
6082 C CG  . LEU B 229 ? 0.5816 1.0783 1.5256 -0.2788 -0.1631 -0.1900 227 LEU B CG  
6083 C CD1 . LEU B 229 ? 0.5948 1.0741 1.5040 -0.3021 -0.0937 -0.1873 227 LEU B CD1 
6084 C CD2 . LEU B 229 ? 0.5482 1.0859 1.5597 -0.2474 -0.1621 -0.1935 227 LEU B CD2 
6085 N N   . THR B 230 ? 0.6789 1.0406 1.3861 -0.2108 -0.3423 -0.1460 228 THR B N   
6086 C CA  . THR B 230 ? 0.7159 1.0083 1.3037 -0.2047 -0.3767 -0.1303 228 THR B CA  
6087 C C   . THR B 230 ? 0.7553 1.0117 1.2521 -0.2076 -0.3185 -0.1174 228 THR B C   
6088 O O   . THR B 230 ? 0.6175 0.8992 1.1353 -0.1972 -0.2695 -0.1126 228 THR B O   
6089 C CB  . THR B 230 ? 0.7530 1.0335 1.3230 -0.1721 -0.4127 -0.1176 228 THR B CB  
6090 O OG1 . THR B 230 ? 0.7831 1.0736 1.4001 -0.1623 -0.4589 -0.1237 228 THR B OG1 
6091 C CG2 . THR B 230 ? 0.8748 1.0753 1.3032 -0.1685 -0.4356 -0.0997 228 THR B CG2 
6092 N N   . SER B 231 ? 0.7860 0.9787 1.1757 -0.2194 -0.3217 -0.1119 229 SER B N   
6093 C CA  . SER B 231 ? 0.8471 0.9964 1.1418 -0.2181 -0.2713 -0.1002 229 SER B CA  
6094 C C   . SER B 231 ? 0.8844 0.9798 1.0748 -0.1986 -0.2854 -0.0849 229 SER B C   
6095 O O   . SER B 231 ? 0.9582 1.0315 1.1244 -0.1929 -0.3372 -0.0828 229 SER B O   
6096 C CB  . SER B 231 ? 0.7978 0.9111 1.0498 -0.2445 -0.2598 -0.1080 229 SER B CB  
6097 O OG  . SER B 231 ? 0.9598 1.0223 1.1153 -0.2393 -0.2226 -0.0980 229 SER B OG  
6098 N N   . HIS B 232 ? 0.9195 0.9905 1.0476 -0.1896 -0.2393 -0.0747 230 HIS B N   
6099 C CA  . HIS B 232 ? 1.0104 1.0303 1.0414 -0.1752 -0.2416 -0.0629 230 HIS B CA  
6100 C C   . HIS B 232 ? 1.0208 0.9973 0.9759 -0.1797 -0.2008 -0.0625 230 HIS B C   
6101 O O   . HIS B 232 ? 1.0112 1.0022 0.9922 -0.1853 -0.1653 -0.0654 230 HIS B O   
6102 C CB  . HIS B 232 ? 0.9826 1.0278 1.0352 -0.1510 -0.2298 -0.0512 230 HIS B CB  
6103 C CG  . HIS B 232 ? 1.0403 1.1332 1.1828 -0.1424 -0.2649 -0.0536 230 HIS B CG  
6104 N ND1 . HIS B 232 ? 1.1102 1.1816 1.2365 -0.1362 -0.3219 -0.0505 230 HIS B ND1 
6105 C CD2 . HIS B 232 ? 0.9362 1.0940 1.1866 -0.1387 -0.2509 -0.0603 230 HIS B CD2 
6106 C CE1 . HIS B 232 ? 0.9977 1.1229 1.2279 -0.1261 -0.3452 -0.0557 230 HIS B CE1 
6107 N NE2 . HIS B 232 ? 1.0537 1.2346 1.3632 -0.1279 -0.2994 -0.0632 230 HIS B NE2 
6108 N N   . THR B 233 ? 1.0284 0.9472 0.8883 -0.1776 -0.2061 -0.0600 231 THR B N   
6109 C CA  . THR B 233 ? 0.9632 0.8423 0.7595 -0.1784 -0.1667 -0.0629 231 THR B CA  
6110 C C   . THR B 233 ? 0.8654 0.7676 0.6794 -0.1589 -0.1257 -0.0539 231 THR B C   
6111 O O   . THR B 233 ? 0.8972 0.8226 0.7311 -0.1444 -0.1290 -0.0442 231 THR B O   
6112 C CB  . THR B 233 ? 1.0824 0.8933 0.7744 -0.1838 -0.1774 -0.0663 231 THR B CB  
6113 O OG1 . THR B 233 ? 1.2339 1.0154 0.9009 -0.2040 -0.2175 -0.0758 231 THR B OG1 
6114 C CG2 . THR B 233 ? 1.0885 0.8646 0.7294 -0.1816 -0.1319 -0.0732 231 THR B CG2 
6115 N N   . VAL B 234 ? 0.8678 0.7601 0.6748 -0.1584 -0.0905 -0.0577 232 VAL B N   
6116 C CA  . VAL B 234 ? 0.8340 0.7421 0.6556 -0.1408 -0.0560 -0.0508 232 VAL B CA  
6117 C C   . VAL B 234 ? 0.8003 0.6669 0.5591 -0.1332 -0.0350 -0.0554 232 VAL B C   
6118 O O   . VAL B 234 ? 0.7846 0.6125 0.5049 -0.1412 -0.0270 -0.0671 232 VAL B O   
6119 C CB  . VAL B 234 ? 0.7561 0.6786 0.6172 -0.1445 -0.0352 -0.0514 232 VAL B CB  
6120 C CG1 . VAL B 234 ? 0.7200 0.6494 0.5872 -0.1264 -0.0066 -0.0443 232 VAL B CG1 
6121 C CG2 . VAL B 234 ? 0.7285 0.6936 0.6559 -0.1559 -0.0476 -0.0503 232 VAL B CG2 
6122 N N   . MET B 235 ? 0.7974 0.6721 0.5500 -0.1186 -0.0235 -0.0484 233 MET B N   
6123 C CA  . MET B 235 ? 0.8555 0.6961 0.5587 -0.1135 0.0014  -0.0557 233 MET B CA  
6124 C C   . MET B 235 ? 0.8008 0.6513 0.5343 -0.0998 0.0316  -0.0591 233 MET B C   
6125 O O   . MET B 235 ? 0.7272 0.6108 0.5095 -0.0914 0.0333  -0.0501 233 MET B O   
6126 C CB  . MET B 235 ? 0.8285 0.6673 0.5078 -0.1077 0.0004  -0.0479 233 MET B CB  
6127 C CG  . MET B 235 ? 0.8892 0.6979 0.5175 -0.1209 -0.0333 -0.0451 233 MET B CG  
6128 S SD  . MET B 235 ? 1.1481 0.8873 0.6879 -0.1414 -0.0326 -0.0624 233 MET B SD  
6129 C CE  . MET B 235 ? 1.2461 0.9709 0.7663 -0.1560 -0.0930 -0.0564 233 MET B CE  
6130 N N   . PRO B 236 ? 0.8310 0.6499 0.5363 -0.0975 0.0547  -0.0734 234 PRO B N   
6131 C CA  . PRO B 236 ? 0.7207 0.5475 0.4616 -0.0814 0.0766  -0.0780 234 PRO B CA  
6132 C C   . PRO B 236 ? 0.7577 0.6169 0.5302 -0.0665 0.0860  -0.0688 234 PRO B C   
6133 O O   . PRO B 236 ? 0.7689 0.6343 0.5248 -0.0684 0.0856  -0.0634 234 PRO B O   
6134 C CB  . PRO B 236 ? 0.8521 0.6394 0.5601 -0.0824 0.0995  -0.0996 234 PRO B CB  
6135 C CG  . PRO B 236 ? 0.8566 0.6206 0.5044 -0.0971 0.0989  -0.1021 234 PRO B CG  
6136 C CD  . PRO B 236 ? 0.9713 0.7428 0.6112 -0.1094 0.0623  -0.0882 234 PRO B CD  
6137 N N   . LEU B 237 ? 0.6823 0.5557 0.4958 -0.0523 0.0918  -0.0668 235 LEU B N   
6138 C CA  . LEU B 237 ? 0.6629 0.5647 0.5087 -0.0383 0.0978  -0.0592 235 LEU B CA  
6139 C C   . LEU B 237 ? 0.6607 0.5558 0.5244 -0.0255 0.1187  -0.0747 235 LEU B C   
6140 O O   . LEU B 237 ? 0.6689 0.5401 0.5334 -0.0227 0.1261  -0.0899 235 LEU B O   
6141 C CB  . LEU B 237 ? 0.6038 0.5225 0.4797 -0.0328 0.0861  -0.0460 235 LEU B CB  
6142 C CG  . LEU B 237 ? 0.6033 0.5401 0.4816 -0.0445 0.0716  -0.0332 235 LEU B CG  
6143 C CD1 . LEU B 237 ? 0.5692 0.5119 0.4679 -0.0429 0.0694  -0.0240 235 LEU B CD1 
6144 C CD2 . LEU B 237 ? 0.5431 0.5040 0.4233 -0.0436 0.0679  -0.0261 235 LEU B CD2 
6145 N N   . SER B 238 ? 0.5807 0.4977 0.4651 -0.0176 0.1282  -0.0726 236 SER B N   
6146 C CA  . SER B 238 ? 0.6276 0.5464 0.5432 -0.0066 0.1493  -0.0901 236 SER B CA  
6147 C C   . SER B 238 ? 0.6636 0.6111 0.6248 0.0075  0.1437  -0.0828 236 SER B C   
6148 O O   . SER B 238 ? 0.6445 0.5951 0.6498 0.0224  0.1432  -0.0931 236 SER B O   
6149 C CB  . SER B 238 ? 0.6254 0.5320 0.5100 -0.0188 0.1763  -0.1029 236 SER B CB  
6150 O OG  . SER B 238 ? 0.7971 0.7118 0.6540 -0.0277 0.1716  -0.0872 236 SER B OG  
6151 N N   . ALA B 239 ? 0.6068 0.5727 0.5589 0.0037  0.1365  -0.0661 237 ALA B N   
6152 C CA  . ALA B 239 ? 0.6134 0.6026 0.6008 0.0145  0.1325  -0.0601 237 ALA B CA  
6153 C C   . ALA B 239 ? 0.5589 0.5480 0.5587 0.0232  0.1096  -0.0485 237 ALA B C   
6154 O O   . ALA B 239 ? 0.5430 0.5216 0.5194 0.0162  0.0989  -0.0391 237 ALA B O   
6155 C CB  . ALA B 239 ? 0.6376 0.6399 0.6067 0.0071  0.1345  -0.0480 237 ALA B CB  
6156 N N   . PRO B 240 ? 0.5569 0.5537 0.5907 0.0362  0.1019  -0.0497 238 PRO B N   
6157 C CA  . PRO B 240 ? 0.5174 0.5024 0.5467 0.0416  0.0799  -0.0373 238 PRO B CA  
6158 C C   . PRO B 240 ? 0.4805 0.4760 0.4860 0.0327  0.0779  -0.0205 238 PRO B C   
6159 O O   . PRO B 240 ? 0.4868 0.5026 0.4906 0.0279  0.0875  -0.0176 238 PRO B O   
6160 C CB  . PRO B 240 ? 0.4792 0.4692 0.5493 0.0568  0.0698  -0.0445 238 PRO B CB  
6161 C CG  . PRO B 240 ? 0.6162 0.6344 0.7115 0.0546  0.0912  -0.0545 238 PRO B CG  
6162 C CD  . PRO B 240 ? 0.6275 0.6404 0.7044 0.0446  0.1125  -0.0637 238 PRO B CD  
6163 N N   . THR B 241 ? 0.4389 0.4159 0.4243 0.0297  0.0663  -0.0104 239 THR B N   
6164 C CA  . THR B 241 ? 0.4923 0.4797 0.4628 0.0212  0.0690  0.0014  239 THR B CA  
6165 C C   . THR B 241 ? 0.5200 0.5215 0.5028 0.0287  0.0680  0.0040  239 THR B C   
6166 O O   . THR B 241 ? 0.4935 0.5127 0.4749 0.0244  0.0747  0.0097  239 THR B O   
6167 C CB  . THR B 241 ? 0.4723 0.4306 0.4143 0.0125  0.0637  0.0091  239 THR B CB  
6168 O OG1 . THR B 241 ? 0.5340 0.4595 0.4650 0.0216  0.0476  0.0103  239 THR B OG1 
6169 C CG2 . THR B 241 ? 0.5093 0.4531 0.4399 0.0025  0.0652  0.0062  239 THR B CG2 
6170 N N   . LEU B 242 ? 0.4594 0.4524 0.4586 0.0403  0.0573  -0.0015 240 LEU B N   
6171 C CA  . LEU B 242 ? 0.4606 0.4647 0.4750 0.0468  0.0534  -0.0014 240 LEU B CA  
6172 C C   . LEU B 242 ? 0.4655 0.4820 0.5230 0.0567  0.0525  -0.0156 240 LEU B C   
6173 O O   . LEU B 242 ? 0.4598 0.4637 0.5342 0.0639  0.0442  -0.0248 240 LEU B O   
6174 C CB  . LEU B 242 ? 0.4576 0.4316 0.4466 0.0487  0.0357  0.0057  240 LEU B CB  
6175 C CG  . LEU B 242 ? 0.5182 0.4846 0.4702 0.0368  0.0456  0.0161  240 LEU B CG  
6176 C CD1 . LEU B 242 ? 0.5210 0.4415 0.4301 0.0344  0.0306  0.0222  240 LEU B CD1 
6177 C CD2 . LEU B 242 ? 0.5241 0.5210 0.4912 0.0366  0.0582  0.0166  240 LEU B CD2 
6178 N N   . VAL B 243 ? 0.5342 0.5742 0.6127 0.0563  0.0628  -0.0192 241 VAL B N   
6179 C CA  . VAL B 243 ? 0.5139 0.5696 0.6410 0.0620  0.0682  -0.0356 241 VAL B CA  
6180 C C   . VAL B 243 ? 0.4213 0.4678 0.5763 0.0743  0.0407  -0.0400 241 VAL B C   
6181 O O   . VAL B 243 ? 0.4644 0.4885 0.5864 0.0753  0.0211  -0.0279 241 VAL B O   
6182 C CB  . VAL B 243 ? 0.6000 0.6768 0.7345 0.0537  0.0893  -0.0372 241 VAL B CB  
6183 C CG1 . VAL B 243 ? 0.7069 0.7821 0.8065 0.0422  0.1087  -0.0325 241 VAL B CG1 
6184 C CG2 . VAL B 243 ? 0.4855 0.5628 0.6073 0.0535  0.0797  -0.0262 241 VAL B CG2 
6185 N N   . PRO B 244 ? 0.4209 0.4805 0.6355 0.0831  0.0374  -0.0585 242 PRO B N   
6186 C CA  . PRO B 244 ? 0.3962 0.4471 0.6435 0.0957  0.0032  -0.0635 242 PRO B CA  
6187 C C   . PRO B 244 ? 0.4736 0.5319 0.7146 0.0908  -0.0017 -0.0572 242 PRO B C   
6188 O O   . PRO B 244 ? 0.4471 0.5324 0.7074 0.0821  0.0230  -0.0621 242 PRO B O   
6189 C CB  . PRO B 244 ? 0.4279 0.5034 0.7586 0.1050  0.0079  -0.0895 242 PRO B CB  
6190 C CG  . PRO B 244 ? 0.3948 0.4797 0.7193 0.0968  0.0456  -0.0968 242 PRO B CG  
6191 C CD  . PRO B 244 ? 0.4408 0.5232 0.6985 0.0805  0.0656  -0.0779 242 PRO B CD  
6192 N N   . GLN B 245 ? 0.4380 0.4643 0.6430 0.0944  -0.0330 -0.0461 243 GLN B N   
6193 C CA  . GLN B 245 ? 0.4332 0.4581 0.6230 0.0895  -0.0395 -0.0407 243 GLN B CA  
6194 C C   . GLN B 245 ? 0.4354 0.4855 0.6980 0.0943  -0.0509 -0.0582 243 GLN B C   
6195 O O   . GLN B 245 ? 0.4278 0.4828 0.7483 0.1062  -0.0726 -0.0732 243 GLN B O   
6196 C CB  . GLN B 245 ? 0.3938 0.3686 0.5184 0.0900  -0.0692 -0.0270 243 GLN B CB  
6197 C CG  . GLN B 245 ? 0.4689 0.4348 0.5672 0.0837  -0.0740 -0.0225 243 GLN B CG  
6198 C CD  . GLN B 245 ? 0.4251 0.4129 0.5040 0.0728  -0.0362 -0.0159 243 GLN B CD  
6199 O OE1 . GLN B 245 ? 0.4297 0.4545 0.5492 0.0702  -0.0132 -0.0222 243 GLN B OE1 
6200 N NE2 . GLN B 245 ? 0.4578 0.4189 0.4739 0.0657  -0.0294 -0.0042 243 GLN B NE2 
6201 N N   . GLU B 246 ? 0.3718 0.4384 0.6370 0.0848  -0.0361 -0.0579 244 GLU B N   
6202 C CA  . GLU B 246 ? 0.3970 0.4862 0.7278 0.0848  -0.0455 -0.0740 244 GLU B CA  
6203 C C   . GLU B 246 ? 0.3659 0.4377 0.6569 0.0779  -0.0556 -0.0648 244 GLU B C   
6204 O O   . GLU B 246 ? 0.4302 0.4982 0.6728 0.0687  -0.0305 -0.0525 244 GLU B O   
6205 C CB  . GLU B 246 ? 0.3799 0.5106 0.7655 0.0752  -0.0043 -0.0886 244 GLU B CB  
6206 C CG  . GLU B 246 ? 0.4365 0.5824 0.8595 0.0800  0.0125  -0.1015 244 GLU B CG  
6207 C CD  . GLU B 246 ? 0.5559 0.7320 1.0148 0.0655  0.0598  -0.1160 244 GLU B CD  
6208 O OE1 . GLU B 246 ? 0.5428 0.7257 0.9954 0.0514  0.0777  -0.1140 244 GLU B OE1 
6209 O OE2 . GLU B 246 ? 0.6104 0.7942 1.0912 0.0655  0.0792  -0.1282 244 GLU B OE2 
6210 N N   . HIS B 247 ? 0.4345 0.4921 0.7447 0.0832  -0.0952 -0.0715 245 HIS B N   
6211 C CA  . HIS B 247 ? 0.4178 0.4571 0.6949 0.0755  -0.1055 -0.0669 245 HIS B CA  
6212 C C   . HIS B 247 ? 0.4231 0.4985 0.7786 0.0691  -0.1012 -0.0850 245 HIS B C   
6213 O O   . HIS B 247 ? 0.3741 0.4771 0.8142 0.0748  -0.1143 -0.1039 245 HIS B O   
6214 C CB  . HIS B 247 ? 0.4797 0.4656 0.7054 0.0817  -0.1544 -0.0608 245 HIS B CB  
6215 C CG  . HIS B 247 ? 0.6332 0.5763 0.7703 0.0818  -0.1513 -0.0428 245 HIS B CG  
6216 N ND1 . HIS B 247 ? 0.5843 0.4978 0.6414 0.0719  -0.1343 -0.0300 245 HIS B ND1 
6217 C CD2 . HIS B 247 ? 0.5901 0.5146 0.7095 0.0890  -0.1601 -0.0374 245 HIS B CD2 
6218 C CE1 . HIS B 247 ? 0.6694 0.5508 0.6663 0.0712  -0.1304 -0.0183 245 HIS B CE1 
6219 N NE2 . HIS B 247 ? 0.7105 0.5955 0.7398 0.0809  -0.1470 -0.0212 245 HIS B NE2 
6220 N N   . TYR B 248 ? 0.4255 0.5001 0.7574 0.0566  -0.0820 -0.0807 246 TYR B N   
6221 C CA  . TYR B 248 ? 0.4145 0.5187 0.8114 0.0454  -0.0709 -0.0963 246 TYR B CA  
6222 C C   . TYR B 248 ? 0.4298 0.5080 0.8064 0.0407  -0.1003 -0.0971 246 TYR B C   
6223 O O   . TYR B 248 ? 0.4982 0.5340 0.7936 0.0425  -0.1129 -0.0830 246 TYR B O   
6224 C CB  . TYR B 248 ? 0.4004 0.5207 0.7855 0.0315  -0.0189 -0.0913 246 TYR B CB  
6225 C CG  . TYR B 248 ? 0.3868 0.5214 0.7684 0.0335  0.0111  -0.0878 246 TYR B CG  
6226 C CD1 . TYR B 248 ? 0.3568 0.5172 0.8031 0.0394  0.0113  -0.1039 246 TYR B CD1 
6227 C CD2 . TYR B 248 ? 0.4435 0.5638 0.7589 0.0304  0.0364  -0.0700 246 TYR B CD2 
6228 C CE1 . TYR B 248 ? 0.3991 0.5671 0.8357 0.0400  0.0391  -0.1022 246 TYR B CE1 
6229 C CE2 . TYR B 248 ? 0.4383 0.5670 0.7455 0.0309  0.0594  -0.0673 246 TYR B CE2 
6230 C CZ  . TYR B 248 ? 0.4620 0.6125 0.8251 0.0348  0.0619  -0.0832 246 TYR B CZ  
6231 O OH  . TYR B 248 ? 0.4617 0.6155 0.8110 0.0340  0.0854  -0.0819 246 TYR B OH  
6232 N N   . VAL B 249 ? 0.4778 0.5813 0.9309 0.0327  -0.1082 -0.1161 247 VAL B N   
6233 C CA  . VAL B 249 ? 0.4418 0.5216 0.8836 0.0261  -0.1384 -0.1201 247 VAL B CA  
6234 C C   . VAL B 249 ? 0.5594 0.6326 0.9668 0.0099  -0.1026 -0.1138 247 VAL B C   
6235 O O   . VAL B 249 ? 0.6587 0.7022 1.0337 0.0040  -0.1216 -0.1137 247 VAL B O   
6236 C CB  . VAL B 249 ? 0.4807 0.5897 1.0285 0.0244  -0.1713 -0.1457 247 VAL B CB  
6237 C CG1 . VAL B 249 ? 0.4440 0.5430 1.0155 0.0440  -0.2244 -0.1509 247 VAL B CG1 
6238 C CG2 . VAL B 249 ? 0.4281 0.5945 1.0725 0.0121  -0.1274 -0.1640 247 VAL B CG2 
6239 N N   . ARG B 250 ? 0.4942 0.5877 0.9027 0.0025  -0.0538 -0.1086 248 ARG B N   
6240 C CA  . ARG B 250 ? 0.5171 0.5983 0.8908 -0.0116 -0.0213 -0.1010 248 ARG B CA  
6241 C C   . ARG B 250 ? 0.4140 0.4906 0.7360 -0.0082 0.0131  -0.0836 248 ARG B C   
6242 O O   . ARG B 250 ? 0.4193 0.5123 0.7503 -0.0002 0.0198  -0.0819 248 ARG B O   
6243 C CB  . ARG B 250 ? 0.4926 0.6019 0.9382 -0.0320 0.0023  -0.1178 248 ARG B CB  
6244 C CG  . ARG B 250 ? 0.6524 0.7617 1.1438 -0.0419 -0.0254 -0.1342 248 ARG B CG  
6245 C CD  . ARG B 250 ? 0.6922 0.8390 1.2721 -0.0638 0.0043  -0.1548 248 ARG B CD  
6246 N NE  . ARG B 250 ? 0.7168 0.9046 1.3603 -0.0604 0.0234  -0.1667 248 ARG B NE  
6247 C CZ  . ARG B 250 ? 0.5780 0.7996 1.3083 -0.0503 -0.0051 -0.1869 248 ARG B CZ  
6248 N NH1 . ARG B 250 ? 0.5018 0.7240 1.2750 -0.0461 -0.0555 -0.1993 248 ARG B NH1 
6249 N NH2 . ARG B 250 ? 0.5166 0.7699 1.2944 -0.0447 0.0159  -0.1967 248 ARG B NH2 
6250 N N   . ILE B 251 ? 0.4530 0.5051 0.7229 -0.0139 0.0321  -0.0715 249 ILE B N   
6251 C CA  . ILE B 251 ? 0.4242 0.4715 0.6530 -0.0117 0.0604  -0.0564 249 ILE B CA  
6252 C C   . ILE B 251 ? 0.4330 0.5040 0.7012 -0.0249 0.0902  -0.0633 249 ILE B C   
6253 O O   . ILE B 251 ? 0.4283 0.5032 0.7287 -0.0430 0.1061  -0.0735 249 ILE B O   
6254 C CB  . ILE B 251 ? 0.4925 0.5067 0.6686 -0.0140 0.0701  -0.0446 249 ILE B CB  
6255 C CG1 . ILE B 251 ? 0.5411 0.5298 0.6806 -0.0036 0.0463  -0.0430 249 ILE B CG1 
6256 C CG2 . ILE B 251 ? 0.4430 0.4507 0.5805 -0.0090 0.0898  -0.0292 249 ILE B CG2 
6257 C CD1 . ILE B 251 ? 0.5550 0.5117 0.6506 -0.0027 0.0560  -0.0350 249 ILE B CD1 
6258 N N   . THR B 252 ? 0.4845 0.5677 0.7469 -0.0185 0.1010  -0.0593 250 THR B N   
6259 C CA  . THR B 252 ? 0.4744 0.5765 0.7696 -0.0313 0.1314  -0.0690 250 THR B CA  
6260 C C   . THR B 252 ? 0.5428 0.6234 0.7773 -0.0356 0.1557  -0.0534 250 THR B C   
6261 O O   . THR B 252 ? 0.5811 0.6537 0.7754 -0.0215 0.1450  -0.0398 250 THR B O   
6262 C CB  . THR B 252 ? 0.5313 0.6642 0.8798 -0.0209 0.1214  -0.0828 250 THR B CB  
6263 O OG1 . THR B 252 ? 0.4999 0.6440 0.8958 -0.0130 0.0862  -0.0945 250 THR B OG1 
6264 C CG2 . THR B 252 ? 0.5389 0.6942 0.9367 -0.0364 0.1573  -0.1007 250 THR B CG2 
6265 N N   . GLY B 253 ? 0.4718 0.5389 0.6977 -0.0571 0.1873  -0.0558 251 GLY B N   
6266 C CA  . GLY B 253 ? 0.5947 0.6320 0.7572 -0.0646 0.2075  -0.0420 251 GLY B CA  
6267 C C   . GLY B 253 ? 0.6680 0.6660 0.7662 -0.0599 0.1952  -0.0208 251 GLY B C   
6268 O O   . GLY B 253 ? 0.8462 0.8131 0.8881 -0.0643 0.2033  -0.0077 251 GLY B O   
6269 N N   . LEU B 254 ? 0.6043 0.5990 0.7090 -0.0508 0.1742  -0.0184 252 LEU B N   
6270 C CA  . LEU B 254 ? 0.6085 0.5699 0.6644 -0.0415 0.1607  -0.0019 252 LEU B CA  
6271 C C   . LEU B 254 ? 0.6901 0.6306 0.7500 -0.0512 0.1600  -0.0052 252 LEU B C   
6272 O O   . LEU B 254 ? 0.6654 0.6263 0.7714 -0.0566 0.1565  -0.0199 252 LEU B O   
6273 C CB  . LEU B 254 ? 0.5053 0.4807 0.5595 -0.0171 0.1364  0.0029  252 LEU B CB  
6274 C CG  . LEU B 254 ? 0.5344 0.5267 0.5816 -0.0072 0.1344  0.0074  252 LEU B CG  
6275 C CD1 . LEU B 254 ? 0.4249 0.4290 0.4733 0.0117  0.1156  0.0093  252 LEU B CD1 
6276 C CD2 . LEU B 254 ? 0.5002 0.4661 0.5026 -0.0105 0.1405  0.0207  252 LEU B CD2 
6277 N N   . TYR B 255 ? 0.6759 0.5727 0.6881 -0.0531 0.1599  0.0083  253 TYR B N   
6278 C CA  . TYR B 255 ? 0.5576 0.4247 0.5649 -0.0636 0.1602  0.0066  253 TYR B CA  
6279 C C   . TYR B 255 ? 0.6174 0.4639 0.6022 -0.0421 0.1380  0.0147  253 TYR B C   
6280 O O   . TYR B 255 ? 0.5951 0.4085 0.5395 -0.0336 0.1322  0.0290  253 TYR B O   
6281 C CB  . TYR B 255 ? 0.7433 0.5655 0.7111 -0.0887 0.1831  0.0134  253 TYR B CB  
6282 C CG  . TYR B 255 ? 0.8076 0.6525 0.8018 -0.1115 0.2128  0.0008  253 TYR B CG  
6283 C CD1 . TYR B 255 ? 0.7859 0.6571 0.8400 -0.1298 0.2276  -0.0194 253 TYR B CD1 
6284 C CD2 . TYR B 255 ? 0.8668 0.7101 0.8336 -0.1136 0.2253  0.0059  253 TYR B CD2 
6285 C CE1 . TYR B 255 ? 0.8346 0.7321 0.9270 -0.1494 0.2581  -0.0357 253 TYR B CE1 
6286 C CE2 . TYR B 255 ? 0.8738 0.7374 0.8673 -0.1341 0.2570  -0.0094 253 TYR B CE2 
6287 C CZ  . TYR B 255 ? 0.8900 0.7828 0.9505 -0.1513 0.2750  -0.0310 253 TYR B CZ  
6288 O OH  . TYR B 255 ? 1.0813 0.9984 1.1809 -0.1709 0.3100  -0.0504 253 TYR B OH  
6289 N N   . PRO B 256 ? 0.5892 0.4507 0.5985 -0.0330 0.1243  0.0045  254 PRO B N   
6290 C CA  . PRO B 256 ? 0.5986 0.4410 0.5882 -0.0134 0.1096  0.0078  254 PRO B CA  
6291 C C   . PRO B 256 ? 0.6412 0.4331 0.6022 -0.0176 0.1100  0.0136  254 PRO B C   
6292 O O   . PRO B 256 ? 0.6999 0.4711 0.6603 -0.0387 0.1189  0.0106  254 PRO B O   
6293 C CB  . PRO B 256 ? 0.6131 0.4736 0.6256 -0.0105 0.0981  -0.0068 254 PRO B CB  
6294 C CG  . PRO B 256 ? 0.6175 0.4902 0.6634 -0.0324 0.1029  -0.0173 254 PRO B CG  
6295 C CD  . PRO B 256 ? 0.5926 0.4846 0.6478 -0.0408 0.1201  -0.0124 254 PRO B CD  
6296 N N   . THR B 257 ? 0.6376 0.4090 0.5790 0.0028  0.1003  0.0208  255 THR B N   
6297 C CA  . THR B 257 ? 0.6704 0.3890 0.5856 0.0044  0.0957  0.0264  255 THR B CA  
6298 C C   . THR B 257 ? 0.6822 0.3870 0.6044 0.0021  0.0936  0.0125  255 THR B C   
6299 O O   . THR B 257 ? 0.6877 0.4212 0.6295 0.0033  0.0916  -0.0005 255 THR B O   
6300 C CB  . THR B 257 ? 0.7158 0.4213 0.6228 0.0307  0.0826  0.0342  255 THR B CB  
6301 O OG1 . THR B 257 ? 0.7625 0.4108 0.6456 0.0343  0.0743  0.0395  255 THR B OG1 
6302 C CG2 . THR B 257 ? 0.6370 0.3746 0.5708 0.0507  0.0810  0.0213  255 THR B CG2 
6303 N N   . LEU B 258 ? 0.7970 0.4499 0.6962 -0.0019 0.0915  0.0156  256 LEU B N   
6304 C CA  . LEU B 258 ? 0.9570 0.5878 0.8568 -0.0055 0.0889  0.0020  256 LEU B CA  
6305 C C   . LEU B 258 ? 0.9127 0.5205 0.8051 0.0212  0.0814  -0.0026 256 LEU B C   
6306 O O   . LEU B 258 ? 0.8746 0.4815 0.7696 0.0256  0.0810  -0.0183 256 LEU B O   
6307 C CB  . LEU B 258 ? 0.9432 0.5274 0.8242 -0.0307 0.0945  0.0054  256 LEU B CB  
6308 C CG  . LEU B 258 ? 1.0273 0.6357 0.9283 -0.0620 0.1086  0.0019  256 LEU B CG  
6309 C CD1 . LEU B 258 ? 0.9761 0.5308 0.8494 -0.0892 0.1209  0.0090  256 LEU B CD1 
6310 C CD2 . LEU B 258 ? 0.8713 0.5149 0.8110 -0.0699 0.1032  -0.0179 256 LEU B CD2 
6311 N N   . ASN B 259 ? 0.9006 0.4885 0.7847 0.0388  0.0748  0.0093  257 ASN B N   
6312 C CA  . ASN B 259 ? 0.8583 0.4279 0.7500 0.0669  0.0682  0.0029  257 ASN B CA  
6313 C C   . ASN B 259 ? 0.8396 0.4549 0.7592 0.0877  0.0672  0.0034  257 ASN B C   
6314 O O   . ASN B 259 ? 0.8786 0.5067 0.7972 0.0873  0.0602  0.0183  257 ASN B O   
6315 C CB  . ASN B 259 ? 0.8002 0.3060 0.6692 0.0728  0.0548  0.0145  257 ASN B CB  
6316 C CG  . ASN B 259 ? 1.0187 0.5083 0.9095 0.1057  0.0457  0.0059  257 ASN B CG  
6317 O OD1 . ASN B 259 ? 1.0977 0.5787 0.9978 0.1136  0.0542  -0.0130 257 ASN B OD1 
6318 N ND2 . ASN B 259 ? 1.1490 0.6319 1.0496 0.1249  0.0274  0.0179  257 ASN B ND2 
6319 N N   . ILE B 260 ? 0.7298 0.3660 0.6707 0.1032  0.0759  -0.0138 258 ILE B N   
6320 C CA  . ILE B 260 ? 0.7011 0.3811 0.6737 0.1203  0.0794  -0.0167 258 ILE B CA  
6321 C C   . ILE B 260 ? 0.6615 0.3319 0.6619 0.1447  0.0860  -0.0344 258 ILE B C   
6322 O O   . ILE B 260 ? 0.7250 0.3632 0.7129 0.1451  0.0943  -0.0489 258 ILE B O   
6323 C CB  . ILE B 260 ? 0.6964 0.4210 0.6680 0.1079  0.0919  -0.0221 258 ILE B CB  
6324 C CG1 . ILE B 260 ? 0.7783 0.5458 0.7803 0.1214  0.0970  -0.0236 258 ILE B CG1 
6325 C CG2 . ILE B 260 ? 0.7223 0.4332 0.6748 0.1007  0.1035  -0.0402 258 ILE B CG2 
6326 C CD1 . ILE B 260 ? 0.6276 0.4082 0.6423 0.1259  0.0812  -0.0059 258 ILE B CD1 
6327 N N   . SER B 261 ? 0.6448 0.3435 0.6871 0.1646  0.0829  -0.0357 259 SER B N   
6328 C CA  . SER B 261 ? 0.6622 0.3627 0.7483 0.1885  0.0938  -0.0571 259 SER B CA  
6329 C C   . SER B 261 ? 0.6487 0.3735 0.7337 0.1819  0.1268  -0.0789 259 SER B C   
6330 O O   . SER B 261 ? 0.6141 0.3691 0.6818 0.1660  0.1351  -0.0747 259 SER B O   
6331 C CB  . SER B 261 ? 0.6496 0.3773 0.7921 0.2105  0.0776  -0.0535 259 SER B CB  
6332 O OG  . SER B 261 ? 0.6893 0.4383 0.8909 0.2307  0.0963  -0.0794 259 SER B OG  
6333 N N   . ASP B 262 ? 0.8266 0.2562 0.7564 0.0049  0.0696  -0.1386 260 ASP B N   
6334 C CA  . ASP B 262 ? 0.8599 0.3121 0.7775 0.0001  0.0840  -0.1627 260 ASP B CA  
6335 C C   . ASP B 262 ? 0.8520 0.3714 0.8143 0.0256  0.1008  -0.1662 260 ASP B C   
6336 O O   . ASP B 262 ? 0.7941 0.3391 0.7469 0.0183  0.1150  -0.1833 260 ASP B O   
6337 C CB  . ASP B 262 ? 0.9251 0.3240 0.8042 0.0129  0.0915  -0.1873 260 ASP B CB  
6338 C CG  . ASP B 262 ? 1.0142 0.4000 0.9152 0.0640  0.0992  -0.1924 260 ASP B CG  
6339 O OD1 . ASP B 262 ? 1.1115 0.5276 1.0544 0.0884  0.0946  -0.1745 260 ASP B OD1 
6340 O OD2 . ASP B 262 ? 1.1615 0.5088 1.0385 0.0804  0.1082  -0.2147 260 ASP B OD2 
6341 N N   . GLU B 263 ? 0.8478 0.3986 0.8567 0.0532  0.0975  -0.1492 261 GLU B N   
6342 C CA  . GLU B 263 ? 0.8155 0.4490 0.8738 0.0716  0.1044  -0.1462 261 GLU B CA  
6343 C C   . GLU B 263 ? 0.6908 0.3837 0.7589 0.0410  0.0946  -0.1313 261 GLU B C   
6344 O O   . GLU B 263 ? 0.6900 0.4441 0.7876 0.0467  0.1012  -0.1311 261 GLU B O   
6345 C CB  . GLU B 263 ? 0.7413 0.3925 0.8427 0.1068  0.0953  -0.1300 261 GLU B CB  
6346 C CG  . GLU B 263 ? 0.9827 0.5954 1.0810 0.1461  0.0974  -0.1386 261 GLU B CG  
6347 C CD  . GLU B 263 ? 1.0509 0.7026 1.1949 0.1809  0.0838  -0.1214 261 GLU B CD  
6348 O OE1 . GLU B 263 ? 1.0135 0.7438 1.2067 0.1898  0.0895  -0.1225 261 GLU B OE1 
6349 O OE2 . GLU B 263 ? 1.0706 0.6730 1.1969 0.1961  0.0655  -0.1058 261 GLU B OE2 
6350 N N   . PHE B 264 ? 0.6776 0.3535 0.7237 0.0090  0.0794  -0.1189 262 PHE B N   
6351 C CA  . PHE B 264 ? 0.6633 0.3929 0.7226 -0.0141 0.0687  -0.1040 262 PHE B CA  
6352 C C   . PHE B 264 ? 0.6525 0.3681 0.6789 -0.0503 0.0608  -0.1088 262 PHE B C   
6353 O O   . PHE B 264 ? 0.6167 0.3743 0.6546 -0.0679 0.0497  -0.0966 262 PHE B O   
6354 C CB  . PHE B 264 ? 0.6556 0.3996 0.7368 -0.0133 0.0557  -0.0789 262 PHE B CB  
6355 C CG  . PHE B 264 ? 0.6453 0.4065 0.7558 0.0195  0.0562  -0.0715 262 PHE B CG  
6356 C CD1 . PHE B 264 ? 0.5995 0.4203 0.7408 0.0290  0.0571  -0.0687 262 PHE B CD1 
6357 C CD2 . PHE B 264 ? 0.7026 0.4167 0.8075 0.0397  0.0527  -0.0665 262 PHE B CD2 
6358 C CE1 . PHE B 264 ? 0.5518 0.3929 0.7220 0.0559  0.0530  -0.0622 262 PHE B CE1 
6359 C CE2 . PHE B 264 ? 0.6734 0.4063 0.8062 0.0710  0.0473  -0.0583 262 PHE B CE2 
6360 C CZ  . PHE B 264 ? 0.6680 0.4686 0.8358 0.0781  0.0466  -0.0568 262 PHE B CZ  
6361 N N   . SER B 265 ? 0.6979 0.3545 0.6829 -0.0604 0.0647  -0.1274 263 SER B N   
6362 C CA  . SER B 265 ? 0.7283 0.3702 0.6787 -0.0978 0.0523  -0.1335 263 SER B CA  
6363 C C   . SER B 265 ? 0.6892 0.3762 0.6338 -0.1070 0.0505  -0.1362 263 SER B C   
6364 O O   . SER B 265 ? 0.6335 0.3358 0.5679 -0.1353 0.0315  -0.1304 263 SER B O   
6365 C CB  . SER B 265 ? 0.7210 0.2821 0.6184 -0.1055 0.0583  -0.1574 263 SER B CB  
6366 O OG  . SER B 265 ? 0.8679 0.4139 0.7458 -0.0816 0.0811  -0.1808 263 SER B OG  
6367 N N   . SER B 266 ? 0.6192 0.3275 0.5698 -0.0846 0.0691  -0.1443 264 SER B N   
6368 C CA  . SER B 266 ? 0.7056 0.4459 0.6406 -0.0958 0.0691  -0.1452 264 SER B CA  
6369 C C   . SER B 266 ? 0.6297 0.4228 0.5967 -0.1032 0.0499  -0.1207 264 SER B C   
6370 O O   . SER B 266 ? 0.6213 0.4293 0.5678 -0.1187 0.0393  -0.1170 264 SER B O   
6371 C CB  . SER B 266 ? 0.6409 0.3973 0.5811 -0.0736 0.0969  -0.1574 264 SER B CB  
6372 O OG  . SER B 266 ? 0.6737 0.4669 0.6701 -0.0477 0.1020  -0.1458 264 SER B OG  
6373 N N   . ASN B 267 ? 0.5234 0.3403 0.5351 -0.0909 0.0453  -0.1041 265 ASN B N   
6374 C CA  . ASN B 267 ? 0.5546 0.4184 0.5965 -0.0918 0.0324  -0.0839 265 ASN B CA  
6375 C C   . ASN B 267 ? 0.5481 0.4213 0.6042 -0.1088 0.0139  -0.0713 265 ASN B C   
6376 O O   . ASN B 267 ? 0.5367 0.4484 0.6225 -0.1050 0.0064  -0.0557 265 ASN B O   
6377 C CB  . ASN B 267 ? 0.5273 0.4159 0.6058 -0.0676 0.0412  -0.0749 265 ASN B CB  
6378 C CG  . ASN B 267 ? 0.5210 0.4191 0.6002 -0.0535 0.0584  -0.0852 265 ASN B CG  
6379 O OD1 . ASN B 267 ? 0.5147 0.4185 0.5719 -0.0633 0.0627  -0.0905 265 ASN B OD1 
6380 N ND2 . ASN B 267 ? 0.4938 0.3965 0.5994 -0.0315 0.0676  -0.0865 265 ASN B ND2 
6381 N N   . VAL B 268 ? 0.4954 0.3347 0.5318 -0.1284 0.0079  -0.0787 266 VAL B N   
6382 C CA  . VAL B 268 ? 0.5977 0.4523 0.6562 -0.1482 -0.0061 -0.0663 266 VAL B CA  
6383 C C   . VAL B 268 ? 0.5535 0.4567 0.6283 -0.1607 -0.0264 -0.0570 266 VAL B C   
6384 O O   . VAL B 268 ? 0.5099 0.4563 0.6256 -0.1612 -0.0318 -0.0419 266 VAL B O   
6385 C CB  . VAL B 268 ? 0.5943 0.3955 0.6239 -0.1720 -0.0091 -0.0773 266 VAL B CB  
6386 C CG1 . VAL B 268 ? 0.5233 0.3505 0.5775 -0.2026 -0.0254 -0.0653 266 VAL B CG1 
6387 C CG2 . VAL B 268 ? 0.6536 0.4073 0.6762 -0.1540 0.0081  -0.0801 266 VAL B CG2 
6388 N N   . ALA B 269 ? 0.5571 0.4532 0.5987 -0.1696 -0.0377 -0.0654 267 ALA B N   
6389 C CA  . ALA B 269 ? 0.6034 0.5428 0.6592 -0.1761 -0.0615 -0.0542 267 ALA B CA  
6390 C C   . ALA B 269 ? 0.5313 0.5083 0.6195 -0.1493 -0.0562 -0.0397 267 ALA B C   
6391 O O   . ALA B 269 ? 0.4712 0.4931 0.5999 -0.1454 -0.0682 -0.0262 267 ALA B O   
6392 C CB  . ALA B 269 ? 0.5757 0.4898 0.5760 -0.1895 -0.0754 -0.0643 267 ALA B CB  
6393 N N   . ASN B 270 ? 0.4915 0.4513 0.5639 -0.1308 -0.0377 -0.0437 268 ASN B N   
6394 C CA  . ASN B 270 ? 0.4940 0.4792 0.5891 -0.1092 -0.0332 -0.0321 268 ASN B CA  
6395 C C   . ASN B 270 ? 0.4694 0.4792 0.6081 -0.0981 -0.0257 -0.0230 268 ASN B C   
6396 O O   . ASN B 270 ? 0.4361 0.4731 0.5981 -0.0841 -0.0281 -0.0126 268 ASN B O   
6397 C CB  . ASN B 270 ? 0.4417 0.4066 0.5137 -0.0985 -0.0150 -0.0392 268 ASN B CB  
6398 C CG  . ASN B 270 ? 0.4618 0.4089 0.4881 -0.1087 -0.0203 -0.0429 268 ASN B CG  
6399 O OD1 . ASN B 270 ? 0.6118 0.5626 0.6238 -0.1182 -0.0429 -0.0360 268 ASN B OD1 
6400 N ND2 . ASN B 270 ? 0.5239 0.4537 0.5270 -0.1070 0.0002  -0.0532 268 ASN B ND2 
6401 N N   . TYR B 271 ? 0.4395 0.4332 0.5828 -0.1037 -0.0154 -0.0268 269 TYR B N   
6402 C CA  . TYR B 271 ? 0.4006 0.4115 0.5741 -0.0964 -0.0067 -0.0167 269 TYR B CA  
6403 C C   . TYR B 271 ? 0.4737 0.5251 0.6801 -0.1085 -0.0164 -0.0074 269 TYR B C   
6404 O O   . TYR B 271 ? 0.3208 0.4009 0.5549 -0.0985 -0.0082 0.0019  269 TYR B O   
6405 C CB  . TYR B 271 ? 0.4539 0.4281 0.6163 -0.1004 0.0046  -0.0203 269 TYR B CB  
6406 C CG  . TYR B 271 ? 0.5091 0.4556 0.6555 -0.0813 0.0157  -0.0274 269 TYR B CG  
6407 C CD1 . TYR B 271 ? 0.4212 0.3852 0.5728 -0.0634 0.0190  -0.0265 269 TYR B CD1 
6408 C CD2 . TYR B 271 ? 0.5622 0.4653 0.6912 -0.0808 0.0221  -0.0351 269 TYR B CD2 
6409 C CE1 . TYR B 271 ? 0.4236 0.3748 0.5714 -0.0479 0.0278  -0.0328 269 TYR B CE1 
6410 C CE2 . TYR B 271 ? 0.5210 0.4085 0.6463 -0.0589 0.0312  -0.0416 269 TYR B CE2 
6411 C CZ  . TYR B 271 ? 0.4786 0.3964 0.6174 -0.0435 0.0338  -0.0403 269 TYR B CZ  
6412 O OH  . TYR B 271 ? 0.5430 0.4577 0.6884 -0.0238 0.0416  -0.0468 269 TYR B OH  
6413 N N   . GLN B 272 ? 0.4047 0.4615 0.6092 -0.1307 -0.0333 -0.0109 270 GLN B N   
6414 C CA  . GLN B 272 ? 0.4604 0.5698 0.7075 -0.1427 -0.0459 -0.0023 270 GLN B CA  
6415 C C   . GLN B 272 ? 0.4127 0.5607 0.6811 -0.1204 -0.0572 0.0049  270 GLN B C   
6416 O O   . GLN B 272 ? 0.3390 0.5371 0.6539 -0.1112 -0.0556 0.0136  270 GLN B O   
6417 C CB  . GLN B 272 ? 0.4767 0.5801 0.7140 -0.1761 -0.0659 -0.0088 270 GLN B CB  
6418 C CG  . GLN B 272 ? 0.4986 0.5547 0.7130 -0.1991 -0.0547 -0.0158 270 GLN B CG  
6419 C CD  . GLN B 272 ? 0.6031 0.6599 0.8166 -0.2390 -0.0745 -0.0207 270 GLN B CD  
6420 O OE1 . GLN B 272 ? 0.7576 0.8602 0.9940 -0.2490 -0.0987 -0.0180 270 GLN B OE1 
6421 N NE2 . GLN B 272 ? 0.6902 0.6925 0.8748 -0.2597 -0.0659 -0.0280 270 GLN B NE2 
6422 N N   . LYS B 273 ? 0.4066 0.5287 0.6390 -0.1109 -0.0669 0.0015  271 LYS B N   
6423 C CA  . LYS B 273 ? 0.4041 0.5457 0.6453 -0.0884 -0.0786 0.0097  271 LYS B CA  
6424 C C   . LYS B 273 ? 0.3321 0.4829 0.5930 -0.0624 -0.0586 0.0143  271 LYS B C   
6425 O O   . LYS B 273 ? 0.3433 0.5252 0.6338 -0.0426 -0.0637 0.0215  271 LYS B O   
6426 C CB  . LYS B 273 ? 0.4918 0.5910 0.6782 -0.0882 -0.0874 0.0061  271 LYS B CB  
6427 C CG  . LYS B 273 ? 0.5984 0.7036 0.7804 -0.0704 -0.1070 0.0169  271 LYS B CG  
6428 C CD  . LYS B 273 ? 0.5623 0.6194 0.6795 -0.0786 -0.1138 0.0148  271 LYS B CD  
6429 C CE  . LYS B 273 ? 0.6646 0.7212 0.7666 -0.0704 -0.1451 0.0281  271 LYS B CE  
6430 N NZ  . LYS B 273 ? 0.6689 0.7441 0.8061 -0.0389 -0.1485 0.0396  271 LYS B NZ  
6431 N N   . VAL B 274 ? 0.3198 0.4421 0.5631 -0.0606 -0.0370 0.0093  272 VAL B N   
6432 C CA  . VAL B 274 ? 0.3702 0.4953 0.6225 -0.0398 -0.0200 0.0123  272 VAL B CA  
6433 C C   . VAL B 274 ? 0.4107 0.5808 0.7070 -0.0358 -0.0118 0.0181  272 VAL B C   
6434 O O   . VAL B 274 ? 0.2948 0.4788 0.6040 -0.0139 -0.0033 0.0206  272 VAL B O   
6435 C CB  . VAL B 274 ? 0.3590 0.4506 0.5874 -0.0415 -0.0038 0.0072  272 VAL B CB  
6436 C CG1 . VAL B 274 ? 0.3647 0.4624 0.6013 -0.0274 0.0119  0.0109  272 VAL B CG1 
6437 C CG2 . VAL B 274 ? 0.3582 0.4191 0.5543 -0.0382 -0.0059 0.0014  272 VAL B CG2 
6438 N N   . GLY B 275 ? 0.3131 0.5051 0.6313 -0.0584 -0.0122 0.0194  273 GLY B N   
6439 C CA  . GLY B 275 ? 0.3939 0.6345 0.7567 -0.0605 0.0007  0.0251  273 GLY B CA  
6440 C C   . GLY B 275 ? 0.2685 0.5702 0.6828 -0.0542 -0.0144 0.0292  273 GLY B C   
6441 O O   . GLY B 275 ? 0.3432 0.6985 0.8055 -0.0530 -0.0008 0.0330  273 GLY B O   
6442 N N   . MET B 276 ? 0.2955 0.5930 0.7017 -0.0495 -0.0423 0.0291  274 MET B N   
6443 C CA  . MET B 276 ? 0.2981 0.6534 0.7536 -0.0408 -0.0647 0.0349  274 MET B CA  
6444 C C   . MET B 276 ? 0.2520 0.6026 0.7063 -0.0009 -0.0721 0.0383  274 MET B C   
6445 O O   . MET B 276 ? 0.3094 0.6959 0.7955 0.0126  -0.0979 0.0445  274 MET B O   
6446 C CB  . MET B 276 ? 0.3408 0.6932 0.7838 -0.0678 -0.0976 0.0345  274 MET B CB  
6447 C CG  . MET B 276 ? 0.3811 0.7367 0.8280 -0.1090 -0.0932 0.0302  274 MET B CG  
6448 S SD  . MET B 276 ? 0.5259 0.8811 0.9579 -0.1441 -0.1343 0.0271  274 MET B SD  
6449 C CE  . MET B 276 ? 0.3877 0.8220 0.8784 -0.1219 -0.1590 0.0344  274 MET B CE  
6450 N N   . GLN B 277 ? 0.2557 0.5602 0.6732 0.0180  -0.0528 0.0349  275 GLN B N   
6451 C CA  . GLN B 277 ? 0.3147 0.6025 0.7244 0.0542  -0.0572 0.0370  275 GLN B CA  
6452 C C   . GLN B 277 ? 0.2357 0.4902 0.6198 0.0676  -0.0271 0.0304  275 GLN B C   
6453 O O   . GLN B 277 ? 0.2815 0.5099 0.6372 0.0485  -0.0117 0.0261  275 GLN B O   
6454 C CB  . GLN B 277 ? 0.3287 0.5670 0.6895 0.0545  -0.0848 0.0412  275 GLN B CB  
6455 C CG  . GLN B 277 ? 0.3087 0.4850 0.6064 0.0347  -0.0775 0.0358  275 GLN B CG  
6456 C CD  . GLN B 277 ? 0.4849 0.6208 0.7356 0.0293  -0.1025 0.0411  275 GLN B CD  
6457 O OE1 . GLN B 277 ? 0.3690 0.5170 0.6173 0.0130  -0.1249 0.0442  275 GLN B OE1 
6458 N NE2 . GLN B 277 ? 0.3823 0.4670 0.5903 0.0398  -0.0991 0.0423  275 GLN B NE2 
6459 N N   . LYS B 278 ? 0.3084 0.5613 0.7007 0.1021  -0.0208 0.0293  276 LYS B N   
6460 C CA  . LYS B 278 ? 0.2852 0.5067 0.6501 0.1147  0.0067  0.0212  276 LYS B CA  
6461 C C   . LYS B 278 ? 0.3273 0.4801 0.6275 0.1011  0.0045  0.0180  276 LYS B C   
6462 O O   . LYS B 278 ? 0.3460 0.4824 0.6239 0.0889  0.0219  0.0131  276 LYS B O   
6463 C CB  . LYS B 278 ? 0.2960 0.5183 0.6749 0.1564  0.0116  0.0182  276 LYS B CB  
6464 C CG  . LYS B 278 ? 0.4876 0.6532 0.8170 0.1708  0.0321  0.0079  276 LYS B CG  
6465 C CD  . LYS B 278 ? 0.4244 0.6082 0.7538 0.1618  0.0652  0.0009  276 LYS B CD  
6466 C CE  . LYS B 278 ? 0.4178 0.6694 0.8069 0.1822  0.0876  -0.0016 276 LYS B CE  
6467 N NZ  . LYS B 278 ? 0.7022 0.9502 1.0689 0.1800  0.1244  -0.0102 276 LYS B NZ  
6468 N N   . TYR B 279 ? 0.3558 0.4702 0.6259 0.1015  -0.0173 0.0218  277 TYR B N   
6469 C CA  . TYR B 279 ? 0.3349 0.3949 0.5522 0.0850  -0.0177 0.0187  277 TYR B CA  
6470 C C   . TYR B 279 ? 0.4211 0.4691 0.6205 0.0649  -0.0376 0.0243  277 TYR B C   
6471 O O   . TYR B 279 ? 0.3701 0.4266 0.5777 0.0717  -0.0582 0.0322  277 TYR B O   
6472 C CB  . TYR B 279 ? 0.3332 0.3399 0.5126 0.1026  -0.0151 0.0149  277 TYR B CB  
6473 C CG  . TYR B 279 ? 0.4471 0.4203 0.6097 0.1208  -0.0349 0.0218  277 TYR B CG  
6474 C CD1 . TYR B 279 ? 0.4401 0.3730 0.5630 0.1030  -0.0515 0.0285  277 TYR B CD1 
6475 C CD2 . TYR B 279 ? 0.3768 0.3534 0.5590 0.1571  -0.0350 0.0216  277 TYR B CD2 
6476 C CE1 . TYR B 279 ? 0.4207 0.3118 0.5179 0.1185  -0.0711 0.0379  277 TYR B CE1 
6477 C CE2 . TYR B 279 ? 0.4914 0.4282 0.6544 0.1779  -0.0558 0.0296  277 TYR B CE2 
6478 C CZ  . TYR B 279 ? 0.4642 0.3546 0.5813 0.1573  -0.0753 0.0391  277 TYR B CZ  
6479 O OH  . TYR B 279 ? 0.6709 0.5120 0.7599 0.1771  -0.0978 0.0500  277 TYR B OH  
6480 N N   . SER B 280 ? 0.4305 0.4615 0.6060 0.0412  -0.0314 0.0200  278 SER B N   
6481 C CA  . SER B 280 ? 0.4077 0.4254 0.5598 0.0201  -0.0425 0.0216  278 SER B CA  
6482 C C   . SER B 280 ? 0.4268 0.4066 0.5407 0.0069  -0.0345 0.0173  278 SER B C   
6483 O O   . SER B 280 ? 0.3508 0.3262 0.4653 0.0076  -0.0211 0.0115  278 SER B O   
6484 C CB  . SER B 280 ? 0.3622 0.4092 0.5344 0.0024  -0.0397 0.0179  278 SER B CB  
6485 O OG  . SER B 280 ? 0.4817 0.5370 0.6670 0.0006  -0.0210 0.0123  278 SER B OG  
6486 N N   . THR B 281 ? 0.4200 0.3740 0.4993 -0.0065 -0.0434 0.0209  279 THR B N   
6487 C CA  . THR B 281 ? 0.4124 0.3385 0.4598 -0.0238 -0.0333 0.0172  279 THR B CA  
6488 C C   . THR B 281 ? 0.4965 0.4322 0.5362 -0.0446 -0.0250 0.0105  279 THR B C   
6489 O O   . THR B 281 ? 0.4858 0.4226 0.5135 -0.0510 -0.0349 0.0124  279 THR B O   
6490 C CB  . THR B 281 ? 0.4900 0.3697 0.4937 -0.0262 -0.0445 0.0270  279 THR B CB  
6491 O OG1 . THR B 281 ? 0.4939 0.3661 0.4760 -0.0304 -0.0613 0.0355  279 THR B OG1 
6492 C CG2 . THR B 281 ? 0.4414 0.3013 0.4482 -0.0012 -0.0521 0.0315  279 THR B CG2 
6493 N N   . LEU B 282 ? 0.3944 0.3374 0.4407 -0.0539 -0.0076 0.0013  280 LEU B N   
6494 C CA  . LEU B 282 ? 0.4450 0.3966 0.4865 -0.0686 0.0057  -0.0083 280 LEU B CA  
6495 C C   . LEU B 282 ? 0.4578 0.4001 0.4796 -0.0859 0.0197  -0.0113 280 LEU B C   
6496 O O   . LEU B 282 ? 0.4262 0.3799 0.4678 -0.0860 0.0267  -0.0141 280 LEU B O   
6497 C CB  . LEU B 282 ? 0.4204 0.3975 0.4980 -0.0607 0.0152  -0.0175 280 LEU B CB  
6498 C CG  . LEU B 282 ? 0.4634 0.4452 0.5378 -0.0698 0.0317  -0.0302 280 LEU B CG  
6499 C CD1 . LEU B 282 ? 0.4525 0.4189 0.4983 -0.0795 0.0280  -0.0340 280 LEU B CD1 
6500 C CD2 . LEU B 282 ? 0.4400 0.4396 0.5496 -0.0574 0.0399  -0.0375 280 LEU B CD2 
6501 N N   . GLN B 283 ? 0.4656 0.3884 0.4468 -0.1032 0.0236  -0.0103 281 GLN B N   
6502 C CA  . GLN B 283 ? 0.4653 0.3846 0.4277 -0.1250 0.0430  -0.0137 281 GLN B CA  
6503 C C   . GLN B 283 ? 0.4625 0.4137 0.4480 -0.1270 0.0667  -0.0307 281 GLN B C   
6504 O O   . GLN B 283 ? 0.4614 0.4049 0.4249 -0.1296 0.0718  -0.0379 281 GLN B O   
6505 C CB  . GLN B 283 ? 0.4575 0.3354 0.3558 -0.1448 0.0398  -0.0036 281 GLN B CB  
6506 C CG  . GLN B 283 ? 0.4812 0.3588 0.3600 -0.1730 0.0657  -0.0068 281 GLN B CG  
6507 C CD  . GLN B 283 ? 0.6078 0.4330 0.4131 -0.1964 0.0622  0.0077  281 GLN B CD  
6508 O OE1 . GLN B 283 ? 0.7151 0.5037 0.4819 -0.1888 0.0373  0.0201  281 GLN B OE1 
6509 N NE2 . GLN B 283 ? 0.5936 0.4163 0.3794 -0.2261 0.0863  0.0076  281 GLN B NE2 
6510 N N   . GLY B 284 ? 0.4455 0.4307 0.4748 -0.1241 0.0791  -0.0379 282 GLY B N   
6511 C CA  . GLY B 284 ? 0.3565 0.3757 0.4173 -0.1191 0.1010  -0.0540 282 GLY B CA  
6512 C C   . GLY B 284 ? 0.4407 0.4841 0.5064 -0.1401 0.1261  -0.0598 282 GLY B C   
6513 O O   . GLY B 284 ? 0.4509 0.5243 0.5536 -0.1446 0.1267  -0.0587 282 GLY B O   
6514 N N   . PRO B 285 ? 0.4004 0.4319 0.4264 -0.1567 0.1473  -0.0660 283 PRO B N   
6515 C CA  . PRO B 285 ? 0.4287 0.4914 0.4627 -0.1791 0.1794  -0.0734 283 PRO B CA  
6516 C C   . PRO B 285 ? 0.3929 0.5202 0.5039 -0.1616 0.1960  -0.0890 283 PRO B C   
6517 O O   . PRO B 285 ? 0.4167 0.5527 0.5613 -0.1311 0.1856  -0.0953 283 PRO B O   
6518 C CB  . PRO B 285 ? 0.4877 0.5210 0.4586 -0.1927 0.2004  -0.0808 283 PRO B CB  
6519 C CG  . PRO B 285 ? 0.5007 0.4774 0.4177 -0.1892 0.1686  -0.0679 283 PRO B CG  
6520 C CD  . PRO B 285 ? 0.4378 0.4278 0.4062 -0.1589 0.1438  -0.0670 283 PRO B CD  
6521 N N   . PRO B 286 ? 0.4352 0.6098 0.5769 -0.1806 0.2217  -0.0946 284 PRO B N   
6522 C CA  . PRO B 286 ? 0.3801 0.6207 0.5997 -0.1573 0.2305  -0.1072 284 PRO B CA  
6523 C C   . PRO B 286 ? 0.4023 0.6466 0.6328 -0.1268 0.2484  -0.1262 284 PRO B C   
6524 O O   . PRO B 286 ? 0.4323 0.6490 0.6131 -0.1339 0.2720  -0.1363 284 PRO B O   
6525 C CB  . PRO B 286 ? 0.4194 0.6923 0.6451 -0.1806 0.2480  -0.1053 284 PRO B CB  
6526 C CG  . PRO B 286 ? 0.4449 0.6699 0.6117 -0.2162 0.2363  -0.0878 284 PRO B CG  
6527 C CD  . PRO B 286 ? 0.4574 0.6198 0.5576 -0.2170 0.2344  -0.0861 284 PRO B CD  
6528 N N   . GLY B 287 ? 0.4496 0.7187 0.7370 -0.0924 0.2341  -0.1305 285 GLY B N   
6529 C CA  . GLY B 287 ? 0.4149 0.6804 0.7154 -0.0584 0.2464  -0.1473 285 GLY B CA  
6530 C C   . GLY B 287 ? 0.4247 0.6226 0.6678 -0.0519 0.2411  -0.1514 285 GLY B C   
6531 O O   . GLY B 287 ? 0.4589 0.6377 0.6870 -0.0357 0.2613  -0.1700 285 GLY B O   
6532 N N   . THR B 288 ? 0.3985 0.5553 0.6052 -0.0627 0.2093  -0.1331 286 THR B N   
6533 C CA  . THR B 288 ? 0.4156 0.5110 0.5667 -0.0613 0.1955  -0.1320 286 THR B CA  
6534 C C   . THR B 288 ? 0.4630 0.5427 0.6366 -0.0367 0.1693  -0.1258 286 THR B C   
6535 O O   . THR B 288 ? 0.4691 0.5043 0.6087 -0.0336 0.1614  -0.1287 286 THR B O   
6536 C CB  . THR B 288 ? 0.4008 0.4624 0.4947 -0.0897 0.1793  -0.1158 286 THR B CB  
6537 O OG1 . THR B 288 ? 0.3813 0.4576 0.4991 -0.0935 0.1573  -0.0979 286 THR B OG1 
6538 C CG2 . THR B 288 ? 0.4360 0.4943 0.4858 -0.1172 0.2057  -0.1208 286 THR B CG2 
6539 N N   . GLY B 289 ? 0.3988 0.5113 0.6234 -0.0235 0.1547  -0.1164 287 GLY B N   
6540 C CA  . GLY B 289 ? 0.3773 0.4741 0.6192 -0.0010 0.1328  -0.1092 287 GLY B CA  
6541 C C   . GLY B 289 ? 0.4255 0.5086 0.6552 -0.0095 0.1057  -0.0897 287 GLY B C   
6542 O O   . GLY B 289 ? 0.4514 0.5011 0.6629 -0.0050 0.0923  -0.0835 287 GLY B O   
6543 N N   . LYS B 290 ? 0.3526 0.4604 0.5923 -0.0227 0.0991  -0.0809 288 LYS B N   
6544 C CA  . LYS B 290 ? 0.3284 0.4198 0.5526 -0.0283 0.0770  -0.0653 288 LYS B CA  
6545 C C   . LYS B 290 ? 0.3941 0.4830 0.6376 -0.0081 0.0609  -0.0585 288 LYS B C   
6546 O O   . LYS B 290 ? 0.4228 0.4849 0.6462 -0.0063 0.0502  -0.0499 288 LYS B O   
6547 C CB  . LYS B 290 ? 0.3768 0.4855 0.6023 -0.0466 0.0742  -0.0600 288 LYS B CB  
6548 C CG  . LYS B 290 ? 0.4115 0.5086 0.6030 -0.0704 0.0879  -0.0616 288 LYS B CG  
6549 C CD  . LYS B 290 ? 0.3360 0.4421 0.5253 -0.0923 0.0861  -0.0558 288 LYS B CD  
6550 C CE  . LYS B 290 ? 0.3892 0.5485 0.6246 -0.0991 0.1015  -0.0651 288 LYS B CE  
6551 N NZ  . LYS B 290 ? 0.3121 0.4823 0.5395 -0.1089 0.1313  -0.0760 288 LYS B NZ  
6552 N N   . SER B 291 ? 0.3032 0.4222 0.5858 0.0068  0.0588  -0.0613 289 SER B N   
6553 C CA  . SER B 291 ? 0.4064 0.5169 0.6983 0.0257  0.0407  -0.0522 289 SER B CA  
6554 C C   . SER B 291 ? 0.3917 0.4644 0.6693 0.0399  0.0435  -0.0531 289 SER B C   
6555 O O   . SER B 291 ? 0.3567 0.4021 0.6180 0.0451  0.0310  -0.0417 289 SER B O   
6556 C CB  . SER B 291 ? 0.3058 0.4596 0.6446 0.0398  0.0325  -0.0540 289 SER B CB  
6557 O OG  . SER B 291 ? 0.5695 0.7476 0.9418 0.0537  0.0502  -0.0679 289 SER B OG  
6558 N N   . HIS B 292 ? 0.3920 0.4581 0.6704 0.0438  0.0614  -0.0672 290 HIS B N   
6559 C CA  . HIS B 292 ? 0.4137 0.4331 0.6702 0.0523  0.0643  -0.0705 290 HIS B CA  
6560 C C   . HIS B 292 ? 0.4313 0.4201 0.6501 0.0314  0.0577  -0.0618 290 HIS B C   
6561 O O   . HIS B 292 ? 0.4441 0.4001 0.6487 0.0332  0.0497  -0.0537 290 HIS B O   
6562 C CB  . HIS B 292 ? 0.4184 0.4330 0.6738 0.0573  0.0872  -0.0911 290 HIS B CB  
6563 C CG  . HIS B 292 ? 0.4788 0.4398 0.7139 0.0707  0.0903  -0.0985 290 HIS B CG  
6564 N ND1 . HIS B 292 ? 0.4816 0.4303 0.7396 0.1026  0.0878  -0.1004 290 HIS B ND1 
6565 C CD2 . HIS B 292 ? 0.5216 0.4337 0.7133 0.0557  0.0938  -0.1046 290 HIS B CD2 
6566 C CE1 . HIS B 292 ? 0.6090 0.4956 0.8341 0.1066  0.0916  -0.1076 290 HIS B CE1 
6567 N NE2 . HIS B 292 ? 0.6471 0.5123 0.8321 0.0760  0.0952  -0.1110 290 HIS B NE2 
6568 N N   . PHE B 293 ? 0.4528 0.4537 0.6571 0.0112  0.0604  -0.0621 291 PHE B N   
6569 C CA  . PHE B 293 ? 0.4443 0.4291 0.6242 -0.0052 0.0516  -0.0532 291 PHE B CA  
6570 C C   . PHE B 293 ? 0.3708 0.3588 0.5570 -0.0012 0.0392  -0.0378 291 PHE B C   
6571 O O   . PHE B 293 ? 0.4226 0.3933 0.5991 -0.0063 0.0350  -0.0305 291 PHE B O   
6572 C CB  . PHE B 293 ? 0.3997 0.3966 0.5642 -0.0218 0.0531  -0.0541 291 PHE B CB  
6573 C CG  . PHE B 293 ? 0.4133 0.4023 0.5612 -0.0339 0.0413  -0.0449 291 PHE B CG  
6574 C CD1 . PHE B 293 ? 0.4318 0.4326 0.5880 -0.0309 0.0320  -0.0327 291 PHE B CD1 
6575 C CD2 . PHE B 293 ? 0.4169 0.3891 0.5416 -0.0473 0.0388  -0.0495 291 PHE B CD2 
6576 C CE1 . PHE B 293 ? 0.4329 0.4351 0.5839 -0.0371 0.0226  -0.0251 291 PHE B CE1 
6577 C CE2 . PHE B 293 ? 0.4872 0.4632 0.6070 -0.0568 0.0244  -0.0404 291 PHE B CE2 
6578 C CZ  . PHE B 293 ? 0.4081 0.4025 0.5456 -0.0496 0.0174  -0.0280 291 PHE B CZ  
6579 N N   . ALA B 294 ? 0.3515 0.3618 0.5517 0.0052  0.0345  -0.0334 292 ALA B N   
6580 C CA  . ALA B 294 ? 0.3639 0.3735 0.5594 0.0077  0.0246  -0.0211 292 ALA B CA  
6581 C C   . ALA B 294 ? 0.3846 0.3715 0.5753 0.0172  0.0207  -0.0132 292 ALA B C   
6582 O O   . ALA B 294 ? 0.3999 0.3748 0.5758 0.0118  0.0199  -0.0035 292 ALA B O   
6583 C CB  . ALA B 294 ? 0.3464 0.3776 0.5515 0.0102  0.0180  -0.0207 292 ALA B CB  
6584 N N   . ILE B 295 ? 0.4278 0.4077 0.6305 0.0321  0.0192  -0.0167 293 ILE B N   
6585 C CA  . ILE B 295 ? 0.3991 0.3458 0.5898 0.0425  0.0128  -0.0067 293 ILE B CA  
6586 C C   . ILE B 295 ? 0.4726 0.3828 0.6449 0.0313  0.0206  -0.0073 293 ILE B C   
6587 O O   . ILE B 295 ? 0.4899 0.3702 0.6416 0.0258  0.0183  0.0051  293 ILE B O   
6588 C CB  . ILE B 295 ? 0.4539 0.4027 0.6661 0.0675  0.0052  -0.0094 293 ILE B CB  
6589 C CG1 . ILE B 295 ? 0.4704 0.4623 0.7052 0.0732  -0.0066 -0.0084 293 ILE B CG1 
6590 C CG2 . ILE B 295 ? 0.4457 0.3474 0.6371 0.0801  -0.0043 0.0036  293 ILE B CG2 
6591 C CD1 . ILE B 295 ? 0.5039 0.4922 0.7125 0.0636  -0.0176 0.0045  293 ILE B CD1 
6592 N N   . GLY B 296 ? 0.4233 0.3329 0.5977 0.0239  0.0298  -0.0216 294 GLY B N   
6593 C CA  . GLY B 296 ? 0.4632 0.3379 0.6173 0.0078  0.0338  -0.0240 294 GLY B CA  
6594 C C   . GLY B 296 ? 0.5012 0.3856 0.6487 -0.0143 0.0318  -0.0128 294 GLY B C   
6595 O O   . GLY B 296 ? 0.6152 0.4719 0.7489 -0.0298 0.0323  -0.0076 294 GLY B O   
6596 N N   . LEU B 297 ? 0.4505 0.3742 0.6094 -0.0164 0.0305  -0.0096 295 LEU B N   
6597 C CA  . LEU B 297 ? 0.4478 0.3892 0.6089 -0.0308 0.0309  -0.0002 295 LEU B CA  
6598 C C   . LEU B 297 ? 0.5001 0.4232 0.6502 -0.0336 0.0340  0.0138  295 LEU B C   
6599 O O   . LEU B 297 ? 0.4954 0.4222 0.6467 -0.0520 0.0389  0.0203  295 LEU B O   
6600 C CB  . LEU B 297 ? 0.4578 0.4332 0.6285 -0.0243 0.0295  0.0004  295 LEU B CB  
6601 C CG  . LEU B 297 ? 0.4714 0.4735 0.6521 -0.0313 0.0308  0.0060  295 LEU B CG  
6602 C CD1 . LEU B 297 ? 0.4611 0.4728 0.6507 -0.0474 0.0259  0.0024  295 LEU B CD1 
6603 C CD2 . LEU B 297 ? 0.5929 0.6111 0.7744 -0.0197 0.0285  0.0045  295 LEU B CD2 
6604 N N   . ALA B 298 ? 0.5195 0.4250 0.6584 -0.0171 0.0306  0.0194  296 ALA B N   
6605 C CA  . ALA B 298 ? 0.4916 0.3709 0.6074 -0.0201 0.0324  0.0351  296 ALA B CA  
6606 C C   . ALA B 298 ? 0.5283 0.3609 0.6278 -0.0330 0.0342  0.0392  296 ALA B C   
6607 O O   . ALA B 298 ? 0.5905 0.4048 0.6716 -0.0505 0.0411  0.0526  296 ALA B O   
6608 C CB  . ALA B 298 ? 0.5058 0.3743 0.6088 0.0015  0.0217  0.0409  296 ALA B CB  
6609 N N   . LEU B 299 ? 0.5647 0.3736 0.6668 -0.0260 0.0301  0.0272  297 LEU B N   
6610 C CA  . LEU B 299 ? 0.5952 0.3475 0.6754 -0.0384 0.0310  0.0279  297 LEU B CA  
6611 C C   . LEU B 299 ? 0.5017 0.2649 0.5865 -0.0726 0.0365  0.0243  297 LEU B C   
6612 O O   . LEU B 299 ? 0.5265 0.2514 0.5917 -0.0963 0.0391  0.0321  297 LEU B O   
6613 C CB  . LEU B 299 ? 0.6487 0.3711 0.7288 -0.0166 0.0275  0.0122  297 LEU B CB  
6614 C CG  . LEU B 299 ? 0.7044 0.4178 0.7884 0.0190  0.0189  0.0165  297 LEU B CG  
6615 C CD1 . LEU B 299 ? 0.6256 0.3233 0.7211 0.0434  0.0206  -0.0024 297 LEU B CD1 
6616 C CD2 . LEU B 299 ? 0.6496 0.3084 0.7000 0.0209  0.0115  0.0378  297 LEU B CD2 
6617 N N   . TYR B 300 ? 0.5953 0.4092 0.7051 -0.0774 0.0361  0.0139  298 TYR B N   
6618 C CA  . TYR B 300 ? 0.5706 0.4036 0.6905 -0.1084 0.0355  0.0112  298 TYR B CA  
6619 C C   . TYR B 300 ? 0.4493 0.3188 0.5859 -0.1255 0.0430  0.0267  298 TYR B C   
6620 O O   . TYR B 300 ? 0.4640 0.3417 0.6095 -0.1565 0.0439  0.0294  298 TYR B O   
6621 C CB  . TYR B 300 ? 0.4519 0.3228 0.5880 -0.1060 0.0290  -0.0025 298 TYR B CB  
6622 C CG  . TYR B 300 ? 0.4202 0.3050 0.5632 -0.1373 0.0211  -0.0065 298 TYR B CG  
6623 C CD1 . TYR B 300 ? 0.4785 0.3154 0.5946 -0.1559 0.0159  -0.0182 298 TYR B CD1 
6624 C CD2 . TYR B 300 ? 0.3878 0.3331 0.5644 -0.1472 0.0172  0.0004  298 TYR B CD2 
6625 C CE1 . TYR B 300 ? 0.5518 0.4015 0.6720 -0.1887 0.0041  -0.0223 298 TYR B CE1 
6626 C CE2 . TYR B 300 ? 0.4189 0.3853 0.6088 -0.1760 0.0051  -0.0024 298 TYR B CE2 
6627 C CZ  . TYR B 300 ? 0.4754 0.3942 0.6357 -0.1992 -0.0030 -0.0135 298 TYR B CZ  
6628 O OH  . TYR B 300 ? 0.4919 0.4313 0.6626 -0.2320 -0.0196 -0.0169 298 TYR B OH  
6629 N N   . TYR B 301 ? 0.4805 0.3735 0.6213 -0.1075 0.0494  0.0356  299 TYR B N   
6630 C CA  . TYR B 301 ? 0.5319 0.4574 0.6834 -0.1193 0.0628  0.0484  299 TYR B CA  
6631 C C   . TYR B 301 ? 0.5126 0.3960 0.6264 -0.1126 0.0697  0.0626  299 TYR B C   
6632 O O   . TYR B 301 ? 0.5429 0.4401 0.6485 -0.0949 0.0741  0.0669  299 TYR B O   
6633 C CB  . TYR B 301 ? 0.4743 0.4595 0.6550 -0.1036 0.0651  0.0444  299 TYR B CB  
6634 C CG  . TYR B 301 ? 0.4472 0.4716 0.6610 -0.1098 0.0546  0.0344  299 TYR B CG  
6635 C CD1 . TYR B 301 ? 0.4958 0.5532 0.7385 -0.1366 0.0548  0.0367  299 TYR B CD1 
6636 C CD2 . TYR B 301 ? 0.4130 0.4414 0.6272 -0.0915 0.0427  0.0240  299 TYR B CD2 
6637 C CE1 . TYR B 301 ? 0.4289 0.5219 0.6991 -0.1416 0.0390  0.0292  299 TYR B CE1 
6638 C CE2 . TYR B 301 ? 0.3525 0.4090 0.5864 -0.0974 0.0302  0.0175  299 TYR B CE2 
6639 C CZ  . TYR B 301 ? 0.4284 0.5167 0.6896 -0.1209 0.0262  0.0203  299 TYR B CZ  
6640 O OH  . TYR B 301 ? 0.3061 0.4223 0.5845 -0.1262 0.0080  0.0154  299 TYR B OH  
6641 N N   . PRO B 302 ? 0.4967 0.3215 0.5804 -0.1277 0.0692  0.0707  300 PRO B N   
6642 C CA  . PRO B 302 ? 0.6218 0.3925 0.6603 -0.1173 0.0691  0.0862  300 PRO B CA  
6643 C C   . PRO B 302 ? 0.6237 0.4122 0.6448 -0.1220 0.0847  0.1009  300 PRO B C   
6644 O O   . PRO B 302 ? 0.7295 0.4861 0.7133 -0.1040 0.0789  0.1106  300 PRO B O   
6645 C CB  . PRO B 302 ? 0.6315 0.3338 0.6410 -0.1407 0.0677  0.0931  300 PRO B CB  
6646 C CG  . PRO B 302 ? 0.6340 0.3730 0.6758 -0.1760 0.0747  0.0858  300 PRO B CG  
6647 C CD  . PRO B 302 ? 0.5161 0.3136 0.5991 -0.1571 0.0666  0.0670  300 PRO B CD  
6648 N N   . SER B 303 ? 0.5275 0.3662 0.5730 -0.1447 0.1043  0.1025  301 SER B N   
6649 C CA  . SER B 303 ? 0.6688 0.5200 0.6915 -0.1499 0.1255  0.1149  301 SER B CA  
6650 C C   . SER B 303 ? 0.6333 0.5344 0.6723 -0.1236 0.1296  0.1044  301 SER B C   
6651 O O   . SER B 303 ? 0.7046 0.6134 0.7187 -0.1235 0.1485  0.1108  301 SER B O   
6652 C CB  . SER B 303 ? 0.5672 0.4493 0.6090 -0.1892 0.1507  0.1227  301 SER B CB  
6653 O OG  . SER B 303 ? 0.6847 0.6422 0.7938 -0.1931 0.1527  0.1086  301 SER B OG  
6654 N N   . ALA B 304 ? 0.4773 0.4053 0.5503 -0.1028 0.1135  0.0884  302 ALA B N   
6655 C CA  . ALA B 304 ? 0.5435 0.5133 0.6330 -0.0810 0.1168  0.0776  302 ALA B CA  
6656 C C   . ALA B 304 ? 0.4881 0.4259 0.5347 -0.0589 0.1064  0.0780  302 ALA B C   
6657 O O   . ALA B 304 ? 0.5527 0.4519 0.5799 -0.0504 0.0865  0.0807  302 ALA B O   
6658 C CB  . ALA B 304 ? 0.4082 0.4115 0.5432 -0.0716 0.1025  0.0629  302 ALA B CB  
6659 N N   . ARG B 305 ? 0.4523 0.4072 0.4850 -0.0491 0.1196  0.0744  303 ARG B N   
6660 C CA  . ARG B 305 ? 0.5413 0.4713 0.5339 -0.0309 0.1075  0.0712  303 ARG B CA  
6661 C C   . ARG B 305 ? 0.4485 0.3999 0.4725 -0.0139 0.0916  0.0554  303 ARG B C   
6662 O O   . ARG B 305 ? 0.4348 0.4207 0.4898 -0.0091 0.1015  0.0458  303 ARG B O   
6663 C CB  . ARG B 305 ? 0.5840 0.5136 0.5373 -0.0307 0.1312  0.0719  303 ARG B CB  
6664 C CG  . ARG B 305 ? 0.5903 0.4984 0.5011 -0.0140 0.1201  0.0634  303 ARG B CG  
6665 C CD  . ARG B 305 ? 0.7551 0.6557 0.6171 -0.0165 0.1496  0.0631  303 ARG B CD  
6666 N NE  . ARG B 305 ? 0.7762 0.6593 0.5992 -0.0015 0.1448  0.0489  303 ARG B NE  
6667 C CZ  . ARG B 305 ? 0.7781 0.6224 0.5537 0.0015  0.1166  0.0496  303 ARG B CZ  
6668 N NH1 . ARG B 305 ? 0.7945 0.6129 0.5519 -0.0050 0.0925  0.0659  303 ARG B NH1 
6669 N NH2 . ARG B 305 ? 0.8024 0.6313 0.5457 0.0113  0.1118  0.0339  303 ARG B NH2 
6670 N N   . ILE B 306 ? 0.4547 0.3866 0.4725 -0.0051 0.0671  0.0535  304 ILE B N   
6671 C CA  . ILE B 306 ? 0.4751 0.4248 0.5207 0.0048  0.0535  0.0403  304 ILE B CA  
6672 C C   . ILE B 306 ? 0.4869 0.4212 0.5036 0.0138  0.0377  0.0360  304 ILE B C   
6673 O O   . ILE B 306 ? 0.5425 0.4540 0.5327 0.0155  0.0235  0.0440  304 ILE B O   
6674 C CB  . ILE B 306 ? 0.4223 0.3749 0.4996 0.0032  0.0415  0.0385  304 ILE B CB  
6675 C CG1 . ILE B 306 ? 0.4406 0.4025 0.5396 -0.0107 0.0534  0.0417  304 ILE B CG1 
6676 C CG2 . ILE B 306 ? 0.3947 0.3657 0.4948 0.0092  0.0320  0.0259  304 ILE B CG2 
6677 C CD1 . ILE B 306 ? 0.4893 0.4458 0.6092 -0.0135 0.0439  0.0368  304 ILE B CD1 
6678 N N   . VAL B 307 ? 0.5118 0.4560 0.5321 0.0186  0.0375  0.0241  305 VAL B N   
6679 C CA  . VAL B 307 ? 0.5333 0.4642 0.5304 0.0214  0.0204  0.0172  305 VAL B CA  
6680 C C   . VAL B 307 ? 0.4666 0.4152 0.5004 0.0198  0.0075  0.0099  305 VAL B C   
6681 O O   . VAL B 307 ? 0.4849 0.4450 0.5401 0.0197  0.0154  0.0043  305 VAL B O   
6682 C CB  . VAL B 307 ? 0.6082 0.5237 0.5700 0.0253  0.0317  0.0080  305 VAL B CB  
6683 C CG1 . VAL B 307 ? 0.5675 0.4649 0.5048 0.0224  0.0110  -0.0012 305 VAL B CG1 
6684 C CG2 . VAL B 307 ? 0.5999 0.4981 0.5183 0.0250  0.0485  0.0145  305 VAL B CG2 
6685 N N   . TYR B 308 ? 0.4395 0.3924 0.4816 0.0188  -0.0120 0.0109  306 TYR B N   
6686 C CA  . TYR B 308 ? 0.4469 0.4215 0.5234 0.0146  -0.0209 0.0035  306 TYR B CA  
6687 C C   . TYR B 308 ? 0.4394 0.4084 0.4975 0.0064  -0.0344 -0.0043 306 TYR B C   
6688 O O   . TYR B 308 ? 0.4981 0.4589 0.5330 0.0056  -0.0511 -0.0023 306 TYR B O   
6689 C CB  . TYR B 308 ? 0.4176 0.4090 0.5245 0.0201  -0.0312 0.0074  306 TYR B CB  
6690 C CG  . TYR B 308 ? 0.4376 0.4246 0.5584 0.0249  -0.0187 0.0123  306 TYR B CG  
6691 C CD1 . TYR B 308 ? 0.3602 0.3607 0.5080 0.0213  -0.0083 0.0055  306 TYR B CD1 
6692 C CD2 . TYR B 308 ? 0.3575 0.3208 0.4569 0.0297  -0.0180 0.0240  306 TYR B CD2 
6693 C CE1 . TYR B 308 ? 0.3630 0.3539 0.5175 0.0221  0.0008  0.0079  306 TYR B CE1 
6694 C CE2 . TYR B 308 ? 0.4342 0.3866 0.5425 0.0292  -0.0076 0.0279  306 TYR B CE2 
6695 C CZ  . TYR B 308 ? 0.4444 0.4110 0.5809 0.0252  0.0009  0.0187  306 TYR B CZ  
6696 O OH  . TYR B 308 ? 0.3953 0.3459 0.5350 0.0212  0.0090  0.0205  306 TYR B OH  
6697 N N   . THR B 309 ? 0.4331 0.4011 0.4959 -0.0017 -0.0296 -0.0123 307 THR B N   
6698 C CA  . THR B 309 ? 0.4550 0.4072 0.4944 -0.0142 -0.0414 -0.0204 307 THR B CA  
6699 C C   . THR B 309 ? 0.4282 0.3974 0.4956 -0.0297 -0.0433 -0.0251 307 THR B C   
6700 O O   . THR B 309 ? 0.4421 0.4237 0.5333 -0.0285 -0.0309 -0.0235 307 THR B O   
6701 C CB  . THR B 309 ? 0.5498 0.4611 0.5441 -0.0094 -0.0311 -0.0259 307 THR B CB  
6702 O OG1 . THR B 309 ? 0.6008 0.4843 0.5593 -0.0227 -0.0454 -0.0350 307 THR B OG1 
6703 C CG2 . THR B 309 ? 0.4339 0.3404 0.4409 -0.0048 -0.0166 -0.0270 307 THR B CG2 
6704 N N   . ALA B 310 ? 0.4849 0.4540 0.5457 -0.0477 -0.0592 -0.0308 308 ALA B N   
6705 C CA  . ALA B 310 ? 0.4430 0.4245 0.5229 -0.0700 -0.0596 -0.0352 308 ALA B CA  
6706 C C   . ALA B 310 ? 0.5160 0.4737 0.5648 -0.0923 -0.0773 -0.0425 308 ALA B C   
6707 O O   . ALA B 310 ? 0.5333 0.4717 0.5497 -0.0887 -0.0913 -0.0449 308 ALA B O   
6708 C CB  . ALA B 310 ? 0.3953 0.4355 0.5341 -0.0730 -0.0595 -0.0337 308 ALA B CB  
6709 N N   . CYS B 311 ? 0.4952 0.4484 0.5468 -0.1186 -0.0766 -0.0461 309 CYS B N   
6710 C CA  . CYS B 311 ? 0.5993 0.5225 0.6175 -0.1461 -0.0942 -0.0541 309 CYS B CA  
6711 C C   . CYS B 311 ? 0.5529 0.5298 0.6069 -0.1632 -0.1183 -0.0561 309 CYS B C   
6712 O O   . CYS B 311 ? 0.5999 0.5542 0.6192 -0.1749 -0.1409 -0.0621 309 CYS B O   
6713 C CB  . CYS B 311 ? 0.6807 0.5742 0.6850 -0.1735 -0.0860 -0.0554 309 CYS B CB  
6714 S SG  . CYS B 311 ? 0.7435 0.5583 0.6932 -0.1534 -0.0687 -0.0530 309 CYS B SG  
6715 N N   . SER B 312 ? 0.4665 0.5147 0.5891 -0.1633 -0.1150 -0.0521 310 SER B N   
6716 C CA  . SER B 312 ? 0.5322 0.6455 0.7052 -0.1771 -0.1383 -0.0535 310 SER B CA  
6717 C C   . SER B 312 ? 0.4376 0.5837 0.6354 -0.1437 -0.1514 -0.0470 310 SER B C   
6718 O O   . SER B 312 ? 0.4497 0.5871 0.6479 -0.1136 -0.1345 -0.0410 310 SER B O   
6719 C CB  . SER B 312 ? 0.4185 0.5959 0.6578 -0.1978 -0.1241 -0.0546 310 SER B CB  
6720 O OG  . SER B 312 ? 0.4928 0.7160 0.7824 -0.1683 -0.1068 -0.0507 310 SER B OG  
6721 N N   . HIS B 313 ? 0.5323 0.7132 0.7484 -0.1510 -0.1847 -0.0471 311 HIS B N   
6722 C CA  . HIS B 313 ? 0.5031 0.7111 0.7403 -0.1189 -0.2020 -0.0382 311 HIS B CA  
6723 C C   . HIS B 313 ? 0.4908 0.7627 0.8072 -0.0972 -0.1862 -0.0348 311 HIS B C   
6724 O O   . HIS B 313 ? 0.4856 0.7522 0.8059 -0.0632 -0.1833 -0.0268 311 HIS B O   
6725 C CB  . HIS B 313 ? 0.5288 0.7639 0.7701 -0.1314 -0.2469 -0.0378 311 HIS B CB  
6726 C CG  . HIS B 313 ? 0.5568 0.7191 0.7058 -0.1430 -0.2654 -0.0408 311 HIS B CG  
6727 N ND1 . HIS B 313 ? 0.6504 0.7640 0.7396 -0.1173 -0.2696 -0.0329 311 HIS B ND1 
6728 C CD2 . HIS B 313 ? 0.5893 0.7157 0.6906 -0.1789 -0.2796 -0.0520 311 HIS B CD2 
6729 C CE1 . HIS B 313 ? 0.7134 0.7668 0.7217 -0.1348 -0.2827 -0.0404 311 HIS B CE1 
6730 N NE2 . HIS B 313 ? 0.6676 0.7243 0.6805 -0.1712 -0.2902 -0.0528 311 HIS B NE2 
6731 N N   . ALA B 314 ? 0.4670 0.7944 0.8421 -0.1178 -0.1735 -0.0417 312 ALA B N   
6732 C CA  . ALA B 314 ? 0.4402 0.8274 0.8877 -0.0971 -0.1528 -0.0424 312 ALA B CA  
6733 C C   . ALA B 314 ? 0.4095 0.7494 0.8269 -0.0740 -0.1205 -0.0403 312 ALA B C   
6734 O O   . ALA B 314 ? 0.4519 0.8032 0.8943 -0.0409 -0.1145 -0.0372 312 ALA B O   
6735 C CB  . ALA B 314 ? 0.2774 0.7240 0.7758 -0.1289 -0.1357 -0.0501 312 ALA B CB  
6736 N N   . ALA B 315 ? 0.4527 0.7371 0.8158 -0.0913 -0.1017 -0.0420 313 ALA B N   
6737 C CA  . ALA B 315 ? 0.4407 0.6860 0.7780 -0.0734 -0.0751 -0.0400 313 ALA B CA  
6738 C C   . ALA B 315 ? 0.4798 0.6884 0.7866 -0.0437 -0.0842 -0.0317 313 ALA B C   
6739 O O   . ALA B 315 ? 0.4922 0.6955 0.8076 -0.0215 -0.0701 -0.0294 313 ALA B O   
6740 C CB  . ALA B 315 ? 0.4457 0.6397 0.7316 -0.0953 -0.0602 -0.0414 313 ALA B CB  
6741 N N   . VAL B 316 ? 0.3974 0.5752 0.6620 -0.0460 -0.1063 -0.0276 314 VAL B N   
6742 C CA  . VAL B 316 ? 0.4110 0.5539 0.6413 -0.0223 -0.1132 -0.0181 314 VAL B CA  
6743 C C   . VAL B 316 ? 0.4529 0.6292 0.7260 0.0027  -0.1264 -0.0116 314 VAL B C   
6744 O O   . VAL B 316 ? 0.4433 0.5962 0.7076 0.0245  -0.1177 -0.0046 314 VAL B O   
6745 C CB  . VAL B 316 ? 0.4459 0.5497 0.6165 -0.0317 -0.1332 -0.0166 314 VAL B CB  
6746 C CG1 . VAL B 316 ? 0.4809 0.5535 0.6149 -0.0101 -0.1406 -0.0049 314 VAL B CG1 
6747 C CG2 . VAL B 316 ? 0.4311 0.4898 0.5552 -0.0472 -0.1164 -0.0236 314 VAL B CG2 
6748 N N   . ASP B 317 ? 0.4406 0.6717 0.7627 0.0000  -0.1484 -0.0138 315 ASP B N   
6749 C CA  . ASP B 317 ? 0.4252 0.6889 0.7917 0.0297  -0.1656 -0.0070 315 ASP B CA  
6750 C C   . ASP B 317 ? 0.4308 0.7111 0.8408 0.0504  -0.1374 -0.0118 315 ASP B C   
6751 O O   . ASP B 317 ? 0.4322 0.7014 0.8514 0.0816  -0.1425 -0.0047 315 ASP B O   
6752 C CB  . ASP B 317 ? 0.4631 0.7947 0.8841 0.0224  -0.1970 -0.0092 315 ASP B CB  
6753 C CG  . ASP B 317 ? 0.4680 0.7758 0.8375 0.0053  -0.2330 -0.0038 315 ASP B CG  
6754 O OD1 . ASP B 317 ? 0.5609 0.7987 0.8523 0.0061  -0.2316 0.0024  315 ASP B OD1 
6755 O OD2 . ASP B 317 ? 0.5251 0.8856 0.9316 -0.0103 -0.2620 -0.0069 315 ASP B OD2 
6756 N N   . ALA B 318 ? 0.3985 0.6976 0.8279 0.0331  -0.1079 -0.0237 316 ALA B N   
6757 C CA  . ALA B 318 ? 0.4600 0.7654 0.9165 0.0500  -0.0787 -0.0308 316 ALA B CA  
6758 C C   . ALA B 318 ? 0.4440 0.6811 0.8476 0.0626  -0.0675 -0.0245 316 ALA B C   
6759 O O   . ALA B 318 ? 0.4763 0.7018 0.8922 0.0866  -0.0577 -0.0259 316 ALA B O   
6760 C CB  . ALA B 318 ? 0.4164 0.7472 0.8881 0.0236  -0.0499 -0.0433 316 ALA B CB  
6761 N N   . LEU B 319 ? 0.3885 0.5798 0.7344 0.0461  -0.0682 -0.0187 317 LEU B N   
6762 C CA  . LEU B 319 ? 0.5004 0.6366 0.8027 0.0543  -0.0588 -0.0116 317 LEU B CA  
6763 C C   . LEU B 319 ? 0.4440 0.5563 0.7335 0.0769  -0.0786 0.0015  317 LEU B C   
6764 O O   . LEU B 319 ? 0.4653 0.5428 0.7417 0.0903  -0.0703 0.0061  317 LEU B O   
6765 C CB  . LEU B 319 ? 0.4406 0.5442 0.6935 0.0346  -0.0535 -0.0092 317 LEU B CB  
6766 C CG  . LEU B 319 ? 0.5191 0.6260 0.7708 0.0161  -0.0334 -0.0181 317 LEU B CG  
6767 C CD1 . LEU B 319 ? 0.5155 0.5970 0.7268 0.0010  -0.0358 -0.0166 317 LEU B CD1 
6768 C CD2 . LEU B 319 ? 0.4297 0.5178 0.6766 0.0210  -0.0143 -0.0197 317 LEU B CD2 
6769 N N   . CYS B 320 ? 0.4480 0.5725 0.7345 0.0787  -0.1071 0.0086  318 CYS B N   
6770 C CA  . CYS B 320 ? 0.5054 0.6050 0.7751 0.1009  -0.1309 0.0238  318 CYS B CA  
6771 C C   . CYS B 320 ? 0.5310 0.6464 0.8501 0.1316  -0.1325 0.0228  318 CYS B C   
6772 O O   . CYS B 320 ? 0.5559 0.6250 0.8518 0.1516  -0.1375 0.0344  318 CYS B O   
6773 C CB  . CYS B 320 ? 0.4736 0.5906 0.7340 0.0961  -0.1661 0.0300  318 CYS B CB  
6774 S SG  . CYS B 320 ? 0.5881 0.6684 0.7739 0.0661  -0.1667 0.0304  318 CYS B SG  
6775 N N   . GLU B 321 ? 0.4523 0.6297 0.8379 0.1356  -0.1258 0.0086  319 GLU B N   
6776 C CA  . GLU B 321 ? 0.4403 0.6383 0.8787 0.1700  -0.1246 0.0043  319 GLU B CA  
6777 C C   . GLU B 321 ? 0.4732 0.6229 0.8920 0.1775  -0.0940 -0.0023 319 GLU B C   
6778 O O   . GLU B 321 ? 0.5660 0.6792 0.9804 0.2062  -0.0972 0.0025  319 GLU B O   
6779 C CB  . GLU B 321 ? 0.4523 0.7325 0.9568 0.1660  -0.1162 -0.0101 319 GLU B CB  
6780 C CG  . GLU B 321 ? 0.4210 0.7525 0.9487 0.1609  -0.1493 -0.0030 319 GLU B CG  
6781 C CD  . GLU B 321 ? 0.5555 0.8945 1.0979 0.1962  -0.1713 0.0088  319 GLU B CD  
6782 O OE1 . GLU B 321 ? 0.7200 1.0198 1.2532 0.2253  -0.1593 0.0110  319 GLU B OE1 
6783 O OE2 . GLU B 321 ? 0.6635 1.0453 1.2248 0.1941  -0.2014 0.0161  319 GLU B OE2 
6784 N N   . LYS B 322 ? 0.4196 0.5627 0.8193 0.1504  -0.0658 -0.0127 320 LYS B N   
6785 C CA  . LYS B 322 ? 0.5051 0.6028 0.8819 0.1524  -0.0405 -0.0199 320 LYS B CA  
6786 C C   . LYS B 322 ? 0.5342 0.5602 0.8531 0.1518  -0.0484 -0.0037 320 LYS B C   
6787 O O   . LYS B 322 ? 0.6123 0.5906 0.9146 0.1628  -0.0390 -0.0052 320 LYS B O   
6788 C CB  . LYS B 322 ? 0.4683 0.5773 0.8348 0.1223  -0.0148 -0.0322 320 LYS B CB  
6789 C CG  . LYS B 322 ? 0.4668 0.5298 0.8029 0.1173  0.0073  -0.0399 320 LYS B CG  
6790 C CD  . LYS B 322 ? 0.3959 0.4647 0.7606 0.1389  0.0256  -0.0575 320 LYS B CD  
6791 C CE  . LYS B 322 ? 0.4924 0.6262 0.8985 0.1315  0.0430  -0.0726 320 LYS B CE  
6792 N NZ  . LYS B 322 ? 0.5976 0.7356 1.0236 0.1502  0.0691  -0.0931 320 LYS B NZ  
6793 N N   . ALA B 323 ? 0.4900 0.5051 0.7744 0.1374  -0.0643 0.0110  321 ALA B N   
6794 C CA  . ALA B 323 ? 0.5754 0.5277 0.8041 0.1335  -0.0685 0.0276  321 ALA B CA  
6795 C C   . ALA B 323 ? 0.6169 0.5340 0.8398 0.1631  -0.0898 0.0412  321 ALA B C   
6796 O O   . ALA B 323 ? 0.7281 0.5816 0.9113 0.1644  -0.0867 0.0517  321 ALA B O   
6797 C CB  . ALA B 323 ? 0.5385 0.4900 0.7294 0.1123  -0.0758 0.0375  321 ALA B CB  
6798 N N   . LEU B 324 ? 0.6189 0.5761 0.8817 0.1863  -0.1133 0.0421  322 LEU B N   
6799 C CA  . LEU B 324 ? 0.6076 0.5333 0.8682 0.2204  -0.1396 0.0568  322 LEU B CA  
6800 C C   . LEU B 324 ? 0.6873 0.5734 0.9515 0.2408  -0.1210 0.0494  322 LEU B C   
6801 O O   . LEU B 324 ? 0.7327 0.5628 0.9622 0.2580  -0.1306 0.0644  322 LEU B O   
6802 C CB  . LEU B 324 ? 0.5528 0.5479 0.8638 0.2378  -0.1642 0.0558  322 LEU B CB  
6803 C CG  . LEU B 324 ? 0.7452 0.7200 1.0301 0.2574  -0.1981 0.0778  322 LEU B CG  
6804 C CD1 . LEU B 324 ? 0.7148 0.6316 0.9231 0.2387  -0.2168 0.0986  322 LEU B CD1 
6805 C CD2 . LEU B 324 ? 0.6919 0.7500 1.0331 0.2660  -0.2196 0.0742  322 LEU B CD2 
6806 N N   . LYS B 325 ? 0.6839 0.5945 0.9801 0.2358  -0.0920 0.0263  323 LYS B N   
6807 C CA  . LYS B 325 ? 0.6838 0.5544 0.9727 0.2515  -0.0711 0.0151  323 LYS B CA  
6808 C C   . LYS B 325 ? 0.7124 0.5022 0.9472 0.2310  -0.0587 0.0179  323 LYS B C   
6809 O O   . LYS B 325 ? 0.7640 0.4983 0.9748 0.2425  -0.0479 0.0133  323 LYS B O   
6810 C CB  . LYS B 325 ? 0.5894 0.5160 0.9241 0.2519  -0.0441 -0.0118 323 LYS B CB  
6811 C CG  . LYS B 325 ? 0.7224 0.7331 1.1163 0.2688  -0.0487 -0.0174 323 LYS B CG  
6812 C CD  . LYS B 325 ? 0.8294 0.8774 1.2530 0.2681  -0.0154 -0.0428 323 LYS B CD  
6813 C CE  . LYS B 325 ? 0.7237 0.8551 1.2083 0.2851  -0.0147 -0.0478 323 LYS B CE  
6814 N NZ  . LYS B 325 ? 0.7311 0.8893 1.2348 0.2862  0.0215  -0.0714 323 LYS B NZ  
6815 N N   . TYR B 326 ? 0.6802 0.4669 0.8857 0.1953  -0.0557 0.0258  324 TYR B N   
6816 C CA  . TYR B 326 ? 0.7245 0.4565 0.8839 0.1662  -0.0388 0.0266  324 TYR B CA  
6817 C C   . TYR B 326 ? 0.8025 0.5011 0.9112 0.1415  -0.0458 0.0501  324 TYR B C   
6818 O O   . TYR B 326 ? 0.7893 0.4319 0.8596 0.1213  -0.0362 0.0558  324 TYR B O   
6819 C CB  . TYR B 326 ? 0.6012 0.3744 0.7755 0.1397  -0.0158 0.0073  324 TYR B CB  
6820 C CG  . TYR B 326 ? 0.6900 0.4834 0.8983 0.1558  -0.0003 -0.0176 324 TYR B CG  
6821 C CD1 . TYR B 326 ? 0.7343 0.4712 0.9224 0.1602  0.0126  -0.0305 324 TYR B CD1 
6822 C CD2 . TYR B 326 ? 0.6369 0.5032 0.8927 0.1634  0.0038  -0.0292 324 TYR B CD2 
6823 C CE1 . TYR B 326 ? 0.7564 0.5087 0.9682 0.1754  0.0311  -0.0557 324 TYR B CE1 
6824 C CE2 . TYR B 326 ? 0.6240 0.5117 0.9083 0.1760  0.0235  -0.0523 324 TYR B CE2 
6825 C CZ  . TYR B 326 ? 0.6709 0.5015 0.9317 0.1836  0.0382  -0.0662 324 TYR B CZ  
6826 O OH  . TYR B 326 ? 0.6801 0.5302 0.9568 0.1947  0.0610  -0.0902 324 TYR B OH  
6827 N N   . LEU B 327 ? 0.7769 0.5059 0.8813 0.1402  -0.0608 0.0630  325 LEU B N   
6828 C CA  . LEU B 327 ? 0.7418 0.4461 0.7957 0.1151  -0.0607 0.0819  325 LEU B CA  
6829 C C   . LEU B 327 ? 0.8132 0.4746 0.8283 0.1319  -0.0867 0.1059  325 LEU B C   
6830 O O   . LEU B 327 ? 0.9042 0.5843 0.9440 0.1623  -0.1110 0.1072  325 LEU B O   
6831 C CB  . LEU B 327 ? 0.6595 0.4239 0.7241 0.0965  -0.0542 0.0757  325 LEU B CB  
6832 C CG  . LEU B 327 ? 0.6866 0.4887 0.7796 0.0779  -0.0317 0.0567  325 LEU B CG  
6833 C CD1 . LEU B 327 ? 0.6120 0.4579 0.7063 0.0631  -0.0276 0.0538  325 LEU B CD1 
6834 C CD2 . LEU B 327 ? 0.6301 0.3955 0.7037 0.0562  -0.0144 0.0576  325 LEU B CD2 
6835 N N   . PRO B 328 ? 0.8607 0.4667 0.8147 0.1116  -0.0829 0.1261  326 PRO B N   
6836 C CA  . PRO B 328 ? 0.9073 0.4640 0.8097 0.1245  -0.1088 0.1521  326 PRO B CA  
6837 C C   . PRO B 328 ? 0.8806 0.4842 0.7812 0.1293  -0.1284 0.1548  326 PRO B C   
6838 O O   . PRO B 328 ? 0.8473 0.4881 0.7422 0.1058  -0.1131 0.1478  326 PRO B O   
6839 C CB  . PRO B 328 ? 0.9348 0.4308 0.7708 0.0901  -0.0900 0.1704  326 PRO B CB  
6840 C CG  . PRO B 328 ? 0.9867 0.4888 0.8509 0.0684  -0.0613 0.1534  326 PRO B CG  
6841 C CD  . PRO B 328 ? 0.8455 0.4326 0.7737 0.0740  -0.0551 0.1277  326 PRO B CD  
6842 N N   . ILE B 329 ? 1.0070 0.6057 0.9113 0.1609  -0.1645 0.1650  327 ILE B N   
6843 C CA  . ILE B 329 ? 0.9774 0.6218 0.8831 0.1651  -0.1901 0.1661  327 ILE B CA  
6844 C C   . ILE B 329 ? 0.9159 0.5234 0.7365 0.1391  -0.1894 0.1835  327 ILE B C   
6845 O O   . ILE B 329 ? 0.8752 0.5195 0.6862 0.1279  -0.1956 0.1771  327 ILE B O   
6846 C CB  . ILE B 329 ? 0.9024 0.5639 0.8398 0.2016  -0.2261 0.1714  327 ILE B CB  
6847 C CG1 . ILE B 329 ? 0.8838 0.6089 0.8430 0.2037  -0.2553 0.1666  327 ILE B CG1 
6848 C CG2 . ILE B 329 ? 0.9291 0.5231 0.8051 0.2074  -0.2369 0.1962  327 ILE B CG2 
6849 C CD1 . ILE B 329 ? 0.8871 0.6612 0.9038 0.2346  -0.2808 0.1647  327 ILE B CD1 
6850 N N   . ASP B 330 ? 1.0338 0.5659 0.7880 0.1262  -0.1784 0.2043  328 ASP B N   
6851 C CA  . ASP B 330 ? 1.0132 0.5064 0.6794 0.1011  -0.1734 0.2221  328 ASP B CA  
6852 C C   . ASP B 330 ? 1.0292 0.5572 0.6946 0.0679  -0.1310 0.2064  328 ASP B C   
6853 O O   . ASP B 330 ? 1.0762 0.5876 0.6763 0.0480  -0.1206 0.2141  328 ASP B O   
6854 C CB  . ASP B 330 ? 1.0606 0.4848 0.6719 0.0914  -0.1650 0.2435  328 ASP B CB  
6855 C CG  . ASP B 330 ? 1.3145 0.7215 0.9279 0.1215  -0.2001 0.2550  328 ASP B CG  
6856 O OD1 . ASP B 330 ? 1.4268 0.8815 1.0856 0.1487  -0.2307 0.2470  328 ASP B OD1 
6857 O OD2 . ASP B 330 ? 1.4926 0.8408 1.0645 0.1170  -0.1970 0.2723  328 ASP B OD2 
6858 N N   . LYS B 331 ? 0.8311 0.4053 0.5653 0.0634  -0.1067 0.1845  329 LYS B N   
6859 C CA  . LYS B 331 ? 0.8412 0.4528 0.5876 0.0376  -0.0692 0.1696  329 LYS B CA  
6860 C C   . LYS B 331 ? 0.7656 0.4456 0.5630 0.0443  -0.0720 0.1453  329 LYS B C   
6861 O O   . LYS B 331 ? 0.7834 0.4983 0.6014 0.0298  -0.0450 0.1307  329 LYS B O   
6862 C CB  . LYS B 331 ? 0.8253 0.4309 0.6029 0.0237  -0.0431 0.1657  329 LYS B CB  
6863 C CG  . LYS B 331 ? 1.0003 0.5365 0.7166 0.0030  -0.0310 0.1897  329 LYS B CG  
6864 C CD  . LYS B 331 ? 1.0263 0.5383 0.7687 -0.0075 -0.0187 0.1880  329 LYS B CD  
6865 C CE  . LYS B 331 ? 1.0005 0.5758 0.8050 -0.0227 0.0059  0.1648  329 LYS B CE  
6866 N NZ  . LYS B 331 ? 1.1107 0.6555 0.9301 -0.0375 0.0144  0.1629  329 LYS B NZ  
6867 N N   . CYS B 332 ? 0.7472 0.4466 0.5659 0.0656  -0.1056 0.1420  330 CYS B N   
6868 C CA  . CYS B 332 ? 0.7882 0.5472 0.6532 0.0689  -0.1125 0.1210  330 CYS B CA  
6869 C C   . CYS B 332 ? 0.7904 0.5466 0.6097 0.0675  -0.1378 0.1243  330 CYS B C   
6870 O O   . CYS B 332 ? 0.8263 0.5430 0.5945 0.0742  -0.1631 0.1434  330 CYS B O   
6871 C CB  . CYS B 332 ? 0.6877 0.4826 0.6252 0.0906  -0.1294 0.1118  330 CYS B CB  
6872 S SG  . CYS B 332 ? 0.7446 0.5355 0.7277 0.0937  -0.1037 0.1041  330 CYS B SG  
6873 N N   . SER B 333 ? 0.7517 0.5438 0.5837 0.0577  -0.1333 0.1057  331 SER B N   
6874 C CA  . SER B 333 ? 0.8198 0.6085 0.6086 0.0528  -0.1595 0.1042  331 SER B CA  
6875 C C   . SER B 333 ? 0.7483 0.5866 0.5849 0.0468  -0.1642 0.0819  331 SER B C   
6876 O O   . SER B 333 ? 0.7666 0.6220 0.6294 0.0389  -0.1349 0.0673  331 SER B O   
6877 C CB  . SER B 333 ? 0.9344 0.6785 0.6358 0.0367  -0.1396 0.1079  331 SER B CB  
6878 O OG  . SER B 333 ? 0.9064 0.6407 0.5572 0.0297  -0.1644 0.1025  331 SER B OG  
6879 N N   . ARG B 334 ? 0.7883 0.6487 0.6358 0.0491  -0.2031 0.0806  332 ARG B N   
6880 C CA  . ARG B 334 ? 0.6979 0.6003 0.5822 0.0366  -0.2117 0.0613  332 ARG B CA  
6881 C C   . ARG B 334 ? 0.8069 0.6762 0.6146 0.0177  -0.2205 0.0541  332 ARG B C   
6882 O O   . ARG B 334 ? 0.8248 0.6676 0.5760 0.0172  -0.2507 0.0648  332 ARG B O   
6883 C CB  . ARG B 334 ? 0.6748 0.6308 0.6258 0.0466  -0.2486 0.0624  332 ARG B CB  
6884 C CG  . ARG B 334 ? 0.7042 0.7088 0.6988 0.0273  -0.2569 0.0437  332 ARG B CG  
6885 C CD  . ARG B 334 ? 0.6507 0.6898 0.7115 0.0264  -0.2236 0.0317  332 ARG B CD  
6886 N NE  . ARG B 334 ? 0.6603 0.7511 0.7722 0.0078  -0.2320 0.0175  332 ARG B NE  
6887 C CZ  . ARG B 334 ? 0.7269 0.8050 0.8075 -0.0197 -0.2345 0.0055  332 ARG B CZ  
6888 N NH1 . ARG B 334 ? 0.7563 0.7731 0.7571 -0.0275 -0.2250 0.0030  332 ARG B NH1 
6889 N NH2 . ARG B 334 ? 0.6430 0.7687 0.7729 -0.0404 -0.2433 -0.0052 332 ARG B NH2 
6890 N N   . ILE B 335 ? 0.7621 0.6267 0.5619 0.0034  -0.1955 0.0359  333 ILE B N   
6891 C CA  . ILE B 335 ? 0.8270 0.6524 0.5513 -0.0133 -0.1996 0.0241  333 ILE B CA  
6892 C C   . ILE B 335 ? 0.7963 0.6489 0.5436 -0.0309 -0.2331 0.0115  333 ILE B C   
6893 O O   . ILE B 335 ? 0.7923 0.6849 0.6069 -0.0368 -0.2272 0.0022  333 ILE B O   
6894 C CB  . ILE B 335 ? 0.7791 0.5779 0.4794 -0.0155 -0.1550 0.0107  333 ILE B CB  
6895 C CG1 . ILE B 335 ? 0.8400 0.6229 0.5258 -0.0029 -0.1218 0.0234  333 ILE B CG1 
6896 C CG2 . ILE B 335 ? 0.8714 0.6224 0.4900 -0.0294 -0.1572 -0.0051 333 ILE B CG2 
6897 C CD1 . ILE B 335 ? 0.9652 0.7245 0.6197 -0.0026 -0.0803 0.0112  333 ILE B CD1 
6898 N N   . ILE B 336 ? 0.8483 0.6780 0.5359 -0.0427 -0.2686 0.0117  334 ILE B N   
6899 C CA  . ILE B 336 ? 0.9567 0.8145 0.6639 -0.0648 -0.3075 0.0010  334 ILE B CA  
6900 C C   . ILE B 336 ? 1.0143 0.8109 0.6227 -0.0879 -0.3171 -0.0146 334 ILE B C   
6901 O O   . ILE B 336 ? 1.1342 0.8817 0.6553 -0.0856 -0.3259 -0.0084 334 ILE B O   
6902 C CB  . ILE B 336 ? 0.9212 0.8269 0.6702 -0.0569 -0.3564 0.0173  334 ILE B CB  
6903 C CG1 . ILE B 336 ? 0.8995 0.8621 0.7478 -0.0321 -0.3435 0.0279  334 ILE B CG1 
6904 C CG2 . ILE B 336 ? 1.0039 0.9461 0.7748 -0.0847 -0.3994 0.0061  334 ILE B CG2 
6905 C CD1 . ILE B 336 ? 0.8980 0.9080 0.8247 -0.0430 -0.3205 0.0128  334 ILE B CD1 
6906 N N   . PRO B 337 ? 1.0548 0.8448 0.6653 -0.1116 -0.3150 -0.0353 335 PRO B N   
6907 C CA  . PRO B 337 ? 1.1570 0.8814 0.6688 -0.1355 -0.3283 -0.0532 335 PRO B CA  
6908 C C   . PRO B 337 ? 1.1772 0.9230 0.6810 -0.1494 -0.3767 -0.0469 335 PRO B C   
6909 O O   . PRO B 337 ? 1.2464 1.0578 0.8292 -0.1624 -0.4021 -0.0459 335 PRO B O   
6910 C CB  . PRO B 337 ? 1.1171 0.8363 0.6546 -0.1566 -0.3148 -0.0733 335 PRO B CB  
6911 C CG  . PRO B 337 ? 1.0751 0.8803 0.7320 -0.1561 -0.3200 -0.0631 335 PRO B CG  
6912 C CD  . PRO B 337 ? 0.9063 0.7406 0.6015 -0.1202 -0.3006 -0.0431 335 PRO B CD  
6913 N N   . ALA B 338 ? 1.3409 1.0382 0.7581 -0.1445 -0.3813 -0.0421 336 ALA B N   
6914 C CA  . ALA B 338 ? 1.3025 1.0198 0.7125 -0.1524 -0.4236 -0.0333 336 ALA B CA  
6915 C C   . ALA B 338 ? 1.2511 0.9539 0.6382 -0.1840 -0.4380 -0.0536 336 ALA B C   
6916 O O   . ALA B 338 ? 1.4467 1.1729 0.8349 -0.1959 -0.4765 -0.0501 336 ALA B O   
6917 C CB  . ALA B 338 ? 1.4037 1.0692 0.7239 -0.1384 -0.4224 -0.0195 336 ALA B CB  
6918 N N   . VAL B 342 ? 1.0006 1.2806 1.1607 0.0024  -0.3964 -0.0899 340 VAL B N   
6919 C CA  . VAL B 342 ? 0.8385 1.1582 1.0664 0.0202  -0.3821 -0.0839 340 VAL B CA  
6920 C C   . VAL B 342 ? 0.8748 1.1702 1.0835 0.0498  -0.3857 -0.0699 340 VAL B C   
6921 O O   . VAL B 342 ? 0.9626 1.2060 1.1092 0.0552  -0.3843 -0.0669 340 VAL B O   
6922 C CB  . VAL B 342 ? 0.8488 1.1743 1.1048 0.0118  -0.3477 -0.0930 340 VAL B CB  
6923 C CG1 . VAL B 342 ? 0.8936 1.2421 1.1997 0.0332  -0.3285 -0.0868 340 VAL B CG1 
6924 C CG2 . VAL B 342 ? 0.7776 1.1333 1.0642 -0.0161 -0.3434 -0.1045 340 VAL B CG2 
6925 N N   . GLU B 343 ? 0.8234 1.1540 1.0836 0.0688  -0.3889 -0.0612 341 GLU B N   
6926 C CA  . GLU B 343 ? 0.7653 1.0721 1.0102 0.0971  -0.3912 -0.0475 341 GLU B CA  
6927 C C   . GLU B 343 ? 0.7792 1.0708 1.0324 0.1068  -0.3589 -0.0488 341 GLU B C   
6928 O O   . GLU B 343 ? 0.8439 1.1650 1.1447 0.1000  -0.3356 -0.0569 341 GLU B O   
6929 C CB  . GLU B 343 ? 0.7231 1.0714 1.0192 0.1146  -0.4068 -0.0379 341 GLU B CB  
6930 C CG  . GLU B 343 ? 0.7509 1.1121 1.0340 0.1080  -0.4434 -0.0344 341 GLU B CG  
6931 C CD  . GLU B 343 ? 0.8139 1.2348 1.1671 0.1191  -0.4571 -0.0287 341 GLU B CD  
6932 O OE1 . GLU B 343 ? 0.8950 1.3447 1.3053 0.1322  -0.4356 -0.0278 341 GLU B OE1 
6933 O OE2 . GLU B 343 ? 0.8952 1.3344 1.2457 0.1147  -0.4891 -0.0254 341 GLU B OE2 
6934 N N   . CYS B 344 ? 0.7229 0.9662 0.9264 0.1217  -0.3572 -0.0405 342 CYS B N   
6935 C CA  . CYS B 344 ? 0.6978 0.9225 0.9017 0.1300  -0.3290 -0.0413 342 CYS B CA  
6936 C C   . CYS B 344 ? 0.6365 0.8391 0.8327 0.1568  -0.3288 -0.0276 342 CYS B C   
6937 O O   . CYS B 344 ? 0.7142 0.9253 0.9198 0.1710  -0.3473 -0.0177 342 CYS B O   
6938 C CB  . CYS B 344 ? 0.7859 0.9676 0.9314 0.1179  -0.3221 -0.0464 342 CYS B CB  
6939 S SG  . CYS B 344 ? 1.1768 1.2923 1.2323 0.1284  -0.3411 -0.0329 342 CYS B SG  
6940 N N   . PHE B 345 ? 0.7480 0.9207 0.9265 0.1635  -0.3075 -0.0266 343 PHE B N   
6941 C CA  . PHE B 345 ? 0.6944 0.8365 0.8579 0.1865  -0.3031 -0.0142 343 PHE B CA  
6942 C C   . PHE B 345 ? 0.7539 0.8485 0.8492 0.1935  -0.3260 -0.0013 343 PHE B C   
6943 O O   . PHE B 345 ? 0.8664 0.9282 0.9058 0.1814  -0.3306 -0.0025 343 PHE B O   
6944 C CB  . PHE B 345 ? 0.6937 0.8132 0.8493 0.1867  -0.2753 -0.0175 343 PHE B CB  
6945 C CG  . PHE B 345 ? 0.7435 0.8305 0.8880 0.2073  -0.2650 -0.0070 343 PHE B CG  
6946 C CD1 . PHE B 345 ? 0.7355 0.8455 0.9301 0.2176  -0.2486 -0.0092 343 PHE B CD1 
6947 C CD2 . PHE B 345 ? 0.7383 0.7665 0.8172 0.2124  -0.2651 0.0047  343 PHE B CD2 
6948 C CE1 . PHE B 345 ? 0.7141 0.7891 0.8951 0.2352  -0.2377 -0.0008 343 PHE B CE1 
6949 C CE2 . PHE B 345 ? 0.8051 0.7986 0.8711 0.2286  -0.2535 0.0140  343 PHE B CE2 
6950 C CZ  . PHE B 345 ? 0.7492 0.7657 0.8669 0.2413  -0.2417 0.0107  343 PHE B CZ  
6951 N N   . ASP B 346 ? 0.6911 0.7779 0.7866 0.2129  -0.3388 0.0114  344 ASP B N   
6952 C CA  . ASP B 346 ? 0.7365 0.7788 0.7665 0.2184  -0.3618 0.0244  344 ASP B CA  
6953 C C   . ASP B 346 ? 0.7987 0.7914 0.7945 0.2390  -0.3552 0.0393  344 ASP B C   
6954 O O   . ASP B 346 ? 0.9572 0.9221 0.9164 0.2496  -0.3745 0.0524  344 ASP B O   
6955 C CB  . ASP B 346 ? 0.8199 0.8964 0.8717 0.2195  -0.3919 0.0273  344 ASP B CB  
6956 C CG  . ASP B 346 ? 0.8818 1.0107 1.0122 0.2347  -0.3909 0.0285  344 ASP B CG  
6957 O OD1 . ASP B 346 ? 0.9375 1.0721 1.1012 0.2439  -0.3654 0.0263  344 ASP B OD1 
6958 O OD2 . ASP B 346 ? 0.8564 1.0198 1.0138 0.2375  -0.4152 0.0319  344 ASP B OD2 
6959 N N   . LYS B 347 ? 0.8195 0.7982 0.8246 0.2439  -0.3279 0.0376  345 LYS B N   
6960 C CA  . LYS B 347 ? 0.8756 0.8062 0.8516 0.2615  -0.3183 0.0508  345 LYS B CA  
6961 C C   . LYS B 347 ? 0.9116 0.7780 0.8161 0.2544  -0.3027 0.0561  345 LYS B C   
6962 O O   . LYS B 347 ? 0.9997 0.8160 0.8673 0.2650  -0.2939 0.0681  345 LYS B O   
6963 C CB  . LYS B 347 ? 0.8756 0.8318 0.9131 0.2736  -0.2976 0.0465  345 LYS B CB  
6964 C CG  . LYS B 347 ? 0.8358 0.8524 0.9427 0.2823  -0.3094 0.0438  345 LYS B CG  
6965 C CD  . LYS B 347 ? 0.8244 0.8568 0.9825 0.2969  -0.2872 0.0416  345 LYS B CD  
6966 C CE  . LYS B 347 ? 0.6753 0.7620 0.8968 0.3092  -0.2991 0.0429  345 LYS B CE  
6967 N NZ  . LYS B 347 ? 0.7223 0.8126 0.9832 0.3283  -0.2777 0.0440  345 LYS B NZ  
6968 N N   . PHE B 348 ? 0.8114 0.6764 0.6944 0.2358  -0.2974 0.0481  346 PHE B N   
6969 C CA  . PHE B 348 ? 0.8381 0.6507 0.6576 0.2184  -0.2710 0.0519  346 PHE B CA  
6970 C C   . PHE B 348 ? 0.9451 0.7250 0.6964 0.2108  -0.2896 0.0572  346 PHE B C   
6971 O O   . PHE B 348 ? 0.9752 0.7823 0.7348 0.2112  -0.3200 0.0531  346 PHE B O   
6972 C CB  . PHE B 348 ? 0.8176 0.6541 0.6636 0.1949  -0.2384 0.0378  346 PHE B CB  
6973 C CG  . PHE B 348 ? 0.7025 0.5616 0.6019 0.1974  -0.2166 0.0321  346 PHE B CG  
6974 C CD1 . PHE B 348 ? 0.7212 0.5539 0.6193 0.2142  -0.2119 0.0408  346 PHE B CD1 
6975 C CD2 . PHE B 348 ? 0.7148 0.6153 0.6591 0.1819  -0.1998 0.0180  346 PHE B CD2 
6976 C CE1 . PHE B 348 ? 0.7550 0.6032 0.6953 0.2146  -0.1909 0.0340  346 PHE B CE1 
6977 C CE2 . PHE B 348 ? 0.6522 0.5685 0.6372 0.1825  -0.1803 0.0124  346 PHE B CE2 
6978 C CZ  . PHE B 348 ? 0.6265 0.5167 0.6089 0.1983  -0.1757 0.0198  346 PHE B CZ  
6979 N N   . LYS B 349 ? 0.9760 0.6954 0.6576 0.2024  -0.2706 0.0659  347 LYS B N   
6980 C CA  . LYS B 349 ? 1.0466 0.7289 0.6558 0.1914  -0.2803 0.0689  347 LYS B CA  
6981 C C   . LYS B 349 ? 0.9084 0.6260 0.5374 0.1697  -0.2713 0.0519  347 LYS B C   
6982 O O   . LYS B 349 ? 1.0054 0.7532 0.6807 0.1588  -0.2437 0.0414  347 LYS B O   
6983 C CB  . LYS B 349 ? 1.1151 0.7267 0.6501 0.1843  -0.2532 0.0803  347 LYS B CB  
6984 C CG  . LYS B 349 ? 1.0907 0.7054 0.6500 0.1691  -0.2083 0.0745  347 LYS B CG  
6985 C CD  . LYS B 349 ? 1.2857 0.8324 0.7800 0.1642  -0.1835 0.0877  347 LYS B CD  
6986 C CE  . LYS B 349 ? 1.2624 0.7550 0.6683 0.1578  -0.1890 0.0947  347 LYS B CE  
6987 N NZ  . LYS B 349 ? 1.3651 0.7923 0.7085 0.1484  -0.1570 0.1060  347 LYS B NZ  
6988 N N   . VAL B 350 ? 0.9497 0.6601 0.5404 0.1634  -0.2958 0.0491  348 VAL B N   
6989 C CA  . VAL B 350 ? 0.9569 0.6976 0.5640 0.1439  -0.2921 0.0325  348 VAL B CA  
6990 C C   . VAL B 350 ? 0.9534 0.6449 0.4924 0.1256  -0.2634 0.0303  348 VAL B C   
6991 O O   . VAL B 350 ? 1.0704 0.7033 0.5293 0.1258  -0.2674 0.0402  348 VAL B O   
6992 C CB  . VAL B 350 ? 0.9854 0.7526 0.5983 0.1456  -0.3373 0.0281  348 VAL B CB  
6993 C CG1 . VAL B 350 ? 1.0443 0.8194 0.6453 0.1221  -0.3328 0.0121  348 VAL B CG1 
6994 C CG2 . VAL B 350 ? 0.9899 0.8224 0.6922 0.1604  -0.3575 0.0255  348 VAL B CG2 
6995 N N   . ASN B 351 ? 0.9261 0.6397 0.4961 0.1105  -0.2331 0.0178  349 ASN B N   
6996 C CA  . ASN B 351 ? 1.0489 0.7261 0.5676 0.0935  -0.2049 0.0123  349 ASN B CA  
6997 C C   . ASN B 351 ? 1.1148 0.7376 0.5815 0.0931  -0.1742 0.0239  349 ASN B C   
6998 O O   . ASN B 351 ? 1.1490 0.7179 0.5389 0.0860  -0.1657 0.0268  349 ASN B O   
6999 C CB  . ASN B 351 ? 1.1252 0.7798 0.5870 0.0847  -0.2291 0.0061  349 ASN B CB  
7000 C CG  . ASN B 351 ? 0.9862 0.6953 0.5018 0.0796  -0.2548 -0.0075 349 ASN B CG  
7001 O OD1 . ASN B 351 ? 0.9426 0.7052 0.5365 0.0820  -0.2498 -0.0128 349 ASN B OD1 
7002 N ND2 . ASN B 351 ? 0.9687 0.6619 0.4393 0.0705  -0.2815 -0.0135 349 ASN B ND2 
7003 N N   . SER B 352 ? 1.0303 0.6651 0.5373 0.0992  -0.1564 0.0302  350 SER B N   
7004 C CA  . SER B 352 ? 1.0867 0.6784 0.5594 0.0950  -0.1224 0.0396  350 SER B CA  
7005 C C   . SER B 352 ? 1.0512 0.6779 0.5830 0.0847  -0.0881 0.0312  350 SER B C   
7006 O O   . SER B 352 ? 1.0844 0.7394 0.6703 0.0885  -0.0826 0.0325  350 SER B O   
7007 C CB  . SER B 352 ? 1.1249 0.6941 0.5884 0.1092  -0.1323 0.0548  350 SER B CB  
7008 O OG  . SER B 352 ? 1.2474 0.7698 0.6716 0.1019  -0.0991 0.0640  350 SER B OG  
7009 N N   . THR B 353 ? 0.9652 0.5873 0.4840 0.0721  -0.0656 0.0224  351 THR B N   
7010 C CA  . THR B 353 ? 0.9513 0.6092 0.5277 0.0639  -0.0372 0.0144  351 THR B CA  
7011 C C   . THR B 353 ? 0.9814 0.6309 0.5719 0.0598  -0.0068 0.0224  351 THR B C   
7012 O O   . THR B 353 ? 0.9520 0.6386 0.6015 0.0552  0.0092  0.0179  351 THR B O   
7013 C CB  . THR B 353 ? 1.0353 0.6832 0.5894 0.0540  -0.0192 0.0042  351 THR B CB  
7014 O OG1 . THR B 353 ? 1.0673 0.7193 0.6041 0.0546  -0.0491 -0.0039 351 THR B OG1 
7015 C CG2 . THR B 353 ? 1.0347 0.7234 0.6535 0.0487  0.0047  -0.0035 351 THR B CG2 
7016 N N   . LEU B 354 ? 1.0789 0.6795 0.6160 0.0602  0.0006  0.0343  352 LEU B N   
7017 C CA  . LEU B 354 ? 1.1285 0.7183 0.6767 0.0524  0.0319  0.0413  352 LEU B CA  
7018 C C   . LEU B 354 ? 1.0674 0.6674 0.6471 0.0589  0.0196  0.0481  352 LEU B C   
7019 O O   . LEU B 354 ? 1.0683 0.6550 0.6537 0.0510  0.0420  0.0543  352 LEU B O   
7020 C CB  . LEU B 354 ? 1.1352 0.6610 0.6060 0.0459  0.0543  0.0504  352 LEU B CB  
7021 C CG  . LEU B 354 ? 1.2594 0.7731 0.7081 0.0354  0.0854  0.0432  352 LEU B CG  
7022 C CD1 . LEU B 354 ? 1.0527 0.6233 0.5816 0.0301  0.1043  0.0333  352 LEU B CD1 
7023 C CD2 . LEU B 354 ? 1.2307 0.7221 0.6245 0.0391  0.0656  0.0370  352 LEU B CD2 
7024 N N   . GLU B 355 ? 1.0202 0.6427 0.6211 0.0724  -0.0140 0.0463  353 GLU B N   
7025 C CA  . GLU B 355 ? 1.0210 0.6528 0.6534 0.0804  -0.0241 0.0509  353 GLU B CA  
7026 C C   . GLU B 355 ? 0.8572 0.5341 0.5582 0.0712  -0.0081 0.0430  353 GLU B C   
7027 O O   . GLU B 355 ? 0.8731 0.5866 0.6083 0.0650  -0.0024 0.0331  353 GLU B O   
7028 C CB  . GLU B 355 ? 0.9916 0.6393 0.6335 0.0986  -0.0620 0.0503  353 GLU B CB  
7029 C CG  . GLU B 355 ? 1.0450 0.6444 0.6186 0.1100  -0.0834 0.0615  353 GLU B CG  
7030 C CD  . GLU B 355 ? 1.1671 0.7129 0.6999 0.1146  -0.0759 0.0765  353 GLU B CD  
7031 O OE1 . GLU B 355 ? 1.1814 0.7302 0.7438 0.1092  -0.0563 0.0773  353 GLU B OE1 
7032 O OE2 . GLU B 355 ? 1.2385 0.7353 0.7053 0.1225  -0.0901 0.0878  353 GLU B OE2 
7033 N N   . GLN B 356 ? 0.7957 0.4659 0.5130 0.0700  -0.0018 0.0477  354 GLN B N   
7034 C CA  . GLN B 356 ? 0.7681 0.4761 0.5439 0.0595  0.0110  0.0408  354 GLN B CA  
7035 C C   . GLN B 356 ? 0.7033 0.4611 0.5283 0.0662  -0.0073 0.0299  354 GLN B C   
7036 O O   . GLN B 356 ? 0.6817 0.4753 0.5479 0.0570  0.0015  0.0224  354 GLN B O   
7037 C CB  . GLN B 356 ? 0.7606 0.4461 0.5376 0.0564  0.0176  0.0468  354 GLN B CB  
7038 C CG  . GLN B 356 ? 0.7502 0.4696 0.5814 0.0432  0.0280  0.0399  354 GLN B CG  
7039 C CD  . GLN B 356 ? 0.7259 0.4143 0.5493 0.0347  0.0382  0.0453  354 GLN B CD  
7040 O OE1 . GLN B 356 ? 0.8288 0.4677 0.6060 0.0390  0.0402  0.0551  354 GLN B OE1 
7041 N NE2 . GLN B 356 ? 0.7240 0.4379 0.5891 0.0217  0.0440  0.0392  354 GLN B NE2 
7042 N N   . TYR B 357 ? 0.6919 0.4525 0.5143 0.0823  -0.0324 0.0296  355 TYR B N   
7043 C CA  . TYR B 357 ? 0.6475 0.4536 0.5164 0.0883  -0.0480 0.0195  355 TYR B CA  
7044 C C   . TYR B 357 ? 0.6515 0.4685 0.5084 0.0947  -0.0670 0.0159  355 TYR B C   
7045 O O   . TYR B 357 ? 0.6811 0.4824 0.5137 0.1080  -0.0877 0.0210  355 TYR B O   
7046 C CB  . TYR B 357 ? 0.6269 0.4324 0.5129 0.1007  -0.0587 0.0207  355 TYR B CB  
7047 C CG  . TYR B 357 ? 0.6138 0.4028 0.5056 0.0912  -0.0403 0.0229  355 TYR B CG  
7048 C CD1 . TYR B 357 ? 0.6070 0.4164 0.5248 0.0734  -0.0233 0.0178  355 TYR B CD1 
7049 C CD2 . TYR B 357 ? 0.7273 0.4776 0.5962 0.0994  -0.0407 0.0307  355 TYR B CD2 
7050 C CE1 . TYR B 357 ? 0.6565 0.4524 0.5800 0.0619  -0.0094 0.0192  355 TYR B CE1 
7051 C CE2 . TYR B 357 ? 0.7568 0.4883 0.6277 0.0875  -0.0240 0.0317  355 TYR B CE2 
7052 C CZ  . TYR B 357 ? 0.6427 0.3989 0.5417 0.0676  -0.0092 0.0256  355 TYR B CZ  
7053 O OH  . TYR B 357 ? 0.6647 0.4042 0.5666 0.0532  0.0044  0.0259  355 TYR B OH  
7054 N N   . VAL B 358 ? 0.6671 0.5094 0.5403 0.0853  -0.0614 0.0074  356 VAL B N   
7055 C CA  . VAL B 358 ? 0.6724 0.5238 0.5338 0.0870  -0.0776 0.0019  356 VAL B CA  
7056 C C   . VAL B 358 ? 0.5825 0.4808 0.4951 0.0874  -0.0887 -0.0088 356 VAL B C   
7057 O O   . VAL B 358 ? 0.5925 0.5137 0.5393 0.0792  -0.0749 -0.0143 356 VAL B O   
7058 C CB  . VAL B 358 ? 0.6932 0.5285 0.5258 0.0755  -0.0601 -0.0003 356 VAL B CB  
7059 C CG1 . VAL B 358 ? 0.7652 0.6153 0.5953 0.0732  -0.0742 -0.0099 356 VAL B CG1 
7060 C CG2 . VAL B 358 ? 0.8005 0.5846 0.5719 0.0754  -0.0513 0.0098  356 VAL B CG2 
7061 N N   . PHE B 359 ? 0.6235 0.5357 0.5411 0.0960  -0.1141 -0.0113 357 PHE B N   
7062 C CA  . PHE B 359 ? 0.6086 0.5653 0.5746 0.0955  -0.1244 -0.0214 357 PHE B CA  
7063 C C   . PHE B 359 ? 0.6595 0.6225 0.6115 0.0886  -0.1382 -0.0283 357 PHE B C   
7064 O O   . PHE B 359 ? 0.6409 0.5859 0.5582 0.0935  -0.1576 -0.0246 357 PHE B O   
7065 C CB  . PHE B 359 ? 0.5650 0.5393 0.5600 0.1110  -0.1412 -0.0197 357 PHE B CB  
7066 C CG  . PHE B 359 ? 0.5598 0.5209 0.5629 0.1176  -0.1277 -0.0142 357 PHE B CG  
7067 C CD1 . PHE B 359 ? 0.5731 0.4917 0.5361 0.1237  -0.1245 -0.0028 357 PHE B CD1 
7068 C CD2 . PHE B 359 ? 0.4934 0.4798 0.5391 0.1160  -0.1172 -0.0206 357 PHE B CD2 
7069 C CE1 . PHE B 359 ? 0.5890 0.4913 0.5568 0.1275  -0.1118 0.0014  357 PHE B CE1 
7070 C CE2 . PHE B 359 ? 0.5562 0.5258 0.6041 0.1202  -0.1051 -0.0169 357 PHE B CE2 
7071 C CZ  . PHE B 359 ? 0.4928 0.4206 0.5029 0.1256  -0.1027 -0.0061 357 PHE B CZ  
7072 N N   . CYS B 360 ? 0.5646 0.5488 0.5390 0.0766  -0.1290 -0.0380 358 CYS B N   
7073 C CA  . CYS B 360 ? 0.5856 0.5681 0.5407 0.0672  -0.1386 -0.0455 358 CYS B CA  
7074 C C   . CYS B 360 ? 0.5342 0.5466 0.5270 0.0561  -0.1317 -0.0563 358 CYS B C   
7075 O O   . CYS B 360 ? 0.5781 0.6016 0.5978 0.0539  -0.1135 -0.0566 358 CYS B O   
7076 C CB  . CYS B 360 ? 0.6996 0.6393 0.5996 0.0616  -0.1240 -0.0427 358 CYS B CB  
7077 S SG  . CYS B 360 ? 0.7390 0.6637 0.6028 0.0487  -0.1314 -0.0533 358 CYS B SG  
7078 N N   . THR B 361 ? 0.4956 0.5175 0.4862 0.0478  -0.1472 -0.0649 359 THR B N   
7079 C CA  . THR B 361 ? 0.5526 0.5946 0.5702 0.0349  -0.1398 -0.0751 359 THR B CA  
7080 C C   . THR B 361 ? 0.5312 0.5431 0.5175 0.0265  -0.1190 -0.0773 359 THR B C   
7081 O O   . THR B 361 ? 0.5923 0.5695 0.5339 0.0285  -0.1128 -0.0733 359 THR B O   
7082 C CB  . THR B 361 ? 0.5127 0.5760 0.5417 0.0263  -0.1636 -0.0843 359 THR B CB  
7083 O OG1 . THR B 361 ? 0.6156 0.6537 0.5975 0.0265  -0.1831 -0.0831 359 THR B OG1 
7084 C CG2 . THR B 361 ? 0.4475 0.5547 0.5306 0.0333  -0.1771 -0.0847 359 THR B CG2 
7085 N N   . VAL B 362 ? 0.4637 0.4871 0.4733 0.0177  -0.1066 -0.0834 360 VAL B N   
7086 C CA  . VAL B 362 ? 0.5294 0.5262 0.5171 0.0132  -0.0853 -0.0846 360 VAL B CA  
7087 C C   . VAL B 362 ? 0.6255 0.5896 0.5642 0.0063  -0.0896 -0.0908 360 VAL B C   
7088 O O   . VAL B 362 ? 0.7093 0.6404 0.6136 0.0084  -0.0724 -0.0888 360 VAL B O   
7089 C CB  . VAL B 362 ? 0.5267 0.5385 0.5455 0.0059  -0.0745 -0.0891 360 VAL B CB  
7090 C CG1 . VAL B 362 ? 0.5541 0.5366 0.5506 0.0033  -0.0550 -0.0905 360 VAL B CG1 
7091 C CG2 . VAL B 362 ? 0.4885 0.5237 0.5447 0.0121  -0.0681 -0.0826 360 VAL B CG2 
7092 N N   . ASN B 363 ? 0.5729 0.5453 0.5076 -0.0028 -0.1122 -0.0989 361 ASN B N   
7093 C CA  . ASN B 363 ? 0.7176 0.6556 0.6012 -0.0129 -0.1180 -0.1068 361 ASN B CA  
7094 C C   . ASN B 363 ? 0.7562 0.6622 0.5878 -0.0059 -0.1242 -0.1009 361 ASN B C   
7095 O O   . ASN B 363 ? 0.8358 0.6995 0.6126 -0.0117 -0.1177 -0.1056 361 ASN B O   
7096 C CB  . ASN B 363 ? 0.7816 0.7397 0.6774 -0.0276 -0.1433 -0.1175 361 ASN B CB  
7097 C CG  . ASN B 363 ? 0.9161 0.8808 0.8349 -0.0410 -0.1312 -0.1265 361 ASN B CG  
7098 O OD1 . ASN B 363 ? 0.9595 0.9619 0.9247 -0.0474 -0.1392 -0.1298 361 ASN B OD1 
7099 N ND2 . ASN B 363 ? 0.9573 0.8828 0.8427 -0.0447 -0.1098 -0.1301 361 ASN B ND2 
7100 N N   . ALA B 364 ? 0.7010 0.6212 0.5438 0.0062  -0.1355 -0.0909 362 ALA B N   
7101 C CA  . ALA B 364 ? 0.7131 0.5999 0.5032 0.0129  -0.1431 -0.0835 362 ALA B CA  
7102 C C   . ALA B 364 ? 0.7140 0.5785 0.4910 0.0223  -0.1146 -0.0734 362 ALA B C   
7103 O O   . ALA B 364 ? 0.7452 0.5793 0.4785 0.0280  -0.1162 -0.0655 362 ALA B O   
7104 C CB  . ALA B 364 ? 0.7358 0.6463 0.5414 0.0212  -0.1756 -0.0777 362 ALA B CB  
7105 N N   . LEU B 365 ? 0.6407 0.5196 0.4545 0.0232  -0.0896 -0.0730 363 LEU B N   
7106 C CA  . LEU B 365 ? 0.6839 0.5505 0.4971 0.0304  -0.0638 -0.0636 363 LEU B CA  
7107 C C   . LEU B 365 ? 0.7249 0.5429 0.4774 0.0286  -0.0454 -0.0630 363 LEU B C   
7108 O O   . LEU B 365 ? 0.7064 0.5027 0.4319 0.0215  -0.0375 -0.0722 363 LEU B O   
7109 C CB  . LEU B 365 ? 0.6417 0.5321 0.5032 0.0300  -0.0435 -0.0644 363 LEU B CB  
7110 C CG  . LEU B 365 ? 0.7050 0.6362 0.6222 0.0333  -0.0515 -0.0615 363 LEU B CG  
7111 C CD1 . LEU B 365 ? 0.5862 0.5325 0.5389 0.0316  -0.0330 -0.0619 363 LEU B CD1 
7112 C CD2 . LEU B 365 ? 0.7173 0.6486 0.6364 0.0416  -0.0539 -0.0512 363 LEU B CD2 
7113 N N   . PRO B 366 ? 0.8116 0.6076 0.5388 0.0340  -0.0355 -0.0530 364 PRO B N   
7114 C CA  . PRO B 366 ? 0.8517 0.6008 0.5232 0.0318  -0.0106 -0.0522 364 PRO B CA  
7115 C C   . PRO B 366 ? 0.8182 0.5753 0.5228 0.0331  0.0256  -0.0506 364 PRO B C   
7116 O O   . PRO B 366 ? 0.8078 0.6034 0.5723 0.0360  0.0282  -0.0475 364 PRO B O   
7117 C CB  . PRO B 366 ? 0.8501 0.5748 0.4846 0.0365  -0.0179 -0.0406 364 PRO B CB  
7118 C CG  . PRO B 366 ? 0.8630 0.6279 0.5577 0.0430  -0.0245 -0.0334 364 PRO B CG  
7119 C CD  . PRO B 366 ? 0.8252 0.6334 0.5693 0.0420  -0.0453 -0.0420 364 PRO B CD  
7120 N N   . GLU B 367 ? 0.7987 0.5183 0.4628 0.0311  0.0535  -0.0529 365 GLU B N   
7121 C CA  . GLU B 367 ? 0.8314 0.5590 0.5285 0.0339  0.0894  -0.0503 365 GLU B CA  
7122 C C   . GLU B 367 ? 0.9069 0.6332 0.6077 0.0350  0.1012  -0.0380 365 GLU B C   
7123 O O   . GLU B 367 ? 1.0059 0.6905 0.6491 0.0328  0.1106  -0.0341 365 GLU B O   
7124 C CB  . GLU B 367 ? 0.8629 0.5510 0.5187 0.0325  0.1186  -0.0580 365 GLU B CB  
7125 C CG  . GLU B 367 ? 0.9163 0.6207 0.6087 0.0351  0.1281  -0.0665 365 GLU B CG  
7126 C CD  . GLU B 367 ? 1.1321 0.7880 0.7699 0.0333  0.1492  -0.0774 365 GLU B CD  
7127 O OE1 . GLU B 367 ? 1.1883 0.8117 0.7933 0.0347  0.1811  -0.0761 365 GLU B OE1 
7128 O OE2 . GLU B 367 ? 1.1940 0.8420 0.8202 0.0294  0.1357  -0.0878 365 GLU B OE2 
7129 N N   . THR B 368 ? 0.8181 0.5856 0.5818 0.0370  0.1006  -0.0321 366 THR B N   
7130 C CA  . THR B 368 ? 0.7480 0.5151 0.5191 0.0356  0.1103  -0.0212 366 THR B CA  
7131 C C   . THR B 368 ? 0.7129 0.5249 0.5576 0.0353  0.1196  -0.0182 366 THR B C   
7132 O O   . THR B 368 ? 0.7041 0.5443 0.5895 0.0379  0.1187  -0.0233 366 THR B O   
7133 C CB  . THR B 368 ? 0.8042 0.5636 0.5531 0.0372  0.0806  -0.0157 366 THR B CB  
7134 O OG1 . THR B 368 ? 0.8383 0.5885 0.5872 0.0348  0.0925  -0.0051 366 THR B OG1 
7135 C CG2 . THR B 368 ? 0.7641 0.5653 0.5608 0.0406  0.0521  -0.0190 366 THR B CG2 
7136 N N   . THR B 369 ? 0.7045 0.5199 0.5629 0.0313  0.1278  -0.0093 367 THR B N   
7137 C CA  . THR B 369 ? 0.6410 0.4966 0.5648 0.0283  0.1331  -0.0057 367 THR B CA  
7138 C C   . THR B 369 ? 0.6614 0.5259 0.5947 0.0264  0.1100  -0.0011 367 THR B C   
7139 O O   . THR B 369 ? 0.6951 0.5336 0.5866 0.0291  0.0945  0.0010  367 THR B O   
7140 C CB  . THR B 369 ? 0.6769 0.5301 0.6149 0.0219  0.1677  -0.0004 367 THR B CB  
7141 O OG1 . THR B 369 ? 0.7407 0.5538 0.6283 0.0164  0.1768  0.0060  367 THR B OG1 
7142 C CG2 . THR B 369 ? 0.6807 0.5274 0.6163 0.0262  0.1942  -0.0057 367 THR B CG2 
7143 N N   . ALA B 370 ? 0.6027 0.5024 0.5902 0.0226  0.1070  0.0005  368 ALA B N   
7144 C CA  . ALA B 370 ? 0.6060 0.5108 0.6018 0.0202  0.0887  0.0037  368 ALA B CA  
7145 C C   . ALA B 370 ? 0.5574 0.4961 0.6086 0.0122  0.0918  0.0054  368 ALA B C   
7146 O O   . ALA B 370 ? 0.5009 0.4663 0.5895 0.0116  0.1004  0.0039  368 ALA B O   
7147 C CB  . ALA B 370 ? 0.5999 0.5110 0.5897 0.0283  0.0605  -0.0018 368 ALA B CB  
7148 N N   . ASP B 371 ? 0.5598 0.4948 0.6142 0.0061  0.0838  0.0088  369 ASP B N   
7149 C CA  . ASP B 371 ? 0.5647 0.5290 0.6662 -0.0038 0.0816  0.0096  369 ASP B CA  
7150 C C   . ASP B 371 ? 0.4862 0.4766 0.6113 0.0008  0.0603  0.0038  369 ASP B C   
7151 O O   . ASP B 371 ? 0.4958 0.5163 0.6608 -0.0031 0.0588  0.0034  369 ASP B O   
7152 C CB  . ASP B 371 ? 0.5172 0.4617 0.6078 -0.0140 0.0817  0.0140  369 ASP B CB  
7153 C CG  . ASP B 371 ? 0.6341 0.5482 0.6977 -0.0208 0.1051  0.0206  369 ASP B CG  
7154 O OD1 . ASP B 371 ? 0.7382 0.6669 0.8259 -0.0280 0.1264  0.0226  369 ASP B OD1 
7155 O OD2 . ASP B 371 ? 0.5934 0.4681 0.6120 -0.0186 0.1033  0.0244  369 ASP B OD2 
7156 N N   . ILE B 372 ? 0.4781 0.4574 0.5798 0.0091  0.0438  -0.0001 370 ILE B N   
7157 C CA  . ILE B 372 ? 0.4164 0.4161 0.5355 0.0125  0.0266  -0.0060 370 ILE B CA  
7158 C C   . ILE B 372 ? 0.4753 0.4694 0.5730 0.0234  0.0177  -0.0110 370 ILE B C   
7159 O O   . ILE B 372 ? 0.5168 0.4882 0.5824 0.0292  0.0148  -0.0101 370 ILE B O   
7160 C CB  . ILE B 372 ? 0.4523 0.4483 0.5731 0.0085  0.0154  -0.0071 370 ILE B CB  
7161 C CG1 . ILE B 372 ? 0.4667 0.4648 0.6049 -0.0058 0.0221  -0.0030 370 ILE B CG1 
7162 C CG2 . ILE B 372 ? 0.4750 0.4899 0.6108 0.0109  0.0018  -0.0135 370 ILE B CG2 
7163 C CD1 . ILE B 372 ? 0.4162 0.3993 0.5455 -0.0109 0.0138  -0.0048 370 ILE B CD1 
7164 N N   . VAL B 373 ? 0.4549 0.4684 0.5695 0.0253  0.0121  -0.0160 371 VAL B N   
7165 C CA  . VAL B 373 ? 0.3934 0.4063 0.4945 0.0320  0.0018  -0.0223 371 VAL B CA  
7166 C C   . VAL B 373 ? 0.3990 0.4285 0.5180 0.0311  -0.0108 -0.0270 371 VAL B C   
7167 O O   . VAL B 373 ? 0.3885 0.4328 0.5294 0.0261  -0.0105 -0.0271 371 VAL B O   
7168 C CB  . VAL B 373 ? 0.4493 0.4636 0.5488 0.0334  0.0091  -0.0251 371 VAL B CB  
7169 C CG1 . VAL B 373 ? 0.3491 0.3654 0.4390 0.0361  -0.0034 -0.0327 371 VAL B CG1 
7170 C CG2 . VAL B 373 ? 0.4118 0.4040 0.4858 0.0347  0.0243  -0.0219 371 VAL B CG2 
7171 N N   . VAL B 374 ? 0.4139 0.4404 0.5235 0.0364  -0.0215 -0.0305 372 VAL B N   
7172 C CA  . VAL B 374 ? 0.4055 0.4465 0.5308 0.0363  -0.0297 -0.0362 372 VAL B CA  
7173 C C   . VAL B 374 ? 0.4601 0.5115 0.5862 0.0383  -0.0365 -0.0428 372 VAL B C   
7174 O O   . VAL B 374 ? 0.4035 0.4494 0.5154 0.0439  -0.0437 -0.0439 372 VAL B O   
7175 C CB  . VAL B 374 ? 0.4014 0.4341 0.5229 0.0416  -0.0344 -0.0359 372 VAL B CB  
7176 C CG1 . VAL B 374 ? 0.4119 0.4592 0.5503 0.0419  -0.0384 -0.0430 372 VAL B CG1 
7177 C CG2 . VAL B 374 ? 0.4379 0.4558 0.5552 0.0364  -0.0272 -0.0301 372 VAL B CG2 
7178 N N   . PHE B 375 ? 0.4476 0.5117 0.5880 0.0326  -0.0352 -0.0468 373 PHE B N   
7179 C CA  . PHE B 375 ? 0.4047 0.4775 0.5471 0.0307  -0.0398 -0.0538 373 PHE B CA  
7180 C C   . PHE B 375 ? 0.4525 0.5403 0.6128 0.0279  -0.0420 -0.0592 373 PHE B C   
7181 O O   . PHE B 375 ? 0.3717 0.4609 0.5384 0.0220  -0.0369 -0.0588 373 PHE B O   
7182 C CB  . PHE B 375 ? 0.3573 0.4252 0.4968 0.0261  -0.0327 -0.0533 373 PHE B CB  
7183 C CG  . PHE B 375 ? 0.3648 0.4324 0.4980 0.0223  -0.0357 -0.0604 373 PHE B CG  
7184 C CD1 . PHE B 375 ? 0.3791 0.4598 0.5200 0.0196  -0.0448 -0.0675 373 PHE B CD1 
7185 C CD2 . PHE B 375 ? 0.3594 0.4131 0.4809 0.0209  -0.0283 -0.0604 373 PHE B CD2 
7186 C CE1 . PHE B 375 ? 0.4253 0.5056 0.5612 0.0127  -0.0482 -0.0747 373 PHE B CE1 
7187 C CE2 . PHE B 375 ? 0.3681 0.4156 0.4792 0.0154  -0.0304 -0.0678 373 PHE B CE2 
7188 C CZ  . PHE B 375 ? 0.3893 0.4502 0.5071 0.0098  -0.0412 -0.0751 373 PHE B CZ  
7189 N N   . ASP B 376 ? 0.4318 0.5305 0.6002 0.0323  -0.0495 -0.0640 374 ASP B N   
7190 C CA  . ASP B 376 ? 0.4562 0.5702 0.6446 0.0309  -0.0477 -0.0698 374 ASP B CA  
7191 C C   . ASP B 376 ? 0.4336 0.5628 0.6342 0.0223  -0.0480 -0.0774 374 ASP B C   
7192 O O   . ASP B 376 ? 0.4164 0.5433 0.6085 0.0183  -0.0525 -0.0788 374 ASP B O   
7193 C CB  . ASP B 376 ? 0.4328 0.5526 0.6306 0.0428  -0.0540 -0.0703 374 ASP B CB  
7194 C CG  . ASP B 376 ? 0.5868 0.7149 0.8024 0.0441  -0.0460 -0.0752 374 ASP B CG  
7195 O OD1 . ASP B 376 ? 0.4935 0.6206 0.7093 0.0341  -0.0360 -0.0780 374 ASP B OD1 
7196 O OD2 . ASP B 376 ? 0.6745 0.8072 0.9014 0.0561  -0.0491 -0.0759 374 ASP B OD2 
7197 N N   . GLU B 377 ? 0.4599 0.6016 0.6779 0.0182  -0.0413 -0.0829 375 GLU B N   
7198 C CA  . GLU B 377 ? 0.4430 0.5989 0.6746 0.0072  -0.0382 -0.0904 375 GLU B CA  
7199 C C   . GLU B 377 ? 0.3552 0.4944 0.5675 -0.0026 -0.0355 -0.0885 375 GLU B C   
7200 O O   . GLU B 377 ? 0.3785 0.5196 0.5894 -0.0089 -0.0399 -0.0925 375 GLU B O   
7201 C CB  . GLU B 377 ? 0.4358 0.6158 0.6891 0.0095  -0.0498 -0.0962 375 GLU B CB  
7202 C CG  . GLU B 377 ? 0.5358 0.7384 0.8192 0.0195  -0.0503 -0.0995 375 GLU B CG  
7203 C CD  . GLU B 377 ? 0.6421 0.8784 0.9595 0.0172  -0.0602 -0.1069 375 GLU B CD  
7204 O OE1 . GLU B 377 ? 0.6640 0.9030 0.9772 0.0051  -0.0671 -0.1104 375 GLU B OE1 
7205 O OE2 . GLU B 377 ? 0.7845 1.0446 1.1346 0.0275  -0.0610 -0.1096 375 GLU B OE2 
7206 N N   . ILE B 378 ? 0.3811 0.5027 0.5785 -0.0041 -0.0287 -0.0825 376 ILE B N   
7207 C CA  . ILE B 378 ? 0.4048 0.5089 0.5857 -0.0089 -0.0264 -0.0786 376 ILE B CA  
7208 C C   . ILE B 378 ? 0.3953 0.4963 0.5753 -0.0216 -0.0199 -0.0836 376 ILE B C   
7209 O O   . ILE B 378 ? 0.3940 0.4803 0.5617 -0.0258 -0.0189 -0.0830 376 ILE B O   
7210 C CB  . ILE B 378 ? 0.4154 0.5060 0.5862 -0.0055 -0.0246 -0.0695 376 ILE B CB  
7211 C CG1 . ILE B 378 ? 0.4514 0.5284 0.6123 -0.0029 -0.0245 -0.0638 376 ILE B CG1 
7212 C CG2 . ILE B 378 ? 0.4033 0.4873 0.5689 -0.0130 -0.0191 -0.0690 376 ILE B CG2 
7213 C CD1 . ILE B 378 ? 0.4192 0.4956 0.5764 0.0035  -0.0271 -0.0645 376 ILE B CD1 
7214 N N   . SER B 379 ? 0.4239 0.5350 0.6149 -0.0282 -0.0130 -0.0887 377 SER B N   
7215 C CA  . SER B 379 ? 0.3778 0.4842 0.5669 -0.0427 -0.0043 -0.0936 377 SER B CA  
7216 C C   . SER B 379 ? 0.4463 0.5626 0.6452 -0.0492 -0.0095 -0.1008 377 SER B C   
7217 O O   . SER B 379 ? 0.4794 0.5814 0.6678 -0.0614 -0.0043 -0.1032 377 SER B O   
7218 C CB  . SER B 379 ? 0.3775 0.4946 0.5785 -0.0492 0.0077  -0.0989 377 SER B CB  
7219 O OG  . SER B 379 ? 0.4452 0.5936 0.6785 -0.0451 0.0054  -0.1063 377 SER B OG  
7220 N N   . MET B 380 ? 0.4341 0.5713 0.6494 -0.0418 -0.0209 -0.1040 378 MET B N   
7221 C CA  . MET B 380 ? 0.3975 0.5464 0.6214 -0.0487 -0.0304 -0.1115 378 MET B CA  
7222 C C   . MET B 380 ? 0.4376 0.5619 0.6329 -0.0468 -0.0371 -0.1091 378 MET B C   
7223 O O   . MET B 380 ? 0.4343 0.5613 0.6277 -0.0537 -0.0466 -0.1156 378 MET B O   
7224 C CB  . MET B 380 ? 0.4290 0.6099 0.6809 -0.0401 -0.0429 -0.1148 378 MET B CB  
7225 C CG  . MET B 380 ? 0.4631 0.6734 0.7512 -0.0418 -0.0352 -0.1199 378 MET B CG  
7226 S SD  . MET B 380 ? 0.5133 0.7415 0.8251 -0.0655 -0.0275 -0.1311 378 MET B SD  
7227 C CE  . MET B 380 ? 0.4695 0.7148 0.7903 -0.0692 -0.0528 -0.1368 378 MET B CE  
7228 N N   . ALA B 381 ? 0.4170 0.5175 0.5909 -0.0382 -0.0321 -0.1004 379 ALA B N   
7229 C CA  . ALA B 381 ? 0.4495 0.5264 0.5983 -0.0339 -0.0340 -0.0982 379 ALA B CA  
7230 C C   . ALA B 381 ? 0.4109 0.4603 0.5418 -0.0425 -0.0245 -0.0989 379 ALA B C   
7231 O O   . ALA B 381 ? 0.3865 0.4307 0.5197 -0.0486 -0.0162 -0.0969 379 ALA B O   
7232 C CB  . ALA B 381 ? 0.4633 0.5331 0.6052 -0.0189 -0.0325 -0.0883 379 ALA B CB  
7233 N N   . THR B 382 ? 0.4510 0.4783 0.5595 -0.0431 -0.0249 -0.1018 380 THR B N   
7234 C CA  . THR B 382 ? 0.4516 0.4453 0.5387 -0.0480 -0.0148 -0.1021 380 THR B CA  
7235 C C   . THR B 382 ? 0.4337 0.4072 0.5075 -0.0317 -0.0076 -0.0935 380 THR B C   
7236 O O   . THR B 382 ? 0.4116 0.3956 0.4891 -0.0206 -0.0104 -0.0894 380 THR B O   
7237 C CB  . THR B 382 ? 0.4610 0.4395 0.5303 -0.0624 -0.0182 -0.1139 380 THR B CB  
7238 O OG1 . THR B 382 ? 0.5304 0.4990 0.5799 -0.0552 -0.0235 -0.1159 380 THR B OG1 
7239 C CG2 . THR B 382 ? 0.5006 0.5100 0.5932 -0.0781 -0.0281 -0.1228 380 THR B CG2 
7240 N N   . ASN B 383 ? 0.4112 0.3552 0.4712 -0.0301 0.0028  -0.0903 381 ASN B N   
7241 C CA  . ASN B 383 ? 0.4055 0.3325 0.4587 -0.0136 0.0114  -0.0830 381 ASN B CA  
7242 C C   . ASN B 383 ? 0.4292 0.3435 0.4620 -0.0110 0.0135  -0.0896 381 ASN B C   
7243 O O   . ASN B 383 ? 0.4743 0.3855 0.5072 0.0027  0.0210  -0.0840 381 ASN B O   
7244 C CB  . ASN B 383 ? 0.4218 0.3169 0.4642 -0.0103 0.0217  -0.0785 381 ASN B CB  
7245 C CG  . ASN B 383 ? 0.4007 0.3054 0.4595 -0.0066 0.0189  -0.0673 381 ASN B CG  
7246 O OD1 . ASN B 383 ? 0.4164 0.3506 0.4944 -0.0053 0.0113  -0.0631 381 ASN B OD1 
7247 N ND2 . ASN B 383 ? 0.4822 0.3577 0.5289 -0.0053 0.0246  -0.0624 381 ASN B ND2 
7248 N N   . TYR B 384 ? 0.4301 0.3370 0.4447 -0.0252 0.0070  -0.1013 382 TYR B N   
7249 C CA  . TYR B 384 ? 0.4553 0.3472 0.4427 -0.0246 0.0059  -0.1078 382 TYR B CA  
7250 C C   . TYR B 384 ? 0.5071 0.4252 0.5053 -0.0161 -0.0022 -0.1027 382 TYR B C   
7251 O O   . TYR B 384 ? 0.5177 0.4222 0.4995 -0.0062 0.0058  -0.1000 382 TYR B O   
7252 C CB  . TYR B 384 ? 0.5023 0.3841 0.4692 -0.0441 -0.0048 -0.1215 382 TYR B CB  
7253 C CG  . TYR B 384 ? 0.5667 0.4171 0.4910 -0.0455 -0.0043 -0.1293 382 TYR B CG  
7254 C CD1 . TYR B 384 ? 0.5404 0.4033 0.4550 -0.0438 -0.0177 -0.1300 382 TYR B CD1 
7255 C CD2 . TYR B 384 ? 0.6086 0.4114 0.4972 -0.0480 0.0104  -0.1357 382 TYR B CD2 
7256 C CE1 . TYR B 384 ? 0.6350 0.4638 0.5022 -0.0460 -0.0173 -0.1368 382 TYR B CE1 
7257 C CE2 . TYR B 384 ? 0.6561 0.4242 0.4984 -0.0502 0.0128  -0.1440 382 TYR B CE2 
7258 C CZ  . TYR B 384 ? 0.6750 0.4562 0.5051 -0.0499 -0.0015 -0.1444 382 TYR B CZ  
7259 O OH  . TYR B 384 ? 0.7772 0.5191 0.5534 -0.0531 0.0006  -0.1523 382 TYR B OH  
7260 N N   . ASP B 385 ? 0.4565 0.4095 0.4809 -0.0199 -0.0159 -0.1015 383 ASP B N   
7261 C CA  . ASP B 385 ? 0.5071 0.4806 0.5403 -0.0112 -0.0235 -0.0961 383 ASP B CA  
7262 C C   . ASP B 385 ? 0.4550 0.4293 0.4989 0.0027  -0.0112 -0.0850 383 ASP B C   
7263 O O   . ASP B 385 ? 0.4849 0.4549 0.5183 0.0102  -0.0085 -0.0811 383 ASP B O   
7264 C CB  . ASP B 385 ? 0.3990 0.4077 0.4615 -0.0157 -0.0375 -0.0971 383 ASP B CB  
7265 C CG  . ASP B 385 ? 0.5546 0.5710 0.6180 -0.0308 -0.0497 -0.1081 383 ASP B CG  
7266 O OD1 . ASP B 385 ? 0.6676 0.6720 0.7065 -0.0352 -0.0595 -0.1141 383 ASP B OD1 
7267 O OD2 . ASP B 385 ? 0.5824 0.6165 0.6702 -0.0396 -0.0495 -0.1108 383 ASP B OD2 
7268 N N   . LEU B 386 ? 0.4180 0.3974 0.4823 0.0050  -0.0045 -0.0793 384 LEU B N   
7269 C CA  . LEU B 386 ? 0.4293 0.4150 0.5098 0.0164  0.0037  -0.0687 384 LEU B CA  
7270 C C   . LEU B 386 ? 0.4559 0.4200 0.5210 0.0252  0.0187  -0.0671 384 LEU B C   
7271 O O   . LEU B 386 ? 0.4241 0.3949 0.4973 0.0325  0.0249  -0.0607 384 LEU B O   
7272 C CB  . LEU B 386 ? 0.3329 0.3231 0.4324 0.0171  0.0054  -0.0628 384 LEU B CB  
7273 C CG  . LEU B 386 ? 0.3993 0.4067 0.5113 0.0084  -0.0044 -0.0637 384 LEU B CG  
7274 C CD1 . LEU B 386 ? 0.3930 0.3943 0.5118 0.0091  -0.0021 -0.0570 384 LEU B CD1 
7275 C CD2 . LEU B 386 ? 0.3769 0.4072 0.5033 0.0106  -0.0113 -0.0607 384 LEU B CD2 
7276 N N   . SER B 387 ? 0.5000 0.4356 0.5420 0.0236  0.0269  -0.0735 385 SER B N   
7277 C CA  . SER B 387 ? 0.4887 0.3993 0.5141 0.0328  0.0456  -0.0733 385 SER B CA  
7278 C C   . SER B 387 ? 0.5325 0.4331 0.5290 0.0314  0.0463  -0.0770 385 SER B C   
7279 O O   . SER B 387 ? 0.5036 0.3971 0.4968 0.0398  0.0622  -0.0727 385 SER B O   
7280 C CB  . SER B 387 ? 0.5070 0.3829 0.5096 0.0312  0.0551  -0.0804 385 SER B CB  
7281 O OG  . SER B 387 ? 0.5440 0.3897 0.5222 0.0391  0.0751  -0.0833 385 SER B OG  
7282 N N   . VAL B 388 ? 0.4935 0.3933 0.4690 0.0205  0.0292  -0.0844 386 VAL B N   
7283 C CA  . VAL B 388 ? 0.5261 0.4126 0.4677 0.0191  0.0254  -0.0869 386 VAL B CA  
7284 C C   . VAL B 388 ? 0.5487 0.4546 0.5073 0.0265  0.0261  -0.0766 386 VAL B C   
7285 O O   . VAL B 388 ? 0.5794 0.4672 0.5143 0.0307  0.0379  -0.0739 386 VAL B O   
7286 C CB  . VAL B 388 ? 0.5450 0.4343 0.4696 0.0067  0.0014  -0.0955 386 VAL B CB  
7287 C CG1 . VAL B 388 ? 0.6009 0.4802 0.4931 0.0073  -0.0086 -0.0948 386 VAL B CG1 
7288 C CG2 . VAL B 388 ? 0.5438 0.4055 0.4423 -0.0039 0.0025  -0.1071 386 VAL B CG2 
7289 N N   . VAL B 389 ? 0.4713 0.4101 0.4675 0.0268  0.0152  -0.0712 387 VAL B N   
7290 C CA  . VAL B 389 ? 0.4702 0.4244 0.4819 0.0319  0.0156  -0.0622 387 VAL B CA  
7291 C C   . VAL B 389 ? 0.4910 0.4408 0.5139 0.0389  0.0381  -0.0553 387 VAL B C   
7292 O O   . VAL B 389 ? 0.4948 0.4363 0.5062 0.0413  0.0477  -0.0507 387 VAL B O   
7293 C CB  . VAL B 389 ? 0.3981 0.3836 0.4455 0.0302  0.0024  -0.0592 387 VAL B CB  
7294 C CG1 . VAL B 389 ? 0.4843 0.4811 0.5474 0.0342  0.0052  -0.0503 387 VAL B CG1 
7295 C CG2 . VAL B 389 ? 0.4165 0.4111 0.4594 0.0248  -0.0173 -0.0656 387 VAL B CG2 
7296 N N   . ASN B 390 ? 0.4911 0.4463 0.5378 0.0423  0.0470  -0.0541 388 ASN B N   
7297 C CA  . ASN B 390 ? 0.5089 0.4671 0.5771 0.0504  0.0673  -0.0473 388 ASN B CA  
7298 C C   . ASN B 390 ? 0.5905 0.5174 0.6261 0.0541  0.0893  -0.0508 388 ASN B C   
7299 O O   . ASN B 390 ? 0.7036 0.6330 0.7525 0.0593  0.1088  -0.0453 388 ASN B O   
7300 C CB  . ASN B 390 ? 0.4919 0.4608 0.5915 0.0555  0.0689  -0.0445 388 ASN B CB  
7301 C CG  . ASN B 390 ? 0.5344 0.5327 0.6657 0.0520  0.0514  -0.0388 388 ASN B CG  
7302 O OD1 . ASN B 390 ? 0.6099 0.6254 0.7537 0.0488  0.0457  -0.0343 388 ASN B OD1 
7303 N ND2 . ASN B 390 ? 0.4814 0.4805 0.6208 0.0516  0.0438  -0.0391 388 ASN B ND2 
7304 N N   . ALA B 391 ? 0.6025 0.4990 0.5944 0.0502  0.0875  -0.0605 389 ALA B N   
7305 C CA  . ALA B 391 ? 0.6008 0.4599 0.5523 0.0528  0.1096  -0.0653 389 ALA B CA  
7306 C C   . ALA B 391 ? 0.5782 0.4222 0.4924 0.0484  0.1087  -0.0641 389 ALA B C   
7307 O O   . ALA B 391 ? 0.6570 0.4778 0.5486 0.0514  0.1330  -0.0632 389 ALA B O   
7308 C CB  . ALA B 391 ? 0.6003 0.4263 0.5137 0.0484  0.1078  -0.0771 389 ALA B CB  
7309 N N   . ARG B 392 ? 0.5566 0.4113 0.4629 0.0420  0.0822  -0.0637 390 ARG B N   
7310 C CA  . ARG B 392 ? 0.6291 0.4651 0.4953 0.0392  0.0774  -0.0612 390 ARG B CA  
7311 C C   . ARG B 392 ? 0.6598 0.5161 0.5528 0.0414  0.0800  -0.0501 390 ARG B C   
7312 O O   . ARG B 392 ? 0.7167 0.5506 0.5760 0.0406  0.0866  -0.0458 390 ARG B O   
7313 C CB  . ARG B 392 ? 0.6139 0.4495 0.4579 0.0329  0.0457  -0.0665 390 ARG B CB  
7314 C CG  . ARG B 392 ? 0.6951 0.5021 0.4994 0.0265  0.0418  -0.0785 390 ARG B CG  
7315 C CD  . ARG B 392 ? 0.7745 0.5885 0.5654 0.0188  0.0083  -0.0835 390 ARG B CD  
7316 N NE  . ARG B 392 ? 0.8208 0.6113 0.5806 0.0091  0.0030  -0.0961 390 ARG B NE  
7317 C CZ  . ARG B 392 ? 0.8561 0.6522 0.6052 -0.0007 -0.0256 -0.1031 390 ARG B CZ  
7318 N NH1 . ARG B 392 ? 0.8600 0.6838 0.6261 0.0005  -0.0515 -0.0984 390 ARG B NH1 
7319 N NH2 . ARG B 392 ? 0.8663 0.6391 0.5880 -0.0121 -0.0281 -0.1154 390 ARG B NH2 
7320 N N   . LEU B 393 ? 0.5616 0.4552 0.5094 0.0431  0.0755  -0.0454 391 LEU B N   
7321 C CA  . LEU B 393 ? 0.6052 0.5172 0.5774 0.0424  0.0737  -0.0363 391 LEU B CA  
7322 C C   . LEU B 393 ? 0.6827 0.6173 0.7020 0.0443  0.0924  -0.0307 391 LEU B C   
7323 O O   . LEU B 393 ? 0.6591 0.6191 0.7172 0.0460  0.0861  -0.0308 391 LEU B O   
7324 C CB  . LEU B 393 ? 0.5357 0.4708 0.5268 0.0407  0.0468  -0.0362 391 LEU B CB  
7325 C CG  . LEU B 393 ? 0.6363 0.5581 0.5926 0.0402  0.0252  -0.0401 391 LEU B CG  
7326 C CD1 . LEU B 393 ? 0.6341 0.5814 0.6175 0.0407  0.0046  -0.0389 391 LEU B CD1 
7327 C CD2 . LEU B 393 ? 0.6914 0.5799 0.6006 0.0409  0.0303  -0.0357 391 LEU B CD2 
7328 N N   . ARG B 394 ? 0.4935 0.4184 0.5094 0.0436  0.1152  -0.0256 392 ARG B N   
7329 C CA  . ARG B 394 ? 0.5769 0.5293 0.6445 0.0438  0.1313  -0.0193 392 ARG B CA  
7330 C C   . ARG B 394 ? 0.5164 0.4837 0.5998 0.0362  0.1191  -0.0128 392 ARG B C   
7331 O O   . ARG B 394 ? 0.7087 0.6528 0.7560 0.0323  0.1175  -0.0107 392 ARG B O   
7332 C CB  . ARG B 394 ? 0.6486 0.5847 0.7089 0.0455  0.1658  -0.0181 392 ARG B CB  
7333 C CG  . ARG B 394 ? 0.7405 0.6592 0.7872 0.0544  0.1808  -0.0254 392 ARG B CG  
7334 C CD  . ARG B 394 ? 0.8882 0.8263 0.9613 0.0596  0.1608  -0.0288 392 ARG B CD  
7335 N NE  . ARG B 394 ? 0.9700 0.9023 1.0555 0.0700  0.1800  -0.0322 392 ARG B NE  
7336 C CZ  . ARG B 394 ? 1.0730 1.0259 1.2056 0.0776  0.2019  -0.0271 392 ARG B CZ  
7337 N NH1 . ARG B 394 ? 1.0402 1.0283 1.2202 0.0738  0.2027  -0.0184 392 ARG B NH1 
7338 N NH2 . ARG B 394 ? 0.9493 0.8880 1.0846 0.0894  0.2228  -0.0311 392 ARG B NH2 
7339 N N   . ALA B 395 ? 0.4304 0.4324 0.5638 0.0342  0.1097  -0.0095 393 ALA B N   
7340 C CA  . ALA B 395 ? 0.4404 0.4537 0.5864 0.0259  0.0959  -0.0053 393 ALA B CA  
7341 C C   . ALA B 395 ? 0.4249 0.4732 0.6269 0.0207  0.0974  -0.0002 393 ALA B C   
7342 O O   . ALA B 395 ? 0.4218 0.4911 0.6574 0.0263  0.1007  0.0003  393 ALA B O   
7343 C CB  . ALA B 395 ? 0.4543 0.4682 0.5880 0.0272  0.0691  -0.0096 393 ALA B CB  
7344 N N   . LYS B 396 ? 0.4347 0.4873 0.6458 0.0099  0.0935  0.0039  394 LYS B N   
7345 C CA  . LYS B 396 ? 0.4228 0.5091 0.6853 0.0016  0.0891  0.0082  394 LYS B CA  
7346 C C   . LYS B 396 ? 0.3990 0.5002 0.6728 0.0015  0.0624  0.0061  394 LYS B C   
7347 O O   . LYS B 396 ? 0.4222 0.5522 0.7366 -0.0004 0.0546  0.0091  394 LYS B O   
7348 C CB  . LYS B 396 ? 0.4582 0.5385 0.7215 -0.0134 0.0949  0.0122  394 LYS B CB  
7349 C CG  . LYS B 396 ? 0.5428 0.6015 0.7872 -0.0166 0.1230  0.0152  394 LYS B CG  
7350 C CD  . LYS B 396 ? 0.6225 0.6711 0.8646 -0.0335 0.1263  0.0192  394 LYS B CD  
7351 C CE  . LYS B 396 ? 0.5818 0.6076 0.8059 -0.0399 0.1572  0.0234  394 LYS B CE  
7352 N NZ  . LYS B 396 ? 0.6790 0.6886 0.8956 -0.0578 0.1598  0.0274  394 LYS B NZ  
7353 N N   . HIS B 397 ? 0.4217 0.5037 0.6605 0.0036  0.0485  0.0013  395 HIS B N   
7354 C CA  . HIS B 397 ? 0.4194 0.5099 0.6620 0.0024  0.0272  -0.0016 395 HIS B CA  
7355 C C   . HIS B 397 ? 0.3877 0.4629 0.5993 0.0111  0.0202  -0.0080 395 HIS B C   
7356 O O   . HIS B 397 ? 0.4528 0.5072 0.6342 0.0149  0.0242  -0.0101 395 HIS B O   
7357 C CB  . HIS B 397 ? 0.3899 0.4760 0.6299 -0.0095 0.0180  -0.0011 395 HIS B CB  
7358 C CG  . HIS B 397 ? 0.3246 0.4284 0.5980 -0.0221 0.0216  0.0043  395 HIS B CG  
7359 N ND1 . HIS B 397 ? 0.3721 0.5018 0.6784 -0.0284 0.0080  0.0065  395 HIS B ND1 
7360 C CD2 . HIS B 397 ? 0.3807 0.4808 0.6606 -0.0309 0.0368  0.0082  395 HIS B CD2 
7361 C CE1 . HIS B 397 ? 0.3905 0.5359 0.7269 -0.0408 0.0128  0.0110  395 HIS B CE1 
7362 N NE2 . HIS B 397 ? 0.3810 0.5089 0.7029 -0.0433 0.0320  0.0119  395 HIS B NE2 
7363 N N   . TYR B 398 ? 0.4516 0.5367 0.6708 0.0135  0.0088  -0.0106 396 TYR B N   
7364 C CA  . TYR B 398 ? 0.4248 0.5004 0.6220 0.0189  0.0024  -0.0172 396 TYR B CA  
7365 C C   . TYR B 398 ? 0.4229 0.5028 0.6209 0.0140  -0.0116 -0.0200 396 TYR B C   
7366 O O   . TYR B 398 ? 0.4906 0.5816 0.7052 0.0096  -0.0179 -0.0172 396 TYR B O   
7367 C CB  . TYR B 398 ? 0.3688 0.4459 0.5696 0.0254  0.0069  -0.0184 396 TYR B CB  
7368 C CG  . TYR B 398 ? 0.4200 0.4873 0.6141 0.0310  0.0239  -0.0175 396 TYR B CG  
7369 C CD1 . TYR B 398 ? 0.4430 0.5215 0.6636 0.0323  0.0367  -0.0114 396 TYR B CD1 
7370 C CD2 . TYR B 398 ? 0.4782 0.5251 0.6397 0.0346  0.0276  -0.0231 396 TYR B CD2 
7371 C CE1 . TYR B 398 ? 0.5829 0.6502 0.7963 0.0375  0.0568  -0.0113 396 TYR B CE1 
7372 C CE2 . TYR B 398 ? 0.5254 0.5569 0.6727 0.0387  0.0450  -0.0231 396 TYR B CE2 
7373 C CZ  . TYR B 398 ? 0.5834 0.6240 0.7561 0.0406  0.0616  -0.0174 396 TYR B CZ  
7374 O OH  . TYR B 398 ? 0.5276 0.5511 0.6856 0.0449  0.0834  -0.0180 396 TYR B OH  
7375 N N   . VAL B 399 ? 0.3861 0.4567 0.5659 0.0153  -0.0162 -0.0254 397 VAL B N   
7376 C CA  . VAL B 399 ? 0.3830 0.4547 0.5607 0.0115  -0.0248 -0.0297 397 VAL B CA  
7377 C C   . VAL B 399 ? 0.4000 0.4729 0.5707 0.0154  -0.0270 -0.0364 397 VAL B C   
7378 O O   . VAL B 399 ? 0.3901 0.4593 0.5514 0.0210  -0.0270 -0.0397 397 VAL B O   
7379 C CB  . VAL B 399 ? 0.3727 0.4335 0.5412 0.0097  -0.0260 -0.0308 397 VAL B CB  
7380 C CG1 . VAL B 399 ? 0.3526 0.4114 0.5179 0.0048  -0.0312 -0.0356 397 VAL B CG1 
7381 C CG2 . VAL B 399 ? 0.3715 0.4287 0.5458 0.0034  -0.0220 -0.0244 397 VAL B CG2 
7382 N N   . TYR B 400 ? 0.3527 0.4299 0.5268 0.0114  -0.0298 -0.0382 398 TYR B N   
7383 C CA  . TYR B 400 ? 0.3815 0.4604 0.5515 0.0113  -0.0301 -0.0450 398 TYR B CA  
7384 C C   . TYR B 400 ? 0.3541 0.4331 0.5218 0.0072  -0.0312 -0.0500 398 TYR B C   
7385 O O   . TYR B 400 ? 0.3472 0.4214 0.5110 0.0008  -0.0325 -0.0483 398 TYR B O   
7386 C CB  . TYR B 400 ? 0.3485 0.4257 0.5193 0.0092  -0.0289 -0.0431 398 TYR B CB  
7387 C CG  . TYR B 400 ? 0.4001 0.4747 0.5736 0.0149  -0.0243 -0.0389 398 TYR B CG  
7388 C CD1 . TYR B 400 ? 0.3988 0.4679 0.5627 0.0183  -0.0207 -0.0434 398 TYR B CD1 
7389 C CD2 . TYR B 400 ? 0.3674 0.4450 0.5536 0.0167  -0.0232 -0.0307 398 TYR B CD2 
7390 C CE1 . TYR B 400 ? 0.4053 0.4665 0.5662 0.0234  -0.0130 -0.0408 398 TYR B CE1 
7391 C CE2 . TYR B 400 ? 0.4412 0.5169 0.6331 0.0233  -0.0148 -0.0275 398 TYR B CE2 
7392 C CZ  . TYR B 400 ? 0.3764 0.4412 0.5527 0.0267  -0.0081 -0.0329 398 TYR B CZ  
7393 O OH  . TYR B 400 ? 0.5827 0.6401 0.7589 0.0331  0.0036  -0.0310 398 TYR B OH  
7394 N N   . ILE B 401 ? 0.3978 0.4816 0.5677 0.0113  -0.0308 -0.0563 399 ILE B N   
7395 C CA  . ILE B 401 ? 0.3995 0.4844 0.5710 0.0100  -0.0277 -0.0623 399 ILE B CA  
7396 C C   . ILE B 401 ? 0.4014 0.4979 0.5815 0.0072  -0.0246 -0.0695 399 ILE B C   
7397 O O   . ILE B 401 ? 0.3539 0.4605 0.5417 0.0101  -0.0283 -0.0718 399 ILE B O   
7398 C CB  . ILE B 401 ? 0.3971 0.4795 0.5704 0.0190  -0.0287 -0.0633 399 ILE B CB  
7399 C CG1 . ILE B 401 ? 0.3775 0.4455 0.5407 0.0184  -0.0301 -0.0562 399 ILE B CG1 
7400 C CG2 . ILE B 401 ? 0.3872 0.4697 0.5645 0.0200  -0.0223 -0.0704 399 ILE B CG2 
7401 C CD1 . ILE B 401 ? 0.3769 0.4347 0.5359 0.0274  -0.0306 -0.0553 399 ILE B CD1 
7402 N N   . GLY B 402 ? 0.3826 0.4759 0.5593 -0.0003 -0.0175 -0.0733 400 GLY B N   
7403 C CA  . GLY B 402 ? 0.3532 0.4571 0.5394 -0.0060 -0.0111 -0.0804 400 GLY B CA  
7404 C C   . GLY B 402 ? 0.4093 0.5015 0.5827 -0.0156 -0.0002 -0.0832 400 GLY B C   
7405 O O   . GLY B 402 ? 0.4100 0.4876 0.5684 -0.0161 0.0016  -0.0818 400 GLY B O   
7406 N N   . ASP B 403 ? 0.3970 0.4919 0.5721 -0.0250 0.0075  -0.0874 401 ASP B N   
7407 C CA  . ASP B 403 ? 0.4006 0.4792 0.5568 -0.0361 0.0203  -0.0897 401 ASP B CA  
7408 C C   . ASP B 403 ? 0.3826 0.4550 0.5318 -0.0476 0.0249  -0.0895 401 ASP B C   
7409 O O   . ASP B 403 ? 0.3799 0.4698 0.5503 -0.0525 0.0316  -0.0967 401 ASP B O   
7410 C CB  . ASP B 403 ? 0.4148 0.5043 0.5860 -0.0351 0.0351  -0.0995 401 ASP B CB  
7411 C CG  . ASP B 403 ? 0.3826 0.4496 0.5272 -0.0471 0.0521  -0.1026 401 ASP B CG  
7412 O OD1 . ASP B 403 ? 0.4409 0.4824 0.5527 -0.0561 0.0489  -0.0959 401 ASP B OD1 
7413 O OD2 . ASP B 403 ? 0.4042 0.4775 0.5597 -0.0467 0.0690  -0.1114 401 ASP B OD2 
7414 N N   . PRO B 404 ? 0.4026 0.4494 0.5231 -0.0526 0.0207  -0.0811 402 PRO B N   
7415 C CA  . PRO B 404 ? 0.4709 0.5039 0.5794 -0.0632 0.0261  -0.0801 402 PRO B CA  
7416 C C   . PRO B 404 ? 0.3640 0.3918 0.4664 -0.0772 0.0456  -0.0876 402 PRO B C   
7417 O O   . PRO B 404 ? 0.4125 0.4271 0.5047 -0.0887 0.0532  -0.0878 402 PRO B O   
7418 C CB  . PRO B 404 ? 0.4756 0.4804 0.5538 -0.0619 0.0161  -0.0678 402 PRO B CB  
7419 C CG  . PRO B 404 ? 0.5123 0.5131 0.5797 -0.0589 0.0116  -0.0659 402 PRO B CG  
7420 C CD  . PRO B 404 ? 0.4419 0.4707 0.5406 -0.0491 0.0097  -0.0717 402 PRO B CD  
7421 N N   . ALA B 405 ? 0.3839 0.4193 0.4918 -0.0768 0.0562  -0.0941 403 ALA B N   
7422 C CA  . ALA B 405 ? 0.3521 0.3831 0.4559 -0.0897 0.0794  -0.1021 403 ALA B CA  
7423 C C   . ALA B 405 ? 0.3100 0.3810 0.4632 -0.0898 0.0889  -0.1133 403 ALA B C   
7424 O O   . ALA B 405 ? 0.3224 0.3987 0.4845 -0.1006 0.1109  -0.1214 403 ALA B O   
7425 C CB  . ALA B 405 ? 0.4196 0.4307 0.4966 -0.0898 0.0894  -0.1037 403 ALA B CB  
7426 N N   . GLN B 406 ? 0.3209 0.4204 0.5066 -0.0782 0.0727  -0.1138 404 GLN B N   
7427 C CA  . GLN B 406 ? 0.3039 0.4440 0.5383 -0.0775 0.0747  -0.1231 404 GLN B CA  
7428 C C   . GLN B 406 ? 0.3287 0.4738 0.5696 -0.0876 0.0662  -0.1234 404 GLN B C   
7429 O O   . GLN B 406 ? 0.3647 0.4790 0.5722 -0.0951 0.0642  -0.1172 404 GLN B O   
7430 C CB  . GLN B 406 ? 0.3249 0.4878 0.5845 -0.0577 0.0620  -0.1234 404 GLN B CB  
7431 C CG  . GLN B 406 ? 0.3397 0.4950 0.5942 -0.0504 0.0760  -0.1261 404 GLN B CG  
7432 C CD  . GLN B 406 ? 0.3952 0.5698 0.6757 -0.0306 0.0669  -0.1270 404 GLN B CD  
7433 O OE1 . GLN B 406 ? 0.3907 0.5445 0.6488 -0.0214 0.0628  -0.1226 404 GLN B OE1 
7434 N NE2 . GLN B 406 ? 0.3363 0.5498 0.6641 -0.0245 0.0631  -0.1325 404 GLN B NE2 
7435 N N   . LEU B 407 ? 0.3017 0.4840 0.5848 -0.0874 0.0598  -0.1307 405 LEU B N   
7436 C CA  . LEU B 407 ? 0.2863 0.4737 0.5766 -0.1015 0.0540  -0.1342 405 LEU B CA  
7437 C C   . LEU B 407 ? 0.4501 0.6221 0.7195 -0.0938 0.0327  -0.1279 405 LEU B C   
7438 O O   . LEU B 407 ? 0.4001 0.5780 0.6709 -0.0765 0.0188  -0.1237 405 LEU B O   
7439 C CB  . LEU B 407 ? 0.2351 0.4706 0.5803 -0.1060 0.0524  -0.1448 405 LEU B CB  
7440 C CG  . LEU B 407 ? 0.3338 0.5857 0.7044 -0.1178 0.0790  -0.1526 405 LEU B CG  
7441 C CD1 . LEU B 407 ? 0.2546 0.5567 0.6824 -0.1155 0.0745  -0.1598 405 LEU B CD1 
7442 C CD2 . LEU B 407 ? 0.3258 0.5476 0.6682 -0.1423 0.0967  -0.1533 405 LEU B CD2 
7443 N N   . PRO B 408 ? 0.3969 0.5458 0.6448 -0.1066 0.0325  -0.1275 406 PRO B N   
7444 C CA  . PRO B 408 ? 0.4323 0.5652 0.6611 -0.1005 0.0164  -0.1237 406 PRO B CA  
7445 C C   . PRO B 408 ? 0.4079 0.5656 0.6602 -0.1076 0.0035  -0.1329 406 PRO B C   
7446 O O   . PRO B 408 ? 0.4190 0.6092 0.7072 -0.1184 0.0059  -0.1417 406 PRO B O   
7447 C CB  . PRO B 408 ? 0.4885 0.5790 0.6805 -0.1110 0.0258  -0.1193 406 PRO B CB  
7448 C CG  . PRO B 408 ? 0.4564 0.5531 0.6608 -0.1325 0.0422  -0.1270 406 PRO B CG  
7449 C CD  . PRO B 408 ? 0.3872 0.5166 0.6220 -0.1278 0.0501  -0.1302 406 PRO B CD  
7450 N N   . ALA B 409 ? 0.4811 0.6226 0.7126 -0.1019 -0.0101 -0.1309 407 ALA B N   
7451 C CA  . ALA B 409 ? 0.4993 0.6546 0.7409 -0.1113 -0.0245 -0.1397 407 ALA B CA  
7452 C C   . ALA B 409 ? 0.4366 0.5845 0.6794 -0.1371 -0.0153 -0.1482 407 ALA B C   
7453 O O   . ALA B 409 ? 0.4724 0.5845 0.6875 -0.1445 -0.0002 -0.1448 407 ALA B O   
7454 C CB  . ALA B 409 ? 0.5076 0.6356 0.7148 -0.1022 -0.0363 -0.1364 407 ALA B CB  
7455 N N   . PRO B 410 ? 0.4379 0.6183 0.7128 -0.1518 -0.0248 -0.1589 408 PRO B N   
7456 C CA  . PRO B 410 ? 0.5049 0.6771 0.7805 -0.1796 -0.0163 -0.1676 408 PRO B CA  
7457 C C   . PRO B 410 ? 0.6165 0.7365 0.8422 -0.1876 -0.0170 -0.1684 408 PRO B C   
7458 O O   . PRO B 410 ? 0.5989 0.7052 0.8018 -0.1781 -0.0324 -0.1680 408 PRO B O   
7459 C CB  . PRO B 410 ? 0.4512 0.6652 0.7615 -0.1832 -0.0333 -0.1706 408 PRO B CB  
7460 C CG  . PRO B 410 ? 0.5349 0.7639 0.8474 -0.1624 -0.0563 -0.1681 408 PRO B CG  
7461 C CD  . PRO B 410 ? 0.4605 0.6864 0.7727 -0.1437 -0.0452 -0.1625 408 PRO B CD  
7462 N N   . ARG B 411 ? 0.5689 0.6551 0.7738 -0.2043 0.0017  -0.1688 409 ARG B N   
7463 C CA  . ARG B 411 ? 0.6209 0.6534 0.7794 -0.2139 0.0043  -0.1705 409 ARG B CA  
7464 C C   . ARG B 411 ? 0.6150 0.6518 0.7814 -0.2393 0.0037  -0.1782 409 ARG B C   
7465 O O   . ARG B 411 ? 0.6177 0.6438 0.7838 -0.2537 0.0213  -0.1767 409 ARG B O   
7466 C CB  . ARG B 411 ? 0.7432 0.7264 0.8643 -0.2067 0.0233  -0.1593 409 ARG B CB  
7467 C CG  . ARG B 411 ? 0.5963 0.5567 0.6909 -0.1782 0.0186  -0.1481 409 ARG B CG  
7468 C CD  . ARG B 411 ? 0.6556 0.6515 0.7747 -0.1573 0.0139  -0.1401 409 ARG B CD  
7469 N NE  . ARG B 411 ? 0.5902 0.5612 0.6857 -0.1343 0.0151  -0.1275 409 ARG B NE  
7470 C CZ  . ARG B 411 ? 0.5388 0.5294 0.6468 -0.1163 0.0121  -0.1191 409 ARG B CZ  
7471 N NH1 . ARG B 411 ? 0.6241 0.6563 0.7643 -0.1151 0.0073  -0.1220 409 ARG B NH1 
7472 N NH2 . ARG B 411 ? 0.5461 0.5144 0.6356 -0.0988 0.0134  -0.1078 409 ARG B NH2 
7473 N N   . THR B 412 ? 0.6070 0.6569 0.7765 -0.2431 -0.0179 -0.1844 410 THR B N   
7474 C CA  . THR B 412 ? 0.5634 0.6251 0.7463 -0.2649 -0.0247 -0.1902 410 THR B CA  
7475 C C   . THR B 412 ? 0.5747 0.5840 0.7207 -0.2838 -0.0082 -0.1921 410 THR B C   
7476 O O   . THR B 412 ? 0.6280 0.6474 0.7899 -0.3043 -0.0065 -0.1960 410 THR B O   
7477 C CB  . THR B 412 ? 0.7175 0.7902 0.8974 -0.2651 -0.0538 -0.1959 410 THR B CB  
7478 O OG1 . THR B 412 ? 0.7849 0.8066 0.9111 -0.2581 -0.0559 -0.1983 410 THR B OG1 
7479 C CG2 . THR B 412 ? 0.7217 0.8495 0.9422 -0.2474 -0.0716 -0.1924 410 THR B CG2 
7480 N N   . LEU B 413 ? 0.6329 0.5860 0.7313 -0.2765 0.0042  -0.1887 411 LEU B N   
7481 C CA  . LEU B 413 ? 0.6260 0.5222 0.6834 -0.2905 0.0189  -0.1891 411 LEU B CA  
7482 C C   . LEU B 413 ? 0.6317 0.5064 0.6810 -0.2927 0.0440  -0.1806 411 LEU B C   
7483 O O   . LEU B 413 ? 0.7161 0.5536 0.7409 -0.3080 0.0574  -0.1803 411 LEU B O   
7484 C CB  . LEU B 413 ? 0.7231 0.5624 0.7280 -0.2791 0.0180  -0.1897 411 LEU B CB  
7485 C CG  . LEU B 413 ? 0.7221 0.5667 0.7175 -0.2760 -0.0043 -0.1981 411 LEU B CG  
7486 C CD1 . LEU B 413 ? 0.7578 0.5387 0.6971 -0.2637 0.0029  -0.1981 411 LEU B CD1 
7487 C CD2 . LEU B 413 ? 0.6922 0.5533 0.7000 -0.2992 -0.0185 -0.2072 411 LEU B CD2 
7488 N N   . LEU B 414 ? 0.6124 0.5058 0.6776 -0.2781 0.0502  -0.1736 412 LEU B N   
7489 C CA  . LEU B 414 ? 0.6499 0.5190 0.7011 -0.2794 0.0722  -0.1646 412 LEU B CA  
7490 C C   . LEU B 414 ? 0.6986 0.6007 0.7812 -0.2984 0.0833  -0.1674 412 LEU B C   
7491 O O   . LEU B 414 ? 0.6984 0.6574 0.8278 -0.2958 0.0792  -0.1701 412 LEU B O   
7492 C CB  . LEU B 414 ? 0.7026 0.5799 0.7588 -0.2587 0.0733  -0.1571 412 LEU B CB  
7493 C CG  . LEU B 414 ? 0.6862 0.5500 0.7339 -0.2608 0.0928  -0.1481 412 LEU B CG  
7494 C CD1 . LEU B 414 ? 0.6215 0.4145 0.6148 -0.2645 0.1064  -0.1392 412 LEU B CD1 
7495 C CD2 . LEU B 414 ? 0.6176 0.5012 0.6743 -0.2348 0.0870  -0.1388 412 LEU B CD2 
7496 N N   . THR B 415 ? 0.6651 0.5300 0.7217 -0.3162 0.0988  -0.1666 413 THR B N   
7497 C CA  . THR B 415 ? 0.7395 0.6285 0.8212 -0.3366 0.1131  -0.1700 413 THR B CA  
7498 C C   . THR B 415 ? 0.8347 0.6821 0.8824 -0.3418 0.1392  -0.1613 413 THR B C   
7499 O O   . THR B 415 ? 0.9424 0.8121 1.0110 -0.3549 0.1554  -0.1632 413 THR B O   
7500 C CB  . THR B 415 ? 0.7480 0.6346 0.8330 -0.3591 0.1077  -0.1791 413 THR B CB  
7501 O OG1 . THR B 415 ? 0.7911 0.6092 0.8194 -0.3620 0.1122  -0.1765 413 THR B OG1 
7502 C CG2 . THR B 415 ? 0.7130 0.6457 0.8340 -0.3564 0.0798  -0.1875 413 THR B CG2 
7503 N N   . LYS B 416 ? 0.8185 0.6047 0.8133 -0.3311 0.1435  -0.1512 414 LYS B N   
7504 C CA  . LYS B 416 ? 0.7733 0.5089 0.7245 -0.3348 0.1647  -0.1405 414 LYS B CA  
7505 C C   . LYS B 416 ? 0.8784 0.5970 0.8106 -0.3121 0.1621  -0.1287 414 LYS B C   
7506 O O   . LYS B 416 ? 0.9448 0.6362 0.8567 -0.2944 0.1495  -0.1235 414 LYS B O   
7507 C CB  . LYS B 416 ? 0.8615 0.5321 0.7629 -0.3420 0.1701  -0.1372 414 LYS B CB  
7508 C CG  . LYS B 416 ? 0.8589 0.5425 0.7766 -0.3624 0.1657  -0.1500 414 LYS B CG  
7509 C CD  . LYS B 416 ? 0.9354 0.5506 0.8006 -0.3650 0.1689  -0.1472 414 LYS B CD  
7510 C CE  . LYS B 416 ? 1.0060 0.6331 0.8846 -0.3784 0.1560  -0.1606 414 LYS B CE  
7511 N NZ  . LYS B 416 ? 1.1366 0.6951 0.9622 -0.3757 0.1581  -0.1584 414 LYS B NZ  
7512 N N   . GLY B 417 ? 0.8168 0.5494 0.7545 -0.3127 0.1743  -0.1247 415 GLY B N   
7513 C CA  . GLY B 417 ? 0.7859 0.4983 0.7012 -0.2942 0.1713  -0.1129 415 GLY B CA  
7514 C C   . GLY B 417 ? 0.7835 0.5559 0.7462 -0.2845 0.1631  -0.1184 415 GLY B C   
7515 O O   . GLY B 417 ? 0.8867 0.7152 0.8996 -0.2860 0.1542  -0.1302 415 GLY B O   
7516 N N   . THR B 418 ? 0.7946 0.5536 0.7383 -0.2719 0.1641  -0.1084 416 THR B N   
7517 C CA  . THR B 418 ? 0.6672 0.4793 0.6468 -0.2530 0.1534  -0.1096 416 THR B CA  
7518 C C   . THR B 418 ? 0.7524 0.5567 0.7191 -0.2219 0.1297  -0.0984 416 THR B C   
7519 O O   . THR B 418 ? 0.8175 0.5732 0.7398 -0.2117 0.1265  -0.0844 416 THR B O   
7520 C CB  . THR B 418 ? 0.7297 0.5411 0.6981 -0.2577 0.1713  -0.1066 416 THR B CB  
7521 O OG1 . THR B 418 ? 0.8675 0.6986 0.8605 -0.2849 0.1956  -0.1188 416 THR B OG1 
7522 C CG2 . THR B 418 ? 0.7388 0.5942 0.7356 -0.2357 0.1593  -0.1067 416 THR B CG2 
7523 N N   . LEU B 419 ? 0.6469 0.4989 0.6536 -0.2070 0.1134  -0.1040 417 LEU B N   
7524 C CA  . LEU B 419 ? 0.6499 0.5025 0.6526 -0.1791 0.0934  -0.0948 417 LEU B CA  
7525 C C   . LEU B 419 ? 0.6719 0.5416 0.6772 -0.1655 0.0902  -0.0883 417 LEU B C   
7526 O O   . LEU B 419 ? 0.6302 0.5431 0.6697 -0.1654 0.0915  -0.0963 417 LEU B O   
7527 C CB  . LEU B 419 ? 0.5654 0.4534 0.6020 -0.1722 0.0789  -0.1040 417 LEU B CB  
7528 C CG  . LEU B 419 ? 0.7566 0.6445 0.7906 -0.1460 0.0618  -0.0963 417 LEU B CG  
7529 C CD1 . LEU B 419 ? 0.7276 0.5638 0.7250 -0.1398 0.0622  -0.0877 417 LEU B CD1 
7530 C CD2 . LEU B 419 ? 0.6309 0.5557 0.6957 -0.1421 0.0498  -0.1063 417 LEU B CD2 
7531 N N   . GLU B 420 ? 0.6842 0.5187 0.6531 -0.1539 0.0851  -0.0739 418 GLU B N   
7532 C CA  . GLU B 420 ? 0.6124 0.4564 0.5765 -0.1434 0.0801  -0.0678 418 GLU B CA  
7533 C C   . GLU B 420 ? 0.6024 0.4831 0.5975 -0.1227 0.0620  -0.0676 418 GLU B C   
7534 O O   . GLU B 420 ? 0.5434 0.4290 0.5507 -0.1122 0.0516  -0.0669 418 GLU B O   
7535 C CB  . GLU B 420 ? 0.6985 0.4935 0.6131 -0.1385 0.0758  -0.0517 418 GLU B CB  
7536 C CG  . GLU B 420 ? 0.8898 0.6458 0.7647 -0.1595 0.0957  -0.0505 418 GLU B CG  
7537 C CD  . GLU B 420 ? 0.9696 0.7467 0.8518 -0.1715 0.1119  -0.0596 418 GLU B CD  
7538 O OE1 . GLU B 420 ? 0.9946 0.7792 0.8705 -0.1614 0.1037  -0.0561 418 GLU B OE1 
7539 O OE2 . GLU B 420 ? 0.9970 0.7832 0.8927 -0.1913 0.1337  -0.0709 418 GLU B OE2 
7540 N N   . PRO B 421 ? 0.5838 0.4862 0.5883 -0.1175 0.0601  -0.0684 419 PRO B N   
7541 C CA  . PRO B 421 ? 0.4095 0.3445 0.4424 -0.1001 0.0450  -0.0687 419 PRO B CA  
7542 C C   . PRO B 421 ? 0.5079 0.4307 0.5329 -0.0834 0.0284  -0.0568 419 PRO B C   
7543 O O   . PRO B 421 ? 0.4486 0.3941 0.4980 -0.0716 0.0192  -0.0581 419 PRO B O   
7544 C CB  . PRO B 421 ? 0.4449 0.3892 0.4752 -0.1002 0.0488  -0.0700 419 PRO B CB  
7545 C CG  . PRO B 421 ? 0.4829 0.4187 0.5040 -0.1192 0.0709  -0.0776 419 PRO B CG  
7546 C CD  . PRO B 421 ? 0.5604 0.4549 0.5471 -0.1279 0.0738  -0.0701 419 PRO B CD  
7547 N N   . GLU B 422 ? 0.5375 0.4247 0.5300 -0.0817 0.0245  -0.0447 420 GLU B N   
7548 C CA  . GLU B 422 ? 0.5754 0.4549 0.5680 -0.0644 0.0091  -0.0329 420 GLU B CA  
7549 C C   . GLU B 422 ? 0.5907 0.4656 0.5941 -0.0584 0.0109  -0.0348 420 GLU B C   
7550 O O   . GLU B 422 ? 0.6312 0.5025 0.6409 -0.0423 0.0019  -0.0264 420 GLU B O   
7551 C CB  . GLU B 422 ? 0.5382 0.3805 0.4940 -0.0631 0.0021  -0.0185 420 GLU B CB  
7552 C CG  . GLU B 422 ? 0.7084 0.5077 0.6325 -0.0711 0.0117  -0.0149 420 GLU B CG  
7553 C CD  . GLU B 422 ? 0.8872 0.6477 0.7749 -0.0645 -0.0002 0.0024  420 GLU B CD  
7554 O OE1 . GLU B 422 ? 0.7253 0.4892 0.6258 -0.0455 -0.0167 0.0133  420 GLU B OE1 
7555 O OE2 . GLU B 422 ? 1.0568 0.7834 0.9032 -0.0781 0.0068  0.0056  420 GLU B OE2 
7556 N N   . TYR B 423 ? 0.4890 0.3645 0.4958 -0.0716 0.0227  -0.0465 421 TYR B N   
7557 C CA  . TYR B 423 ? 0.4954 0.3589 0.5037 -0.0702 0.0257  -0.0507 421 TYR B CA  
7558 C C   . TYR B 423 ? 0.5375 0.4347 0.5732 -0.0738 0.0255  -0.0642 421 TYR B C   
7559 O O   . TYR B 423 ? 0.5618 0.4485 0.5948 -0.0768 0.0280  -0.0706 421 TYR B O   
7560 C CB  . TYR B 423 ? 0.5562 0.3796 0.5355 -0.0861 0.0380  -0.0518 421 TYR B CB  
7561 C CG  . TYR B 423 ? 0.6466 0.4279 0.5911 -0.0818 0.0370  -0.0368 421 TYR B CG  
7562 C CD1 . TYR B 423 ? 0.5964 0.3648 0.5381 -0.0599 0.0252  -0.0234 421 TYR B CD1 
7563 C CD2 . TYR B 423 ? 0.7374 0.4917 0.6522 -0.0993 0.0477  -0.0354 421 TYR B CD2 
7564 C CE1 . TYR B 423 ? 0.6755 0.4060 0.5863 -0.0542 0.0203  -0.0082 421 TYR B CE1 
7565 C CE2 . TYR B 423 ? 0.6842 0.3948 0.5603 -0.0952 0.0446  -0.0202 421 TYR B CE2 
7566 C CZ  . TYR B 423 ? 0.6763 0.3755 0.5508 -0.0718 0.0289  -0.0062 421 TYR B CZ  
7567 O OH  . TYR B 423 ? 0.8319 0.4885 0.6690 -0.0659 0.0219  0.0103  421 TYR B OH  
7568 N N   . PHE B 424 ? 0.5499 0.4837 0.6085 -0.0734 0.0219  -0.0686 422 PHE B N   
7569 C CA  . PHE B 424 ? 0.4295 0.3949 0.5134 -0.0746 0.0183  -0.0796 422 PHE B CA  
7570 C C   . PHE B 424 ? 0.3785 0.3441 0.4647 -0.0593 0.0105  -0.0772 422 PHE B C   
7571 O O   . PHE B 424 ? 0.5007 0.4666 0.5873 -0.0626 0.0092  -0.0852 422 PHE B O   
7572 C CB  . PHE B 424 ? 0.4306 0.4305 0.5371 -0.0733 0.0162  -0.0828 422 PHE B CB  
7573 C CG  . PHE B 424 ? 0.4558 0.4612 0.5657 -0.0889 0.0280  -0.0885 422 PHE B CG  
7574 C CD1 . PHE B 424 ? 0.4435 0.4266 0.5382 -0.1059 0.0395  -0.0913 422 PHE B CD1 
7575 C CD2 . PHE B 424 ? 0.5082 0.5392 0.6362 -0.0868 0.0300  -0.0917 422 PHE B CD2 
7576 C CE1 . PHE B 424 ? 0.4585 0.4470 0.5573 -0.1216 0.0542  -0.0969 422 PHE B CE1 
7577 C CE2 . PHE B 424 ? 0.3743 0.4107 0.5072 -0.1004 0.0450  -0.0978 422 PHE B CE2 
7578 C CZ  . PHE B 424 ? 0.4334 0.4500 0.5526 -0.1183 0.0578  -0.1004 422 PHE B CZ  
7579 N N   . ASN B 425 ? 0.4060 0.3716 0.4933 -0.0438 0.0055  -0.0668 423 ASN B N   
7580 C CA  . ASN B 425 ? 0.4095 0.3747 0.5005 -0.0289 0.0022  -0.0633 423 ASN B CA  
7581 C C   . ASN B 425 ? 0.4237 0.3865 0.5183 -0.0158 -0.0018 -0.0500 423 ASN B C   
7582 O O   . ASN B 425 ? 0.4571 0.4172 0.5468 -0.0190 -0.0048 -0.0441 423 ASN B O   
7583 C CB  . ASN B 425 ? 0.3782 0.3703 0.4842 -0.0262 -0.0030 -0.0697 423 ASN B CB  
7584 C CG  . ASN B 425 ? 0.3707 0.3885 0.4929 -0.0246 -0.0082 -0.0678 423 ASN B CG  
7585 O OD1 . ASN B 425 ? 0.3992 0.4188 0.5248 -0.0170 -0.0108 -0.0591 423 ASN B OD1 
7586 N ND2 . ASN B 425 ? 0.3752 0.4130 0.5088 -0.0317 -0.0100 -0.0764 423 ASN B ND2 
7587 N N   . SER B 426 ? 0.4087 0.3731 0.5118 -0.0019 -0.0019 -0.0455 424 SER B N   
7588 C CA  . SER B 426 ? 0.4249 0.3924 0.5396 0.0105  -0.0069 -0.0328 424 SER B CA  
7589 C C   . SER B 426 ? 0.3754 0.3668 0.5021 0.0079  -0.0162 -0.0296 424 SER B C   
7590 O O   . SER B 426 ? 0.4080 0.3979 0.5355 0.0099  -0.0242 -0.0203 424 SER B O   
7591 C CB  . SER B 426 ? 0.4028 0.3723 0.5306 0.0250  -0.0013 -0.0301 424 SER B CB  
7592 O OG  . SER B 426 ? 0.4344 0.3754 0.5467 0.0283  0.0090  -0.0333 424 SER B OG  
7593 N N   . VAL B 427 ? 0.3231 0.3335 0.4567 0.0038  -0.0163 -0.0371 425 VAL B N   
7594 C CA  . VAL B 427 ? 0.3026 0.3300 0.4446 0.0017  -0.0233 -0.0349 425 VAL B CA  
7595 C C   . VAL B 427 ? 0.4171 0.4366 0.5441 -0.0090 -0.0249 -0.0360 425 VAL B C   
7596 O O   . VAL B 427 ? 0.4179 0.4366 0.5410 -0.0106 -0.0321 -0.0301 425 VAL B O   
7597 C CB  . VAL B 427 ? 0.3863 0.4307 0.5369 0.0021  -0.0224 -0.0418 425 VAL B CB  
7598 C CG1 . VAL B 427 ? 0.3710 0.4261 0.5253 -0.0012 -0.0274 -0.0414 425 VAL B CG1 
7599 C CG2 . VAL B 427 ? 0.3627 0.4105 0.5224 0.0119  -0.0194 -0.0388 425 VAL B CG2 
7600 N N   . CYS B 428 ? 0.4111 0.4230 0.5278 -0.0181 -0.0175 -0.0440 426 CYS B N   
7601 C CA  . CYS B 428 ? 0.4749 0.4766 0.5754 -0.0295 -0.0143 -0.0455 426 CYS B CA  
7602 C C   . CYS B 428 ? 0.4431 0.4183 0.5221 -0.0296 -0.0181 -0.0348 426 CYS B C   
7603 O O   . CYS B 428 ? 0.4662 0.4305 0.5268 -0.0359 -0.0207 -0.0315 426 CYS B O   
7604 C CB  . CYS B 428 ? 0.4821 0.4851 0.5823 -0.0407 -0.0037 -0.0565 426 CYS B CB  
7605 S SG  . CYS B 428 ? 0.6793 0.7160 0.8062 -0.0400 -0.0031 -0.0679 426 CYS B SG  
7606 N N   . ARG B 429 ? 0.4107 0.3719 0.4886 -0.0220 -0.0188 -0.0292 427 ARG B N   
7607 C CA  . ARG B 429 ? 0.4590 0.3949 0.5192 -0.0180 -0.0254 -0.0168 427 ARG B CA  
7608 C C   . ARG B 429 ? 0.4455 0.3928 0.5124 -0.0123 -0.0407 -0.0073 427 ARG B C   
7609 O O   . ARG B 429 ? 0.4769 0.4068 0.5199 -0.0173 -0.0488 -0.0003 427 ARG B O   
7610 C CB  . ARG B 429 ? 0.4479 0.3689 0.5120 -0.0063 -0.0228 -0.0123 427 ARG B CB  
7611 C CG  . ARG B 429 ? 0.4882 0.3799 0.5345 0.0006  -0.0301 0.0017  427 ARG B CG  
7612 C CD  . ARG B 429 ? 0.5720 0.4369 0.6126 0.0089  -0.0212 0.0030  427 ARG B CD  
7613 N NE  . ARG B 429 ? 0.7234 0.5570 0.7467 0.0184  -0.0290 0.0179  427 ARG B NE  
7614 C CZ  . ARG B 429 ? 0.8429 0.6460 0.8302 0.0085  -0.0320 0.0236  427 ARG B CZ  
7615 N NH1 . ARG B 429 ? 0.7801 0.5778 0.7458 -0.0123 -0.0227 0.0141  427 ARG B NH1 
7616 N NH2 . ARG B 429 ? 0.8380 0.6134 0.8100 0.0203  -0.0432 0.0396  427 ARG B NH2 
7617 N N   . LEU B 430 ? 0.4157 0.3900 0.5122 -0.0035 -0.0452 -0.0069 428 LEU B N   
7618 C CA  . LEU B 430 ? 0.4145 0.4027 0.5216 -0.0011 -0.0602 0.0010  428 LEU B CA  
7619 C C   . LEU B 430 ? 0.4506 0.4344 0.5357 -0.0147 -0.0633 -0.0033 428 LEU B C   
7620 O O   . LEU B 430 ? 0.4530 0.4255 0.5204 -0.0187 -0.0767 0.0042  428 LEU B O   
7621 C CB  . LEU B 430 ? 0.4669 0.4840 0.6084 0.0066  -0.0596 -0.0003 428 LEU B CB  
7622 C CG  . LEU B 430 ? 0.4709 0.4959 0.6390 0.0217  -0.0576 0.0064  428 LEU B CG  
7623 C CD1 . LEU B 430 ? 0.5725 0.6236 0.7686 0.0249  -0.0537 0.0040  428 LEU B CD1 
7624 C CD2 . LEU B 430 ? 0.5610 0.5832 0.7366 0.0292  -0.0729 0.0205  428 LEU B CD2 
7625 N N   . MET B 431 ? 0.4323 0.4235 0.5170 -0.0214 -0.0512 -0.0155 429 MET B N   
7626 C CA  . MET B 431 ? 0.4470 0.4335 0.5133 -0.0323 -0.0500 -0.0212 429 MET B CA  
7627 C C   . MET B 431 ? 0.4551 0.4110 0.4826 -0.0425 -0.0481 -0.0191 429 MET B C   
7628 O O   . MET B 431 ? 0.5722 0.5152 0.5747 -0.0511 -0.0517 -0.0196 429 MET B O   
7629 C CB  . MET B 431 ? 0.4836 0.4850 0.5622 -0.0341 -0.0363 -0.0340 429 MET B CB  
7630 C CG  . MET B 431 ? 0.4019 0.4269 0.5100 -0.0246 -0.0383 -0.0352 429 MET B CG  
7631 S SD  . MET B 431 ? 0.5347 0.5755 0.6562 -0.0239 -0.0269 -0.0480 429 MET B SD  
7632 C CE  . MET B 431 ? 0.5242 0.5593 0.6331 -0.0296 -0.0256 -0.0523 429 MET B CE  
7633 N N   . LYS B 432 ? 0.5057 0.4448 0.5226 -0.0428 -0.0417 -0.0169 430 LYS B N   
7634 C CA  . LYS B 432 ? 0.5422 0.4468 0.5175 -0.0538 -0.0372 -0.0143 430 LYS B CA  
7635 C C   . LYS B 432 ? 0.6274 0.5082 0.5802 -0.0492 -0.0557 0.0016  430 LYS B C   
7636 O O   . LYS B 432 ? 0.6351 0.4831 0.5443 -0.0587 -0.0574 0.0060  430 LYS B O   
7637 C CB  . LYS B 432 ? 0.4983 0.3926 0.4702 -0.0598 -0.0190 -0.0206 430 LYS B CB  
7638 C CG  . LYS B 432 ? 0.4556 0.3733 0.4481 -0.0667 -0.0024 -0.0360 430 LYS B CG  
7639 C CD  . LYS B 432 ? 0.4815 0.3903 0.4520 -0.0788 0.0090  -0.0425 430 LYS B CD  
7640 C CE  . LYS B 432 ? 0.5786 0.4491 0.5070 -0.0926 0.0205  -0.0398 430 LYS B CE  
7641 N NZ  . LYS B 432 ? 0.5778 0.4381 0.4837 -0.1050 0.0369  -0.0478 430 LYS B NZ  
7642 N N   . THR B 433 ? 0.5473 0.4429 0.5284 -0.0343 -0.0694 0.0107  431 THR B N   
7643 C CA  . THR B 433 ? 0.6107 0.4892 0.5800 -0.0262 -0.0894 0.0271  431 THR B CA  
7644 C C   . THR B 433 ? 0.5899 0.4866 0.5698 -0.0252 -0.1119 0.0331  431 THR B C   
7645 O O   . THR B 433 ? 0.7344 0.6090 0.6791 -0.0323 -0.1276 0.0404  431 THR B O   
7646 C CB  . THR B 433 ? 0.5844 0.4668 0.5812 -0.0090 -0.0890 0.0337  431 THR B CB  
7647 O OG1 . THR B 433 ? 0.5816 0.5022 0.6252 -0.0002 -0.0858 0.0284  431 THR B OG1 
7648 C CG2 . THR B 433 ? 0.6025 0.4579 0.5799 -0.0133 -0.0691 0.0282  431 THR B CG2 
7649 N N   . ILE B 434 ? 0.5548 0.4894 0.5802 -0.0182 -0.1141 0.0302  432 ILE B N   
7650 C CA  . ILE B 434 ? 0.5724 0.5271 0.6132 -0.0200 -0.1345 0.0350  432 ILE B CA  
7651 C C   . ILE B 434 ? 0.5571 0.5138 0.5833 -0.0348 -0.1289 0.0228  432 ILE B C   
7652 O O   . ILE B 434 ? 0.5613 0.5247 0.5869 -0.0416 -0.1458 0.0250  432 ILE B O   
7653 C CB  . ILE B 434 ? 0.5697 0.5626 0.6678 -0.0062 -0.1386 0.0392  432 ILE B CB  
7654 C CG1 . ILE B 434 ? 0.4631 0.4769 0.5843 -0.0067 -0.1186 0.0263  432 ILE B CG1 
7655 C CG2 . ILE B 434 ? 0.6632 0.6523 0.7781 0.0114  -0.1384 0.0493  432 ILE B CG2 
7656 C CD1 . ILE B 434 ? 0.5880 0.6356 0.7593 0.0036  -0.1192 0.0297  432 ILE B CD1 
7657 N N   . GLY B 435 ? 0.5406 0.4919 0.5571 -0.0397 -0.1061 0.0100  433 GLY B N   
7658 C CA  . GLY B 435 ? 0.4784 0.4301 0.4839 -0.0502 -0.0975 -0.0019 433 GLY B CA  
7659 C C   . GLY B 435 ? 0.4815 0.4635 0.5260 -0.0445 -0.0901 -0.0087 433 GLY B C   
7660 O O   . GLY B 435 ? 0.4128 0.4174 0.4929 -0.0344 -0.0944 -0.0035 433 GLY B O   
7661 N N   . PRO B 436 ? 0.4709 0.4512 0.5078 -0.0501 -0.0772 -0.0204 434 PRO B N   
7662 C CA  . PRO B 436 ? 0.4490 0.4516 0.5158 -0.0449 -0.0717 -0.0258 434 PRO B CA  
7663 C C   . PRO B 436 ? 0.4791 0.4883 0.5537 -0.0491 -0.0862 -0.0219 434 PRO B C   
7664 O O   . PRO B 436 ? 0.4863 0.4786 0.5345 -0.0601 -0.0974 -0.0209 434 PRO B O   
7665 C CB  . PRO B 436 ? 0.4661 0.4602 0.5190 -0.0485 -0.0545 -0.0385 434 PRO B CB  
7666 C CG  . PRO B 436 ? 0.5602 0.5250 0.5710 -0.0603 -0.0547 -0.0397 434 PRO B CG  
7667 C CD  . PRO B 436 ? 0.5132 0.4690 0.5135 -0.0604 -0.0647 -0.0290 434 PRO B CD  
7668 N N   . ASP B 437 ? 0.4319 0.4639 0.5407 -0.0422 -0.0858 -0.0199 435 ASP B N   
7669 C CA  . ASP B 437 ? 0.4317 0.4714 0.5518 -0.0487 -0.0963 -0.0174 435 ASP B CA  
7670 C C   . ASP B 437 ? 0.4955 0.5160 0.5904 -0.0581 -0.0911 -0.0272 435 ASP B C   
7671 O O   . ASP B 437 ? 0.5260 0.5365 0.6073 -0.0704 -0.1030 -0.0268 435 ASP B O   
7672 C CB  . ASP B 437 ? 0.4854 0.5494 0.6438 -0.0403 -0.0910 -0.0143 435 ASP B CB  
7673 C CG  . ASP B 437 ? 0.5062 0.5877 0.6915 -0.0305 -0.0948 -0.0049 435 ASP B CG  
7674 O OD1 . ASP B 437 ? 0.6270 0.7153 0.8213 -0.0331 -0.1113 0.0038  435 ASP B OD1 
7675 O OD2 . ASP B 437 ? 0.5226 0.6097 0.7191 -0.0196 -0.0818 -0.0062 435 ASP B OD2 
7676 N N   . MET B 438 ? 0.4849 0.4994 0.5738 -0.0523 -0.0738 -0.0361 436 MET B N   
7677 C CA  . MET B 438 ? 0.4216 0.4175 0.4911 -0.0566 -0.0651 -0.0456 436 MET B CA  
7678 C C   . MET B 438 ? 0.4658 0.4495 0.5171 -0.0538 -0.0498 -0.0544 436 MET B C   
7679 O O   . MET B 438 ? 0.4488 0.4451 0.5130 -0.0463 -0.0429 -0.0545 436 MET B O   
7680 C CB  . MET B 438 ? 0.3602 0.3653 0.4508 -0.0492 -0.0585 -0.0469 436 MET B CB  
7681 C CG  . MET B 438 ? 0.4854 0.5023 0.5955 -0.0545 -0.0693 -0.0390 436 MET B CG  
7682 S SD  . MET B 438 ? 0.4684 0.4949 0.6010 -0.0447 -0.0588 -0.0377 436 MET B SD  
7683 C CE  . MET B 438 ? 0.4247 0.4712 0.5751 -0.0296 -0.0528 -0.0352 436 MET B CE  
7684 N N   . PHE B 439 ? 0.4236 0.3817 0.4453 -0.0608 -0.0430 -0.0626 437 PHE B N   
7685 C CA  . PHE B 439 ? 0.4652 0.4114 0.4708 -0.0595 -0.0251 -0.0718 437 PHE B CA  
7686 C C   . PHE B 439 ? 0.5076 0.4378 0.5051 -0.0563 -0.0111 -0.0821 437 PHE B C   
7687 O O   . PHE B 439 ? 0.5347 0.4412 0.5086 -0.0647 -0.0157 -0.0842 437 PHE B O   
7688 C CB  . PHE B 439 ? 0.5039 0.4254 0.4695 -0.0726 -0.0278 -0.0710 437 PHE B CB  
7689 C CG  . PHE B 439 ? 0.5758 0.4861 0.5260 -0.0732 -0.0061 -0.0795 437 PHE B CG  
7690 C CD1 . PHE B 439 ? 0.5804 0.5074 0.5477 -0.0695 0.0001  -0.0773 437 PHE B CD1 
7691 C CD2 . PHE B 439 ? 0.6263 0.5073 0.5436 -0.0791 0.0098  -0.0900 437 PHE B CD2 
7692 C CE1 . PHE B 439 ? 0.5457 0.4646 0.5024 -0.0727 0.0218  -0.0852 437 PHE B CE1 
7693 C CE2 . PHE B 439 ? 0.5741 0.4467 0.4807 -0.0804 0.0334  -0.0981 437 PHE B CE2 
7694 C CZ  . PHE B 439 ? 0.6029 0.4965 0.5313 -0.0779 0.0393  -0.0955 437 PHE B CZ  
7695 N N   . LEU B 440 ? 0.5232 0.4659 0.5411 -0.0441 0.0053  -0.0886 438 LEU B N   
7696 C CA  . LEU B 440 ? 0.4631 0.3914 0.4775 -0.0369 0.0211  -0.0984 438 LEU B CA  
7697 C C   . LEU B 440 ? 0.5484 0.4553 0.5348 -0.0437 0.0395  -0.1078 438 LEU B C   
7698 O O   . LEU B 440 ? 0.5091 0.4324 0.5113 -0.0404 0.0524  -0.1112 438 LEU B O   
7699 C CB  . LEU B 440 ? 0.4061 0.3622 0.4615 -0.0185 0.0263  -0.0993 438 LEU B CB  
7700 C CG  . LEU B 440 ? 0.4672 0.4406 0.5442 -0.0122 0.0105  -0.0898 438 LEU B CG  
7701 C CD1 . LEU B 440 ? 0.4165 0.4124 0.5260 0.0055  0.0136  -0.0906 438 LEU B CD1 
7702 C CD2 . LEU B 440 ? 0.4735 0.4236 0.5324 -0.0178 0.0030  -0.0867 438 LEU B CD2 
7703 N N   . GLY B 441 ? 0.5621 0.4303 0.5043 -0.0552 0.0417  -0.1125 439 GLY B N   
7704 C CA  . GLY B 441 ? 0.5986 0.4391 0.5027 -0.0650 0.0589  -0.1205 439 GLY B CA  
7705 C C   . GLY B 441 ? 0.6458 0.4703 0.5456 -0.0571 0.0886  -0.1342 439 GLY B C   
7706 O O   . GLY B 441 ? 0.6082 0.4071 0.4734 -0.0662 0.1071  -0.1416 439 GLY B O   
7707 N N   . THR B 442 ? 0.5530 0.3894 0.4856 -0.0396 0.0955  -0.1378 440 THR B N   
7708 C CA  . THR B 442 ? 0.6700 0.4898 0.6013 -0.0291 0.1247  -0.1509 440 THR B CA  
7709 C C   . THR B 442 ? 0.5983 0.4637 0.5926 -0.0082 0.1350  -0.1521 440 THR B C   
7710 O O   . THR B 442 ? 0.5397 0.4278 0.5692 0.0066  0.1217  -0.1463 440 THR B O   
7711 C CB  . THR B 442 ? 0.6344 0.4154 0.5396 -0.0264 0.1254  -0.1554 440 THR B CB  
7712 O OG1 . THR B 442 ? 0.8529 0.5899 0.6964 -0.0491 0.1170  -0.1567 440 THR B OG1 
7713 C CG2 . THR B 442 ? 0.7218 0.4864 0.6318 -0.0107 0.1573  -0.1687 440 THR B CG2 
7714 N N   . CYS B 443 ? 0.5619 0.4397 0.5689 -0.0082 0.1584  -0.1595 441 CYS B N   
7715 C CA  . CYS B 443 ? 0.5033 0.4270 0.5737 0.0097  0.1693  -0.1624 441 CYS B CA  
7716 C C   . CYS B 443 ? 0.5152 0.4267 0.5987 0.0294  0.1900  -0.1718 441 CYS B C   
7717 O O   . CYS B 443 ? 0.6332 0.5027 0.6770 0.0250  0.2132  -0.1819 441 CYS B O   
7718 C CB  . CYS B 443 ? 0.6153 0.5579 0.6971 -0.0008 0.1882  -0.1670 441 CYS B CB  
7719 S SG  . CYS B 443 ? 0.4967 0.5003 0.6620 0.0171  0.2042  -0.1729 441 CYS B SG  
7720 N N   . ARG B 444 ? 0.5536 0.4034 0.6719 -0.1772 -0.0116 0.0196  442 ARG B N   
7721 C CA  . ARG B 444 ? 0.5629 0.3605 0.7134 -0.1827 -0.0285 0.0305  442 ARG B CA  
7722 C C   . ARG B 444 ? 0.5480 0.3216 0.6804 -0.1632 -0.0281 0.0401  442 ARG B C   
7723 O O   . ARG B 444 ? 0.5793 0.3077 0.7458 -0.1615 -0.0442 0.0455  442 ARG B O   
7724 C CB  . ARG B 444 ? 0.5868 0.3837 0.7705 -0.2189 -0.0341 0.0724  442 ARG B CB  
7725 C CG  . ARG B 444 ? 0.6946 0.5147 0.9086 -0.2418 -0.0360 0.0637  442 ARG B CG  
7726 C CD  . ARG B 444 ? 0.7623 0.5762 1.0153 -0.2795 -0.0434 0.1065  442 ARG B CD  
7727 N NE  . ARG B 444 ? 0.8397 0.5959 1.1213 -0.2701 -0.0627 0.1085  442 ARG B NE  
7728 C CZ  . ARG B 444 ? 0.7960 0.5300 1.1208 -0.2796 -0.0768 0.0992  442 ARG B CZ  
7729 N NH1 . ARG B 444 ? 0.7795 0.5443 1.1223 -0.3024 -0.0731 0.0946  442 ARG B NH1 
7730 N NH2 . ARG B 444 ? 0.8862 0.5696 1.2411 -0.2664 -0.0953 0.0951  442 ARG B NH2 
7731 N N   . ARG B 445 ? 0.5137 0.3160 0.6017 -0.1481 -0.0121 0.0406  443 ARG B N   
7732 C CA  . ARG B 445 ? 0.5812 0.3692 0.6527 -0.1327 -0.0113 0.0525  443 ARG B CA  
7733 C C   . ARG B 445 ? 0.5675 0.3440 0.6264 -0.1024 -0.0091 0.0167  443 ARG B C   
7734 O O   . ARG B 445 ? 0.5098 0.2587 0.5829 -0.0892 -0.0160 0.0158  443 ARG B O   
7735 C CB  . ARG B 445 ? 0.4872 0.3174 0.5204 -0.1383 0.0049  0.0743  443 ARG B CB  
7736 C CG  . ARG B 445 ? 0.5691 0.3961 0.5783 -0.1200 0.0080  0.0788  443 ARG B CG  
7737 C CD  . ARG B 445 ? 0.4930 0.3668 0.4651 -0.1196 0.0263  0.0779  443 ARG B CD  
7738 N NE  . ARG B 445 ? 0.4905 0.4000 0.4567 -0.1479 0.0328  0.1032  443 ARG B NE  
7739 C CZ  . ARG B 445 ? 0.5536 0.5127 0.4973 -0.1532 0.0503  0.0970  443 ARG B CZ  
7740 N NH1 . ARG B 445 ? 0.4114 0.3840 0.3438 -0.1318 0.0602  0.0675  443 ARG B NH1 
7741 N NH2 . ARG B 445 ? 0.4648 0.4637 0.4014 -0.1821 0.0579  0.1197  443 ARG B NH2 
7742 N N   . CYS B 446 ? 0.5175 0.3178 0.5543 -0.0927 -0.0010 -0.0114 444 CYS B N   
7743 C CA  . CYS B 446 ? 0.5185 0.3228 0.5310 -0.0688 0.0051  -0.0363 444 CYS B CA  
7744 C C   . CYS B 446 ? 0.5815 0.3721 0.6072 -0.0606 -0.0028 -0.0745 444 CYS B C   
7745 O O   . CYS B 446 ? 0.5352 0.3252 0.5781 -0.0720 -0.0119 -0.0889 444 CYS B O   
7746 C CB  . CYS B 446 ? 0.4674 0.3091 0.4465 -0.0641 0.0164  -0.0381 444 CYS B CB  
7747 S SG  . CYS B 446 ? 0.5176 0.3837 0.4817 -0.0705 0.0287  -0.0085 444 CYS B SG  
7748 N N   . PRO B 447 ? 0.5919 0.3772 0.6110 -0.0422 0.0015  -0.0940 445 PRO B N   
7749 C CA  . PRO B 447 ? 0.6162 0.4046 0.6371 -0.0342 -0.0011 -0.1380 445 PRO B CA  
7750 C C   . PRO B 447 ? 0.5764 0.3993 0.5628 -0.0394 -0.0006 -0.1490 445 PRO B C   
7751 O O   . PRO B 447 ? 0.5435 0.3888 0.5031 -0.0407 0.0051  -0.1258 445 PRO B O   
7752 C CB  . PRO B 447 ? 0.6032 0.3985 0.6124 -0.0150 0.0106  -0.1502 445 PRO B CB  
7753 C CG  . PRO B 447 ? 0.5534 0.3528 0.5464 -0.0133 0.0182  -0.1108 445 PRO B CG  
7754 C CD  . PRO B 447 ? 0.5702 0.3521 0.5830 -0.0295 0.0090  -0.0793 445 PRO B CD  
7755 N N   . ALA B 448 ? 0.5791 0.4075 0.5705 -0.0420 -0.0090 -0.1866 446 ALA B N   
7756 C CA  . ALA B 448 ? 0.6066 0.4699 0.5683 -0.0491 -0.0147 -0.1951 446 ALA B CA  
7757 C C   . ALA B 448 ? 0.6221 0.5192 0.5343 -0.0404 -0.0050 -0.1814 446 ALA B C   
7758 O O   . ALA B 448 ? 0.5816 0.5028 0.4767 -0.0454 -0.0111 -0.1656 446 ALA B O   
7759 C CB  . ALA B 448 ? 0.5679 0.4378 0.5367 -0.0530 -0.0254 -0.2438 446 ALA B CB  
7760 N N   . GLU B 449 ? 0.5641 0.4640 0.4602 -0.0281 0.0085  -0.1853 447 GLU B N   
7761 C CA  . GLU B 449 ? 0.6296 0.5607 0.4829 -0.0234 0.0165  -0.1686 447 GLU B CA  
7762 C C   . GLU B 449 ? 0.6233 0.5509 0.4777 -0.0234 0.0173  -0.1281 447 GLU B C   
7763 O O   . GLU B 449 ? 0.6577 0.6083 0.4902 -0.0242 0.0137  -0.1108 447 GLU B O   
7764 C CB  . GLU B 449 ? 0.5936 0.5305 0.4379 -0.0126 0.0328  -0.1802 447 GLU B CB  
7765 C CG  . GLU B 449 ? 0.6822 0.6269 0.5351 -0.0105 0.0347  -0.2299 447 GLU B CG  
7766 C CD  . GLU B 449 ? 0.7413 0.6472 0.6484 -0.0011 0.0361  -0.2452 447 GLU B CD  
7767 O OE1 . GLU B 449 ? 0.7296 0.5988 0.6715 -0.0057 0.0244  -0.2287 447 GLU B OE1 
7768 O OE2 . GLU B 449 ? 0.8001 0.7152 0.7188 0.0098  0.0479  -0.2729 447 GLU B OE2 
7769 N N   . ILE B 450 ? 0.6073 0.5087 0.4896 -0.0232 0.0209  -0.1130 448 ILE B N   
7770 C CA  . ILE B 450 ? 0.5004 0.4052 0.3853 -0.0240 0.0240  -0.0835 448 ILE B CA  
7771 C C   . ILE B 450 ? 0.5013 0.4194 0.3993 -0.0337 0.0137  -0.0798 448 ILE B C   
7772 O O   . ILE B 450 ? 0.5287 0.4651 0.4255 -0.0316 0.0122  -0.0661 448 ILE B O   
7773 C CB  . ILE B 450 ? 0.5056 0.3885 0.4090 -0.0239 0.0310  -0.0692 448 ILE B CB  
7774 C CG1 . ILE B 450 ? 0.5630 0.4386 0.4597 -0.0123 0.0395  -0.0720 448 ILE B CG1 
7775 C CG2 . ILE B 450 ? 0.5402 0.4349 0.4462 -0.0273 0.0354  -0.0477 448 ILE B CG2 
7776 C CD1 . ILE B 450 ? 0.4761 0.3316 0.3924 -0.0123 0.0410  -0.0567 448 ILE B CD1 
7777 N N   . VAL B 451 ? 0.4653 0.3749 0.3847 -0.0444 0.0054  -0.0930 449 VAL B N   
7778 C CA  . VAL B 451 ? 0.5501 0.4772 0.4890 -0.0555 -0.0040 -0.0908 449 VAL B CA  
7779 C C   . VAL B 451 ? 0.5303 0.4859 0.4521 -0.0522 -0.0164 -0.0968 449 VAL B C   
7780 O O   . VAL B 451 ? 0.5489 0.5264 0.4847 -0.0527 -0.0224 -0.0853 449 VAL B O   
7781 C CB  . VAL B 451 ? 0.5925 0.5033 0.5618 -0.0705 -0.0122 -0.1036 449 VAL B CB  
7782 C CG1 . VAL B 451 ? 0.5017 0.4368 0.4967 -0.0841 -0.0207 -0.1011 449 VAL B CG1 
7783 C CG2 . VAL B 451 ? 0.5505 0.4322 0.5384 -0.0756 -0.0046 -0.0883 449 VAL B CG2 
7784 N N   . ASP B 452 ? 0.5588 0.5190 0.4521 -0.0493 -0.0213 -0.1146 450 ASP B N   
7785 C CA  . ASP B 452 ? 0.6258 0.6183 0.4959 -0.0500 -0.0364 -0.1145 450 ASP B CA  
7786 C C   . ASP B 452 ? 0.5704 0.5743 0.4297 -0.0408 -0.0350 -0.0841 450 ASP B C   
7787 O O   . ASP B 452 ? 0.5334 0.5602 0.3969 -0.0413 -0.0518 -0.0705 450 ASP B O   
7788 C CB  . ASP B 452 ? 0.6067 0.6113 0.4413 -0.0520 -0.0388 -0.1419 450 ASP B CB  
7789 C CG  . ASP B 452 ? 0.7746 0.7720 0.6282 -0.0619 -0.0474 -0.1788 450 ASP B CG  
7790 O OD1 . ASP B 452 ? 0.8137 0.7998 0.7063 -0.0701 -0.0548 -0.1769 450 ASP B OD1 
7791 O OD2 . ASP B 452 ? 0.8851 0.8907 0.7185 -0.0626 -0.0460 -0.2123 450 ASP B OD2 
7792 N N   . THR B 453 ? 0.5452 0.5324 0.3973 -0.0325 -0.0179 -0.0729 451 THR B N   
7793 C CA  . THR B 453 ? 0.5682 0.5619 0.4171 -0.0251 -0.0178 -0.0460 451 THR B CA  
7794 C C   . THR B 453 ? 0.5235 0.5189 0.4143 -0.0220 -0.0217 -0.0347 451 THR B C   
7795 O O   . THR B 453 ? 0.5476 0.5574 0.4527 -0.0179 -0.0361 -0.0187 451 THR B O   
7796 C CB  . THR B 453 ? 0.5701 0.5477 0.4065 -0.0186 0.0009  -0.0406 451 THR B CB  
7797 O OG1 . THR B 453 ? 0.5908 0.5749 0.3955 -0.0206 0.0069  -0.0566 451 THR B OG1 
7798 C CG2 . THR B 453 ? 0.5140 0.4955 0.3528 -0.0132 -0.0010 -0.0136 451 THR B CG2 
7799 N N   . VAL B 454 ? 0.5274 0.5120 0.4419 -0.0248 -0.0099 -0.0430 452 VAL B N   
7800 C CA  . VAL B 454 ? 0.5098 0.5058 0.4634 -0.0228 -0.0076 -0.0386 452 VAL B CA  
7801 C C   . VAL B 454 ? 0.5263 0.5465 0.5101 -0.0285 -0.0227 -0.0451 452 VAL B C   
7802 O O   . VAL B 454 ? 0.5335 0.5732 0.5555 -0.0229 -0.0279 -0.0423 452 VAL B O   
7803 C CB  . VAL B 454 ? 0.5260 0.5123 0.4872 -0.0276 0.0118  -0.0417 452 VAL B CB  
7804 C CG1 . VAL B 454 ? 0.4840 0.4509 0.4214 -0.0207 0.0228  -0.0346 452 VAL B CG1 
7805 C CG2 . VAL B 454 ? 0.4782 0.4562 0.4398 -0.0417 0.0128  -0.0497 452 VAL B CG2 
7806 N N   . SER B 455 ? 0.5601 0.5810 0.5346 -0.0393 -0.0311 -0.0571 453 SER B N   
7807 C CA  . SER B 455 ? 0.5520 0.5993 0.5569 -0.0461 -0.0485 -0.0637 453 SER B CA  
7808 C C   . SER B 455 ? 0.5740 0.6417 0.5847 -0.0364 -0.0704 -0.0503 453 SER B C   
7809 O O   . SER B 455 ? 0.5920 0.6841 0.6496 -0.0331 -0.0814 -0.0482 453 SER B O   
7810 C CB  . SER B 455 ? 0.5241 0.5667 0.5152 -0.0595 -0.0575 -0.0819 453 SER B CB  
7811 O OG  . SER B 455 ? 0.5241 0.5929 0.5517 -0.0694 -0.0730 -0.0898 453 SER B OG  
7812 N N   . ALA B 456 ? 0.5661 0.6272 0.5338 -0.0325 -0.0775 -0.0393 454 ALA B N   
7813 C CA  . ALA B 456 ? 0.6374 0.7170 0.6059 -0.0270 -0.1025 -0.0171 454 ALA B CA  
7814 C C   . ALA B 456 ? 0.6306 0.7017 0.6327 -0.0129 -0.0998 0.0025  454 ALA B C   
7815 O O   . ALA B 456 ? 0.6373 0.7229 0.6763 -0.0057 -0.1230 0.0197  454 ALA B O   
7816 C CB  . ALA B 456 ? 0.5842 0.6680 0.4902 -0.0332 -0.1092 -0.0100 454 ALA B CB  
7817 N N   . LEU B 457 ? 0.5805 0.6282 0.5764 -0.0086 -0.0744 -0.0011 455 LEU B N   
7818 C CA  . LEU B 457 ? 0.5827 0.6201 0.6087 0.0037  -0.0715 0.0121  455 LEU B CA  
7819 C C   . LEU B 457 ? 0.5662 0.6175 0.6592 0.0116  -0.0686 -0.0027 455 LEU B C   
7820 O O   . LEU B 457 ? 0.5263 0.5792 0.6670 0.0240  -0.0808 0.0058  455 LEU B O   
7821 C CB  . LEU B 457 ? 0.5803 0.5933 0.5754 0.0038  -0.0470 0.0103  455 LEU B CB  
7822 C CG  . LEU B 457 ? 0.6459 0.6458 0.6710 0.0142  -0.0412 0.0174  455 LEU B CG  
7823 C CD1 . LEU B 457 ? 0.6645 0.6601 0.6972 0.0180  -0.0637 0.0486  455 LEU B CD1 
7824 C CD2 . LEU B 457 ? 0.5993 0.5811 0.5952 0.0120  -0.0171 0.0106  455 LEU B CD2 
7825 N N   . VAL B 458 ? 0.5359 0.6000 0.6390 0.0039  -0.0527 -0.0255 456 VAL B N   
7826 C CA  . VAL B 458 ? 0.4921 0.5797 0.6551 0.0089  -0.0424 -0.0441 456 VAL B CA  
7827 C C   . VAL B 458 ? 0.4942 0.6137 0.6835 -0.0025 -0.0407 -0.0601 456 VAL B C   
7828 O O   . VAL B 458 ? 0.5171 0.6677 0.7581 -0.0010 -0.0295 -0.0785 456 VAL B O   
7829 C CB  . VAL B 458 ? 0.5476 0.6264 0.7004 0.0082  -0.0139 -0.0558 456 VAL B CB  
7830 C CG1 . VAL B 458 ? 0.4873 0.5424 0.6408 0.0211  -0.0171 -0.0455 456 VAL B CG1 
7831 C CG2 . VAL B 458 ? 0.4871 0.5502 0.5849 -0.0072 0.0021  -0.0545 456 VAL B CG2 
7832 N N   . TYR B 459 ? 0.4950 0.6115 0.6536 -0.0153 -0.0506 -0.0567 457 TYR B N   
7833 C CA  . TYR B 459 ? 0.4652 0.6091 0.6505 -0.0302 -0.0484 -0.0708 457 TYR B CA  
7834 C C   . TYR B 459 ? 0.5407 0.7027 0.7409 -0.0329 -0.0790 -0.0689 457 TYR B C   
7835 O O   . TYR B 459 ? 0.4976 0.6748 0.7086 -0.0491 -0.0811 -0.0796 457 TYR B O   
7836 C CB  . TYR B 459 ? 0.4736 0.5977 0.6200 -0.0485 -0.0301 -0.0739 457 TYR B CB  
7837 C CG  . TYR B 459 ? 0.4952 0.6112 0.6300 -0.0499 -0.0025 -0.0737 457 TYR B CG  
7838 C CD1 . TYR B 459 ? 0.4205 0.5724 0.5954 -0.0511 0.0146  -0.0849 457 TYR B CD1 
7839 C CD2 . TYR B 459 ? 0.4664 0.5455 0.5521 -0.0505 0.0060  -0.0649 457 TYR B CD2 
7840 C CE1 . TYR B 459 ? 0.3959 0.5481 0.5540 -0.0552 0.0383  -0.0861 457 TYR B CE1 
7841 C CE2 . TYR B 459 ? 0.4504 0.5259 0.5247 -0.0530 0.0270  -0.0627 457 TYR B CE2 
7842 C CZ  . TYR B 459 ? 0.4141 0.5268 0.5206 -0.0565 0.0426  -0.0727 457 TYR B CZ  
7843 O OH  . TYR B 459 ? 0.3848 0.5014 0.4741 -0.0616 0.0622  -0.0720 457 TYR B OH  
7844 N N   . ASP B 460 ? 0.5823 0.7446 0.7854 -0.0195 -0.1052 -0.0530 458 ASP B N   
7845 C CA  . ASP B 460 ? 0.5435 0.7294 0.7595 -0.0221 -0.1398 -0.0469 458 ASP B CA  
7846 C C   . ASP B 460 ? 0.5889 0.7713 0.7587 -0.0414 -0.1446 -0.0576 458 ASP B C   
7847 O O   . ASP B 460 ? 0.5145 0.7243 0.7078 -0.0511 -0.1647 -0.0665 458 ASP B O   
7848 C CB  . ASP B 460 ? 0.6165 0.8446 0.9173 -0.0177 -0.1496 -0.0577 458 ASP B CB  
7849 C CG  . ASP B 460 ? 0.7626 0.9965 1.1224 0.0044  -0.1501 -0.0538 458 ASP B CG  
7850 O OD1 . ASP B 460 ? 0.8448 1.0621 1.1999 0.0173  -0.1732 -0.0288 458 ASP B OD1 
7851 O OD2 . ASP B 460 ? 0.8873 1.1446 1.3009 0.0075  -0.1276 -0.0764 458 ASP B OD2 
7852 N N   . ASN B 461 ? 0.5641 0.7136 0.6744 -0.0467 -0.1272 -0.0603 459 ASN B N   
7853 C CA  . ASN B 461 ? 0.6320 0.7739 0.7017 -0.0621 -0.1318 -0.0765 459 ASN B CA  
7854 C C   . ASN B 461 ? 0.5525 0.7022 0.6589 -0.0789 -0.1266 -0.0969 459 ASN B C   
7855 O O   . ASN B 461 ? 0.6188 0.7764 0.7200 -0.0924 -0.1429 -0.1137 459 ASN B O   
7856 C CB  . ASN B 461 ? 0.6215 0.7860 0.6629 -0.0646 -0.1647 -0.0716 459 ASN B CB  
7857 C CG  . ASN B 461 ? 0.6997 0.8564 0.6933 -0.0552 -0.1683 -0.0475 459 ASN B CG  
7858 O OD1 . ASN B 461 ? 0.6598 0.7951 0.6045 -0.0565 -0.1503 -0.0529 459 ASN B OD1 
7859 N ND2 . ASN B 461 ? 0.7183 0.8937 0.7326 -0.0464 -0.1926 -0.0191 459 ASN B ND2 
7860 N N   . LYS B 462 ? 0.5597 0.7104 0.7034 -0.0809 -0.1038 -0.0962 460 LYS B N   
7861 C CA  . LYS B 462 ? 0.5293 0.6922 0.7116 -0.1011 -0.0971 -0.1083 460 LYS B CA  
7862 C C   . LYS B 462 ? 0.5581 0.6875 0.7231 -0.1129 -0.0723 -0.1073 460 LYS B C   
7863 O O   . LYS B 462 ? 0.5526 0.6856 0.7464 -0.1340 -0.0681 -0.1118 460 LYS B O   
7864 C CB  . LYS B 462 ? 0.5464 0.7539 0.7943 -0.1003 -0.0914 -0.1076 460 LYS B CB  
7865 C CG  . LYS B 462 ? 0.5757 0.8185 0.8598 -0.0868 -0.1196 -0.1062 460 LYS B CG  
7866 C CD  . LYS B 462 ? 0.5304 0.8245 0.8944 -0.0907 -0.1148 -0.1156 460 LYS B CD  
7867 C CE  . LYS B 462 ? 0.5050 0.8074 0.8851 -0.0914 -0.0769 -0.1186 460 LYS B CE  
7868 N NZ  . LYS B 462 ? 0.6209 0.9076 0.9887 -0.0668 -0.0697 -0.1124 460 LYS B NZ  
7869 N N   . LEU B 463 ? 0.4822 0.5805 0.6061 -0.1013 -0.0581 -0.0985 461 LEU B N   
7870 C CA  . LEU B 463 ? 0.5185 0.5833 0.6271 -0.1110 -0.0404 -0.0941 461 LEU B CA  
7871 C C   . LEU B 463 ? 0.5460 0.5776 0.6288 -0.1138 -0.0522 -0.1088 461 LEU B C   
7872 O O   . LEU B 463 ? 0.5013 0.5270 0.5475 -0.1003 -0.0602 -0.1160 461 LEU B O   
7873 C CB  . LEU B 463 ? 0.4892 0.5410 0.5724 -0.0972 -0.0211 -0.0802 461 LEU B CB  
7874 C CG  . LEU B 463 ? 0.4909 0.5110 0.5591 -0.1060 -0.0062 -0.0702 461 LEU B CG  
7875 C CD1 . LEU B 463 ? 0.4584 0.4936 0.5600 -0.1308 0.0023  -0.0609 461 LEU B CD1 
7876 C CD2 . LEU B 463 ? 0.4921 0.5050 0.5346 -0.0918 0.0091  -0.0590 461 LEU B CD2 
7877 N N   . LYS B 464 ? 0.4870 0.4997 0.5924 -0.1326 -0.0532 -0.1143 462 LYS B N   
7878 C CA  . LYS B 464 ? 0.5742 0.5546 0.6705 -0.1357 -0.0648 -0.1367 462 LYS B CA  
7879 C C   . LYS B 464 ? 0.5412 0.4784 0.6332 -0.1348 -0.0522 -0.1271 462 LYS B C   
7880 O O   . LYS B 464 ? 0.4938 0.4275 0.5973 -0.1423 -0.0385 -0.1002 462 LYS B O   
7881 C CB  . LYS B 464 ? 0.5285 0.5139 0.6673 -0.1577 -0.0821 -0.1540 462 LYS B CB  
7882 C CG  . LYS B 464 ? 0.6833 0.7175 0.8394 -0.1613 -0.0966 -0.1591 462 LYS B CG  
7883 C CD  . LYS B 464 ? 0.7188 0.7714 0.8328 -0.1445 -0.1120 -0.1733 462 LYS B CD  
7884 C CE  . LYS B 464 ? 0.7845 0.8866 0.9199 -0.1442 -0.1291 -0.1684 462 LYS B CE  
7885 N NZ  . LYS B 464 ? 0.9102 1.0329 1.0040 -0.1333 -0.1505 -0.1760 462 LYS B NZ  
7886 N N   . ALA B 465 ? 0.5502 0.4599 0.6268 -0.1260 -0.0576 -0.1503 463 ALA B N   
7887 C CA  . ALA B 465 ? 0.5672 0.4357 0.6484 -0.1215 -0.0498 -0.1443 463 ALA B CA  
7888 C C   . ALA B 465 ? 0.6044 0.4376 0.7366 -0.1387 -0.0628 -0.1545 463 ALA B C   
7889 O O   . ALA B 465 ? 0.6568 0.4929 0.8108 -0.1486 -0.0785 -0.1839 463 ALA B O   
7890 C CB  . ALA B 465 ? 0.5924 0.4547 0.6374 -0.1000 -0.0457 -0.1664 463 ALA B CB  
7891 N N   . HIS B 466 ? 0.6443 0.4439 0.7988 -0.1434 -0.0589 -0.1284 464 HIS B N   
7892 C CA  . HIS B 466 ? 0.7221 0.4776 0.9335 -0.1583 -0.0742 -0.1311 464 HIS B CA  
7893 C C   . HIS B 466 ? 0.7451 0.4641 0.9663 -0.1379 -0.0789 -0.1613 464 HIS B C   
7894 O O   . HIS B 466 ? 0.7800 0.4794 1.0340 -0.1377 -0.0921 -0.1960 464 HIS B O   
7895 C CB  . HIS B 466 ? 0.7038 0.4468 0.9386 -0.1789 -0.0713 -0.0776 464 HIS B CB  
7896 C CG  . HIS B 466 ? 0.7027 0.4000 1.0015 -0.1981 -0.0902 -0.0684 464 HIS B CG  
7897 N ND1 . HIS B 466 ? 0.8245 0.5178 1.1521 -0.2050 -0.1029 -0.0969 464 HIS B ND1 
7898 C CD2 . HIS B 466 ? 0.7639 0.4345 1.0803 -0.2026 -0.0932 -0.0283 464 HIS B CD2 
7899 C CE1 . HIS B 466 ? 0.7803 0.4417 1.1467 -0.2132 -0.1127 -0.0759 464 HIS B CE1 
7900 N NE2 . HIS B 466 ? 0.7478 0.3958 1.1082 -0.2115 -0.1079 -0.0334 464 HIS B NE2 
7901 N N   . LYS B 467 ? 0.6798 0.3986 0.8699 -0.1184 -0.0656 -0.1486 465 LYS B N   
7902 C CA  . LYS B 467 ? 0.7286 0.4218 0.9314 -0.0971 -0.0665 -0.1768 465 LYS B CA  
7903 C C   . LYS B 467 ? 0.7513 0.4759 0.9181 -0.0824 -0.0610 -0.2289 465 LYS B C   
7904 O O   . LYS B 467 ? 0.7335 0.4990 0.8555 -0.0854 -0.0562 -0.2296 465 LYS B O   
7905 C CB  . LYS B 467 ? 0.6211 0.3124 0.8023 -0.0831 -0.0541 -0.1440 465 LYS B CB  
7906 C CG  . LYS B 467 ? 0.6807 0.3495 0.8867 -0.0989 -0.0602 -0.0891 465 LYS B CG  
7907 C CD  . LYS B 467 ? 0.6281 0.2990 0.8115 -0.0836 -0.0509 -0.0642 465 LYS B CD  
7908 C CE  . LYS B 467 ? 0.6961 0.3474 0.9025 -0.1008 -0.0611 -0.0088 465 LYS B CE  
7909 N NZ  . LYS B 467 ? 0.6541 0.3057 0.8464 -0.0855 -0.0576 0.0114  465 LYS B NZ  
7910 N N   . ASP B 468 ? 0.6587 0.3759 0.8387 -0.0651 -0.0601 -0.2630 466 ASP B N   
7911 C CA  . ASP B 468 ? 0.6677 0.4263 0.8048 -0.0533 -0.0513 -0.3056 466 ASP B CA  
7912 C C   . ASP B 468 ? 0.7314 0.5099 0.8274 -0.0368 -0.0324 -0.3004 466 ASP B C   
7913 O O   . ASP B 468 ? 0.7354 0.4981 0.8324 -0.0339 -0.0266 -0.2621 466 ASP B O   
7914 C CB  . ASP B 468 ? 0.7419 0.4987 0.9120 -0.0448 -0.0561 -0.3445 466 ASP B CB  
7915 C CG  . ASP B 468 ? 0.9459 0.6826 1.1603 -0.0613 -0.0750 -0.3510 466 ASP B CG  
7916 O OD1 . ASP B 468 ? 0.9280 0.6853 1.1205 -0.0769 -0.0820 -0.3559 466 ASP B OD1 
7917 O OD2 . ASP B 468 ? 1.0131 0.7157 1.2877 -0.0586 -0.0843 -0.3506 466 ASP B OD2 
7918 N N   . LYS B 469 ? 0.7373 0.5588 0.7914 -0.0278 -0.0217 -0.3294 467 LYS B N   
7919 C CA  . LYS B 469 ? 0.7040 0.5487 0.7223 -0.0142 -0.0026 -0.3225 467 LYS B CA  
7920 C C   . LYS B 469 ? 0.6905 0.5085 0.7557 0.0015  0.0019  -0.3203 467 LYS B C   
7921 O O   . LYS B 469 ? 0.6669 0.4683 0.7813 0.0058  -0.0063 -0.3406 467 LYS B O   
7922 C CB  . LYS B 469 ? 0.7739 0.6745 0.7416 -0.0124 0.0072  -0.3477 467 LYS B CB  
7923 C CG  . LYS B 469 ? 0.7693 0.7059 0.6796 -0.0257 0.0025  -0.3366 467 LYS B CG  
7924 C CD  . LYS B 469 ? 0.8416 0.8335 0.7041 -0.0267 0.0095  -0.3539 467 LYS B CD  
7925 C CE  . LYS B 469 ? 0.8750 0.9044 0.6810 -0.0396 0.0007  -0.3322 467 LYS B CE  
7926 N NZ  . LYS B 469 ? 0.9910 1.0294 0.7655 -0.0371 0.0107  -0.2927 467 LYS B NZ  
7927 N N   . SER B 470 ? 0.6936 0.5092 0.7481 0.0099  0.0133  -0.2954 468 SER B N   
7928 C CA  . SER B 470 ? 0.6915 0.4856 0.7914 0.0247  0.0145  -0.2880 468 SER B CA  
7929 C C   . SER B 470 ? 0.6081 0.4432 0.6961 0.0391  0.0323  -0.3118 468 SER B C   
7930 O O   . SER B 470 ? 0.6249 0.4515 0.7623 0.0520  0.0310  -0.3209 468 SER B O   
7931 C CB  . SER B 470 ? 0.6670 0.4376 0.7675 0.0237  0.0139  -0.2396 468 SER B CB  
7932 O OG  . SER B 470 ? 0.6858 0.4937 0.7264 0.0237  0.0300  -0.2190 468 SER B OG  
7933 N N   . ALA B 471 ? 0.6634 0.5457 0.6906 0.0352  0.0474  -0.3182 469 ALA B N   
7934 C CA  . ALA B 471 ? 0.6630 0.5913 0.6719 0.0430  0.0665  -0.3316 469 ALA B CA  
7935 C C   . ALA B 471 ? 0.6910 0.6140 0.7129 0.0538  0.0762  -0.3073 469 ALA B C   
7936 O O   . ALA B 471 ? 0.7842 0.7382 0.8143 0.0621  0.0899  -0.3193 469 ALA B O   
7937 C CB  . ALA B 471 ? 0.6573 0.6014 0.7057 0.0499  0.0672  -0.3749 469 ALA B CB  
7938 N N   . GLN B 472 ? 0.6333 0.5205 0.6603 0.0524  0.0693  -0.2744 470 GLN B N   
7939 C CA  . GLN B 472 ? 0.6472 0.5295 0.6853 0.0605  0.0758  -0.2471 470 GLN B CA  
7940 C C   . GLN B 472 ? 0.5822 0.4733 0.5674 0.0487  0.0780  -0.1997 470 GLN B C   
7941 O O   . GLN B 472 ? 0.5831 0.4598 0.5761 0.0499  0.0744  -0.1650 470 GLN B O   
7942 C CB  . GLN B 472 ? 0.6657 0.4994 0.7675 0.0681  0.0570  -0.2313 470 GLN B CB  
7943 C CG  . GLN B 472 ? 0.6880 0.5168 0.8472 0.0788  0.0489  -0.2621 470 GLN B CG  
7944 C CD  . GLN B 472 ? 0.7557 0.5412 0.9800 0.0852  0.0268  -0.2377 470 GLN B CD  
7945 O OE1 . GLN B 472 ? 0.7677 0.5525 1.0108 0.0939  0.0258  -0.2163 470 GLN B OE1 
7946 N NE2 . GLN B 472 ? 0.7510 0.5036 1.0113 0.0792  0.0071  -0.2378 470 GLN B NE2 
7947 N N   . CYS B 473 ? 0.5880 0.5029 0.5240 0.0373  0.0811  -0.1991 471 CYS B N   
7948 C CA  . CYS B 473 ? 0.5775 0.5019 0.4730 0.0279  0.0815  -0.1599 471 CYS B CA  
7949 C C   . CYS B 473 ? 0.5790 0.5484 0.4383 0.0254  0.0972  -0.1609 471 CYS B C   
7950 O O   . CYS B 473 ? 0.5729 0.5741 0.4028 0.0188  0.1007  -0.1819 471 CYS B O   
7951 C CB  . CYS B 473 ? 0.5829 0.4996 0.4611 0.0164  0.0681  -0.1524 471 CYS B CB  
7952 S SG  . CYS B 473 ? 0.5908 0.4615 0.5118 0.0129  0.0516  -0.1451 471 CYS B SG  
7953 N N   . PHE B 474 ? 0.5947 0.5705 0.4559 0.0279  0.1057  -0.1375 472 PHE B N   
7954 C CA  . PHE B 474 ? 0.5585 0.5777 0.3942 0.0229  0.1217  -0.1344 472 PHE B CA  
7955 C C   . PHE B 474 ? 0.5511 0.5686 0.3686 0.0146  0.1182  -0.0908 472 PHE B C   
7956 O O   . PHE B 474 ? 0.4323 0.4181 0.2646 0.0166  0.1076  -0.0701 472 PHE B O   
7957 C CB  . PHE B 474 ? 0.4656 0.5007 0.3350 0.0334  0.1370  -0.1534 472 PHE B CB  
7958 C CG  . PHE B 474 ? 0.5087 0.5433 0.4127 0.0451  0.1393  -0.2011 472 PHE B CG  
7959 C CD1 . PHE B 474 ? 0.5128 0.5813 0.4016 0.0415  0.1433  -0.2254 472 PHE B CD1 
7960 C CD2 . PHE B 474 ? 0.4781 0.4710 0.4356 0.0584  0.1268  -0.2057 472 PHE B CD2 
7961 C CE1 . PHE B 474 ? 0.6244 0.6873 0.5533 0.0516  0.1397  -0.2637 472 PHE B CE1 
7962 C CE2 . PHE B 474 ? 0.5222 0.5073 0.5234 0.0694  0.1222  -0.2429 472 PHE B CE2 
7963 C CZ  . PHE B 474 ? 0.6354 0.6553 0.6229 0.0659  0.1283  -0.2717 472 PHE B CZ  
7964 N N   . LYS B 475 ? 0.4679 0.5228 0.2554 0.0035  0.1268  -0.0778 473 LYS B N   
7965 C CA  . LYS B 475 ? 0.4332 0.4851 0.2123 -0.0053 0.1210  -0.0363 473 LYS B CA  
7966 C C   . LYS B 475 ? 0.5838 0.6770 0.3514 -0.0161 0.1370  -0.0236 473 LYS B C   
7967 O O   . LYS B 475 ? 0.4831 0.6173 0.2294 -0.0219 0.1489  -0.0411 473 LYS B O   
7968 C CB  . LYS B 475 ? 0.4506 0.4993 0.2049 -0.0139 0.1035  -0.0168 473 LYS B CB  
7969 C CG  . LYS B 475 ? 0.5163 0.6079 0.2275 -0.0261 0.1043  -0.0241 473 LYS B CG  
7970 C CD  . LYS B 475 ? 0.4980 0.5867 0.1914 -0.0342 0.0812  0.0019  473 LYS B CD  
7971 C CE  . LYS B 475 ? 0.5807 0.7191 0.2258 -0.0503 0.0785  0.0036  473 LYS B CE  
7972 N NZ  . LYS B 475 ? 0.5630 0.7019 0.1941 -0.0581 0.0512  0.0315  473 LYS B NZ  
7973 N N   . MET B 476 ? 0.5252 0.6076 0.3116 -0.0196 0.1356  0.0062  474 MET B N   
7974 C CA  . MET B 476 ? 0.5853 0.7042 0.3666 -0.0343 0.1485  0.0273  474 MET B CA  
7975 C C   . MET B 476 ? 0.6279 0.7258 0.4161 -0.0446 0.1321  0.0717  474 MET B C   
7976 O O   . MET B 476 ? 0.4777 0.5333 0.2907 -0.0353 0.1172  0.0761  474 MET B O   
7977 C CB  . MET B 476 ? 0.5518 0.6804 0.3695 -0.0276 0.1644  0.0129  474 MET B CB  
7978 C CG  . MET B 476 ? 0.7562 0.9052 0.5848 -0.0146 0.1792  -0.0328 474 MET B CG  
7979 S SD  . MET B 476 ? 1.0572 1.2149 0.9421 -0.0046 0.1909  -0.0435 474 MET B SD  
7980 C CE  . MET B 476 ? 0.4313 0.6205 0.3107 -0.0289 0.1996  -0.0016 474 MET B CE  
7981 N N   . PHE B 477 ? 0.4868 0.6147 0.2574 -0.0642 0.1338  0.1034  475 PHE B N   
7982 C CA  . PHE B 477 ? 0.4957 0.6023 0.2848 -0.0754 0.1161  0.1486  475 PHE B CA  
7983 C C   . PHE B 477 ? 0.5871 0.7029 0.4067 -0.0848 0.1273  0.1614  475 PHE B C   
7984 O O   . PHE B 477 ? 0.5264 0.6768 0.3347 -0.0966 0.1392  0.1637  475 PHE B O   
7985 C CB  . PHE B 477 ? 0.5373 0.6539 0.2992 -0.0873 0.0987  0.1738  475 PHE B CB  
7986 C CG  . PHE B 477 ? 0.6137 0.7043 0.4047 -0.0965 0.0750  0.2192  475 PHE B CG  
7987 C CD1 . PHE B 477 ? 0.5323 0.5837 0.3495 -0.0869 0.0532  0.2305  475 PHE B CD1 
7988 C CD2 . PHE B 477 ? 0.5942 0.7013 0.3909 -0.1143 0.0723  0.2496  475 PHE B CD2 
7989 C CE1 . PHE B 477 ? 0.6172 0.6412 0.4753 -0.0916 0.0287  0.2655  475 PHE B CE1 
7990 C CE2 . PHE B 477 ? 0.6142 0.6944 0.4469 -0.1215 0.0470  0.2891  475 PHE B CE2 
7991 C CZ  . PHE B 477 ? 0.6156 0.6527 0.4824 -0.1086 0.0245  0.2946  475 PHE B CZ  
7992 N N   . TYR B 478 ? 0.4746 0.5568 0.3380 -0.0780 0.1211  0.1641  476 TYR B N   
7993 C CA  . TYR B 478 ? 0.5725 0.6639 0.4715 -0.0881 0.1299  0.1753  476 TYR B CA  
7994 C C   . TYR B 478 ? 0.5083 0.5514 0.4551 -0.0854 0.1090  0.1875  476 TYR B C   
7995 O O   . TYR B 478 ? 0.5029 0.5164 0.4672 -0.0675 0.1027  0.1591  476 TYR B O   
7996 C CB  . TYR B 478 ? 0.4671 0.5777 0.3768 -0.0756 0.1496  0.1367  476 TYR B CB  
7997 C CG  . TYR B 478 ? 0.4327 0.5622 0.3817 -0.0855 0.1599  0.1435  476 TYR B CG  
7998 C CD1 . TYR B 478 ? 0.5441 0.7191 0.4883 -0.1060 0.1757  0.1598  476 TYR B CD1 
7999 C CD2 . TYR B 478 ? 0.4222 0.5247 0.4122 -0.0745 0.1518  0.1283  476 TYR B CD2 
8000 C CE1 . TYR B 478 ? 0.4824 0.6769 0.4678 -0.1161 0.1849  0.1643  476 TYR B CE1 
8001 C CE2 . TYR B 478 ? 0.4514 0.5735 0.4810 -0.0840 0.1588  0.1324  476 TYR B CE2 
8002 C CZ  . TYR B 478 ? 0.4282 0.5989 0.4593 -0.1055 0.1770  0.1529  476 TYR B CZ  
8003 O OH  . TYR B 478 ? 0.5778 0.7711 0.6548 -0.1165 0.1840  0.1569  476 TYR B OH  
8004 N N   . LYS B 479 ? 0.4757 0.5135 0.4456 -0.1047 0.0978  0.2290  477 LYS B N   
8005 C CA  . LYS B 479 ? 0.5755 0.5663 0.6006 -0.1021 0.0759  0.2360  477 LYS B CA  
8006 C C   . LYS B 479 ? 0.5885 0.5740 0.6529 -0.0987 0.0824  0.2115  477 LYS B C   
8007 O O   . LYS B 479 ? 0.5184 0.4712 0.6137 -0.0858 0.0703  0.1870  477 LYS B O   
8008 C CB  . LYS B 479 ? 0.6480 0.6300 0.6929 -0.1190 0.0566  0.2749  477 LYS B CB  
8009 C CG  . LYS B 479 ? 0.7231 0.7132 0.7304 -0.1206 0.0440  0.2948  477 LYS B CG  
8010 C CD  . LYS B 479 ? 0.6512 0.5988 0.6976 -0.1111 0.0134  0.3057  477 LYS B CD  
8011 C CE  . LYS B 479 ? 0.6698 0.6326 0.6833 -0.1151 -0.0016 0.3297  477 LYS B CE  
8012 N NZ  . LYS B 479 ? 0.7756 0.7027 0.8325 -0.1030 -0.0317 0.3369  477 LYS B NZ  
8013 N N   . GLY B 480 ? 0.5364 0.5606 0.6001 -0.1108 0.1018  0.2148  478 GLY B N   
8014 C CA  . GLY B 480 ? 0.4278 0.4547 0.5302 -0.1091 0.1063  0.1934  478 GLY B CA  
8015 C C   . GLY B 480 ? 0.4416 0.4394 0.6042 -0.1223 0.0884  0.2095  478 GLY B C   
8016 O O   . GLY B 480 ? 0.4786 0.4677 0.6560 -0.1394 0.0775  0.2453  478 GLY B O   
8017 N N   . VAL B 481 ? 0.4868 0.4706 0.6822 -0.1133 0.0821  0.1774  479 VAL B N   
8018 C CA  . VAL B 481 ? 0.4712 0.4277 0.7300 -0.1241 0.0643  0.1790  479 VAL B CA  
8019 C C   . VAL B 481 ? 0.4422 0.3672 0.7119 -0.1046 0.0495  0.1372  479 VAL B C   
8020 O O   . VAL B 481 ? 0.3956 0.3344 0.6415 -0.0906 0.0552  0.1044  479 VAL B O   
8021 C CB  . VAL B 481 ? 0.4313 0.4169 0.7256 -0.1391 0.0723  0.1778  479 VAL B CB  
8022 C CG1 . VAL B 481 ? 0.4943 0.4495 0.8548 -0.1464 0.0513  0.1637  479 VAL B CG1 
8023 C CG2 . VAL B 481 ? 0.5006 0.5210 0.7912 -0.1630 0.0864  0.2200  479 VAL B CG2 
8024 N N   . ILE B 482 ? 0.5234 0.4099 0.8320 -0.1047 0.0299  0.1387  480 ILE B N   
8025 C CA  . ILE B 482 ? 0.5033 0.3674 0.8265 -0.0878 0.0182  0.0947  480 ILE B CA  
8026 C C   . ILE B 482 ? 0.4306 0.2842 0.8158 -0.0960 0.0056  0.0685  480 ILE B C   
8027 O O   . ILE B 482 ? 0.4609 0.2940 0.9045 -0.1113 -0.0073 0.0891  480 ILE B O   
8028 C CB  . ILE B 482 ? 0.5241 0.3569 0.8613 -0.0789 0.0043  0.1024  480 ILE B CB  
8029 C CG1 . ILE B 482 ? 0.4730 0.3198 0.7470 -0.0719 0.0146  0.1247  480 ILE B CG1 
8030 C CG2 . ILE B 482 ? 0.4624 0.2815 0.8232 -0.0628 -0.0043 0.0503  480 ILE B CG2 
8031 C CD1 . ILE B 482 ? 0.5746 0.3957 0.8662 -0.0660 -0.0022 0.1422  480 ILE B CD1 
8032 N N   . THR B 483 ? 0.4113 0.2815 0.7834 -0.0875 0.0074  0.0243  481 THR B N   
8033 C CA  . THR B 483 ? 0.4618 0.3277 0.8862 -0.0940 -0.0060 -0.0124 481 THR B CA  
8034 C C   . THR B 483 ? 0.5016 0.3629 0.9231 -0.0788 -0.0117 -0.0625 481 THR B C   
8035 O O   . THR B 483 ? 0.4202 0.2922 0.7887 -0.0649 -0.0021 -0.0687 481 THR B O   
8036 C CB  . THR B 483 ? 0.4262 0.3284 0.8398 -0.1020 -0.0013 -0.0223 481 THR B CB  
8037 O OG1 . THR B 483 ? 0.4655 0.3958 0.8111 -0.0890 0.0117  -0.0252 481 THR B OG1 
8038 C CG2 . THR B 483 ? 0.4215 0.3323 0.8640 -0.1213 0.0032  0.0187  481 THR B CG2 
8039 N N   . HIS B 484 ? 0.5270 0.3757 1.0092 -0.0831 -0.0266 -0.1011 482 HIS B N   
8040 C CA  . HIS B 484 ? 0.5296 0.3831 1.0163 -0.0695 -0.0299 -0.1547 482 HIS B CA  
8041 C C   . HIS B 484 ? 0.6203 0.5057 1.1104 -0.0755 -0.0348 -0.2042 482 HIS B C   
8042 O O   . HIS B 484 ? 0.5669 0.4525 1.0934 -0.0866 -0.0445 -0.2022 482 HIS B O   
8043 C CB  . HIS B 484 ? 0.5877 0.4192 1.1277 -0.0575 -0.0422 -0.1533 482 HIS B CB  
8044 C CG  . HIS B 484 ? 0.6089 0.4155 1.1448 -0.0524 -0.0428 -0.1036 482 HIS B CG  
8045 N ND1 . HIS B 484 ? 0.5217 0.3286 1.0335 -0.0376 -0.0374 -0.1092 482 HIS B ND1 
8046 C CD2 . HIS B 484 ? 0.5283 0.3157 1.0781 -0.0617 -0.0493 -0.0470 482 HIS B CD2 
8047 C CE1 . HIS B 484 ? 0.5918 0.3788 1.1035 -0.0374 -0.0425 -0.0586 482 HIS B CE1 
8048 N NE2 . HIS B 484 ? 0.5691 0.3463 1.0999 -0.0526 -0.0494 -0.0197 482 HIS B NE2 
8049 N N   . ASP B 485 ? 0.7113 0.6289 1.1590 -0.0695 -0.0281 -0.2463 483 ASP B N   
8050 C CA  . ASP B 485 ? 0.7472 0.7046 1.1886 -0.0747 -0.0331 -0.2940 483 ASP B CA  
8051 C C   . ASP B 485 ? 0.7120 0.6813 1.1786 -0.0605 -0.0320 -0.3345 483 ASP B C   
8052 O O   . ASP B 485 ? 0.7939 0.7335 1.3073 -0.0488 -0.0349 -0.3218 483 ASP B O   
8053 C CB  . ASP B 485 ? 0.6699 0.6703 1.0364 -0.0817 -0.0270 -0.2996 483 ASP B CB  
8054 C CG  . ASP B 485 ? 0.6989 0.7076 1.0056 -0.0691 -0.0112 -0.2844 483 ASP B CG  
8055 O OD1 . ASP B 485 ? 0.7845 0.8008 1.0977 -0.0623 -0.0058 -0.3219 483 ASP B OD1 
8056 O OD2 . ASP B 485 ? 0.8256 0.8356 1.0842 -0.0665 -0.0043 -0.2385 483 ASP B OD2 
8057 N N   . VAL B 486 ? 0.7262 0.7445 1.1656 -0.0626 -0.0285 -0.3801 484 VAL B N   
8058 C CA  . VAL B 486 ? 0.6436 0.6832 1.1195 -0.0517 -0.0258 -0.4227 484 VAL B CA  
8059 C C   . VAL B 486 ? 0.6712 0.7100 1.1394 -0.0380 -0.0140 -0.4168 484 VAL B C   
8060 O O   . VAL B 486 ? 0.7950 0.8185 1.3261 -0.0256 -0.0183 -0.4239 484 VAL B O   
8061 C CB  . VAL B 486 ? 0.6911 0.7925 1.1335 -0.0607 -0.0223 -0.4698 484 VAL B CB  
8062 C CG1 . VAL B 486 ? 0.6159 0.7487 1.0998 -0.0508 -0.0159 -0.5173 484 VAL B CG1 
8063 C CG2 . VAL B 486 ? 0.7173 0.8185 1.1775 -0.0736 -0.0375 -0.4776 484 VAL B CG2 
8064 N N   . SER B 487 ? 0.7116 0.7687 1.1069 -0.0406 -0.0011 -0.4031 485 SER B N   
8065 C CA  . SER B 487 ? 0.6771 0.7410 1.0619 -0.0296 0.0108  -0.4002 485 SER B CA  
8066 C C   . SER B 487 ? 0.7244 0.7581 1.0656 -0.0275 0.0165  -0.3552 485 SER B C   
8067 O O   . SER B 487 ? 0.7961 0.8385 1.1205 -0.0198 0.0266  -0.3512 485 SER B O   
8068 C CB  . SER B 487 ? 0.7740 0.9050 1.1169 -0.0350 0.0248  -0.4357 485 SER B CB  
8069 O OG  . SER B 487 ? 0.9300 1.0886 1.1934 -0.0498 0.0291  -0.4240 485 SER B OG  
8070 N N   . SER B 488 ? 0.6456 0.6479 0.9722 -0.0350 0.0108  -0.3230 486 SER B N   
8071 C CA  . SER B 488 ? 0.6248 0.6092 0.9049 -0.0325 0.0185  -0.2771 486 SER B CA  
8072 C C   . SER B 488 ? 0.5581 0.4998 0.8635 -0.0337 0.0103  -0.2267 486 SER B C   
8073 O O   . SER B 488 ? 0.6308 0.5496 0.9968 -0.0391 -0.0023 -0.2317 486 SER B O   
8074 C CB  . SER B 488 ? 0.5877 0.6122 0.7885 -0.0414 0.0257  -0.2652 486 SER B CB  
8075 O OG  . SER B 488 ? 0.5647 0.5771 0.7220 -0.0360 0.0330  -0.2167 486 SER B OG  
8076 N N   . ALA B 489 ? 0.5245 0.4591 0.7843 -0.0305 0.0178  -0.1789 487 ALA B N   
8077 C CA  . ALA B 489 ? 0.5192 0.4269 0.7892 -0.0336 0.0152  -0.1301 487 ALA B CA  
8078 C C   . ALA B 489 ? 0.5006 0.4284 0.7157 -0.0375 0.0234  -0.1034 487 ALA B C   
8079 O O   . ALA B 489 ? 0.4009 0.3520 0.5666 -0.0344 0.0300  -0.1096 487 ALA B O   
8080 C CB  . ALA B 489 ? 0.4181 0.2994 0.6951 -0.0250 0.0152  -0.1004 487 ALA B CB  
8081 N N   . ILE B 490 ? 0.3826 0.3030 0.6134 -0.0452 0.0226  -0.0729 488 ILE B N   
8082 C CA  . ILE B 490 ? 0.4034 0.3445 0.6004 -0.0473 0.0301  -0.0511 488 ILE B CA  
8083 C C   . ILE B 490 ? 0.4277 0.3591 0.6291 -0.0507 0.0376  -0.0106 488 ILE B C   
8084 O O   . ILE B 490 ? 0.4412 0.3540 0.6839 -0.0595 0.0322  0.0048  488 ILE B O   
8085 C CB  . ILE B 490 ? 0.4730 0.4358 0.6905 -0.0574 0.0218  -0.0663 488 ILE B CB  
8086 C CG1 . ILE B 490 ? 0.4523 0.4363 0.6530 -0.0574 0.0142  -0.1060 488 ILE B CG1 
8087 C CG2 . ILE B 490 ? 0.4299 0.4145 0.6299 -0.0576 0.0282  -0.0423 488 ILE B CG2 
8088 C CD1 . ILE B 490 ? 0.5070 0.5160 0.7280 -0.0690 0.0016  -0.1243 488 ILE B CD1 
8089 N N   . ASN B 491 ? 0.3642 0.3102 0.5249 -0.0450 0.0496  0.0065  489 ASN B N   
8090 C CA  . ASN B 491 ? 0.4725 0.4241 0.6296 -0.0502 0.0606  0.0390  489 ASN B CA  
8091 C C   . ASN B 491 ? 0.4301 0.4123 0.5738 -0.0476 0.0708  0.0399  489 ASN B C   
8092 O O   . ASN B 491 ? 0.4372 0.4264 0.5465 -0.0366 0.0784  0.0386  489 ASN B O   
8093 C CB  . ASN B 491 ? 0.4039 0.3434 0.5297 -0.0440 0.0652  0.0539  489 ASN B CB  
8094 C CG  . ASN B 491 ? 0.4082 0.3555 0.5346 -0.0558 0.0725  0.0891  489 ASN B CG  
8095 O OD1 . ASN B 491 ? 0.4062 0.3819 0.5298 -0.0626 0.0854  0.0987  489 ASN B OD1 
8096 N ND2 . ASN B 491 ? 0.3991 0.3264 0.5308 -0.0594 0.0639  0.1090  489 ASN B ND2 
8097 N N   . ARG B 492 ? 0.3973 0.3974 0.5766 -0.0574 0.0689  0.0397  490 ARG B N   
8098 C CA  . ARG B 492 ? 0.3563 0.3890 0.5378 -0.0532 0.0760  0.0378  490 ARG B CA  
8099 C C   . ARG B 492 ? 0.3173 0.3704 0.4845 -0.0518 0.0963  0.0537  490 ARG B C   
8100 O O   . ARG B 492 ? 0.3389 0.4081 0.4938 -0.0386 0.1024  0.0442  490 ARG B O   
8101 C CB  . ARG B 492 ? 0.3371 0.3884 0.5674 -0.0658 0.0682  0.0338  490 ARG B CB  
8102 C CG  . ARG B 492 ? 0.5026 0.5454 0.7374 -0.0650 0.0477  0.0084  490 ARG B CG  
8103 C CD  . ARG B 492 ? 0.5402 0.6033 0.8214 -0.0775 0.0350  -0.0023 490 ARG B CD  
8104 N NE  . ARG B 492 ? 0.6248 0.6863 0.8947 -0.0764 0.0163  -0.0307 490 ARG B NE  
8105 C CZ  . ARG B 492 ? 0.6693 0.7486 0.9689 -0.0870 -0.0005 -0.0501 490 ARG B CZ  
8106 N NH1 . ARG B 492 ? 0.8894 0.9902 1.2367 -0.0980 -0.0028 -0.0430 490 ARG B NH1 
8107 N NH2 . ARG B 492 ? 0.7347 0.8170 1.0147 -0.0881 -0.0151 -0.0792 490 ARG B NH2 
8108 N N   . PRO B 493 ? 0.3311 0.3876 0.5009 -0.0658 0.1063  0.0769  491 PRO B N   
8109 C CA  . PRO B 493 ? 0.3401 0.4254 0.4853 -0.0662 0.1273  0.0870  491 PRO B CA  
8110 C C   . PRO B 493 ? 0.3737 0.4480 0.4747 -0.0481 0.1296  0.0729  491 PRO B C   
8111 O O   . PRO B 493 ? 0.4006 0.5014 0.4941 -0.0389 0.1431  0.0599  491 PRO B O   
8112 C CB  . PRO B 493 ? 0.4049 0.4878 0.5510 -0.0875 0.1297  0.1206  491 PRO B CB  
8113 C CG  . PRO B 493 ? 0.4088 0.4758 0.6060 -0.1008 0.1150  0.1268  491 PRO B CG  
8114 C CD  . PRO B 493 ? 0.3760 0.4136 0.5745 -0.0839 0.0975  0.0961  491 PRO B CD  
8115 N N   . GLN B 494 ? 0.4318 0.4696 0.5105 -0.0427 0.1167  0.0724  492 GLN B N   
8116 C CA  . GLN B 494 ? 0.4301 0.4585 0.4712 -0.0285 0.1182  0.0604  492 GLN B CA  
8117 C C   . GLN B 494 ? 0.3939 0.4257 0.4406 -0.0137 0.1155  0.0391  492 GLN B C   
8118 O O   . GLN B 494 ? 0.3856 0.4218 0.4165 -0.0029 0.1214  0.0279  492 GLN B O   
8119 C CB  . GLN B 494 ? 0.3895 0.3833 0.4149 -0.0260 0.1044  0.0619  492 GLN B CB  
8120 C CG  . GLN B 494 ? 0.3660 0.3532 0.3820 -0.0362 0.1028  0.0856  492 GLN B CG  
8121 C CD  . GLN B 494 ? 0.4318 0.3883 0.4441 -0.0301 0.0881  0.0824  492 GLN B CD  
8122 O OE1 . GLN B 494 ? 0.3776 0.3217 0.3915 -0.0207 0.0823  0.0607  492 GLN B OE1 
8123 N NE2 . GLN B 494 ? 0.3581 0.3074 0.3668 -0.0366 0.0815  0.1050  492 GLN B NE2 
8124 N N   . ILE B 495 ? 0.4063 0.4365 0.4787 -0.0140 0.1037  0.0338  493 ILE B N   
8125 C CA  . ILE B 495 ? 0.4195 0.4567 0.5028 -0.0023 0.0964  0.0218  493 ILE B CA  
8126 C C   . ILE B 495 ? 0.3385 0.4096 0.4506 0.0026  0.1092  0.0170  493 ILE B C   
8127 O O   . ILE B 495 ? 0.3627 0.4378 0.4824 0.0169  0.1085  0.0059  493 ILE B O   
8128 C CB  . ILE B 495 ? 0.4053 0.4403 0.5047 -0.0071 0.0782  0.0185  493 ILE B CB  
8129 C CG1 . ILE B 495 ? 0.4055 0.4154 0.4765 -0.0094 0.0687  0.0140  493 ILE B CG1 
8130 C CG2 . ILE B 495 ? 0.4083 0.4579 0.5256 0.0021  0.0666  0.0145  493 ILE B CG2 
8131 C CD1 . ILE B 495 ? 0.4535 0.4684 0.5344 -0.0170 0.0529  0.0036  493 ILE B CD1 
8132 N N   . GLY B 496 ? 0.3412 0.4389 0.4754 -0.0099 0.1215  0.0244  494 GLY B N   
8133 C CA  . GLY B 496 ? 0.3127 0.4533 0.4763 -0.0066 0.1388  0.0157  494 GLY B CA  
8134 C C   . GLY B 496 ? 0.3145 0.4640 0.4532 0.0024  0.1552  0.0029  494 GLY B C   
8135 O O   . GLY B 496 ? 0.3587 0.5305 0.5232 0.0167  0.1622  -0.0184 494 GLY B O   
8136 N N   . VAL B 497 ? 0.3233 0.4564 0.4168 -0.0053 0.1593  0.0129  495 VAL B N   
8137 C CA  . VAL B 497 ? 0.3911 0.5344 0.4564 0.0012  0.1724  -0.0025 495 VAL B CA  
8138 C C   . VAL B 497 ? 0.3945 0.5127 0.4672 0.0223  0.1605  -0.0240 495 VAL B C   
8139 O O   . VAL B 497 ? 0.3407 0.4773 0.4261 0.0340  0.1708  -0.0499 495 VAL B O   
8140 C CB  . VAL B 497 ? 0.4615 0.5897 0.4782 -0.0114 0.1718  0.0162  495 VAL B CB  
8141 C CG1 . VAL B 497 ? 0.3625 0.4932 0.3472 -0.0034 0.1778  -0.0036 495 VAL B CG1 
8142 C CG2 . VAL B 497 ? 0.4077 0.5705 0.4208 -0.0344 0.1855  0.0406  495 VAL B CG2 
8143 N N   . VAL B 498 ? 0.3837 0.4623 0.4525 0.0261  0.1385  -0.0143 496 VAL B N   
8144 C CA  . VAL B 498 ? 0.3471 0.4004 0.4219 0.0412  0.1246  -0.0254 496 VAL B CA  
8145 C C   . VAL B 498 ? 0.3793 0.4506 0.5088 0.0550  0.1211  -0.0384 496 VAL B C   
8146 O O   . VAL B 498 ? 0.4565 0.5231 0.6080 0.0698  0.1193  -0.0571 496 VAL B O   
8147 C CB  . VAL B 498 ? 0.3585 0.3768 0.4135 0.0373  0.1040  -0.0093 496 VAL B CB  
8148 C CG1 . VAL B 498 ? 0.4484 0.4438 0.5115 0.0480  0.0883  -0.0122 496 VAL B CG1 
8149 C CG2 . VAL B 498 ? 0.3033 0.3061 0.3169 0.0272  0.1071  -0.0012 496 VAL B CG2 
8150 N N   . ARG B 499 ? 0.3749 0.4674 0.5350 0.0509  0.1180  -0.0303 497 ARG B N   
8151 C CA  . ARG B 499 ? 0.3118 0.4245 0.5323 0.0648  0.1106  -0.0406 497 ARG B CA  
8152 C C   . ARG B 499 ? 0.3486 0.4943 0.6002 0.0766  0.1327  -0.0711 497 ARG B C   
8153 O O   . ARG B 499 ? 0.3805 0.5239 0.6788 0.0960  0.1241  -0.0890 497 ARG B O   
8154 C CB  . ARG B 499 ? 0.3029 0.4417 0.5518 0.0553  0.1063  -0.0294 497 ARG B CB  
8155 C CG  . ARG B 499 ? 0.3057 0.4695 0.6238 0.0695  0.0941  -0.0373 497 ARG B CG  
8156 C CD  . ARG B 499 ? 0.5289 0.7133 0.8699 0.0574  0.0824  -0.0238 497 ARG B CD  
8157 N NE  . ARG B 499 ? 0.7481 0.9556 1.0776 0.0379  0.1053  -0.0210 497 ARG B NE  
8158 C CZ  . ARG B 499 ? 0.8351 1.0595 1.1843 0.0224  0.0994  -0.0113 497 ARG B CZ  
8159 N NH1 . ARG B 499 ? 0.6603 0.8861 1.0363 0.0241  0.0718  -0.0066 497 ARG B NH1 
8160 N NH2 . ARG B 499 ? 0.7729 1.0139 1.1158 0.0028  0.1195  -0.0043 497 ARG B NH2 
8161 N N   . GLU B 500 ? 0.3884 0.5679 0.6173 0.0642  0.1605  -0.0780 498 GLU B N   
8162 C CA  . GLU B 500 ? 0.4261 0.6500 0.6774 0.0720  0.1862  -0.1129 498 GLU B CA  
8163 C C   . GLU B 500 ? 0.4603 0.6571 0.6968 0.0852  0.1832  -0.1364 498 GLU B C   
8164 O O   . GLU B 500 ? 0.5020 0.7153 0.7866 0.1034  0.1886  -0.1730 498 GLU B O   
8165 C CB  . GLU B 500 ? 0.4072 0.6779 0.6248 0.0495  0.2155  -0.1078 498 GLU B CB  
8166 C CG  . GLU B 500 ? 0.5436 0.8713 0.7787 0.0528  0.2396  -0.1395 498 GLU B CG  
8167 C CD  . GLU B 500 ? 0.7213 1.0759 1.0327 0.0683  0.2366  -0.1571 498 GLU B CD  
8168 O OE1 . GLU B 500 ? 0.7132 1.0908 1.0563 0.0590  0.2376  -0.1393 498 GLU B OE1 
8169 O OE2 . GLU B 500 ? 0.7653 1.1169 1.1089 0.0886  0.2312  -0.1884 498 GLU B OE2 
8170 N N   . PHE B 501 ? 0.4615 0.6185 0.6386 0.0761  0.1742  -0.1189 499 PHE B N   
8171 C CA  . PHE B 501 ? 0.4884 0.6183 0.6528 0.0855  0.1692  -0.1398 499 PHE B CA  
8172 C C   . PHE B 501 ? 0.4810 0.5770 0.7019 0.1058  0.1452  -0.1469 499 PHE B C   
8173 O O   . PHE B 501 ? 0.4788 0.5705 0.7332 0.1206  0.1453  -0.1803 499 PHE B O   
8174 C CB  . PHE B 501 ? 0.4864 0.5803 0.5860 0.0717  0.1600  -0.1149 499 PHE B CB  
8175 C CG  . PHE B 501 ? 0.4887 0.5497 0.5783 0.0787  0.1500  -0.1310 499 PHE B CG  
8176 C CD1 . PHE B 501 ? 0.5035 0.5847 0.5663 0.0756  0.1648  -0.1584 499 PHE B CD1 
8177 C CD2 . PHE B 501 ? 0.5471 0.5607 0.6525 0.0851  0.1249  -0.1171 499 PHE B CD2 
8178 C CE1 . PHE B 501 ? 0.5679 0.6189 0.6264 0.0804  0.1539  -0.1755 499 PHE B CE1 
8179 C CE2 . PHE B 501 ? 0.5330 0.5160 0.6348 0.0883  0.1151  -0.1292 499 PHE B CE2 
8180 C CZ  . PHE B 501 ? 0.5234 0.5230 0.6045 0.0867  0.1292  -0.1602 499 PHE B CZ  
8181 N N   . LEU B 502 ? 0.4624 0.5356 0.6975 0.1054  0.1223  -0.1154 500 LEU B N   
8182 C CA  . LEU B 502 ? 0.4814 0.5236 0.7683 0.1208  0.0942  -0.1106 500 LEU B CA  
8183 C C   . LEU B 502 ? 0.5273 0.6007 0.8968 0.1413  0.0978  -0.1408 500 LEU B C   
8184 O O   . LEU B 502 ? 0.5588 0.6099 0.9853 0.1595  0.0811  -0.1553 500 LEU B O   
8185 C CB  . LEU B 502 ? 0.3581 0.3820 0.6332 0.1116  0.0694  -0.0693 500 LEU B CB  
8186 C CG  . LEU B 502 ? 0.5300 0.5182 0.7428 0.0960  0.0581  -0.0424 500 LEU B CG  
8187 C CD1 . LEU B 502 ? 0.5106 0.4953 0.7165 0.0867  0.0359  -0.0103 500 LEU B CD1 
8188 C CD2 . LEU B 502 ? 0.4659 0.4162 0.6836 0.1015  0.0456  -0.0452 500 LEU B CD2 
8189 N N   . THR B 503 ? 0.4791 0.6055 0.8633 0.1381  0.1193  -0.1510 501 THR B N   
8190 C CA  . THR B 503 ? 0.4170 0.5802 0.8751 0.1541  0.1230  -0.1786 501 THR B CA  
8191 C C   . THR B 503 ? 0.4325 0.6018 0.8857 0.1586  0.1352  -0.2169 501 THR B C   
8192 O O   . THR B 503 ? 0.4633 0.6301 0.9744 0.1732  0.1230  -0.2370 501 THR B O   
8193 C CB  . THR B 503 ? 0.4359 0.6574 0.9008 0.1430  0.1443  -0.1763 501 THR B CB  
8194 O OG1 . THR B 503 ? 0.5379 0.7503 1.0196 0.1391  0.1218  -0.1414 501 THR B OG1 
8195 C CG2 . THR B 503 ? 0.4111 0.6734 0.9264 0.1524  0.1525  -0.2054 501 THR B CG2 
8196 N N   . ARG B 504 ? 0.4596 0.6380 0.8467 0.1449  0.1569  -0.2269 502 ARG B N   
8197 C CA  . ARG B 504 ? 0.5105 0.6999 0.8876 0.1460  0.1677  -0.2637 502 ARG B CA  
8198 C C   . ARG B 504 ? 0.5312 0.6654 0.9042 0.1516  0.1473  -0.2689 502 ARG B C   
8199 O O   . ARG B 504 ? 0.5595 0.6977 0.9382 0.1540  0.1506  -0.3025 502 ARG B O   
8200 C CB  . ARG B 504 ? 0.5839 0.8144 0.8892 0.1254  0.1966  -0.2671 502 ARG B CB  
8201 C CG  . ARG B 504 ? 0.6141 0.9020 0.9144 0.1128  0.2192  -0.2570 502 ARG B CG  
8202 C CD  . ARG B 504 ? 0.7057 1.0250 0.9313 0.0900  0.2409  -0.2520 502 ARG B CD  
8203 N NE  . ARG B 504 ? 0.8378 1.1970 1.0452 0.0709  0.2577  -0.2234 502 ARG B NE  
8204 C CZ  . ARG B 504 ? 0.7129 1.1200 0.9586 0.0693  0.2720  -0.2299 502 ARG B CZ  
8205 N NH1 . ARG B 504 ? 0.7907 1.2220 1.0858 0.0840  0.2766  -0.2692 502 ARG B NH1 
8206 N NH2 . ARG B 504 ? 0.8247 1.2583 1.0602 0.0503  0.2826  -0.1968 502 ARG B NH2 
8207 N N   . ASN B 505 ? 0.4636 0.5490 0.8307 0.1523  0.1261  -0.2367 503 ASN B N   
8208 C CA  . ASN B 505 ? 0.5296 0.5612 0.8905 0.1535  0.1060  -0.2339 503 ASN B CA  
8209 C C   . ASN B 505 ? 0.5308 0.5158 0.9309 0.1604  0.0732  -0.1970 503 ASN B C   
8210 O O   . ASN B 505 ? 0.4500 0.4005 0.8186 0.1528  0.0625  -0.1669 503 ASN B O   
8211 C CB  . ASN B 505 ? 0.5321 0.5566 0.8159 0.1376  0.1182  -0.2271 503 ASN B CB  
8212 C CG  . ASN B 505 ? 0.6291 0.6971 0.8695 0.1276  0.1427  -0.2564 503 ASN B CG  
8213 O OD1 . ASN B 505 ? 0.6593 0.7268 0.9110 0.1304  0.1407  -0.2872 503 ASN B OD1 
8214 N ND2 . ASN B 505 ? 0.5818 0.6885 0.7736 0.1137  0.1638  -0.2439 503 ASN B ND2 
8215 N N   . PRO B 506 ? 0.5022 0.4872 0.9712 0.1731  0.0548  -0.1961 504 PRO B N   
8216 C CA  . PRO B 506 ? 0.5261 0.4764 1.0271 0.1758  0.0199  -0.1518 504 PRO B CA  
8217 C C   . PRO B 506 ? 0.5869 0.4806 1.0727 0.1677  -0.0051 -0.1235 504 PRO B C   
8218 O O   . PRO B 506 ? 0.6024 0.4725 1.0865 0.1617  -0.0309 -0.0769 504 PRO B O   
8219 C CB  . PRO B 506 ? 0.5140 0.4766 1.0944 0.1897  0.0050  -0.1643 504 PRO B CB  
8220 C CG  . PRO B 506 ? 0.5445 0.5262 1.1379 0.1944  0.0257  -0.2171 504 PRO B CG  
8221 C CD  . PRO B 506 ? 0.5170 0.5356 1.0395 0.1839  0.0625  -0.2340 504 PRO B CD  
8222 N N   . ALA B 507 ? 0.6292 0.5051 1.1021 0.1642  0.0005  -0.1474 505 ALA B N   
8223 C CA  . ALA B 507 ? 0.5933 0.4190 1.0566 0.1533  -0.0232 -0.1178 505 ALA B CA  
8224 C C   . ALA B 507 ? 0.6397 0.4510 1.0386 0.1388  -0.0208 -0.0837 505 ALA B C   
8225 O O   . ALA B 507 ? 0.6379 0.4143 1.0263 0.1255  -0.0437 -0.0437 505 ALA B O   
8226 C CB  . ALA B 507 ? 0.5630 0.3772 1.0290 0.1515  -0.0172 -0.1538 505 ALA B CB  
8227 N N   . TRP B 508 ? 0.5753 0.4217 0.9215 0.1341  0.0069  -0.0939 506 TRP B N   
8228 C CA  . TRP B 508 ? 0.5701 0.4177 0.8352 0.1117  0.0119  -0.0623 506 TRP B CA  
8229 C C   . TRP B 508 ? 0.5325 0.3852 0.7873 0.1031  -0.0051 -0.0192 506 TRP B C   
8230 O O   . TRP B 508 ? 0.5030 0.3647 0.6973 0.0862  0.0009  0.0003  506 TRP B O   
8231 C CB  . TRP B 508 ? 0.4922 0.3765 0.7052 0.1064  0.0440  -0.0856 506 TRP B CB  
8232 C CG  . TRP B 508 ? 0.5089 0.3893 0.6995 0.1041  0.0571  -0.1160 506 TRP B CG  
8233 C CD1 . TRP B 508 ? 0.4924 0.3808 0.7199 0.1171  0.0659  -0.1622 506 TRP B CD1 
8234 C CD2 . TRP B 508 ? 0.4175 0.2925 0.5456 0.0876  0.0627  -0.1066 506 TRP B CD2 
8235 N NE1 . TRP B 508 ? 0.5113 0.3986 0.6977 0.1078  0.0747  -0.1804 506 TRP B NE1 
8236 C CE2 . TRP B 508 ? 0.4374 0.3161 0.5645 0.0902  0.0719  -0.1445 506 TRP B CE2 
8237 C CE3 . TRP B 508 ? 0.4207 0.2914 0.4993 0.0716  0.0600  -0.0736 506 TRP B CE3 
8238 C CZ2 . TRP B 508 ? 0.5226 0.3999 0.6000 0.0768  0.0757  -0.1449 506 TRP B CZ2 
8239 C CZ3 . TRP B 508 ? 0.4998 0.3682 0.5359 0.0606  0.0653  -0.0760 506 TRP B CZ3 
8240 C CH2 . TRP B 508 ? 0.4522 0.3235 0.4875 0.0629  0.0717  -0.1087 506 TRP B CH2 
8241 N N   . ARG B 509 ? 0.5630 0.4119 0.8792 0.1146  -0.0282 -0.0060 507 ARG B N   
8242 C CA  . ARG B 509 ? 0.5691 0.4289 0.8760 0.1053  -0.0482 0.0341  507 ARG B CA  
8243 C C   . ARG B 509 ? 0.6329 0.4660 0.9120 0.0861  -0.0731 0.0786  507 ARG B C   
8244 O O   . ARG B 509 ? 0.5590 0.4060 0.8183 0.0735  -0.0906 0.1133  507 ARG B O   
8245 C CB  . ARG B 509 ? 0.6492 0.5207 1.0357 0.1243  -0.0672 0.0345  507 ARG B CB  
8246 C CG  . ARG B 509 ? 0.7074 0.5424 1.1676 0.1362  -0.0985 0.0454  507 ARG B CG  
8247 C CD  . ARG B 509 ? 0.8452 0.7023 1.3702 0.1482  -0.1170 0.0471  507 ARG B CD  
8248 N NE  . ARG B 509 ? 0.8384 0.7344 1.3964 0.1658  -0.0895 -0.0003 507 ARG B NE  
8249 C CZ  . ARG B 509 ? 0.7577 0.6804 1.3750 0.1774  -0.0980 -0.0088 507 ARG B CZ  
8250 N NH1 . ARG B 509 ? 0.7434 0.6575 1.3942 0.1748  -0.1353 0.0282  507 ARG B NH1 
8251 N NH2 . ARG B 509 ? 0.7395 0.7028 1.3799 0.1890  -0.0680 -0.0535 507 ARG B NH2 
8252 N N   . LYS B 510 ? 0.6587 0.4591 0.9360 0.0812  -0.0746 0.0776  508 LYS B N   
8253 C CA  . LYS B 510 ? 0.6244 0.4050 0.8725 0.0583  -0.0931 0.1197  508 LYS B CA  
8254 C C   . LYS B 510 ? 0.6126 0.4062 0.7842 0.0397  -0.0690 0.1142  508 LYS B C   
8255 O O   . LYS B 510 ? 0.7181 0.4990 0.8660 0.0205  -0.0755 0.1374  508 LYS B O   
8256 C CB  . LYS B 510 ? 0.7154 0.4503 1.0218 0.0619  -0.1139 0.1261  508 LYS B CB  
8257 C CG  . LYS B 510 ? 0.7161 0.4356 1.0409 0.0746  -0.0933 0.0746  508 LYS B CG  
8258 C CD  . LYS B 510 ? 0.7884 0.4832 1.1596 0.0719  -0.1113 0.0737  508 LYS B CD  
8259 C CE  . LYS B 510 ? 0.8958 0.5833 1.2856 0.0834  -0.0933 0.0181  508 LYS B CE  
8260 N NZ  . LYS B 510 ? 0.9117 0.6260 1.3318 0.1076  -0.0760 -0.0307 508 LYS B NZ  
8261 N N   . ALA B 511 ? 0.4978 0.3183 0.6365 0.0445  -0.0425 0.0856  509 ALA B N   
8262 C CA  . ALA B 511 ? 0.5861 0.4184 0.6655 0.0315  -0.0212 0.0763  509 ALA B CA  
8263 C C   . ALA B 511 ? 0.5793 0.4388 0.6142 0.0148  -0.0220 0.0966  509 ALA B C   
8264 O O   . ALA B 511 ? 0.4744 0.3495 0.5171 0.0136  -0.0359 0.1132  509 ALA B O   
8265 C CB  . ALA B 511 ? 0.5243 0.3703 0.5961 0.0436  0.0045  0.0384  509 ALA B CB  
8266 N N   . VAL B 512 ? 0.5268 0.3953 0.5183 0.0022  -0.0073 0.0911  510 VAL B N   
8267 C CA  . VAL B 512 ? 0.5070 0.4055 0.4592 -0.0120 -0.0024 0.0959  510 VAL B CA  
8268 C C   . VAL B 512 ? 0.4021 0.3116 0.3447 -0.0034 0.0177  0.0675  510 VAL B C   
8269 O O   . VAL B 512 ? 0.4816 0.3797 0.4250 0.0039  0.0304  0.0503  510 VAL B O   
8270 C CB  . VAL B 512 ? 0.5387 0.4452 0.4596 -0.0326 -0.0003 0.1079  510 VAL B CB  
8271 C CG1 . VAL B 512 ? 0.5635 0.5075 0.4491 -0.0449 0.0088  0.1001  510 VAL B CG1 
8272 C CG2 . VAL B 512 ? 0.5876 0.4845 0.5186 -0.0463 -0.0223 0.1451  510 VAL B CG2 
8273 N N   . PHE B 513 ? 0.4215 0.3537 0.3571 -0.0060 0.0179  0.0644  511 PHE B N   
8274 C CA  . PHE B 513 ? 0.4409 0.3813 0.3739 -0.0012 0.0333  0.0433  511 PHE B CA  
8275 C C   . PHE B 513 ? 0.4311 0.3838 0.3384 -0.0123 0.0411  0.0338  511 PHE B C   
8276 O O   . PHE B 513 ? 0.3844 0.3582 0.2747 -0.0252 0.0353  0.0374  511 PHE B O   
8277 C CB  . PHE B 513 ? 0.4115 0.3683 0.3626 0.0015  0.0285  0.0415  511 PHE B CB  
8278 C CG  . PHE B 513 ? 0.3965 0.3591 0.3520 0.0030  0.0417  0.0253  511 PHE B CG  
8279 C CD1 . PHE B 513 ? 0.3800 0.3537 0.3239 -0.0063 0.0435  0.0146  511 PHE B CD1 
8280 C CD2 . PHE B 513 ? 0.3812 0.3406 0.3563 0.0123  0.0522  0.0204  511 PHE B CD2 
8281 C CE1 . PHE B 513 ? 0.3758 0.3485 0.3339 -0.0057 0.0516  0.0036  511 PHE B CE1 
8282 C CE2 . PHE B 513 ? 0.3735 0.3379 0.3540 0.0096  0.0620  0.0141  511 PHE B CE2 
8283 C CZ  . PHE B 513 ? 0.3474 0.3141 0.3227 0.0010  0.0598  0.0078  511 PHE B CZ  
8284 N N   . ILE B 514 ? 0.3397 0.2836 0.2458 -0.0077 0.0532  0.0210  512 ILE B N   
8285 C CA  . ILE B 514 ? 0.4228 0.3777 0.3192 -0.0139 0.0600  0.0079  512 ILE B CA  
8286 C C   . ILE B 514 ? 0.4675 0.4188 0.3802 -0.0075 0.0657  -0.0041 512 ILE B C   
8287 O O   . ILE B 514 ? 0.4694 0.4077 0.3895 -0.0001 0.0689  0.0007  512 ILE B O   
8288 C CB  . ILE B 514 ? 0.4244 0.3725 0.3119 -0.0165 0.0636  0.0091  512 ILE B CB  
8289 C CG1 . ILE B 514 ? 0.4449 0.3937 0.3224 -0.0265 0.0557  0.0272  512 ILE B CG1 
8290 C CG2 . ILE B 514 ? 0.4311 0.3963 0.3193 -0.0209 0.0707  -0.0077 512 ILE B CG2 
8291 C CD1 . ILE B 514 ? 0.4446 0.3899 0.3177 -0.0337 0.0585  0.0297  512 ILE B CD1 
8292 N N   . SER B 515 ? 0.4449 0.4103 0.3656 -0.0121 0.0659  -0.0198 513 SER B N   
8293 C CA  . SER B 515 ? 0.4299 0.3876 0.3766 -0.0079 0.0675  -0.0294 513 SER B CA  
8294 C C   . SER B 515 ? 0.4486 0.4190 0.4080 -0.0103 0.0692  -0.0533 513 SER B C   
8295 O O   . SER B 515 ? 0.4423 0.4365 0.3849 -0.0179 0.0720  -0.0644 513 SER B O   
8296 C CB  . SER B 515 ? 0.4012 0.3609 0.3665 -0.0095 0.0633  -0.0296 513 SER B CB  
8297 O OG  . SER B 515 ? 0.4293 0.4054 0.4067 -0.0159 0.0595  -0.0525 513 SER B OG  
8298 N N   . PRO B 516 ? 0.4105 0.3689 0.4034 -0.0047 0.0673  -0.0614 514 PRO B N   
8299 C CA  . PRO B 516 ? 0.4395 0.4115 0.4598 -0.0038 0.0683  -0.0916 514 PRO B CA  
8300 C C   . PRO B 516 ? 0.4834 0.4715 0.5240 -0.0089 0.0663  -0.1209 514 PRO B C   
8301 O O   . PRO B 516 ? 0.4378 0.4402 0.5098 -0.0070 0.0679  -0.1549 514 PRO B O   
8302 C CB  . PRO B 516 ? 0.4608 0.4078 0.5185 0.0056  0.0614  -0.0827 514 PRO B CB  
8303 C CG  . PRO B 516 ? 0.4625 0.3908 0.4954 0.0059  0.0599  -0.0465 514 PRO B CG  
8304 C CD  . PRO B 516 ? 0.4518 0.3862 0.4626 0.0002  0.0633  -0.0415 514 PRO B CD  
8305 N N   . TYR B 517 ? 0.5038 0.4928 0.5337 -0.0148 0.0620  -0.1130 515 TYR B N   
8306 C CA  . TYR B 517 ? 0.5280 0.5327 0.5792 -0.0213 0.0569  -0.1420 515 TYR B CA  
8307 C C   . TYR B 517 ? 0.5041 0.5360 0.5161 -0.0324 0.0540  -0.1372 515 TYR B C   
8308 O O   . TYR B 517 ? 0.4565 0.4785 0.4496 -0.0317 0.0510  -0.1053 515 TYR B O   
8309 C CB  . TYR B 517 ? 0.4557 0.4303 0.5531 -0.0188 0.0482  -0.1339 515 TYR B CB  
8310 C CG  . TYR B 517 ? 0.4533 0.3979 0.5972 -0.0100 0.0442  -0.1297 515 TYR B CG  
8311 C CD1 . TYR B 517 ? 0.4757 0.4173 0.6755 -0.0065 0.0383  -0.1655 515 TYR B CD1 
8312 C CD2 . TYR B 517 ? 0.4243 0.3459 0.5601 -0.0057 0.0439  -0.0904 515 TYR B CD2 
8313 C CE1 . TYR B 517 ? 0.4871 0.3984 0.7391 0.0022  0.0291  -0.1567 515 TYR B CE1 
8314 C CE2 . TYR B 517 ? 0.4429 0.3399 0.6200 0.0000  0.0352  -0.0794 515 TYR B CE2 
8315 C CZ  . TYR B 517 ? 0.4826 0.3719 0.7206 0.0046  0.0263  -0.1096 515 TYR B CZ  
8316 O OH  . TYR B 517 ? 0.5661 0.4282 0.8545 0.0111  0.0126  -0.0942 515 TYR B OH  
8317 N N   . ASN B 518 ? 0.5723 0.6428 0.5748 -0.0427 0.0538  -0.1705 516 ASN B N   
8318 C CA  A ASN B 518 ? 0.5374 0.6407 0.5031 -0.0562 0.0459  -0.1655 516 ASN B CA  
8319 C CA  B ASN B 518 ? 0.6678 0.7708 0.6331 -0.0561 0.0459  -0.1648 516 ASN B CA  
8320 C C   . ASN B 518 ? 0.5941 0.6854 0.5789 -0.0567 0.0327  -0.1531 516 ASN B C   
8321 O O   . ASN B 518 ? 0.5257 0.6288 0.4858 -0.0617 0.0234  -0.1281 516 ASN B O   
8322 C CB  A ASN B 518 ? 0.7080 0.8626 0.6619 -0.0697 0.0482  -0.2104 516 ASN B CB  
8323 C CB  B ASN B 518 ? 0.7391 0.8956 0.6866 -0.0703 0.0490  -0.2067 516 ASN B CB  
8324 C CG  A ASN B 518 ? 0.7450 0.9355 0.6559 -0.0790 0.0598  -0.2096 516 ASN B CG  
8325 C CG  B ASN B 518 ? 0.7166 0.8808 0.7091 -0.0711 0.0450  -0.2559 516 ASN B CG  
8326 O OD1 A ASN B 518 ? 0.7531 0.9644 0.6777 -0.0784 0.0733  -0.2452 516 ASN B OD1 
8327 O OD1 B ASN B 518 ? 0.7901 0.9615 0.8142 -0.0666 0.0540  -0.2970 516 ASN B OD1 
8328 N ND2 A ASN B 518 ? 0.7391 0.9381 0.6043 -0.0882 0.0541  -0.1681 516 ASN B ND2 
8329 N ND2 B ASN B 518 ? 0.7138 0.8783 0.7163 -0.0769 0.0303  -0.2551 516 ASN B ND2 
8330 N N   . SER B 519 ? 0.4788 0.5476 0.5140 -0.0524 0.0301  -0.1679 517 SER B N   
8331 C CA  . SER B 519 ? 0.4913 0.5538 0.5508 -0.0558 0.0191  -0.1565 517 SER B CA  
8332 C C   . SER B 519 ? 0.4267 0.4661 0.4821 -0.0478 0.0221  -0.1122 517 SER B C   
8333 O O   . SER B 519 ? 0.4522 0.5034 0.5054 -0.0503 0.0143  -0.0956 517 SER B O   
8334 C CB  . SER B 519 ? 0.4598 0.5050 0.5799 -0.0573 0.0145  -0.1827 517 SER B CB  
8335 O OG  . SER B 519 ? 0.5788 0.6553 0.7058 -0.0667 0.0085  -0.2315 517 SER B OG  
8336 N N   . GLN B 520 ? 0.4148 0.4264 0.4716 -0.0382 0.0326  -0.0955 518 GLN B N   
8337 C CA  . GLN B 520 ? 0.4654 0.4641 0.5127 -0.0315 0.0377  -0.0612 518 GLN B CA  
8338 C C   . GLN B 520 ? 0.4582 0.4736 0.4695 -0.0306 0.0340  -0.0486 518 GLN B C   
8339 O O   . GLN B 520 ? 0.4683 0.4874 0.4857 -0.0275 0.0306  -0.0309 518 GLN B O   
8340 C CB  . GLN B 520 ? 0.4068 0.3806 0.4513 -0.0235 0.0477  -0.0487 518 GLN B CB  
8341 C CG  . GLN B 520 ? 0.3994 0.3664 0.4305 -0.0174 0.0550  -0.0215 518 GLN B CG  
8342 C CD  . GLN B 520 ? 0.4092 0.3732 0.4692 -0.0209 0.0585  -0.0067 518 GLN B CD  
8343 O OE1 . GLN B 520 ? 0.4277 0.4005 0.5166 -0.0284 0.0530  -0.0114 518 GLN B OE1 
8344 N NE2 . GLN B 520 ? 0.3677 0.3243 0.4189 -0.0182 0.0677  0.0114  518 GLN B NE2 
8345 N N   . ASN B 521 ? 0.4334 0.4613 0.4129 -0.0343 0.0339  -0.0566 519 ASN B N   
8346 C CA  . ASN B 521 ? 0.4911 0.5321 0.4397 -0.0369 0.0268  -0.0373 519 ASN B CA  
8347 C C   . ASN B 521 ? 0.4884 0.5538 0.4417 -0.0436 0.0098  -0.0326 519 ASN B C   
8348 O O   . ASN B 521 ? 0.5158 0.5798 0.4728 -0.0390 0.0004  -0.0082 519 ASN B O   
8349 C CB  . ASN B 521 ? 0.4463 0.5058 0.3606 -0.0461 0.0300  -0.0455 519 ASN B CB  
8350 C CG  . ASN B 521 ? 0.5449 0.5833 0.4555 -0.0391 0.0433  -0.0433 519 ASN B CG  
8351 O OD1 . ASN B 521 ? 0.4072 0.4171 0.3357 -0.0277 0.0488  -0.0354 519 ASN B OD1 
8352 N ND2 . ASN B 521 ? 0.4034 0.4618 0.2895 -0.0480 0.0485  -0.0499 519 ASN B ND2 
8353 N N   . ALA B 522 ? 0.4827 0.5722 0.4412 -0.0543 0.0036  -0.0585 520 ALA B N   
8354 C CA  . ALA B 522 ? 0.4997 0.6182 0.4619 -0.0628 -0.0159 -0.0559 520 ALA B CA  
8355 C C   . ALA B 522 ? 0.5190 0.6246 0.5236 -0.0535 -0.0199 -0.0401 520 ALA B C   
8356 O O   . ALA B 522 ? 0.5314 0.6518 0.5424 -0.0526 -0.0360 -0.0204 520 ALA B O   
8357 C CB  . ALA B 522 ? 0.4777 0.6250 0.4432 -0.0764 -0.0209 -0.0953 520 ALA B CB  
8358 N N   . VAL B 523 ? 0.5053 0.5876 0.5430 -0.0476 -0.0062 -0.0472 521 VAL B N   
8359 C CA  . VAL B 523 ? 0.4968 0.5757 0.5738 -0.0416 -0.0048 -0.0326 521 VAL B CA  
8360 C C   . VAL B 523 ? 0.5169 0.5866 0.5879 -0.0280 -0.0005 -0.0082 521 VAL B C   
8361 O O   . VAL B 523 ? 0.5071 0.5908 0.6043 -0.0225 -0.0088 0.0034  521 VAL B O   
8362 C CB  . VAL B 523 ? 0.4668 0.5258 0.5752 -0.0428 0.0096  -0.0385 521 VAL B CB  
8363 C CG1 . VAL B 523 ? 0.4389 0.5046 0.5844 -0.0402 0.0156  -0.0223 521 VAL B CG1 
8364 C CG2 . VAL B 523 ? 0.4524 0.5153 0.5817 -0.0553 0.0018  -0.0663 521 VAL B CG2 
8365 N N   . ALA B 524 ? 0.5062 0.5540 0.5493 -0.0220 0.0111  -0.0034 522 ALA B N   
8366 C CA  . ALA B 524 ? 0.5022 0.5381 0.5441 -0.0095 0.0148  0.0133  522 ALA B CA  
8367 C C   . ALA B 524 ? 0.5411 0.5885 0.5807 -0.0085 -0.0063 0.0291  522 ALA B C   
8368 O O   . ALA B 524 ? 0.5281 0.5738 0.5960 0.0033  -0.0110 0.0401  522 ALA B O   
8369 C CB  . ALA B 524 ? 0.4694 0.4816 0.4821 -0.0064 0.0279  0.0129  522 ALA B CB  
8370 N N   . SER B 525 ? 0.5551 0.6173 0.5638 -0.0216 -0.0200 0.0303  523 SER B N   
8371 C CA  . SER B 525 ? 0.5457 0.6220 0.5479 -0.0254 -0.0446 0.0541  523 SER B CA  
8372 C C   . SER B 525 ? 0.5540 0.6484 0.6014 -0.0196 -0.0625 0.0616  523 SER B C   
8373 O O   . SER B 525 ? 0.5283 0.6193 0.6007 -0.0104 -0.0793 0.0842  523 SER B O   
8374 C CB  . SER B 525 ? 0.5342 0.6381 0.4903 -0.0459 -0.0545 0.0514  523 SER B CB  
8375 O OG  . SER B 525 ? 0.5734 0.6956 0.5180 -0.0542 -0.0815 0.0824  523 SER B OG  
8376 N N   . LYS B 526 ? 0.5406 0.6543 0.6070 -0.0248 -0.0609 0.0426  524 LYS B N   
8377 C CA  . LYS B 526 ? 0.5439 0.6822 0.6574 -0.0215 -0.0789 0.0480  524 LYS B CA  
8378 C C   . LYS B 526 ? 0.4999 0.6285 0.6662 -0.0026 -0.0649 0.0485  524 LYS B C   
8379 O O   . LYS B 526 ? 0.5069 0.6492 0.7182 0.0079  -0.0813 0.0603  524 LYS B O   
8380 C CB  . LYS B 526 ? 0.5224 0.6860 0.6440 -0.0359 -0.0821 0.0251  524 LYS B CB  
8381 N N   . ILE B 527 ? 0.4898 0.5994 0.6533 0.0014  -0.0355 0.0352  525 ILE B N   
8382 C CA  . ILE B 527 ? 0.4844 0.5979 0.6926 0.0148  -0.0179 0.0305  525 ILE B CA  
8383 C C   . ILE B 527 ? 0.4605 0.5553 0.6751 0.0321  -0.0158 0.0367  525 ILE B C   
8384 O O   . ILE B 527 ? 0.4112 0.5193 0.6772 0.0469  -0.0143 0.0325  525 ILE B O   
8385 C CB  . ILE B 527 ? 0.4692 0.5768 0.6695 0.0078  0.0102  0.0184  525 ILE B CB  
8386 C CG1 . ILE B 527 ? 0.4744 0.5972 0.6870 -0.0091 0.0053  0.0111  525 ILE B CG1 
8387 C CG2 . ILE B 527 ? 0.3946 0.5157 0.6296 0.0179  0.0323  0.0135  525 ILE B CG2 
8388 C CD1 . ILE B 527 ? 0.4585 0.5754 0.6776 -0.0181 0.0280  0.0074  525 ILE B CD1 
8389 N N   . LEU B 528 ? 0.5125 0.5787 0.6823 0.0305  -0.0161 0.0433  526 LEU B N   
8390 C CA  . LEU B 528 ? 0.4490 0.4919 0.6259 0.0445  -0.0133 0.0456  526 LEU B CA  
8391 C C   . LEU B 528 ? 0.4574 0.4878 0.6382 0.0461  -0.0431 0.0699  526 LEU B C   
8392 O O   . LEU B 528 ? 0.4758 0.4894 0.6914 0.0609  -0.0488 0.0723  526 LEU B O   
8393 C CB  . LEU B 528 ? 0.4479 0.4666 0.5792 0.0406  0.0077  0.0375  526 LEU B CB  
8394 C CG  . LEU B 528 ? 0.4558 0.4815 0.5745 0.0355  0.0337  0.0225  526 LEU B CG  
8395 C CD1 . LEU B 528 ? 0.4291 0.4309 0.5040 0.0317  0.0456  0.0199  526 LEU B CD1 
8396 C CD2 . LEU B 528 ? 0.4327 0.4795 0.5917 0.0456  0.0506  0.0092  526 LEU B CD2 
8397 N N   . GLY B 529 ? 0.4830 0.5228 0.6303 0.0297  -0.0628 0.0879  527 GLY B N   
8398 C CA  . GLY B 529 ? 0.4800 0.5135 0.6252 0.0255  -0.0934 0.1199  527 GLY B CA  
8399 C C   . GLY B 529 ? 0.4751 0.4784 0.5871 0.0202  -0.0898 0.1316  527 GLY B C   
8400 O O   . GLY B 529 ? 0.4828 0.4759 0.6000 0.0156  -0.1153 0.1636  527 GLY B O   
8401 N N   . LEU B 530 ? 0.4764 0.4666 0.5594 0.0192  -0.0624 0.1108  528 LEU B N   
8402 C CA  . LEU B 530 ? 0.5172 0.4826 0.5711 0.0129  -0.0571 0.1183  528 LEU B CA  
8403 C C   . LEU B 530 ? 0.5271 0.5111 0.5231 -0.0108 -0.0585 0.1281  528 LEU B C   
8404 O O   . LEU B 530 ? 0.4892 0.4994 0.4635 -0.0189 -0.0519 0.1126  528 LEU B O   
8405 C CB  . LEU B 530 ? 0.4555 0.4042 0.5048 0.0221  -0.0279 0.0895  528 LEU B CB  
8406 C CG  . LEU B 530 ? 0.5256 0.4648 0.6217 0.0429  -0.0175 0.0694  528 LEU B CG  
8407 C CD1 . LEU B 530 ? 0.4941 0.4284 0.5657 0.0441  0.0104  0.0451  528 LEU B CD1 
8408 C CD2 . LEU B 530 ? 0.5841 0.4975 0.7216 0.0532  -0.0350 0.0797  528 LEU B CD2 
8409 N N   . PRO B 531 ? 0.5671 0.5416 0.5414 -0.0236 -0.0666 0.1514  529 PRO B N   
8410 C CA  . PRO B 531 ? 0.5606 0.5614 0.4792 -0.0470 -0.0599 0.1530  529 PRO B CA  
8411 C C   . PRO B 531 ? 0.4802 0.4808 0.3824 -0.0430 -0.0301 0.1154  529 PRO B C   
8412 O O   . PRO B 531 ? 0.5050 0.4785 0.4264 -0.0279 -0.0159 0.1004  529 PRO B O   
8413 C CB  . PRO B 531 ? 0.6293 0.6150 0.5396 -0.0600 -0.0698 0.1851  529 PRO B CB  
8414 C CG  . PRO B 531 ? 0.6912 0.6315 0.6546 -0.0389 -0.0740 0.1861  529 PRO B CG  
8415 C CD  . PRO B 531 ? 0.6213 0.5630 0.6265 -0.0189 -0.0816 0.1754  529 PRO B CD  
8416 N N   . THR B 532 ? 0.5099 0.5434 0.3796 -0.0567 -0.0224 0.0989  530 THR B N   
8417 C CA  . THR B 532 ? 0.4762 0.5095 0.3412 -0.0523 0.0009  0.0642  530 THR B CA  
8418 C C   . THR B 532 ? 0.5589 0.6150 0.3909 -0.0685 0.0121  0.0557  530 THR B C   
8419 O O   . THR B 532 ? 0.5588 0.6473 0.3613 -0.0885 0.0041  0.0706  530 THR B O   
8420 C CB  . THR B 532 ? 0.4333 0.4839 0.3090 -0.0502 0.0021  0.0399  530 THR B CB  
8421 O OG1 . THR B 532 ? 0.6200 0.7121 0.4703 -0.0683 -0.0096 0.0385  530 THR B OG1 
8422 C CG2 . THR B 532 ? 0.4925 0.5278 0.4063 -0.0353 -0.0051 0.0461  530 THR B CG2 
8423 N N   . GLN B 533 ? 0.5448 0.5888 0.3838 -0.0608 0.0304  0.0327  531 GLN B N   
8424 C CA  . GLN B 533 ? 0.5937 0.6622 0.4148 -0.0722 0.0441  0.0160  531 GLN B CA  
8425 C C   . GLN B 533 ? 0.4744 0.5317 0.3192 -0.0587 0.0580  -0.0159 531 GLN B C   
8426 O O   . GLN B 533 ? 0.5014 0.5244 0.3672 -0.0433 0.0590  -0.0126 531 GLN B O   
8427 C CB  . GLN B 533 ? 0.5928 0.6522 0.4053 -0.0797 0.0458  0.0382  531 GLN B CB  
8428 C CG  . GLN B 533 ? 0.5975 0.6715 0.3884 -0.0992 0.0308  0.0754  531 GLN B CG  
8429 C CD  . GLN B 533 ? 0.6795 0.8095 0.4351 -0.1256 0.0387  0.0727  531 GLN B CD  
8430 O OE1 . GLN B 533 ? 0.6901 0.8360 0.4436 -0.1317 0.0559  0.0575  531 GLN B OE1 
8431 N NE2 . GLN B 533 ? 0.6424 0.8085 0.3713 -0.1423 0.0259  0.0866  531 GLN B NE2 
8432 N N   . THR B 534 ? 0.4412 0.5305 0.2854 -0.0652 0.0674  -0.0469 532 THR B N   
8433 C CA  . THR B 534 ? 0.5276 0.6040 0.4035 -0.0523 0.0771  -0.0729 532 THR B CA  
8434 C C   . THR B 534 ? 0.5431 0.6135 0.4185 -0.0517 0.0847  -0.0653 532 THR B C   
8435 O O   . THR B 534 ? 0.5339 0.6215 0.3850 -0.0656 0.0863  -0.0491 532 THR B O   
8436 C CB  . THR B 534 ? 0.5305 0.6425 0.4203 -0.0567 0.0841  -0.1157 532 THR B CB  
8437 O OG1 . THR B 534 ? 0.5240 0.6852 0.3866 -0.0742 0.0938  -0.1256 532 THR B OG1 
8438 C CG2 . THR B 534 ? 0.5644 0.6848 0.4569 -0.0598 0.0746  -0.1273 532 THR B CG2 
8439 N N   . VAL B 535 ? 0.5040 0.5515 0.4089 -0.0374 0.0872  -0.0742 533 VAL B N   
8440 C CA  . VAL B 535 ? 0.5385 0.5833 0.4470 -0.0367 0.0918  -0.0692 533 VAL B CA  
8441 C C   . VAL B 535 ? 0.4957 0.5876 0.3993 -0.0510 0.1034  -0.0872 533 VAL B C   
8442 O O   . VAL B 535 ? 0.4593 0.5616 0.3483 -0.0625 0.1068  -0.0718 533 VAL B O   
8443 C CB  . VAL B 535 ? 0.4723 0.4934 0.4152 -0.0206 0.0889  -0.0761 533 VAL B CB  
8444 C CG1 . VAL B 535 ? 0.4574 0.4762 0.4026 -0.0204 0.0897  -0.0684 533 VAL B CG1 
8445 C CG2 . VAL B 535 ? 0.4906 0.4774 0.4349 -0.0113 0.0806  -0.0587 533 VAL B CG2 
8446 N N   . ASP B 536 ? 0.4959 0.6206 0.4149 -0.0521 0.1105  -0.1225 534 ASP B N   
8447 C CA  . ASP B 536 ? 0.5914 0.7709 0.5105 -0.0655 0.1240  -0.1464 534 ASP B CA  
8448 C C   . ASP B 536 ? 0.5460 0.7529 0.4204 -0.0885 0.1218  -0.1199 534 ASP B C   
8449 O O   . ASP B 536 ? 0.6566 0.8932 0.5270 -0.1019 0.1274  -0.1148 534 ASP B O   
8450 C CB  . ASP B 536 ? 0.5636 0.7647 0.5196 -0.0587 0.1242  -0.1885 534 ASP B CB  
8451 C CG  . ASP B 536 ? 0.7011 0.8724 0.7148 -0.0361 0.1213  -0.2098 534 ASP B CG  
8452 O OD1 . ASP B 536 ? 0.6099 0.7339 0.6290 -0.0245 0.1115  -0.1912 534 ASP B OD1 
8453 O OD2 . ASP B 536 ? 0.7953 0.9878 0.8538 -0.0305 0.1234  -0.2374 534 ASP B OD2 
8454 N N   . SER B 537 ? 0.4961 0.6955 0.3405 -0.0945 0.1120  -0.1019 535 SER B N   
8455 C CA  . SER B 537 ? 0.5742 0.7961 0.3818 -0.1159 0.1045  -0.0702 535 SER B CA  
8456 C C   . SER B 537 ? 0.5843 0.7768 0.3791 -0.1218 0.0990  -0.0269 535 SER B C   
8457 O O   . SER B 537 ? 0.5145 0.7247 0.2920 -0.1405 0.0933  0.0005  535 SER B O   
8458 C CB  . SER B 537 ? 0.5877 0.8146 0.3732 -0.1204 0.0918  -0.0638 535 SER B CB  
8459 O OG  . SER B 537 ? 0.7033 0.8850 0.4850 -0.1103 0.0821  -0.0406 535 SER B OG  
8460 N N   . SER B 538 ? 0.4194 0.5642 0.2298 -0.1057 0.0976  -0.0206 536 SER B N   
8461 C CA  . SER B 538 ? 0.3984 0.5059 0.2106 -0.1067 0.0879  0.0146  536 SER B CA  
8462 C C   . SER B 538 ? 0.3956 0.5173 0.2165 -0.1174 0.0979  0.0150  536 SER B C   
8463 O O   . SER B 538 ? 0.4259 0.5272 0.2469 -0.1270 0.0897  0.0450  536 SER B O   
8464 C CB  . SER B 538 ? 0.3681 0.4212 0.2028 -0.0817 0.0795  0.0148  536 SER B CB  
8465 O OG  . SER B 538 ? 0.3424 0.3874 0.2000 -0.0690 0.0874  -0.0070 536 SER B OG  
8466 N N   . GLN B 539 ? 0.4341 0.5882 0.2717 -0.1149 0.1137  -0.0192 537 GLN B N   
8467 C CA  . GLN B 539 ? 0.4808 0.6536 0.3354 -0.1239 0.1233  -0.0221 537 GLN B CA  
8468 C C   . GLN B 539 ? 0.5199 0.7165 0.3575 -0.1498 0.1200  0.0077  537 GLN B C   
8469 O O   . GLN B 539 ? 0.4436 0.6738 0.2638 -0.1607 0.1183  0.0086  537 GLN B O   
8470 C CB  . GLN B 539 ? 0.3730 0.5843 0.2585 -0.1149 0.1367  -0.0660 537 GLN B CB  
8471 C CG  . GLN B 539 ? 0.4539 0.6883 0.3682 -0.1204 0.1462  -0.0743 537 GLN B CG  
8472 C CD  . GLN B 539 ? 0.4647 0.7246 0.4253 -0.1034 0.1541  -0.1188 537 GLN B CD  
8473 O OE1 . GLN B 539 ? 0.4404 0.6711 0.4293 -0.0807 0.1486  -0.1329 537 GLN B OE1 
8474 N NE2 . GLN B 539 ? 0.4281 0.7382 0.4007 -0.1133 0.1623  -0.1386 537 GLN B NE2 
8475 N N   . GLY B 540 ? 0.5001 0.6778 0.3457 -0.1609 0.1169  0.0323  538 GLY B N   
8476 C CA  . GLY B 540 ? 0.6324 0.8230 0.4711 -0.1850 0.1102  0.0656  538 GLY B CA  
8477 C C   . GLY B 540 ? 0.6706 0.8164 0.4993 -0.1905 0.0885  0.1087  538 GLY B C   
8478 O O   . GLY B 540 ? 0.5346 0.6786 0.3677 -0.2093 0.0789  0.1406  538 GLY B O   
8479 N N   . SER B 541 ? 0.5710 0.6812 0.3923 -0.1741 0.0795  0.1099  539 SER B N   
8480 C CA  . SER B 541 ? 0.6344 0.7013 0.4570 -0.1739 0.0566  0.1462  539 SER B CA  
8481 C C   . SER B 541 ? 0.5390 0.5450 0.3926 -0.1521 0.0475  0.1393  539 SER B C   
8482 O O   . SER B 541 ? 0.4981 0.4966 0.3627 -0.1327 0.0572  0.1055  539 SER B O   
8483 C CB  . SER B 541 ? 0.4992 0.5741 0.3017 -0.1653 0.0490  0.1460  539 SER B CB  
8484 O OG  . SER B 541 ? 0.7310 0.8577 0.5131 -0.1808 0.0497  0.1477  539 SER B OG  
8485 N N   . GLU B 542 ? 0.5516 0.5159 0.4249 -0.1535 0.0263  0.1691  540 GLU B N   
8486 C CA  . GLU B 542 ? 0.6360 0.5467 0.5440 -0.1310 0.0167  0.1551  540 GLU B CA  
8487 C C   . GLU B 542 ? 0.5918 0.4694 0.5173 -0.1182 -0.0032 0.1715  540 GLU B C   
8488 O O   . GLU B 542 ? 0.5359 0.4211 0.4562 -0.1331 -0.0178 0.2084  540 GLU B O   
8489 C CB  . GLU B 542 ? 0.4943 0.3838 0.4318 -0.1447 0.0105  0.1634  540 GLU B CB  
8490 C CG  . GLU B 542 ? 0.5917 0.4703 0.5450 -0.1719 -0.0083 0.2126  540 GLU B CG  
8491 C CD  . GLU B 542 ? 0.6792 0.5352 0.6691 -0.1870 -0.0146 0.2179  540 GLU B CD  
8492 O OE1 . GLU B 542 ? 0.6926 0.5443 0.6922 -0.1749 -0.0048 0.1803  540 GLU B OE1 
8493 O OE2 . GLU B 542 ? 0.7288 0.5810 0.7383 -0.1998 -0.0285 0.2458  540 GLU B OE2 
8494 N N   . TYR B 543 ? 0.5831 0.4296 0.5310 -0.0912 -0.0040 0.1439  541 TYR B N   
8495 C CA  . TYR B 543 ? 0.5638 0.3838 0.5390 -0.0742 -0.0197 0.1493  541 TYR B CA  
8496 C C   . TYR B 543 ? 0.5435 0.3277 0.5565 -0.0538 -0.0210 0.1188  541 TYR B C   
8497 O O   . TYR B 543 ? 0.5305 0.3187 0.5333 -0.0486 -0.0068 0.0888  541 TYR B O   
8498 C CB  . TYR B 543 ? 0.5843 0.4279 0.5378 -0.0608 -0.0121 0.1376  541 TYR B CB  
8499 C CG  . TYR B 543 ? 0.5707 0.4591 0.4811 -0.0781 -0.0041 0.1477  541 TYR B CG  
8500 C CD1 . TYR B 543 ? 0.5897 0.4967 0.4877 -0.0968 -0.0193 0.1843  541 TYR B CD1 
8501 C CD2 . TYR B 543 ? 0.6003 0.5154 0.4857 -0.0758 0.0171  0.1189  541 TYR B CD2 
8502 C CE1 . TYR B 543 ? 0.7114 0.6681 0.5670 -0.1140 -0.0104 0.1859  541 TYR B CE1 
8503 C CE2 . TYR B 543 ? 0.6541 0.6128 0.5081 -0.0899 0.0254  0.1182  541 TYR B CE2 
8504 C CZ  . TYR B 543 ? 0.7034 0.6857 0.5396 -0.1095 0.0133  0.1486  541 TYR B CZ  
8505 O OH  . TYR B 543 ? 0.7946 0.8287 0.5964 -0.1253 0.0230  0.1410  541 TYR B OH  
8506 N N   . ASP B 544 ? 0.5310 0.2843 0.5904 -0.0419 -0.0393 0.1242  542 ASP B N   
8507 C CA  . ASP B 544 ? 0.5358 0.2607 0.6360 -0.0231 -0.0396 0.0875  542 ASP B CA  
8508 C C   . ASP B 544 ? 0.5412 0.2872 0.6214 -0.0027 -0.0185 0.0473  542 ASP B C   
8509 O O   . ASP B 544 ? 0.5726 0.3201 0.6466 0.0027  -0.0070 0.0138  542 ASP B O   
8510 C CB  . ASP B 544 ? 0.5401 0.2288 0.7077 -0.0127 -0.0647 0.0977  542 ASP B CB  
8511 C CG  . ASP B 544 ? 0.8033 0.4669 0.9987 -0.0349 -0.0889 0.1399  542 ASP B CG  
8512 O OD1 . ASP B 544 ? 0.7890 0.4440 0.9836 -0.0496 -0.0864 0.1354  542 ASP B OD1 
8513 O OD2 . ASP B 544 ? 0.8883 0.5571 1.1005 -0.0369 -0.1076 0.1718  542 ASP B OD2 
8514 N N   . TYR B 545 ? 0.4542 0.2196 0.5243 0.0064  -0.0147 0.0522  543 TYR B N   
8515 C CA  . TYR B 545 ? 0.4857 0.2733 0.5410 0.0221  0.0045  0.0215  543 TYR B CA  
8516 C C   . TYR B 545 ? 0.4531 0.2707 0.4638 0.0149  0.0150  0.0339  543 TYR B C   
8517 O O   . TYR B 545 ? 0.5402 0.3659 0.5449 0.0064  0.0053  0.0605  543 TYR B O   
8518 C CB  . TYR B 545 ? 0.4512 0.2349 0.5541 0.0421  -0.0004 0.0075  543 TYR B CB  
8519 C CG  . TYR B 545 ? 0.5561 0.3151 0.7092 0.0535  -0.0060 -0.0220 543 TYR B CG  
8520 C CD1 . TYR B 545 ? 0.5680 0.3414 0.7149 0.0627  0.0125  -0.0666 543 TYR B CD1 
8521 C CD2 . TYR B 545 ? 0.5946 0.3174 0.8034 0.0535  -0.0316 -0.0054 543 TYR B CD2 
8522 C CE1 . TYR B 545 ? 0.5973 0.3528 0.7916 0.0727  0.0080  -0.1027 543 TYR B CE1 
8523 C CE2 . TYR B 545 ? 0.6444 0.3412 0.9099 0.0649  -0.0384 -0.0384 543 TYR B CE2 
8524 C CZ  . TYR B 545 ? 0.6496 0.3644 0.9074 0.0751  -0.0174 -0.0913 543 TYR B CZ  
8525 O OH  . TYR B 545 ? 0.7294 0.4363 1.0303 0.0823  -0.0225 -0.1267 543 TYR B OH  
8526 N N   . VAL B 546 ? 0.4031 0.2381 0.3853 0.0171  0.0326  0.0144  544 VAL B N   
8527 C CA  . VAL B 546 ? 0.3943 0.2529 0.3452 0.0117  0.0417  0.0203  544 VAL B CA  
8528 C C   . VAL B 546 ? 0.4687 0.3421 0.4179 0.0227  0.0547  0.0032  544 VAL B C   
8529 O O   . VAL B 546 ? 0.4793 0.3537 0.4286 0.0288  0.0626  -0.0158 544 VAL B O   
8530 C CB  . VAL B 546 ? 0.4339 0.2998 0.3588 -0.0002 0.0471  0.0206  544 VAL B CB  
8531 C CG1 . VAL B 546 ? 0.4127 0.3005 0.3189 -0.0017 0.0560  0.0184  544 VAL B CG1 
8532 C CG2 . VAL B 546 ? 0.3825 0.2448 0.3073 -0.0163 0.0374  0.0410  544 VAL B CG2 
8533 N N   . ILE B 547 ? 0.4542 0.3429 0.4018 0.0227  0.0564  0.0103  545 ILE B N   
8534 C CA  . ILE B 547 ? 0.4280 0.3336 0.3742 0.0275  0.0687  0.0012  545 ILE B CA  
8535 C C   . ILE B 547 ? 0.4259 0.3401 0.3539 0.0189  0.0710  0.0074  545 ILE B C   
8536 O O   . ILE B 547 ? 0.4292 0.3488 0.3568 0.0130  0.0643  0.0146  545 ILE B O   
8537 C CB  . ILE B 547 ? 0.4030 0.3196 0.3789 0.0355  0.0676  0.0005  545 ILE B CB  
8538 C CG1 . ILE B 547 ? 0.4172 0.3245 0.4246 0.0471  0.0641  -0.0117 545 ILE B CG1 
8539 C CG2 . ILE B 547 ? 0.4414 0.3803 0.4167 0.0354  0.0820  -0.0052 545 ILE B CG2 
8540 C CD1 . ILE B 547 ? 0.4470 0.3690 0.4964 0.0582  0.0625  -0.0166 545 ILE B CD1 
8541 N N   . PHE B 548 ? 0.3548 0.2722 0.2705 0.0177  0.0785  0.0034  546 PHE B N   
8542 C CA  . PHE B 548 ? 0.3854 0.3063 0.2968 0.0121  0.0783  0.0065  546 PHE B CA  
8543 C C   . PHE B 548 ? 0.4407 0.3700 0.3599 0.0115  0.0837  0.0113  546 PHE B C   
8544 O O   . PHE B 548 ? 0.3566 0.2925 0.2678 0.0122  0.0899  0.0131  546 PHE B O   
8545 C CB  . PHE B 548 ? 0.4226 0.3384 0.3224 0.0100  0.0767  0.0040  546 PHE B CB  
8546 C CG  . PHE B 548 ? 0.5165 0.4354 0.4244 0.0077  0.0747  0.0042  546 PHE B CG  
8547 C CD1 . PHE B 548 ? 0.3964 0.3213 0.3127 0.0042  0.0729  -0.0039 546 PHE B CD1 
8548 C CD2 . PHE B 548 ? 0.4083 0.3271 0.3190 0.0083  0.0735  0.0122  546 PHE B CD2 
8549 C CE1 . PHE B 548 ? 0.3664 0.2941 0.3030 0.0049  0.0705  -0.0108 546 PHE B CE1 
8550 C CE2 . PHE B 548 ? 0.3931 0.3097 0.3244 0.0080  0.0672  0.0140  546 PHE B CE2 
8551 C CZ  . PHE B 548 ? 0.4934 0.4128 0.4423 0.0081  0.0659  -0.0008 546 PHE B CZ  
8552 N N   . THR B 549 ? 0.3360 0.2681 0.2708 0.0077  0.0809  0.0131  547 THR B N   
8553 C CA  . THR B 549 ? 0.5042 0.4398 0.4541 0.0032  0.0828  0.0222  547 THR B CA  
8554 C C   . THR B 549 ? 0.4261 0.3511 0.3895 0.0009  0.0750  0.0207  547 THR B C   
8555 O O   . THR B 549 ? 0.4266 0.3518 0.4003 0.0005  0.0708  0.0062  547 THR B O   
8556 C CB  . THR B 549 ? 0.3756 0.3220 0.3473 0.0001  0.0838  0.0228  547 THR B CB  
8557 O OG1 . THR B 549 ? 0.4306 0.3764 0.4111 -0.0014 0.0754  0.0116  547 THR B OG1 
8558 C CG2 . THR B 549 ? 0.3284 0.2888 0.2993 0.0053  0.0909  0.0211  547 THR B CG2 
8559 N N   . GLN B 550 ? 0.3946 0.3145 0.3601 -0.0008 0.0722  0.0343  548 GLN B N   
8560 C CA  . GLN B 550 ? 0.4298 0.3378 0.4218 -0.0001 0.0616  0.0330  548 GLN B CA  
8561 C C   . GLN B 550 ? 0.4539 0.3552 0.4858 -0.0039 0.0563  0.0283  548 GLN B C   
8562 O O   . GLN B 550 ? 0.3957 0.2898 0.4587 -0.0007 0.0488  0.0113  548 GLN B O   
8563 C CB  . GLN B 550 ? 0.4034 0.3080 0.3922 -0.0021 0.0544  0.0560  548 GLN B CB  
8564 C CG  . GLN B 550 ? 0.4170 0.3115 0.4325 0.0035  0.0413  0.0518  548 GLN B CG  
8565 C CD  . GLN B 550 ? 0.5103 0.4042 0.5221 0.0005  0.0290  0.0803  548 GLN B CD  
8566 O OE1 . GLN B 550 ? 0.4914 0.3957 0.4765 -0.0087 0.0319  0.1039  548 GLN B OE1 
8567 N NE2 . GLN B 550 ? 0.4099 0.2982 0.4482 0.0073  0.0150  0.0775  548 GLN B NE2 
8568 N N   . THR B 551 ? 0.4512 0.3578 0.4889 -0.0111 0.0601  0.0397  549 THR B N   
8569 C CA  . THR B 551 ? 0.4381 0.3403 0.5160 -0.0174 0.0547  0.0340  549 THR B CA  
8570 C C   . THR B 551 ? 0.4469 0.3292 0.5687 -0.0233 0.0422  0.0520  549 THR B C   
8571 O O   . THR B 551 ? 0.4720 0.3528 0.6193 -0.0350 0.0402  0.0697  549 THR B O   
8572 C CB  . THR B 551 ? 0.4271 0.3331 0.5146 -0.0135 0.0517  -0.0010 549 THR B CB  
8573 O OG1 . THR B 551 ? 0.4112 0.3331 0.4578 -0.0097 0.0590  -0.0094 549 THR B OG1 
8574 C CG2 . THR B 551 ? 0.3526 0.2616 0.4740 -0.0216 0.0468  -0.0118 549 THR B CG2 
8575 N N   . THR B 552 ? 0.4096 0.2772 0.5475 -0.0163 0.0319  0.0499  550 THR B N   
8576 C CA  . THR B 552 ? 0.4386 0.2825 0.6296 -0.0199 0.0140  0.0695  550 THR B CA  
8577 C C   . THR B 552 ? 0.4952 0.3347 0.6771 -0.0138 0.0048  0.0881  550 THR B C   
8578 O O   . THR B 552 ? 0.4355 0.2907 0.5704 -0.0080 0.0137  0.0820  550 THR B O   
8579 C CB  . THR B 552 ? 0.5134 0.3408 0.7683 -0.0147 0.0030  0.0350  550 THR B CB  
8580 O OG1 . THR B 552 ? 0.5095 0.3435 0.7651 -0.0004 0.0041  0.0012  550 THR B OG1 
8581 C CG2 . THR B 552 ? 0.4260 0.2642 0.6851 -0.0210 0.0102  0.0095  550 THR B CG2 
8582 N N   . GLU B 553 ? 0.5459 0.3628 0.7794 -0.0159 -0.0164 0.1123  551 GLU B N   
8583 C CA  . GLU B 553 ? 0.5665 0.3780 0.8066 -0.0103 -0.0329 0.1338  551 GLU B CA  
8584 C C   . GLU B 553 ? 0.5710 0.3617 0.8871 0.0049  -0.0507 0.1077  551 GLU B C   
8585 O O   . GLU B 553 ? 0.6762 0.4546 1.0301 0.0085  -0.0739 0.1319  551 GLU B O   
8586 C CB  . GLU B 553 ? 0.5765 0.3837 0.8155 -0.0274 -0.0476 0.1940  551 GLU B CB  
8587 C CG  . GLU B 553 ? 0.6074 0.4441 0.7729 -0.0352 -0.0409 0.2211  551 GLU B CG  
8588 C CD  . GLU B 553 ? 0.7044 0.5533 0.8589 -0.0558 -0.0517 0.2726  551 GLU B CD  
8589 O OE1 . GLU B 553 ? 0.7012 0.5584 0.8552 -0.0699 -0.0414 0.2816  551 GLU B OE1 
8590 O OE2 . GLU B 553 ? 0.7255 0.5837 0.8712 -0.0577 -0.0700 0.2968  551 GLU B OE2 
8591 N N   . THR B 554 ? 0.5923 0.3860 0.9319 0.0134  -0.0405 0.0557  552 THR B N   
8592 C CA  . THR B 554 ? 0.6102 0.3953 1.0243 0.0284  -0.0524 0.0180  552 THR B CA  
8593 C C   . THR B 554 ? 0.5394 0.3426 0.9447 0.0420  -0.0509 0.0030  552 THR B C   
8594 O O   . THR B 554 ? 0.4736 0.2961 0.8105 0.0387  -0.0403 0.0183  552 THR B O   
8595 C CB  . THR B 554 ? 0.5702 0.3681 1.0001 0.0298  -0.0388 -0.0379 552 THR B CB  
8596 O OG1 . THR B 554 ? 0.5340 0.3628 0.8968 0.0299  -0.0148 -0.0628 552 THR B OG1 
8597 C CG2 . THR B 554 ? 0.4354 0.2216 0.8740 0.0153  -0.0410 -0.0252 552 THR B CG2 
8598 N N   . ALA B 555 ? 0.4706 0.2823 0.9396 0.0541  -0.0603 -0.0300 553 ALA B N   
8599 C CA  . ALA B 555 ? 0.4613 0.2950 0.9351 0.0669  -0.0570 -0.0516 553 ALA B CA  
8600 C C   . ALA B 555 ? 0.4874 0.3523 0.9047 0.0656  -0.0268 -0.0892 553 ALA B C   
8601 O O   . ALA B 555 ? 0.4851 0.3729 0.8607 0.0656  -0.0183 -0.0859 553 ALA B O   
8602 C CB  . ALA B 555 ? 0.4391 0.2879 0.9915 0.0756  -0.0699 -0.0829 553 ALA B CB  
8603 N N   . HIS B 556 ? 0.5321 0.4052 0.9410 0.0599  -0.0121 -0.1215 554 HIS B N   
8604 C CA  . HIS B 556 ? 0.5258 0.4359 0.8698 0.0523  0.0136  -0.1473 554 HIS B CA  
8605 C C   . HIS B 556 ? 0.4758 0.3858 0.7368 0.0420  0.0212  -0.1065 554 HIS B C   
8606 O O   . HIS B 556 ? 0.4789 0.4137 0.6965 0.0391  0.0343  -0.1118 554 HIS B O   
8607 C CB  . HIS B 556 ? 0.4294 0.3476 0.7775 0.0455  0.0219  -0.1812 554 HIS B CB  
8608 C CG  . HIS B 556 ? 0.5272 0.4817 0.8033 0.0339  0.0428  -0.1949 554 HIS B CG  
8609 N ND1 . HIS B 556 ? 0.4849 0.4851 0.7517 0.0322  0.0588  -0.2349 554 HIS B ND1 
8610 C CD2 . HIS B 556 ? 0.5020 0.4563 0.7163 0.0223  0.0487  -0.1709 554 HIS B CD2 
8611 C CE1 . HIS B 556 ? 0.4612 0.4849 0.6598 0.0182  0.0713  -0.2292 554 HIS B CE1 
8612 N NE2 . HIS B 556 ? 0.4813 0.4756 0.6511 0.0139  0.0641  -0.1918 554 HIS B NE2 
8613 N N   . SER B 557 ? 0.4175 0.3018 0.6611 0.0356  0.0133  -0.0670 555 SER B N   
8614 C CA  . SER B 557 ? 0.4447 0.3324 0.6173 0.0271  0.0221  -0.0371 555 SER B CA  
8615 C C   . SER B 557 ? 0.4599 0.3464 0.6138 0.0292  0.0144  -0.0094 555 SER B C   
8616 O O   . SER B 557 ? 0.4223 0.3167 0.5210 0.0238  0.0230  0.0040  555 SER B O   
8617 C CB  . SER B 557 ? 0.4791 0.3519 0.6413 0.0178  0.0210  -0.0121 555 SER B CB  
8618 O OG  . SER B 557 ? 0.6043 0.4580 0.7862 0.0151  0.0054  0.0261  555 SER B OG  
8619 N N   . CYS B 558 ? 0.4555 0.3328 0.6587 0.0367  -0.0041 -0.0012 556 CYS B N   
8620 C CA  . CYS B 558 ? 0.3757 0.2559 0.5639 0.0374  -0.0164 0.0262  556 CYS B CA  
8621 C C   . CYS B 558 ? 0.3828 0.2826 0.5940 0.0468  -0.0174 0.0010  556 CYS B C   
8622 O O   . CYS B 558 ? 0.4245 0.3298 0.6326 0.0481  -0.0310 0.0198  556 CYS B O   
8623 C CB  . CYS B 558 ? 0.4632 0.3219 0.6902 0.0364  -0.0427 0.0658  556 CYS B CB  
8624 S SG  . CYS B 558 ? 0.5963 0.4410 0.7944 0.0194  -0.0414 0.1057  556 CYS B SG  
8625 N N   . ASN B 559 ? 0.3687 0.2857 0.6022 0.0513  -0.0029 -0.0416 557 ASN B N   
8626 C CA  . ASN B 559 ? 0.4063 0.3520 0.6634 0.0574  0.0012  -0.0686 557 ASN B CA  
8627 C C   . ASN B 559 ? 0.3729 0.3332 0.5702 0.0485  0.0088  -0.0560 557 ASN B C   
8628 O O   . ASN B 559 ? 0.3402 0.3036 0.4822 0.0382  0.0251  -0.0560 557 ASN B O   
8629 C CB  . ASN B 559 ? 0.3713 0.3432 0.6489 0.0581  0.0208  -0.1173 557 ASN B CB  
8630 C CG  . ASN B 559 ? 0.3975 0.4095 0.7061 0.0622  0.0291  -0.1489 557 ASN B CG  
8631 O OD1 . ASN B 559 ? 0.4287 0.4622 0.6951 0.0526  0.0403  -0.1445 557 ASN B OD1 
8632 N ND2 . ASN B 559 ? 0.3570 0.3807 0.7470 0.0761  0.0235  -0.1826 557 ASN B ND2 
8633 N N   . VAL B 560 ? 0.3582 0.3259 0.5725 0.0524  -0.0064 -0.0445 558 VAL B N   
8634 C CA  . VAL B 560 ? 0.4202 0.3994 0.5852 0.0432  -0.0034 -0.0342 558 VAL B CA  
8635 C C   . VAL B 560 ? 0.3701 0.3733 0.5140 0.0344  0.0205  -0.0602 558 VAL B C   
8636 O O   . VAL B 560 ? 0.3890 0.3897 0.4820 0.0235  0.0282  -0.0514 558 VAL B O   
8637 C CB  . VAL B 560 ? 0.4388 0.4290 0.6359 0.0485  -0.0262 -0.0231 558 VAL B CB  
8638 C CG1 . VAL B 560 ? 0.5446 0.5132 0.7419 0.0504  -0.0524 0.0159  558 VAL B CG1 
8639 C CG2 . VAL B 560 ? 0.3848 0.3989 0.6601 0.0604  -0.0284 -0.0527 558 VAL B CG2 
8640 N N   . ASN B 561 ? 0.3642 0.3940 0.5499 0.0376  0.0317  -0.0925 559 ASN B N   
8641 C CA  . ASN B 561 ? 0.3610 0.4215 0.5226 0.0242  0.0546  -0.1114 559 ASN B CA  
8642 C C   . ASN B 561 ? 0.3853 0.4321 0.4928 0.0142  0.0666  -0.1038 559 ASN B C   
8643 O O   . ASN B 561 ? 0.3967 0.4464 0.4615 0.0005  0.0748  -0.0931 559 ASN B O   
8644 C CB  . ASN B 561 ? 0.3647 0.4680 0.5808 0.0278  0.0669  -0.1517 559 ASN B CB  
8645 C CG  . ASN B 561 ? 0.3924 0.5191 0.6679 0.0365  0.0569  -0.1617 559 ASN B CG  
8646 O OD1 . ASN B 561 ? 0.4070 0.5101 0.7077 0.0482  0.0321  -0.1416 559 ASN B OD1 
8647 N ND2 . ASN B 561 ? 0.2910 0.4700 0.5907 0.0293  0.0753  -0.1913 559 ASN B ND2 
8648 N N   . ARG B 562 ? 0.3844 0.4150 0.4997 0.0205  0.0649  -0.1079 560 ARG B N   
8649 C CA  . ARG B 562 ? 0.3474 0.3663 0.4173 0.0122  0.0726  -0.0992 560 ARG B CA  
8650 C C   . ARG B 562 ? 0.4002 0.3911 0.4273 0.0092  0.0664  -0.0672 560 ARG B C   
8651 O O   . ARG B 562 ? 0.4332 0.4232 0.4226 -0.0004 0.0733  -0.0589 560 ARG B O   
8652 C CB  . ARG B 562 ? 0.3553 0.3613 0.4503 0.0193  0.0687  -0.1097 560 ARG B CB  
8653 C CG  . ARG B 562 ? 0.4025 0.3987 0.4589 0.0117  0.0735  -0.1010 560 ARG B CG  
8654 C CD  . ARG B 562 ? 0.5217 0.5187 0.6119 0.0152  0.0721  -0.1246 560 ARG B CD  
8655 N NE  . ARG B 562 ? 0.4543 0.4925 0.5607 0.0113  0.0841  -0.1654 560 ARG B NE  
8656 C CZ  . ARG B 562 ? 0.4857 0.5372 0.6524 0.0210  0.0831  -0.1998 560 ARG B CZ  
8657 N NH1 . ARG B 562 ? 0.4662 0.4877 0.6863 0.0354  0.0667  -0.1920 560 ARG B NH1 
8658 N NH2 . ARG B 562 ? 0.4947 0.5942 0.6708 0.0152  0.0979  -0.2421 560 ARG B NH2 
8659 N N   . PHE B 563 ? 0.4216 0.3928 0.4567 0.0166  0.0522  -0.0497 561 PHE B N   
8660 C CA  . PHE B 563 ? 0.3834 0.3373 0.3785 0.0133  0.0486  -0.0273 561 PHE B CA  
8661 C C   . PHE B 563 ? 0.4799 0.4420 0.4540 0.0054  0.0519  -0.0290 561 PHE B C   
8662 O O   . PHE B 563 ? 0.5165 0.4680 0.4599 0.0003  0.0559  -0.0225 561 PHE B O   
8663 C CB  . PHE B 563 ? 0.4333 0.3765 0.4370 0.0186  0.0323  -0.0078 561 PHE B CB  
8664 C CG  . PHE B 563 ? 0.4285 0.3622 0.3905 0.0142  0.0323  0.0101  561 PHE B CG  
8665 C CD1 . PHE B 563 ? 0.4901 0.4160 0.4336 0.0121  0.0430  0.0123  561 PHE B CD1 
8666 C CD2 . PHE B 563 ? 0.5185 0.4575 0.4618 0.0116  0.0220  0.0211  561 PHE B CD2 
8667 C CE1 . PHE B 563 ? 0.5902 0.5153 0.5022 0.0089  0.0462  0.0226  561 PHE B CE1 
8668 C CE2 . PHE B 563 ? 0.4476 0.3873 0.3523 0.0067  0.0253  0.0298  561 PHE B CE2 
8669 C CZ  . PHE B 563 ? 0.4769 0.4105 0.3684 0.0060  0.0389  0.0293  561 PHE B CZ  
8670 N N   . ASN B 564 ? 0.4253 0.4065 0.4242 0.0043  0.0492  -0.0388 562 ASN B N   
8671 C CA  . ASN B 564 ? 0.4437 0.4338 0.4310 -0.0063 0.0515  -0.0402 562 ASN B CA  
8672 C C   . ASN B 564 ? 0.4182 0.4104 0.3842 -0.0182 0.0648  -0.0400 562 ASN B C   
8673 O O   . ASN B 564 ? 0.4607 0.4385 0.4062 -0.0257 0.0634  -0.0310 562 ASN B O   
8674 C CB  . ASN B 564 ? 0.3774 0.3961 0.4046 -0.0066 0.0484  -0.0529 562 ASN B CB  
8675 C CG  . ASN B 564 ? 0.4512 0.4834 0.4741 -0.0215 0.0519  -0.0543 562 ASN B CG  
8676 O OD1 . ASN B 564 ? 0.4827 0.4971 0.4839 -0.0264 0.0442  -0.0456 562 ASN B OD1 
8677 N ND2 . ASN B 564 ? 0.3797 0.4470 0.4278 -0.0301 0.0637  -0.0678 562 ASN B ND2 
8678 N N   . VAL B 565 ? 0.4415 0.4533 0.4149 -0.0210 0.0756  -0.0504 563 VAL B N   
8679 C CA  . VAL B 565 ? 0.4596 0.4798 0.4090 -0.0355 0.0849  -0.0443 563 VAL B CA  
8680 C C   . VAL B 565 ? 0.4057 0.3946 0.3289 -0.0324 0.0799  -0.0282 563 VAL B C   
8681 O O   . VAL B 565 ? 0.4281 0.4067 0.3359 -0.0418 0.0779  -0.0135 563 VAL B O   
8682 C CB  . VAL B 565 ? 0.3791 0.4361 0.3369 -0.0405 0.0973  -0.0631 563 VAL B CB  
8683 C CG1 . VAL B 565 ? 0.4192 0.4861 0.3435 -0.0568 0.1023  -0.0500 563 VAL B CG1 
8684 C CG2 . VAL B 565 ? 0.3677 0.4662 0.3558 -0.0462 0.1062  -0.0828 563 VAL B CG2 
8685 N N   . ALA B 566 ? 0.4482 0.4227 0.3735 -0.0196 0.0768  -0.0300 564 ALA B N   
8686 C CA  . ALA B 566 ? 0.4344 0.3880 0.3421 -0.0164 0.0744  -0.0183 564 ALA B CA  
8687 C C   . ALA B 566 ? 0.4290 0.3619 0.3264 -0.0163 0.0693  -0.0090 564 ALA B C   
8688 O O   . ALA B 566 ? 0.4304 0.3531 0.3211 -0.0202 0.0673  0.0002  564 ALA B O   
8689 C CB  . ALA B 566 ? 0.4465 0.3911 0.3630 -0.0054 0.0724  -0.0198 564 ALA B CB  
8690 N N   . ILE B 567 ? 0.4953 0.4232 0.3953 -0.0121 0.0649  -0.0127 565 ILE B N   
8691 C CA  . ILE B 567 ? 0.4709 0.3825 0.3629 -0.0112 0.0605  -0.0131 565 ILE B CA  
8692 C C   . ILE B 567 ? 0.5295 0.4365 0.4290 -0.0224 0.0568  -0.0126 565 ILE B C   
8693 O O   . ILE B 567 ? 0.5771 0.4658 0.4792 -0.0223 0.0520  -0.0156 565 ILE B O   
8694 C CB  . ILE B 567 ? 0.5621 0.4763 0.4470 -0.0054 0.0559  -0.0181 565 ILE B CB  
8695 C CG1 . ILE B 567 ? 0.5518 0.4792 0.4475 -0.0090 0.0486  -0.0212 565 ILE B CG1 
8696 C CG2 . ILE B 567 ? 0.5183 0.4361 0.3987 0.0014  0.0584  -0.0110 565 ILE B CG2 
8697 C CD1 . ILE B 567 ? 0.5995 0.5335 0.4840 -0.0061 0.0391  -0.0213 565 ILE B CD1 
8698 N N   . THR B 568 ? 0.4909 0.4160 0.3995 -0.0331 0.0590  -0.0106 566 THR B N   
8699 C CA  . THR B 568 ? 0.4629 0.3865 0.3819 -0.0484 0.0556  -0.0052 566 THR B CA  
8700 C C   . THR B 568 ? 0.4343 0.3518 0.3508 -0.0599 0.0555  0.0141  566 THR B C   
8701 O O   . THR B 568 ? 0.5071 0.4255 0.4341 -0.0774 0.0522  0.0266  566 THR B O   
8702 C CB  . THR B 568 ? 0.3895 0.3440 0.3234 -0.0581 0.0595  -0.0106 566 THR B CB  
8703 O OG1 . THR B 568 ? 0.4693 0.4516 0.4031 -0.0572 0.0702  -0.0143 566 THR B OG1 
8704 C CG2 . THR B 568 ? 0.4601 0.4176 0.4036 -0.0496 0.0516  -0.0241 566 THR B CG2 
8705 N N   . ARG B 569 ? 0.4561 0.3700 0.3611 -0.0528 0.0570  0.0201  567 ARG B N   
8706 C CA  . ARG B 569 ? 0.4526 0.3627 0.3550 -0.0635 0.0518  0.0429  567 ARG B CA  
8707 C C   . ARG B 569 ? 0.4687 0.3413 0.3901 -0.0587 0.0383  0.0507  567 ARG B C   
8708 O O   . ARG B 569 ? 0.4677 0.3306 0.3983 -0.0702 0.0275  0.0759  567 ARG B O   
8709 C CB  . ARG B 569 ? 0.4918 0.4158 0.3791 -0.0576 0.0554  0.0440  567 ARG B CB  
8710 C CG  . ARG B 569 ? 0.5023 0.4620 0.3796 -0.0597 0.0677  0.0290  567 ARG B CG  
8711 C CD  . ARG B 569 ? 0.3575 0.3525 0.2311 -0.0805 0.0751  0.0320  567 ARG B CD  
8712 N NE  . ARG B 569 ? 0.3497 0.3491 0.2408 -0.0803 0.0792  0.0192  567 ARG B NE  
8713 C CZ  . ARG B 569 ? 0.4680 0.4977 0.3652 -0.0987 0.0861  0.0211  567 ARG B CZ  
8714 N NH1 . ARG B 569 ? 0.3839 0.4405 0.2660 -0.1219 0.0897  0.0403  567 ARG B NH1 
8715 N NH2 . ARG B 569 ? 0.4814 0.5185 0.4008 -0.0958 0.0883  0.0062  567 ARG B NH2 
8716 N N   . ALA B 570 ? 0.4595 0.3139 0.3898 -0.0431 0.0376  0.0292  568 ALA B N   
8717 C CA  . ALA B 570 ? 0.4985 0.3220 0.4544 -0.0340 0.0274  0.0241  568 ALA B CA  
8718 C C   . ALA B 570 ? 0.4971 0.2986 0.4800 -0.0442 0.0166  0.0223  568 ALA B C   
8719 O O   . ALA B 570 ? 0.4895 0.2996 0.4683 -0.0504 0.0193  0.0092  568 ALA B O   
8720 C CB  . ALA B 570 ? 0.4289 0.2540 0.3798 -0.0149 0.0348  -0.0036 568 ALA B CB  
8721 N N   . LYS B 571 ? 0.5142 0.2862 0.5318 -0.0457 0.0015  0.0357  569 LYS B N   
8722 C CA  . LYS B 571 ? 0.5630 0.3052 0.6201 -0.0545 -0.0126 0.0323  569 LYS B CA  
8723 C C   . LYS B 571 ? 0.5768 0.2965 0.6650 -0.0350 -0.0164 -0.0076 569 LYS B C   
8724 O O   . LYS B 571 ? 0.6070 0.3099 0.7210 -0.0397 -0.0238 -0.0286 569 LYS B O   
8725 C CB  . LYS B 571 ? 0.5460 0.2658 0.6336 -0.0710 -0.0315 0.0750  569 LYS B CB  
8726 C CG  . LYS B 571 ? 0.6066 0.3580 0.6615 -0.0963 -0.0267 0.1139  569 LYS B CG  
8727 C CD  . LYS B 571 ? 0.7198 0.4520 0.8030 -0.1190 -0.0482 0.1630  569 LYS B CD  
8728 C CE  . LYS B 571 ? 0.6672 0.3893 0.7592 -0.1094 -0.0630 0.1874  569 LYS B CE  
8729 N NZ  . LYS B 571 ? 0.8829 0.6049 0.9953 -0.1253 -0.0829 0.2280  569 LYS B NZ  
8730 N N   . VAL B 572 ? 0.5867 0.3108 0.6756 -0.0144 -0.0108 -0.0222 570 VAL B N   
8731 C CA  . VAL B 572 ? 0.5874 0.2992 0.7106 0.0041  -0.0115 -0.0647 570 VAL B CA  
8732 C C   . VAL B 572 ? 0.6068 0.3546 0.6925 0.0183  0.0093  -0.0939 570 VAL B C   
8733 O O   . VAL B 572 ? 0.6004 0.3621 0.6742 0.0208  0.0165  -0.1302 570 VAL B O   
8734 C CB  . VAL B 572 ? 0.6153 0.2975 0.7985 0.0153  -0.0279 -0.0560 570 VAL B CB  
8735 C CG1 . VAL B 572 ? 0.6437 0.3213 0.8696 0.0368  -0.0251 -0.1099 570 VAL B CG1 
8736 C CG2 . VAL B 572 ? 0.6416 0.2856 0.8662 -0.0023 -0.0526 -0.0208 570 VAL B CG2 
8737 N N   . GLY B 573 ? 0.5706 0.3363 0.6384 0.0252  0.0178  -0.0773 571 GLY B N   
8738 C CA  . GLY B 573 ? 0.5114 0.3109 0.5500 0.0355  0.0365  -0.0980 571 GLY B CA  
8739 C C   . GLY B 573 ? 0.5257 0.3465 0.5234 0.0299  0.0449  -0.0698 571 GLY B C   
8740 O O   . GLY B 573 ? 0.4833 0.2968 0.4788 0.0219  0.0377  -0.0390 571 GLY B O   
8741 N N   . ILE B 574 ? 0.4808 0.3304 0.4470 0.0326  0.0597  -0.0815 572 ILE B N   
8742 C CA  . ILE B 574 ? 0.4416 0.3088 0.3790 0.0285  0.0665  -0.0594 572 ILE B CA  
8743 C C   . ILE B 574 ? 0.4941 0.3903 0.4178 0.0340  0.0812  -0.0710 572 ILE B C   
8744 O O   . ILE B 574 ? 0.4519 0.3648 0.3649 0.0349  0.0880  -0.0943 572 ILE B O   
8745 C CB  . ILE B 574 ? 0.5201 0.3901 0.4317 0.0170  0.0639  -0.0472 572 ILE B CB  
8746 C CG1 . ILE B 574 ? 0.5470 0.4309 0.4432 0.0149  0.0687  -0.0291 572 ILE B CG1 
8747 C CG2 . ILE B 574 ? 0.4920 0.3742 0.3855 0.0149  0.0652  -0.0655 572 ILE B CG2 
8748 C CD1 . ILE B 574 ? 0.4789 0.3657 0.3663 0.0061  0.0651  -0.0190 572 ILE B CD1 
8749 N N   . LEU B 575 ? 0.4665 0.3727 0.3907 0.0350  0.0858  -0.0548 573 LEU B N   
8750 C CA  . LEU B 575 ? 0.4437 0.3791 0.3550 0.0344  0.0993  -0.0551 573 LEU B CA  
8751 C C   . LEU B 575 ? 0.3903 0.3265 0.2841 0.0259  0.0971  -0.0305 573 LEU B C   
8752 O O   . LEU B 575 ? 0.4497 0.3755 0.3545 0.0251  0.0911  -0.0178 573 LEU B O   
8753 C CB  . LEU B 575 ? 0.4177 0.3659 0.3601 0.0430  0.1059  -0.0615 573 LEU B CB  
8754 C CG  . LEU B 575 ? 0.4903 0.4729 0.4246 0.0385  0.1212  -0.0573 573 LEU B CG  
8755 C CD1 . LEU B 575 ? 0.4237 0.4362 0.3312 0.0334  0.1344  -0.0738 573 LEU B CD1 
8756 C CD2 . LEU B 575 ? 0.3797 0.3773 0.3541 0.0470  0.1264  -0.0642 573 LEU B CD2 
8757 N N   . CYS B 576 ? 0.3481 0.2982 0.2177 0.0192  0.0998  -0.0248 574 CYS B N   
8758 C CA  . CYS B 576 ? 0.4069 0.3563 0.2719 0.0127  0.0954  -0.0028 574 CYS B CA  
8759 C C   . CYS B 576 ? 0.5246 0.4967 0.3871 0.0066  0.1042  0.0099  574 CYS B C   
8760 O O   . CYS B 576 ? 0.4032 0.3995 0.2441 0.0007  0.1105  0.0099  574 CYS B O   
8761 C CB  . CYS B 576 ? 0.4308 0.3768 0.2804 0.0084  0.0858  0.0022  574 CYS B CB  
8762 S SG  . CYS B 576 ? 0.5460 0.4714 0.4041 0.0102  0.0763  -0.0068 574 CYS B SG  
8763 N N   . ILE B 577 ? 0.4145 0.3831 0.2985 0.0052  0.1043  0.0210  575 ILE B N   
8764 C CA  . ILE B 577 ? 0.5558 0.5427 0.4451 -0.0046 0.1102  0.0393  575 ILE B CA  
8765 C C   . ILE B 577 ? 0.5484 0.5198 0.4427 -0.0112 0.0967  0.0611  575 ILE B C   
8766 O O   . ILE B 577 ? 0.4734 0.4252 0.3925 -0.0087 0.0884  0.0606  575 ILE B O   
8767 C CB  . ILE B 577 ? 0.5133 0.5053 0.4322 -0.0037 0.1152  0.0375  575 ILE B CB  
8768 C CG1 . ILE B 577 ? 0.5016 0.4995 0.4302 0.0078  0.1208  0.0149  575 ILE B CG1 
8769 C CG2 . ILE B 577 ? 0.4966 0.5146 0.4231 -0.0170 0.1245  0.0559  575 ILE B CG2 
8770 C CD1 . ILE B 577 ? 0.3467 0.3726 0.2648 0.0099  0.1354  -0.0014 575 ILE B CD1 
8771 N N   . MET B 578 ? 0.5602 0.5434 0.4343 -0.0196 0.0931  0.0789  576 MET B N   
8772 C CA  . MET B 578 ? 0.4737 0.4406 0.3604 -0.0234 0.0752  0.1013  576 MET B CA  
8773 C C   . MET B 578 ? 0.5781 0.5450 0.4889 -0.0363 0.0701  0.1331  576 MET B C   
8774 O O   . MET B 578 ? 0.5776 0.5702 0.4788 -0.0487 0.0818  0.1473  576 MET B O   
8775 C CB  . MET B 578 ? 0.4058 0.3847 0.2615 -0.0268 0.0667  0.1093  576 MET B CB  
8776 C CG  . MET B 578 ? 0.6292 0.6059 0.4676 -0.0169 0.0691  0.0791  576 MET B CG  
8777 S SD  . MET B 578 ? 0.5042 0.4492 0.3778 -0.0048 0.0628  0.0622  576 MET B SD  
8778 C CE  . MET B 578 ? 0.5310 0.4662 0.4289 -0.0048 0.0410  0.0808  576 MET B CE  
8779 N N   . SER B 579 ? 0.6120 0.5517 0.5599 -0.0341 0.0520  0.1435  577 SER B N   
8780 C CA  . SER B 579 ? 0.5164 0.4455 0.5009 -0.0461 0.0396  0.1767  577 SER B CA  
8781 C C   . SER B 579 ? 0.5147 0.4355 0.5076 -0.0499 0.0162  0.2083  577 SER B C   
8782 O O   . SER B 579 ? 0.6474 0.5713 0.6511 -0.0665 0.0054  0.2509  577 SER B O   
8783 C CB  . SER B 579 ? 0.4849 0.3858 0.5243 -0.0393 0.0335  0.1585  577 SER B CB  
8784 O OG  . SER B 579 ? 0.4847 0.3951 0.5204 -0.0378 0.0498  0.1348  577 SER B OG  
8785 N N   . ASP B 580 ? 0.5594 0.4728 0.5492 -0.0366 0.0069  0.1915  578 ASP B N   
8786 C CA  . ASP B 580 ? 0.5526 0.4602 0.5572 -0.0371 -0.0190 0.2185  578 ASP B CA  
8787 C C   . ASP B 580 ? 0.6081 0.5498 0.5497 -0.0465 -0.0180 0.2328  578 ASP B C   
8788 O O   . ASP B 580 ? 0.5226 0.4784 0.4278 -0.0395 -0.0046 0.2007  578 ASP B O   
8789 C CB  . ASP B 580 ? 0.6282 0.5161 0.6729 -0.0177 -0.0290 0.1879  578 ASP B CB  
8790 C CG  . ASP B 580 ? 0.6484 0.5349 0.7133 -0.0149 -0.0570 0.2108  578 ASP B CG  
8791 O OD1 . ASP B 580 ? 0.7037 0.5813 0.7963 -0.0241 -0.0798 0.2547  578 ASP B OD1 
8792 O OD2 . ASP B 580 ? 0.6589 0.5538 0.7177 -0.0043 -0.0584 0.1872  578 ASP B OD2 
8793 N N   . ARG B 581 ? 0.6021 0.5585 0.5328 -0.0642 -0.0340 0.2814  579 ARG B N   
8794 C CA  . ARG B 581 ? 0.6526 0.6498 0.5210 -0.0752 -0.0345 0.2896  579 ARG B CA  
8795 C C   . ARG B 581 ? 0.6604 0.6560 0.5250 -0.0633 -0.0515 0.2764  579 ARG B C   
8796 O O   . ARG B 581 ? 0.6737 0.6988 0.4864 -0.0657 -0.0434 0.2560  579 ARG B O   
8797 C CB  . ARG B 581 ? 0.6285 0.6435 0.4972 -0.0926 -0.0489 0.3264  579 ARG B CB  
8798 C CG  . ARG B 581 ? 0.7450 0.8063 0.5533 -0.1050 -0.0500 0.3301  579 ARG B CG  
8799 C CD  . ARG B 581 ? 0.8194 0.9165 0.5740 -0.1098 -0.0160 0.2968  579 ARG B CD  
8800 N NE  . ARG B 581 ? 0.9402 1.0812 0.6417 -0.1190 -0.0170 0.2888  579 ARG B NE  
8801 C CZ  . ARG B 581 ? 0.9077 1.0796 0.5920 -0.1375 -0.0301 0.3197  579 ARG B CZ  
8802 N NH1 . ARG B 581 ? 0.8879 1.0576 0.5980 -0.1511 -0.0373 0.3590  579 ARG B NH1 
8803 N NH2 . ARG B 581 ? 0.9564 1.1660 0.5958 -0.1445 -0.0352 0.3096  579 ARG B NH2 
8804 N N   . ASP B 582 ? 0.7266 0.6901 0.6535 -0.0494 -0.0743 0.2796  580 ASP B N   
8805 C CA  . ASP B 582 ? 0.6501 0.6160 0.5863 -0.0375 -0.0911 0.2641  580 ASP B CA  
8806 C C   . ASP B 582 ? 0.5656 0.5386 0.4730 -0.0278 -0.0665 0.2108  580 ASP B C   
8807 O O   . ASP B 582 ? 0.5184 0.5163 0.3845 -0.0317 -0.0679 0.1998  580 ASP B O   
8808 C CB  . ASP B 582 ? 0.7134 0.6462 0.7358 -0.0215 -0.1142 0.2668  580 ASP B CB  
8809 C CG  . ASP B 582 ? 0.7675 0.7079 0.8124 -0.0087 -0.1315 0.2501  580 ASP B CG  
8810 O OD1 . ASP B 582 ? 0.7797 0.7469 0.7727 -0.0130 -0.1264 0.2359  580 ASP B OD1 
8811 O OD2 . ASP B 582 ? 0.8323 0.7533 0.9539 0.0056  -0.1513 0.2492  580 ASP B OD2 
8812 N N   . LEU B 583 ? 0.5492 0.5012 0.4806 -0.0167 -0.0463 0.1784  581 LEU B N   
8813 C CA  . LEU B 583 ? 0.5997 0.5556 0.5095 -0.0098 -0.0265 0.1359  581 LEU B CA  
8814 C C   . LEU B 583 ? 0.5689 0.5462 0.4198 -0.0192 -0.0077 0.1266  581 LEU B C   
8815 O O   . LEU B 583 ? 0.5741 0.5604 0.4015 -0.0174 -0.0011 0.0998  581 LEU B O   
8816 C CB  . LEU B 583 ? 0.4420 0.3767 0.3867 0.0006  -0.0119 0.1093  581 LEU B CB  
8817 C CG  . LEU B 583 ? 0.5538 0.4770 0.5583 0.0123  -0.0245 0.0986  581 LEU B CG  
8818 C CD1 . LEU B 583 ? 0.5640 0.4760 0.5947 0.0185  -0.0085 0.0707  581 LEU B CD1 
8819 C CD2 . LEU B 583 ? 0.5268 0.4647 0.5304 0.0159  -0.0306 0.0829  581 LEU B CD2 
8820 N N   . TYR B 584 ? 0.5290 0.5168 0.3620 -0.0297 0.0011  0.1464  582 TYR B N   
8821 C CA  . TYR B 584 ? 0.5984 0.6148 0.3827 -0.0376 0.0211  0.1319  582 TYR B CA  
8822 C C   . TYR B 584 ? 0.5176 0.5662 0.2585 -0.0464 0.0116  0.1308  582 TYR B C   
8823 O O   . TYR B 584 ? 0.5105 0.5762 0.2228 -0.0459 0.0249  0.0969  582 TYR B O   
8824 C CB  . TYR B 584 ? 0.4928 0.5248 0.2700 -0.0503 0.0324  0.1563  582 TYR B CB  
8825 C CG  . TYR B 584 ? 0.5871 0.6613 0.3181 -0.0599 0.0544  0.1402  582 TYR B CG  
8826 C CD1 . TYR B 584 ? 0.5927 0.6667 0.3300 -0.0510 0.0778  0.1056  582 TYR B CD1 
8827 C CD2 . TYR B 584 ? 0.5606 0.6754 0.2499 -0.0759 0.0503  0.1544  582 TYR B CD2 
8828 C CE1 . TYR B 584 ? 0.6095 0.7252 0.3166 -0.0570 0.0987  0.0836  582 TYR B CE1 
8829 C CE2 . TYR B 584 ? 0.6896 0.8396 0.3533 -0.0794 0.0709  0.1254  582 TYR B CE2 
8830 C CZ  . TYR B 584 ? 0.5557 0.7050 0.2313 -0.0689 0.0951  0.0895  582 TYR B CZ  
8831 O OH  . TYR B 584 ? 0.5908 0.7744 0.2530 -0.0699 0.1137  0.0586  582 TYR B OH  
8832 N N   . ASP B 585 ? 0.5392 0.5969 0.2795 -0.0547 -0.0142 0.1666  583 ASP B N   
8833 C CA  . ASP B 585 ? 0.6360 0.7309 0.3313 -0.0659 -0.0274 0.1682  583 ASP B CA  
8834 C C   . ASP B 585 ? 0.5822 0.6664 0.2903 -0.0543 -0.0364 0.1349  583 ASP B C   
8835 O O   . ASP B 585 ? 0.5824 0.6958 0.2532 -0.0615 -0.0402 0.1157  583 ASP B O   
8836 C CB  . ASP B 585 ? 0.6235 0.7337 0.3161 -0.0802 -0.0574 0.2243  583 ASP B CB  
8837 C CG  . ASP B 585 ? 0.8425 0.9715 0.5230 -0.0941 -0.0448 0.2430  583 ASP B CG  
8838 O OD1 . ASP B 585 ? 0.8370 0.9760 0.5014 -0.0951 -0.0148 0.2185  583 ASP B OD1 
8839 O OD2 . ASP B 585 ? 0.7765 0.9129 0.4671 -0.1049 -0.0661 0.2824  583 ASP B OD2 
8840 N N   . LYS B 586 ? 0.5977 0.6452 0.3595 -0.0387 -0.0397 0.1266  584 LYS B N   
8841 C CA  . LYS B 586 ? 0.5033 0.5431 0.2838 -0.0302 -0.0452 0.0971  584 LYS B CA  
8842 C C   . LYS B 586 ? 0.5479 0.5814 0.3143 -0.0272 -0.0216 0.0548  584 LYS B C   
8843 O O   . LYS B 586 ? 0.6288 0.6632 0.3994 -0.0265 -0.0261 0.0304  584 LYS B O   
8844 C CB  . LYS B 586 ? 0.5105 0.5232 0.3542 -0.0170 -0.0533 0.1012  584 LYS B CB  
8845 C CG  . LYS B 586 ? 0.5637 0.5828 0.4393 -0.0163 -0.0856 0.1335  584 LYS B CG  
8846 C CD  . LYS B 586 ? 0.6126 0.6073 0.5606 -0.0015 -0.0906 0.1329  584 LYS B CD  
8847 C CE  . LYS B 586 ? 0.6786 0.6795 0.6733 0.0027  -0.1264 0.1602  584 LYS B CE  
8848 N NZ  . LYS B 586 ? 0.8243 0.8006 0.8958 0.0168  -0.1334 0.1641  584 LYS B NZ  
8849 N N   . LEU B 587 ? 0.5601 0.5869 0.3168 -0.0258 0.0009  0.0473  585 LEU B N   
8850 C CA  . LEU B 587 ? 0.5084 0.5254 0.2630 -0.0211 0.0194  0.0112  585 LEU B CA  
8851 C C   . LEU B 587 ? 0.5543 0.5998 0.2717 -0.0287 0.0218  -0.0146 585 LEU B C   
8852 O O   . LEU B 587 ? 0.5541 0.6326 0.2359 -0.0378 0.0271  -0.0089 585 LEU B O   
8853 C CB  . LEU B 587 ? 0.5190 0.5242 0.2820 -0.0163 0.0390  0.0122  585 LEU B CB  
8854 C CG  . LEU B 587 ? 0.5074 0.4835 0.3087 -0.0081 0.0403  0.0207  585 LEU B CG  
8855 C CD1 . LEU B 587 ? 0.4588 0.4291 0.2655 -0.0051 0.0572  0.0191  585 LEU B CD1 
8856 C CD2 . LEU B 587 ? 0.5336 0.4932 0.3550 -0.0039 0.0378  0.0022  585 LEU B CD2 
8857 N N   . GLN B 588 ? 0.5196 0.5562 0.2468 -0.0271 0.0181  -0.0447 586 GLN B N   
8858 C CA  . GLN B 588 ? 0.5829 0.6443 0.2838 -0.0336 0.0191  -0.0799 586 GLN B CA  
8859 C C   . GLN B 588 ? 0.6512 0.7024 0.3633 -0.0262 0.0402  -0.1130 586 GLN B C   
8860 O O   . GLN B 588 ? 0.6254 0.6619 0.3577 -0.0234 0.0399  -0.1474 586 GLN B O   
8861 C CB  . GLN B 588 ? 0.5275 0.5843 0.2419 -0.0374 0.0007  -0.0965 586 GLN B CB  
8862 C CG  . GLN B 588 ? 0.5519 0.6177 0.2713 -0.0412 -0.0221 -0.0642 586 GLN B CG  
8863 C CD  . GLN B 588 ? 0.7183 0.7918 0.4495 -0.0476 -0.0416 -0.0825 586 GLN B CD  
8864 O OE1 . GLN B 588 ? 0.6889 0.7641 0.4167 -0.0521 -0.0397 -0.1206 586 GLN B OE1 
8865 N NE2 . GLN B 588 ? 0.6160 0.6941 0.3693 -0.0478 -0.0615 -0.0579 586 GLN B NE2 
8866 N N   . PHE B 589 ? 0.5701 0.6298 0.2761 -0.0233 0.0568  -0.1013 587 PHE B N   
8867 C CA  . PHE B 589 ? 0.5085 0.5608 0.2353 -0.0137 0.0757  -0.1273 587 PHE B CA  
8868 C C   . PHE B 589 ? 0.6426 0.7438 0.3402 -0.0191 0.0923  -0.1428 587 PHE B C   
8869 O O   . PHE B 589 ? 0.6232 0.7570 0.2862 -0.0311 0.0872  -0.1210 587 PHE B O   
8870 C CB  . PHE B 589 ? 0.5219 0.5452 0.2778 -0.0050 0.0823  -0.1018 587 PHE B CB  
8871 C CG  . PHE B 589 ? 0.5765 0.5598 0.3609 -0.0011 0.0704  -0.0867 587 PHE B CG  
8872 C CD1 . PHE B 589 ? 0.6248 0.5936 0.4197 -0.0037 0.0577  -0.0993 587 PHE B CD1 
8873 C CD2 . PHE B 589 ? 0.5543 0.5200 0.3565 0.0031  0.0731  -0.0622 587 PHE B CD2 
8874 C CE1 . PHE B 589 ? 0.5263 0.4681 0.3465 -0.0035 0.0504  -0.0845 587 PHE B CE1 
8875 C CE2 . PHE B 589 ? 0.5759 0.5159 0.3998 0.0041  0.0654  -0.0517 587 PHE B CE2 
8876 C CZ  . PHE B 589 ? 0.5903 0.5205 0.4222 0.0003  0.0553  -0.0616 587 PHE B CZ  
8877 N N   . THR B 590 ? 0.6330 0.7305 0.3617 -0.0078 0.1064  -0.1704 588 THR B N   
8878 C CA  . THR B 590 ? 0.6045 0.7416 0.3270 -0.0096 0.1205  -0.1821 588 THR B CA  
8879 C C   . THR B 590 ? 0.5830 0.7337 0.3003 -0.0132 0.1324  -0.1465 588 THR B C   
8880 O O   . THR B 590 ? 0.5248 0.6508 0.2696 -0.0047 0.1373  -0.1363 588 THR B O   
8881 C CB  . THR B 590 ? 0.6009 0.7304 0.3690 0.0046  0.1285  -0.2267 588 THR B CB  
8882 O OG1 . THR B 590 ? 0.6104 0.7279 0.3871 0.0050  0.1157  -0.2590 588 THR B OG1 
8883 C CG2 . THR B 590 ? 0.6221 0.7990 0.3892 0.0025  0.1463  -0.2416 588 THR B CG2 
8884 N N   . SER B 591 ? 0.5944 0.7847 0.2786 -0.0280 0.1355  -0.1260 589 SER B N   
8885 C CA  . SER B 591 ? 0.5879 0.7915 0.2713 -0.0351 0.1452  -0.0903 589 SER B CA  
8886 C C   . SER B 591 ? 0.6571 0.8811 0.3703 -0.0278 0.1666  -0.1145 589 SER B C   
8887 O O   . SER B 591 ? 0.6909 0.9450 0.4060 -0.0268 0.1754  -0.1504 589 SER B O   
8888 C CB  . SER B 591 ? 0.6369 0.8747 0.2799 -0.0558 0.1383  -0.0566 589 SER B CB  
8889 O OG  . SER B 591 ? 0.7676 1.0486 0.3887 -0.0632 0.1434  -0.0848 589 SER B OG  
8890 N N   . LEU B 592 ? 0.6676 0.8791 0.4075 -0.0234 0.1743  -0.0962 590 LEU B N   
8891 C CA  . LEU B 592 ? 0.5974 0.8317 0.3712 -0.0171 0.1931  -0.1138 590 LEU B CA  
8892 C C   . LEU B 592 ? 0.6227 0.8833 0.3884 -0.0336 0.2021  -0.0760 590 LEU B C   
8893 O O   . LEU B 592 ? 0.6483 0.8886 0.4052 -0.0426 0.1923  -0.0350 590 LEU B O   
8894 C CB  . LEU B 592 ? 0.6501 0.8505 0.4733 0.0024  0.1930  -0.1282 590 LEU B CB  
8895 C CG  . LEU B 592 ? 0.7298 0.8957 0.5733 0.0183  0.1818  -0.1617 590 LEU B CG  
8896 C CD1 . LEU B 592 ? 0.5213 0.6545 0.4162 0.0346  0.1793  -0.1669 590 LEU B CD1 
8897 C CD2 . LEU B 592 ? 0.5528 0.7440 0.4056 0.0224  0.1870  -0.2045 590 LEU B CD2 
8898 N N   . GLU B 593 ? 0.6015 0.9078 0.3752 -0.0384 0.2201  -0.0908 591 GLU B N   
8899 C CA  . GLU B 593 ? 0.6777 1.0138 0.4463 -0.0571 0.2298  -0.0564 591 GLU B CA  
8900 C C   . GLU B 593 ? 0.6527 0.9765 0.4688 -0.0499 0.2372  -0.0476 591 GLU B C   
8901 O O   . GLU B 593 ? 0.7805 1.0986 0.6376 -0.0304 0.2426  -0.0799 591 GLU B O   
8902 C CB  . GLU B 593 ? 0.6767 1.0754 0.4330 -0.0682 0.2476  -0.0770 591 GLU B CB  
8903 N N   . ILE B 594 ? 0.7233 1.0431 0.5389 -0.0664 0.2345  -0.0033 592 ILE B N   
8904 C CA  . ILE B 594 ? 0.8368 1.1502 0.6994 -0.0640 0.2403  0.0069  592 ILE B CA  
8905 C C   . ILE B 594 ? 0.7341 1.0979 0.6263 -0.0641 0.2627  -0.0144 592 ILE B C   
8906 O O   . ILE B 594 ? 0.6892 1.0943 0.5606 -0.0824 0.2737  -0.0047 592 ILE B O   
8907 C CB  . ILE B 594 ? 0.8313 1.1252 0.6917 -0.0842 0.2289  0.0583  592 ILE B CB  
8908 C CG1 . ILE B 594 ? 0.7965 1.0453 0.6305 -0.0839 0.2052  0.0788  592 ILE B CG1 
8909 C CG2 . ILE B 594 ? 0.6015 0.8892 0.5141 -0.0834 0.2325  0.0653  592 ILE B CG2 
8910 C CD1 . ILE B 594 ? 0.8893 1.1493 0.6771 -0.0975 0.1951  0.0971  592 ILE B CD1 
8911 N N   . PRO B 595 ? 0.7522 1.1184 0.6956 -0.0449 0.2689  -0.0428 593 PRO B N   
8912 C CA  . PRO B 595 ? 0.7536 1.1688 0.7368 -0.0429 0.2885  -0.0637 593 PRO B CA  
8913 C C   . PRO B 595 ? 0.7747 1.2146 0.7718 -0.0660 0.2976  -0.0269 593 PRO B C   
8914 O O   . PRO B 595 ? 0.8643 1.2747 0.8481 -0.0815 0.2855  0.0136  593 PRO B O   
8915 C CB  . PRO B 595 ? 0.7147 1.1126 0.7563 -0.0162 0.2827  -0.0926 593 PRO B CB  
8916 C CG  . PRO B 595 ? 0.7068 1.0529 0.7273 -0.0031 0.2640  -0.0999 593 PRO B CG  
8917 C CD  . PRO B 595 ? 0.7572 1.0815 0.7269 -0.0236 0.2555  -0.0579 593 PRO B CD  
# 
